|
Name |
Accession |
Description |
Interval |
E-value |
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
505-726 |
2.20e-86 |
|
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: 273.61 E-value: 2.20e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366319 505 LRKEYagkqkhclsKKKAKIATRNVSFCVRKGEILGLLGHNGAGKSTSLKMISGDTKVTAGQVLLKG----SREGDTPGF 580
Cdd:cd03263 6 LTKTY---------KKGTKPAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYINGysirTDRKAARQS 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366319 581 LGYCPQENALWPNLTVKEHLEIFAAVRGLRKSHAAVAITRLADALKLQDQLKSPVKTLSEGVKRKLCFVLSILGNPSILL 660
Cdd:cd03263 77 LGYCPQFDALFDELTVREHLRFYARLKGLPKSEIKEEVELLLRVLGLTDKANKRARTLSGGMKRKLSLAIALIGGPSVLL 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1720366319 661 LDEPSTGLDPEGQQQIWQAIRAIIKNtdRGALLTTHYMAEAEALCDRVAILVSGRLRCIGSIQHLK 726
Cdd:cd03263 157 LDEPTSGLDPASRRAIWDLILEVRKG--RSIILTTHSMDEAEALCDRIAIMSDGKLRCIGSPQELK 220
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
517-729 |
1.06e-73 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 240.74 E-value: 1.06e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366319 517 LSKK-KAKIATRNVSFCVRKGEILGLLGHNGAGKSTSLKMISGDTKVTAGQVLLKG---SREGDTP-GFLGYCPQENALW 591
Cdd:COG1131 6 LTKRyGDKTALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRVLGedvARDPAEVrRRIGYVPQEPALY 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366319 592 PNLTVKEHLEIFAAVRGLRKSHAAVAITRLADALKLQDQLKSPVKTLSEGVKRKLCFVLSILGNPSILLLDEPSTGLDPE 671
Cdd:COG1131 86 PDLTVRENLRFFARLYGLPRKEARERIDELLELFGLTDAADRKVGTLSGGMKQRLGLALALLHDPELLILDEPTSGLDPE 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1720366319 672 GQQQIWQAIRAiIKNTDRGALLTTHYMAEAEALCDRVAILVSGRLRCIGSIQHLKSKF 729
Cdd:COG1131 166 ARRELWELLRE-LAAEGKTVLLSTHYLEEAERLCDRVAIIDKGRIVADGTPDELKARL 222
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
277-818 |
1.70e-60 |
|
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: 224.12 E-value: 1.70e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366319 277 VSGLFPSAYWVGQAMVDIPLYCF-----VFLFMSLMDYLFRFPDTMFSIISHVIQIPCSV---GYAISLIFLTYVISFIS 348
Cdd:TIGR01257 1715 ISGVSPTTYWLTNFLWDIMNYAVsaglvVGIFIGFQKKAYTSPENLPALVALLMLYGWAVipmMYPASFLFDVPSTAYVA 1794
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366319 349 RK------GKKNSGIwslsFYIITVFSVAVILLAFDVDGTQYYIIFlipPSTLVGCLILSLHL------FIGQIFEE--- 413
Cdd:TIGR01257 1795 LScanlfiGINSSAI----TFVLELFENNRTLLRFNAMLRKLLIVF---PHFCLGRGLIDLALsqavtdVYAQFGEEhsa 1867
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366319 414 -------------GQVIEPFLVFLIPFLHVFIFIFTlrclEWKfgkKTMRKDPIFrisPRNNDVYQnpeepedededvqm 480
Cdd:TIGR01257 1868 npfqwdligknlvAMAVEGVVYFLLTLLIQHHFFLS----RWI---AEPAKEPIF---DEDDDVAE-------------- 1923
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366319 481 ERMRtanalVSTSFDEKPVIIASCLRKEYAGKqkhclskkkAKIATRNVSFCVRKGEILGLLGHNGAGKSTSLKMISGDT 560
Cdd:TIGR01257 1924 ERQR-----IISGGNKTDILRLNELTKVYSGT---------SSPAVDRLCVGVRPGECFGLLGVNGAGKTTTFKMLTGDT 1989
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366319 561 KVTAGQVLLKG----SREGDTPGFLGYCPQENALWPNLTVKEHLEIFAAVRGLrkshAAVAITRLAD----ALKLQDQLK 632
Cdd:TIGR01257 1990 TVTSGDATVAGksilTNISDVHQNMGYCPQFDAIDDLLTGREHLYLYARLRGV----PAEEIEKVANwsiqSLGLSLYAD 2065
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366319 633 SPVKTLSEGVKRKLCFVLSILGNPSILLLDEPSTGLDPEGQQQIWQAIRAIIKNtDRGALLTTHYMAEAEALCDRVAILV 712
Cdd:TIGR01257 2066 RLAGTYSGGNKRKLSTAIALIGCPPLVLLDEPTTGMDPQARRMLWNTIVSIIRE-GRAVVLTSHSMEECEALCTRLAIMV 2144
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366319 713 SGRLRCIGSIQHLKSKFGKDYLLEMKVKT-----LEQVEPLNTEILRLFPQASRQERYSSLMAYKLPVEAvqpLSQAFFK 787
Cdd:TIGR01257 2145 KGAFQCLGTIQHLKSKFGDGYIVTMKIKSpkddlLPDLNPVEQFFQGNFPGSVQRERHYNMLQFQVSSSS---LARIFQL 2221
|
570 580 590
....*....|....*....|....*....|.
gi 1720366319 788 LEKVKQTFDLEEYSLSQSTLEQVFLELSKEQ 818
Cdd:TIGR01257 2222 LISHKDSLLIEEYSVTQTTLDQVFVNFAKQQ 2252
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
517-732 |
4.13e-60 |
|
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: 204.32 E-value: 4.13e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366319 517 LSKK-KAKIATRNVSFCVRKGEILGLLGHNGAGKSTSLKMISGDTKVTAGQVLLKG-SREGDTPGF---LGYCPQENALW 591
Cdd:COG4555 7 LSKKyGKVPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIDGeDVRKEPREArrqIGVLPDERGLY 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366319 592 PNLTVKEHLEIFAAVRGLRKSHAAVAITRLADALKLQDQLKSPVKTLSEGVKRKLCFVLSILGNPSILLLDEPSTGLDPE 671
Cdd:COG4555 87 DRLTVRENIRYFAELYGLFDEELKKRIEELIELLGLEEFLDRRVGELSTGMKKKVALARALVHDPKVLLLDEPTNGLDVM 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1720366319 672 GQQQIWQAIRAiIKNTDRGALLTTHYMAEAEALCDRVAILVSGRLRCIGSIQHLKSKFGKD 732
Cdd:COG4555 167 ARRLLREILRA-LKKEGKTVLFSSHIMQEVEALCDRVVILHKGKVVAQGSLDELREEIGEE 226
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
517-716 |
1.31e-56 |
|
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: 191.84 E-value: 1.31e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366319 517 LSKK-KAKIATRNVSFCVRKGEILGLLGHNGAGKSTSLKMISGDTKVTAGQVLLKG----SREGDTPGFLGYCPQENALW 591
Cdd:cd03230 6 LSKRyGKKTALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVLGkdikKEPEEVKRRIGYLPEEPSLY 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366319 592 PNLTVKEHLEifaavrglrkshaavaitrladalklqdqlkspvktLSEGVKRKLCFVLSILGNPSILLLDEPSTGLDPE 671
Cdd:cd03230 86 ENLTVRENLK------------------------------------LSGGMKQRLALAQALLHDPELLILDEPTSGLDPE 129
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1720366319 672 GQQQIWQAIRAiIKNTDRGALLTTHYMAEAEALCDRVAILVSGRL 716
Cdd:cd03230 130 SRREFWELLRE-LKKEGKTILLSSHILEEAERLCDRVAILNNGRI 173
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
517-818 |
5.68e-56 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 194.56 E-value: 5.68e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366319 517 LSKKKA-KIATRNVSFCVRKGEILGLLGHNGAGKSTSLKMISGDTKVTAGQVLLKGSREG-DTPGFLGYCPQENALWPNL 594
Cdd:COG4152 7 LTKRFGdKTAVDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDSGEVLWDGEPLDpEDRRRIGYLPEERGLYPKM 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366319 595 TVKEHLEIFAAVRGLRKSHAAVAITRLADALKLQDQLKSPVKTLSEGVKRKLCFVLSILGNPSILLLDEPSTGLDPEGQQ 674
Cdd:COG4152 87 KVGEQLVYLARLKGLSKAEAKRRADEWLERLGLGDRANKKVEELSKGNQQKVQLIAALLHDPELLILDEPFSGLDPVNVE 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366319 675 QIWQAIRAIIkntDRGA--LLTTHYMAEAEALCDRVAILVSGRLRCIGSIQHLKSKFGKdyllemkvKTLEQVEPLNTEI 752
Cdd:COG4152 167 LLKDVIRELA---AKGTtvIFSSHQMELVEELCDRIVIINKGRKVLSGSVDEIRRQFGR--------NTLRLEADGDAGW 235
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1720366319 753 LRLFPQASRQERYSSLMAYKLPVEAV-QPLsqaffkLEKVKQTFDLEEYSLSQSTLEQVFLELSKEQ 818
Cdd:COG4152 236 LRALPGVTVVEEDGDGAELKLEDGADaQEL------LRALLARGPVREFEEVRPSLNEIFIEVVGEK 296
|
|
| drrA |
TIGR01188 |
daunorubicin resistance ABC transporter ATP-binding subunit; This model describes daunorubicin ... |
525-814 |
2.89e-55 |
|
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: 192.99 E-value: 2.89e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366319 525 ATRNVSFCVRKGEILGLLGHNGAGKSTSLKMISGDTKVTAGQVLLKG---SREGDT-PGFLGYCPQENALWPNLTVKEHL 600
Cdd:TIGR01188 8 AVDGVNFKVREGEVFGFLGPNGAGKTTTIRMLTTLLRPTSGTARVAGydvVREPRKvRRSIGIVPQYASVDEDLTGRENL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366319 601 EIFAAVRGLRKSHAAVAITRLADALKLQDQLKSPVKTLSEGVKRKLCFVLSILGNPSILLLDEPSTGLDPEGQQQIWQAI 680
Cdd:TIGR01188 88 EMMGRLYGLPKDEAEERAEELLELFELGEAADRPVGTYSGGMRRRLDIAASLIHQPDVLFLDEPTTGLDPRTRRAIWDYI 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366319 681 RAiIKNTDRGALLTTHYMAEAEALCDRVAILVSGRLRCIGSIQHLKSKFGKDYlLEMKVKTLEQVEPLNTEILRLFPQAS 760
Cdd:TIGR01188 168 RA-LKEEGVTILLTTHYMEEADKLCDRIAIIDHGRIIAEGTPEELKRRLGKDT-LESRPRDIQSLKVEVSMLIAELGETG 245
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 1720366319 761 RQERYSSLMAYKLPVEAVQPLSQAFFKLEKVKQT-FDLEEYSLSQSTLEQVFLEL 814
Cdd:TIGR01188 246 LGLLAVTVDSDRIKILVPDGDETVPEIVEAAIRNgIRIRSISTERPSLDDVFLKL 300
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
525-726 |
9.03e-54 |
|
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: 186.04 E-value: 9.03e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366319 525 ATRNVSFCVRKGEILGLLGHNGAGKSTSLKMISGDTKVTAGQVLLKG----SREGDTPGFLGYCPQENALWPNLTVKEHL 600
Cdd:cd03265 15 AVRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATVAGhdvvREPREVRRRIGIVFQDLSVDDELTGWENL 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366319 601 EIFAAVRGLRKSHAAVAITRLADALKLQDQLKSPVKTLSEGVKRKLCFVLSILGNPSILLLDEPSTGLDPEGQQQIWQAI 680
Cdd:cd03265 95 YIHARLYGVPGAERRERIDELLDFVGLLEAADRLVKTYSGGMRRRLEIARSLVHRPEVLFLDEPTIGLDPQTRAHVWEYI 174
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1720366319 681 RAIIKNTDRGALLTTHYMAEAEALCDRVAILVSGRLRCIGSIQHLK 726
Cdd:cd03265 175 EKLKEEFGMTILLTTHYMEEAEQLCDRVAIIDHGRIIAEGTPEELK 220
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
521-720 |
6.36e-48 |
|
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: 169.00 E-value: 6.36e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366319 521 KAKIATRNVSFCVRKGEILGLLGHNGAGKSTSLKMISGDTKVTAGQVLLKGSREGDTPG-FLGYCPQENALWPNLTVKEH 599
Cdd:cd03269 11 GRVTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDGKPLDIAARnRIGYLPEERGLYPKMKVIDQ 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366319 600 LEIFAAVRGLRKSHAAVAITRLADALKLQDQLKSPVKTLSEGVKRKLCFVLSILGNPSILLLDEPSTGLDPEGQQQIWQA 679
Cdd:cd03269 91 LVYLAQLKGLKKEEARRRIDEWLERLELSEYANKRVEELSKGNQQKVQFIAAVIHDPELLILDEPFSGLDPVNVELLKDV 170
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1720366319 680 IRAiIKNTDRGALLTTHYMAEAEALCDRVAILVSGRLRCIG 720
Cdd:cd03269 171 IRE-LARAGKTVILSTHQMELVEELCDRVLLLNKGRAVLYG 210
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
499-817 |
7.31e-48 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 172.96 E-value: 7.31e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366319 499 VIIASCLRKEY---------AGKQKHCLS-KKKAKIATRNVSFCVRKGEILGLLGHNGAGKSTSLKMISGDTKVTAGQVL 568
Cdd:COG4586 1 IIEVENLSKTYrvyekepglKGALKGLFRrEYREVEAVDDISFTIEPGEIVGFIGPNGAGKSTTIKMLTGILVPTSGEVR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366319 569 lkgsregdtpgFLGYCP----------------QENALWPNLTVKEHLEIFAAVRGLRKSHAAVAITRLADALKLQDQLK 632
Cdd:COG4586 81 -----------VLGYVPfkrrkefarrigvvfgQRSQLWWDLPAIDSFRLLKAIYRIPDAEYKKRLDELVELLDLGELLD 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366319 633 SPVKTLSEGVKRKLCFVLSILGNPSILLLDEPSTGLDPEGQQQIWQAIRAIikNTDRGA--LLTTHYMAEAEALCDRVAI 710
Cdd:COG4586 150 TPVRQLSLGQRMRCELAAALLHRPKILFLDEPTIGLDVVSKEAIREFLKEY--NRERGTtiLLTSHDMDDIEALCDRVIV 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366319 711 LVSGRLRCIGSIQHLKSKFGKDyllemKVKTLEQVEPLNTEILRLFPQASRQERYSslmaYKLPVEAVQPLSQAffkLEK 790
Cdd:COG4586 228 IDHGRIIYDGSLEELKERFGPY-----KTIVLELAEPVPPLELPRGGEVIEREGNR----VRLEVDPRESLAEV---LAR 295
|
330 340
....*....|....*....|....*..
gi 1720366319 791 VKQTFDLEEYSLSQSTLEQVFLELSKE 817
Cdd:COG4586 296 LLARYPVRDLTIEEPPIEEVIRRIYKE 322
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
516-717 |
1.28e-44 |
|
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: 159.69 E-value: 1.28e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366319 516 CLSKK-KAKIATRNVSFCVRKGEILGLLGHNGAGKSTSLKMISGDTKVTAGQVLLKGS---REGDTPGFLGYCPQENALW 591
Cdd:cd03268 5 DLTKTyGKKRVLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEITFDGKsyqKNIEALRRIGALIEAPGFY 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366319 592 PNLTVKEHLEIFAAVRGLRKShaavAITRLADALKLQDQLKSPVKTLSEGVKRKLCFVLSILGNPSILLLDEPSTGLDPE 671
Cdd:cd03268 85 PNLTARENLRLLARLLGIRKK----RIDEVLDVVGLKDSAKKKVKGFSLGMKQRLGIALALLGNPDLLILDEPTNGLDPD 160
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1720366319 672 GQQQIWQAIRAiIKNTDRGALLTTHYMAEAEALCDRVAILVSGRLR 717
Cdd:cd03268 161 GIKELRELILS-LRDQGITVLISSHLLSEIQKVADRIGIINKGKLI 205
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
523-717 |
2.64e-42 |
|
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: 153.12 E-value: 2.64e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366319 523 KIATRNVSFCVRKGeILGLLGHNGAGKSTSLKMISGDTKVTAGQVLLKGSREGDTP----GFLGYCPQENALWPNLTVKE 598
Cdd:cd03264 13 KRALDGVSLTLGPG-MYGLLGPNGAGKTTLMRILATLTPPSSGTIRIDGQDVLKQPqklrRRIGYLPQEFGVYPNFTVRE 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366319 599 HLEIFAAVRGLRKSHAAVAITRLADALKLQDQLKSPVKTLSEGVKRKLCFVLSILGNPSILLLDEPSTGLDPEgqQQIwq 678
Cdd:cd03264 92 FLDYIAWLKGIPSKEVKARVDEVLELVNLGDRAKKKIGSLSGGMRRRVGIAQALVGDPSILIVDEPTAGLDPE--ERI-- 167
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1720366319 679 AIRAIIKN--TDRGALLTTHYMAEAEALCDRVAILVSGRLR 717
Cdd:cd03264 168 RFRNLLSElgEDRIVILSTHIVEDVESLCNQVAVLNKGKLV 208
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
519-720 |
6.14e-42 |
|
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: 152.52 E-value: 6.14e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366319 519 KKKAKIATRNVSFCVRKGEILGLLGHNGAGKSTSLKMISGDTKVTAGQVLLKGSREGDTP----GFLGYCPQENALWPNL 594
Cdd:cd03266 14 VKKTVQAVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDGFDVVKEPaearRRLGFVSDSTGLYDRL 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366319 595 TVKEHLEIFAAVRGLRKSHAAVAITRLADALKLQDQLKSPVKTLSEGVKRKLCFVLSILGNPSILLLDEPSTGLDPEGQQ 674
Cdd:cd03266 94 TARENLEYFAGLYGLKGDELTARLEELADRLGMEELLDRRVGGFSTGMRQKVAIARALVHDPPVLLLDEPTTGLDVMATR 173
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1720366319 675 QIWQAIRAiIKNTDRGALLTTHYMAEAEALCDRVAILVSGRLRCIG 720
Cdd:cd03266 174 ALREFIRQ-LRALGKCILFSTHIMQEVERLCDRVVVLHRGRVVYEG 218
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
523-815 |
1.37e-41 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 154.58 E-value: 1.37e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366319 523 KIATRNVSFCVRKGEILGLLGHNGAGKSTSLKMISGDTKVTAGQVLLKG----SREGDTPGFLGYCPQENALWPNLTVKE 598
Cdd:PRK13537 20 KLVVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCGepvpSRARHARQRVGVVPQFDNLDPDFTVRE 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366319 599 HLEIFAAVRGLRKSHAAVAITRLADALKLQDQLKSPVKTLSEGVKRKLCFVLSILGNPSILLLDEPSTGLDPEGQQQIWQ 678
Cdd:PRK13537 100 NLLVFGRYFGLSAAAARALVPPLLEFAKLENKADAKVGELSGGMKRRLTLARALVNDPDVLVLDEPTTGLDPQARHLMWE 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366319 679 AIRAIIKntdRGA--LLTTHYMAEAEALCDRVAILVSGRLRCIGSIQHL-KSKFGKDyLLEMKVKTLeqvEPLNTEilrL 755
Cdd:PRK13537 180 RLRSLLA---RGKtiLLTTHFMEEAERLCDRLCVIEEGRKIAEGAPHALiESEIGCD-VIEIYGPDP---VALRDE---L 249
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1720366319 756 FPQASRQE-RYSSLMAYklpVEAVQPLSQAffklekVKQTFDLeEYSLSQSTLEQVFLELS 815
Cdd:PRK13537 250 APLAERTEiSGETLFCY---VRDPEPLHAR------LKGRAGL-RYLHRPANLEDVFLRLT 300
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
519-716 |
6.32e-41 |
|
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: 150.18 E-value: 6.32e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366319 519 KKKAKIATRNVSFCVRKGEILGLLGHNGAGKSTSLKMISGDTKVTAGQVLLKGSREGD-TPGFL-------GycpQENAL 590
Cdd:cd03267 30 KYREVEALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRVAGLVPWKrRKKFLrrigvvfG---QKTQL 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366319 591 WPNLTVKEHLEIFAAVRGLRKSHAAVAITRLADALKLQDQLKSPVKTLSEGVKRKLCFVLSILGNPSILLLDEPSTGLDP 670
Cdd:cd03267 107 WWDLPVIDSFYLLAAIYDLPPARFKKRLDELSELLDLEELLDTPVRQLSLGQRMRAEIAAALLHEPEILFLDEPTIGLDV 186
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1720366319 671 EGQQQIWQAIRAIIKNTDRGALLTTHYMAEAEALCDRVAILVSGRL 716
Cdd:cd03267 187 VAQENIRNFLKEYNRERGTTVLLTSHYMKDIEALARRVLVIDKGRL 232
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
527-696 |
2.00e-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: 147.63 E-value: 2.00e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366319 527 RNVSFCVRKGEILGLLGHNGAGKSTSLKMISGDTKVTAGQVLLKG----SREGDTPGFLGYCPQENALWPNLTVKEHLEI 602
Cdd:COG4133 19 SGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWNGepirDAREDYRRRLAYLGHADGLKPELTVRENLRF 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366319 603 FAAVRGLRKSHAAvaITRLADALKLQDQLKSPVKTLSEGVKRKLCFVLSILGNPSILLLDEPSTGLDPEGQQQIWQAIRA 682
Cdd:COG4133 99 WAALYGLRADREA--IDEALEAVGLAGLADLPVRQLSAGQKRRVALARLLLSPAPLWLLDEPFTALDAAGVALLAELIAA 176
|
170
....*....|....*.
gi 1720366319 683 iikNTDRG--ALLTTH 696
Cdd:COG4133 177 ---HLARGgaVLLTTH 189
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
525-715 |
1.33e-38 |
|
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: 142.96 E-value: 1.33e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366319 525 ATRNVSFCVRKGEILGLLGHNGAGKSTSLKMISGDTKVTAGQVLLKGSREGDTPGF------LGYCPQENALWPNLTVKE 598
Cdd:cd03224 15 ILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDGRDITGLPPHeraragIGYVPEGRRIFPELTVEE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366319 599 HLEIFAAVRGLRKSHAavaitRLADAL----KLQDQLKSPVKTLSEGVKRKLCFVLSILGNPSILLLDEPSTGLDPEGQQ 674
Cdd:cd03224 95 NLLLGAYARRRAKRKA-----RLERVYelfpRLKERRKQLAGTLSGGEQQMLAIARALMSRPKLLLLDEPSEGLAPKIVE 169
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1720366319 675 QIWQAIRAIIKnTDRGALLTTHYMAEAEALCDRVAILVSGR 715
Cdd:cd03224 170 EIFEAIRELRD-EGVTILLVEQNARFALEIADRAYVLERGR 209
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
523-715 |
1.96e-37 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 143.43 E-value: 1.96e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366319 523 KIATRNVSFCVRKGEILGLLGHNGAGKSTSLKMISGDTKVTAGQVLLKG----SREGDTPGFLGYCPQENALWPNLTVKE 598
Cdd:PRK13536 54 KAVVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKITVLGvpvpARARLARARIGVVPQFDNLDLEFTVRE 133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366319 599 HLEIFAAVRGLRKSHAAVAITRLADALKLQDQLKSPVKTLSEGVKRKLCFVLSILGNPSILLLDEPSTGLDPEGQQQIWQ 678
Cdd:PRK13536 134 NLLVFGRYFGMSTREIEAVIPSLLEFARLESKADARVSDLSGGMKRRLTLARALINDPQLLILDEPTTGLDPHARHLIWE 213
|
170 180 190
....*....|....*....|....*....|....*....
gi 1720366319 679 AIRAIIKntdRGA--LLTTHYMAEAEALCDRVAILVSGR 715
Cdd:PRK13536 214 RLRSLLA---RGKtiLLTTHFMEEAERLCDRLCVLEAGR 249
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
517-720 |
8.62e-37 |
|
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: 137.65 E-value: 8.62e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366319 517 LSKK-KAKIATRNVSFCVRKGEILGLLGHNGAGKSTSLKMISGDTKVTAGQVLLKGSREGDTP---GFLGYCPQENALWP 592
Cdd:cd03259 6 LSKTyGSVRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDGRDVTGVPperRNIGMVFQDYALFP 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366319 593 NLTVKEHLEIFAAVRGLRKSHAAVAITRLADALKLQDQLKSPVKTLSEGVKRKLCFVLSILGNPSILLLDEPSTGLDPEG 672
Cdd:cd03259 86 HLTVAENIAFGLKLRGVPKAEIRARVRELLELVGLEGLLNRYPHELSGGQQQRVALARALAREPSLLLLDEPLSALDAKL 165
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1720366319 673 QQQIWQAIRAIIKNTDRGALLTTHYMAEAEALCDRVAILVSGRLRCIG 720
Cdd:cd03259 166 REELREELKELQRELGITTIYVTHDQEEALALADRIAVMNEGRIVQVG 213
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
527-715 |
7.83e-36 |
|
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid transport and metabolism];
Pssm-ID: 440179 [Multi-domain] Cd Length: 236 Bit Score: 135.49 E-value: 7.83e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366319 527 RNVSFCVRKGEILGLLGHNGAGKSTSLKMISGDTKVTAGQVLLKG-----------SREGdtpgfLGYCPQENALWPNLT 595
Cdd:COG0410 20 HGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRSGSIRFDGeditglpphriARLG-----IGYVPEGRRIFPSLT 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366319 596 VKEHLEIFAAVRGLRKSHAAvaitRLADAL----KLQDQLKSPVKTLSEGVKRklcfVLSI----LGNPSILLLDEPSTG 667
Cdd:COG0410 95 VEENLLLGAYARRDRAEVRA----DLERVYelfpRLKERRRQRAGTLSGGEQQ----MLAIgralMSRPKLLLLDEPSLG 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1720366319 668 LDPEGQQQIWQAIRAIIkntDRGA--LLTTHYMAEAEALCDRVAILVSGR 715
Cdd:COG0410 167 LAPLIVEEIFEIIRRLN---REGVtiLLVEQNARFALEIADRAYVLERGR 213
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
528-817 |
3.39e-35 |
|
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim protein) in eukaryotes. It is the member of ABC transporter superfamily. Rim protein is a membrane glycoprotein which is localized in the photoreceptor outer segment discs. Mutation/s in its genetic loci is implicated in the recessive Stargardt's disease. [Transport and binding proteins, Other]
Pssm-ID: 130324 [Multi-domain] Cd Length: 2272 Bit Score: 145.16 E-value: 3.39e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366319 528 NVSFcvRKGEILGLLGHNGAGKSTSLKMISGDTKVTAGQVLLkGSREGDTP-----GFLGYCPQENALWPNLTVKEHLEI 602
Cdd:TIGR01257 950 NITF--YENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLV-GGKDIETNldavrQSLGMCPQHNILFHHLTVAEHILF 1026
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366319 603 FAAVRGLRKSHAAVAITRLADALKLQDQLKSPVKTLSEGVKRKLCFVLSILGNPSILLLDEPSTGLDPEGQQQIWQAIra 682
Cdd:TIGR01257 1027 YAQLKGRSWEEAQLEMEAMLEDTGLHHKRNEEAQDLSGGMQRKLSVAIAFVGDAKVVVLDEPTSGVDPYSRRSIWDLL-- 1104
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366319 683 IIKNTDRGALLTTHYMAEAEALCDRVAILVSGRLRCIGSIQHLKSKFGKDYLLEM--KVKTLEQ---------------- 744
Cdd:TIGR01257 1105 LKYRSGRTIIMSTHHMDEADLLGDRIAIISQGRLYCSGTPLFLKNCFGTGFYLTLvrKMKNIQSqrggcegtcsctskgf 1184
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366319 745 --------------------VEPLNTEILRLFPQASRQERYSSLMAYKLPVEAVQPLSQA--FFKLEKVKQTFDLEEYSL 802
Cdd:TIGR01257 1185 strcparvdeitpeqvldgdVNELMDLVYHHVPEAKLVECIGQELIFLLPNKNFKQRAYAslFRELEETLADLGLSSFGI 1264
|
330
....*....|....*
gi 1720366319 803 SQSTLEQVFLELSKE 817
Cdd:TIGR01257 1265 SDTPLEEIFLKVTED 1279
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
527-666 |
4.60e-35 |
|
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: 130.46 E-value: 4.60e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366319 527 RNVSFCVRKGEILGLLGHNGAGKSTSLKMISGDTKVTAGQVLLKG-----SREGDTPGFLGYCPQENALWPNLTVKEHLE 601
Cdd:pfam00005 2 KNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGqdltdDERKSLRKEIGYVFQDPQLFPRLTVRENLR 81
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1720366319 602 IFAAVRGLRKSHAAVAITRLADALKLQDQLKSPV----KTLSEGVKRKLCFVLSILGNPSILLLDEPST 666
Cdd:pfam00005 82 LGLLLKGLSKREKDARAEEALEKLGLGDLADRPVgerpGTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
517-721 |
1.72e-34 |
|
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: 131.51 E-value: 1.72e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366319 517 LSKK-KAKIATRNVSFCVRKGEILGLLGHNGAGKSTSLKMISGDTKVTAGQVLLKG-----------SREGdtpgfLGYC 584
Cdd:cd03218 6 LSKRyGKRKVVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDGqditklpmhkrARLG-----IGYL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366319 585 PQENALWPNLTVKEHLEIFAAVRGLRKSHAAVAITRLADALKLQDQLKSPVKTLSEGVKRKLCFVLSILGNPSILLLDEP 664
Cdd:cd03218 81 PQEASIFRKLTVEENILAVLEIRGLSKKEREEKLEELLEEFHITHLRKSKASSLSGGERRRVEIARALATNPKFLLLDEP 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1720366319 665 STGLDPEGQQQIwQAIRAIIKNTDRGALLTTHYMAEAEALCDRVAILVSGRLRCIGS 721
Cdd:cd03218 161 FAGVDPIAVQDI-QKIIKILKDRGIGVLITDHNVRETLSITDRAYIIYEGKVLAEGT 216
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
525-716 |
5.50e-34 |
|
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: 130.25 E-value: 5.50e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366319 525 ATRNVSFCVRKGEILGLLGHNGAGKSTSLKMISGDTKVTAGQVLLKGSREGDTP-------GfLGYCPQENALWPNLTVK 597
Cdd:cd03219 15 ALDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFDGEDITGLPpheiarlG-IGRTFQIPRLFPELTVL 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366319 598 EHLEI---------FAAVRGLRKSHAAVA-ITRLADALKLQDQLKSPVKTLSEGVKRKLCFVLSILGNPSILLLDEPSTG 667
Cdd:cd03219 94 ENVMVaaqartgsgLLLARARREEREARErAEELLERVGLADLADRPAGELSYGQQRRLEIARALATDPKLLLLDEPAAG 173
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1720366319 668 LDPEGQQQIWQAIRAiIKNTDRGALLTTHYMAEAEALCDRVAILVSGRL 716
Cdd:cd03219 174 LNPEETEELAELIRE-LRERGITVLLVEHDMDVVMSLADRVTVLDQGRV 221
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
525-716 |
1.20e-33 |
|
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: 130.16 E-value: 1.20e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366319 525 ATRNVSFCVRKGEILGLLGHNGAGKSTSLKMISGDTKVTAGQVLLKG-----------SREGdtpgfLGYCPQENALWPN 593
Cdd:COG0411 19 AVDDVSLEVERGEIVGLIGPNGAGKTTLFNLITGFYRPTSGRILFDGrditglpphriARLG-----IARTFQNPRLFPE 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366319 594 LTVKEHLEI----------FAAVRGLRKSHAAVAITR-----LADALKLQDQLKSPVKTLSEGVKRKLCFVLSILGNPSI 658
Cdd:COG0411 94 LTVLENVLVaaharlgrglLAALLRLPRARREEREAReraeeLLERVGLADRADEPAGNLSYGQQRRLEIARALATEPKL 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1720366319 659 LLLDEPSTGLDPEGQQQIWQAIRAIIKNTDRGALLTTHYMAEAEALCDRVAILVSGRL 716
Cdd:COG0411 174 LLLDEPAAGLNPEETEELAELIRRLRDERGITILLIEHDMDLVMGLADRIVVLDFGRV 231
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
519-715 |
6.85e-33 |
|
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: 126.43 E-value: 6.85e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366319 519 KKKAKIATRNVSFCVRKGEILGLLGHNGAGKSTSLKMISGDTKVTAGQVLLKGSREGDTP-----GFLGYCPQEnalwP- 592
Cdd:cd03225 10 PDGARPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDLTKLSlkelrRKVGLVFQN----Pd 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366319 593 ----NLTVKEhlEI-FAAV-RGLRKSHAAVAITRLADALKLQDQLKSPVKTLSEGVKRKLCfVLSIL-GNPSILLLDEPS 665
Cdd:cd03225 86 dqffGPTVEE--EVaFGLEnLGLPEEEIEERVEEALELVGLEGLRDRSPFTLSGGQKQRVA-IAGVLaMDPDILLLDEPT 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1720366319 666 TGLDPEGQQQIWQAIRAiIKNTDRGALLTTHYMAEAEALCDRVAILVSGR 715
Cdd:cd03225 163 AGLDPAGRRELLELLKK-LKAEGKTIIIVTHDLDLLLELADRVIVLEDGK 211
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
527-736 |
1.02e-32 |
|
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: 126.68 E-value: 1.02e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366319 527 RNVSFCVRKGEILGLLGHNGAGKSTSLKMISGDTKVTAGQVLLKGS--REGDTPGF---LGYCPQ--ENALWpNLTVKEh 599
Cdd:COG1122 18 DDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVDGKdiTKKNLRELrrkVGLVFQnpDDQLF-APTVEE- 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366319 600 lEI-FAAV-RGLRKSHAAVAITRLADALKLQDQLKSPVKTLSEGVKRKLCF--VLSIlgNPSILLLDEPSTGLDPEGQQQ 675
Cdd:COG1122 96 -DVaFGPEnLGLPREEIRERVEEALELVGLEHLADRPPHELSGGQKQRVAIagVLAM--EPEVLVLDEPTAGLDPRGRRE 172
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1720366319 676 IWQAIRAiIKNTDRGALLTTHYMAEAEALCDRVAILVSGRLRCIGSIQHLkskFGKDYLLE 736
Cdd:COG1122 173 LLELLKR-LNKEGKTVIIVTHDLDLVAELADRVIVLDDGRIVADGTPREV---FSDYELLE 229
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
498-721 |
3.72e-32 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 125.14 E-value: 3.72e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366319 498 PVIIASCLRKEYAGKQkhclskkkakiATRNVSFCVRKGEILGLLGHNGAGKSTSLKMISGDTKVTAGQVLLKG------ 571
Cdd:COG1137 2 MTLEAENLVKSYGKRT-----------VVKDVSLEVNQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGRIFLDGedithl 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366319 572 -----SREGdtpgfLGYCPQENALWPNLTVKEHLEIFAAVRGLRKSHAAVAITRLADALKLQDQLKSPVKTLSEGVKRKL 646
Cdd:COG1137 71 pmhkrARLG-----IGYLPQEASIFRKLTVEDNILAVLELRKLSKKEREERLEELLEEFGITHLRKSKAYSLSGGERRRV 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366319 647 CFVLSILGNPSILLLDEPSTGLDP----EgqqqiwqaIRAIIKN-TDRGA--LLTTHYMAEAEALCDRVAILVSGRLRCI 719
Cdd:COG1137 146 EIARALATNPKFILLDEPFAGVDPiavaD--------IQKIIRHlKERGIgvLITDHNVRETLGICDRAYIISEGKVLAE 217
|
..
gi 1720366319 720 GS 721
Cdd:COG1137 218 GT 219
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
527-721 |
4.14e-32 |
|
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: 125.54 E-value: 4.14e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366319 527 RNVSFCVRKGEILGLLGHNGAGKSTSLKMISGDTKVTAGQVLLKGSREGDTPG-----FLGYCPQENALWPNLTVKE--- 598
Cdd:COG1120 18 DDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDGRDLASLSRrelarRIAYVPQEPPAPFGLTVRElva 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366319 599 -----HLEIFAAVRglRKSHAAV--AITRLaDALKLQDQlksPVKTLSEGVKRKLCFVLSILGNPSILLLDEPSTGLDPE 671
Cdd:COG1120 98 lgrypHLGLFGRPS--AEDREAVeeALERT-GLEHLADR---PVDELSGGERQRVLIARALAQEPPLLLLDEPTSHLDLA 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1720366319 672 GQQQIWQAIRAIIKNTDRGALLTTHYMAEAEALCDRVAILVSGRLRCIGS 721
Cdd:COG1120 172 HQLEVLELLRRLARERGRTVVMVLHDLNLAARYADRLVLLKDGRIVAQGP 221
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
523-724 |
2.02e-31 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 123.28 E-value: 2.02e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366319 523 KIATRNVSFCVRKGEILGLLGHNGAGKSTSLKMISGDTKVTAGQVLLKGSREGDTPGFLGYCPQENALWPN--LTVKE-- 598
Cdd:COG1121 19 RPVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLFGKPPRRARRRIGYVPQRAEVDWDfpITVRDvv 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366319 599 ------HLEIFaavRGLRKSHAAvAITRLADALKLQDQLKSPVKTLSEGVKRKLCFVLSILGNPSILLLDEPSTGLDPEG 672
Cdd:COG1121 99 lmgrygRRGLF---RRPSRADRE-AVDEALERVGLEDLADRPIGELSGGQQQRVLLARALAQDPDLLLLDEPFAGVDAAT 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1720366319 673 QQQIWQAIRAiIKNTDRGALLTTHYMAEAEALCDRVaILVSGRLRCIGSIQH 724
Cdd:COG1121 175 EEALYELLRE-LRREGKTILVVTHDLGAVREYFDRV-LLLNRGLVAHGPPEE 224
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
517-715 |
2.55e-31 |
|
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: 120.04 E-value: 2.55e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366319 517 LSKK-KAKIATRNVSFCVRKGEILGLLGHNGAGKSTSLKMISGDTKVTAGQVLLKGSREGDTPGF-----LGYCPQenal 590
Cdd:cd00267 5 LSFRyGGRTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGKDIAKLPLEelrrrIGYVPQ---- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366319 591 wpnltvkehleifaavrglrkshaavaitrladalklqdqlkspvktLSEGVKRKLCFVLSILGNPSILLLDEPSTGLDP 670
Cdd:cd00267 81 -----------------------------------------------LSGGQRQRVALARALLLNPDLLLLDEPTSGLDP 113
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1720366319 671 EGQQQIWQAIRAIIKNtDRGALLTTHYMAEAEALCDRVAILVSGR 715
Cdd:cd00267 114 ASRERLLELLRELAEE-GRTVIIVTHDPELAELAADRVIVLKDGK 157
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
497-725 |
4.41e-31 |
|
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: 128.48 E-value: 4.41e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366319 497 KPVIIASCLRKEYAGKQKHclskkkakiATRNVSFCVRKGEILGLLGHNGAGKSTSLKMISG---DTKVTAGQVLLKGSR 573
Cdd:COG1123 2 TPLLEVRDLSVRYPGGDVP---------AVDGVSLTIAPGETVALVGESGSGKSTLALALMGllpHGGRISGEVLLDGRD 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366319 574 EGDTPGFL-----GYCPQE--NALWPnLTVKEHLEIFAAVRGLRKSHAAVAITRLADALKLQDQLKSPVKTLSEGVKRKL 646
Cdd:COG1123 73 LLELSEALrgrriGMVFQDpmTQLNP-VTVGDQIAEALENLGLSRAEARARVLELLEAVGLERRLDRYPHQLSGGQRQRV 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1720366319 647 CFVLSILGNPSILLLDEPSTGLDPEGQQQIWQAIRAIIKNTDRGALLTTHYMAEAEALCDRVAILVSGRLRCIGSIQHL 725
Cdd:COG1123 152 AIAMALALDPDLLIADEPTTALDVTTQAEILDLLRELQRERGTTVLLITHDLGVVAEIADRVVVMDDGRIVEDGPPEEI 230
|
|
| galliderm_ABC |
TIGR03740 |
gallidermin-class lantibiotic protection ABC transporter, ATP-binding subunit; Model TIGR03731 ... |
513-722 |
6.25e-31 |
|
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: 121.35 E-value: 6.25e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366319 513 QKHCLSKK-KAKIATRNVSFCVRKGEILGLLGHNGAGKSTSLKMISGDTKVTAGQVLLKGSR--EGDTPGfLGYCPQENA 589
Cdd:TIGR03740 2 ETKNLSKRfGKQTAVNNISLTVPKNSVYGLLGPNGAGKSTLLKMITGILRPTSGEIIFDGHPwtRKDLHK-IGSLIESPP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366319 590 LWPNLTVKEHLEIFAAVRGLRKSHaavaITRLADALKLQDQLKSPVKTLSEGVKRKLCFVLSILGNPSILLLDEPSTGLD 669
Cdd:TIGR03740 81 LYENLTARENLKVHTTLLGLPDSR----IDEVLNIVDLTNTGKKKAKQFSLGMKQRLGIAIALLNHPKLLILDEPTNGLD 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1720366319 670 PEGQQQIWQAIRAIiknTDRG--ALLTTHYMAEAEALCDRVAILVSGRLRCIGSI 722
Cdd:TIGR03740 157 PIGIQELRELIRSF---PEQGitVILSSHILSEVQQLADHIGIISEGVLGYQGKI 208
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
520-720 |
7.00e-31 |
|
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type transporter and the ATPase component of a molybdate transport system that also includes the periplasmic binding protein ModA and the membrane protein ModB. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213264 [Multi-domain] Cd Length: 214 Bit Score: 120.86 E-value: 7.00e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366319 520 KKAKIATRNVSFCVrKGEILGLLGHNGAGKSTSLKMISGDTKVTAGQVLLKG-----SREG-DTPGF---LGYCPQENAL 590
Cdd:cd03297 8 KRLPDFTLKIDFDL-NEEVTGIFGASGAGKSTLLRCIAGLEKPDGGTIVLNGtvlfdSRKKiNLPPQqrkIGLVFQQYAL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366319 591 WPNLTVKEHLEIfaAVRGLRKSHAAVAITRLADALKLQDQLKSPVKTLSEGVKRKLCFVLSILGNPSILLLDEPSTGLDP 670
Cdd:cd03297 87 FPHLNVRENLAF--GLKRKRNREDRISVDELLDLLGLDHLLNRYPAQLSGGEKQRVALARALAAQPELLLLDEPFSALDR 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1720366319 671 EGQQQIWQAIRAIIKNTDRGALLTTHYMAEAEALCDRVAILVSGRLRCIG 720
Cdd:cd03297 165 ALRLQLLPELKQIKKNLNIPVIFVTHDLSEAEYLADRIVVMEDGRLQYIG 214
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
523-711 |
2.46e-30 |
|
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: 119.18 E-value: 2.46e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366319 523 KIATRNVSFCVRKGEILGLLGHNGAGKSTSLKMISGDTKVTAGQVLLKGSREGDTPGFLGYCPQ-ENALW--PnLTVKE- 598
Cdd:cd03235 12 HPVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFGKPLEKERKRIGYVPQrRSIDRdfP-ISVRDv 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366319 599 -------HLEIFaavRGLRKSHAAvAITRLADALKLQDQLKSPVKTLSEGVKRKLCFVLSILGNPSILLLDEPSTGLDPE 671
Cdd:cd03235 91 vlmglygHKGLF---RRLSKADKA-KVDEALERVGLSELADRQIGELSGGQQQRVLLARALVQDPDLLLLDEPFAGVDPK 166
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1720366319 672 GQQQIWQAIRAiIKNTDRGALLTTHYMAEAEALCDRVAIL 711
Cdd:cd03235 167 TQEDIYELLRE-LRREGMTILVVTHDLGLVLEYFDRVLLL 205
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
500-715 |
6.94e-30 |
|
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: 117.96 E-value: 6.94e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366319 500 IIASCLRKEYAGKQKhclskkkAKIATRNVSFCVRKGEILGLLGHNGAGKSTSLKMISGDTKVTAGQVLLKGSREGDTPG 579
Cdd:cd03293 1 LEVRNVSKTYGGGGG-------AVTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVDGEPVTGPGP 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366319 580 FLGYCPQENALWPNLTVKEHLEIFAAVRGLRKSHAAVAITRLADALKLQDQLKSPVKTLSEGVKRKLCFVLSILGNPSIL 659
Cdd:cd03293 74 DRGYVFQQDALLPWLTVLDNVALGLELQGVPKAEARERAEELLELVGLSGFENAYPHQLSGGMRQRVALARALAVDPDVL 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1720366319 660 LLDEPSTGLDPEGQQQIWQAIRAIIKNTDRGALLTTHYMAEAEALCDRVAILvSGR 715
Cdd:cd03293 154 LLDEPFSALDALTREQLQEELLDIWRETGKTVLLVTHDIDEAVFLADRVVVL-SAR 208
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
517-721 |
7.91e-30 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 121.74 E-value: 7.91e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366319 517 LSKK-KAKIATRNVSFCVRKGEILGLLGHNGAGKSTSLKMISGDTKVTAGQVLLKGSREGDTP----GFlGYCPQENALW 591
Cdd:COG3842 11 VSKRyGDVTALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRILLDGRDVTGLPpekrNV-GMVFQDYALF 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366319 592 PNLTVKEHLEIFAAVRGLRKSHAAVAITRLADALKLQDQLKSPVKTLSEG-----------VKRklcfvlsilgnPSILL 660
Cdd:COG3842 90 PHLTVAENVAFGLRMRGVPKAEIRARVAELLELVGLEGLADRYPHQLSGGqqqrvalaralAPE-----------PRVLL 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1720366319 661 LDEPSTGLDPEGQQQIWQAIRAIIKNTDRGALLTTHYMAEAEALCDRVAILVSGRLRCIGS 721
Cdd:COG3842 159 LDEPLSALDAKLREEMREELRRLQRELGITFIYVTHDQEEALALADRIAVMNDGRIEQVGT 219
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
500-720 |
2.15e-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: 116.86 E-value: 2.15e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366319 500 IIASCLRKEYAGKQKHCLSKKKAKIAT-----------RNVSFCVRKGEILGLLGHNGAGKSTSLKMISGDTKVTAGQVL 568
Cdd:cd03220 1 IELENVSKSYPTYKGGSSSLKKLGILGrkgevgefwalKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366319 569 LKGSregDTPGF-LGYcpqenALWPNLTVKEHLEIFAAVRGLRKSHAAVAITRLADALKLQDQLKSPVKTLSEGVKRKLC 647
Cdd:cd03220 81 VRGR---VSSLLgLGG-----GFNPELTGRENIYLNGRLLGLSRKEIDEKIDEIIEFSELGDFIDLPVKTYSSGMKARLA 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1720366319 648 FVLSILGNPSILLLDEP-STGlDPEGQQQIWQAIRAIIKNTdRGALLTTHYMAEAEALCDRVAILVSGRLRCIG 720
Cdd:cd03220 153 FAIATALEPDILLIDEVlAVG-DAAFQEKCQRRLRELLKQG-KTVILVSHDPSSIKRLCDRALVLEKGKIRFDG 224
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
505-716 |
1.13e-28 |
|
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: 114.51 E-value: 1.13e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366319 505 LRKEYAGKqkhclskKKAKIATRNVSFCVRKGEILGLLGHNGAGKSTSLKMISGDTKVTAGQVLLKGSregDTPGF---- 580
Cdd:cd03255 6 LSKTYGGG-------GEKVQALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRVDGT---DISKLseke 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366319 581 --------LGYCPQENALWPNLTVKEHLEIFAAVRGLRKSHAAVAITRLADALKLQDQLKSPVKTLSEGVKRKLCFVLSI 652
Cdd:cd03255 76 laafrrrhIGFVFQSFNLLPDLTALENVELPLLLAGVPKKERRERAEELLERVGLGDRLNHYPSELSGGQQQRVAIARAL 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1720366319 653 LGNPSILLLDEPSTGLDPEGQQQIWQAIRAIIKNTDRGALLTTHYMaEAEALCDRVAILVSGRL 716
Cdd:cd03255 156 ANDPKIILADEPTGNLDSETGKEVMELLRELNKEAGTTIVVVTHDP-ELAEYADRIIELRDGKI 218
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
517-734 |
1.54e-28 |
|
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: 114.74 E-value: 1.54e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366319 517 LSKKKAKIATRNVSFCVRKGEILGLLGHNGAGKSTSLKMISGDTKVTAGQVLLKGSREGDTP----GFlGYCPQENALWP 592
Cdd:cd03299 6 LSKDWKEFKLKNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNGKDITNLPpekrDI-SYVPQNYALFP 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366319 593 NLTVKEHLEIFAAVRGLRKSHAAVAITRLADALKLQDQLKSPVKTLSEGVKRKLCFVLSILGNPSILLLDEPSTGLDPEG 672
Cdd:cd03299 85 HMTVYKNIAYGLKKRKVDKKEIERKVLEIAEMLGIDHLLNRKPETLSGGEQQRVAIARALVVNPKILLLDEPFSALDVRT 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1720366319 673 QQQIWQAIRAIIKNTDRGALLTTHYMAEAEALCDRVAILVSGRLRCIGSIQ----HLKSKFGKDYL 734
Cdd:cd03299 165 KEKLREELKKIRKEFGVTVLHVTHDFEEAWALADKVAIMLNGKLIQVGKPEevfkKPKNEFVAEFL 230
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
518-722 |
1.65e-28 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 114.79 E-value: 1.65e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366319 518 SKKKAKIATRNVSFCVRKGEILGLLGHNGAGKSTSLKMISGDTKVTAGQVLLKGSregdTPGFLGYcpqeNA-LWPNLTV 596
Cdd:COG1134 34 TRREEFWALKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTSGRVEVNGR----VSALLEL----GAgFHPELTG 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366319 597 KEHLEIFAAVRGLRKShaavAITRLADALK----LQDQLKSPVKTLSEGVKRKLCFVLSILGNPSILLLDEP-STGlDPE 671
Cdd:COG1134 106 RENIYLNGRLLGLSRK----EIDEKFDEIVefaeLGDFIDQPVKTYSSGMRARLAFAVATAVDPDILLVDEVlAVG-DAA 180
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1720366319 672 GQQQIWQAIRAIIKNTdRGALLTTHYMAEAEALCDRVAILVSGRLRCIGSI 722
Cdd:COG1134 181 FQKKCLARIRELRESG-RTVIFVSHSMGAVRRLCDRAIWLEKGRLVMDGDP 230
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
525-716 |
3.33e-28 |
|
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: 113.37 E-value: 3.33e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366319 525 ATRNVSFCVRKGEILGLLGHNGAGKSTSLKMISGDTKVTAGQVLLKG--------SREGDTPGFLGYCPQE--NALWPNL 594
Cdd:cd03257 20 ALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGkdllklsrRLRKIRRKEIQMVFQDpmSSLNPRM 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366319 595 TVKEHL-EIFAAVRGLRK-SHAAVAITRLADALKL-QDQLKSPVKTLSEGVKRKLCFVLSILGNPSILLLDEPSTGLDPE 671
Cdd:cd03257 100 TIGEQIaEPLRIHGKLSKkEARKEAVLLLLVGVGLpEEVLNRYPHELSGGQRQRVAIARALALNPKLLIADEPTSALDVS 179
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1720366319 672 GQQQIWQAIRAIIKNTDRGALLTTHYMAEAEALCDRVAILVSGRL 716
Cdd:cd03257 180 VQAQILDLLKKLQEELGLTLLFITHDLGVVAKIADRVAVMYAGKI 224
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
523-715 |
7.24e-28 |
|
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: 110.74 E-value: 7.24e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366319 523 KIATRNVSFCVRKGEILGLLGHNGAGKSTSLKMISGDTKVTAGQVLLKGSREGDTPGFL-------GYCPQENALWPNLT 595
Cdd:cd03229 13 KTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGEDLTDLEDELpplrrriGMVFQDFALFPHLT 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366319 596 VKEHLEIfaavrglrkshaavaitrladalklqdqlkspvkTLSEGVKRKLCFVLSILGNPSILLLDEPSTGLDPEGQQQ 675
Cdd:cd03229 93 VLENIAL----------------------------------GLSGGQQQRVALARALAMDPDVLLLDEPTSALDPITRRE 138
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1720366319 676 IWQAIRAIIKNTDRGALLTTHYMAEAEALCDRVAILVSGR 715
Cdd:cd03229 139 VRALLKSLQAQLGITVVLVTHDLDEAARLADRVVVLRDGK 178
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
523-720 |
2.34e-26 |
|
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: 107.73 E-value: 2.34e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366319 523 KIATRNVSFCVRKGEILGLLGHNGAGKSTSLKMISGDTKVTAGQVLLKGSREGDTPGF---LGYCPQENALWPNLTVKEH 599
Cdd:cd03301 13 VTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGRDVTDLPPKdrdIAMVFQNYALYPHMTVYDN 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366319 600 LEIFAAVRGLRKSHAAVAITRLADALKLQDQLKSPVKTLSEGVKRKLCFVLSILGNPSILLLDEPSTGLDPEGQQQIWQA 679
Cdd:cd03301 93 IAFGLKLRKVPKDEIDERVREVAELLQIEHLLDRKPKQLSGGQRQRVALGRAIVREPKVFLMDEPLSNLDAKLRVQMRAE 172
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1720366319 680 IRAIIKNTDRGALLTTHYMAEAEALCDRVAILVSGRLRCIG 720
Cdd:cd03301 173 LKRLQQRLGTTTIYVTHDQVEAMTMADRIAVMNDGQIQQIG 213
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
527-720 |
2.64e-26 |
|
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: 106.37 E-value: 2.64e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366319 527 RNVSFCVRKGEILGLLGHNGAGKSTSLKMISGDTKVTAGQVLLKGSREGDTPG-----FLGYCPQenALwpnltvkehle 601
Cdd:cd03214 16 DDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDGKDLASLSPkelarKIAYVPQ--AL----------- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366319 602 ifaavrglrkshAAVAITRLADalklqdqlkSPVKTLSEGVKRKLCFVLSILGNPSILLLDEPSTGLDPEGQQQIWQAIR 681
Cdd:cd03214 83 ------------ELLGLAHLAD---------RPFNELSGGERQRVLLARALAQEPPILLLDEPTSHLDIAHQIELLELLR 141
|
170 180 190
....*....|....*....|....*....|....*....
gi 1720366319 682 AIIKNTDRGALLTTHYMAEAEALCDRVAILVSGRLRCIG 720
Cdd:cd03214 142 RLARERGKTVVMVLHDLNLAARYADRVILLKDGRIVAQG 180
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
495-725 |
8.78e-26 |
|
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440740 [Multi-domain] Cd Length: 514 Bit Score: 112.30 E-value: 8.78e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366319 495 DEKPVIIASCLRKEYAGKqkhclsKKKAKIATRNVSFCVRKGEILGLLGHNGAGKSTSLKMISGDTKVTAGQVLLKG--- 571
Cdd:COG1123 256 AAEPLLEVRNLSKRYPVR------GKGGVRAVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRPTSGSILFDGkdl 329
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366319 572 --SREGDTPGF---LGYCPQ--ENALWPNLTVKEHLEIFAAVRGLRKSHAAVAitRLADALKL----QDQLKSPVKTLSE 640
Cdd:COG1123 330 tkLSRRSLRELrrrVQMVFQdpYSSLNPRMTVGDIIAEPLRLHGLLSRAERRE--RVAELLERvglpPDLADRYPHELSG 407
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366319 641 GVKRKLCFVLSILGNPSILLLDEPSTGLDPEGQQQIWQAIRAIIKNTDRGALLTTHYMAEAEALCDRVAILVSGRLRCIG 720
Cdd:COG1123 408 GQRQRVAIARALALEPKLLILDEPTSALDVSVQAQILNLLRDLQRELGLTYLFISHDLAVVRYIADRVAVMYDGRIVEDG 487
|
....*
gi 1720366319 721 SIQHL 725
Cdd:COG1123 488 PTEEV 492
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
505-725 |
3.29e-25 |
|
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: 104.97 E-value: 3.29e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366319 505 LRKEYAGKqkhclskKKAKIATRNVSFCVRKGEILGLLGHNGAGKSTSLKMISGDTKVTAGQVLLKGSREGDTPGF---- 580
Cdd:cd03258 7 VSKVFGDT-------GGKVTALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGSVLVDGTDLTLLSGKelrk 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366319 581 ----LGYCPQENALWPNLTVKEHLEIFAAVRGLRKSHAAVAITRLADALKLQDQLKSPVKTLSEGVKRKLCFVLSILGNP 656
Cdd:cd03258 80 arrrIGMIFQHFNLLSSRTVFENVALPLEIAGVPKAEIEERVLELLELVGLEDKADAYPAQLSGGQKQRVGIARALANNP 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1720366319 657 SILLLDEPSTGLDPEGQQQIWQAIRAIIKNTDRGALLTTHYMAEAEALCDRVAILVSGRLRCIGSIQHL 725
Cdd:cd03258 160 KVLLCDEATSALDPETTQSILALLRDINRELGLTIVLITHEMEVVKRICDRVAVMEKGEVVEEGTVEEV 228
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
527-696 |
5.71e-25 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 103.42 E-value: 5.71e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366319 527 RNVSFCVRKGEILGLLGHNGAGKSTSLKMISGDTKVTAGQVLLKGSREGDT--PGFLGYCPQENALWPNLTVKEHLEIFA 604
Cdd:PRK13539 19 SGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDGGDIDDPdvAEACHYLGHRNAMKPALTVAENLEFWA 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366319 605 AVRGLRKSHAAVAItrlaDALKLQDQLKSPVKTLSEGVKRKLCFVLSILGNPSILLLDEPSTGLDPEGQQQIWQAIRAii 684
Cdd:PRK13539 99 AFLGGEELDIAAAL----EAVGLAPLAHLPFGYLSAGQKRRVALARLLVSNRPIWILDEPTAALDAAAVALFAELIRA-- 172
|
170
....*....|....
gi 1720366319 685 kNTDRG--ALLTTH 696
Cdd:PRK13539 173 -HLAQGgiVIAATH 185
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
527-716 |
6.31e-25 |
|
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: 103.01 E-value: 6.31e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366319 527 RNVSFCVRKGEILGLLGHNGAGKSTSLKMISGDTKVTA--GQVLLKG--SREGDTPGFLGYCPQENALWPNLTVKEHLEI 602
Cdd:cd03213 26 KNVSGKAKPGELTAIMGPSGAGKSTLLNALAGRRTGLGvsGEVLINGrpLDKRSFRKIIGYVPQDDILHPTLTVRETLMF 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366319 603 FAAVRGLrkshaavaitrladalklqdqlkspvktlSEGVKRKLCFVLSILGNPSILLLDEPSTGLDPEGQQQIWQAIRA 682
Cdd:cd03213 106 AAKLRGL-----------------------------SGGERKRVSIALELVSNPSLLFLDEPTSGLDSSSALQVMSLLRR 156
|
170 180 190
....*....|....*....|....*....|....*
gi 1720366319 683 iIKNTDRGALLTTHY-MAEAEALCDRVAILVSGRL 716
Cdd:cd03213 157 -LADTGRTIICSIHQpSSEIFELFDKLLLLSQGRV 190
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
527-715 |
1.42e-24 |
|
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: 103.63 E-value: 1.42e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366319 527 RNVSFCVRKGEILGLLGHNGAGKSTSLKMISGDTKVTAGQVL-LKGSREGDTPGF-----LGYCPQENALW--PNLTVke 598
Cdd:COG1119 20 DDISWTVKPGEHWAILGPNGAGKSTLLSLITGDLPPTYGNDVrLFGERRGGEDVWelrkrIGLVSPALQLRfpRDETV-- 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366319 599 hLEI----FAAVRGLRKSHAAVAITR---LADALKLQDQLKSPVKTLSEGVKRKlcfVL---SILGNPSILLLDEPSTGL 668
Cdd:COG1119 98 -LDVvlsgFFDSIGLYREPTDEQRERareLLELLGLAHLADRPFGTLSQGEQRR---VLiarALVKDPELLILDEPTAGL 173
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1720366319 669 DPEGQQQIWQAIRAIIKNTDRGALLTTHYMAEAEALCDRVAILVSGR 715
Cdd:COG1119 174 DLGARELLLALLDKLAAEGAPTLVLVTHHVEEIPPGITHVLLLKDGR 220
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
527-716 |
1.67e-24 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 102.44 E-value: 1.67e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366319 527 RNVSFCVRKGEILGLLGHNGAGKSTSLKMISGDTKVTAGQVLLKGS-----REGDTPGF---LGYCPQENALWPNLTVKE 598
Cdd:COG2884 19 SDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLVNGQdlsrlKRREIPYLrrrIGVVFQDFRLLPDRTVYE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366319 599 HLEIFAAVRGLRKSHAAvaiTRLADALK---LQDQLKSPVKTLSEGVKRKLCFVLSILGNPSILLLDEPSTGLDPEGQQQ 675
Cdd:COG2884 99 NVALPLRVTGKSRKEIR---RRVREVLDlvgLSDKAKALPHELSGGEQQRVAIARALVNRPELLLADEPTGNLDPETSWE 175
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1720366319 676 IWQAIRAIikNtDRGA--LLTTHYMAEAEALCDRVAILVSGRL 716
Cdd:COG2884 176 IMELLEEI--N-RRGTtvLIATHDLELVDRMPKRVLELEDGRL 215
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
522-725 |
8.77e-24 |
|
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: 106.77 E-value: 8.77e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366319 522 AKIATRNVSFCVRKGEILGLLGHNGAGKSTSLKMISGDTKVTAGQVLLKGS-----REGDTPGFLGYCPQENALWpNLTV 596
Cdd:COG4987 347 GRPVLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFLDPQSGSITLGGVdlrdlDEDDLRRRIAVVPQRPHLF-DTTL 425
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366319 597 KEHLEIF------AAVRglrkshAAVAITRLADALK-LQDQLKSPV----KTLSEGVKRKLCFVLSILGNPSILLLDEPS 665
Cdd:COG4987 426 RENLRLArpdatdEELW------AALERVGLGDWLAaLPDGLDTWLgeggRRLSGGERRRLALARALLRDAPILLLDEPT 499
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366319 666 TGLDPEGQQQIWQAIRAIIKntDRGALLTTHYMAEAEAlCDRVAILVSGRLRCIGSIQHL 725
Cdd:COG4987 500 EGLDAATEQALLADLLEALA--GRTVLLITHRLAGLER-MDRILVLEDGRIVEQGTHEEL 556
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
527-716 |
1.29e-23 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 105.49 E-value: 1.29e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366319 527 RNVSFCVRKGEILGLLGHNGAGKSTSLKMISGDTKVTAGQVLLKGSR-EGDTP------GfLGYCPQENALWPNLTVKEH 599
Cdd:COG1129 21 DGVSLELRPGEVHALLGENGAGKSTLMKILSGVYQPDSGEILLDGEPvRFRSPrdaqaaG-IAIIHQELNLVPNLSVAEN 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366319 600 leIF----AAVRGLRKSHAAVAITR-LADALKLQDQLKSPVKTLSEGvKRKLcfVL---SILGNPSILLLDEPSTGLDPE 671
Cdd:COG1129 100 --IFlgrePRRGGLIDWRAMRRRAReLLARLGLDIDPDTPVGDLSVA-QQQL--VEiarALSRDARVLILDEPTASLTER 174
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1720366319 672 GQQQIWQAIRAIiknTDRGA--LLTTHYMAEAEALCDRVAILVSGRL 716
Cdd:COG1129 175 EVERLFRIIRRL---KAQGVaiIYISHRLDEVFEIADRVTVLRDGRL 218
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
524-716 |
1.76e-23 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 105.11 E-value: 1.76e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366319 524 IATRNVSFCVRKGEILGLLGHNGAGKSTSLKMISGDTKVTAGQVLLKGSR-EGDTPGF-----LGYCPQENALWPNLTVK 597
Cdd:COG3845 19 VANDDVSLTVRPGEIHALLGENGAGKSTLMKILYGLYQPDSGEILIDGKPvRIRSPRDaialgIGMVHQHFMLVPNLTVA 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366319 598 EHLeIFAA--VRGLRKSHAAVA--ITRLADALKLQDQLKSPVKTLSEGVKRKLCFVLSILGNPSILLLDEPSTGLDPEGQ 673
Cdd:COG3845 99 ENI-VLGLepTKGGRLDRKAARarIRELSERYGLDVDPDAKVEDLSVGEQQRVEILKALYRGARILILDEPTAVLTPQEA 177
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1720366319 674 QQIWQAIRAIiknTDRGA--LLTTHYMAEAEALCDRVAILVSGRL 716
Cdd:COG3845 178 DELFEILRRL---AAEGKsiIFITHKLREVMAIADRVTVLRRGKV 219
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
525-747 |
1.79e-23 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 106.75 E-value: 1.79e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366319 525 ATRNVSFCVRKGEILGLLGHNGAGKSTSLKMISGDTKVTAGQVLLKGsREGDtPGFL------GYCPQENALWPNLTVKE 598
Cdd:NF033858 281 AVDHVSFRIRRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGEAWLFG-QPVD-AGDIatrrrvGYMSQAFSLYGELTVRQ 358
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366319 599 HLEIFAAVRGLRKSHAAVAITRLADALKLQDQLKSPVKTLSEGVKRKLCFVLSILGNPSILLLDEPSTGLDPEGQQQIWQ 678
Cdd:NF033858 359 NLELHARLFHLPAAEIAARVAEMLERFDLADVADALPDSLPLGIRQRLSLAVAVIHKPELLILDEPTSGVDPVARDMFWR 438
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1720366319 679 AI-------RAIIkntdrgaLLTTHYMAEAEaLCDRVAILVSGRLRCIGSIQHLKSKFGKDYLLEMKVKTLEQVEP 747
Cdd:NF033858 439 LLielsredGVTI-------FISTHFMNEAE-RCDRISLMHAGRVLASDTPAALVAARGAATLEEAFIAYLEEAAG 506
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
525-716 |
2.69e-23 |
|
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: 97.11 E-value: 2.69e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366319 525 ATRNVSFCVRKGEILGLLGHNGAGKSTSLKMISGDTKVTAGQVLLKGSRegdtpgflgycpqenalwpnltvkehleifa 604
Cdd:cd03216 15 ALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVDGKE------------------------------- 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366319 605 avrglrkshaaVAITRLADALKL------QdqlkspvktLSEGVKRKLCFVLSILGNPSILLLDEPSTGLDPEGQQQIWQ 678
Cdd:cd03216 64 -----------VSFASPRDARRAgiamvyQ---------LSVGERQMVEIARALARNARLLILDEPTAALTPAEVERLFK 123
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1720366319 679 AIRAIiknTDRGA--LLTTHYMAEAEALCDRVAILVSGRL 716
Cdd:cd03216 124 VIRRL---RAQGVavIFISHRLDEVFEIADRVTVLRDGRV 160
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
527-726 |
3.23e-23 |
|
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: 99.11 E-value: 3.23e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366319 527 RNVSFCVRKGEILGLLGHNGAGKSTSLKMISGDTKVTAGQVLLKG------SREGDTPGFL--GYCPQENALWPNLTV-- 596
Cdd:cd03261 17 KGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGedisglSEAELYRLRRrmGMLFQSGALFDSLTVfe 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366319 597 ------KEHL-----EIFAAVR------GLRkshaavaitrlADALKLQDQLkspvktlSEGVKRKLCFVLSILGNPSIL 659
Cdd:cd03261 97 nvafplREHTrlseeEIREIVLekleavGLR-----------GAEDLYPAEL-------SGGMKKRVALARALALDPELL 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1720366319 660 LLDEPSTGLDPEGQQQIWQAIRAIIKNTDRGALLTTHYMAEAEALCDRVAILVSGRLRCIGSIQHLK 726
Cdd:cd03261 159 LYDEPTAGLDPIASGVIDDLIRSLKKELGLTSIMVTHDLDTAFAIADRIAVLYDGKIVAEGTPEELR 225
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
505-721 |
3.87e-23 |
|
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: 98.85 E-value: 3.87e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366319 505 LRKEYAGKqkhclskkkakIATRNVSFCVRKGEILGLLGHNGAGKSTSLKMISGDTKVTAGQVLLKGSREGDTPGF---L 581
Cdd:cd03300 6 VSKFYGGF-----------VALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGKDITNLPPHkrpV 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366319 582 GYCPQENALWPNLTVKEHLEIFAAVRGLRKSHAAVAITRLADALKLQDQLKSPVKTLSEGVKRKLCFVLSILGNPSILLL 661
Cdd:cd03300 75 NTVFQNYALFPHLTVFENIAFGLRLKKLPKAEIKERVAEALDLVQLEGYANRKPSQLSGGQQQRVAIARALVNEPKVLLL 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366319 662 DEPSTGLDPEGQQQIWQAIRAIIKNTDRGALLTTHYMAEAEALCDRVAILVSGRLRCIGS 721
Cdd:cd03300 155 DEPLGALDLKLRKDMQLELKRLQKELGITFVFVTHDQEEALTMSDRIAVMNKGKIQQIGT 214
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
527-726 |
9.12e-23 |
|
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: 98.13 E-value: 9.12e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366319 527 RNVSFCVRKGEILGLLGHNGAGKSTSLKMISGDTKVTAGQVLLKG------SREGDTP-----GFLGycpQENALWPNLT 595
Cdd:COG1127 22 DGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEILVDGqditglSEKELYElrrriGMLF---QGGALFDSLT 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366319 596 VKEHLEIfaavrGLRKsHaavaiTRLADALKlqDQLkspvktlsegVKRKLCFV------------LS------------ 651
Cdd:COG1127 99 VFENVAF-----PLRE-H-----TDLSEAEI--REL----------VLEKLELVglpgaadkmpseLSggmrkrvalara 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1720366319 652 ILGNPSILLLDEPSTGLDPEGQQQIWQAIRAIIKNTDRGALLTTHYMAEAEALCDRVAILVSGRLRCIGSIQHLK 726
Cdd:COG1127 156 LALDPEILLYDEPTAGLDPITSAVIDELIRELRDELGLTSVVVTHDLDSAFAIADRVAVLADGKIIAEGTPEELL 230
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
527-722 |
9.65e-23 |
|
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits of nitrate transport in bacteria and archaea. This protein belongs to the ATP-binding cassette (ABC) superfamily. It is thought that the two subunits encoded by ntrC and ntrD form the binding surface for interaction with ATP. This model is restricted in identifying ATP binding subunit associated with the nitrate transport. Nitrate assimilation is aided by other proteins derived from the operon which among others include products of ntrA - a regulatory protein; ntrB - a hydropbobic transmembrane permease and narB - a reductase. [Transport and binding proteins, Anions, Transport and binding proteins, Other]
Pssm-ID: 130252 [Multi-domain] Cd Length: 230 Bit Score: 97.54 E-value: 9.65e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366319 527 RNVSFCVRKGEILGLLGHNGAGKSTSLKMISGDTKVTAGQVLLKGsREGDTPG------FLGYcpqenALWPNLTVKEH- 599
Cdd:TIGR01184 2 KGVNLTIQQGEFISLIGHSGCGKSTLLNLISGLAQPTSGGVILEG-KQITEPGpdrmvvFQNY-----SLLPWLTVRENi 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366319 600 -LEIFAAVRGLRKSHAAVAITRLADALKLQDQLKSPVKTLSEGVKRKLCFVLSILGNPSILLLDEPSTGLDPEGQQQIWQ 678
Cdd:TIGR01184 76 aLAVDRVLPDLSKSERRAIVEEHIALVGLTEAADKRPGQLSGGMKQRVAIARALSIRPKVLLLDEPFGALDALTRGNLQE 155
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1720366319 679 AIRAIIKNTDRGALLTTHYMAEAEALCDRVAILVSGRLRCIGSI 722
Cdd:TIGR01184 156 ELMQIWEEHRVTVLMVTHDVDEALLLSDRVVMLTNGPAANIGQI 199
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
528-723 |
1.41e-22 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 97.92 E-value: 1.41e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366319 528 NVSFCVRKGEILGLLGHNGAGKSTSLKMISGDTKVTAGQVLLKGSREGDTPGF-----LGYCPQENALWPNLTVKEHLEI 602
Cdd:PRK13548 20 DVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLNGRPLADWSPAelarrRAVLPQHSSLSFPFTVEEVVAM 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366319 603 FAAVRGLRKSHAAVAIT---RLADALKLQDqlkSPVKTLSEGVK------RKLCFVLSILGNPSILLLDEPSTGLDPEGQ 673
Cdd:PRK13548 100 GRAPHGLSRAEDDALVAaalAQVDLAHLAG---RDYPQLSGGEQqrvqlaRVLAQLWEPDGPPRWLLLDEPTSALDLAHQ 176
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1720366319 674 QQIWQAIRAIIKNTDRGALLTTHYMAEAEALCDRVAILVSGRLRCIGSIQ 723
Cdd:PRK13548 177 HHVLRLARQLAHERGLAVIVVLHDLNLAARYADRIVLLHQGRLVADGTPA 226
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
527-715 |
3.11e-22 |
|
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: 94.37 E-value: 3.11e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366319 527 RNVSFCVRKGEILGLLGHNGAGKSTSLKMISGDTKVTAGQVL-----LKGSREGDTPGFLGYCPQENALWpNLTVKEHLe 601
Cdd:cd03228 19 KDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILidgvdLRDLDLESLRKNIAYVPQDPFLF-SGTIRENI- 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366319 602 ifaavrglrkshaavaitrladalklqdqlkspvktLSEGVKRKLCFVLSILGNPSILLLDEPSTGLDPEGQQQIWQAIR 681
Cdd:cd03228 97 ------------------------------------LSGGQRQRIAIARALLRDPPILILDEATSALDPETEALILEALR 140
|
170 180 190
....*....|....*....|....*....|....
gi 1720366319 682 AIIKntDRGALLTTHYMAEAEaLCDRVAILVSGR 715
Cdd:cd03228 141 ALAK--GKTVIVIAHRLSTIR-DADRIIVLDDGR 171
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
527-735 |
3.51e-22 |
|
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: 102.22 E-value: 3.51e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366319 527 RNVSFCVRKGEILGLLGHNGAGKSTSLKMISGDTKVTAGQVLLKGS--REGDTPGF---LGYCPQENALWP-----NLTV 596
Cdd:COG2274 492 DNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEPTSGRILIDGIdlRQIDPASLrrqIGVVLQDVFLFSgtireNITL 571
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366319 597 -KEHLEIFAAVRGLRKSHAavaitrLADALKLQDQLKSPV----KTLSEGVKRKLCFVLSILGNPSILLLDEPSTGLDPE 671
Cdd:COG2274 572 gDPDATDEEIIEAARLAGL------HDFIEALPMGYDTVVgeggSNLSGGQRQRLAIARALLRNPRILILDEATSALDAE 645
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1720366319 672 GQQQIWQAIRAIIKNtdRGALLTTHYMAEAeALCDRVAILVSGRLRCIGSIQHLKSKFGKDYLL 735
Cdd:COG2274 646 TEAIILENLRRLLKG--RTVIIIAHRLSTI-RLADRIIVLDKGRIVEDGTHEELLARKGLYAEL 706
|
|
| PhnC |
COG3638 |
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and ... |
498-716 |
3.59e-22 |
|
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 442855 [Multi-domain] Cd Length: 249 Bit Score: 96.66 E-value: 3.59e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366319 498 PVIIASCLRKEYAGKQKhclskkkakiATRNVSFCVRKGEILGLLGHNGAGKSTSLKMISGDTKVTAGQVLLKGSREGDT 577
Cdd:COG3638 1 PMLELRNLSKRYPGGTP----------ALDDVSLEIERGEFVALIGPSGAGKSTLLRCLNGLVEPTSGEILVDGQDVTAL 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366319 578 PGF--------LGYCPQENALWPNLTVKE--------HLEIFAAVRGL-RKSHAAVAITRLaDALKLQDQLKSPVKTLSE 640
Cdd:COG3638 71 RGRalrrlrrrIGMIFQQFNLVPRLSVLTnvlagrlgRTSTWRSLLGLfPPEDRERALEAL-ERVGLADKAYQRADQLSG 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366319 641 G------VKRKLCfvlsilGNPSILLLDEPSTGLDPEGQQQIWQAIRAIikNTDRG--ALLTTHYMAEAEALCDRVAILV 712
Cdd:COG3638 150 GqqqrvaIARALV------QEPKLILADEPVASLDPKTARQVMDLLRRI--AREDGitVVVNLHQVDLARRYADRIIGLR 221
|
....
gi 1720366319 713 SGRL 716
Cdd:COG3638 222 DGRV 225
|
|
| ECF_ATPase_1 |
TIGR04520 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
523-738 |
4.81e-22 |
|
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette (ABC) proteins by homology, but belong to energy coupling factor (ECF) transport systems. The architecture in general is two ATPase subunits (or a double-length fusion protein), a T component, and a substrate capture (S) component that is highly variable, and may be interchangeable in genomes with only one T component. This model identifies many but not examples of the upstream member of the pair of ECF ATPases in Firmicutes and Mollicutes. [Transport and binding proteins, Unknown substrate]
Pssm-ID: 275313 [Multi-domain] Cd Length: 268 Bit Score: 96.73 E-value: 4.81e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366319 523 KIATRNVSFCVRKGEILGLLGHNGAGKSTSLKMISGDTKVTAGQVLLKGSREGDtpgflgycpqENALW----------- 591
Cdd:TIGR04520 15 KPALKNVSLSIEKGEFVAIIGHNGSGKSTLAKLLNGLLLPTSGKVTVDGLDTLD----------EENLWeirkkvgmvfq 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366319 592 -P-----NLTVKE------------HLEIfaavrglrkshaavaITRLADALK---LQDQLKSPVKTLSEGVKRKLCfVL 650
Cdd:TIGR04520 85 nPdnqfvGATVEDdvafglenlgvpREEM---------------RKRVDEALKlvgMEDFRDREPHLLSGGQKQRVA-IA 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366319 651 SILG-NPSILLLDEPSTGLDPEGQQQIWQAIRAIIKNTDRGALLTTHYMAEAeALCDRVAILVSGRLRCIGSIQHLKSKf 729
Cdd:TIGR04520 149 GVLAmRPDIIILDEATSMLDPKGRKEVLETIRKLNKEEGITVISITHDMEEA-VLADRVIVMNKGKIVAEGTPREIFSQ- 226
|
....*....
gi 1720366319 730 gKDYLLEMK 738
Cdd:TIGR04520 227 -VELLKEIG 234
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
519-716 |
4.83e-22 |
|
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: 95.42 E-value: 4.83e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366319 519 KKKAKIATRNVSFCVRKGEILGLLGHNGAGKSTSLKMISG---DTKVTAGQVLLKG--SREGDTPGFLGYCPQENALWPN 593
Cdd:cd03234 16 WNKYARILNDVSLHVESGQVMAILGSSGSGKTTLLDAISGrveGGGTTSGQILFNGqpRKPDQFQKCVAYVRQDDILLPG 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366319 594 LTVKEHLEIFAAVRGLRKSHAA-------------VAITRLADALklqdqlkspVKTLSEGVKRKLCFVLSILGNPSILL 660
Cdd:cd03234 96 LTVRETLTYTAILRLPRKSSDAirkkrvedvllrdLALTRIGGNL---------VKGISGGERRRVSIAVQLLWDPKVLI 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1720366319 661 LDEPSTGLDPEGQQQIWQAIRAIIKnTDRGALLTTHY-MAEAEALCDRVAILVSGRL 716
Cdd:cd03234 167 LDEPTSGLDSFTALNLVSTLSQLAR-RNRIVILTIHQpRSDLFRLFDRILLLSSGEI 222
|
|
| ECF_ATPase_2 |
TIGR04521 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
522-721 |
6.59e-22 |
|
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette (ABC) proteins by homology, but belong to energy coupling factor (ECF) transport systems. The architecture in general is two ATPase subunits (or a double-length fusion protein), a T component, and a substrate capture (S) component that is highly variable, and may be interchangeable in genomes with only one T component. This model identifies many but not examples of the downstream member of the pair of ECF ATPases in Firmicutes and Mollicutes. [Transport and binding proteins, Unknown substrate]
Pssm-ID: 275314 [Multi-domain] Cd Length: 277 Bit Score: 96.37 E-value: 6.59e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366319 522 AKIATRNVSFCVRKGEILGLLGHNGAGKSTSLKMISGDTKVTAGQVLLKGSREGDTPGF--------LGYCPQ--ENALW 591
Cdd:TIGR04521 17 EKKALDDVSLTIEDGEFVAIIGHTGSGKSTLIQHLNGLLKPTSGTVTIDGRDITAKKKKklkdlrkkVGLVFQfpEHQLF 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366319 592 PNlTVKEhlEI-FAAVR-GLRKSHAAVAITRLADALKLQDQL--KSPVKtLSEGVKRKLCF--VLSIlgNPSILLLDEPS 665
Cdd:TIGR04521 97 EE-TVYK--DIaFGPKNlGLSEEEAEERVKEALELVGLDEEYleRSPFE-LSGGQMRRVAIagVLAM--EPEVLILDEPT 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1720366319 666 TGLDPEGQQQIWQAIRAIIKNTDRGALLTTHYMAEAEALCDRVAILVSGRLRCIGS 721
Cdd:TIGR04521 171 AGLDPKGRKEILDLFKRLHKEKGLTVILVTHSMEDVAEYADRVIVMHKGKIVLDGT 226
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
522-716 |
1.16e-21 |
|
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: 93.27 E-value: 1.16e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366319 522 AKIATRNVSFCVRKGEILGLLGHNGAGKSTSLKMISGDTKVTAGQVLLKGSR-EGDTPGF-----LGYCP---QENALWP 592
Cdd:cd03215 12 VKGAVRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITLDGKPvTRRSPRDairagIAYVPedrKREGLVL 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366319 593 NLTVKEHLeifaavrglrkshaavAITRLadalklqdqlkspvktLSEGVKRKLCFVLSILGNPSILLLDEPSTGLDPEG 672
Cdd:cd03215 92 DLSVAENI----------------ALSSL----------------LSGGNQQKVVLARWLARDPRVLILDEPTRGVDVGA 139
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1720366319 673 QQQIWQAIRAIiknTDRGA--LLTTHYMAEAEALCDRVAILVSGRL 716
Cdd:cd03215 140 KAEIYRLIREL---ADAGKavLLISSELDELLGLCDRILVMYEGRI 182
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
523-715 |
1.46e-21 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 95.15 E-value: 1.46e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366319 523 KIATRNVSFCVRKGEILGLLGHNGAGKSTSLKMISGDTKVTAGQVLLKG---------------SREGDTPgFLGYCPqe 587
Cdd:COG1101 19 KRALDGLNLTIEEGDFVTVIGSNGAGKSTLLNAIAGSLPPDSGSILIDGkdvtklpeykrakyiGRVFQDP-MMGTAP-- 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366319 588 nalwpNLTVKEHLEIfAAVRG--------LRKSHAAVAITRLAD-ALKLQDQLKSPVKTLSEGVKRKLCFVLSILGNPSI 658
Cdd:COG1101 96 -----SMTIEENLAL-AYRRGkrrglrrgLTKKRRELFRELLATlGLGLENRLDTKVGLLSGGQRQALSLLMATLTKPKL 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1720366319 659 LLLDEPSTGLDPEGQQQIWQAIRAIIKNTDRGALLTTHYMAEAEALCDRVAILVSGR 715
Cdd:COG1101 170 LLLDEHTAALDPKTAALVLELTEKIVEENNLTTLMVTHNMEQALDYGNRLIMMHEGR 226
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
525-716 |
2.10e-21 |
|
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: 93.42 E-value: 2.10e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366319 525 ATRNVSFCVRKGEILGLLGHNGAGKSTSLKMISGDTKVTAGQVLLKGS----------REGdtpgfLGYCPQENALWpNL 594
Cdd:cd03245 19 ALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGTdirqldpadlRRN-----IGYVPQDVTLF-YG 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366319 595 TVKEHLEIFAAV----RGLRKSHAAVA---ITRLADALKLQDQLKSpvKTLSEGVKRKLCFVLSILGNPSILLLDEPSTG 667
Cdd:cd03245 93 TLRDNITLGAPLaddeRILRAAELAGVtdfVNKHPNGLDLQIGERG--RGLSGGQRQAVALARALLNDPPILLLDEPTSA 170
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1720366319 668 LDPEGQQQIWQAIRAIIKntDRGALLTTHYMAeAEALCDRVAILVSGRL 716
Cdd:cd03245 171 MDMNSEERLKERLRQLLG--DKTLIIITHRPS-LLDLVDRIIVMDSGRI 216
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
525-728 |
5.16e-21 |
|
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease components [Energy production and conversion, Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 444012 [Multi-domain] Cd Length: 563 Bit Score: 97.91 E-value: 5.16e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366319 525 ATRNVSFCVRKGEILGLLGHNGAGKSTSLKMISGDTKVTAGQVLLKGS--REGDTPGF---LGYCPQeNALWPNLTVKEH 599
Cdd:COG4988 352 ALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPPYSGSILINGVdlSDLDPASWrrqIAWVPQ-NPYLFAGTIREN 430
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366319 600 LEIFAAVRGLRKSHAAVAITRLADALK-LQDQLKSPV----KTLSEGVKRKLCFVLSILGNPSILLLDEPSTGLDPEGQQ 674
Cdd:COG4988 431 LRLGRPDASDEELEAALEAAGLDEFVAaLPDGLDTPLgeggRGLSGGQAQRLALARALLRDAPLLLLDEPTAHLDAETEA 510
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1720366319 675 QIWQAIRAIIKntDRGALLTTHYMAEAeALCDRVAILVSGRLRCIGSIQHLKSK 728
Cdd:COG4988 511 EILQALRRLAK--GRTVILITHRLALL-AQADRILVLDDGRIVEQGTHEELLAK 561
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
499-721 |
6.16e-21 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 92.65 E-value: 6.16e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366319 499 VIIASCLRKEYAGKQkhclskkkakiATRNVSFCVRKGEILGLLGHNGAGKSTSLKMISGDTKVTAGQVLLKG------- 571
Cdd:PRK10895 3 TLTAKNLAKAYKGRR-----------VVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDedisllp 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366319 572 ----SREGdtpgfLGYCPQENALWPNLTVKEHLEIFAAVR-GLRKSHAAVAITRLADALKLQDQLKSPVKTLSEGVKRKL 646
Cdd:PRK10895 72 lharARRG-----IGYLPQEASIFRRLSVYDNLMAVLQIRdDLSAEQREDRANELMEEFHIEHLRDSMGQSLSGGERRRV 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1720366319 647 CFVLSILGNPSILLLDEPSTGLDPEGQQQIWQAIRAiIKNTDRGALLTTHYMAEAEALCDRVAILVSGRLRCIGS 721
Cdd:PRK10895 147 EIARALAANPKFILLDEPFAGVDPISVIDIKRIIEH-LRDSGLGVLITDHNVRETLAVCERAYIVSQGHLIAHGT 220
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
497-671 |
1.38e-20 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 96.29 E-value: 1.38e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366319 497 KPVIIASCLRKEYAGKqkhclskkkaKIAtRNVSFCVRKGEILGLLGHNGAGKSTSLKMISGDTKVTAGQVllkgsREGD 576
Cdd:COG0488 313 KKVLELEGLSKSYGDK----------TLL-DDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPDSGTV-----KLGE 376
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366319 577 TpGFLGYCPQENA-LWPNLTVKEHLEifAAVRGLRKSHaavAITRLADALKLQDQLKSPVKTLSEGVKRKLCFVLSILGN 655
Cdd:COG0488 377 T-VKIGYFDQHQEeLDPDKTVLDELR--DGAPGGTEQE---VRGYLGRFLFSGDDAFKPVGVLSGGEKARLALAKLLLSP 450
|
170
....*....|....*.
gi 1720366319 656 PSILLLDEPSTGLDPE 671
Cdd:COG0488 451 PNVLLLDEPTNHLDIE 466
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
527-714 |
2.75e-20 |
|
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of the ABC component of a cobalt transport family found in bacteria, archaea, and eukaryota. The transition metal cobalt is an essential component of many enzymes and must be transported into cells in appropriate amounts when needed. The CbiMNQO family ABC transport system is involved in cobalt transport in association with the cobalamin (vitamin B12) biosynthetic pathways. Most cobalt (Cbi) transport systems possess a separate CbiN component, the cobalt-binding periplasmic protein, and they are encoded by the conserved gene cluster cbiMNQO. Both the CbiM and CbiQ proteins are integral cytoplasmic membrane proteins, and the CbiO protein has the linker peptide and the Walker A and B motifs commonly found in the ATPase components of the ABC-type transport systems.
Pssm-ID: 213193 [Multi-domain] Cd Length: 205 Bit Score: 90.01 E-value: 2.75e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366319 527 RNVSFCVRKGEILGLLGHNGAGKSTSLKMISGDTKVTAGQVLLKGSR--EGDTPGFLGYCPQEnalwPNL-----TVKEH 599
Cdd:cd03226 17 DDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLNGKPikAKERRKSIGYVMQD----VDYqlftdSVREE 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366319 600 LEIfaavrGLRKSHAAVAITR-LADALKLQD-QLKSPvKTLSEGVKRKLCFVLSILGNPSILLLDEPSTGLDPEGQQQIW 677
Cdd:cd03226 93 LLL-----GLKELDAGNEQAEtVLKDLDLYAlKERHP-LSLSGGQKQRLAIAAALLSGKDLLIFDEPTSGLDYKNMERVG 166
|
170 180 190
....*....|....*....|....*....|....*..
gi 1720366319 678 QAIRaIIKNTDRGALLTTHYMAEAEALCDRVAILVSG 714
Cdd:cd03226 167 ELIR-ELAAQGKAVIVITHDYEFLAKVCDRVLLLANG 202
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
525-734 |
3.09e-20 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 93.75 E-value: 3.09e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366319 525 ATRNVSFCVRKGEILGLLGHNGAGKSTSLKMISGDTKVTAGQVLLKGSREGDTPGF---LGYCPQENALWPNLTVKEHLE 601
Cdd:PRK11607 34 AVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVDLSHVPPYqrpINMMFQSYALFPHMTVEQNIA 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366319 602 IFAAVRGLRKSHAAVAITRLADALKLQDQLKSPVKTLSEGVKRKLCFVLSILGNPSILLLDEPSTGLDPEGQQQIWQAIR 681
Cdd:PRK11607 114 FGLKQDKLPKAEIASRVNEMLGLVHMQEFAKRKPHQLSGGQRQRVALARSLAKRPKLLLLDEPMGALDKKLRDRMQLEVV 193
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1720366319 682 AIIKNTDRGALLTTHYMAEAEALCDRVAILVSGRLRCIGS----IQHLKSKFGKDYL 734
Cdd:PRK11607 194 DILERVGVTCVMVTHDQEEAMTMAGRIAIMNRGKFVQIGEpeeiYEHPTTRYSAEFI 250
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
517-720 |
6.68e-20 |
|
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: 90.40 E-value: 6.68e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366319 517 LSKKKAKIATRNVSFCVRKGEILGLLGHNGAGKSTSLKMISGDTKVTAGQVLLKGsreGDTPGF------------LGYC 584
Cdd:cd03294 31 LKKTGQTVGVNDVSLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGKVLIDG---QDIAAMsrkelrelrrkkISMV 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366319 585 PQENALWPNLTVKEHLEIFAAVRGLRKshaAVAITRLADALK---LQDQLKSPVKTLSEGVKRKLCFVLSILGNPSILLL 661
Cdd:cd03294 108 FQSFALLPHRTVLENVAFGLEVQGVPR---AEREERAAEALElvgLEGWEHKYPDELSGGMQQRVGLARALAVDPDILLM 184
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1720366319 662 DEPSTGLDP----EGQQQIWQairaIIKNTDRGALLTTHYMAEAEALCDRVAILVSGRLRCIG 720
Cdd:cd03294 185 DEAFSALDPlirrEMQDELLR----LQAELQKTIVFITHDLDEALRLGDRIAIMKDGRLVQVG 243
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
527-716 |
1.34e-19 |
|
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: 86.89 E-value: 1.34e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366319 527 RNVSFCVRKGEILGLLGHNGAGKSTSLKMISGDTKVTAGQVLLKGS-----REGDTPGFLGYCPQENALWPNlTVKEHLe 601
Cdd:cd03246 19 RNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDGAdisqwDPNELGDHVGYLPQDDELFSG-SIAENI- 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366319 602 ifaavrglrkshaavaitrladalklqdqlkspvktLSEGVKRKLCFVLSILGNPSILLLDEPSTGLDPEGQQQIWQAIR 681
Cdd:cd03246 97 ------------------------------------LSGGQRQRLGLARALYGNPRILVLDEPNSHLDVEGERALNQAIA 140
|
170 180 190
....*....|....*....|....*....|....*..
gi 1720366319 682 AIIKntdRGA--LLTTHYMaEAEALCDRVAILVSGRL 716
Cdd:cd03246 141 ALKA---AGAtrIVIAHRP-ETLASADRILVLEDGRV 173
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
525-716 |
1.79e-19 |
|
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: 90.11 E-value: 1.79e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366319 525 ATRNVSFCVRKGEILGLLGHNGAGKSTSLKMISG---DTKVTAGQVLLKGS-------------REGDtpgfLGYCPQE- 587
Cdd:COG0444 20 AVDGVSFDVRRGETLGLVGESGSGKSTLARAILGllpPPGITSGEILFDGEdllklsekelrkiRGRE----IQMIFQDp 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366319 588 -NALWPNLTVKEHL-EIFAAVRGLRKshaAVAITRLADALKLQdQLKSPVKT-------LSEGVKRKLCFVLSILGNPSI 658
Cdd:COG0444 96 mTSLNPVMTVGDQIaEPLRIHGGLSK---AEARERAIELLERV-GLPDPERRldrypheLSGGMRQRVMIARALALEPKL 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1720366319 659 LLLDEPSTGLDPEGQQQIWQAIRAIIKNTDRGALLTTHYMAEAEALCDRVAILVSGRL 716
Cdd:COG0444 172 LIADEPTTALDVTIQAQILNLLKDLQRELGLAILFITHDLGVVAEIADRVAVMYAGRI 229
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
520-721 |
2.74e-19 |
|
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: 88.13 E-value: 2.74e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366319 520 KKAKIATRNVSFCVRKGEILGLLGHNGAGKSTSLKMISGDTKVTAGQVLLKGSREGDTPGF-----LGYCPQENALWPNL 594
Cdd:cd03295 11 GGGKKAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGEDIREQDPVelrrkIGYVIQQIGLFPHM 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366319 595 TVKEHLeifAAVRGLRKSHAAVAITRLADALKLQDQlkSPVK-------TLSEGVKRKLCFVLSILGNPSILLLDEPSTG 667
Cdd:cd03295 91 TVEENI---ALVPKLLKWPKEKIRERADELLALVGL--DPAEfadryphELSGGQQQRVGVARALAADPPLLLMDEPFGA 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1720366319 668 LDPEGQQQIWQAIRAIIKNTDRGALLTTHYMAEAEALCDRVAILVSGRLRCIGS 721
Cdd:cd03295 166 LDPITRDQLQEEFKRLQQELGKTIVFVTHDIDEAFRLADRIAIMKNGEIVQVGT 219
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
527-716 |
2.94e-19 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 92.00 E-value: 2.94e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366319 527 RNVSFCVRKGEILGLLGHNGAGKSTSLKMISGDTKVTAGQVLLKGSR-EGDTP------GfLGYCP---QENALWPNLTV 596
Cdd:COG1129 269 RDVSFSVRAGEILGIAGLVGAGRTELARALFGADPADSGEIRLDGKPvRIRSPrdairaG-IAYVPedrKGEGLVLDLSI 347
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366319 597 KE-----HLEIFAAVRGLRKSHAAVAITRLADALKL----QDQlksPVKTLSEGVKRKLcfVLS--ILGNPSILLLDEPS 665
Cdd:COG1129 348 REnitlaSLDRLSRGGLLDRRRERALAEEYIKRLRIktpsPEQ---PVGNLSGGNQQKV--VLAkwLATDPKVLILDEPT 422
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1720366319 666 TGLDPEGQQQIWQAIRAIiknTDRGA--LLTTHYMAEAEALCDRVAILVSGRL 716
Cdd:COG1129 423 RGIDVGAKAEIYRLIREL---AAEGKavIVISSELPELLGLSDRILVMREGRI 472
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
525-762 |
4.23e-19 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 92.88 E-value: 4.23e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366319 525 ATRNVSFCVRKGEILGLLGHNGAGKSTSLKMISGDTKVTAGQV-LLKGS------REGDTPGfLGYCPQ---ENaLWPNL 594
Cdd:NF033858 16 ALDDVSLDIPAGCMVGLIGPDGVGKSSLLSLIAGARKIQQGRVeVLGGDmadarhRRAVCPR-IAYMPQglgKN-LYPTL 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366319 595 TVKEHLEIFAAVRGLRKSHAAVAITRLADALKLQDQLKSPVKTLSEGVKRK--LCFVLsiLGNPSILLLDEPSTGLDPEG 672
Cdd:NF033858 94 SVFENLDFFGRLFGQDAAERRRRIDELLRATGLAPFADRPAGKLSGGMKQKlgLCCAL--IHDPDLLILDEPTTGVDPLS 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366319 673 QQQIWQAIRAIikNTDRGA---LLTTHYMAEAEAlCDRVAILVSGRLRCIGSIQHLKSKFGKDyllemkvkTLEQVepln 749
Cdd:NF033858 172 RRQFWELIDRI--RAERPGmsvLVATAYMEEAER-FDWLVAMDAGRVLATGTPAELLARTGAD--------TLEAA---- 236
|
250
....*....|...
gi 1720366319 750 teILRLFPQASRQ 762
Cdd:NF033858 237 --FIALLPEEKRR 247
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
525-716 |
4.47e-19 |
|
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: 86.69 E-value: 4.47e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366319 525 ATRNVSFCVRKGEILGLLGHNGAGKSTSLKMISGDTKVTAGQVLLKGSREGDTPG--------FLGYCPQENALWPNLTV 596
Cdd:cd03292 16 ALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQDVSDLRGraipylrrKIGVVFQDFRLLPDRNV 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366319 597 KEHLEIfaAVRGLRKSHAAVAiTRLADALKLQDqLKSPVKT----LSEGVKRKLCFVLSILGNPSILLLDEPSTGLDPEg 672
Cdd:cd03292 96 YENVAF--ALEVTGVPPREIR-KRVPAALELVG-LSHKHRAlpaeLSGGEQQRVAIARAIVNSPTILIADEPTGNLDPD- 170
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1720366319 673 qqQIWQAIRAIIKNTDRGA--LLTTHYMAEAEALCDRVAILVSGRL 716
Cdd:cd03292 171 --TTWEIMNLLKKINKAGTtvVVATHAKELVDTTRHRVIALERGKL 214
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
525-721 |
4.78e-19 |
|
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex cysAWTP involved in sulfate import. Responsible for energy coupling to the transport system. The complex is composed of two ATP-binding proteins (cysA), two transmembrane proteins (cysT and cysW), and a solute-binding protein (cysP). ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213263 [Multi-domain] Cd Length: 239 Bit Score: 87.39 E-value: 4.78e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366319 525 ATRNVSFCVRKGEILGLLGHNGAGKSTSLKMISGDTKVTAGQVLLKGSREGDTPGF---LGYCPQENALWPNLTVKEHLE 601
Cdd:cd03296 17 ALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGGEDATDVPVQernVGFVFQHYALFRHMTVFDNVA 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366319 602 IFAAVRGLRKSHAAVAITRLADAL-------KLQDQLKSpvkTLSEGVKRKLCFVLSILGNPSILLLDEPSTGLDPEGQQ 674
Cdd:cd03296 97 FGLRVKPRSERPPEAEIRAKVHELlklvqldWLADRYPA---QLSGGQRQRVALARALAVEPKVLLLDEPFGALDAKVRK 173
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1720366319 675 QIWQAIRAIIKNTDRGALLTTHYMAEAEALCDRVAILVSGRLRCIGS 721
Cdd:cd03296 174 ELRRWLRRLHDELHVTTVFVTHDQEEALEVADRVVVMNKGRIEQVGT 220
|
|
| cbiO |
TIGR01166 |
cobalt transport protein ATP-binding subunit; This model describes the ATP binding subunit of ... |
525-683 |
5.27e-19 |
|
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: 85.55 E-value: 5.27e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366319 525 ATRNVSFCVRKGEILGLLGHNGAGKSTSLKMISGDTKVTAGQVLLKG-----SREG---------------DTPGFLGYC 584
Cdd:TIGR01166 7 VLKGLNFAAERGEVLALLGANGAGKSTLLLHLNGLLRPQSGAVLIDGepldySRKGllerrqrvglvfqdpDDQLFAADV 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366319 585 PQENALWP-NLTVKEHlEIFAAVRGlrkshaavAITrladALKLQDQLKSPVKTLSEGVKRKLCFVLSILGNPSILLLDE 663
Cdd:TIGR01166 87 DQDVAFGPlNLGLSEA-EVERRVRE--------ALT----AVGASGLRERPTHCLSGGEKKRVAIAGAVAMRPDVLLLDE 153
|
170 180
....*....|....*....|
gi 1720366319 664 PSTGLDPEGQQQIWQAIRAI 683
Cdd:TIGR01166 154 PTAGLDPAGREQMLAILRRL 173
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
525-716 |
8.15e-19 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 90.74 E-value: 8.15e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366319 525 ATRNVSFCVRKGEILGLLGHNGAGKSTSLKMISGDTKVTAGQVLLKGS--REGDTPGFLG------YcpQENALWPNLTV 596
Cdd:PRK11288 19 ALDDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSILIDGQemRFASTTAALAagvaiiY--QELHLVPEMTV 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366319 597 KEHLEI--FAAVRGLRKSHAAVAITRLA-DALKLQDQLKSPVKTLSEGVKRKLCFVLSILGNPSILLLDEPSTGLDPEGQ 673
Cdd:PRK11288 97 AENLYLgqLPHKGGIVNRRLLNYEAREQlEHLGVDIDPDTPLKYLSIGQRQMVEIAKALARNARVIAFDEPTSSLSAREI 176
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1720366319 674 QQIWQAIRAiIKNTDRGALLTTHYMAEAEALCDRVAILVSGRL 716
Cdd:PRK11288 177 EQLFRVIRE-LRAEGRVILYVSHRMEEIFALCDAITVFKDGRY 218
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
527-669 |
8.90e-19 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 90.51 E-value: 8.90e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366319 527 RNVSFCVRKGEILGLLGHNGAGKSTSLKMISGDTKVTAGQVLL-KGSRegdtpgfLGYCPQENALWPNLTVKE-----HL 600
Cdd:COG0488 15 DDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEVSIpKGLR-------IGYLPQEPPLDDDLTVLDtvldgDA 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366319 601 EIFAAVRGLRKSHAAVA---------------------------ITRLADALKL-QDQLKSPVKTLSEGVKRK--LCFVL 650
Cdd:COG0488 88 ELRALEAELEELEAKLAepdedlerlaelqeefealggweaearAEEILSGLGFpEEDLDRPVSELSGGWRRRvaLARAL 167
|
170
....*....|....*....
gi 1720366319 651 siLGNPSILLLDEPSTGLD 669
Cdd:COG0488 168 --LSEPDLLLLDEPTNHLD 184
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
505-716 |
1.01e-18 |
|
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: 86.08 E-value: 1.01e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366319 505 LRKEYAGKQkhclskkkakiATRNVSFCVRKGEILGLLGHNGAGKSTSLK----MISGDTKV-TAGQVLLKGSREGDtpg 579
Cdd:cd03260 6 LNVYYGDKH-----------ALKDISLDIPKGEITALIGPSGCGKSTLLRllnrLNDLIPGApDEGEVLLDGKDIYD--- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366319 580 flgycPQENALW-----------PNL---TVKEHLEIFAAVRGLRKSHAAVAITRlaDALK---LQDQLKSPVK--TLSE 640
Cdd:cd03260 72 -----LDVDVLElrrrvgmvfqkPNPfpgSIYDNVAYGLRLHGIKLKEELDERVE--EALRkaaLWDEVKDRLHalGLSG 144
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1720366319 641 GVKRKLCFVLSILGNPSILLLDEPSTGLDPEGQQQIWQAIRAIikNTDRGALLTTHYMAEAEALCDRVAILVSGRL 716
Cdd:cd03260 145 GQQQRLCLARALANEPEVLLLDEPTSALDPISTAKIEELIAEL--KKEYTIVIVTHNMQQAARVADRTAFLLNGRL 218
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
525-730 |
1.02e-18 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 88.64 E-value: 1.02e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366319 525 ATRNVSFCVRKGEILGLLGHNGAGKSTSlkmisgdtkvtAGQVLLKGSREGDTP-GFLGYCPQENALW------------ 591
Cdd:NF000106 28 AVDGVDLDVREGTVLGVLGP*GAA**RG-----------ALPAHV*GPDAGRRPwRF*TWCANRRALRrtig*hrpvr*g 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366319 592 --PNLTVKEHLEIFAAVRGLRKSHAAVAITRLADALKLQDQLKSPVKTLSEGVKRKLCFVLSILGNPSILLLDEPSTGLD 669
Cdd:NF000106 97 rrESFSGRENLYMIGR*LDLSRKDARARADELLERFSLTEAAGRAAAKYSGGMRRRLDLAASMIGRPAVLYLDEPTTGLD 176
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1720366319 670 PEGQQQIWQAIRAIIKNtdrGA--LLTTHYMAEAEALCDRVAILVSGRLRCIGSIQHLKSKFG 730
Cdd:NF000106 177 PRTRNEVWDEVRSMVRD---GAtvLLTTQYMEEAEQLAHELTVIDRGRVIADGKVDELKTKVG 236
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
530-725 |
3.27e-18 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 84.42 E-value: 3.27e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366319 530 SFCVRKGEILGLLGHNGAGKSTSLKMISGDTKVTAGQVLLKGSREGDTPgflgycP---------QENALWPNLTVKEHL 600
Cdd:COG3840 19 DLTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILWNGQDLTALP------PaerpvsmlfQENNLFPHLTVAQNI 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366319 601 EIfaAVR-GLRKShaAVAITRLADALK---LQDQLKSPVKTLSEGVKRKL----CFVlsiLGNPsILLLDEPSTGLDPEG 672
Cdd:COG3840 93 GL--GLRpGLKLT--AEQRAQVEQALErvgLAGLLDRLPGQLSGGQRQRValarCLV---RKRP-ILLLDEPFSALDPAL 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1720366319 673 QQQIWQAIRAIIKNTDRGALLTTHYMAEAEALCDRVAILVSGRLRCIGSIQHL 725
Cdd:COG3840 165 RQEMLDLVDELCRERGLTVLMVTHDPEDAARIADRVLLVADGRIAADGPTAAL 217
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
529-720 |
3.54e-18 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 87.59 E-value: 3.54e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366319 529 VSFCVRKGEILGLLGHNGAGKSTSLKMISGDTKVTAGQVLLKG----SREGDTPG-FLGYCPQENALWPNLTVKE----- 598
Cdd:PRK09536 22 VDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGddveALSARAASrRVASVPQDTSLSFEFDVRQvvemg 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366319 599 ---HLEIFAAV-----RGLRKSHAAVAITRLADalklqdqlkSPVKTLSEGVKRKLCFVLSILGNPSILLLDEPSTGLDP 670
Cdd:PRK09536 102 rtpHRSRFDTWtetdrAAVERAMERTGVAQFAD---------RPVTSLSGGERQRVLLARALAQATPVLLLDEPTASLDI 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1720366319 671 EGQQQIWQAIRAIIkNTDRGALLTTHYMAEAEALCDRVAILVSGRLRCIG 720
Cdd:PRK09536 173 NHQVRTLELVRRLV-DDGKTAVAAIHDLDLAARYCDELVLLADGRVRAAG 221
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
527-696 |
5.86e-18 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 82.93 E-value: 5.86e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366319 527 RNVSFCVRKGEILGLLGHNGAGKSTSLKMISGDTKVTAGQVLLKG---SREGDTPG----FLGYcpqENALWPNLTVKEH 599
Cdd:PRK13538 18 SGLSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVLWQGepiRRQRDEYHqdllYLGH---QPGIKTELTALEN 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366319 600 LEIFAAVRGLrkSHAAVAITRLAdALKLQDQLKSPVKTLSEGVKRKLCFVLSILGNPSILLLDEPSTGLDPEGQQQIwqa 679
Cdd:PRK13538 95 LRFYQRLHGP--GDDEALWEALA-QVGLAGFEDVPVRQLSAGQQRRVALARLWLTRAPLWILDEPFTAIDKQGVARL--- 168
|
170
....*....|....*....
gi 1720366319 680 IRAIIKNTDRG--ALLTTH 696
Cdd:PRK13538 169 EALLAQHAEQGgmVILTTH 187
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
497-721 |
8.03e-18 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 86.15 E-value: 8.03e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366319 497 KPVIIASCLRKEYAGKQkhclskkkakiATRNVSFCVRKGEILGLLGHNGAGKSTSLKMISGDTKVTAGQVLLKGSREGD 576
Cdd:PRK09452 12 SPLVELRGISKSFDGKE-----------VISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLDGQDITH 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366319 577 TPG--------FLGYcpqenALWPNLTVKEHLEIfaavrGLR--KSHAAVAITRLADALK---LQDQLKSPVKTLSEGVK 643
Cdd:PRK09452 81 VPAenrhvntvFQSY-----ALFPHMTVFENVAF-----GLRmqKTPAAEITPRVMEALRmvqLEEFAQRKPHQLSGGQQ 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1720366319 644 RKLCFVLSILGNPSILLLDEPSTGLDPEGQQQIWQAIRAIIKNTDRGALLTTHYMAEAEALCDRVAILVSGRLRCIGS 721
Cdd:PRK09452 151 QRVAIARAVVNKPKVLLLDESLSALDYKLRKQMQNELKALQRKLGITFVFVTHDQEEALTMSDRIVVMRDGRIEQDGT 228
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
528-696 |
1.16e-17 |
|
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: 81.91 E-value: 1.16e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366319 528 NVSFCVRKGEILGLLGHNGAGKSTSLKMISG--DTKVTAGQVLLKGSREGDT-PGFLGYCPQENALWPNLTVKEHLEIFA 604
Cdd:cd03232 25 NISGYVKPGTLTALMGESGAGKTTLLDVLAGrkTAGVITGEILINGRPLDKNfQRSTGYVEQQDVHSPNLTVREALRFSA 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366319 605 AVRGLRKSHAavaitrladalklqdqlkspvKTLSEGVKrklcfvlsILGNPSILLLDEPSTGLDPEGQQQIWQAIRAII 684
Cdd:cd03232 105 LLRGLSVEQR---------------------KRLTIGVE--------LAAKPSILFLDEPTSGLDSQAAYNIVRFLKKLA 155
|
170
....*....|..
gi 1720366319 685 kNTDRGALLTTH 696
Cdd:cd03232 156 -DSGQAILCTIH 166
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
533-708 |
1.34e-17 |
|
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI), is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI's are not transport proteins and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLI's have an N-terminal Fe-S domain and two nucleotide-binding domains which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity of more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213204 [Multi-domain] Cd Length: 246 Bit Score: 83.23 E-value: 1.34e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366319 533 VRKGEILGLLGHNGAGKSTSLKMISGDTKVTAGQVLLkgsrEGDTpgfLGYCPQEnalwpnLTVKEHLEIFAAVRGLRKS 612
Cdd:cd03237 22 ISESEVIGILGPNGIGKTTFIKMLAGVLKPDEGDIEI----ELDT---VSYKPQY------IKADYEGTVRDLLSSITKD 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366319 613 HAAVA--ITRLADALKLQDQLKSPVKTLSEGVKRKLCFVLSILGNPSILLLDEPSTGLDPEGQQQIWQAIRAIIKNTDRG 690
Cdd:cd03237 89 FYTHPyfKTEIAKPLQIEQILDREVPELSGGELQRVAIAACLSKDADIYLLDEPSAYLDVEQRLMASKVIRRFAENNEKT 168
|
170
....*....|....*...
gi 1720366319 691 ALLTTHYMAEAEALCDRV 708
Cdd:cd03237 169 AFVVEHDIIMIDYLADRL 186
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
497-714 |
1.66e-17 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 86.64 E-value: 1.66e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366319 497 KPVIIASCLRKEYAGKQkhclskkkakiATRNVSFCVRKGEILGLLGHNGAGKSTSLKMISGDTKVTAGQVLLKGSREGD 576
Cdd:PRK15439 9 PPLLCARSISKQYSGVE-----------VLKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIGGNPCAR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366319 577 -TPGF---LG-Y-CPQENALWPNLTVKEHLeIFaavrGLRKSHAAVA-ITRLADALKLQDQLKSPVKTLsEGVKRKLCFV 649
Cdd:PRK15439 78 lTPAKahqLGiYlVPQEPLLFPNLSVKENI-LF----GLPKRQASMQkMKQLLAALGCQLDLDSSAGSL-EVADRQIVEI 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1720366319 650 L-SILGNPSILLLDEPSTGLDPEGQQQIWQAIRAiIKNTDRGALLTTHYMAEAEALCDRVAILVSG 714
Cdd:PRK15439 152 LrGLMRDSRILILDEPTASLTPAETERLFSRIRE-LLAQGVGIVFISHKLPEIRQLADRISVMRDG 216
|
|
| ABC_phnC |
TIGR02315 |
phosphonate ABC transporter, ATP-binding protein; Phosphonates are a class of ... |
522-716 |
1.83e-17 |
|
phosphonate ABC transporter, ATP-binding protein; Phosphonates are a class of phosphorus-containing organic compound with a stable direct C-P bond rather than a C-O-P linkage. A number of bacterial species have operons, typically about 14 genes in size, with genes for ATP-dependent transport of phosphonates, degradation, and regulation of the expression of the system. Members of this protein family are the ATP-binding cassette component of tripartite ABC transporters of phosphonates. [Transport and binding proteins, Anions]
Pssm-ID: 131368 [Multi-domain] Cd Length: 243 Bit Score: 82.73 E-value: 1.83e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366319 522 AKIATRNVSFCVRKGEILGLLGHNGAGKSTSLKMISGDTKVTAGQVLLKGSREGDTPG--------FLGYCPQENALWPN 593
Cdd:TIGR02315 14 GKQALKNINLNINPGEFVAIIGPSGAGKSTLLRCINRLVEPSSGSILLEGTDITKLRGkklrklrrRIGMIFQHYNLIER 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366319 594 LTVKEHLEI--FAAVRGLR-------KSHAAVAITRLaDALKLQDQLKSPVKTLSEGVKRKLCFVLSILGNPSILLLDEP 664
Cdd:TIGR02315 94 LTVLENVLHgrLGYKPTWRsllgrfsEEDKERALSAL-ERVGLADKAYQRADQLSGGQQQRVAIARALAQQPDLILADEP 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1720366319 665 STGLDPEGQQQIWQAIRAIIKNTDRGALLTTHYMAEAEALCDRVAILVSGRL 716
Cdd:TIGR02315 173 IASLDPKTSKQVMDYLKRINKEDGITVIINLHQVDLAKKYADRIVGLKAGEI 224
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
519-735 |
2.41e-17 |
|
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a central component of the secretion machinery that translocates the toxin, hemolysin A, in a Sec-independent fashion across both membranes of E. coli. The hemolysin A (HlyA) transport machinery is composed of the ATP-binding cassette (ABC) transporter HlyB located in the inner membrane, hemolysin D (HlyD), also anchored in the inner membrane, and TolC, which resides in the outer membrane. HlyD apparently forms a continuous channel that bridges the entire periplasm, interacting with TolC and HlyB. This arrangement prevents the appearance of periplasmic intermediates of HlyA during substrate transport. Little is known about the molecular details of HlyA transport, but it is evident that ATP-hydrolysis by the ABC-transporter HlyB is a necessary source of energy.
Pssm-ID: 213219 [Multi-domain] Cd Length: 237 Bit Score: 82.15 E-value: 2.41e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366319 519 KKKAKIATRNVSFCVRKGEILGLLGHNGAGKSTSLKMISGDTKVTAGQVLLKGSREGDT-PGFL----GYCPQENALWpN 593
Cdd:cd03252 11 KPDGPVILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGHDLALAdPAWLrrqvGVVLQENVLF-N 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366319 594 LTVKEHLeifAAVRGLRKSHAAVAITRLADALKLQDQLKSPVKT--------LSEGVKRKLCFVLSILGNPSILLLDEPS 665
Cdd:cd03252 90 RSIRDNI---ALADPGMSMERVIEAAKLAGAHDFISELPEGYDTivgeqgagLSGGQRQRIAIARALIHNPRILIFDEAT 166
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366319 666 TGLDPEGQQQIWQAIRAIIKNtdRGALLTTHYMAEAEAlCDRVAILVSGRLRCIGSIQHLKSKFGKDYLL 735
Cdd:cd03252 167 SALDYESEHAIMRNMHDICAG--RTVIIIAHRLSTVKN-ADRIIVMEKGRIVEQGSHDELLAENGLYAYL 233
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
533-716 |
2.82e-17 |
|
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: 81.39 E-value: 2.82e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366319 533 VRKGEILGLLGHNGAGKSTSLKMISGDTKVTAGQVLLKG-----SREGDTPGFLGYcpQENALWPNLTVKEHLEIfAAVR 607
Cdd:cd03298 21 FAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLINGvdvtaAPPADRPVSMLF--QENNLFAHLTVEQNVGL-GLSP 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366319 608 GLR-KSHAAVAITRLADALKLQDQLKSPVKTLSEGVKRKLCFVLSILGNPSILLLDEPSTGLDPEGQQQIWQAIRAIIKN 686
Cdd:cd03298 98 GLKlTAEDRQAIEVALARVGLAGLEKRLPGELSGGERQRVALARVLVRDKPVLLLDEPFAALDPALRAEMLDLVLDLHAE 177
|
170 180 190
....*....|....*....|....*....|
gi 1720366319 687 TDRGALLTTHYMAEAEALCDRVAILVSGRL 716
Cdd:cd03298 178 TKMTVLMVTHQPEDAKRLAQRVVFLDNGRI 207
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
515-715 |
3.54e-17 |
|
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: 81.85 E-value: 3.54e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366319 515 HCLSK--KKAKIATRNVSFCVRKGEILGLLGHNGAGKSTSLKMISGDTKVTAGQVLLKGSREGDTPGF--------LGYC 584
Cdd:cd03256 4 ENLSKtyPNGKKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGTDINKLKGKalrqlrrqIGMI 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366319 585 PQENALWPNLTVKE--------HLEIFAAVRGLRKSHAAVAITRLADALKLQDQLKSPVKTLSEGVKRKLCFVLSILGNP 656
Cdd:cd03256 84 FQQFNLIERLSVLEnvlsgrlgRRSTWRSLFGLFPKEEKQRALAALERVGLLDKAYQRADQLSGGQQQRVAIARALMQQP 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1720366319 657 SILLLDEPSTGLDPEGQQQIWQAIRAIIKNTDRGALLTTHYMAEAEALCDRVAILVSGR 715
Cdd:cd03256 164 KLILADEPVASLDPASSRQVMDLLKRINREEGITVIVSLHQVDLAREYADRIVGLKDGR 222
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
506-731 |
3.76e-17 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 85.87 E-value: 3.76e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366319 506 RKEYAGKQKHCLSKKKA-KIATRNVSFCVRKGEILGLLGHNGAGKSTSLKMIS----GDTKVtAGQVLLKGSREgDTPGF 580
Cdd:TIGR00955 20 WKQLVSRLRGCFCRERPrKHLLKNVSGVAKPGELLAVMGSSGAGKTTLMNALAfrspKGVKG-SGSVLLNGMPI-DAKEM 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366319 581 ---LGYCPQENALWPNLTVKEHLEIFAAVR---GLRKSHAAVAITRLADALKLQD------QLKSPVKTLSEGVKRKLCF 648
Cdd:TIGR00955 98 raiSAYVQQDDLFIPTLTVREHLMFQAHLRmprRVTKKEKRERVDEVLQALGLRKcantriGVPGRVKGLSGGERKRLAF 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366319 649 VLSILGNPSILLLDEPSTGLDPEGQQQIWQAIRAiIKNTDRGALLTTHY-MAEAEALCDRVAILVSGRLRCIGSIQHLKS 727
Cdd:TIGR00955 178 ASELLTDPPLLFCDEPTSGLDSFMAYSVVQVLKG-LAQKGKTIICTIHQpSSELFELFDKIILMAEGRVAYLGSPDQAVP 256
|
....
gi 1720366319 728 KFGK 731
Cdd:TIGR00955 257 FFSD 260
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
522-722 |
3.84e-17 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 82.79 E-value: 3.84e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366319 522 AKIATRNVSFCVRKGEILGLLGHNGAGKSTSLKMISGDTKVTAGQVLLKGSREGDTPGFLGYCPQENAL---WPNL---- 594
Cdd:PRK13637 19 EKKALDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDGVDITDKKVKLSDIRKKVGLvfqYPEYqlfe 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366319 595 -TVKEHLEIFAAVRGLRKSHAAVAITRLADALKLQDQL---KSPVKtLSEGVKRKLCFVLSILGNPSILLLDEPSTGLDP 670
Cdd:PRK13637 99 eTIEKDIAFGPINLGLSEEEIENRVKRAMNIVGLDYEDykdKSPFE-LSGGQKRRVAIAGVVAMEPKILILDEPTAGLDP 177
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1720366319 671 EGQQQIWQAIRAIIKNTDRGALLTTHYMAEAEALCDRVAILVSGRLRCIGSI 722
Cdd:PRK13637 178 KGRDEILNKIKELHKEYNMTIILVSHSMEDVAKLADRIIVMNKGKCELQGTP 229
|
|
| COG4559 |
COG4559 |
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism]; |
527-723 |
4.31e-17 |
|
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443620 [Multi-domain] Cd Length: 258 Bit Score: 82.09 E-value: 4.31e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366319 527 RNVSFCVRKGEILGLLGHNGAGKSTSLKMISGDTKVTAGQVLLKGSREGDTPG-----FLGYCPQENALWPNLTVKEHLE 601
Cdd:COG4559 18 DDVSLTLRPGELTAIIGPNGAGKSTLLKLLTGELTPSSGEVRLNGRPLAAWSPwelarRRAVLPQHSSLAFPFTVEEVVA 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366319 602 IFAAVRGLRKSHAAVAITR---LADALKLQDQLkspVKTLSEGVK------RKLCFVL-SILGNPSILLLDEPSTGLDPE 671
Cdd:COG4559 98 LGRAPHGSSAAQDRQIVREalaLVGLAHLAGRS---YQTLSGGEQqrvqlaRVLAQLWePVDGGPRWLFLDEPTSALDLA 174
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1720366319 672 GQQQIWQAIRAIiknTDRGA--------L-LTTHYmaeaealCDRVAILVSGRLRCIGSIQ 723
Cdd:COG4559 175 HQHAVLRLARQL---ARRGGgvvavlhdLnLAAQY-------ADRILLLHQGRLVAQGTPE 225
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
527-716 |
4.54e-17 |
|
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: 80.65 E-value: 4.54e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366319 527 RNVSFCVRKGEILGLLGHNGAGKSTSLKMISGDTKVTAGQVLLKGSREGDTPGFL-------GYCPQENALWPNLTVKEH 599
Cdd:cd03262 17 KGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIDGLKLTDDKKNInelrqkvGMVFQQFNLFPHLTVLEN 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366319 600 LeIFA--AVRGLRKShAAVAITRlaDALK---LQDQLKSPVKTLSEGVKRKLCFVLSILGNPSILLLDEPSTGLDPEGQQ 674
Cdd:cd03262 97 I-TLApiKVKGMSKA-EAEERAL--ELLEkvgLADKADAYPAQLSGGQQQRVAIARALAMNPKVMLFDEPTSALDPELVG 172
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1720366319 675 QIWQAIRAIIKnTDRGALLTTHYMAEAEALCDRVAILVSGRL 716
Cdd:cd03262 173 EVLDVMKDLAE-EGMTMVVVTHEMGFAREVADRVIFMDDGRI 213
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
529-696 |
7.07e-17 |
|
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: 79.84 E-value: 7.07e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366319 529 VSFCVRKGEILGLLGHNGAGKSTSLKMISGDTKVTAGQVLLKGSREGDTPGFLG----YCPQENALWPNLTVKEHLEIFA 604
Cdd:cd03231 19 LSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNGGPLDFQRDSIArgllYLGHAPGIKTTLSVLENLRFWH 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366319 605 AVrglrksHAAVAITRLADALKLQDQLKSPVKTLSEGVKRKLCFVLSILGNPSILLLDEPSTGLDPEGQQQIWQAIRAii 684
Cdd:cd03231 99 AD------HSDEQVEEALARVGLNGFEDRPVAQLSAGQQRRVALARLLLSGRPLWILDEPTTALDKAGVARFAEAMAG-- 170
|
170
....*....|....
gi 1720366319 685 kNTDRG--ALLTTH 696
Cdd:cd03231 171 -HCARGgmVVLTTH 183
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
527-721 |
2.56e-16 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 83.29 E-value: 2.56e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366319 527 RNVSFCVRKGEILGLLGHNGAGKSTSLKMISGDTKVTAGQVLLkgsreGDTP----------GFLGYCPQENALWpNLTV 596
Cdd:COG1132 357 KDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYDPTSGRILI-----DGVDirdltleslrRQIGVVPQDTFLF-SGTI 430
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366319 597 KEHL----------EIFAAvrgLRKSHAAVAITRLAdalklqDQLKSPV----KTLSEGVKRKLCFVLSILGNPSILLLD 662
Cdd:COG1132 431 RENIrygrpdatdeEVEEA---AKAAQAHEFIEALP------DGYDTVVgergVNLSGGQRQRIAIARALLKDPPILILD 501
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1720366319 663 EPSTGLDPEGQQQIWQAIRAIIKntDRGALLTTHYMAEAEAlCDRVAILVSGRLRCIGS 721
Cdd:COG1132 502 EATSALDTETEALIQEALERLMK--GRTTIVIAHRLSTIRN-ADRILVLDDGRIVEQGT 557
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
525-711 |
2.99e-16 |
|
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: 82.72 E-value: 2.99e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366319 525 ATRNVSFCVRKGEILGLLGHNGAGKSTSLKMISGDTKVTAGQVLLKGsreGDTPGF--------LGYCPQENALWPNlTV 596
Cdd:TIGR02857 337 ALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSIAVNG---VPLADAdadswrdqIAWVPQHPFLFAG-TI 412
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366319 597 KEHLEIF---AAVRGLRKSHAAVAITRLADALK--LQDQLKSPVKTLSEGVKRKLCFVLSILGNPSILLLDEPSTGLDPE 671
Cdd:TIGR02857 413 AENIRLArpdASDAEIREALERAGLDEFVAALPqgLDTPIGEGGAGLSGGQAQRLALARAFLRDAPLLLLDEPTAHLDAE 492
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1720366319 672 GQQQIWQAIRAIIKNtdRGALLTTHYMAEAEaLCDRVAIL 711
Cdd:TIGR02857 493 TEAEVLEALRALAQG--RTVLLVTHRLALAA-LADRIVVL 529
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
514-720 |
3.75e-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: 82.54 E-value: 3.75e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366319 514 KHCLSKKKAKI-ATRNVSFCVRKGEILGLLGHNGAGKSTSLKMISGDTKVTAGQVLLkgsREGD------TPGF------ 580
Cdd:TIGR03269 287 KRYISVDRGVVkAVDNVSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGEVNV---RVGDewvdmtKPGPdgrgra 363
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366319 581 ---LGYCPQENALWPNLTVKEHLEIFAAVR-----GLRKshaAVAITRLA--DALKLQDQLKSPVKTLSEGVKRKLCFVL 650
Cdd:TIGR03269 364 kryIGILHQEYDLYPHRTVLDNLTEAIGLElpdelARMK---AVITLKMVgfDEEKAEEILDKYPDELSEGERHRVALAQ 440
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366319 651 SILGNPSILLLDEPSTGLDPEGQQQIWQAIRAIIKNTDRGALLTTHYMAEAEALCDRVAILVSGRLRCIG 720
Cdd:TIGR03269 441 VLIKEPRIVILDEPTGTMDPITKVDVTHSILKAREEMEQTFIIVSHDMDFVLDVCDRAALMRDGKIVKIG 510
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
523-728 |
4.45e-16 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 79.26 E-value: 4.45e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366319 523 KIATRNVSFCVRKGEILGLLGHNGAGKSTSLKMISGDTKVTAGQVLLKG---SREG--DTPGFLGYCPQEnalwPN---- 593
Cdd:PRK13632 22 NNALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIDGitiSKENlkEIRKKIGIIFQN----PDnqfi 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366319 594 -LTVKEHLEIFAAVRGLRKSHAAVAITRLADALKLQDQLKSPVKTLSEGVKRKLCfVLSILG-NPSILLLDEPSTGLDPE 671
Cdd:PRK13632 98 gATVEDDIAFGLENKKVPPKKMKDIIDDLAKKVGMEDYLDKEPQNLSGGQKQRVA-IASVLAlNPEIIIFDESTSMLDPK 176
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1720366319 672 GQQQIWQAIRAIIKNTDRGALLTTHYMAEAeALCDRVAILVSGRLRCIGSIQH-LKSK 728
Cdd:PRK13632 177 GKREIKKIMVDLRKTRKKTLISITHDMDEA-ILADKVIVFSEGKLIAQGKPKEiLNNK 233
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
527-721 |
5.69e-16 |
|
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: 77.18 E-value: 5.69e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366319 527 RNVSFCVRKGEILGLLGHNGAGKSTSLKMISG--DTKVTAGQVLLKGSREGDTPgflgycPQENALwpnltvkehLEIFA 604
Cdd:cd03217 17 KGVNLTIKKGEVHALMGPNGSGKSTLAKTIMGhpKYEVTEGEILFKGEDITDLP------PEERAR---------LGIFL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366319 605 AvrglrkSHAAVAITrladALKLQDQLKSPVKTLSEGvKRKLCFVLSILG-NPSILLLDEPSTGLDPEGQQQIWQAIRAi 683
Cdd:cd03217 82 A------FQYPPEIP----GVKNADFLRYVNEGFSGG-EKKRNEILQLLLlEPDLAILDEPDSGLDIDALRLVAEVINK- 149
|
170 180 190
....*....|....*....|....*....|....*....
gi 1720366319 684 IKNTDRGALLTTHYMAEAEAL-CDRVAILVSGRLRCIGS 721
Cdd:cd03217 150 LREEGKSVLIITHYQRLLDYIkPDRVHVLYDGRIVKSGD 188
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
531-696 |
6.56e-16 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 77.58 E-value: 6.56e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366319 531 FCVRKGEILGLLGHNGAGKSTSLKMISGDTKVTAGQVLLKG--SREGDTPGFLGYCPQENALWPNLTVKEHLEIFAAVRG 608
Cdd:PRK13543 32 FHVDAGEALLVQGDNGAGKTTLLRVLAGLLHVESGQIQIDGktATRGDRSRFMAYLGHLPGLKADLSTLENLHFLCGLHG 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366319 609 LRKSH---AAVAITRLADalkLQDQLkspVKTLSEGVKRKLCFVLSILGNPSILLLDEPSTGLDPEGQQQIWQAIRAIIK 685
Cdd:PRK13543 112 RRAKQmpgSALAIVGLAG---YEDTL---VRQLSAGQKKRLALARLWLSPAPLWLLDEPYANLDLEGITLVNRMISAHLR 185
|
170
....*....|.
gi 1720366319 686 nTDRGALLTTH 696
Cdd:PRK13543 186 -GGGAALVTTH 195
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
505-716 |
1.28e-15 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 78.97 E-value: 1.28e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366319 505 LRKEYAgkqkhclSKKKAKIATRNVSFCVRKGEILGLLGHNGAGKSTSLKMISGDTKVTAGQVLLKG-------SREgdt 577
Cdd:COG1135 7 LSKTFP-------TKGGPVTALDDVSLTIEKGEIFGIIGYSGAGKSTLIRCINLLERPTSGSVLVDGvdltalsERE--- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366319 578 pgfL-------GYCPQENALWPNLTVKEH----LEIfaavRGLRKSHAAVAITRLADALKLQDQLKSPVKTLSEGVK--- 643
Cdd:COG1135 77 ---LraarrkiGMIFQHFNLLSSRTVAENvalpLEI----AGVPKAEIRKRVAELLELVGLSDKADAYPSQLSGGQKqrv 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1720366319 644 ---RKLCfvlsilGNPSILLLDEPSTGLDPEGQQQIWQAIRAIikNTDRGA--LLTTHYMAEAEALCDRVAILVSGRL 716
Cdd:COG1135 150 giaRALA------NNPKVLLCDEATSALDPETTRSILDLLKDI--NRELGLtiVLITHEMDVVRRICDRVAVLENGRI 219
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
526-720 |
2.01e-15 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 78.92 E-value: 2.01e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366319 526 TRNVSFCVRKGEILGLLGHNGAGKSTSLKMISGDTKVTAGQVLLKGSREGDTPGF---LGYCPQENALWPNLTVKEHLEI 602
Cdd:PRK11000 19 SKDINLDIHEGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLFIGEKRMNDVPPAergVGMVFQSYALYPHLSVAENMSF 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366319 603 FAAVRGLRKSHAAVAITRLADALKLQDQLKSPVKTLSEGVKRKLCFVLSILGNPSILLLDEPSTGLDPEGQQQIWQAIRA 682
Cdd:PRK11000 99 GLKLAGAKKEEINQRVNQVAEVLQLAHLLDRKPKALSGGQRQRVAIGRTLVAEPSVFLLDEPLSNLDAALRVQMRIEISR 178
|
170 180 190
....*....|....*....|....*....|....*...
gi 1720366319 683 IIKNTDRGALLTTHYMAEAEALCDRVAILVSGRLRCIG 720
Cdd:PRK11000 179 LHKRLGRTMIYVTHDQVEAMTLADKIVVLDAGRVAQVG 216
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
525-716 |
2.43e-15 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 77.04 E-value: 2.43e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366319 525 ATRNVSFCVRKGEILGLLGHNGAGKSTSLKMISGDTKVTAGQVLLKGS------------REgdTPGFLGYCPQENALWP 592
Cdd:PRK13639 17 ALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIKGEpikydkksllevRK--TVGIVFQNPDDQLFAP 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366319 593 nlTVKEHLEIFAAVRGLRKSHAAvaiTRLADALK---LQDQLKSPVKTLSEGVKRKLCFVLSILGNPSILLLDEPSTGLD 669
Cdd:PRK13639 95 --TVEEDVAFGPLNLGLSKEEVE---KRVKEALKavgMEGFENKPPHHLSGGQKKRVAIAGILAMKPEIIVLDEPTSGLD 169
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1720366319 670 PEGQQQIwqaIRAIIKNTDRG--ALLTTHYMAEAEALCDRVAILVSGRL 716
Cdd:PRK13639 170 PMGASQI---MKLLYDLNKEGitIIISTHDVDLVPVYADKVYVMSDGKI 215
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
527-716 |
2.58e-15 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 76.66 E-value: 2.58e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366319 527 RNVSFCVRKGEILGLLGHNGAGKSTS----LKMISGDTKVTAGQVLLKGSR--EGDTPGFLGYCPQEN---ALWPNLTVK 597
Cdd:PRK10418 20 HGVSLTLQRGRVLALVGGSGSGKSLTcaaaLGILPAGVRQTAGRVLLDGKPvaPCALRGRKIATIMQNprsAFNPLHTMH 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366319 598 EH-LEIFAAVRGLRKSHAAVAITR---LADALKLqdqLKSPVKTLSEGVKRKLCFVLSILGNPSILLLDEPSTGLDPEGQ 673
Cdd:PRK10418 100 THaRETCLALGKPADDATLTAALEavgLENAARV---LKLYPFEMSGGMLQRMMIALALLCEAPFIIADEPTTDLDVVAQ 176
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1720366319 674 QQIWQAIRAIIKNTDRGALLTTHYMAEAEALCDRVAILVSGRL 716
Cdd:PRK10418 177 ARILDLLESIVQKRALGMLLVTHDMGVVARLADDVAVMSHGRI 219
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
528-714 |
2.71e-15 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 76.69 E-value: 2.71e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366319 528 NVSFCVRKGEILGLLGHNGAGKSTSLKMISGDTKVTAGQVllkgsrEGDTPGFLGYCPQENALWPN--LTVKEhleiFAA 605
Cdd:PRK09544 22 DVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVI------KRNGKLRIGYVPQKLYLDTTlpLTVNR----FLR 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366319 606 VR-GLRKSHAAVAITRLaDALKLQDQlksPVKTLSEGVKRKLCFVLSILGNPSILLLDEPSTGLDPEGQQQIWQAIRAII 684
Cdd:PRK09544 92 LRpGTKKEDILPALKRV-QAGHLIDA---PMQKLSGGETQRVLLARALLNRPQLLVLDEPTQGVDVNGQVALYDLIDQLR 167
|
170 180 190
....*....|....*....|....*....|....*
gi 1720366319 685 KNTDRGALLTTH----YMAEA-EALCDRVAILVSG 714
Cdd:PRK09544 168 RELDCAVLMVSHdlhlVMAKTdEVLCLNHHICCSG 202
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
519-716 |
2.96e-15 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 77.05 E-value: 2.96e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366319 519 KKKAKIATRNVSFCVRKGEILGLLGHNGAGKSTSLKMISGDTKVTAGQVLLKG---SREGDT------PGFLGYCP---- 585
Cdd:PRK13633 19 ESTEKLALDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVYVDGldtSDEENLwdirnkAGMVFQNPdnqi 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366319 586 ------QENALWP-NLTVkEHLEIfaavrglRKshaavaitRLADALK---LQDQLKSPVKTLSEGVKRKLCFVLSILGN 655
Cdd:PRK13633 99 vativeEDVAFGPeNLGI-PPEEI-------RE--------RVDESLKkvgMYEYRRHAPHLLSGGQKQRVAIAGILAMR 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1720366319 656 PSILLLDEPSTGLDPEGQQQIWQAIRAIIKNTDRGALLTTHYMAEAeALCDRVAILVSGRL 716
Cdd:PRK13633 163 PECIIFDEPTAMLDPSGRREVVNTIKELNKKYGITIILITHYMEEA-VEADRIIVMDSGKV 222
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
528-716 |
3.09e-15 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 76.20 E-value: 3.09e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366319 528 NVSFCVRKGEILGLLGHNGAGKSTSLKM-------------ISGD-----TKVTAGQV-LLKGSregdtpgfLGYCPQEN 588
Cdd:COG4161 20 DINLECPSGETLVLLGPSGAGKSSLLRVlnlletpdsgqlnIAGHqfdfsQKPSEKAIrLLRQK--------VGMVFQQY 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366319 589 ALWPNLTVKEHLeIFAAVR--GLRKSHAAVAITRLADALKLQDQLKSPVKTLSEGVKRKLCFVLSILGNPSILLLDEPST 666
Cdd:COG4161 92 NLWPHLTVMENL-IEAPCKvlGLSKEQAREKAMKLLARLRLTDKADRFPLHLSGGQQQRVAIARALMMEPQVLLFDEPTA 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1720366319 667 GLDPEGQQQIWQAIRAiIKNTDRGALLTTHYMAEAEALCDRVAILVSGRL 716
Cdd:COG4161 171 ALDPEITAQVVEIIRE-LSQTGITQVIVTHEVEFARKVASQVVYMEKGRI 219
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
524-715 |
3.93e-15 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 76.18 E-value: 3.93e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366319 524 IATRNVSFCVRKGEILGLLGHNGAGKSTSLKMISGDTKVTAGQVLLKGSREGDTPGF----LGYCP--QENALWPNLTVK 597
Cdd:PRK11300 19 LAVNNVNLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTILLRGQHIEGLPGHqiarMGVVRtfQHVRLFREMTVI 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366319 598 E--------HLE--IFA---AVRGLRKSHAAvAITRLA---DALKLQDQLKSPVKTLSEGVKRKLCFVLSILGNPSILLL 661
Cdd:PRK11300 99 EnllvaqhqQLKtgLFSgllKTPAFRRAESE-ALDRAAtwlERVGLLEHANRQAGNLAYGQQRRLEIARCMVTQPEILML 177
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1720366319 662 DEPSTGLDPEGQQQIWQAIRAIIKNTDRGALLTTHYMAEAEALCDRVAILVSGR 715
Cdd:PRK11300 178 DEPAAGLNPKETKELDELIAELRNEHNVTVLLIEHDMKLVMGISDRIYVVNQGT 231
|
|
| SufC |
COG0396 |
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, ... |
527-715 |
4.38e-15 |
|
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440165 [Multi-domain] Cd Length: 245 Bit Score: 75.87 E-value: 4.38e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366319 527 RNVSFCVRKGEILGLLGHNGAGKSTSLKMISGDTK--VTAGQVLLKG-----------SREGdtpgfLGYC---PQEnal 590
Cdd:COG0396 17 KGVNLTIKPGEVHAIMGPNGSGKSTLAKVLMGHPKyeVTSGSILLDGedilelspderARAG-----IFLAfqyPVE--- 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366319 591 WPNLTVKEHLEIFAAVRGLRKSHAAVAITRLADALKL----QDQLKSPV-KTLSEGVKRKLCFVLSILGNPSILLLDEPS 665
Cdd:COG0396 89 IPGVSVSNFLRTALNARRGEELSAREFLKLLKEKMKElgldEDFLDRYVnEGFSGGEKKRNEILQMLLLEPKLAILDETD 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1720366319 666 TGLDpegqqqIWqAIRAI------IKNTDRGALLTTHYmaeaEAL-----CDRVAILVSGR 715
Cdd:COG0396 169 SGLD------ID-ALRIVaegvnkLRSPDRGILIITHY----QRIldyikPDFVHVLVDGR 218
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
525-723 |
5.00e-15 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 78.67 E-value: 5.00e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366319 525 ATRNVSFCVRKGEILGLLGHNGAGKSTSLKMISGDTKVTAGQVLLKGsREGD--TPGF-----LGYCPQENALWPNLTVK 597
Cdd:PRK09700 20 ALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINN-INYNklDHKLaaqlgIGIIYQELSVIDELTVL 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366319 598 EHLEI----FAAVRGLR-------KSHAAVAITRLAdalkLQDQLKSPVKTLSEGVKRKLCFVLSILGNPSILLLDEPST 666
Cdd:PRK09700 99 ENLYIgrhlTKKVCGVNiidwremRVRAAMMLLRVG----LKVDLDEKVANLSISHKQMLEIAKTLMLDAKVIIMDEPTS 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1720366319 667 GLDPEGQQQIWQAIRAiIKNTDRGALLTTHYMAEAEALCDRVAILVSGRLRCIGSIQ 723
Cdd:PRK09700 175 SLTNKEVDYLFLIMNQ-LRKEGTAIVYISHKLAEIRRICDRYTVMKDGSSVCSGMVS 230
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
527-703 |
5.53e-15 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 74.44 E-value: 5.53e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366319 527 RNVSFCVRKGEILGLLGHNGAGKSTSLKMISG--DTKVTA-GQVLLKGSREGDTPGF---LGYCPQENALWPNLTVKEHL 600
Cdd:COG4136 18 APLSLTVAPGEILTLMGPSGSGKSTLLAAIAGtlSPAFSAsGEVLLNGRRLTALPAEqrrIGILFQDDLLFPHLSVGENL 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366319 601 eIFAAVRGLRKS--HAAVAiTRLADAlKLQDQLKSPVKTLSEGVKRKLCFVLSILGNPSILLLDEPSTGLDPEGQQQIWQ 678
Cdd:COG4136 98 -AFALPPTIGRAqrRARVE-QALEEA-GLAGFADRDPATLSGGQRARVALLRALLAEPRALLLDEPFSKLDAALRAQFRE 174
|
170 180
....*....|....*....|....*..
gi 1720366319 679 AIRAIIKntDRG--ALLTTHYMAEAEA 703
Cdd:COG4136 175 FVFEQIR--QRGipALLVTHDEEDAPA 199
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
528-728 |
5.60e-15 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 76.31 E-value: 5.60e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366319 528 NVSFCVRKGEILGLLGHNGAGKSTSLKMISGDTKVTAGQVLLKGSREgdtpgflgycpQENALW------------PN-- 593
Cdd:PRK13650 25 DVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIIDGDLL-----------TEENVWdirhkigmvfqnPDnq 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366319 594 ---LTVKEHLEIFAAVRGLrkSHAAVaITRLADALKL---QD-QLKSPVKtLSEGVKRKLCFVLSILGNPSILLLDEPST 666
Cdd:PRK13650 94 fvgATVEDDVAFGLENKGI--PHEEM-KERVNEALELvgmQDfKEREPAR-LSGGQKQRVAIAGAVAMRPKIIILDEATS 169
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1720366319 667 GLDPEGQQQIWQAIRAIIKNTDRGALLTTHYMAEAeALCDRVAILVSGRLRCIGSIQHLKSK 728
Cdd:PRK13650 170 MLDPEGRLELIKTIKGIRDDYQMTVISITHDLDEV-ALSDRVLVMKNGQVESTSTPRELFSR 230
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
527-730 |
7.17e-15 |
|
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC transporter that is expressed in the mitochondria. Although the specific function of ATM1 is unknown, its disruption results in the accumulation of excess mitochondrial iron, loss of mitochondrial cytochromes, oxidative damage to mitochondrial DNA, and decreased levels of cytosolic heme proteins. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213220 [Multi-domain] Cd Length: 236 Bit Score: 74.96 E-value: 7.17e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366319 527 RNVSFCVRKGEILGLLGHNGAGKSTSLKMISGDTKVTAGQVLLKGS--REGDTPGF---LGYCPQENALWpNLTVKEHL- 600
Cdd:cd03253 18 KDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDGQdiREVTLDSLrraIGVVPQDTVLF-NDTIGYNIr 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366319 601 ---------EIFAAVrglRKSHAAVAITRLADA---------LKlqdqlkspvktLSEGVKRKLCFVLSILGNPSILLLD 662
Cdd:cd03253 97 ygrpdatdeEVIEAA---KAAQIHDKIMRFPDGydtivgergLK-----------LSGGEKQRVAIARAILKNPPILLLD 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1720366319 663 EPSTGLDPEGQQQIWQAIRAIIKNtdRGALLTTHYMAEAeALCDRVAILVSGRLRCIGSIQHLKSKFG 730
Cdd:cd03253 163 EATSALDTHTEREIQAALRDVSKG--RTTIVIAHRLSTI-VNADKIIVLKDGRIVERGTHEELLAKGG 227
|
|
| tagH |
PRK13545 |
teichoic acids export protein ATP-binding subunit; Provisional |
525-772 |
8.29e-15 |
|
teichoic acids export protein ATP-binding subunit; Provisional
Pssm-ID: 184130 [Multi-domain] Cd Length: 549 Bit Score: 78.39 E-value: 8.29e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366319 525 ATRNVSFCVRKGEILGLLGHNGAGKSTSLKMISGDTKVTAGQVLLKGSREGDTPGflgycpqeNALWPNLTVKEHLEIFA 604
Cdd:PRK13545 39 ALNNISFEVPEGEIVGIIGLNGSGKSTLSNLIAGVTMPNKGTVDIKGSAALIAIS--------SGLNGQLTGIENIELKG 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366319 605 AVRGLRKSHAAVAITRLADALKLQDQLKSPVKTLSEGVKRKLCFVLSILGNPSILLLDEPSTGLDPEGQQQIWQAIRAiI 684
Cdd:PRK13545 111 LMMGLTKEKIKEIIPEIIEFADIGKFIYQPVKTYSSGMKSRLGFAISVHINPDILVIDEALSVGDQTFTKKCLDKMNE-F 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366319 685 KNTDRGALLTTHYMAEAEALCDRVAILVSGRLRCIGSIQHLKSKFGkDYLLEMKVKTLEQVEPLNTEILRLFPQASRQER 764
Cdd:PRK13545 190 KEQGKTIFFISHSLSQVKSFCTKALWLHYGQVKEYGDIKEVVDHYD-EFLKKYNQMSVEERKDFREEQISQFQHGLLQED 268
|
....*...
gi 1720366319 765 YSSLMAYK 772
Cdd:PRK13545 269 QTGRERKR 276
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
527-696 |
9.43e-15 |
|
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: 72.10 E-value: 9.43e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366319 527 RNVSFCVRKGEILGLLGHNGAGKSTSLKMISGDTKVTAGQVLLKGSREgdtpgfLGYCPQenalwpnltvkehleifaav 606
Cdd:cd03221 17 KDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIVTWGSTVK------IGYFEQ-------------------- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366319 607 rglrkshaavaitrladalklqdqlkspvktLSEGVKRKLCFVLSILGNPSILLLDEPSTGLDPEGQQQIWQAiraiIKN 686
Cdd:cd03221 71 -------------------------------LSGGEKMRLALAKLLLENPNLLLLDEPTNHLDLESIEALEEA----LKE 115
|
170
....*....|
gi 1720366319 687 TDRGALLTTH 696
Cdd:cd03221 116 YPGTVILVSH 125
|
|
| BtuD |
COG4138 |
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ... |
517-669 |
1.16e-14 |
|
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism];
Pssm-ID: 443313 [Multi-domain] Cd Length: 248 Bit Score: 74.49 E-value: 1.16e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366319 517 LSKKKAKIATR--NVSFCVRKGEILGLLGHNGAGKSTSLKMISGDTKvTAGQVLLKGSREGDTPG-----FLGYCPQENA 589
Cdd:COG4138 1 LQLNDVAVAGRlgPISAQVNAGELIHLIGPNGAGKSTLLARMAGLLP-GQGEILLNGRPLSDWSAaelarHRAYLSQQQS 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366319 590 LWPNLTVKEHLEIFAAvRGLRKSHAAVAITRLADALKLQDQLKSPVKTLSEGVKRKLCFVLSIL-----GNPS--ILLLD 662
Cdd:COG4138 80 PPFAMPVFQYLALHQP-AGASSEAVEQLLAQLAEALGLEDKLSRPLTQLSGGEWQRVRLAAVLLqvwptINPEgqLLLLD 158
|
....*..
gi 1720366319 663 EPSTGLD 669
Cdd:COG4138 159 EPMNSLD 165
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
527-716 |
1.46e-14 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 77.37 E-value: 1.46e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366319 527 RNVSFCVRKGEILGLLGHNGAGKSTSLKMISGDTKVTAGQVLLKGSR-EGDTP------GfLGYCPQE---NALWPNLTV 596
Cdd:COG3845 275 KDVSLEVRAGEILGIAGVAGNGQSELAEALAGLRPPASGSIRLDGEDiTGLSPrerrrlG-VAYIPEDrlgRGLVPDMSV 353
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366319 597 KEHLeIFAAVRGLRKSHAAV----AITRLADAL------KLQDqLKSPVKTLSEGVKRKlcFVLS--ILGNPSILLLDEP 664
Cdd:COG3845 354 AENL-ILGRYRRPPFSRGGFldrkAIRAFAEELieefdvRTPG-PDTPARSLSGGNQQK--VILAreLSRDPKLLIAAQP 429
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1720366319 665 STGLDPEGQQQIWQAIRAIiknTDRGA--LLTTHYMAEAEALCDRVAILVSGRL 716
Cdd:COG3845 430 TRGLDVGAIEFIHQRLLEL---RDAGAavLLISEDLDEILALSDRIAVMYEGRI 480
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
527-716 |
1.50e-14 |
|
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: 73.66 E-value: 1.50e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366319 527 RNVSFCVRKGEILGLLGHNGAGKSTSLKMISGDTKVTAGQVLLKG---------------SREGDTPGFLGYCPQENALW 591
Cdd:cd03248 31 QDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDGkpisqyehkylhskvSLVGQEPVLFARSLQDNIAY 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366319 592 pNLTVKEHLEIFAAVrglRKSHAAVAITRLADALKLQDQLKSpvKTLSEGVKRKLCFVLSILGNPSILLLDEPSTGLDPE 671
Cdd:cd03248 111 -GLQSCSFECVKEAA---QKAHAHSFISELASGYDTEVGEKG--SQLSGGQKQRVAIARALIRNPQVLILDEATSALDAE 184
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1720366319 672 GQQQIWQAIRAiiKNTDRGALLTTHYMAEAEAlCDRVAILVSGRL 716
Cdd:cd03248 185 SEQQVQQALYD--WPERRTVLVIAHRLSTVER-ADQILVLDGGRI 226
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
505-716 |
1.87e-14 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 75.61 E-value: 1.87e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366319 505 LRKEYAGKqkhclskKKAKIATRNVSFCVRKGEILGLLGHNGAGKSTSLKMISGDTKVTAGQVLLKG------SREGDT- 577
Cdd:PRK11153 7 ISKVFPQG-------GRTIHALNNVSLHIPAGEIFGVIGASGAGKSTLIRCINLLERPTSGRVLVDGqdltalSEKELRk 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366319 578 ---------PGFlgycpqenalwpNL----TVKEH----LEIfaavRGLRKSHAAVAITRLADALKLQDQLKSPVKTLSE 640
Cdd:PRK11153 80 arrqigmifQHF------------NLlssrTVFDNvalpLEL----AGTPKAEIKARVTELLELVGLSDKADRYPAQLSG 143
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1720366319 641 GVKRKLCFVLSILGNPSILLLDEPSTGLDPEGQQQIWQAIRAIikNTDRG--ALLTTHYMAEAEALCDRVAILVSGRL 716
Cdd:PRK11153 144 GQKQRVAIARALASNPKVLLCDEATSALDPATTRSILELLKDI--NRELGltIVLITHEMDVVKRICDRVAVIDAGRL 219
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
514-719 |
1.94e-14 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 76.75 E-value: 1.94e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366319 514 KHCLSKKKAKIatRNVSFCVRKGEILGLLGHNGAGKSTSLKMISGDTKVTAGQVLLKGSR-EGDTP--------GFLGYC 584
Cdd:PRK09700 269 RNVTSRDRKKV--RDISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEIRLNGKDiSPRSPldavkkgmAYITES 346
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366319 585 PQENALWPNLTVKEHLEI--------FAAVRGLRKSHAAvaiTRLADALKLQDQLKSP-----VKTLSEGVKRKLCFVLS 651
Cdd:PRK09700 347 RRDNGFFPNFSIAQNMAIsrslkdggYKGAMGLFHEVDE---QRTAENQRELLALKCHsvnqnITELSGGNQQKVLISKW 423
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1720366319 652 ILGNPSILLLDEPSTGLDPEGQQQIWQAIRAiIKNTDRGALLTTHYMAEAEALCDRVAILVSGRLRCI 719
Cdd:PRK09700 424 LCCCPEVIIFDEPTRGIDVGAKAEIYKVMRQ-LADDGKVILMVSSELPEIITVCDRIAVFCEGRLTQI 490
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
525-716 |
2.92e-14 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 72.99 E-value: 2.92e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366319 525 ATRNVSFCVRKGEILGLLGHNGAGKSTSLKMISGDTKVTAGQVLLKGSREGDTPGF------LGYCPQENALWPNLTVKE 598
Cdd:PRK11614 20 ALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDGKDITDWQTAkimreaVAIVPEGRRVFSRMTVEE 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366319 599 HLEI--FAAVRGLRKSHaavaITRLADAL-KLQDQLKSPVKTLSEGVKRKLCFVLSILGNPSILLLDEPSTGLDPEGQQQ 675
Cdd:PRK11614 100 NLAMggFFAERDQFQER----IKWVYELFpRLHERRIQRAGTMSGGEQQMLAIGRALMSQPRLLLLDEPSLGLAPIIIQQ 175
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1720366319 676 IWQAIRAiIKNTDRGALLTTHYMAEAEALCDRVAILVSGRL 716
Cdd:PRK11614 176 IFDTIEQ-LREQGMTIFLVEQNANQALKLADRGYVLENGHV 215
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
525-725 |
3.42e-14 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 73.51 E-value: 3.42e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366319 525 ATRNVSFCVRKGEILGLLGHNGAGKSTSLK----MISGDtKVTAGQVLLKG---SREGDTPGFL-------GYCPQENAL 590
Cdd:PRK09984 19 ALHAVDLNIHHGEMVALLGPSGSGKSTLLRhlsgLITGD-KSAGSHIELLGrtvQREGRLARDIrksrantGYIFQQFNL 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366319 591 WPNLTVKEHLEI------------FAAVRGLRKSHAAVAITRLADALKLQDQlkspVKTLSEGVKRKLCFVLSILGNPSI 658
Cdd:PRK09984 98 VNRLSVLENVLIgalgstpfwrtcFSWFTREQKQRALQALTRVGMVHFAHQR----VSTLSGGQQQRVAIARALMQQAKV 173
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1720366319 659 LLLDEPSTGLDPEGQQQIWQAIRAIIKNTDRGALLTTHYMAEAEALCDRVAILVSGRLRCIGSIQHL 725
Cdd:PRK09984 174 ILADEPIASLDPESARIVMDTLRDINQNDGITVVVTLHQVDYALRYCERIVALRQGHVFYDGSSQQF 240
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
521-716 |
4.07e-14 |
|
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: 71.19 E-value: 4.07e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366319 521 KAKIATRNVSFCVRKGEILGLLGHNGAGKSTSLKMISGDTKVTAGQVLLKGSR----EGDTPGFLGYCPQENALWpNLTV 596
Cdd:cd03247 13 QEQQVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDGVPvsdlEKALSSLISVLNQRPYLF-DTTL 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366319 597 KEHLeifaavrGLRkshaavaitrladalklqdqlkspvktLSEGVKRKLCFVLSILGNPSILLLDEPSTGLDPEGQQQI 676
Cdd:cd03247 92 RNNL-------GRR---------------------------FSGGERQRLALARILLQDAPIVLLDEPTVGLDPITERQL 137
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1720366319 677 WQAIRAIIKntDRGALLTTHYMAEAEALcDRVAILVSGRL 716
Cdd:cd03247 138 LSLIFEVLK--DKTLIWITHHLTGIEHM-DKILFLENGKI 174
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
525-728 |
4.15e-14 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 73.73 E-value: 4.15e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366319 525 ATRNVSFCVRKGEILGLLGHNGAGKSTSLKMISGDTKVTAGQVLLKG-----SREG-----DTPGFLGYCPqENALWpNL 594
Cdd:PRK13636 21 ALKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGkpidySRKGlmklrESVGMVFQDP-DNQLF-SA 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366319 595 TVKEHLEIFAAVRGLRKSHAAVAITRLADALKLQDQLKSPVKTLSEGVKRKLCFVLSILGNPSILLLDEPSTGLDPEGQQ 674
Cdd:PRK13636 99 SVYQDVSFGAVNLKLPEDEVRKRVDNALKRTGIEHLKDKPTHCLSFGQKKRVAIAGVLVMEPKVLVLDEPTAGLDPMGVS 178
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1720366319 675 QIWQAIRAIIKNTDRGALLTTHYMAEAEALCDRVAILVSGRLRCIGSIQHLKSK 728
Cdd:PRK13636 179 EIMKLLVEMQKELGLTIIIATHDIDIVPLYCDNVFVMKEGRVILQGNPKEVFAE 232
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
517-687 |
4.36e-14 |
|
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: 72.26 E-value: 4.36e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366319 517 LSKKKAKIATRNVSFCVRKGEILGLLGHNGAGKSTSLKMISGDTKVTAGQVLLKGS----------REGdtpgfLGYCPQ 586
Cdd:cd03254 10 FSYDEKKPVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGIdirdisrkslRSM-----IGVVLQ 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366319 587 ----------ENALWPNLTVKEHLEIFAAvrglRKSHAAVAITRLADALklQDQLKSPVKTLSEGVKRKLCFVLSILGNP 656
Cdd:cd03254 85 dtflfsgtimENIRLGRPNATDEEVIEAA----KEAGAHDFIMKLPNGY--DTVLGENGGNLSQGERQLLAIARAMLRDP 158
|
170 180 190
....*....|....*....|....*....|.
gi 1720366319 657 SILLLDEPSTGLDPEGQQQIWQAIRAIIKNT 687
Cdd:cd03254 159 KILILDEATSNIDTETEKLIQEALEKLMKGR 189
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
530-727 |
6.13e-14 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 71.92 E-value: 6.13e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366319 530 SFCVRKGEILGLLGHNGAGKSTSLKMISGDTKVTAGQVLLKGSREGDTPgflgycP---------QENALWPNLTVKEHL 600
Cdd:PRK10771 19 DLTVERGERVAILGPSGAGKSTLLNLIAGFLTPASGSLTLNGQDHTTTP------PsrrpvsmlfQENNLFSHLTVAQNI 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366319 601 EIFAAvRGLRKSHAAVA-ITRLADALKLQDQLKSPVKTLSEGVKRKL----CFVLSilgNPsILLLDEPSTGLDPEGQQQ 675
Cdd:PRK10771 93 GLGLN-PGLKLNAAQREkLHAIARQMGIEDLLARLPGQLSGGQRQRValarCLVRE---QP-ILLLDEPFSALDPALRQE 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1720366319 676 IWQAIRAIIKNTDRGALLTTHYMAEAEALCDRVAILVSGRLRCIGSIQHLKS 727
Cdd:PRK10771 168 MLTLVSQVCQERQLTLLMVSHSLEDAARIAPRSLVVADGRIAWDGPTDELLS 219
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
516-735 |
7.77e-14 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 72.53 E-value: 7.77e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366319 516 CLSKKKAKIATRNVSFCVRKGEILGLLGHNGAGKSTSLKMISGDTKVTAGQVLLKGS-------RE-GDTPGFLGYCPQE 587
Cdd:PRK13652 10 CYSYSGSKEALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIRGEpitkeniREvRKFVGLVFQNPDD 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366319 588 NALWPnlTVKEHLEIFAAVRGLRKSHAAVAITRLADALKLQDQLKSPVKTLSEGVKRKLCFVLSILGNPSILLLDEPSTG 667
Cdd:PRK13652 90 QIFSP--TVEQDIAFGPINLGLDEETVAHRVSSALHMLGLEELRDRVPHHLSGGEKKRVAIAGVIAMEPQVLVLDEPTAG 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1720366319 668 LDPEGQQQIWQAIRAIIKNTDRGALLTTHYMAEAEALCDRVAILVSGRLRCIGSIQHLkskFGKDYLL 735
Cdd:PRK13652 168 LDPQGVKELIDFLNDLPETYGMTVIFSTHQLDLVPEMADYIYVMDKGRIVAYGTVEEI---FLQPDLL 232
|
|
| PRK13546 |
PRK13546 |
teichoic acids export ABC transporter ATP-binding subunit TagH; |
519-744 |
1.11e-13 |
|
teichoic acids export ABC transporter ATP-binding subunit TagH;
Pssm-ID: 184131 [Multi-domain] Cd Length: 264 Bit Score: 72.16 E-value: 1.11e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366319 519 KKKAKIATRNVSFCVRKGEILGLLGHNGAGKSTSLKMISGDTKVTAGQVllkgSREGDtpgfLGYCPQENALWPNLTVKE 598
Cdd:PRK13546 33 KNKTFFALDDISLKAYEGDVIGLVGINGSGKSTLSNIIGGSLSPTVGKV----DRNGE----VSVIAISAGLSGQLTGIE 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366319 599 HLEIFAAVRGLRKSHAAVAITRLADALKLQDQLKSPVKTLSEGVKRKLCFVLSILGNPSILLLDEPSTGLDPEGQQQIWQ 678
Cdd:PRK13546 105 NIEFKMLCMGFKRKEIKAMTPKIIEFSELGEFIYQPVKKYSSGMRAKLGFSINITVNPDILVIDEALSVGDQTFAQKCLD 184
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1720366319 679 AIRAiIKNTDRGALLTTHYMAEAEALCDRVAILVSGRLRCIGSIQHLKSKFgKDYLLEMKVKTLEQ 744
Cdd:PRK13546 185 KIYE-FKEQNKTIFFVSHNLGQVRQFCTKIAWIEGGKLKDYGELDDVLPKY-EAFLNDFKKKSKAE 248
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
523-728 |
1.18e-13 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 72.17 E-value: 1.18e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366319 523 KIATRNVSFCVRKGEILGLLGHNGAGKSTSLKMISGDTKVTAGQVLLKG---SREGDTPGF--------LGYCPQENALW 591
Cdd:PRK13641 20 KKGLDNISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITIAGyhiTPETGNKNLkklrkkvsLVFQFPEAQLF 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366319 592 PNlTVKEHLEIFAAVRGLRKSHAAVAITRLADALKLQDQL--KSPVKtLSEGVKRKLCFVLSILGNPSILLLDEPSTGLD 669
Cdd:PRK13641 100 EN-TVLKDVEFGPKNFGFSEDEAKEKALKWLKKVGLSEDLisKSPFE-LSGGQMRRVAIAGVMAYEPEILCLDEPAAGLD 177
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1720366319 670 PEGQQQIWQairaIIKNTDRGA---LLTTHYMAEAEALCDRVAILVSGRLrcigsIQHLKSK 728
Cdd:PRK13641 178 PEGRKEMMQ----LFKDYQKAGhtvILVTHNMDDVAEYADDVLVLEHGKL-----IKHASPK 230
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
529-669 |
1.22e-13 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 71.50 E-value: 1.22e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366319 529 VSFCVRKGEILGLLGHNGAGKSTSLKMISGdTKVTAGQVLLKGSREGDTPG-----FLGYCPQENALWPNLTVKEHLEIF 603
Cdd:PRK03695 15 LSAEVRAGEILHLVGPNGAGKSTLLARMAG-LLPGSGSIQFAGQPLEAWSAaelarHRAYLSQQQTPPFAMPVFQYLTLH 93
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1720366319 604 AAVrGLRKSHAAVAITRLADALKLQDQLKSPVKTLSEGVKRKLCFVLSIL-----GNPS--ILLLDEPSTGLD 669
Cdd:PRK03695 94 QPD-KTRTEAVASALNEVAEALGLDDKLGRSVNQLSGGEWQRVRLAAVVLqvwpdINPAgqLLLLDEPMNSLD 165
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
538-727 |
1.38e-13 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 72.05 E-value: 1.38e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366319 538 ILGLLGHNGAGKSTSLKMISG-DTKVT----AGQVLLKGSREGDTPGFLGYCPQENALW--PN---LTVKEHleIFAAVR 607
Cdd:PRK14271 49 VTSLMGPTGSGKTTFLRTLNRmNDKVSgyrySGDVLLGGRSIFNYRDVLEFRRRVGMLFqrPNpfpMSIMDN--VLAGVR 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366319 608 GL----RKSHAAVAITRLA-----DALKlqDQLKSPVKTLSEGVKRKLCFVLSILGNPSILLLDEPSTGLDPEGQQQIWQ 678
Cdd:PRK14271 127 AHklvpRKEFRGVAQARLTevglwDAVK--DRLSDSPFRLSGGQQQLLCLARTLAVNPEVLLLDEPTSALDPTTTEKIEE 204
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1720366319 679 AIRAIiknTDR-GALLTTHYMAEAEALCDRVAILVSGRLRCIGSIQHLKS 727
Cdd:PRK14271 205 FIRSL---ADRlTVIIVTHNLAQAARISDRAALFFDGRLVEEGPTEQLFS 251
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
520-735 |
1.38e-13 |
|
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: 71.11 E-value: 1.38e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366319 520 KKAKIATRNVSFCVRKGEILGLLGHNGAGKSTSLKMISGDTKVTAGQVLLKGSregDTPGF--------LGYCPQENALW 591
Cdd:cd03251 12 GDGPPVLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDGH---DVRDYtlaslrrqIGLVSQDVFLF 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366319 592 pNLTVKEHleIFAAVRGlrKSHAAV-AITRLADAL----KLQDQLKSPVK----TLSEGVKRKLCFVLSILGNPSILLLD 662
Cdd:cd03251 89 -NDTVAEN--IAYGRPG--ATREEVeEAARAANAHefimELPEGYDTVIGergvKLSGGQRQRIAIARALLKDPPILILD 163
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1720366319 663 EPSTGLDPEGQQQIWQAIRAIIKNtdRGALLTTHYMAEAEAlCDRVAILVSGRLRCIGSIQHLKSKFGKDYLL 735
Cdd:cd03251 164 EATSALDTESERLVQAALERLMKN--RTTFVIAHRLSTIEN-ADRIVVLEDGKIVERGTHEELLAQGGVYAKL 233
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
525-725 |
1.62e-13 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 74.12 E-value: 1.62e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366319 525 ATRNVSFCVRKGEILGLLGHNGAGKS-TSLKMI----SGDTKVTAGQVLLK------------------GSREGDtpgfL 581
Cdd:PRK10261 31 AVRNLSFSLQRGETLAIVGESGSGKSvTALALMrlleQAGGLVQCDKMLLRrrsrqvielseqsaaqmrHVRGAD----M 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366319 582 GYCPQE--NALWPNLTVKEhlEIFAAVR---GLRKSHAAVAITRLADALKL---QDQLKSPVKTLSEGVKRKLCFVLSIL 653
Cdd:PRK10261 107 AMIFQEpmTSLNPVFTVGE--QIAESIRlhqGASREEAMVEAKRMLDQVRIpeaQTILSRYPHQLSGGMRQRVMIAMALS 184
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1720366319 654 GNPSILLLDEPSTGLDPEGQQQIWQAIRAIIKNTDRGALLTTHYMAEAEALCDRVAILVSGRLRCIGSIQHL 725
Cdd:PRK10261 185 CRPAVLIADEPTTALDVTIQAQILQLIKVLQKEMSMGVIFITHDMGVVAEIADRVLVMYQGEAVETGSVEQI 256
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
527-696 |
1.69e-13 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 69.98 E-value: 1.69e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366319 527 RNVSFCVRKGEILGLLGHNGAGKSTSLKMISGDTKVTAGQVLLKG-SREGDTPGF---LGYCPQENALWPNLTVKEHlei 602
Cdd:PRK13540 18 QQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEILFERqSIKKDLCTYqkqLCFVGHRSGINPYLTLREN--- 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366319 603 faAVRGLRKSHAAVAITRLADALKLQDQLKSPVKTLSEGVKRKLCFVLSILGNPSILLLDEPSTGLDPEGQQQIWQAIRA 682
Cdd:PRK13540 95 --CLYDIHFSPGAVGITELCRLFSLEHLIDYPCGLLSSGQKRQVALLRLWMSKAKLWLLDEPLVALDELSLLTIITKIQE 172
|
170
....*....|....*
gi 1720366319 683 iiKNTDRGA-LLTTH 696
Cdd:PRK13540 173 --HRAKGGAvLLTSH 185
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
517-748 |
2.48e-13 |
|
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: 73.30 E-value: 2.48e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366319 517 LSKK-KAKIATRNVSFCVRKGEILGLLGHNGAGKSTSLKMISG--DTKVTAGQVLLKGSR-----EGDTPGFLGY-CP-- 585
Cdd:TIGR03269 6 LTKKfDGKEVLKNISFTIEEGEVLGILGRSGAGKSVLMHVLRGmdQYEPTSGRIIYHVALcekcgYVERPSKVGEpCPvc 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366319 586 ------QENALWpNLTVKEHLEI-----------FA----------AVRGLRKS--HAAVAITRLADAL---KLQDQLKS 633
Cdd:TIGR03269 86 ggtlepEEVDFW-NLSDKLRRRIrkriaimlqrtFAlygddtvldnVLEALEEIgyEGKEAVGRAVDLIemvQLSHRITH 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366319 634 PVKTLSEGVKRKLCFVLSILGNPSILLLDEPSTGLDPEGQQQIWQAIRAIIKNTDRGALLTTHYMAEAEALCDRVAILVS 713
Cdd:TIGR03269 165 IARDLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALEEAVKASGISMVLTSHWPEVIEDLSDKAIWLEN 244
|
250 260 270
....*....|....*....|....*....|....*
gi 1720366319 714 GRLRCIGSIQHLKSKFGKDYLLEMKVKTLEQVEPL 748
Cdd:TIGR03269 245 GEIKEEGTPDEVVAVFMEGVSEVEKECEVEVGEPI 279
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
527-716 |
3.26e-13 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 73.11 E-value: 3.26e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366319 527 RNVSFCVRKGEILGLLGHNGAGKSTSLKMISGDTKVTAGQVLLKGsREGDTpgflgYCPQE---------------NALW 591
Cdd:PRK10762 269 NDVSFTLRKGEILGVSGLMGAGRTELMKVLYGALPRTSGYVTLDG-HEVVT-----RSPQDglangivyisedrkrDGLV 342
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366319 592 PNLTVKEHLEIFAavrgLRK-SHAAVAITRLADALKLQD-----QLKSP-----VKTLSEGVKRKLCFVLSILGNPSILL 660
Cdd:PRK10762 343 LGMSVKENMSLTA----LRYfSRAGGSLKHADEQQAVSDfirlfNIKTPsmeqaIGLLSGGNQQKVAIARGLMTRPKVLI 418
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1720366319 661 LDEPSTGLDPEGQQQIWQAIRAiIKNTDRGALLTTHYMAEAEALCDRVAILVSGRL 716
Cdd:PRK10762 419 LDEPTRGVDVGAKKEIYQLINQ-FKAEGLSIILVSSEMPEVLGMSDRILVMHEGRI 473
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
540-671 |
3.39e-13 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 73.23 E-value: 3.39e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366319 540 GLLGHNGAGKSTSLKMISGDTKVTAGQVLLkgsregdTPGF-LGYCPQENALWPNLTVKEHLE-----IFAAVRGLRKSH 613
Cdd:PRK11819 37 GVLGLNGAGKSTLLRIMAGVDKEFEGEARP-------APGIkVGYLPQEPQLDPEKTVRENVEegvaeVKAALDRFNEIY 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366319 614 AAVAiTRLA--DAL-----KLQDQLKS------------------------PVKTLSEGVKRK--LCFVLsiLGNPSILL 660
Cdd:PRK11819 110 AAYA-EPDAdfDALaaeqgELQEIIDAadawdldsqleiamdalrcppwdaKVTKLSGGERRRvaLCRLL--LEKPDMLL 186
|
170
....*....|.
gi 1720366319 661 LDEPSTGLDPE 671
Cdd:PRK11819 187 LDEPTNHLDAE 197
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
536-745 |
3.74e-13 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 70.59 E-value: 3.74e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366319 536 GEILGLLGHNGAGKSTSLKMISGDTKVTAGQVLLKGS--REGDTPGF---LGYCPQENALWPNLTVKEHLEIfaavrGLR 610
Cdd:PRK10575 37 GKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQplESWSSKAFarkVAYLPQQLPAAEGMTVRELVAI-----GRY 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366319 611 KSHAAVAITRLADALKLQDQLK----SP-----VKTLSEGVKRKLCFVLSILGNPSILLLDEPSTGLDPEGQQQIWQAIR 681
Cdd:PRK10575 112 PWHGALGRFGAADREKVEEAISlvglKPlahrlVDSLSGGERQRAWIAMLVAQDSRCLLLDEPTSALDIAHQVDVLALVH 191
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1720366319 682 AIIKNTDRGALLTTHYMAEAEALCDRVAILVSGRLRCIGSIQHLkskfgkdylleMKVKTLEQV 745
Cdd:PRK10575 192 RLSQERGLTVIAVLHDINMAARYCDYLVALRGGEMIAQGTPAEL-----------MRGETLEQI 244
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
527-715 |
4.44e-13 |
|
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: 68.83 E-value: 4.44e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366319 527 RNVSFCVRKGEILGLLGHNGAGKSTSLKMISGDTKVtagqvllKGSREGDT--------------PGFLGYCPQENALWP 592
Cdd:cd03233 24 KDFSGVVKPGEMVLVLGRPGSGCSTLLKALANRTEG-------NVSVEGDIhyngipykefaekyPGEIIYVSEEDVHFP 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366319 593 NLTVKEHLEIFAAVRGlrkshaavaitrladalklqDQLkspVKTLSEGVKRKLCFVLSILGNPSILLLDEPSTGLDPEG 672
Cdd:cd03233 97 TLTVRETLDFALRCKG--------------------NEF---VRGISGGERKRVSIAEALVSRASVLCWDNSTRGLDSST 153
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1720366319 673 QQQIWQAIRAIIKNTdRGALLTTHYMA--EAEALCDRVAILVSGR 715
Cdd:cd03233 154 ALEILKCIRTMADVL-KTTTFVSLYQAsdEIYDLFDKVLVLYEGR 197
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
533-698 |
5.49e-13 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 72.53 E-value: 5.49e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366319 533 VRKGEILGLLGHNGAGKSTSLKMISGDTKVTAGQVL--LKGSregdtpgflgYCPQENALWPNLTVKEHLEifAAVRGLR 610
Cdd:PRK13409 362 IYEGEVIGIVGPNGIGKTTFAKLLAGVLKPDEGEVDpeLKIS----------YKPQYIKPDYDGTVEDLLR--SITDDLG 429
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366319 611 KSHaavAITRLADALKLQDQLKSPVKTLSEGVKRKLCFVLSILGNPSILLLDEPSTGLDPEGQQQIWQAIRAIIKNTDRG 690
Cdd:PRK13409 430 SSY---YKSEIIKPLQLERLLDKNVKDLSGGELQRVAIAACLSRDADLYLLDEPSAHLDVEQRLAVAKAIRRIAEEREAT 506
|
170
....*....|
gi 1720366319 691 ALLTTH--YM 698
Cdd:PRK13409 507 ALVVDHdiYM 516
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
505-671 |
6.72e-13 |
|
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: 72.28 E-value: 6.72e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366319 505 LRKEYAGKqKHCLskkkakiatRNVSFCVRKGEILGLLGHNGAGKSTSLKMISGDTKVTAGQVLLKgsregdtPGF-LGY 583
Cdd:TIGR03719 10 VSKVVPPK-KEIL---------KDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKDFNGEARPQ-------PGIkVGY 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366319 584 CPQENALWPNLTVKEHLEifAAVRGLRKshaavAITRL-------------ADAL-----KLQDQLKS------------ 633
Cdd:TIGR03719 73 LPQEPQLDPTKTVRENVE--EGVAEIKD-----ALDRFneisakyaepdadFDKLaaeqaELQEIIDAadawdldsqlei 145
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1720366319 634 ------------PVKTLSEGVKRK--LCFVLsiLGNPSILLLDEPSTGLDPE 671
Cdd:TIGR03719 146 amdalrcppwdaDVTKLSGGERRRvaLCRLL--LSKPDMLLLDEPTNHLDAE 195
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
517-734 |
8.27e-13 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 71.22 E-value: 8.27e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366319 517 LSKKKAKIATRNVSFCVRKGEILGLLGHNGAGKSTSLKMISGDTKVTAGQVLLKG---SREGDTP------GFLGYCPQE 587
Cdd:PRK10070 35 LEKTGLSLGVKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGvdiAKISDAElrevrrKKIAMVFQS 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366319 588 NALWPNLTVKEHLEIFAAVRGLRkshAAVAITRLADALK---LQDQLKSPVKTLSEGVKRKLCFVLSILGNPSILLLDEP 664
Cdd:PRK10070 115 FALMPHMTVLDNTAFGMELAGIN---AEERREKALDALRqvgLENYAHSYPDELSGGMRQRVGLARALAINPDILLMDEA 191
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366319 665 STGLDPEGQQQIWQAIRAIIKNTDRGALLTTHYMAEAEALCDRVAILVSGRLRCIGSIQHLKSKFGKDYL 734
Cdd:PRK10070 192 FSALDPLIRTEMQDELVKLQAKHQRTIVFISHDLDEAMRIGDRIAIMQNGEVVQVGTPDEILNNPANDYV 261
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
522-725 |
8.65e-13 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 69.66 E-value: 8.65e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366319 522 AKIATRNVSFCVRKGEILGLLGHNGAGKSTSLKMI-------SGDTKVtAGQVLlkgsregdtpgflgycpQENALW--- 591
Cdd:PRK13635 19 ATYALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLnglllpeAGTITV-GGMVL-----------------SEETVWdvr 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366319 592 ---------PN-----LTVKEHLEIFAAVRGLRKSHAavaITRLADALKL---QDQLKSPVKTLSEGVKRKLCFVLSILG 654
Cdd:PRK13635 81 rqvgmvfqnPDnqfvgATVQDDVAFGLENIGVPREEM---VERVDQALRQvgmEDFLNREPHRLSGGQKQRVAIAGVLAL 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1720366319 655 NPSILLLDEPSTGLDPEGQQQIWQAIRAIIKNTDRGALLTTHYMAEAeALCDRVAILVSGRLRCIGSIQHL 725
Cdd:PRK13635 158 QPDIIILDEATSMLDPRGRREVLETVRQLKEQKGITVLSITHDLDEA-AQADRVIVMNKGEILEEGTPEEI 227
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
525-716 |
1.27e-12 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 67.98 E-value: 1.27e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366319 525 ATRNVSFCVRKGEILGLLGHNGAGKSTSLKMISGDTKVTAGQVLLKGS-----REGDTPgFL----GYCPQENALWPNLT 595
Cdd:PRK10908 17 ALQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHditrlKNREVP-FLrrqiGMIFQDHHLLMDRT 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366319 596 VKEHLEIFAAVRGLRKSHAAVAITRLADALKLQDQLKSPVKTLSEGVKRKLCFVLSILGNPSILLLDEPSTGLDPEgqqq 675
Cdd:PRK10908 96 VYDNVAIPLIIAGASGDDIRRRVSAALDKVGLLDKAKNFPIQLSGGEQQRVGIARAVVNKPAVLLADEPTGNLDDA---- 171
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1720366319 676 IWQAIRAIIKNTDR---GALLTTHYMAEAEALCDRVAILVSGRL 716
Cdd:PRK10908 172 LSEGILRLFEEFNRvgvTVLMATHDIGLISRRSYRMLTLSDGHL 215
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
527-715 |
1.75e-12 |
|
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440743 [Multi-domain] Cd Length: 239 Bit Score: 68.10 E-value: 1.75e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366319 527 RNVSFCVRKGEILGLLGHNGAGKSTSLKMISGDTKVTAGQVLLKGSREGDTPGFL-------GYCPQENALWPNLTVKEH 599
Cdd:COG1126 18 KGISLDVEKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTITVDGEDLTDSKKDInklrrkvGMVFQQFNLFPHLTVLEN 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366319 600 LEIfaA---VRGLRKSHA-AVAITRLADaLKLQDQLKSPVKTLSEGVK------RKLCFvlsilgNPSILLLDEPSTGLD 669
Cdd:COG1126 98 VTL--ApikVKKMSKAEAeERAMELLER-VGLADKADAYPAQLSGGQQqrvaiaRALAM------EPKVMLFDEPTSALD 168
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1720366319 670 PEGQQQIWQAIRAiIKNTDRGALLTTHYMAEAEALCDRVAILVSGR 715
Cdd:COG1126 169 PELVGEVLDVMRD-LAKEGMTMVVVTHEMGFAREVADRVVFMDGGR 213
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
529-724 |
1.76e-12 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 70.71 E-value: 1.76e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366319 529 VSFCVRKGEILGLLGHNGAGKSTSLKMISGDTKVTAGQVLLKGSR-EGDTPGF-----LGYCPQ---ENALWPNLTVKEH 599
Cdd:PRK11288 272 ISFSVRAGEIVGLFGLVGAGRSELMKLLYGATRRTAGQVYLDGKPiDIRSPRDairagIMLCPEdrkAEGIIPVHSVADN 351
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366319 600 LEIFAAVRGLR----------KSHAAVAITRLADALKLQDQlksPVKTLSEGVKRKlcfvlSILG-----NPSILLLDEP 664
Cdd:PRK11288 352 INISARRHHLRagclinnrweAENADRFIRSLNIKTPSREQ---LIMNLSGGNQQK-----AILGrwlseDMKVILLDEP 423
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366319 665 STGLDPEGQQQIWQAIRAIIKnTDRGALLTTHYMAEAEALCDRVAILVSGRLRciGSIQH 724
Cdd:PRK11288 424 TRGIDVGAKHEIYNVIYELAA-QGVAVLFVSSDLPEVLGVADRIVVMREGRIA--GELAR 480
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
527-731 |
1.94e-12 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 71.29 E-value: 1.94e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366319 527 RNVSFCVRKGEILGLLGHNGAGKSTSLKMISGDTKVTAGQVLLKGSREGDTP--------GFLGYCPQENALWPNLTVKE 598
Cdd:TIGR00956 78 KPMDGLIKPGELTVVLGRPGSGCSTLLKTIASNTDGFHIGVEGVITYDGITPeeikkhyrGDVVYNAETDVHFPHLTVGE 157
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366319 599 HLEiFAA--------VRGLRKSHAAVAITRLADAL---------KLQDQLkspVKTLSEGVKRKLCFVLSILGNPSILLL 661
Cdd:TIGR00956 158 TLD-FAArcktpqnrPDGVSREEYAKHIADVYMATyglshtrntKVGNDF---VRGVSGGERKRVSIAEASLGGAKIQCW 233
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1720366319 662 DEPSTGLDPEGQQQIWQAIRAIIKNTDRGALLTThYMAEAEA--LCDRVAILVSGRLRCIGSIQHLKSKFGK 731
Cdd:TIGR00956 234 DNATRGLDSATALEFIRALKTSANILDTTPLVAI-YQCSQDAyeLFDKVIVLYEGYQIYFGPADKAKQYFEK 304
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
513-696 |
2.11e-12 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 67.53 E-value: 2.11e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366319 513 QKHCLSKK--KAKIAT---RNVSFCVRKGEILGLLGHNGAGKSTSLKMISGDTKVTAGQVLLKG---------------S 572
Cdd:PRK11629 7 QCDNLCKRyqEGSVQTdvlHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGqpmsklssaakaelrN 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366319 573 REgdtpgfLGYCPQENALWPNLTVKEHLEIFAAVRGLRKSHAAVAITRLADALKLQDQLKSPVKTLSEGVKRKLCFVLSI 652
Cdd:PRK11629 87 QK------LGFIYQFHHLLPDFTALENVAMPLLIGKKKPAEINSRALEMLAAVGLEHRANHRPSELSGGERQRVAIARAL 160
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1720366319 653 LGNPSILLLDEPSTGLDPEGQQQIWQAIRAIIKNTDRGALLTTH 696
Cdd:PRK11629 161 VNNPRLVLADEPTGNLDARNADSIFQLLGELNRLQGTAFLVVTH 204
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
523-716 |
2.11e-12 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 68.67 E-value: 2.11e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366319 523 KIATRNVSFCVRKGEILGLLGHNGAGKSTSLKMISG--------DTKVTAGQVLLKGSREGDTPGFLGYCPQE-NALWPN 593
Cdd:PRK13640 20 KPALNDISFSIPRGSWTALIGHNGSGKSTISKLINGlllpddnpNSKITVDGITLTAKTVWDIREKVGIVFQNpDNQFVG 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366319 594 LTVKEHLEIFAAVRGLRKSHAAVAITRLADALKLQDQLKSPVKTLSEGVKRKLCfVLSILG-NPSILLLDEPSTGLDPEG 672
Cdd:PRK13640 100 ATVGDDVAFGLENRAVPRPEMIKIVRDVLADVGMLDYIDSEPANLSGGQKQRVA-IAGILAvEPKIIILDESTSMLDPAG 178
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1720366319 673 QQQIWQAIRAIIKNTDRGALLTTHYMAEAEaLCDRVAILVSGRL 716
Cdd:PRK13640 179 KEQILKLIRKLKKKNNLTVISITHDIDEAN-MADQVLVLDDGKL 221
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
527-716 |
2.13e-12 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 68.02 E-value: 2.13e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366319 527 RNVSFCVRKGEILGLLGHNGAGKSTSLKMIS------GDTKVtAGQVLLKGSREGDTP--------GFLGYCPqeNALwP 592
Cdd:PRK14247 20 DGVNLEIPDNTITALMGPSGSGKSTLLRVFNrlielyPEARV-SGEVYLDGQDIFKMDvielrrrvQMVFQIP--NPI-P 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366319 593 NLTVKEHLEIFAAVRGLRKSHAAVAiTRLADALK-------LQDQLKSPVKTLSEGVKRKLCFVLSILGNPSILLLDEPS 665
Cdd:PRK14247 96 NLSIFENVALGLKLNRLVKSKKELQ-ERVRWALEkaqlwdeVKDRLDAPAGKLSGGQQQRLCIARALAFQPEVLLADEPT 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1720366319 666 TGLDPEGQQQIWQAIRAIIKntDRGALLTTHYMAEAEALCDRVAILVSGRL 716
Cdd:PRK14247 175 ANLDPENTAKIESLFLELKK--DMTIVLVTHFPQQAARISDYVAFLYKGQI 223
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
507-717 |
2.31e-12 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 67.50 E-value: 2.31e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366319 507 KEYAGKQKHCLSkkkakIATrNVSFCVRKGEILGLLGHNGAGKSTSLKMISGDTKVTAGQVLLKGS---------REGDT 577
Cdd:PRK10584 13 KKSVGQGEHELS-----ILT-GVELVVKRGETIALIGESGSGKSTLLAILAGLDDGSSGEVSLVGQplhqmdeeaRAKLR 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366319 578 PGFLGYCPQENALWPNLTVKEHLEIFAAVRGLRKSHAAVAITRLADALKLQDQLKSPVKTLSEGVKRKLCFVLSILGNPS 657
Cdd:PRK10584 87 AKHVGFVFQSFMLIPTLNALENVELPALLRGESSRQSRNGAKALLEQLGLGKRLDHLPAQLSGGEQQRVALARAFNGRPD 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366319 658 ILLLDEPSTGLDPEGQQQIWQAIRAIIKNTDRGALLTTHYMAEAeALCDRVAILVSGRLR 717
Cdd:PRK10584 167 VLFADEPTGNLDRQTGDKIADLLFSLNREHGTTLILVTHDLQLA-ARCDRRLRLVNGQLQ 225
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
528-734 |
3.43e-12 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 66.96 E-value: 3.43e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366319 528 NVSFCVRKGEILGLLGHNGAGKSTSLKMI-------SGDTKVtAGQVLLKGSREGDTPGFL-----GYCPQENALWPNLT 595
Cdd:PRK11124 20 DITLDCPQGETLVLLGPSGAGKSSLLRVLnllemprSGTLNI-AGNHFDFSKTPSDKAIRElrrnvGMVFQQYNLWPHLT 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366319 596 VKEHL-EIFAAVRGLRKSHAAVAITRLADALKLQDQLKSPVKTLSEGVKRKLCFVLSILGNPSILLLDEPSTGLDPEGQQ 674
Cdd:PRK11124 99 VQQNLiEAPCRVLGLSKDQALARAEKLLERLRLKPYADRFPLHLSGGQQQRVAIARALMMEPQVLLFDEPTAALDPEITA 178
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1720366319 675 QIWQAIRAiIKNTDRGALLTTHYMAEAEALCDRVAILVSGRLRCIGSIQHLK----SKFgKDYL 734
Cdd:PRK11124 179 QIVSIIRE-LAETGITQVIVTHEVEVARKTASRVVYMENGHIVEQGDASCFTqpqtEAF-KNYL 240
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
525-734 |
4.38e-12 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 67.32 E-value: 4.38e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366319 525 ATRNVSFCVRKGEILGLLGHNGAGKSTSLKMISGDTKVTAGQVLLKGSREGDTPGFLGYCPQENALWPN-------LTVK 597
Cdd:PRK13644 17 ALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLVSGIDTGDFSKLQGIRKLVGIVFQNpetqfvgRTVE 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366319 598 EHLEIFAAVRGLRKSHAAVAITRLADALKLQDQLKSPVKTLSEGVKRKLCFVLSILGNPSILLLDEPSTGLDPEGQQQIW 677
Cdd:PRK13644 97 EDLAFGPENLCLPPIEIRKRVDRALAEIGLEKYRHRSPKTLSGGQGQCVALAGILTMEPECLIFDEVTSMLDPDSGIAVL 176
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1720366319 678 QAIRAiIKNTDRGALLTTHYMAEAEAlCDRVAILVSGRLRCIGSIQHLKSKFGKDYL 734
Cdd:PRK13644 177 ERIKK-LHEKGKTIVYITHNLEELHD-ADRIIVMDRGKIVLEGEPENVLSDVSLQTL 231
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
538-721 |
5.65e-12 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 66.95 E-value: 5.65e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366319 538 ILGLLGHNGAGKSTSLKMISGDTKVTAGQVLLKG-----SREG-----DTPGFLGYCPQENALWPNLTVkehlEIFAAVR 607
Cdd:PRK13638 29 VTGLVGANGCGKSTLFMNLSGLLRPQKGAVLWQGkpldySKRGllalrQQVATVFQDPEQQIFYTDIDS----DIAFSLR 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366319 608 GLRKSHAAVAiTRLADALKLQDQL---KSPVKTLSEGVKRKLCFVLSILGNPSILLLDEPSTGLDPEGQQQIWQAIRAII 684
Cdd:PRK13638 105 NLGVPEAEIT-RRVDEALTLVDAQhfrHQPIQCLSHGQKKRVAIAGALVLQARYLLLDEPTAGLDPAGRTQMIAIIRRIV 183
|
170 180 190
....*....|....*....|....*....|....*..
gi 1720366319 685 KNTDRgALLTTHYMAEAEALCDRVAILVSGRLRCIGS 721
Cdd:PRK13638 184 AQGNH-VIISSHDIDLIYEISDAVYVLRQGQILTHGA 219
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
527-716 |
7.98e-12 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 68.54 E-value: 7.98e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366319 527 RNVSFCVRKGEILGLLGHNGAGKSTSLKMISGDTKVTAGQVLLKGsRE--GDTPGF-----LGYCP---QENAL------ 590
Cdd:PRK15439 280 RNISLEVRAGEILGLAGVVGAGRTELAETLYGLRPARGGRIMLNG-KEinALSTAQrlargLVYLPedrQSSGLyldapl 358
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366319 591 -WPNLTVKEHLEIF-------AAVrgLRKSHAAVAItRLADAlklqDQlksPVKTLSEGVKRKLCFVLSILGNPSILLLD 662
Cdd:PRK15439 359 aWNVCALTHNRRGFwikpareNAV--LERYRRALNI-KFNHA----EQ---AARTLSGGNQQKVLIAKCLEASPQLLIVD 428
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1720366319 663 EPSTGLDPEGQQQIWQAIRAIIK-NTdrGALLTTHYMAEAEALCDRVAILVSGRL 716
Cdd:PRK15439 429 EPTRGVDVSARNDIYQLIRSIAAqNV--AVLFISSDLEEIEQMADRVLVMHQGEI 481
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
527-671 |
9.48e-12 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 68.38 E-value: 9.48e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366319 527 RNVSFCVRKGEILGLLGHNGAGKSTSLKMISGDTKVTAGQVllKGSREGDtpgfLGYCPQENALW--PNLTVKEHLEIFA 604
Cdd:PRK15064 336 KNLNLLLEAGERLAIIGENGVGKTTLLRTLVGELEPDSGTV--KWSENAN----IGYYAQDHAYDfeNDLTLFDWMSQWR 409
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1720366319 605 -------AVRGlrkshaavAITRLadaLKLQDQLKSPVKTLSEGVKRKLCFVLSILGNPSILLLDEPSTGLDPE 671
Cdd:PRK15064 410 qegddeqAVRG--------TLGRL---LFSQDDIKKSVKVLSGGEKGRMLFGKLMMQKPNVLVMDEPTNHMDME 472
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
525-787 |
9.61e-12 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 66.30 E-value: 9.61e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366319 525 ATRNVSFCVRKGEILGLLGHNGAGKSTSLKMISGDTKVTAGQVLLKGSRegdtpgflgyCPQENALW-----------PN 593
Cdd:PRK13647 20 ALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGRE----------VNAENEKWvrskvglvfqdPD 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366319 594 -----LTVKEHLEIFAAVRGLRKSHAAVAITRLADALKLQDQLKSPVKTLSEGVKRKLCFVLSILGNPSILLLDEPSTGL 668
Cdd:PRK13647 90 dqvfsSTVWDDVAFGPVNMGLDKDEVERRVEEALKAVRMWDFRDKPPYHLSYGQKKRVAIAGVLAMDPDVIVLDEPMAYL 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366319 669 DPEGQQQIwQAIRAIIKNTDRGALLTTHYMAEAEALCDRVAILVSGRLRCIGsiqhlkskfGKDYLLEMKVktLEQVE-- 746
Cdd:PRK13647 170 DPRGQETL-MEILDRLHNQGKTVIVATHDVDLAAEWADQVIVLKEGRVLAEG---------DKSLLTDEDI--VEQAGlr 237
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 1720366319 747 -PLNTEILRLFPQASRQerysslmayKLPV---EAVQPLSQAFFK 787
Cdd:PRK13647 238 lPLVAQIFEDLPELGQS---------KLPLtvkEAVQIIRKLLTK 273
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
527-735 |
1.03e-11 |
|
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 (also known as ABCB6) is a mitochondrial ATP-binding cassette protein involved in iron homeostasis and one of four ABC transporters expressed in the mitochondrial inner membrane, the other three being MDL1(ABC7), MDL2, and ATM1. In fact, the yeast MDL1 (multidrug resistance-like protein 1) and MDL2 (multidrug resistance-like protein 2) transporters are also included in this CD. MDL1 is an ATP-dependent permease that acts as a high-copy suppressor of ATM1 and is thought to have a role in resistance to oxidative stress. Interestingly, subfamily B is more closely related to the carboxyl-terminal component of subfamily C than the two halves of ABCC molecules are with one another.
Pssm-ID: 213216 [Multi-domain] Cd Length: 238 Bit Score: 65.64 E-value: 1.03e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366319 527 RNVSFCVRKGEILGLLGHNGAGKSTSLKMISGDTKVTAGQVLLKGS--REGDTPGF---LGYCPQENALWPNlTVKEHLE 601
Cdd:cd03249 20 KGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEILLDGVdiRDLNLRWLrsqIGLVSQEPVLFDG-TIAENIR 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366319 602 IfaavrGLRKSHA--AVAITRLADA----LKLQDQLKSPV----KTLSEGVKRKLCFVLSILGNPSILLLDEPSTGLDPE 671
Cdd:cd03249 99 Y-----GKPDATDeeVEEAAKKANIhdfiMSLPDGYDTLVgergSQLSGGQKQRIAIARALLRNPKILLLDEATSALDAE 173
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1720366319 672 GQQQIWQAIRAIIKNtdRGALLTTHYMAEAEAlCDRVAILVSGRLRCIGSIQHLKSKFGKDYLL 735
Cdd:cd03249 174 SEKLVQEALDRAMKG--RTTIVIAHRLSTIRN-ADLIAVLQNGQVVEQGTHDELMAQKGVYAKL 234
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
528-723 |
1.06e-11 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 67.42 E-value: 1.06e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366319 528 NVSFCVRKGEILGLLGHNGAGKSTSLKMISGDTKVTAGQVLLKG---SREGDTPGFLGYCPQENALWPNLTVKEHLEIFA 604
Cdd:PRK10851 20 DISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFHGtdvSRLHARDRKVGFVFQHYALFRHMTVFDNIAFGL 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366319 605 AV--RGLRKSHAAV--AITRLADALKLQDQLKSPVKTLSEGVKRKLCFVLSILGNPSILLLDEPSTGLDPEGQQQIWQAI 680
Cdd:PRK10851 100 TVlpRRERPNAAAIkaKVTQLLEMVQLAHLADRYPAQLSGGQKQRVALARALAVEPQILLLDEPFGALDAQVRKELRRWL 179
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1720366319 681 RAIIKNTDRGALLTTHYMAEAEALCDRVAILVSGRLRCIGSIQ 723
Cdd:PRK10851 180 RQLHEELKFTSVFVTHDQEEAMEVADRVVVMSQGNIEQAGTPD 222
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
533-698 |
1.18e-11 |
|
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440858 [Multi-domain] Cd Length: 592 Bit Score: 68.27 E-value: 1.18e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366319 533 VRKGEILGLLGHNGAGKSTSLKMISGDTKVTAGQVLLKGSregdtpgfLGYCPQENALWPNLTVKEHLEifaavrglrkS 612
Cdd:COG1245 363 IREGEVLGIVGPNGIGKTTFAKILAGVLKPDEGEVDEDLK--------ISYKPQYISPDYDGTVEEFLR----------S 424
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366319 613 HAAVAI------TRLADALKLQDQLKSPVKTLSEGVKRKLCFVLSILGNPSILLLDEPSTGLDPEGQQQIWQAIRAIIKN 686
Cdd:COG1245 425 ANTDDFgssyykTEIIKPLGLEKLLDKNVKDLSGGELQRVAIAACLSRDADLYLLDEPSAHLDVEQRLAVAKAIRRFAEN 504
|
170
....*....|....
gi 1720366319 687 TDRGALLTTH--YM 698
Cdd:COG1245 505 RGKTAMVVDHdiYL 518
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
525-729 |
1.22e-11 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 66.06 E-value: 1.22e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366319 525 ATRNVSFCVRKGEILGLLGHNGAGKSTSLKMISGDTKVTAGQVLLKG--SREGDTPGFLGYCPQ-ENALWPNLTVKEHLE 601
Cdd:PRK15056 22 ALRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKISILGqpTRQALQKNLVAYVPQsEEVDWSFPVLVEDVV 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366319 602 I---FAAVRGLR--KSHAAVAITRLADALKLQDQLKSPVKTLSEGVKRKLCFVLSILGNPSILLLDEPSTGLDPEGQQQI 676
Cdd:PRK15056 102 MmgrYGHMGWLRraKKRDRQIVTAALARVDMVEFRHRQIGELSGGQKKRVFLARAIAQQGQVILLDEPFTGVDVKTEARI 181
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1720366319 677 WQAIRAiIKNTDRGALLTTHYMAEAEALCD-----RVAILVSGRLRCIGSIQHLKSKF 729
Cdd:PRK15056 182 ISLLRE-LRDEGKTMLVSTHNLGSVTEFCDytvmvKGTVLASGPTETTFTAENLELAF 238
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
491-696 |
1.30e-11 |
|
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: 67.77 E-value: 1.30e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366319 491 STSFDEKPVIIASCLRKEYAGKQkhclskkkakIATRNVSFCVRKGEILGLLGHNGAGKSTSLKMISGDTKVTAGQVLLK 570
Cdd:TIGR02868 326 GAVGLGKPTLELRDLSAGYPGAP----------PVLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPLQGEVTLD 395
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366319 571 G-----SREGDTPGFLGYCPQENALWpNLTVKEHLEIFAAVRGLRKSHAAVAITRLADALK-LQDQLKSPV----KTLSE 640
Cdd:TIGR02868 396 GvpvssLDQDEVRRRVSVCAQDAHLF-DTTVRENLRLARPDATDEELWAALERVGLADWLRaLPDGLDTVLgeggARLSG 474
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1720366319 641 GVKRKLCFVLSILGNPSILLLDEPSTGLDPEGQQQIWQAIRAIikNTDRGALLTTH 696
Cdd:TIGR02868 475 GERQRLALARALLADAPILLLDEPTEHLDAETADELLEDLLAA--LSGRTVVLITH 528
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
523-733 |
1.44e-11 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 65.49 E-value: 1.44e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366319 523 KIATRNVSFCVRKGEILGLLGHNGAGKSTSLKMISGDTKVTAGQVLLKGSREGDTPGFLGYCPQENALWPNLTVKEHLEI 602
Cdd:PRK11248 14 KPALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDGKPVEGPGAERGVVFQNEGLLPWRNVQDNVAF 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366319 603 FAAVRGLRKSHAAVAITRLADALKLQDQLKSPVKTLSEGVKRKLCFVLSILGNPSILLLDEPSTGLDPEGQQQIWQAIRA 682
Cdd:PRK11248 94 GLQLAGVEKMQRLEIAHQMLKKVGLEGAEKRYIWQLSGGQRQRVGIARALAANPQLLLLDEPFGALDAFTREQMQTLLLK 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1720366319 683 IIKNTDRGALLTTHYMAEAEALCDRVAILVSGRLRCigsIQHLKSKFGKDY 733
Cdd:PRK11248 174 LWQETGKQVLLITHDIEEAVFMATELVLLSPGPGRV---VERLPLNFARRF 221
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
536-669 |
2.71e-11 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 67.21 E-value: 2.71e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366319 536 GEILGLLGHNGAGKSTSLKMISGDTKVT--AGQVLLKGSR-EGDTPGFLGYCPQENALWPNLTVKEHLeIFAAVRGLRKS 612
Cdd:PLN03211 94 GEILAVLGPSGSGKSTLLNALAGRIQGNnfTGTILANNRKpTKQILKRTGFVTQDDILYPHLTVRETL-VFCSLLRLPKS 172
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1720366319 613 HAAVAITRLADAL-------KLQDQL--KSPVKTLSEGVKRKLCFVLSILGNPSILLLDEPSTGLD 669
Cdd:PLN03211 173 LTKQEKILVAESViselgltKCENTIigNSFIRGISGGERKRVSIAHEMLINPSLLILDEPTSGLD 238
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
528-725 |
3.25e-11 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 65.90 E-value: 3.25e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366319 528 NVSFCVRKGEILGLLGHNGAGKSTSLKMISGDTKVTAGQVLLKGSREGDTP--------GFLGYcpqenALWPNLTVKEH 599
Cdd:PRK11432 24 NLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIFIDGEDVTHRSiqqrdicmVFQSY-----ALFPHMSLGEN 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366319 600 LEIFAAVRGLRKSHAAvaiTRLADALKLQDQL---KSPVKTLSEGVKRKLCFVLSILGNPSILLLDEPSTGLDPEGQQQI 676
Cdd:PRK11432 99 VGYGLKMLGVPKEERK---QRVKEALELVDLAgfeDRYVDQISGGQQQRVALARALILKPKVLLFDEPLSNLDANLRRSM 175
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1720366319 677 WQAIRAIIKNTDRGALLTTHYMAEAEALCDRVAILVSGRLRCIGSIQHL 725
Cdd:PRK11432 176 REKIRELQQQFNITSLYVTHDQSEAFAVSDTVIVMNKGKIMQIGSPQEL 224
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
498-731 |
4.69e-11 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 64.32 E-value: 4.69e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366319 498 PVIIASCLRKEYAGKQkhCLSKKKAKIATRNVSFCVRKGEILGLLGHNGAGKSTSLKMISGDTKVTAGQVLLKG------ 571
Cdd:PRK10419 2 TLLNVSGLSHHYAHGG--LSGKHQHQTVLNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWRGeplakl 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366319 572 SREG-------------DTPGflgycpqenALWPNLTVKEHL-EIFAAVRGLRKSHAAVAITRLADALKLQDQL--KSPv 635
Cdd:PRK10419 80 NRAQrkafrrdiqmvfqDSIS---------AVNPRKTVREIIrEPLRHLLSLDKAERLARASEMLRAVDLDDSVldKRP- 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366319 636 KTLSEGVKRKLCFVLSILGNPSILLLDEPSTGLDPEGQQQIWQAIRAIIKNTDRGALLTTHYMAEAEALCDRVAILVSGR 715
Cdd:PRK10419 150 PQLSGGQLQRVCLARALAVEPKLLILDEAVSNLDLVLQAGVIRLLKKLQQQFGTACLFITHDLRLVERFCQRVMVMDNGQ 229
|
250
....*....|....*....
gi 1720366319 716 L---RCIGSIQHLKSKFGK 731
Cdd:PRK10419 230 IvetQPVGDKLTFSSPAGR 248
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
525-721 |
5.23e-11 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 64.26 E-value: 5.23e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366319 525 ATRNVSFCVRKGEILGLLGHNGAGKSTSLKM------------ISGDTKVTAGQVLLKGSREGDTPGFLGYCPQENALWP 592
Cdd:PRK13645 26 ALNNTSLTFKKNKVTCVIGTTGSGKSTMIQLtngliisetgqtIVGDYAIPANLKKIKEVKRLRKEIGLVFQFPEYQLFQ 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366319 593 NlTVKEHLEIFAAVRGLRKSHAAVAITRLADALKL-QDQLKSPVKTLSEGVKRKLCFVLSILGNPSILLLDEPSTGLDPE 671
Cdd:PRK13645 106 E-TIEKDIAFGPVNLGENKQEAYKKVPELLKLVQLpEDYVKRSPFELSGGQKRRVALAGIIAMDGNTLVLDEPTGGLDPK 184
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1720366319 672 GQQQIWQAIRAIIKNTDRGALLTTHYMAEAEALCDRVAILVSGRLRCIGS 721
Cdd:PRK13645 185 GEEDFINLFERLNKEYKKRIIMVTHNMDQVLRIADEVIVMHEGKVISIGS 234
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
518-716 |
5.31e-11 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 63.64 E-value: 5.31e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366319 518 SKKKAkiaTRNVSFCVRKGEILGLLGHNGAGKSTSLKMIS--GD---TKVTAGQVLLKG----SREGDTPGF---LGYCP 585
Cdd:PRK14239 16 NKKKA---LNSVSLDFYPNEITALIGPSGSGKSTLLRSINrmNDlnpEVTITGSIVYNGhniySPRTDTVDLrkeIGMVF 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366319 586 QENALWPnLTVKEHLEIFAAVRGLRKSH---AAVAITRLADAL--KLQDQLKSPVKTLSEGVKRKLCFVLSILGNPSILL 660
Cdd:PRK14239 93 QQPNPFP-MSIYENVVYGLRLKGIKDKQvldEAVEKSLKGASIwdEVKDRLHDSALGLSGGQQQRVCIARVLATSPKIIL 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1720366319 661 LDEPSTGLDPEGQQQIWQAIRAIIKntDRGALLTTHYMAEAEALCDRVAILVSGRL 716
Cdd:PRK14239 172 LDEPTSALDPISAGKIEETLLGLKD--DYTMLLVTRSMQQASRISDRTGFFLDGDL 225
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
499-699 |
5.71e-11 |
|
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of the ABC transporter ATP-binding cassette, but are found outside the common ABC transporter operon structure that features integral membrane permease proteins and substrate-binding proteins encoded next to the ATP-binding cassette (ABC domain) protein. The member protein ChvD from Agrobacterium tumefaciens was identified as both a candidate to interact with VirB8, based on yeast two-hybrid analysis, and as an apparent regulator of VirG. The general function of this protein family is unknown.
Pssm-ID: 274744 [Multi-domain] Cd Length: 552 Bit Score: 66.11 E-value: 5.71e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366319 499 VIIASCLRKEYAGKqkhclskkkakIATRNVSFCVRKGEILGLLGHNGAGKSTSLKMISGDTKVTAGQVLLkgsreGDTP 578
Cdd:TIGR03719 322 VIEAENLTKAFGDK-----------LLIDDLSFKLPPGGIVGVIGPNGAGKSTLFRMITGQEQPDSGTIEI-----GETV 385
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366319 579 GfLGYCPQE-NALWPNLTVKE-------HLEIfaavrGLRKSHAAVAITRLadALKLQDQLKsPVKTLSEGVKRKLCFVL 650
Cdd:TIGR03719 386 K-LAYVDQSrDALDPNKTVWEeisggldIIKL-----GKREIPSRAYVGRF--NFKGSDQQK-KVGQLSGGERNRVHLAK 456
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1720366319 651 SILGNPSILLLDEPSTGLDPEGQQQIWQAIR-----AIIKNTDRGAL--LTTHYMA 699
Cdd:TIGR03719 457 TLKSGGNVLLLDEPTNDLDVETLRALEEALLnfagcAVVISHDRWFLdrIATHILA 512
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
528-715 |
8.49e-11 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 65.50 E-value: 8.49e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366319 528 NVSFCVRKGEILGLLGHNGAGKS-TSLKMI-----------SGDTKVtAGQVLLKGSrEGDTPGFLG----YCPQEN--A 589
Cdd:PRK15134 27 DVSLQIEAGETLALVGESGSGKSvTALSILrllpsppvvypSGDIRF-HGESLLHAS-EQTLRGVRGnkiaMIFQEPmvS 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366319 590 LWPNLTVKEHL-EIFAAVRGLRKSHAAVAITRLADALKLQD---QLKSPVKTLSEGVKRKLCFVLSILGNPSILLLDEPS 665
Cdd:PRK15134 105 LNPLHTLEKQLyEVLSLHRGMRREAARGEILNCLDRVGIRQaakRLTDYPHQLSGGERQRVMIAMALLTRPELLIADEPT 184
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1720366319 666 TGLDPEGQQQIWQAIRAIIKNTDRGALLTTHYMAEAEALCDRVAILVSGR 715
Cdd:PRK15134 185 TALDVSVQAQILQLLRELQQELNMGLLFITHNLSIVRKLADRVAVMQNGR 234
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
525-715 |
9.14e-11 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 65.34 E-value: 9.14e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366319 525 ATRNVSFCVRKGEILGLLGHNGAGKSTSLKMISG-------DTKVT-AGQVL-LKGSREGDTPGfLGYCPQENALWPNLT 595
Cdd:PRK13549 20 ALDNVSLKVRAGEIVSLCGENGAGKSTLMKVLSGvyphgtyEGEIIfEGEELqASNIRDTERAG-IAIIHQELALVKELS 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366319 596 VKEHL----EIfaaVRGLRKSHAAVaitrLADALKLQDQLK------SPVKTLSEGvKRKLCFVLSILG-NPSILLLDEP 664
Cdd:PRK13549 99 VLENIflgnEI---TPGGIMDYDAM----YLRAQKLLAQLKldinpaTPVGNLGLG-QQQLVEIAKALNkQARLLILDEP 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1720366319 665 STGLDpEGQQQIWQAIRAIIKNTDRGALLTTHYMAEAEALCDRVAILVSGR 715
Cdd:PRK13549 171 TASLT-ESETAVLLDIIRDLKAHGIACIYISHKLNEVKAISDTICVIRDGR 220
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
529-716 |
1.06e-10 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 63.19 E-value: 1.06e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366319 529 VSFCVRKGEILGLLGHNGAGKSTSLKMISGDTKVTAGQVLLKGSREGDTP--------GFLGYCPQENALwpNLTVKEHL 600
Cdd:PRK13642 26 VSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDGELLTAENvwnlrrkiGMVFQNPDNQFV--GATVEDDV 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366319 601 EIFAAVRGLRKSHAavaITRLADAL----KLQDQLKSPVKtLSEGVKRKLCFVLSILGNPSILLLDEPSTGLDPEGQQQI 676
Cdd:PRK13642 104 AFGMENQGIPREEM---IKRVDEALlavnMLDFKTREPAR-LSGGQKQRVAVAGIIALRPEIIILDESTSMLDPTGRQEI 179
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1720366319 677 WQAIRAIIKNTDRGALLTTHYMAEAeALCDRVAILVSGRL 716
Cdd:PRK13642 180 MRVIHEIKEKYQLTVLSITHDLDEA-ASSDRILVMKAGEI 218
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
527-708 |
1.19e-10 |
|
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: 62.45 E-value: 1.19e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366319 527 RNVSFCVRKGEILGLLGHNGAGKSTSLKMISGDTKVTAGQVLLKgSREG-----------------DTpgfLGYCPQ-EN 588
Cdd:COG4778 28 DGVSFSVAAGECVALTGPSGAGKSTLLKCIYGNYLPDSGSILVR-HDGGwvdlaqaspreilalrrRT---IGYVSQfLR 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366319 589 ALwPNLTVkehLEIFAA---VRGLRKSHAAVAITRLADALKLQDQLKS-PVKTLSEGVKRKLCFVLSILGNPSILLLDEP 664
Cdd:COG4778 104 VI-PRVSA---LDVVAEpllERGVDREEARARARELLARLNLPERLWDlPPATFSGGEQQRVNIARGFIADPPLLLLDEP 179
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1720366319 665 STGLDPEGQQQIWQAIRAIIkntDRG-ALLT-THYMAEAEALCDRV 708
Cdd:COG4778 180 TASLDAANRAVVVELIEEAK---ARGtAIIGiFHDEEVREAVADRV 222
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
505-721 |
1.26e-10 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 64.09 E-value: 1.26e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366319 505 LRKEYAGKQKhclskkkakiATRNVSFCVRKGEILGLLGHNGAGKSTSLKMISGDTKVTAGQVLLKGSREGD-TPG---- 579
Cdd:PRK11650 9 VRKSYDGKTQ----------VIKGIDLDVADGEFIVLVGPSGCGKSTLLRMVAGLERITSGEIWIGGRVVNElEPAdrdi 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366319 580 ---FLGYcpqenALWPNLTVKEHLEIFAAVRGLRKSHAAVAITRLADALKLQDQLKSPVKTLSEGVKRKLCFVLSILGNP 656
Cdd:PRK11650 79 amvFQNY-----ALYPHMSVRENMAYGLKIRGMPKAEIEERVAEAARILELEPLLDRKPRELSGGQRQRVAMGRAIVREP 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1720366319 657 SILLLDEPSTGLDPEGQQQiwqaIRAIIKNTDR----GALLTTHYMAEAEALCDRVAILVSGRLRCIGS 721
Cdd:PRK11650 154 AVFLFDEPLSNLDAKLRVQ----MRLEIQRLHRrlktTSLYVTHDQVEAMTLADRVVVMNGGVAEQIGT 218
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
525-715 |
1.29e-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: 64.85 E-value: 1.29e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366319 525 ATRNVSFCVRKGEILGLLGHNGAGKSTSLKMISG--DTKVTAGQVLLKGS-------REGDTPGfLGYCPQENALWPNLT 595
Cdd:TIGR02633 16 ALDGIDLEVRPGECVGLCGENGAGKSTLMKILSGvyPHGTWDGEIYWSGSplkasniRDTERAG-IVIIHQELTLVPELS 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366319 596 VKEHL----EIfaAVRGLRKSHAavAITRLADALKLQDQLKS-----PVKTLSEGVKRKLCFVLSILGNPSILLLDEPST 666
Cdd:TIGR02633 95 VAENIflgnEI--TLPGGRMAYN--AMYLRAKNLLRELQLDAdnvtrPVGDYGGGQQQLVEIAKALNKQARLLILDEPSS 170
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1720366319 667 GLDPEGQQQIWQAIRAiIKNTDRGALLTTHYMAEAEALCDRVAILVSGR 715
Cdd:TIGR02633 171 SLTEKETEILLDIIRD-LKAHGVACVYISHKLNEVKAVCDTICVIRDGQ 218
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
527-696 |
1.37e-10 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 61.90 E-value: 1.37e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366319 527 RNVSFCVRKGEILGLLGHNGAGKSTSLKMISGdtkvtagqvllkgsREGDTPGFLGYCPQENALWPNLTVKEHLeifaav 606
Cdd:COG2401 47 RDLNLEIEPGEIVLIVGASGSGKSTLLRLLAG--------------ALKGTPVAGCVDVPDNQFGREASLIDAI------ 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366319 607 rgLRKSHAAVAITRLADAlKLQDQ--LKSPVKTLSEGVKRKLCFVLSILGNPSILLLDEPSTGLDPEGQQQIWQAIRAII 684
Cdd:COG2401 107 --GRKGDFKDAVELLNAV-GLSDAvlWLRRFKELSTGQKFRFRLALLLAERPKLLVIDEFCSHLDRQTAKRVARNLQKLA 183
|
170
....*....|..
gi 1720366319 685 KNTDRGALLTTH 696
Cdd:COG2401 184 RRAGITLVVATH 195
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
525-730 |
1.61e-10 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 64.46 E-value: 1.61e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366319 525 ATRNVSFCVRKGEILGLLGHNGAGKSTSLKMISGDTKVTAGQVLLKGSREGDTPgflgycpqENALWPNLT-VKEHLEIF 603
Cdd:PRK11160 355 VLKGLSLQIKAGEKVALLGRTGCGKSTLLQLLTRAWDPQQGEILLNGQPIADYS--------EAALRQAISvVSQRVHLF 426
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366319 604 AAVrgLRKS--HAAVAIT--RLADALK---LQDQLKSPV----------KTLSEGVKRKLCFVLSILGNPSILLLDEPST 666
Cdd:PRK11160 427 SAT--LRDNllLAAPNASdeALIEVLQqvgLEKLLEDDKglnawlgeggRQLSGGEQRRLGIARALLHDAPLLLLDEPTE 504
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1720366319 667 GLDPEGQQQIWQAIRAIIKntDRGALLTTHYMAEAEALcDRVAILVSGRLRCIGSIQHLKSKFG 730
Cdd:PRK11160 505 GLDAETERQILELLAEHAQ--NKTVLMITHRLTGLEQF-DRICVMDNGQIIEQGTHQELLAQQG 565
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
527-715 |
1.80e-10 |
|
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: 61.33 E-value: 1.80e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366319 527 RNVSFCVRKGEILGLLGHNGAGKSTSLKMISGDTKVTAGQVLLKGSregdtpgfLGYCPQENalW-PNLTVKEHLeIFaa 605
Cdd:cd03250 22 KDINLEVPKGELVAIVGPVGSGKSSLLSALLGELEKLSGSVSVPGS--------IAYVSQEP--WiQNGTIRENI-LF-- 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366319 606 vrGLRKSHAavaitRLADALK---LQDQLKSPVK-----------TLSEGVKRKLCFVLSILGNPSILLLDEPSTGLDPE 671
Cdd:cd03250 89 --GKPFDEE-----RYEKVIKacaLEPDLEILPDgdlteigekgiNLSGGQKQRISLARAVYSDADIYLLDDPLSAVDAH 161
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1720366319 672 GQQQIWQ-AIRAIIKNtDRGALLTTHYMAEAEAlCDRVAILVSGR 715
Cdd:cd03250 162 VGRHIFEnCILGLLLN-NKTRILVTHQLQLLPH-ADQIVVLDNGR 204
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
520-716 |
2.85e-10 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 61.77 E-value: 2.85e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366319 520 KKAKIATRNVSFCVRKGEILGLLGHNGAGKSTSLKMISGD---------TKVTaGQVLLKGSREGDTPGFLGYC-----P 585
Cdd:PRK13547 11 RRHRAILRDLSLRIEPGRVTALLGRNGAGKSTLLKALAGDltgggaprgARVT-GDVTLNGEPLAAIDAPRLARlravlP 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366319 586 QENALWPNLTVKEHLEIFA---AVRGLRKSHAAVAITRLADALKLQDQL-KSPVKTLSEGVKRKLCF--VLSIL------ 653
Cdd:PRK13547 90 QAAQPAFAFSAREIVLLGRyphARRAGALTHRDGEIAWQALALAGATALvGRDVTTLSGGELARVQFarVLAQLwpphda 169
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1720366319 654 -GNPSILLLDEPSTGLDPEGQQQIWQAIRAIIKNTDRGALLTTHYMAEAEALCDRVAILVSGRL 716
Cdd:PRK13547 170 aQPPRYLLLDEPTAALDLAHQHRLLDTVRRLARDWNLGVLAIVHDPNLAARHADRIAMLADGAI 233
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
522-763 |
3.42e-10 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 61.96 E-value: 3.42e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366319 522 AKIATRNVSFCVRKGEILGLLGHNGAGKSTSLKMISGDTKVTAGQVLLkGSREgDTPGF-----------LGYCPQ--EN 588
Cdd:PRK13634 19 ERRALYDVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVTI-GERV-ITAGKknkklkplrkkVGIVFQfpEH 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366319 589 ALW-----------P-NLTVKEHleifaavRGLRKSHAAVAITRLADALkLQdqlKSPVKtLSEGVKRKLCF--VLSIlg 654
Cdd:PRK13634 97 QLFeetvekdicfgPmNFGVSEE-------DAKQKAREMIELVGLPEEL-LA---RSPFE-LSGGQMRRVAIagVLAM-- 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366319 655 NPSILLLDEPSTGLDPEGQQQIWQAIRAIIKNTDRGALLTTHYMAEAEALCDRVAILVSGRLRCIGSIQHLKSKfgKDYL 734
Cdd:PRK13634 163 EPEVLVLDEPTAGLDPKGRKEMMEMFYKLHKEKGLTTVLVTHSMEDAARYADQIVVMHKGTVFLQGTPREIFAD--PDEL 240
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 1720366319 735 LEMKV---------KTLEQ------------VEPLNTEILRLFPQASRQE 763
Cdd:PRK13634 241 EAIGLdlpetvkfkRALEEkfgisfpkpcltLEELAHEVVQLLRKGGHES 290
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
495-715 |
3.68e-10 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 61.48 E-value: 3.68e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366319 495 DEKPVIIASCLRKEYAGKqkhclskkkakIATRNVSFCVRKGEILGLLGHNGAGKSTSLKMISGDTKVTAGQVLLKGsRE 574
Cdd:PRK11701 2 MDQPLLSVRGLTKLYGPR-----------KGCRDVSFDLYPGEVLGIVGESGSGKTTLLNALSARLAPDAGEVHYRM-RD 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366319 575 GDTPG----------FL-----GYCPQ--ENALWPNLT----VKEHL---------EIFA-AVRGLRKshaaVAItrlaD 623
Cdd:PRK11701 70 GQLRDlyalseaerrRLlrtewGFVHQhpRDGLRMQVSaggnIGERLmavgarhygDIRAtAGDWLER----VEI----D 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366319 624 ALKLQDQlksPvKTLSEGVKRKLCFVLSILGNPSILLLDEPSTGLDPEGQQQIWQAIRAIIKNTDRGALLTTHYMAEAEA 703
Cdd:PRK11701 142 AARIDDL---P-TTFSGGMQQRLQIARNLVTHPRLVFMDEPTGGLDVSVQARLLDLLRGLVRELGLAVVIVTHDLAVARL 217
|
250
....*....|..
gi 1720366319 704 LCDRVAILVSGR 715
Cdd:PRK11701 218 LAHRLLVMKQGR 229
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
527-720 |
3.99e-10 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 61.40 E-value: 3.99e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366319 527 RNVSFCVRKGEILGLLGHNGAGKSTSLKM------ISGDTKVTaGQVLLKG----SREGDTPGF---LGYCPQENALWPN 593
Cdd:PRK14267 21 KGVDLKIPQNGVFALMGPSGCGKSTLLRTfnrlleLNEEARVE-GEVRLFGrniySPDVDPIEVrreVGMVFQYPNPFPH 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366319 594 LTVKEHLEIFAAVRGLRKSHAAV------AITRLADALKLQDQLKSPVKTLSEGVKRKLCFVLSILGNPSILLLDEPSTG 667
Cdd:PRK14267 100 LTIYDNVAIGVKLNGLVKSKKELdervewALKKAALWDEVKDRLNDYPSNLSGGQRQRLVIARALAMKPKILLMDEPTAN 179
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1720366319 668 LDPEGQQQIWQAIRAIikNTDRGALLTTHYMAEAEALCDRVAILVSGRLRCIG 720
Cdd:PRK14267 180 IDPVGTAKIEELLFEL--KKEYTIVLVTHSPAQAARVSDYVAFLYLGKLIEVG 230
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
527-696 |
4.42e-10 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 63.71 E-value: 4.42e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366319 527 RNVSFCVRKGEILGLLGHNGAGKSTSLKMISGdtKVTAGQVllkgsrEGDT--PGF----------LGYCPQENALWPNL 594
Cdd:PLN03140 897 REVTGAFRPGVLTALMGVSGAGKTTLMDVLAG--RKTGGYI------EGDIriSGFpkkqetfariSGYCEQNDIHSPQV 968
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366319 595 TVKEHLeIFAAVRGLRKSHAAVAITRLADA---LKLQDQLKSP------VKTLSEGVKRKLCFVLSILGNPSILLLDEPS 665
Cdd:PLN03140 969 TVRESL-IYSAFLRLPKEVSKEEKMMFVDEvmeLVELDNLKDAivglpgVTGLSTEQRKRLTIAVELVANPSIIFMDEPT 1047
|
170 180 190
....*....|....*....|....*....|.
gi 1720366319 666 TGLDPEGQQQIWQAIRAIIkNTDRGALLTTH 696
Cdd:PLN03140 1048 SGLDARAAAIVMRTVRNTV-DTGRTVVCTIH 1077
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
527-721 |
6.38e-10 |
|
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: 59.81 E-value: 6.38e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366319 527 RNVSFCVRKGEILGLLGHNGAGKST---SL-KMISgdtkVTAGQVLLKG---SREG--DTPGFLGYCPQEnalwPNL--- 594
Cdd:cd03244 21 KNISFSIKPGEKVGIVGRTGSGKSSlllALfRLVE----LSSGSILIDGvdiSKIGlhDLRSRISIIPQD----PVLfsg 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366319 595 TVKEHL---------EIFAAvrgLRKSHAAVAITRLADalKLQDQLKSPVKTLSEGVKRKLCFVLSILGNPSILLLDEPS 665
Cdd:cd03244 93 TIRSNLdpfgeysdeELWQA---LERVGLKEFVESLPG--GLDTVVEEGGENLSVGQRQLLCLARALLRKSKILVLDEAT 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1720366319 666 TGLDPEGQQQIWQAIRAIIKntDRGALLTTHYMaEAEALCDRVAILVSGRLRCIGS 721
Cdd:cd03244 168 ASVDPETDALIQKTIREAFK--DCTVLTIAHRL-DTIIDSDRILVLDKGRVVEFDS 220
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
522-721 |
6.85e-10 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 60.90 E-value: 6.85e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366319 522 AKIATRNVSFCVRKGEILGLLGHNGAGKSTSLKMISGDTKVTAGQV------LLKGSREGDTP------GFLGYCPqENA 589
Cdd:PRK13643 18 ASRALFDIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVtvgdivVSSTSKQKEIKpvrkkvGVVFQFP-ESQ 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366319 590 LWPNLTVKEhLEIFAAVRGLRKSHAAVAITRLADALKLQDQL--KSPVKtLSEGVKRKLCFVLSILGNPSILLLDEPSTG 667
Cdd:PRK13643 97 LFEETVLKD-VAFGPQNFGIPKEKAEKIAAEKLEMVGLADEFweKSPFE-LSGGQMRRVAIAGILAMEPEVLVLDEPTAG 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1720366319 668 LDPEGQQQIWQAIRAiIKNTDRGALLTTHYMAEAEALCDRVAILVSGRLRCIGS 721
Cdd:PRK13643 175 LDPKARIEMMQLFES-IHQSGQTVVLVTHLMDDVADYADYVYLLEKGHIISCGT 227
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
519-695 |
9.23e-10 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 62.82 E-value: 9.23e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366319 519 KKKAKIATRNVSFCVRKGEILGLLGHNGAGKSTSLKMISG--DTKVTAGQVLLKGSREGDT--PGFLGYCPQENALWPNL 594
Cdd:TIGR00956 772 KKEKRVILNNVDGWVKPGTLTALMGASGAGKTTLLNVLAErvTTGVITGGDRLVNGRPLDSsfQRSIGYVQQQDLHLPTS 851
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366319 595 TVKEHLEIFAAVR---GLRKSHAAVAITRLADALKLQDQLKSPVKTLSEGV----KRKLCFVLSILGNPSILL-LDEPST 666
Cdd:TIGR00956 852 TVRESLRFSAYLRqpkSVSKSEKMEYVEEVIKLLEMESYADAVVGVPGEGLnveqRKRLTIGVELVAKPKLLLfLDEPTS 931
|
170 180 190
....*....|....*....|....*....|
gi 1720366319 667 GLDpegQQQIWQAIRAIIKNTDRG-ALLTT 695
Cdd:TIGR00956 932 GLD---SQTAWSICKLMRKLADHGqAILCT 958
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
527-716 |
1.41e-09 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 59.60 E-value: 1.41e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366319 527 RNVSFCVRKGEILGLLGHNGAGKSTSLKMISGDTKVTAGQVLLKGS-------REGDTPGF-----------LGYCPQEN 588
Cdd:PRK10619 22 KGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNGQtinlvrdKDGQLKVAdknqlrllrtrLTMVFQHF 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366319 589 ALWPNLTVKEH-LEIFAAVRGLRKSHAAVAITRLADALKLQD--QLKSPVKtLSEGVKRKLCFVLSILGNPSILLLDEPS 665
Cdd:PRK10619 102 NLWSHMTVLENvMEAPIQVLGLSKQEARERAVKYLAKVGIDEraQGKYPVH-LSGGQQQRVSIARALAMEPEVLLFDEPT 180
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1720366319 666 TGLDPEgqqQIWQAIRAIIKNTDRGA--LLTTHYMAEAEALCDRVAILVSGRL 716
Cdd:PRK10619 181 SALDPE---LVGEVLRIMQQLAEEGKtmVVVTHEMGFARHVSSHVIFLHQGKI 230
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
527-721 |
1.80e-09 |
|
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: 58.58 E-value: 1.80e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366319 527 RNVSFCVRKGEILGLLGHNGAGKSTSLKMISGDTKVTAGQVLLKGSREGDTP-----GFLGYCPQENALWPNlTVKEHLE 601
Cdd:cd03369 25 KNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDGIDISTIPledlrSSLTIIPQDPTLFSG-TIRSNLD 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366319 602 IFAavrglRKSHAavaitRLADALKLqdqlKSPVKTLSEGVKRKLCFVLSILGNPSILLLDEPSTGLDPEGQQQIWQAIR 681
Cdd:cd03369 104 PFD-----EYSDE-----EIYGALRV----SEGGLNLSQGQRQLLCLARALLKRPRVLVLDEATASIDYATDALIQKTIR 169
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1720366319 682 AIIKNTdrgALLTTHYMAEAEALCDRVAILVSGRLRCIGS 721
Cdd:cd03369 170 EEFTNS---TILTIAHRLRTIIDYDKILVMDAGEVKEYDH 206
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
523-721 |
2.72e-09 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 58.91 E-value: 2.72e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366319 523 KIATRNVSFCVRKGEILGLLGHNGAGKSTSLKMISG-----DTKVTA-GQVLLKGSREGDTPGF-----LGYCPQENALW 591
Cdd:PRK14246 23 KAILKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRlieiyDSKIKVdGKVLYFGKDIFQIDAIklrkeVGMVFQQPNPF 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366319 592 PNLTVKEHLEIFAAVRGLRKSHAAVAIT-----RLADALKLQDQLKSPVKTLSEGVKRKLCFVLSILGNPSILLLDEPST 666
Cdd:PRK14246 103 PHLSIYDNIAYPLKSHGIKEKREIKKIVeeclrKVGLWKEVYDRLNSPASQLSGGQQQRLTIARALALKPKVLLMDEPTS 182
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1720366319 667 GLDPEGQQQIWQAIRAIIKntDRGALLTTHYMAEAEALCDRVAILVSGRLRCIGS 721
Cdd:PRK14246 183 MIDIVNSQAIEKLITELKN--EIAIVIVSHNPQQVARVADYVAFLYNGELVEWGS 235
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
527-697 |
3.07e-09 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 58.50 E-value: 3.07e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366319 527 RNVSFCVRKGEILGLLGHNGAGKSTSLKMISG--DTKVTAGQVLLKGSREGDTPgflgycPQENAlwpnltvkeHLEIFA 604
Cdd:CHL00131 24 KGLNLSINKGEIHAIMGPNGSGKSTLSKVIAGhpAYKILEGDILFKGESILDLE------PEERA---------HLGIFL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366319 605 AVRglrkshAAVAIT--------RLADALKLQDQLKSPVKTLS--EGVKRKLCFV------LS----------------- 651
Cdd:CHL00131 89 AFQ------YPIEIPgvsnadflRLAYNSKRKFQGLPELDPLEflEIINEKLKLVgmdpsfLSrnvnegfsggekkrnei 162
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1720366319 652 ---ILGNPSILLLDEPSTGLDPEGQQQIWQAIRaIIKNTDRGALLTTHY 697
Cdd:CHL00131 163 lqmALLDSELAILDETDSGLDIDALKIIAEGIN-KLMTSENSIILITHY 210
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
514-719 |
3.48e-09 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 60.13 E-value: 3.48e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366319 514 KHCLSKKKAKIatRNVSFCVRKGEILGLLGHNGAGKSTSLKMISGDTKVTAGQVLLKG-------------------SRE 574
Cdd:PRK10982 254 RNLTSLRQPSI--RDVSFDLHKGEILGIAGLVGAKRTDIVETLFGIREKSAGTITLHGkkinnhnaneainhgfalvTEE 331
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366319 575 GDTPGFLGYCPQE-NALWPNltVKEHLEIFAAVRGLR-KSHAAVAItrlaDALKLQD-QLKSPVKTLSEGVKRKLCFVLS 651
Cdd:PRK10982 332 RRSTGIYAYLDIGfNSLISN--IRNYKNKVGLLDNSRmKSDTQWVI----DSMRVKTpGHRTQIGSLSGGNQQKVIIGRW 405
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1720366319 652 ILGNPSILLLDEPSTGLDPEGQQQIWQAIRAIIKNtDRGALLTTHYMAEAEALCDRVAILVSGRLRCI 719
Cdd:PRK10982 406 LLTQPEILMLDEPTRGIDVGAKFEIYQLIAELAKK-DKGIIIISSEMPELLGITDRILVMSNGLVAGI 472
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
527-768 |
3.65e-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: 58.71 E-value: 3.65e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366319 527 RNVSFCVRKGEILGLLGHNGAGKST----SLKMIS--GDTK---VTAGQVLLKGSREGdtpgfLGYCPQENALWPNlTVK 597
Cdd:cd03289 21 ENISFSISPGQRVGLLGRTGSGKSTllsaFLRLLNteGDIQidgVSWNSVPLQKWRKA-----FGVIPQKVFIFSG-TFR 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366319 598 EHLEIFAavrglrkSHAAVAITRLADAL-----------KLQDQLKSPVKTLSEGVKRKLCFVLSILGNPSILLLDEPST 666
Cdd:cd03289 95 KNLDPYG-------KWSDEEIWKVAEEVglksvieqfpgQLDFVLVDGGCVLSHGHKQLMCLARSVLSKAKILLLDEPSA 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366319 667 GLDPegqqQIWQAIRAIIKN--TDRGALLTTHYMaEAEALCDRVAILVSGRLRCIGSIQHLKSKfgkdyllemkvKTLEQ 744
Cdd:cd03289 168 HLDP----ITYQVIRKTLKQafADCTVILSEHRI-EAMLECQRFLVIEENKVRQYDSIQKLLNE-----------KSHFK 231
|
250 260
....*....|....*....|....
gi 1720366319 745 VEPLNTEILRLFPQASRQERYSSL 768
Cdd:cd03289 232 QAISPSDRLKLFPRRNSSKSKRKP 255
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
522-701 |
4.05e-09 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 58.61 E-value: 4.05e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366319 522 AKIATRNVSFCVRKGEILGLLGHNGAGKSTSLKMISGDTKVTAGQVLLKGSREGDTpgflgycpqenalwpNLT-VKEHL 600
Cdd:PRK13648 21 ASFTLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIFYNNQAITDD---------------NFEkLRKHI 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366319 601 EI---------------FAAVRGLrKSHAAV---AITRLADALK---LQDQLKSPVKTLSEGVKRKLCFVLSILGNPSIL 659
Cdd:PRK13648 86 GIvfqnpdnqfvgsivkYDVAFGL-ENHAVPydeMHRRVSEALKqvdMLERADYEPNALSGGQKQRVAIAGVLALNPSVI 164
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1720366319 660 LLDEPSTGLDPEGQQQIWQAIRAIIKNTDRGALLTTHYMAEA 701
Cdd:PRK13648 165 ILDEATSMLDPDARQNLLDLVRKVKSEHNITIISITHDLSEA 206
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
533-716 |
4.67e-09 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 57.84 E-value: 4.67e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366319 533 VRKGEILGLLGHNGAGKSTSLKMI-------SGDTKVtaGQVLLKGSRE-GDTPGFL-------GYCPQENALWPNLTVK 597
Cdd:PRK11264 26 VKPGEVVAIIGPSGSGKTTLLRCInlleqpeAGTIRV--GDITIDTARSlSQQKGLIrqlrqhvGFVFQNFNLFPHRTVL 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366319 598 EH-LEIFAAVRGLRKSHAAVAITRLADALKLQDQLKSPVKTLSEGVKRKLCFVLSILGNPSILLLDEPSTGLDPEGQQQI 676
Cdd:PRK11264 104 ENiIEGPVIVKGEPKEEATARARELLAKVGLAGKETSYPRRLSGGQQQRVAIARALAMRPEVILFDEPTSALDPELVGEV 183
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1720366319 677 WQAIRAIIKNtDRGALLTTHYMAEAEALCDRVAILVSGRL 716
Cdd:PRK11264 184 LNTIRQLAQE-KRTMVIVTHEMSFARDVADRAIFMDQGRI 222
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
528-696 |
5.80e-09 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 57.42 E-value: 5.80e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366319 528 NVSFCVRKGEILGLLGHNGAGKSTSLKMISGDTKVTAGQVLLKGSREGDTP-----GFLGYCPQENALWPNlTVKEHLEI 602
Cdd:PRK10247 25 NISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFEGEDISTLKpeiyrQQVSYCAQTPTLFGD-TVYDNLIF 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366319 603 FAAVRglrksHAAVAITRLADALKL----QDQLKSPVKTLSEGVKRKLCFVLSILGNPSILLLDEPSTGLDPEGQQQIWQ 678
Cdd:PRK10247 104 PWQIR-----NQQPDPAIFLDDLERfalpDTILTKNIAELSGGEKQRISLIRNLQFMPKVLLLDEITSALDESNKHNVNE 178
|
170
....*....|....*...
gi 1720366319 679 AIRAIIKNTDRGALLTTH 696
Cdd:PRK10247 179 IIHRYVREQNIAVLWVTH 196
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
522-754 |
6.18e-09 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 57.72 E-value: 6.18e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366319 522 AKIATRNVSFCVRKGEILGLLGHNGAGKSTSLKMISGDTKVTAGQVLLKG-------SRE-GDTPGFLgycPQENALWPN 593
Cdd:PRK11231 14 TKRILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDkpismlsSRQlARRLALL---PQHHLTPEG 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366319 594 LTVKE--------HLEIFAAVRGLRKSHAAVA-----ITRLADalklqdqlkSPVKTLSEGvKRKLCFVLSILG-NPSIL 659
Cdd:PRK11231 91 ITVRElvaygrspWLSLWGRLSAEDNARVNQAmeqtrINHLAD---------RRLTDLSGG-QRQRAFLAMVLAqDTPVV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366319 660 LLDEPSTGLDPEGQQQIWQAIRaIIKNTDRGALLTTHYMAEAEALCDRVAILVSGRLRCIGSIQHLkskfgkdylleMKV 739
Cdd:PRK11231 161 LLDEPTTYLDINHQVELMRLMR-ELNTQGKTVVTVLHDLNQASRYCDHLVVLANGHVMAQGTPEEV-----------MTP 228
|
250
....*....|....*
gi 1720366319 740 KTLEQVEPLNTEILR 754
Cdd:PRK11231 229 GLLRTVFDVEAEIHP 243
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
525-725 |
6.80e-09 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 58.20 E-value: 6.80e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366319 525 ATRNVSFCVRKGEILGLLGHNGAGKSTSLKMISGdtkvtagqVLLKGSREGDTPGFLGY----CPQE------------- 587
Cdd:PRK09473 31 AVNDLNFSLRAGETLGIVGESGSGKSQTAFALMG--------LLAANGRIGGSATFNGReilnLPEKelnklraeqismi 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366319 588 -----NALWPNLTVKEHL-EIFAAVRGLRKSHAAVAITRLADALKLQDQLKS----PvKTLSEGVKRKLCFVLSILGNPS 657
Cdd:PRK09473 103 fqdpmTSLNPYMRVGEQLmEVLMLHKGMSKAEAFEESVRMLDAVKMPEARKRmkmyP-HEFSGGMRQRVMIAMALLCRPK 181
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1720366319 658 ILLLDEPSTGLDPEGQQQIWQAIRAIIKNTDRGALLTTHYMAEAEALCDRVAILVSGRLRCIGSIQHL 725
Cdd:PRK09473 182 LLIADEPTTALDVTVQAQIMTLLNELKREFNTAIIMITHDLGVVAGICDKVLVMYAGRTMEYGNARDV 249
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
536-716 |
7.47e-09 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 57.38 E-value: 7.47e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366319 536 GEILGLLGHNGAGKSTSLKMISGDTKVTAGQVL-----LKGSREGDTPGFlgycpQENALWPNLTVKEHLEIfaavrGLR 610
Cdd:PRK11247 38 GQFVAVVGRSGCGKSTLLRLLAGLETPSAGELLagtapLAEAREDTRLMF-----QDARLLPWKKVIDNVGL-----GLK 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366319 611 KSHAAVAITRLAdALKLQDQLKSPVKTLSEGVKRKLCFVLSILGNPSILLLDEPSTGLDP----EGQQQI---WQairai 683
Cdd:PRK11247 108 GQWRDAALQALA-AVGLADRANEWPAALSGGQKQRVALARALIHRPGLLLLDEPLGALDAltriEMQDLIeslWQ----- 181
|
170 180 190
....*....|....*....|....*....|....*
gi 1720366319 684 ikntDRG--ALLTTHYMAEAEALCDRVAILVSGRL 716
Cdd:PRK11247 182 ----QHGftVLLVTHDVSEAVAMADRVLLIEEGKI 212
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
536-680 |
1.04e-08 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 58.64 E-value: 1.04e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366319 536 GEILGLLGHNGAGKSTSLKMISGDTKVTAGQV-LLKGSRegdtpgfLGYCPQenalwpnltvkEHLEIfaavrgLRKSHA 614
Cdd:PRK10636 338 GSRIGLLGRNGAGKSTLIKLLAGELAPVSGEIgLAKGIK-------LGYFAQ-----------HQLEF------LRADES 393
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366319 615 AVA-ITRLADALKLQ-------------DQLKSPVKTLSEGVKRKLCFVLSILGNPSILLLDEPSTGLDPEGQQQIWQAI 680
Cdd:PRK10636 394 PLQhLARLAPQELEQklrdylggfgfqgDKVTEETRRFSGGEKARLVLALIVWQRPNLLLLDEPTNHLDLDMRQALTEAL 473
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
533-711 |
1.39e-08 |
|
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI's are not transport proteins, and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLI's have an N-terminal Fe-S domain and two nucleotide-binding domains, which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213189 [Multi-domain] Cd Length: 177 Bit Score: 55.27 E-value: 1.39e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366319 533 VRKGEILGLLGHNGAGKSTSLKMISGDTKVTagqvllkgsregdtpgflgycpQENALWPNLTVkehleifaavrglrks 612
Cdd:cd03222 22 VKEGEVIGIVGPNGTGKTTAVKILAGQLIPN----------------------GDNDEWDGITP---------------- 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366319 613 haavaitrladalklqdQLKSPVKTLSEGVKRKLCFVLSILGNPSILLLDEPSTGLDPEGQQQIWQAIRAIIKNTDRGAL 692
Cdd:cd03222 64 -----------------VYKPQYIDLSGGELQRVAIAAALLRNATFYLFDEPSAYLDIEQRLNAARAIRRLSEEGKKTAL 126
|
170
....*....|....*....
gi 1720366319 693 LTTHYMAEAEALCDRVAIL 711
Cdd:cd03222 127 VVEHDLAVLDYLSDRIHVF 145
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
527-730 |
1.51e-08 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 58.58 E-value: 1.51e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366319 527 RNVSFCVRKGEILGLLGHNGAGKSTSLKMISGDTKVTAGQVLLKGSR---------------EGDTPGFLGYCPQENALW 591
Cdd:TIGR00958 498 KGLTFTLHPGEVVALVGPSGSGKSTVAALLQNLYQPTGGQVLLDGVPlvqydhhylhrqvalVGQEPVLFSGSVRENIAY 577
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366319 592 pNLTVKEHLEIFAAVrglRKSHAAVAITRLADALKLQDQLKSpvKTLSEGVKRKLCFVLSILGNPSILLLDEPSTGLDPE 671
Cdd:TIGR00958 578 -GLTDTPDEEIMAAA---KAANAHDFIMEFPNGYDTEVGEKG--SQLSGGQKQRIAIARALVRKPRVLILDEATSALDAE 651
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1720366319 672 GQQQIWQAiraiIKNTDRGALLTTHYMAEAEAlCDRVAILVSGRLRCIGSIQHLKSKFG 730
Cdd:TIGR00958 652 CEQLLQES----RSRASRTVLLIAHRLSTVER-ADQILVLKKGSVVEMGTHKQLMEDQG 705
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
528-716 |
1.79e-08 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 55.87 E-value: 1.79e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366319 528 NVSFCVRKGEILGLLGHNGAGKSTSLKMISGDTKVTAGQVLLKGSREGDTPGFL-------GYCPQENALWPNLTVKEHL 600
Cdd:PRK09493 19 NIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGLKVNDPKVDErlirqeaGMVFQQFYLFPHLTALENV 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366319 601 eIFAA--VRGLRKSHAAVAITRLADALKLQDQLKSPVKTLSEGVKRKLCFVLSILGNPSILLLDEPSTGLDPEGQQQIWQ 678
Cdd:PRK09493 99 -MFGPlrVRGASKEEAEKQARELLAKVGLAERAHHYPSELSGGQQQRVAIARALAVKPKLMLFDEPTSALDPELRHEVLK 177
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1720366319 679 AIRAIiknTDRG--ALLTTHYMAEAEALCDRVAILVSGRL 716
Cdd:PRK09493 178 VMQDL---AEEGmtMVIVTHEIGFAEKVASRLIFIDKGRI 214
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
525-747 |
1.87e-08 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 57.71 E-value: 1.87e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366319 525 ATRNVSFCVRKGEILGLLGHNGAGKSTSLKMISGDTKVTAG-------QVLLKGSREGDTPGfLGYCPQENALWPNLTVK 597
Cdd:PRK10762 19 ALSGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGsilylgkEVTFNGPKSSQEAG-IGIIHQELNLIPQLTIA 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366319 598 EHL----EIFAAVRGL--RKSHAAVaiTRLADALKLQDQLKSPVKTLSEGVKR--KLCFVLSIlgNPSILLLDEPSTGLD 669
Cdd:PRK10762 98 ENIflgrEFVNRFGRIdwKKMYAEA--DKLLARLNLRFSSDKLVGELSIGEQQmvEIAKVLSF--ESKVIIMDEPTDALT 173
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1720366319 670 PEGQQQIWQAIRAiIKNTDRGALLTTHYMAEAEALCDRVAILVSGRLrcIGsiQHLKSKFGKDYLLEMKV-KTLEQVEP 747
Cdd:PRK10762 174 DTETESLFRVIRE-LKSQGRGIVYISHRLKEIFEICDDVTVFRDGQF--IA--EREVADLTEDSLIEMMVgRKLEDQYP 247
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
527-725 |
1.89e-08 |
|
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: 58.38 E-value: 1.89e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366319 527 RNVSFCVRKGEILGLLGHNGAGKST----SLKMISGDTK-----VTAGQVLLKGSREGdtpgfLGYCPQENALWPNlTVK 597
Cdd:TIGR01271 1236 QDLSFSVEGGQRVGLLGRTGSGKSTllsaLLRLLSTEGEiqidgVSWNSVTLQTWRKA-----FGVIPQKVFIFSG-TFR 1309
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366319 598 EHLEIFA--AVRGLRKSHAAVAITRLADAL--KLQDQLKSPVKTLSEGVKRKLCFVLSILGNPSILLLDEPSTGLDPegq 673
Cdd:TIGR01271 1310 KNLDPYEqwSDEEIWKVAEEVGLKSVIEQFpdKLDFVLVDGGYVLSNGHKQLMCLARSILSKAKILLLDEPSAHLDP--- 1386
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1720366319 674 qQIWQAIRAIIKNT--DRGALLTTHYMaEAEALCDRVAILVSGRLRCIGSIQHL 725
Cdd:TIGR01271 1387 -VTLQIIRKTLKQSfsNCTVILSEHRV-EALLECQQFLVIEGSSVKQYDSIQKL 1438
|
|
| PRK13541 |
PRK13541 |
cytochrome c biogenesis protein CcmA; Provisional |
543-696 |
2.09e-08 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184128 [Multi-domain] Cd Length: 195 Bit Score: 54.88 E-value: 2.09e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366319 543 GHNGAGKSTSLKMISGDTKVTAGQVLLKGSREGDTPG-FLGYCPQENALWPNLTVKEHLEIFAAVrglrkSHAAVAITRL 621
Cdd:PRK13541 33 GANGCGKSSLLRMIAGIMQPSSGNIYYKNCNINNIAKpYCTYIGHNLGLKLEMTVFENLKFWSEI-----YNSAETLYAA 107
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1720366319 622 ADALKLQDQLKSPVKTLSEGVKRKLCFVLSILGNPSILLLDEPSTGLDPEGQQQIWQAIrAIIKNTDRGALLTTH 696
Cdd:PRK13541 108 IHYFKLHDLLDEKCYSLSSGMQKIVAIARLIACQSDLWLLDEVETNLSKENRDLLNNLI-VMKANSGGIVLLSSH 181
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
528-671 |
2.68e-08 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 57.44 E-value: 2.68e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366319 528 NVSFCVRKGEILGLLGHNGAGKSTSLKMISGDTKVTAGQVLLkgsreGDTPGfLGYCPQE-NALWPNLTVKE-------H 599
Cdd:PRK11819 342 DLSFSLPPGGIVGIIGPNGAGKSTLFKMITGQEQPDSGTIKI-----GETVK-LAYVDQSrDALDPNKTVWEeisggldI 415
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1720366319 600 LEIfaavrGLRK--SHAAVAitrlADALKLQDQLKsPVKTLSEGVKRK--LCFVLSILGNpsILLLDEPSTGLDPE 671
Cdd:PRK11819 416 IKV-----GNREipSRAYVG----RFNFKGGDQQK-KVGVLSGGERNRlhLAKTLKQGGN--VLLLDEPTNDLDVE 479
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
528-717 |
3.11e-08 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 57.25 E-value: 3.11e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366319 528 NVSFCVRKGEILGLLGHNGAGKSTSLKMI--------SGDTKVTAGQVLLKGSREGDTPGfLGYCPQE---NALWPNLTV 596
Cdd:PRK13549 280 DVSFSLRRGEILGIAGLVGAGRTELVQCLfgaypgrwEGEIFIDGKPVKIRNPQQAIAQG-IAMVPEDrkrDGIVPVMGV 358
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366319 597 KEH-----LEIFAAVRGLRKSHAAVAITRLADALKLQ-DQLKSPVKTLSEGVKRKLCFVLSILGNPSILLLDEPSTGLDP 670
Cdd:PRK13549 359 GKNitlaaLDRFTGGSRIDDAAELKTILESIQRLKVKtASPELAIARLSGGNQQKAVLAKCLLLNPKILILDEPTRGIDV 438
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1720366319 671 EGQQQIWQAIRAIIKntdRGA--LLTTHYMAEAEALCDRVAILVSGRLR 717
Cdd:PRK13549 439 GAKYEIYKLINQLVQ---QGVaiIVISSELPEVLGLSDRVLVMHEGKLK 484
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
527-727 |
3.65e-08 |
|
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The CFTR subfamily domain 1. The cystic fibrosis transmembrane regulator (CFTR), the product of the gene mutated in patients with cystic fibrosis, has adapted the ABC transporter structural motif to form a tightly regulated anion channel at the apical surface of many epithelia. Use of the term assembly of a functional ion channel implies the coming together of subunits, or at least smaller not-yet functional components of the active whole. In fact, on the basis of current knowledge only the CFTR polypeptide itself is required to form an ATP- and protein kinase A-dependent low-conductance chloride channel of the type present in the apical membrane of many epithelial cells. CFTR displays the typical organization (IM-ABC)2 and carries a characteristic hydrophilic R-domain that separates IM1-ABC1 from IM2-ABC2.
Pssm-ID: 213258 [Multi-domain] Cd Length: 282 Bit Score: 55.63 E-value: 3.65e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366319 527 RNVSFCVRKGEILGLLGHNGAGKSTSLKMISGDTKVTAGQVllKGSregdtpGFLGYCPQENALWPNlTVKEHLeIFAAV 606
Cdd:cd03291 54 KNINLKIEKGEMLAITGSTGSGKTSLLMLILGELEPSEGKI--KHS------GRISFSSQFSWIMPG-TIKENI-IFGVS 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366319 607 RGLRKSHAAVAITRL-ADALKLQDQLKSPVK----TLSEGVKRKLCFVLSILGNPSILLLDEPSTGLDPEGQQQIWQA-I 680
Cdd:cd03291 124 YDEYRYKSVVKACQLeEDITKFPEKDNTVLGeggiTLSGGQRARISLARAVYKDADLYLLDSPFGYLDVFTEKEIFEScV 203
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1720366319 681 RAIIKNTDRgaLLTTHYMaEAEALCDRVAILVSGRLRCIGSIQHLKS 727
Cdd:cd03291 204 CKLMANKTR--ILVTSKM-EHLKKADKILILHEGSSYFYGTFSELQS 247
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
528-717 |
3.94e-08 |
|
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: 56.76 E-value: 3.94e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366319 528 NVSFCVRKGEILGLLGHNGAGKSTSLKMISGDTK-VTAGQVLLKGsREGDTPGFLGYCPQENALWP-------------- 592
Cdd:TIGR02633 278 DVSFSLRRGEILGVAGLVGAGRTELVQALFGAYPgKFEGNVFING-KPVDIRNPAQAIRAGIAMVPedrkrhgivpilgv 356
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366319 593 --NLTVKEhLEIFAAVRGLRKSHAAVAITRLADALKLQDQLKS-PVKTLSEGVKRKLCFVLSILGNPSILLLDEPSTGLD 669
Cdd:TIGR02633 357 gkNITLSV-LKSFCFKMRIDAAAELQIIGSAIQRLKVKTASPFlPIGRLSGGNQQKAVLAKMLLTNPRVLILDEPTRGVD 435
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1720366319 670 PEGQQQIWQAIRAIIKntdRGA--LLTTHYMAEAEALCDRVAILVSGRLR 717
Cdd:TIGR02633 436 VGAKYEIYKLINQLAQ---EGVaiIVVSSELAEVLGLSDRVLVIGEGKLK 482
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
523-733 |
5.79e-08 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 56.25 E-value: 5.79e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366319 523 KIATRNVSFCVRKGEILGLLGHNGAGKSTS----LKMISGDTKVT-AGQVLLKGSREGDTPgflgYCPQ--------ENA 589
Cdd:PRK15134 299 NVVVKNISFTLRPGETLGLVGESGSGKSTTglalLRLINSQGEIWfDGQPLHNLNRRQLLP----VRHRiqvvfqdpNSS 374
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366319 590 LWPNLTVkehLEIFAavRGLRKSHAAV-AITRLADALKLQDQLKSPVKT-------LSEGVKRKLCFVLSILGNPSILLL 661
Cdd:PRK15134 375 LNPRLNV---LQIIE--EGLRVHQPTLsAAQREQQVIAVMEEVGLDPETrhrypaeFSGGQRQRIAIARALILKPSLIIL 449
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1720366319 662 DEPSTGLDPEGQQQIWQAIRAIIKNTDRGALLTTHYMAEAEALCDRVAILVSGRLRCIGSIQHLKSKFGKDY 733
Cdd:PRK15134 450 DEPTSSLDKTVQAQILALLKSLQQKHQLAYLFISHDLHVVRALCHQVIVLRQGEVVEQGDCERVFAAPQQEY 521
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
533-711 |
5.85e-08 |
|
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: 54.68 E-value: 5.85e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366319 533 VRKGEILGLLGHNGAGKSTSLKMISGDTKVTAGQVLLKGSREGDTPGFLGYCPQ-------ENALWPNLTVKEHLEIFAA 605
Cdd:cd03236 23 PREGQVLGLVGPNGIGKSTALKILAGKLKPNLGKFDDPPDWDEILDEFRGSELQnyftkllEGDVKVIVKPQYVDLIPKA 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366319 606 VRG-----LRKSHAAVAITRLADALKLQDQLKSPVKTLSEGVKRKLCFVLSILGNPSILLLDEPSTGLDPEGQQQIWQAI 680
Cdd:cd03236 103 VKGkvgelLKKKDERGKLDELVDQLELRHVLDRNIDQLSGGELQRVAIAAALARDADFYFFDEPSSYLDIKQRLNAARLI 182
|
170 180 190
....*....|....*....|....*....|.
gi 1720366319 681 RAIIKNtDRGALLTTHYMAEAEALCDRVAIL 711
Cdd:cd03236 183 RELAED-DNYVLVVEHDLAVLDYLSDYIHCL 212
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
525-716 |
5.87e-08 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 55.17 E-value: 5.87e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366319 525 ATRNVSFCVRKGEILGLLGHNGAGKSTSLKMISGDTKVTAGQVLLKG----SREGD--------TPGFLGYCPqENALWP 592
Cdd:PRK13646 22 AIHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVDDititHKTKDkyirpvrkRIGMVFQFP-ESQLFE 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366319 593 NlTVKEhlEIFAAVRGLRKSHAAVAitrlADALKLQDQL--------KSPVKtLSEGVKRKLCFVlSILG-NPSILLLDE 663
Cdd:PRK13646 101 D-TVER--EIIFGPKNFKMNLDEVK----NYAHRLLMDLgfsrdvmsQSPFQ-MSGGQMRKIAIV-SILAmNPDIIVLDE 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1720366319 664 PSTGLDPEGQQQIWQAIRAIIKNTDRGALLTTHYMAEAEALCDRVAILVSGRL 716
Cdd:PRK13646 172 PTAGLDPQSKRQVMRLLKSLQTDENKTIILVSHDMNEVARYADEVIVMKEGSI 224
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
527-598 |
6.64e-08 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 54.32 E-value: 6.64e-08
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1720366319 527 RNVSFCVRKGEILGLLGHNGAGKSTSLKMISGDTKVTAGQVLLKGSREGDTPG-----FLGYCPQENALWPNLTVKE 598
Cdd:COG4604 18 DDVSLTIPKGGITALIGPNGAGKSTLLSMISRLLPPDSGEVLVDGLDVATTPSrelakRLAILRQENHINSRLTVRE 94
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
525-716 |
1.01e-07 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 54.86 E-value: 1.01e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366319 525 ATRNVSFCVRKGEILGLLGHNGAGKSTSLKMISGDTKVTAGQVLLKGSREGDTPGFLGYCPQENA--------------- 589
Cdd:PRK13631 41 ALNNISYTFEKNKIYFIIGNSGSGKSTLVTHFNGLIKSKYGTIQVGDIYIGDKKNNHELITNPYSkkiknfkelrrrvsm 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366319 590 --LWPNLTV-KEHLE---IFAAVR-GLRKSHAAVAITRLADALKLQDQL--KSPVKtLSEGVKRKLCF--VLSIlgNPSI 658
Cdd:PRK13631 121 vfQFPEYQLfKDTIEkdiMFGPVAlGVKKSEAKKLAKFYLNKMGLDDSYleRSPFG-LSGGQKRRVAIagILAI--QPEI 197
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1720366319 659 LLLDEPSTGLDPEGQQQIWQAIRAiIKNTDRGALLTTHYMAEAEALCDRVAILVSGRL 716
Cdd:PRK13631 198 LIFDEPTAGLDPKGEHEMMQLILD-AKANNKTVFVITHTMEHVLEVADEVIVMDKGKI 254
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
529-730 |
1.68e-07 |
|
multi drug resistance-associated protein (MRP); This model describes multi drug resistance-associated protein (MRP) in eukaryotes. The multidrug resistance-associated protein is an integral membrane protein that causes multidrug resistance when overexpressed in mammalian cells. It belongs to ABC transporter superfamily. The protein topology and function was experimentally demonstrated by epitope tagging and immunofluorescence. Insertion of tags in the critical regions associated with drug efflux, abrogated its function. The C-terminal domain seem to highly conserved. [Transport and binding proteins, Other]
Pssm-ID: 188098 [Multi-domain] Cd Length: 1522 Bit Score: 55.34 E-value: 1.68e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366319 529 VSFCVRKGEILGLLGHNGAGKSTSLKMISGDTKVTAGQVLLKGSregdtpgfLGYCPQEnALWPNLTVKEHLEIFAAVRG 608
Cdd:TIGR00957 657 ITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVHMKGS--------VAYVPQQ-AWIQNDSLRENILFGKALNE 727
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366319 609 LRKSHAAVAITRLAD--ALKLQDQLKSPVK--TLSEGVKRKLCFVLSILGNPSILLLDEPSTGLDPEGQQQIWQAI---R 681
Cdd:TIGR00957 728 KYYQQVLEACALLPDleILPSGDRTEIGEKgvNLSGGQKQRVSLARAVYSNADIYLFDDPLSAVDAHVGKHIFEHVigpE 807
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1720366319 682 AIIKNTDRgaLLTTHYMAEAEALcDRVAILVSGRLRCIGSIQHLKSKFG 730
Cdd:TIGR00957 808 GVLKNKTR--ILVTHGISYLPQV-DVIIVMSGGKISEMGSYQELLQRDG 853
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
495-571 |
1.86e-07 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 53.97 E-value: 1.86e-07
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1720366319 495 DEKPVIIASCLRKEYAGKQKhCLSKKKAKI-ATRNVSFCVRKGEILGLLGHNGAGKSTSLKMISGDTKVTAGQVLLKG 571
Cdd:COG4608 3 MAEPLLEVRDLKKHFPVRGG-LFGRTVGVVkAVDGVSFDIRRGETLGLVGESGCGKSTLGRLLLRLEEPTSGEILFDG 79
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
523-716 |
2.05e-07 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 53.12 E-value: 2.05e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366319 523 KIATRNVSFCVRKGEILGLLGHNGAGKSTSLK-------MISGdTKVTaGQVLLKG----SREGDTPGF---LGYCPQ-- 586
Cdd:COG1117 24 KQALKDINLDIPENKVTALIGPSGCGKSTLLRclnrmndLIPG-ARVE-GEILLDGediyDPDVDVVELrrrVGMVFQkp 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366319 587 --------ENALWP----NLTVKEHLEifAAV-RGLRKshAAvaitrLADALKlqDQLKSPVKTLSEGVKRKLCFVLSIL 653
Cdd:COG1117 102 npfpksiyDNVAYGlrlhGIKSKSELD--EIVeESLRK--AA-----LWDEVK--DRLKKSALGLSGGQQQRLCIARALA 170
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1720366319 654 GNPSILLLDEPSTGLDPEGQQQIWQAIR------AIIkntdrgalLTTHYMAEAEALCDRVAILVSGRL 716
Cdd:COG1117 171 VEPEVLLMDEPTSALDPISTAKIEELILelkkdyTIV--------IVTHNMQQAARVSDYTAFFYLGEL 231
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
529-717 |
2.16e-07 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 53.12 E-value: 2.16e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366319 529 VSFCVRKGEILGLLGHNGAGKSTSLKMISGDTKVTaGQVLLKGSREgdtpgFLGYC-------------------PQENa 589
Cdd:PRK14258 26 VSMEIYQSKVTAIIGPSGCGKSTFLKCLNRMNELE-SEVRVEGRVE-----FFNQNiyerrvnlnrlrrqvsmvhPKPN- 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366319 590 LWPnLTVKEHLEIFAAVRGLRKSHAAVAITRLA-DALKLQDQLKSPVKT----LSEGVKRKLCFVLSILGNPSILLLDEP 664
Cdd:PRK14258 99 LFP-MSVYDNVAYGVKIVGWRPKLEIDDIVESAlKDADLWDEIKHKIHKsaldLSGGQQQRLCIARALAVKPKVLLMDEP 177
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1720366319 665 STGLDPEGQQQIWQAIRAIIKNTDRGALLTTHYMAEAEALCDRVAILVSGRLR 717
Cdd:PRK14258 178 CFGLDPIASMKVESLIQSLRLRSELTMVIVSHNLHQVSRLSDFTAFFKGNENR 230
|
|
| ABC2_membrane_3 |
pfam12698 |
ABC-2 family transporter protein; This family is related to the ABC-2 membrane transporter ... |
246-437 |
2.47e-07 |
|
ABC-2 family transporter protein; This family is related to the ABC-2 membrane transporter family pfam01061.
Pssm-ID: 463674 [Multi-domain] Cd Length: 345 Bit Score: 53.55 E-value: 2.47e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366319 246 AFWLILTSAcppYIAMSSVTDYKNRAWFQLRVSGLFPSAYWVGQAMVDIPLYCFVFLFMSLM--DYLFRFPDTMFSIISH 323
Cdd:pfam12698 169 MIIILIGAA---IIAVSIVEEKESRIKERLLVSGVSPLQYWLGKILGDFLVGLLQLLIILLLlfGIGIPFGNLGLLLLLF 245
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366319 324 VIqipcsvgYAISLIFLTYVISFISRKGKKNSGIWSLSFYIITVFSVAVILLAFDVDGTQyyIIFLIPPSTLVGCLILSL 403
Cdd:pfam12698 246 LL-------YGLAYIALGYLLGSLFKNSEDAQSIIGIVILLLSGFFGGLFPLEDPPSFLQ--WIFSIIPFFSPIDGLLRL 316
|
170 180 190
....*....|....*....|....*....|....
gi 1720366319 404 HLFIGQIfeegQVIEPFLVFLIPFLhVFIFIFTL 437
Cdd:pfam12698 317 IYGDSLW----EIAPSLIILLLFAV-VLLLLALL 345
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
528-716 |
4.09e-07 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 52.44 E-value: 4.09e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366319 528 NVSFCVRKGEILGLLGHNGAGKSTSLKMISGDTKVTAGQVLLKG------SREGD------TPGFLGYCPqENALWPNlT 595
Cdd:PRK13649 25 DVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDDtlitstSKNKDikqirkKVGLVFQFP-ESQLFEE-T 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366319 596 VKEHLEIFAAVRGLRKSHA-AVAITRLAdALKLQDQL--KSPVKtLSEGVKRKLCfVLSILG-NPSILLLDEPSTGLDPE 671
Cdd:PRK13649 103 VLKDVAFGPQNFGVSQEEAeALAREKLA-LVGISESLfeKNPFE-LSGGQMRRVA-IAGILAmEPKILVLDEPTAGLDPK 179
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1720366319 672 GQQQIWQairaIIKNTDRGAL---LTTHYMAEAEALCDRVAILVSGRL 716
Cdd:PRK13649 180 GRKELMT----LFKKLHQSGMtivLVTHLMDDVANYADFVYVLEKGKL 223
|
|
| PRK15093 |
PRK15093 |
peptide ABC transporter ATP-binding protein SapD; |
525-715 |
5.11e-07 |
|
peptide ABC transporter ATP-binding protein SapD;
Pssm-ID: 185049 [Multi-domain] Cd Length: 330 Bit Score: 52.50 E-value: 5.11e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366319 525 ATRNVSFCVRKGEILGLLGHNGAGKSTSLKMISGDTK----VTAGQV------LLKGS-RE-----GDTPGFLGYCPQeN 588
Cdd:PRK15093 22 AVDRVSMTLTEGEIRGLVGESGSGKSLIAKAICGVTKdnwrVTADRMrfddidLLRLSpRErrklvGHNVSMIFQEPQ-S 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366319 589 ALWPNLTVKEHLeiFAAVRG------------LRKSHAAVAITRLAdaLK-LQDQLKSPVKTLSEGVKRKLCFVLSILGN 655
Cdd:PRK15093 101 CLDPSERVGRQL--MQNIPGwtykgrwwqrfgWRKRRAIELLHRVG--IKdHKDAMRSFPYELTEGECQKVMIAIALANQ 176
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366319 656 PSILLLDEPSTGLDPEGQQQIWQAIRAIIKNTDRGALLTTHYMAEAEALCDRVAILVSGR 715
Cdd:PRK15093 177 PRLLIADEPTNAMEPTTQAQIFRLLTRLNQNNNTTILLISHDLQMLSQWADKINVLYCGQ 236
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
527-728 |
5.71e-07 |
|
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: 53.38 E-value: 5.71e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366319 527 RNVSFCVRKGEILGLLGHNGAGKSTSLKMISGDTKVTAGQVllKGSregdtpGFLGYCPQENALWPNlTVKEHLEIFAAV 606
Cdd:TIGR01271 443 KNISFKLEKGQLLAVAGSTGSGKSSLLMMIMGELEPSEGKI--KHS------GRISFSPQTSWIMPG-TIKDNIIFGLSY 513
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366319 607 RGLRKSHAAVAITRLADALKLQDQLKSPVK----TLSEGVKRKLCFVLSILGNPSILLLDEPSTGLDPEGQQQIWQA-IR 681
Cdd:TIGR01271 514 DEYRYTSVIKACQLEEDIALFPEKDKTVLGeggiTLSGGQRARISLARAVYKDADLYLLDSPFTHLDVVTEKEIFEScLC 593
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1720366319 682 AIIKNTDRgaLLTTHYMaEAEALCDRVAILVSGRLRCIGSIQHLKSK 728
Cdd:TIGR01271 594 KLMSNKTR--ILVTSKL-EHLKKADKILLLHEGVCYFYGTFSELQAK 637
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
528-701 |
5.88e-07 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 53.09 E-value: 5.88e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366319 528 NVSFCVRKGEILGLLGHNGAGKSTSLKMISGD-TKVTAGQVLLKGSREG------DTPGFLGYCpqENALwpnltvkeHL 600
Cdd:PRK10938 278 NLSWQVNPGEHWQIVGPNGAGKSTLLSLITGDhPQGYSNDLTLFGRRRGsgetiwDIKKHIGYV--SSSL--------HL 347
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366319 601 E--IFAAVRGLRKS--------HAAV--AITRLA----DALKLQDQL-KSPVKTLSEGVKRKLCFVLSILGNPSILLLDE 663
Cdd:PRK10938 348 DyrVSTSVRNVILSgffdsigiYQAVsdRQQKLAqqwlDILGIDKRTaDAPFHSLSWGQQRLALIVRALVKHPTLLILDE 427
|
170 180 190
....*....|....*....|....*....|....*...
gi 1720366319 664 PSTGLDPEGQQQIWQAIRAIIKNTDRGALLTTHYMAEA 701
Cdd:PRK10938 428 PLQGLDPLNRQLVRRFVDVLISEGETQLLFVSHHAEDA 465
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
523-673 |
7.75e-07 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 51.53 E-value: 7.75e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366319 523 KIATRNVSFCVRKGEILGLLGHNGAGKSTSLKMISGDTKVTAGQVLLKG-------SRE-GDTPGFLGycpqENALWP-N 593
Cdd:PRK10253 20 YTVAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGehiqhyaSKEvARRIGLLA----QNATTPgD 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366319 594 LTVKE--------HLEIFAAvrgLRKSHAAvAITRLADALKLQDQLKSPVKTLSEGVKRKLCFVLSILGNPSILLLDEPS 665
Cdd:PRK10253 96 ITVQElvargrypHQPLFTR---WRKEDEE-AVTKAMQATGITHLADQSVDTLSGGQRQRAWIAMVLAQETAIMLLDEPT 171
|
....*...
gi 1720366319 666 TGLDPEGQ 673
Cdd:PRK10253 172 TWLDISHQ 179
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
523-721 |
9.16e-07 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 52.86 E-value: 9.16e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366319 523 KIATRNVSFCVRKGEILGLLGHNGAGKSTSLKMISGDTKVTAGQVLLKGSregdtpgfLGYCPQEnALWPNLTVKEHLEI 602
Cdd:PTZ00243 673 KVLLRDVSVSVPRGKLTVVLGATGSGKSTLLQSLLSQFEISEGRVWAERS--------IAYVPQQ-AWIMNATVRGNILF 743
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366319 603 FAAVRGLRkSHAAVAITRL-ADALKLQDQLKSPVK----TLSEGVKRKLCFVLSILGNPSILLLDEPSTGLDPE-GQQQI 676
Cdd:PTZ00243 744 FDEEDAAR-LADAVRVSQLeADLAQLGGGLETEIGekgvNLSGGQKARVSLARAVYANRDVYLLDDPLSALDAHvGERVV 822
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1720366319 677 WQAIRAIIKNTDRgaLLTTHYMaEAEALCDRVAILVSGRLRCIGS 721
Cdd:PTZ00243 823 EECFLGALAGKTR--VLATHQV-HVVPRADYVVALGDGRVEFSGS 864
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
525-716 |
1.39e-06 |
|
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: 51.99 E-value: 1.39e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366319 525 ATRNVSFCVRKGEILGLLGHNGAGKS-TSL---KMISGDTKVTAGQVLLKGS-------------REGDtpgfLGYCPQE 587
Cdd:COG4172 25 AVKGVSFDIAAGETLALVGESGSGKSvTALsilRLLPDPAAHPSGSILFDGQdllglserelrriRGNR----IAMIFQE 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366319 588 --NALWPNLTVKEHL-EIFAAVRGLRKSHAAVAITRLADALKLQD---QLKSPVKTLSEGVKRKLCFVLSILGNPSILLL 661
Cdd:COG4172 101 pmTSLNPLHTIGKQIaEVLRLHRGLSGAAARARALELLERVGIPDperRLDAYPHQLSGGQRQRVMIAMALANEPDLLIA 180
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1720366319 662 DEPSTGLDPEGQQQIWQAIRAIIKNTDRGALLTTHYMAEAEALCDRVAILVSGRL 716
Cdd:COG4172 181 DEPTTALDVTVQAQILDLLKDLQRELGMALLLITHDLGVVRRFADRVAVMRQGEI 235
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
525-715 |
2.18e-06 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 50.94 E-value: 2.18e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366319 525 ATRNVSFCVRKGEILGLLGHNGAGKSTSLKMISGdtkvtagqVLLKGSREGD------TPGF--------LGYC--PQEN 588
Cdd:NF040905 16 ALDDVNLSVREGEIHALCGENGAGKSTLMKVLSG--------VYPHGSYEGEilfdgeVCRFkdirdseaLGIViiHQEL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366319 589 ALWPNLTVKEHleIF----AAVRGLRKSHAavAITRLADALK---LQDQLKSPVKTLseGV-KRKLCFVLSILG-NPSIL 659
Cdd:NF040905 88 ALIPYLSIAEN--IFlgneRAKRGVIDWNE--TNRRARELLAkvgLDESPDTLVTDI--GVgKQQLVEIAKALSkDVKLL 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1720366319 660 LLDEPSTGLDPEGQQQIWQAIRAiIKNTDRGALLTTHYMAEAEALCDRVAILVSGR 715
Cdd:NF040905 162 ILDEPTAALNEEDSAALLDLLLE-LKAQGITSIIISHKLNEIRRVADSITVLRDGR 216
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
523-671 |
2.51e-06 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 51.10 E-value: 2.51e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366319 523 KIATRNVSFCVRKGEILGLLGHNGAGKSTSLKMISGDTKVTAGQVllkgsREGdTPGFLGYCPQENA-LWPNLTVKEHL- 600
Cdd:PRK11147 332 KQLVKDFSAQVQRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRI-----HCG-TKLEVAYFDQHRAeLDPEKTVMDNLa 405
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366319 601 ----EIfaAVRGlRKSHAavaitrLAdalKLQDQL------KSPVKTLSEGVKRKLcFVLSILGNPSILL-LDEPSTGLD 669
Cdd:PRK11147 406 egkqEV--MVNG-RPRHV------LG---YLQDFLfhpkraMTPVKALSGGERNRL-LLARLFLKPSNLLiLDEPTNDLD 472
|
..
gi 1720366319 670 PE 671
Cdd:PRK11147 473 VE 474
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
525-716 |
2.72e-06 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 50.13 E-value: 2.72e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366319 525 ATRNVSFCVRKGEILGLLGHNGAGKSTSLKMISG----DTKVTAGQVLLKGS-----REGDTPGFLG------YCPQENA 589
Cdd:PRK11022 22 AVDRISYSVKQGEVVGIVGESGSGKSVSSLAIMGlidyPGRVMAEKLEFNGQdlqriSEKERRNLVGaevamiFQDPMTS 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366319 590 LWPNLTVKehLEIFAAVR----GLRKSHAAVAItrlaDALKL------QDQLKSPVKTLSEGVKRKLCFVLSILGNPSIL 659
Cdd:PRK11022 102 LNPCYTVG--FQIMEAIKvhqgGNKKTRRQRAI----DLLNQvgipdpASRLDVYPHQLSGGMSQRVMIAMAIACRPKLL 175
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1720366319 660 LLDEPSTGLDPEGQQQIWQAIRAIIKNTDRGALLTTHYMAEAEALCDRVAILVSGRL 716
Cdd:PRK11022 176 IADEPTTALDVTIQAQIIELLLELQQKENMALVLITHDLALVAEAAHKIIVMYAGQV 232
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
529-753 |
3.53e-06 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 51.13 E-value: 3.53e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366319 529 VSFCVRKGEILGLLGHNGAGKSTSLKMISGDTKVTAGQVLLKG---SREG--DTPGFLGYCPQENALWPNlTVKEHLEIF 603
Cdd:PLN03232 1255 LSFFVSPSEKVGVVGRTGAGKSSMLNALFRIVELEKGRIMIDDcdvAKFGltDLRRVLSIIPQSPVLFSG-TVRFNIDPF 1333
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366319 604 AA------VRGLRKSHAAVAITRlaDALKLQDQLKSPVKTLSEGVKRKLCFVLSILGNPSILLLDEPSTGLDPEGQQQIW 677
Cdd:PLN03232 1334 SEhndadlWEALERAHIKDVIDR--NPFGLDAEVSEGGENFSVGQRQLLSLARALLRRSKILVLDEATASVDVRTDSLIQ 1411
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1720366319 678 QAIRAIIKNTdrgALLTTHYMAEAEALCDRVAILVSGRLRCIGSIQHLKSKFGKDYLlemkvKTLEQVEPLNTEIL 753
Cdd:PLN03232 1412 RTIREEFKSC---TMLVIAHRLNTIIDCDKILVLSSGQVLEYDSPQELLSRDTSAFF-----RMVHSTGPANAQYL 1479
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
525-571 |
3.98e-06 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 49.40 E-value: 3.98e-06
10 20 30 40
....*....|....*....|....*....|....*....|....*..
gi 1720366319 525 ATRNVSFCVRKGEILGLLGHNGAGKSTSLKMISGDTKVTAGQVLLKG 571
Cdd:PRK15112 28 AVKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDD 74
|
|
| SapD |
COG4170 |
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms]; |
528-728 |
5.81e-06 |
|
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms];
Pssm-ID: 443330 [Multi-domain] Cd Length: 331 Bit Score: 49.13 E-value: 5.81e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366319 528 NVSFCVRKGEILGLLGHNGAGKSTSLKMISGDTK----VTA------GQVLLKGS---------REgdtpgfLGYCPQE- 587
Cdd:COG4170 25 RVSLTLNEGEIRGLVGESGSGKSLIAKAICGITKdnwhVTAdrfrwnGIDLLKLSprerrkiigRE------IAMIFQEp 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366319 588 -NALWPNLTVKEHLE----------IFAAVRGLRKSHAA-----VAITrladalKLQDQLKSPVKTLSEGVKRKLCFVLS 651
Cdd:COG4170 99 sSCLDPSAKIGDQLIeaipswtfkgKWWQRFKWRKKRAIellhrVGIK------DHKDIMNSYPHELTEGECQKVMIAMA 172
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1720366319 652 ILGNPSILLLDEPSTGLDPEGQQQIWQAIRAIIKNTDRGALLTTHYMAEAEALCDRVAILVSGRLRCIGSIQHLKSK 728
Cdd:COG4170 173 IANQPRLLIADEPTNAMESTTQAQIFRLLARLNQLQGTSILLISHDLESISQWADTITVLYCGQTVESGPTEQILKS 249
|
|
| AAA_21 |
pfam13304 |
AAA domain, putative AbiEii toxin, Type IV TA system; Several members are annotated as being ... |
638-696 |
6.40e-06 |
|
AAA domain, putative AbiEii toxin, Type IV TA system; Several members are annotated as being of the abortive phage resistance system, in which case the family would be acting as the toxin for a type IV toxin-antitoxin resistance system.
Pssm-ID: 433102 [Multi-domain] Cd Length: 303 Bit Score: 48.93 E-value: 6.40e-06
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1720366319 638 LSEGVKRKLCFVLSIL---GNPSILLLDEPSTGLDPEGQQQIWQAIRaIIKNTDRGALLTTH 696
Cdd:pfam13304 237 LSDGTKRLLALLAALLsalPKGGLLLIDEPESGLHPKLLRRLLELLK-ELSRNGAQLILTTH 297
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
534-686 |
1.04e-05 |
|
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440858 [Multi-domain] Cd Length: 592 Bit Score: 49.01 E-value: 1.04e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366319 534 RKGEILGLLGHNGAGKSTSLKMISG---------DTKVTAGQVL-----------LKGSREGDTPgfLGYCPQENALWPN 593
Cdd:COG1245 97 KKGKVTGILGPNGIGKSTALKILSGelkpnlgdyDEEPSWDEVLkrfrgtelqdyFKKLANGEIK--VAHKPQYVDLIPK 174
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366319 594 L---TVKEHLEIfAAVRGlrkshaavAITRLADALKLQDQLKSPVKTLSEGVKRKLCFVLSILGNPSILLLDEPSTGLDp 670
Cdd:COG1245 175 VfkgTVRELLEK-VDERG--------KLDELAEKLGLENILDRDISELSGGELQRVAIAAALLRDADFYFFDEPSSYLD- 244
|
170
....*....|....*...
gi 1720366319 671 egqqqIWQAIRA--IIKN 686
Cdd:COG1245 245 -----IYQRLNVarLIRE 257
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
523-716 |
2.64e-05 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 47.92 E-value: 2.64e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366319 523 KIATRNVSFCVRKGEILGLLGHNGAGKSTSLKMISGDTKVTaGQVLLKGS--REGDTP------GFLGYCPQ-------E 587
Cdd:PRK11174 363 KTLAGPLNFTLPAGQRIALVGPSGAGKTSLLNALLGFLPYQ-GSLKINGIelRELDPEswrkhlSWVGQNPQlphgtlrD 441
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366319 588 NAL--WPNLTVKEhleIFAAvrgLRKSHAAVAITRLADAL--KLQDQlkspVKTLSEGVKRKLCFVLSILGNPSILLLDE 663
Cdd:PRK11174 442 NVLlgNPDASDEQ---LQQA---LENAWVSEFLPLLPQGLdtPIGDQ----AAGLSVGQAQRLALARALLQPCQLLLLDE 511
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1720366319 664 PSTGLDPEGQQQIWQAIRAIIKntDRGALLTTHYMAEAEAlCDRVAILVSGRL 716
Cdd:PRK11174 512 PTASLDAHSEQLVMQALNAASR--RQTTLMVTHQLEDLAQ-WDQIWVMQDGQI 561
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
533-711 |
4.06e-05 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 47.11 E-value: 4.06e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366319 533 VRKGEILGLLGHNGAGKSTSLKMISGDTKVTAGQVLLKGSREGDTPGFLG------------------YCPQENALWPNL 594
Cdd:PRK13409 96 PKEGKVTGILGPNGIGKTTAVKILSGELIPNLGDYEEEPSWDEVLKRFRGtelqnyfkklyngeikvvHKPQYVDLIPKV 175
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366319 595 ---TVKEHLEIfAAVRGLRKShaavaitrLADALKLQDQLKSPVKTLSEGVKRKLCFVLSILGNPSILLLDEPSTGLDpe 671
Cdd:PRK13409 176 fkgKVRELLKK-VDERGKLDE--------VVERLGLENILDRDISELSGGELQRVAIAAALLRDADFYFFDEPTSYLD-- 244
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1720366319 672 gqqqIWQ------AIRAIIKNtdRGALLTTHYMAEAEALCDRVAIL 711
Cdd:PRK13409 245 ----IRQrlnvarLIRELAEG--KYVLVVEHDLAVLDYLADNVHIA 284
|
|
| sufC |
PRK09580 |
cysteine desulfurase ATPase component; Reviewed |
527-716 |
4.99e-05 |
|
cysteine desulfurase ATPase component; Reviewed
Pssm-ID: 181965 [Multi-domain] Cd Length: 248 Bit Score: 45.55 E-value: 4.99e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366319 527 RNVSFCVRKGEILGLLGHNGAGKSTSLKMISG--DTKVTAGQVLLKGSregdtpGFLGYCPQENA--------LWPNLT- 595
Cdd:PRK09580 18 RGLNLEVRPGEVHAIMGPNGSGKSTLSATLAGreDYEVTGGTVEFKGK------DLLELSPEDRAgegifmafQYPVEIp 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366319 596 -VKEHLEIFAAVRGLRKSHAAVAITRLADALKLQDQ---LKSPVKTLSEGV---------KRKLCFVLSILgNPSILLLD 662
Cdd:PRK09580 92 gVSNQFFLQTALNAVRSYRGQEPLDRFDFQDLMEEKialLKMPEDLLTRSVnvgfsggekKRNDILQMAVL-EPELCILD 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1720366319 663 EPSTGLDPEGQQQIWQAIRAiIKNTDRGALLTTHYMAEAEAL-CDRVAILVSGRL 716
Cdd:PRK09580 171 ESDSGLDIDALKIVADGVNS-LRDGKRSFIIVTHYQRILDYIkPDYVHVLYQGRI 224
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
524-709 |
6.90e-05 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 45.54 E-value: 6.90e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366319 524 IATRNVSFCVRKGEILGLLGHNGAGKSTSLK-------MISG---DTKVTAGQVLLKGSR--EGDTPGFLGYCPQENALW 591
Cdd:PRK14243 24 LAVKNVWLDIPKNQITAFIGPSGCGKSTILRcfnrlndLIPGfrvEGKVTFHGKNLYAPDvdPVEVRRRIGMVFQKPNPF 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366319 592 PNlTVKEHLEIFAAVRGLRKSHAAVAITRLADAL---KLQDQLKSPVKTLSEGVKRKLCFVLSILGNPSILLLDEPSTGL 668
Cdd:PRK14243 104 PK-SIYDNIAYGARINGYKGDMDELVERSLRQAAlwdEVKDKLKQSGLSLSGGQQQRLCIARAIAVQPEVILMDEPCSAL 182
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1720366319 669 DPEGQQQIWQAIRAIIKntDRGALLTTHYMAEAEALCDRVA 709
Cdd:PRK14243 183 DPISTLRIEELMHELKE--QYTIIIVTHNMQQAARVSDMTA 221
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
495-573 |
1.51e-04 |
|
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: 45.06 E-value: 1.51e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366319 495 DEKPVIIASCLRKEYAGKQKHCLSKKKAKIATRNVSFCVRKGEILGLLGHNGAGKSTS----LKMISgdtkvTAGQVLLK 570
Cdd:COG4172 271 DAPPLLEARDLKVWFPIKRGLFRRTVGHVKAVDGVSLTLRRGETLGLVGESGSGKSTLglalLRLIP-----SEGEIRFD 345
|
...
gi 1720366319 571 GSR 573
Cdd:COG4172 346 GQD 348
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
538-722 |
1.70e-04 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 44.87 E-value: 1.70e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366319 538 ILGLLGHNGAGKSTSLKMISGDTKVTAGQVLLKGSREGDTPG--FL-------GYCPQENALWPNLTVKEHLEIfaavrG 608
Cdd:PRK11144 26 ITAIFGRSGAGKTSLINAISGLTRPQKGRIVLNGRVLFDAEKgiCLppekrriGYVFQDARLFPHYKVRGNLRY-----G 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366319 609 LRKSHAAV--AITRLadaLKLQDQLKSPVKTLSEGVKRKLCFVLSILGNPSILLLDEPSTGLD-PEGQ------QQIWQA 679
Cdd:PRK11144 101 MAKSMVAQfdKIVAL---LGIEPLLDRYPGSLSGGEKQRVAIGRALLTAPELLLMDEPLASLDlPRKRellpylERLARE 177
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1720366319 680 IRAIIkntdrgaLLTTHYMAEAEALCDRVAILVSGRLRCIGSI 722
Cdd:PRK11144 178 INIPI-------LYVSHSLDEILRLADRVVVLEQGKVKAFGPL 213
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
525-715 |
1.89e-04 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 44.72 E-value: 1.89e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366319 525 ATRNVSFCVRKGEILGLLGHNGAGKSTSLKMISGDTKVTAGQVLLKG-------SREGDTPGfLGYCPQENALWPNLTVK 597
Cdd:PRK10982 13 ALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGkeidfksSKEALENG-ISMVHQELNLVLQRSVM 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366319 598 EHLEIFA-AVRGLRKSHAAV--AITRLADALKLQDQLKSPVKTLSEGVKRKLCFVLSILGNPSILLLDEPSTGLDPEGQQ 674
Cdd:PRK10982 92 DNMWLGRyPTKGMFVDQDKMyrDTKAIFDELDIDIDPRAKVATLSVSQMQMIEIAKAFSYNAKIVIMDEPTSSLTEKEVN 171
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1720366319 675 QIWQAIRAiIKNTDRGALLTTHYMAEAEALCDRVAILVSGR 715
Cdd:PRK10982 172 HLFTIIRK-LKERGCGIVYISHKMEEIFQLCDEITILRDGQ 211
|
|
| MelB |
COG2211 |
Na+/melibiose symporter or related transporter [Carbohydrate transport and metabolism]; |
268-390 |
2.20e-04 |
|
Na+/melibiose symporter or related transporter [Carbohydrate transport and metabolism];
Pssm-ID: 441813 [Multi-domain] Cd Length: 447 Bit Score: 44.51 E-value: 2.20e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366319 268 KNRAWFQLRVSGLFpsaYWVGQAMVDiplycfvFLFMSLMDYLFRFPDTMFSIIShviqipcsVGYAISLIFLTYVISFI 347
Cdd:COG2211 226 KNRPFLLLLLAYLL---FFLALALVA-------ALLLYYFKYVLGLSAALVGLLL--------ALYFLAALLGAPLWPRL 287
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 1720366319 348 SRK-GKKNSGIWSLSFYIItvfsvAVILLAFdVDGTQYYIIFLI 390
Cdd:COG2211 288 AKRfGKKKAFIIGLLLAAL-----GLLLLFF-LGPGNLWLLLVL 325
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
527-696 |
2.91e-04 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 44.33 E-value: 2.91e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366319 527 RNVSFCVRKGEILGLLGHNGAGKSTSLKMISGDTKVTAGQVLLKGSR----EGDTPGFL-----GYCPQENALWPNLTVK 597
Cdd:PRK10535 25 KGISLDIYAGEMVAIVGASGSGKSTLMNILGCLDKPTSGTYRVAGQDvatlDADALAQLrrehfGFIFQRYHLLSHLTAA 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366319 598 EHLEIFAAVRGL----RKSHAAVAITRLAdalkLQDQLKSPVKTLSEGVKRKLCFVLSILGNPSILLLDEPSTGLDPEGQ 673
Cdd:PRK10535 105 QNVEVPAVYAGLerkqRLLRAQELLQRLG----LEDRVEYQPSQLSGGQQQRVSIARALMNGGQVILADEPTGALDSHSG 180
|
170 180
....*....|....*....|....*.
gi 1720366319 674 QQiwqaIRAIIKN-TDRG--ALLTTH 696
Cdd:PRK10535 181 EE----VMAILHQlRDRGhtVIIVTH 202
|
|
| PvdE |
COG4615 |
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ... |
529-663 |
8.45e-04 |
|
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion transport and metabolism];
Pssm-ID: 443659 [Multi-domain] Cd Length: 547 Bit Score: 42.86 E-value: 8.45e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366319 529 VSFCVRKGEILGLLGHNGAGKSTSLKMISGDTKVTAGQVLLKGSREGDtpgflgycpqENALWpnltvkeHLEIFAAV-- 606
Cdd:COG4615 351 IDLTIRRGELVFIVGGNGSGKSTLAKLLTGLYRPESGEILLDGQPVTA----------DNREA-------YRQLFSAVfs 413
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1720366319 607 ------R--GLRKSHAAVAITRLADALKLQDQLK------SPVKtLSEGVKRKLCFVLSILGNPSILLLDE 663
Cdd:COG4615 414 dfhlfdRllGLDGEADPARARELLERLELDHKVSvedgrfSTTD-LSQGQRKRLALLVALLEDRPILVFDE 483
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
525-694 |
1.26e-03 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 42.39 E-value: 1.26e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366319 525 ATRNVSFCVRKGEILGLLGHNGAGKSTSLKMISGDTKVTAGQVLLKG------------SR---EGDTPGFLGYCPQEN- 588
Cdd:PRK10789 330 ALENVNFTLKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGDIRFHDipltklqldswrSRlavVSQTPFLFSDTVANNi 409
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366319 589 ALW-PNLTvKEHLEifaavrglrksHAAvaitRLA----DALKLQDQLKSPVK----TLSEGVKRKLCFVLSILGNPSIL 659
Cdd:PRK10789 410 ALGrPDAT-QQEIE-----------HVA----RLAsvhdDILRLPQGYDTEVGergvMLSGGQKQRISIARALLLNAEIL 473
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1720366319 660 LLDEPSTGLDPEGQQQI------WQAIRAIIKNTDRGALLT 694
Cdd:PRK10789 474 ILDDALSAVDGRTEHQIlhnlrqWGEGRTVIISAHRLSALT 514
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
636-699 |
1.35e-03 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 42.71 E-value: 1.35e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1720366319 636 KTLSEGVKRKLCFVLSILGNPSILLLDEPSTGLDPEGQQQIWQAIRAIIKNTDRGALLTTHYMA 699
Cdd:PTZ00265 1357 KSLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDIKDKADKTIITIAHRIA 1420
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
529-766 |
1.56e-03 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 42.42 E-value: 1.56e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366319 529 VSFCVRKGEILGLLGHNGAGKSTSLKMISGDTKVTAGQVLLKG---SREG--DTPGFLGYCPQENALWPNlTVKEHLEIF 603
Cdd:PLN03130 1258 LSFEISPSEKVGIVGRTGAGKSSMLNALFRIVELERGRILIDGcdiSKFGlmDLRKVLGIIPQAPVLFSG-TVRFNLDPF 1336
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366319 604 AA------VRGLRKSHAAVAITRlaDALKLQDQLKSPVKTLSEGVKRKLCFVLSILGNPSILLLDEPSTGLDpegqqqiw 677
Cdd:PLN03130 1337 NEhndadlWESLERAHLKDVIRR--NSLGLDAEVSEAGENFSVGQRQLLSLARALLRRSKILVLDEATAAVD-------- 1406
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366319 678 qaIR--AIIKNTDRGALLTTHYMAEAEAL-----CDRVAILVSGRLRCIGSIQHLKSKFGkdyllEMKVKTLEQVEPLNT 750
Cdd:PLN03130 1407 --VRtdALIQKTIREEFKSCTMLIIAHRLntiidCDRILVLDAGRVVEFDTPENLLSNEG-----SAFSKMVQSTGAANA 1479
|
250
....*....|....*.
gi 1720366319 751 EILRLFPQASRQERYS 766
Cdd:PLN03130 1480 QYLRSLVFGGDEDRLA 1495
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
528-569 |
1.99e-03 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 41.80 E-value: 1.99e-03
10 20 30 40
....*....|....*....|....*....|....*....|..
gi 1720366319 528 NVSFCVRKGEILGLLGHNGAGKSTSLKMISGDTKVTAGQVLL 569
Cdd:PRK15064 19 NISVKFGGGNRYGLIGANGCGKSTFMKILGGDLEPSAGNVSL 60
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
527-681 |
2.57e-03 |
|
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: 41.47 E-value: 2.57e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366319 527 RNVSFCVRKGEILGLLGHNGAGKSTSLKMISGDTKVTAGQVLLKGSREGDTpGF------LGYCPQENALWPNlTVKEHL 600
Cdd:TIGR00957 1303 RHINVTIHGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGLNIAKI-GLhdlrfkITIIPQDPVLFSG-SLRMNL 1380
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366319 601 EIFAAVR------GLRKSHAAVAITRLADalKLQDQLKSPVKTLSEGVKRKLCFVLSILGNPSILLLDEPSTGLDPEGQQ 674
Cdd:TIGR00957 1381 DPFSQYSdeevwwALELAHLKTFVSALPD--KLDHECAEGGENLSVGQRQLVCLARALLRKTKILVLDEATAAVDLETDN 1458
|
....*..
gi 1720366319 675 QIWQAIR 681
Cdd:TIGR00957 1459 LIQSTIR 1465
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
530-675 |
2.76e-03 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 41.15 E-value: 2.76e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366319 530 SFCVRKGEILGLLGHNGAGKSTSLKMISGDTkvtagqVLLKGSREGD--TPGFLGYCPQENAL---W-----------PN 593
Cdd:PRK10938 23 SLTLNAGDSWAFVGANGSGKSALARALAGEL------PLLSGERQSQfsHITRLSFEQLQKLVsdeWqrnntdmlspgED 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366319 594 LTVKEHLEIFaavrgLRKSHAAVAITRLADALKLQDQLKSPVKTLSEGVKRKLCFVLSILGNPSILLLDEPSTGLDPEGQ 673
Cdd:PRK10938 97 DTGRTTAEII-----QDEVKDPARCEQLAQQFGITALLDRRFKYLSTGETRKTLLCQALMSEPDLLILDEPFDGLDVASR 171
|
..
gi 1720366319 674 QQ 675
Cdd:PRK10938 172 QQ 173
|
|
| YbjD |
COG3593 |
Predicted ATP-dependent endonuclease of the OLD family, contains P-loop ATPase and TOPRIM ... |
625-696 |
4.20e-03 |
|
Predicted ATP-dependent endonuclease of the OLD family, contains P-loop ATPase and TOPRIM domains [Replication, recombination and repair];
Pssm-ID: 442812 [Multi-domain] Cd Length: 359 Bit Score: 40.37 E-value: 4.20e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1720366319 625 LKLQDQLKSPVKTLSEGVKRKLCFVLSIL-------GNPSILLLDEPSTGLDPEGQQQIWQAIRAIIKNTDRgALLTTH 696
Cdd:COG3593 150 LRIEDGKELPLDRLGSGFQRLILLALLSAlaelkraPANPILLIEEPEAHLHPQAQRRLLKLLKELSEKPNQ-VIITTH 227
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
518-571 |
4.70e-03 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 40.07 E-value: 4.70e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 1720366319 518 SKKKAKIATRNVSFCVRKGEILGLLGHNGAGKSTSLKMISGDTKVTAGQVLLKG 571
Cdd:PRK15079 29 QPPKTLKAVDGVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGEVAWLG 82
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
495-571 |
6.16e-03 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 39.56 E-value: 6.16e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1720366319 495 DEKPVIIASCLRKEYAGKQKhcLSKKKAKI-ATRNVSFCVRKGEILGLLGHNGAGKSTSLKMISGDTKVTAGQVLLKG 571
Cdd:PRK11308 1 SQQPLLQAIDLKKHYPVKRG--LFKPERLVkALDGVSFTLERGKTLAVVGESGCGKSTLARLLTMIETPTGGELYYQG 76
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
632-676 |
6.94e-03 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 39.30 E-value: 6.94e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 1720366319 632 KSPVKtLSEGVKRKLCFVlSILG-NPSILLLDEPSTGLDPEGQQQI 676
Cdd:PRK13651 161 RSPFE-LSGGQKRRVALA-GILAmEPDFLVFDEPTAGLDPQGVKEI 204
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
626-699 |
7.04e-03 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 40.01 E-value: 7.04e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1720366319 626 KLQDQLKSPVKTLSEGVKRKLCFVLSILGNPSILLLDEPSTGLDPEGQQQIWQAIRAIIKNTDRGALLTTHYMA 699
Cdd:PTZ00265 568 KYETLVGSNASKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQKTINNLKGNENRITIIIAHRLS 641
|
|
| COG1106 |
COG1106 |
ATPase/GTPase, AAA15 family [General function prediction only]; |
634-696 |
9.75e-03 |
|
ATPase/GTPase, AAA15 family [General function prediction only];
Pssm-ID: 440723 [Multi-domain] Cd Length: 330 Bit Score: 38.87 E-value: 9.75e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1720366319 634 PVKTLSEGVKRKLCFVLSI---LGNPSILLLDEPSTGLDPEGQQQIWQAIRAIIKNTDRGALLTTH 696
Cdd:COG1106 199 PLSEESDGTKRLLALAGALldaLAKGGVLLIDEIEASLHPSLLRKLLKLFLDLANKNNAQLIFTTH 264
|
|
| |
