|
Name |
Accession |
Description |
Interval |
E-value |
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
128-942 |
7.76e-157 |
|
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: 515.33 E-value: 7.76e-157
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779783 128 AAIVFDHKFKTSNErLPLQVKYSLRFGRiydpeNLFQPSKYQKEIEWNTstlfpsvpslGPRNFLENDGGnpgYIREGFL 207
Cdd:TIGR01257 549 AGVVFPDMYPWTSS-LPPHVKYKIRMDI-----DVVEKTNKIKDRYWDS----------GPRADPVEDFR---YIWGGFA 609
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779783 208 IVQHSVDKAIMmyhsgRAAEDIFANTTIYAERFPHPAFIHDSFLWTFIAMFPWTILFTFTQMALVIVGTIMLEKEKRLKL 287
Cdd:TIGR01257 610 YLQDMVEQGIT-----RSQMQAEPPVGIYLQQMPYPCFVDDSFMIILNRCFPIFMVLAWIYSVSMTVKSIVLEKELRLKE 684
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779783 288 TYmyayvprvclfpaKNRrgcwipgmevtdgcehpeyqlmvGLSNAMLWVSYFITFLLMYFIIICLLCgilfLKITHERV 367
Cdd:TIGR01257 685 TL-------------KNQ-----------------------GVSNAVIWCTWFLDSFSIMSMSIFLLT----IFIMHGRI 724
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779783 368 FQHSDPLFIAFYFMCFAVSSVLLGFLISTLFNKASLATSIAGFLHFLTFFPYLILYHKYDQISLSGKLALCLITNTALAF 447
Cdd:TIGR01257 725 LHYSDPFILFLFLLAFSTATIMQCFLLSTFFSKASLAAACSGVIYFTLYLPHILCFAWQDRMTADLKTAVSLLSPVAFGF 804
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779783 448 GTDLICKLEMKGHGAQWNNFATKVNADDDLTLAHIIGMFLFSAFLYGLVAWYLDAVFPGTYGVPKPWNFFLQKAYWFG-- 525
Cdd:TIGR01257 805 GTEYLVRFEEQGLGLQWSNIGNSPLEGDEFSFLLSMKMMLLDAALYGLLAWYLDQVFPGDYGTPLPWYFLLQESYWLGge 884
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779783 526 ------EPALSREESQVSDL--------LSSDFMEPEPVGLVAGIRIQHLYKefILKNSTLMAVNDLSLNLYEGQITVLL 591
Cdd:TIGR01257 885 gcstreERALEKTEPLTEEMedpehpegINDSFFERELPGLVPGVCVKNLVK--IFEPSGRPAVDRLNITFYENQITAFL 962
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779783 592 GHNGAGKTTTLSILTGLYLPTRGKVYISGYDISSDMVQIRKSLGLCPQDDLLFPMLTVSEHLHFYCVIKGIPLQNQSRET 671
Cdd:TIGR01257 963 GHNGAGKTTTLSILTGLLPPTSGTVLVGGKDIETNLDAVRQSLGMCPQHNILFHHLTVAEHILFYAQLKGRSWEEAQLEM 1042
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779783 672 NRMLTSFGLLQQSNTMSKDLSGGMKRKLSIIIALIGDTKVVILDEPTSGMDPVSRRATWDLLQHYKKDRTILLTTHHMDE 751
Cdd:TIGR01257 1043 EAMLEDTGLHHKRNEEAQDLSGGMQRKLSVAIAFVGDAKVVVLDEPTSGVDPYSRRSIWDLLLKYRSGRTIIMSTHHMDE 1122
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779783 752 ADVLGDRIAILVMGILKCCGSSLFLKKLYGVGYHLVIVK----------------------------------TP----D 793
Cdd:TIGR01257 1123 ADLLGDRIAIISQGRLYCSGTPLFLKNCFGTGFYLTLVRkmkniqsqrggcegtcsctskgfstrcparvdeiTPeqvlD 1202
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779783 794 SNDEKIFQLIKNYIPTAKMETNVAAELSFILP-KEHTHR-FAELFTDLEEKQEELGISGFGVSMTTMDEVFFKVsnledl 871
Cdd:TIGR01257 1203 GDVNELMDLVYHHVPEAKLVECIGQELIFLLPnKNFKQRaYASLFRELEETLADLGLSSFGISDTPLEEIFLKV------ 1276
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779783 872 klnTEIAPSASIVSQSSNEDNQNMNV------PR----------NFERPGYSRRHLD-----------SSFNAGWSLYIQ 924
Cdd:TIGR01257 1277 ---TEDADSGSLFAGGAQQKRENANLrhpcsgPTekagqtpqasHTCSPGQPAAHPEgqpppepedpgVPLNTGARLILQ 1353
|
890
....*....|....*...
gi 1039779783 925 QFRAMFIKRVMFSWRYWK 942
Cdd:TIGR01257 1354 HVQALLVKRFQHTIRSHK 1371
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
556-777 |
5.40e-108 |
|
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: 336.01 E-value: 5.40e-108
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779783 556 IRIQHLYKEFilKNSTLMAVNDLSLNLYEGQITVLLGHNGAGKTTTLSILTGLYLPTRGKVYISGYDISSDMVQIRKSLG 635
Cdd:cd03263 1 LQIRNLTKTY--KKGTKPAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYINGYSIRTDRKAARQSLG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779783 636 LCPQDDLLFPMLTVSEHLHFYCVIKGIPLQNQSRETNRMLTSFGLLQQSNTMSKDLSGGMKRKLSIIIALIGDTKVVILD 715
Cdd:cd03263 79 YCPQFDALFDELTVREHLRFYARLKGLPKSEIKEEVELLLRVLGLTDKANKRARTLSGGMKRKLSLAIALIGGPSVLLLD 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1039779783 716 EPTSGMDPVSRRATWDLLQHYKKDRTILLTTHHMDEADVLGDRIAILVMGILKCCGSSLFLK 777
Cdd:cd03263 159 EPTSGLDPASRRAIWDLILEVRKGRSIILTTHSMDEAEALCDRIAIMSDGKLRCIGSPQELK 220
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
556-772 |
1.68e-77 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 254.22 E-value: 1.68e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779783 556 IRIQHLYKEFilknSTLMAVNDLSLNLYEGQITVLLGHNGAGKTTTLSILTGLYLPTRGKVYISGYDISSDMVQIRKSLG 635
Cdd:COG1131 1 IEVRGLTKRY----GDKTALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRVLGEDVARDPAEVRRRIG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779783 636 LCPQDDLLFPMLTVSEHLHFYCVIKGIPLQNQSRETNRMLTSFGLLQQSNTMSKDLSGGMKRKLSIIIALIGDTKVVILD 715
Cdd:COG1131 77 YVPQEPALYPDLTVRENLRFFARLYGLPRKEARERIDELLELFGLTDAADRKVGTLSGGMKQRLGLALALLHDPELLILD 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1039779783 716 EPTSGMDPVSRRATWDLLQHYKKD-RTILLTTHHMDEADVLGDRIAILVMGILKCCGS 772
Cdd:COG1131 157 EPTSGLDPEARRELWELLRELAAEgKTVLLSTHYLEEAERLCDRVAIIDKGRIVADGT 214
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
556-762 |
1.29e-63 |
|
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: 213.03 E-value: 1.29e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779783 556 IRIQHLYKEFilknSTLMAVNDLSLNLYEGQITVLLGHNGAGKTTTLSILTGLYLPTRGKVYISGYDISSDMVQIRKSLG 635
Cdd:cd03230 1 IEVRNLSKRY----GKKTALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVLGKDIKKEPEEVKRRIG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779783 636 LCPQDDLLFPMLTVSEHLhfycvikgiplqnqsretnrmltsfgllqqsntmskDLSGGMKRKLSIIIALIGDTKVVILD 715
Cdd:cd03230 77 YLPEEPSLYENLTVRENL------------------------------------KLSGGMKQRLALAQALLHDPELLILD 120
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1039779783 716 EPTSGMDPVSRRATWDLLQHYKKD-RTILLTTHHMDEADVLGDRIAIL 762
Cdd:cd03230 121 EPTSGLDPESRREFWELLRELKKEgKTILLSSHILEEAERLCDRVAIL 168
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
556-762 |
1.31e-56 |
|
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: 195.85 E-value: 1.31e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779783 556 IRIQHLYKEFILKnstlMAVNDLSLNLYEGQITVLLGHNGAGKTTTLSILTGLYLPTRGKVYISGYDISSDMVQIRKSLG 635
Cdd:COG4555 2 IEVENLSKKYGKV----PALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIDGEDVRKEPREARRQIG 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779783 636 LCPQDDLLFPMLTVSEHLHFYCVIKGIPLQNQSRETNRMLTSFGLLQQSNTMSKDLSGGMKRKLSIIIALIGDTKVVILD 715
Cdd:COG4555 78 VLPDERGLYDRLTVRENIRYFAELYGLFDEELKKRIEELIELLGLEEFLDRRVGELSTGMKKKVALARALVHDPKVLLLD 157
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1039779783 716 EPTSGMDPVSRRATWDLLQHYKK-DRTILLTTHHMDEADVLGDRIAIL 762
Cdd:COG4555 158 EPTNGLDVMARRLLREILRALKKeGKTVLFSSHIMQEVEALCDRVVIL 205
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
556-777 |
1.70e-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: 189.12 E-value: 1.70e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779783 556 IRIQHLYKEFilknSTLMAVNDLSLNLYEGQITVLLGHNGAGKTTTLSILTGLYLPTRGKVYISGYDISSDMVQIRKSLG 635
Cdd:cd03265 1 IEVENLVKKY----GDFEAVRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATVAGHDVVREPREVRRRIG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779783 636 LCPQDDLLFPMLTVSEHLHFYCVIKGIPLQNQSRETNRMLTSFGLLQQSNTMSKDLSGGMKRKLSIIIALIGDTKVVILD 715
Cdd:cd03265 77 IVFQDLSVDDELTGWENLYIHARLYGVPGAERRERIDELLDFVGLLEAADRLVKTYSGGMRRRLEIARSLVHRPEVLFLD 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1039779783 716 EPTSGMDPVSRRATWDLLQHYKK--DRTILLTTHHMDEADVLGDRIAILVMGILKCCGSSLFLK 777
Cdd:cd03265 157 EPTIGLDPQTRAHVWEYIEKLKEefGMTILLTTHYMEEAEQLCDRVAIIDHGRIIAEGTPEELK 220
|
|
| drrA |
TIGR01188 |
daunorubicin resistance ABC transporter ATP-binding subunit; This model describes daunorubicin ... |
574-865 |
4.79e-53 |
|
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: 187.98 E-value: 4.79e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779783 574 AVNDLSLNLYEGQITVLLGHNGAGKTTTLSILTGLYLPTRGKVYISGYDISSDMVQIRKSLGLCPQDDLLFPMLTVSEHL 653
Cdd:TIGR01188 8 AVDGVNFKVREGEVFGFLGPNGAGKTTTIRMLTTLLRPTSGTARVAGYDVVREPRKVRRSIGIVPQYASVDEDLTGRENL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779783 654 HFYCVIKGIPLQNQSRETNRMLTSFGLLQQSNTMSKDLSGGMKRKLSIIIALIGDTKVVILDEPTSGMDPVSRRATWDLL 733
Cdd:TIGR01188 88 EMMGRLYGLPKDEAEERAEELLELFELGEAADRPVGTYSGGMRRRLDIAASLIHQPDVLFLDEPTTGLDPRTRRAIWDYI 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779783 734 QHYKK-DRTILLTTHHMDEADVLGDRIAILVMGILKCCGSSLFLKKLYGVGYHLVIVKTPDSNDEKIFQLIKNYIPTAKM 812
Cdd:TIGR01188 168 RALKEeGVTILLTTHYMEEADKLCDRIAIIDHGRIIAEGTPEELKRRLGKDTLESRPRDIQSLKVEVSMLIAELGETGLG 247
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 1039779783 813 ETNVAAELSFIlpKEHTHRFAELFTDLEEKQEELGISGFGVSMT--TMDEVFFKV 865
Cdd:TIGR01188 248 LLAVTVDSDRI--KILVPDGDETVPEIVEAAIRNGIRIRSISTErpSLDDVFLKL 300
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
573-771 |
1.18e-50 |
|
ABC-type multidrug transport system, ATPase component; The biological function of this family is not well characterized, but display ABC domains similar to members of ABCA subfamily. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213231 [Multi-domain] Cd Length: 211 Bit Score: 177.77 E-value: 1.18e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779783 573 MAVNDLSLNLYEGqITVLLGHNGAGKTTTLSILTGLYLPTRGKVYISGYDISSDMVQIRKSLGLCPQDDLLFPMLTVSEH 652
Cdd:cd03264 14 RALDGVSLTLGPG-MYGLLGPNGAGKTTLMRILATLTPPSSGTIRIDGQDVLKQPQKLRRRIGYLPQEFGVYPNFTVREF 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779783 653 LHFYCVIKGIPLQNQSRETNRMLTSFGLLQQSNTMSKDLSGGMKRKLSIIIALIGDTKVVILDEPTSGMDPVSRRATWDL 732
Cdd:cd03264 93 LDYIAWLKGIPSKEVKARVDEVLELVNLGDRAKKKIGSLSGGMRRRVGIAQALVGDPSILIVDEPTAGLDPEERIRFRNL 172
|
170 180 190
....*....|....*....|....*....|....*....
gi 1039779783 733 LQHYKKDRTILLTTHHMDEADVLGDRIAILVMGILKCCG 771
Cdd:cd03264 173 LSELGEDRIVILSTHIVEDVESLCNQVAVLNKGKLVFEG 211
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
384-888 |
1.21e-48 |
|
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: 190.22 E-value: 1.21e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779783 384 AVSSVLLGFLISTLFNKASLATSIAGFLHFLTFFPYLILYHKYDQISLSGKlalclITNTALAFGTdlicklEMKGHGAQ 463
Cdd:TIGR01257 1803 GINSSAITFVLELFENNRTLLRFNAMLRKLLIVFPHFCLGRGLIDLALSQA-----VTDVYAQFGE------EHSANPFQ 1871
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779783 464 WNnfatkvnadddltlahIIGMFLFSAFLYGLVAWYLDAVFPgtygvpkpWNFFLQKayWFGEPAlsreESQVSDllSSD 543
Cdd:TIGR01257 1872 WD----------------LIGKNLVAMAVEGVVYFLLTLLIQ--------HHFFLSR--WIAEPA----KEPIFD--EDD 1919
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779783 544 FMEPEPVGLVAG------IRIQHLYKefILKNSTLMAVNDLSLNLYEGQITVLLGHNGAGKTTTLSILTGLYLPTRGKVY 617
Cdd:TIGR01257 1920 DVAEERQRIISGgnktdiLRLNELTK--VYSGTSSPAVDRLCVGVRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDAT 1997
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779783 618 ISGYDISSDMVQIRKSLGLCPQDDLLFPMLTVSEHLHFYCVIKGIPLQNQSRETNRMLTSFGLLQQSNTMSKDLSGGMKR 697
Cdd:TIGR01257 1998 VAGKSILTNISDVHQNMGYCPQFDAIDDLLTGREHLYLYARLRGVPAEEIEKVANWSIQSLGLSLYADRLAGTYSGGNKR 2077
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779783 698 KLSIIIALIGDTKVVILDEPTSGMDPVSRRATWD-LLQHYKKDRTILLTTHHMDEADVLGDRIAILVMGILKCCGSSLFL 776
Cdd:TIGR01257 2078 KLSTAIALIGCPPLVLLDEPTTGMDPQARRMLWNtIVSIIREGRAVVLTSHSMEECEALCTRLAIMVKGAFQCLGTIQHL 2157
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779783 777 KKLYGVGYhLVIVKTPDSNDE------KIFQLIKNYIPTAKMETNVAAELSFILPkehTHRFAELFTDLEEKQEELGISG 850
Cdd:TIGR01257 2158 KSKFGDGY-IVTMKIKSPKDDllpdlnPVEQFFQGNFPGSVQRERHYNMLQFQVS---SSSLARIFQLLISHKDSLLIEE 2233
|
490 500 510
....*....|....*....|....*....|....*...
gi 1039779783 851 FGVSMTTMDEVFFKVSNLEDLKLNTEIAPSASIVSQSS 888
Cdd:TIGR01257 2234 YSVTQTTLDQVFVNFAKQQTETYDLPLHPRAAGASRQA 2271
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
556-765 |
6.34e-46 |
|
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: 164.46 E-value: 6.34e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779783 556 IRIQHLYKEFILKNSTLMAVNDLSLNLYEGQITVLLGHNGAGKTTTLSILTGLYLPTRGKVYISGYDISSDMVQIRKSLG 635
Cdd:cd03266 2 ITADALTKRFRDVKKTVQAVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDGFDVVKEPAEARRRLG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779783 636 LCPQDDLLFPMLTVSEHLHFYCVIKGIPLQNQSRETNRMLTSFGLLQQSNTMSKDLSGGMKRKLSIIIALIGDTKVVILD 715
Cdd:cd03266 82 FVSDSTGLYDRLTARENLEYFAGLYGLKGDELTARLEELADRLGMEELLDRRVGGFSTGMRQKVAIARALVHDPPVLLLD 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1039779783 716 EPTSGMDPVSRRATWDLLQHYKKD-RTILLTTHHMDEADVLGDRIAILVMG 765
Cdd:cd03266 162 EPTTGLDVMATRALREFIRQLRALgKCILFSTHIMQEVERLCDRVVVLHRG 212
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
574-762 |
1.62e-44 |
|
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: 160.33 E-value: 1.62e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779783 574 AVNDLSLNLYEGQITVLLGHNGAGKTTTLSILTGLYLPTRGKVYISGYDISSDMV-QIRKSLGLCPQD-DLLFPMLTVSE 651
Cdd:cd03225 16 ALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDLTKLSLkELRRKVGLVFQNpDDQFFGPTVEE 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779783 652 HLHFYCVIKGIPLQNQSRETNRMLTSFGLLQQSNTMSKDLSGGMKRKLSIIIALIGDTKVVILDEPTSGMDPVSRRATWD 731
Cdd:cd03225 96 EVAFGLENLGLPEEEIEERVEEALELVGLEGLRDRSPFTLSGGQKQRVAIAGVLAMDPDILLLDEPTAGLDPAGRRELLE 175
|
170 180 190
....*....|....*....|....*....|..
gi 1039779783 732 LLQHYKKD-RTILLTTHHMDEADVLGDRIAIL 762
Cdd:cd03225 176 LLKKLKAEgKTIIIVTHDLDLLLELADRVIVL 207
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
556-765 |
9.54e-44 |
|
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: 157.83 E-value: 9.54e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779783 556 IRIQHLYKEFilknSTLMAVNDLSLNLYEGQITVLLGHNGAGKTTTLSILTGLYLPTRGKVYISGYDISSDmvqIRKSLG 635
Cdd:cd03269 1 LEVENVTKRF----GRVTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDGKPLDIA---ARNRIG 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779783 636 LCPQDDLLFPMLTVSEHLHFYCVIKGIPLQNQSRETNRMLTSFGLLQQSNTMSKDLSGGMKRKLSIIIALIGDTKVVILD 715
Cdd:cd03269 74 YLPEERGLYPKMKVIDQLVYLAQLKGLKKEEARRRIDEWLERLELSEYANKRVEELSKGNQQKVQFIAAVIHDPELLILD 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1039779783 716 EPTSGMDPVSRRATWDLLQHYK-KDRTILLTTHHMDEADVLGDRIAILVMG 765
Cdd:cd03269 154 EPFSGLDPVNVELLKDVIRELArAGKTVILSTHQMELVEELCDRVLLLNKG 204
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
556-762 |
2.75e-43 |
|
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: 156.86 E-value: 2.75e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779783 556 IRIQHLYKEFILKNSTLMAVNDLSLNLYEGQITVLLGHNGAGKTTTLSILTGLYLPTRGKVYISGYDISsdmvQIRKSLG 635
Cdd:cd03293 1 LEVRNVSKTYGGGGGAVTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVDGEPVT----GPGPDRG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779783 636 LCPQDDLLFPMLTVSEHLHFYCVIKGIPLQNQSRETNRMLTSFGLLQQSNTMSKDLSGGMKRKLSIIIALIGDTKVVILD 715
Cdd:cd03293 77 YVFQQDALLPWLTVLDNVALGLELQGVPKAEARERAEELLELVGLSGFENAYPHQLSGGMRQRVALARALAVDPDVLLLD 156
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1039779783 716 EPTSGMDPVSRRATWD-LLQHYKKDR-TILLTTHHMDEADVLGDRIAIL 762
Cdd:cd03293 157 EPFSALDALTREQLQEeLLDIWRETGkTVLLVTHDIDEAVFLADRVVVL 205
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
556-865 |
1.81e-42 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 157.19 E-value: 1.81e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779783 556 IRIQHLYKEFilknSTLMAVNDLSLNLYEGQITVLLGHNGAGKTTTLSILTGLYLPTRGKVYISGYDISSDmvqIRKSLG 635
Cdd:COG4152 2 LELKGLTKRF----GDKTAVDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDSGEVLWDGEPLDPE---DRRRIG 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779783 636 LCPQDDLLFPMLTVSEHLHFYCVIKGIPLQNQSRETNRMLTSFGLLQQSNTMSKDLSGGMKRKLSIIIALIGDTKVVILD 715
Cdd:COG4152 75 YLPEERGLYPKMKVGEQLVYLARLKGLSKAEAKRRADEWLERLGLGDRANKKVEELSKGNQQKVQLIAALLHDPELLILD 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779783 716 EPTSGMDPVSRRATWDLLQHYK-KDRTILLTTHHMDEADVLGDRIAILVMGILKCCGSSLFLKKLYGVGYHLVIVKTPDS 794
Cdd:COG4152 155 EPFSGLDPVNVELLKDVIRELAaKGTTVIFSSHQMELVEELCDRIVIINKGRKVLSGSVDEIRRQFGRNTLRLEADGDAG 234
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1039779783 795 NDEKIFQLIKnyiptakmETNVAAELSFILPKEHTHRfaELFTDLEEKQEelgISGFGVSMTTMDEVFFKV 865
Cdd:COG4152 235 WLRALPGVTV--------VEEDGDGAELKLEDGADAQ--ELLRALLARGP---VREFEEVRPSLNEIFIEV 292
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
577-759 |
1.90e-42 |
|
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: 154.17 E-value: 1.90e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779783 577 DLSLNLYEGQITVLLGHNGAGKTTTLSILTGLYLPTRGKVYISGYDISSDMVQIRKSLGLCPQDDLLFPMLTVSEHLHFY 656
Cdd:COG4133 20 GLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWNGEPIRDAREDYRRRLAYLGHADGLKPELTVRENLRFW 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779783 657 CVIKGIPLQNQSREtnRMLTSFGLLQQSNTMSKDLSGGMKRKLSIIIALIGDTKVVILDEPTSGMDPVSRRATWDLLQHY 736
Cdd:COG4133 100 AALYGLRADREAID--EALEAVGLAGLADLPVRQLSAGQKRRVALARLLLSPAPLWLLDEPFTALDAAGVALLAELIAAH 177
|
170 180
....*....|....*....|....
gi 1039779783 737 KKD-RTILLTTHhmDEADVLGDRI 759
Cdd:COG4133 178 LARgGAVLLTTH--QPLELAAARV 199
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
556-762 |
2.57e-42 |
|
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: 154.41 E-value: 2.57e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779783 556 IRIQHLYkeFILKNSTlMAVNDLSLNLYEGQITVLLGHNGAGKTTTLSILTGLYLPTRGKVYISGYDIS-SDMVQIRKSL 634
Cdd:COG1122 1 IELENLS--FSYPGGT-PALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVDGKDITkKNLRELRRKV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779783 635 GLCPQ--DDLLFpMLTVSEHLHFYCVIKGIPLQNQSRETNRMLTSFGL--LQQSNTMskDLSGGMKRKLSIIIALIGDTK 710
Cdd:COG1122 78 GLVFQnpDDQLF-APTVEEDVAFGPENLGLPREEIRERVEEALELVGLehLADRPPH--ELSGGQKQRVAIAGVLAMEPE 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1039779783 711 VVILDEPTSGMDPVSRRATWDLLQHYKKD-RTILLTTHHMDEADVLGDRIAIL 762
Cdd:COG1122 155 VLVLDEPTAGLDPRGRRELLELLKRLNKEgKTVIIVTHDLDLVAELADRVIVL 207
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
575-719 |
1.40e-40 |
|
ABC transporter; ABC transporters for a large family of proteins responsible for translocation of a variety of compounds across biological membranes. ABC transporters are the largest family of proteins in many completely sequenced bacteria. ABC transporters are composed of two copies of this domain and two copies of a transmembrane domain pfam00664. These four domains may belong to a single polypeptide or belong in different polypeptide chains.
Pssm-ID: 394964 [Multi-domain] Cd Length: 150 Bit Score: 146.64 E-value: 1.40e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779783 575 VNDLSLNLYEGQITVLLGHNGAGKTTTLSILTGLYLPTRGKVYISGYDISSDMVQI-RKSLGLCPQDDLLFPMLTVSEHL 653
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDLTDDERKSlRKEIGYVFQDPQLFPRLTVRENL 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779783 654 HFYCVIKGIPLQNQSRETNRMLTSFGLLQQSNT----MSKDLSGGMKRKLSIIIALIGDTKVVILDEPTS 719
Cdd:pfam00005 81 RLGLLLKGLSKREKDARAEEALEKLGLGDLADRpvgeRPGTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
554-765 |
1.45e-39 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 147.54 E-value: 1.45e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779783 554 AGIRIQHLYKEFILKNSTLMAVNDLSLNLYEGQITVLLGHNGAGKTTTLSILTGLYLPTRGKVYISGYDISsdmvQIRKS 633
Cdd:COG1116 6 PALELRGVSKRFPTGGGGVTALDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPTSGEVLVDGKPVT----GPGPD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779783 634 LGLCPQDDLLFPMLTVSEHLHFYCVIKGIPLQNQSRETNRMLTSFGLLQQSNTMSKDLSGGMKRKLSIIIALIGDTKVVI 713
Cdd:COG1116 82 RGVVFQEPALLPWLTVLDNVALGLELRGVPKAERRERARELLELVGLAGFEDAYPHQLSGGMRQRVAIARALANDPEVLL 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1039779783 714 LDEPTSGMDPVSRRATWDLLQ--HYKKDRTILLTTHHMDEADVLGDRiaILVMG 765
Cdd:COG1116 162 MDEPFGALDALTRERLQDELLrlWQETGKTVLFVTHDVDEAVFLADR--VVVLS 213
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
556-762 |
4.84e-39 |
|
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: 144.58 E-value: 4.84e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779783 556 IRIQHLYKEFilkNSTLmAVNDLSLNLYEGQITVLLGHNGAGKTTTLSILTGLYLPTRGKVYISGYDISSDMVQiRKSLG 635
Cdd:cd03259 1 LELKGLSKTY---GSVR-ALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDGRDVTGVPPE-RRNIG 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779783 636 LCPQDDLLFPMLTVSEHLHFYCVIKGIPLQNQSRETNRMLTSFGLLQQSNTMSKDLSGGMKRKLSIIIALIGDTKVVILD 715
Cdd:cd03259 76 MVFQDYALFPHLTVAENIAFGLKLRGVPKAEIRARVRELLELVGLEGLLNRYPHELSGGQQQRVALARALAREPSLLLLD 155
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1039779783 716 EPTSGMDPVSRRATWDLLQHYKKDR--TILLTTHHMDEADVLGDRIAIL 762
Cdd:cd03259 156 EPLSALDAKLREELREELKELQRELgiTTIYVTHDQEEALALADRIAVM 204
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
550-765 |
7.77e-39 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 147.26 E-value: 7.77e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779783 550 VGLVAGIRIQHLYKEFILKnstlMAVNDLSLNLYEGQITVLLGHNGAGKTTTLSILTGLYLPTRGKVYISGYDISSDMVQ 629
Cdd:PRK13537 2 PMSVAPIDFRNVEKRYGDK----LVVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCGEPVPSRARH 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779783 630 IRKSLGLCPQDDLLFPMLTVSEHLHFYCVIKGIPLQnQSRETNRMLTSFGLLQQ-SNTMSKDLSGGMKRKLSIIIALIGD 708
Cdd:PRK13537 78 ARQRVGVVPQFDNLDPDFTVRENLLVFGRYFGLSAA-AARALVPPLLEFAKLENkADAKVGELSGGMKRRLTLARALVND 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1039779783 709 TKVVILDEPTSGMDPVSRRATWDLLQH-YKKDRTILLTTHHMDEADVLGDRIAILVMG 765
Cdd:PRK13537 157 PDVLVLDEPTTGLDPQARHLMWERLRSlLARGKTILLTTHFMEEAERLCDRLCVIEEG 214
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
556-771 |
8.92e-38 |
|
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This family comprises the glycine betaine/L-proline ATP binding subunit in bacteria and its equivalents in archaea. This transport system belong to the larger ATP-Binding Cassette (ABC) transporter superfamily. The characteristic feature of these transporters is the obligatory coupling of ATP hydrolysis to substrate translocation. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213261 [Multi-domain] Cd Length: 269 Bit Score: 142.78 E-value: 8.92e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779783 556 IRIQHLYKEF-------------------ILKNSTL-MAVNDLSLNLYEGQITVLLGHNGAGKTTTLSILTGLYLPTRGK 615
Cdd:cd03294 1 IKIKGLYKIFgknpqkafkllakgkskeeILKKTGQtVGVNDVSLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779783 616 VYISGYDISS----DMVQIR-KSLGLCPQDDLLFPMLTVSEHLHFYCVIKGIPLQNQSRETNRMLTSFGLLQQSNTMSKD 690
Cdd:cd03294 81 VLIDGQDIAAmsrkELRELRrKKISMVFQSFALLPHRTVLENVAFGLEVQGVPRAEREERAAEALELVGLEGWEHKYPDE 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779783 691 LSGGMKRKLSIIIALIGDTKVVILDEPTSGMDPVSRRATWD-LLQ-HYKKDRTILLTTHHMDEADVLGDRIAILVMGILK 768
Cdd:cd03294 161 LSGGMQQRVGLARALAVDPDILLMDEAFSALDPLIRREMQDeLLRlQAELQKTIVFITHDLDEALRLGDRIAIMKDGRLV 240
|
...
gi 1039779783 769 CCG 771
Cdd:cd03294 241 QVG 243
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
574-765 |
1.79e-37 |
|
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: 138.15 E-value: 1.79e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779783 574 AVNDLSLNLYEGQITVLLGHNGAGKTTTLSILTGLYLPTRGKVYISGYDISS-DMVQIRKSLGLCPQddllfpmltvseh 652
Cdd:cd00267 14 ALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGKDIAKlPLEELRRRIGYVPQ------------- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779783 653 lhfycvikgiplqnqsretnrmltsfgllqqsntmskdLSGGMKRKLSIIIALIGDTKVVILDEPTSGMDPVSRRATWDL 732
Cdd:cd00267 81 --------------------------------------LSGGQRQRVALARALLLNPDLLLLDEPTSGLDPASRERLLEL 122
|
170 180 190
....*....|....*....|....*....|....
gi 1039779783 733 L-QHYKKDRTILLTTHHMDEADVLGDRIAILVMG 765
Cdd:cd00267 123 LrELAEEGRTVIIVTHDPELAELAADRVIVLKDG 156
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
556-762 |
2.16e-37 |
|
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: 140.71 E-value: 2.16e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779783 556 IRIQHLYKEF----ILKnstlmavnDLSLNLYEGQITVLLGHNGAGKTTTLSILTGLYLPTRGKVYISGYDIS----SDM 627
Cdd:cd03261 1 IELRGLTKSFggrtVLK--------GVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGEDISglseAEL 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779783 628 VQIRKSLGLCPQDDLLFPMLTVSEHLHFycvikgiPLQNQSRETNRM--------LTSFGLLQQSNTMSKDLSGGMKRKL 699
Cdd:cd03261 73 YRLRRRMGMLFQSGALFDSLTVFENVAF-------PLREHTRLSEEEireivlekLEAVGLRGAEDLYPAELSGGMKKRV 145
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1039779783 700 SIIIALIGDTKVVILDEPTSGMDPVSRRATWDLLQHYKK--DRTILLTTHHMDEADVLGDRIAIL 762
Cdd:cd03261 146 ALARALALDPELLLYDEPTAGLDPIASGVIDDLIRSLKKelGLTSIMVTHDLDTAFAIADRIAVL 210
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
556-759 |
2.83e-37 |
|
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: 139.55 E-value: 2.83e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779783 556 IRIQHLYKEFILKNSTLMAVNDLSLNLYEGQITVLLGHNGAGKTTTLSILTGLYLPTRGKVYISGYDISS----DMVQIR 631
Cdd:cd03255 1 IELKNLSKTYGGGGEKVQALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRVDGTDISKlsekELAAFR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779783 632 -KSLGLCPQDDLLFPMLTVSEHLHFYCVIKGIPLQNQSRETNRMLTSFGLLQQSNTMSKDLSGGMKRKLSIIIALIGDTK 710
Cdd:cd03255 81 rRHIGFVFQSFNLLPDLTALENVELPLLLAGVPKKERRERAEELLERVGLGDRLNHYPSELSGGQQQRVAIARALANDPK 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1039779783 711 VVILDEPTSGMDPVSRRATWDLLQHYKKDR--TILLTTHHMDEADvLGDRI 759
Cdd:cd03255 161 IILADEPTGNLDSETGKEVMELLRELNKEAgtTIVVVTHDPELAE-YADRI 210
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
576-765 |
6.17e-37 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 138.41 E-value: 6.17e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779783 576 NDLSLNLYEGQITVLLGHNGAGKTTTLSILTGLYLPTRGKVYISGYDISS-DMVQIRKSLGLCPQDDLLFPMlTVSEHLH 654
Cdd:COG4619 17 SPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIYLDGKPLSAmPPPEWRRQVAYVPQEPALWGG-TVRDNLP 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779783 655 FYCVIKGIPLQNQsrETNRMLTSFGL----LQQSntmSKDLSGGMKRKLSIIIALIGDTKVVILDEPTSGMDPVSRRATW 730
Cdd:COG4619 96 FPFQLRERKFDRE--RALELLERLGLppdiLDKP---VERLSGGERQRLALIRALLLQPDVLLLDEPTSALDPENTRRVE 170
|
170 180 190
....*....|....*....|....*....|....*..
gi 1039779783 731 DLLQHY--KKDRTILLTTHHMDEADVLGDRIAILVMG 765
Cdd:COG4619 171 ELLREYlaEEGRAVLWVSHDPEQIERVADRVLTLEAG 207
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
556-765 |
2.21e-36 |
|
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter subfamily specific for the transport of dipeptides, oligopeptides (OppD), and nickel (NikDE). The NikABCDE system of E. coli belongs to this family and is composed of the periplasmic binding protein NikA, two integral membrane components (NikB and NikC), and two ATPase (NikD and NikE). The NikABCDE transporter is synthesized under anaerobic conditions to meet the increased demand for nickel resulting from hydrogenase synthesis. The molecular mechanism of nickel uptake in many bacteria and most archaea is not known. Many other members of this ABC family are also involved in the uptake of dipeptides and oligopeptides. The oligopeptide transport system (Opp) is a five-component ABC transport composed of a membrane-anchored substrate binding proteins (SRP), OppA, two transmembrane proteins, OppB and OppC, and two ATP-binding domains, OppD and OppF.
Pssm-ID: 213224 [Multi-domain] Cd Length: 228 Bit Score: 137.25 E-value: 2.21e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779783 556 IRIQHLYKEFILKNSTLMAVNDLSLNLYEGQITVLLGHNGAGKTTTLSILTGLYLPTRGKVYISGYDI---SSDMVQIR- 631
Cdd:cd03257 2 LEVKNLSVSFPTGGGSVKALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGKDLlklSRRLRKIRr 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779783 632 KSLGLCPQDDL--LFPMLTVSEHLHFYCVIKGIPLQNQSRETNRMLTSFGLLQQSNTMSK---DLSGGMKRKLSIIIALI 706
Cdd:cd03257 82 KEIQMVFQDPMssLNPRMTIGEQIAEPLRIHGKLSKKEARKEAVLLLLVGVGLPEEVLNRyphELSGGQRQRVAIARALA 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1039779783 707 GDTKVVILDEPTSGMDPVSRRATWDLLQHYKKDR--TILLTTHHMDEADVLGDRIAILVMG 765
Cdd:cd03257 162 LNPKLLIADEPTSALDVSVQAQILDLLKKLQEELglTLLFITHDLGVVAKIADRVAVMYAG 222
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
556-765 |
5.72e-36 |
|
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: 136.41 E-value: 5.72e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779783 556 IRIQHLYKEFilknSTLMAVNDLSLNLYEGQITVLLGHNGAGKTTTLSILTGLYLPTRGKVYISGYDISSDMVQIRKSLG 635
Cdd:cd03219 1 LEVRGLTKRF----GGLVALDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFDGEDITGLPPHEIARLG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779783 636 LC-----PQddlLFPMLTVSEHL---------HFYCVIKGIPLQNQSRE-TNRMLTSFGLLQQSNTMSKDLSGGMKRKLS 700
Cdd:cd03219 77 IGrtfqiPR---LFPELTVLENVmvaaqartgSGLLLARARREEREARErAEELLERVGLADLADRPAGELSYGQQRRLE 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1039779783 701 IIIALIGDTKVVILDEPTSGMDPVSRRATWDLLQHYK-KDRTILLTTHHMDEADVLGDRIAILVMG 765
Cdd:cd03219 154 IARALATDPKLLLLDEPAAGLNPEETEELAELIRELReRGITVLLVEHDMDVVMSLADRVTVLDQG 219
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
557-765 |
1.17e-35 |
|
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: 136.32 E-value: 1.17e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779783 557 RIQHLYKEFilknSTLMAVNDLSLNLYEGQITVLLGHNGAGKTTTLSILTGLYLPTRGKVYISGYDISSDMVQIRKSLGL 636
Cdd:COG0411 6 EVRGLTKRF----GGLVAVDDVSLEVERGEIVGLIGPNGAGKTTLFNLITGFYRPTSGRILFDGRDITGLPPHRIARLGI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779783 637 C-----PQddlLFPMLTVSEHL----------HFYCVIKGIPLQNQSRETNR-----MLTSFGLLQQSNTMSKDLSGGMK 696
Cdd:COG0411 82 ArtfqnPR---LFPELTVLENVlvaaharlgrGLLAALLRLPRARREEREAReraeeLLERVGLADRADEPAGNLSYGQQ 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1039779783 697 RKLSIIIALIGDTKVVILDEPTSGMDPVSRRATWDLLQHYKKDR--TILLTTHHMDEadVLG--DRIAILVMG 765
Cdd:COG0411 159 RRLEIARALATEPKLLLLDEPAAGLNPEETEELAELIRRLRDERgiTILLIEHDMDL--VMGlaDRIVVLDFG 229
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
556-762 |
1.62e-35 |
|
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: 135.49 E-value: 1.62e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779783 556 IRIQHLYKEF----ILKnstlmavnDLSLNLYEGQITVLLGHNGAGKTTTLSILTGLYLPTRGKVYISGYDIS----SDM 627
Cdd:COG1127 6 IEVRNLTKSFgdrvVLD--------GVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEILVDGQDITglseKEL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779783 628 VQIRKSLGLCPQDDLLFPMLTVSEHLHFycvikgiPLQNQSRETNRM--------LTSFGLLQQSNTMSKDLSGGMKRKL 699
Cdd:COG1127 78 YELRRRIGMLFQGGALFDSLTVFENVAF-------PLREHTDLSEAEirelvlekLELVGLPGAADKMPSELSGGMRKRV 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1039779783 700 SIIIALIGDTKVVILDEPTSGMDPVSRRATWDLLQHYKKDR--TILLTTHHMDEADVLGDRIAIL 762
Cdd:COG1127 151 ALARALALDPEILLYDEPTAGLDPITSAVIDELIRELRDELglTSVVVTHDLDSAFAIADRVAVL 215
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
556-762 |
1.68e-35 |
|
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding component of a bacterial solute transporter that serves a protective role to cells growing in a hyperosmolar environment. ABC (ATP-binding cassette) transporter nucleotide-binding domain; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition, to the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213262 [Multi-domain] Cd Length: 242 Bit Score: 135.51 E-value: 1.68e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779783 556 IRIQHLYKEFilkNSTLMAVNDLSLNLYEGQITVLLGHNGAGKTTTLSILTGLYLPTRGKVYISGYDISS-DMVQIRKSL 634
Cdd:cd03295 1 IEFENVTKRY---GGGKKAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGEDIREqDPVELRRKI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779783 635 GLCPQDDLLFPMLTVSEHLHFYCVIKGIPLQNQSRETNRMLTSFGLLQQS--NTMSKDLSGGMKRKLSIIIALIGDTKVV 712
Cdd:cd03295 78 GYVIQQIGLFPHMTVEENIALVPKLLKWPKEKIRERADELLALVGLDPAEfaDRYPHELSGGQQQRVGVARALAADPPLL 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1039779783 713 ILDEPTSGMDPVSRRATWDLLQHYKKD--RTILLTTHHMDEADVLGDRIAIL 762
Cdd:cd03295 158 LMDEPFGALDPITRDQLQEEFKRLQQElgKTIVFVTHDIDEAFRLADRIAIM 209
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
556-762 |
1.83e-35 |
|
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: 134.27 E-value: 1.83e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779783 556 IRIQHLYKEFILKNstlmAVNDLSLNLYEGQITVLLGHNGAGKTTTLSILTGLYLPTRGKVYISGYDIsSDMVQIRKSLG 635
Cdd:cd03268 1 LKTNDLTKTYGKKR----VLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEITFDGKSY-QKNIEALRRIG 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779783 636 LCPQDDLLFPMLTVSEHLHFYCVIKGIPlqnqSRETNRMLTSFGLLQQSNTMSKDLSGGMKRKLSIIIALIGDTKVVILD 715
Cdd:cd03268 76 ALIEAPGFYPNLTARENLRLLARLLGIR----KKRIDEVLDVVGLKDSAKKKVKGFSLGMKQRLGIALALLGNPDLLILD 151
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1039779783 716 EPTSGMDPVSRRATWDLLQHYKKD-RTILLTTHHMDEADVLGDRIAIL 762
Cdd:cd03268 152 EPTNGLDPDGIKELRELILSLRDQgITVLISSHLLSEIQKVADRIGII 199
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
575-765 |
3.74e-35 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 137.27 E-value: 3.74e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779783 575 VNDLSLNLYEGQITVLLGHNGAGKTTTLSILTGLYLPTRGKVYISGYDISSDMVQIRKSLGLCPQDDLLFPMLTVSEHLH 654
Cdd:PRK13536 57 VNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKITVLGVPVPARARLARARIGVVPQFDNLDLEFTVRENLL 136
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779783 655 FYcvikGIPLQNQSRETNRMLTS---FGLLQ-QSNTMSKDLSGGMKRKLSIIIALIGDTKVVILDEPTSGMDPVSRRATW 730
Cdd:PRK13536 137 VF----GRYFGMSTREIEAVIPSlleFARLEsKADARVSDLSGGMKRRLTLARALINDPQLLILDEPTTGLDPHARHLIW 212
|
170 180 190
....*....|....*....|....*....|....*.
gi 1039779783 731 DLLQH-YKKDRTILLTTHHMDEADVLGDRIAILVMG 765
Cdd:PRK13536 213 ERLRSlLARGKTILLTTHFMEEAERLCDRLCVLEAG 248
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
546-762 |
9.11e-35 |
|
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: 140.42 E-value: 9.11e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779783 546 EPEPVglvagIRIQHLYKEF-ILKNSTLMAVNDLSLNLYEGQITVLLGHNGAGKTTTLSILTGLYLPTRGKVYISGYDIS 624
Cdd:COG1123 256 AAEPL-----LEVRNLSKRYpVRGKGGVRAVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRPTSGSILFDGKDLT 330
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779783 625 ----SDMVQIRKSLGLCPQD--DLLFPMLTVSEHLHFYCVIKGIPLQNQSRE-TNRMLTSFGLlqQSNTMSK---DLSGG 694
Cdd:COG1123 331 klsrRSLRELRRRVQMVFQDpySSLNPRMTVGDIIAEPLRLHGLLSRAERRErVAELLERVGL--PPDLADRyphELSGG 408
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779783 695 MKRKLSIIIALIGDTKVVILDEPTSGMDPVSRRATWDLLQHYKKDR--TILLTTHHMDEADVLGDRIAIL 762
Cdd:COG1123 409 QRQRVAIARALALEPKLLILDEPTSALDVSVQAQILNLLRDLQRELglTYLFISHDLAVVRYIADRVAVM 478
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
556-762 |
2.31e-34 |
|
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP (Multidrug Resistance Protein)-like transporters are involved in drug, peptide, and lipid export. They belong to the subfamily C of the ATP-binding cassette (ABC) superfamily of transport proteins. The ABCC subfamily contains transporters with a diverse functional spectrum that includes ion transport, cell surface receptor, and toxin secretion activities. The MRP-like family, similar to all ABC proteins, have a common four-domain core structure constituted by two membrane-spanning domains, each composed of six transmembrane (TM) helices, and two nucleotide-binding domains (NBD). ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213195 [Multi-domain] Cd Length: 171 Bit Score: 129.43 E-value: 2.31e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779783 556 IRIQHLYkeFILKNSTLMAVNDLSLNLYEGQITVLLGHNGAGKTTTLSILTGLYLPTRGKVYISGYDISS-DMVQIRKSL 634
Cdd:cd03228 1 IEFKNVS--FSYPGRPKPVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGVDLRDlDLESLRKNI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779783 635 GLCPQDDLLFPMlTVSEHLhfycvikgiplqnqsretnrmltsfgllqqsntmskdLSGGMKRKLSIIIALIGDTKVVIL 714
Cdd:cd03228 79 AYVPQDPFLFSG-TIRENI-------------------------------------LSGGQRQRIAIARALLRDPPILIL 120
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1039779783 715 DEPTSGMDPVSRRATWDLLQHYKKDRTILLTTHHMDEADvLGDRIAIL 762
Cdd:cd03228 121 DEATSALDPETEALILEALRALAKGKTVIVIAHRLSTIR-DADRIIVL 167
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
556-765 |
2.22e-33 |
|
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: 126.92 E-value: 2.22e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779783 556 IRIQHLYKEFILKnstlMAVNDLSLNLYEGQITVLLGHNGAGKTTTLSILTGLYLPTRGKVYISGYDISSDMVQI---RK 632
Cdd:cd03229 1 LELKNVSKRYGQK----TVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGEDLTDLEDELpplRR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779783 633 SLGLCPQDDLLFPMLTVSEhlhfycvikgiplqnqsretNRMLTsfgllqqsntmskdLSGGMKRKLSIIIALIGDTKVV 712
Cdd:cd03229 77 RIGMVFQDFALFPHLTVLE--------------------NIALG--------------LSGGQQQRVALARALAMDPDVL 122
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1039779783 713 ILDEPTSGMDPVSRRATWDLLQ--HYKKDRTILLTTHHMDEADVLGDRIAILVMG 765
Cdd:cd03229 123 LLDEPTSALDPITRREVRALLKslQAQLGITVVLVTHDLDEAARLADRVVVLRDG 177
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
575-762 |
1.40e-32 |
|
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: 126.50 E-value: 1.40e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779783 575 VNDLSLNLYEGQITVLLGHNGAGKTTTLSILTGLYLPTRGKVYISGYDISSDMVQIRKSLGLC--PQDDLLFPMLTVSEH 652
Cdd:cd03218 16 VNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDGQDITKLPMHKRARLGIGylPQEASIFRKLTVEEN 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779783 653 LHFYCVIKGIPLQNQSRETNRMLTSFGLLQQSNTMSKDLSGGMKRKLSIIIALIGDTKVVILDEPTSGMDPVSRRATWDL 732
Cdd:cd03218 96 ILAVLEIRGLSKKEREEKLEELLEEFHITHLRKSKASSLSGGERRRVEIARALATNPKFLLLDEPFAGVDPIAVQDIQKI 175
|
170 180 190
....*....|....*....|....*....|..
gi 1039779783 733 LQHYkKDRTI--LLTTHHMDEADVLGDRIAIL 762
Cdd:cd03218 176 IKIL-KDRGIgvLITDHNVRETLSITDRAYII 206
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
554-762 |
2.66e-32 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 129.45 E-value: 2.66e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779783 554 AGIRIQHLYKEFilknSTLMAVNDLSLNLYEGQITVLLGHNGAGKTTTLSILTGLYLPTRGKVYISGYDISSdmVQIRK- 632
Cdd:COG3842 4 PALELENVSKRY----GDVTALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRILLDGRDVTG--LPPEKr 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779783 633 SLGLCPQDDLLFPMLTVSEHLHFYCVIKGIPLQNQSRETNRMLTSFGLLQQSNTMSKDLSGGMKRKLSIIIALIGDTKVV 712
Cdd:COG3842 78 NVGMVFQDYALFPHLTVAENVAFGLRMRGVPKAEIRARVAELLELVGLEGLADRYPHQLSGGQQQRVALARALAPEPRVL 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1039779783 713 ILDEPTSGMDPVSRRATWDLLQHYKKDR--TILLTTHHMDEADVLGDRIAIL 762
Cdd:COG3842 158 LLDEPLSALDAKLREEMREELRRLQRELgiTFIYVTHDQEEALALADRIAVM 209
|
|
| galliderm_ABC |
TIGR03740 |
gallidermin-class lantibiotic protection ABC transporter, ATP-binding subunit; Model TIGR03731 ... |
556-768 |
6.83e-32 |
|
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: 124.43 E-value: 6.83e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779783 556 IRIQHLYKEFilKNSTlmAVNDLSLNLYEGQITVLLGHNGAGKTTTLSILTGLYLPTRGKVYISGYDISSDMVqirKSLG 635
Cdd:TIGR03740 1 LETKNLSKRF--GKQT--AVNNISLTVPKNSVYGLLGPNGAGKSTLLKMITGILRPTSGEIIFDGHPWTRKDL---HKIG 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779783 636 LCPQDDLLFPMLTVSEHLHFYCVIKGIPLQnqsrETNRMLTSFGLLQQSNTMSKDLSGGMKRKLSIIIALIGDTKVVILD 715
Cdd:TIGR03740 74 SLIESPPLYENLTARENLKVHTTLLGLPDS----RIDEVLNIVDLTNTGKKKAKQFSLGMKQRLGIAIALLNHPKLLILD 149
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1039779783 716 EPTSGMDPVSRRATWDLLQHYKKD-RTILLTTHHMDEADVLGDRIAILVMGILK 768
Cdd:TIGR03740 150 EPTNGLDPIGIQELRELIRSFPEQgITVILSSHILSEVQQLADHIGIISEGVLG 203
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
574-765 |
1.01e-31 |
|
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: 123.70 E-value: 1.01e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779783 574 AVNDLSLNLYEGQITVLLGHNGAGKTTTLSILTGLYLPTRGKVYISGYDISS----DMVqiRKSLGLCPQDDLLFPMLTV 649
Cdd:cd03224 15 ILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDGRDITGlpphERA--RAGIGYVPEGRRIFPELTV 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779783 650 SEHLHFYCVIKGIPLQNQSREtnRMLTSFGLLQQ-SNTMSKDLSGGMKRKLSIIIALIGDTKVVILDEPTSGMDPVSRRA 728
Cdd:cd03224 93 EENLLLGAYARRRAKRKARLE--RVYELFPRLKErRKQLAGTLSGGEQQMLAIARALMSRPKLLLLDEPSEGLAPKIVEE 170
|
170 180 190
....*....|....*....|....*....|....*...
gi 1039779783 729 TWDLLQHYKKD-RTILLTTHHMDEADVLGDRIAILVMG 765
Cdd:cd03224 171 IFEAIRELRDEgVTILLVEQNARFALEIADRAYVLERG 208
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
556-762 |
1.29e-31 |
|
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: 123.85 E-value: 1.29e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779783 556 IRIQHLYKEFILKNSTLMAVNDLSLNLYEGQITVLLGHNGAGKTTTLSILTGLYLPTRGKVYISGYDIS----SDMVQIR 631
Cdd:cd03258 2 IELKNVSKVFGDTGGKVTALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGSVLVDGTDLTllsgKELRKAR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779783 632 KSLGLCPQDDLLFPMLTVSEHLHFYCVIKGIPLQNQSRETNRMLTSFGLLQQSNTMSKDLSGGMKRKLSIIIALIGDTKV 711
Cdd:cd03258 82 RRIGMIFQHFNLLSSRTVFENVALPLEIAGVPKAEIEERVLELLELVGLEDKADAYPAQLSGGQKQRVGIARALANNPKV 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1039779783 712 VILDEPTSGMDPVSRRATWDLLQHYKKDR--TILLTTHHMDEADVLGDRIAIL 762
Cdd:cd03258 162 LLCDEATSALDPETTQSILALLRDINRELglTIVLITHEMEVVKRICDRVAVM 214
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
568-771 |
2.66e-31 |
|
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: 122.76 E-value: 2.66e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779783 568 KNSTLMAVNDLSLNLYEGQITVLLGHNGAGKTTTLSILTGLYLP---TRGKVYISGYDISSDmvQIRKSLGLCPQDDLLF 644
Cdd:cd03234 16 WNKYARILNDVSLHVESGQVMAILGSSGSGKTTLLDAISGRVEGggtTSGQILFNGQPRKPD--QFQKCVAYVRQDDILL 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779783 645 PMLTVSEHLHFYCVIKgipLQNQSRETNR--MLTSFGLLQQSNTMS-----KDLSGGMKRKLSIIIALIGDTKVVILDEP 717
Cdd:cd03234 94 PGLTVRETLTYTAILR---LPRKSSDAIRkkRVEDVLLRDLALTRIggnlvKGISGGERRRVSIAVQLLWDPKVLILDEP 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1039779783 718 TSGMDPVSRRATWDLLQHY-KKDRTILLTTHHmDEADV--LGDRIAILVMGILKCCG 771
Cdd:cd03234 171 TSGLDSFTALNLVSTLSQLaRRNRIVILTIHQ-PRSDLfrLFDRILLLSSGEIVYSG 226
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
545-787 |
3.74e-30 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 119.81 E-value: 3.74e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779783 545 MEPEPVglvagIRIQHLYkeFILKNSTlmAVNDLSLNLYEGQITVLLGHNGAGKTTTLSILTGLYLPTRGKVYISGYDIS 624
Cdd:COG1121 1 MMMMPA-----IELENLT--VSYGGRP--VLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLFGKPPR 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779783 625 SDmvqiRKSLGLCPQD---DLLFPMlTVSE--------HLHFYcvikGIPLQNQSRETNRMLTSFGLLQQSNTMSKDLSG 693
Cdd:COG1121 72 RA----RRRIGYVPQRaevDWDFPI-TVRDvvlmgrygRRGLF----RRPSRADREAVDEALERVGLEDLADRPIGELSG 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779783 694 GMKRKLSIIIALIGDTKVVILDEPTSGMDPVSRRATWDLLQHYKK-DRTILLTTHHMDEADVLGDRIAILVMGILkCCG- 771
Cdd:COG1121 143 GQQQRVLLARALAQDPDLLLLDEPFAGVDAATEEALYELLRELRReGKTILVVTHDLGAVREYFDRVLLLNRGLV-AHGp 221
|
250 260
....*....|....*....|.
gi 1039779783 772 -----SSLFLKKLYGVGYHLV 787
Cdd:COG1121 222 peevlTPENLSRAYGGPVALL 242
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
556-767 |
5.05e-30 |
|
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: 119.21 E-value: 5.05e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779783 556 IRIQHLYKEFilknSTLMAVNDLSLNLYEGQITVLLGHNGAGKTTTLSILTGLY-----LPTRGKVYISG---YDISSDM 627
Cdd:cd03260 1 IELRDLNVYY----GDKHALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRLNdlipgAPDEGEVLLDGkdiYDLDVDV 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779783 628 VQIRKSLGLCPQDDLLFPMlTVSEHLHFYCVIKGIPLQNQSRETNR-MLTSFGLLQQ--SNTMSKDLSGGMKRKLSIIIA 704
Cdd:cd03260 77 LELRRRVGMVFQKPNPFPG-SIYDNVAYGLRLHGIKLKEELDERVEeALRKAALWDEvkDRLHALGLSGGQQQRLCLARA 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1039779783 705 LIGDTKVVILDEPTSGMDPVSRRATWDLLQHYKKDRTILLTTHHMDEADVLGDRIAILVMGIL 767
Cdd:cd03260 156 LANEPEVLLLDEPTSALDPISTAKIEELIAELKKEYTIVIVTHNMQQAARVADRTAFLLNGRL 218
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
556-767 |
7.60e-30 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 118.61 E-value: 7.60e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779783 556 IRIQHLYKEFILKNSTLMAVNDLSLNLYEGQITVLLGHNGAGKTTTLSILTGLYLPTRGKVYISGYDISS----DMVQIR 631
Cdd:COG1136 5 LELRNLTKSYGTGEGEVTALRGVSLSIEAGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVLIDGQDISSlserELARLR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779783 632 -KSLGLCPQDDLLFPMLTVSEHLHFYCVIKGIPLQNQSRETNRMLTSFGLLQQSNTMSKDLSGGMKRKLSIIIALIGDTK 710
Cdd:COG1136 85 rRHIGFVFQFFNLLPELTALENVALPLLLAGVSRKERRERARELLERVGLGDRLDHRPSQLSGGQQQRVAIARALVNRPK 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1039779783 711 VVILDEPTSGMDPVSRRATWDLLQHYKKD--RTILLTTHHMDEADvLGDRIAILVMGIL 767
Cdd:COG1136 165 LILADEPTGNLDSKTGEEVLELLRELNRElgTTIVMVTHDPELAA-RADRVIRLRDGRI 222
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
556-808 |
8.13e-30 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 119.71 E-value: 8.13e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779783 556 IRIQHLYkeFILKNSTLMAVNDLSLNLYEGQITVLLGHNGAGKTTTLSILTGLYLPTRGKVYISGYDISSDMV-QIRKSL 634
Cdd:PRK13632 8 IKVENVS--FSYPNSENNALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIDGITISKENLkEIRKKI 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779783 635 GLCPQD-DLLFPMLTVSEHLHFYCVIKGIPLQNQSRETNRMLTSFGLLQQSNTMSKDLSGGMKRKLSIIIALIGDTKVVI 713
Cdd:PRK13632 86 GIIFQNpDNQFIGATVEDDIAFGLENKKVPPKKMKDIIDDLAKKVGMEDYLDKEPQNLSGGQKQRVAIASVLALNPEIII 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779783 714 LDEPTSGMDPVSRRATWDLLQ--HYKKDRTILLTTHHMDEAdVLGDRiaILVMGilkccgsslflkklygvGYHLVIVKT 791
Cdd:PRK13632 166 FDESTSMLDPKGKREIKKIMVdlRKTRKKTLISITHDMDEA-ILADK--VIVFS-----------------EGKLIAQGK 225
|
250
....*....|....*....
gi 1039779783 792 PDS--NDEKIFQLIKNYIP 808
Cdd:PRK13632 226 PKEilNNKEILEKAKIDSP 244
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
574-765 |
9.28e-30 |
|
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: 118.59 E-value: 9.28e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779783 574 AVNDLSLNLYEGQITVLLGHNGAGKTTTLSILTGLYLPTRGKVYISGYDISSDMVQIRKSLGLC-PQDDLLFPMLTVSEH 652
Cdd:cd03267 36 ALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRVAGLVPWKRRKKFLRRIGVVfGQKTQLWWDLPVIDS 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779783 653 LHFYCVIKGIP---LQNQSRETNRMLTSFGLLQQSntmSKDLSGGMKRKLSIIIALIGDTKVVILDEPTSGMDPVSRRAT 729
Cdd:cd03267 116 FYLLAAIYDLPparFKKRLDELSELLDLEELLDTP---VRQLSLGQRMRAEIAAALLHEPEILFLDEPTIGLDVVAQENI 192
|
170 180 190
....*....|....*....|....*....|....*...
gi 1039779783 730 WDLLQHYKKDR--TILLTTHHMDEADVLGDRIAILVMG 765
Cdd:cd03267 193 RNFLKEYNRERgtTVLLTSHYMKDIEALARRVLVIDKG 230
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
556-747 |
1.94e-29 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 117.08 E-value: 1.94e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779783 556 IRIQHLYKEFilKNSTlMAVNDLSLNLYEGQITVLLGHNGAGKTTTLSILTGLYLPTRGKVYISGYDIS----SDMVQIR 631
Cdd:COG2884 2 IRFENVSKRY--PGGR-EALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLVNGQDLSrlkrREIPYLR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779783 632 KSLGLCPQDDLLFPMLTVSEHLHFYCVIKGIPLQNQSRETNRMLTSFGLLQQSNTMSKDLSGGMKRKLSIIIALIGDTKV 711
Cdd:COG2884 79 RRIGVVFQDFRLLPDRTVYENVALPLRVTGKSRKEIRRRVREVLDLVGLSDKAKALPHELSGGEQQRVAIARALVNRPEL 158
|
170 180 190
....*....|....*....|....*....|....*..
gi 1039779783 712 VILDEPTSGMDPVSRRATWDLLQHY-KKDRTILLTTH 747
Cdd:COG2884 159 LLADEPTGNLDPETSWEIMELLEEInRRGTTVLIATH 195
|
|
| LPS_export_lptB |
TIGR04406 |
LPS export ABC transporter ATP-binding protein; Members of this fmaily are LptB, the ... |
556-765 |
2.67e-29 |
|
LPS export ABC transporter ATP-binding protein; Members of this fmaily are LptB, the ATP-binding cassette protein of an ABC transporter involved in lipopolysaccharide export. [Cell envelope, Biosynthesis and degradation of surface polysaccharides and lipopolysaccharides, Transport and binding proteins, Other]
Pssm-ID: 275199 [Multi-domain] Cd Length: 239 Bit Score: 117.38 E-value: 2.67e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779783 556 IRIQHLYKEFILKNstlmAVNDLSLNLYEGQITVLLGHNGAGKTTTLSILTGLYLPTRGKVYISGYDISSDMVQIRKSLG 635
Cdd:TIGR04406 2 LVAENLIKSYKKRK----VVNDVSLSVKSGEIVGLLGPNGAGKTTSFYMIVGLVRPDAGKILIDGQDITHLPMHERARLG 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779783 636 L--CPQDDLLFPMLTVSEHLHfyCV---IKGIPLQNQSRETNRMLTSFGLLQQSNTMSKDLSGGMKRKLSIIIALIGDTK 710
Cdd:TIGR04406 78 IgyLPQEASIFRKLTVEENIM--AVleiRKDLDRAEREERLEALLEEFQISHLRDNKAMSLSGGERRRVEIARALATNPK 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1039779783 711 VVILDEPTSGMDPVsrrATWDL--LQHYKKDRTI--LLTTHHMDEADVLGDRIAILVMG 765
Cdd:TIGR04406 156 FILLDEPFAGVDPI---AVGDIkkIIKHLKERGIgvLITDHNVRETLDICDRAYIISDG 211
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
562-765 |
6.21e-29 |
|
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: 114.96 E-value: 6.21e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779783 562 YKEFILKNSTLMAvndlslnlYEGQITVLLGHNGAGKTTTLSILTGL--YLPTRGKVYISGYDISSDmvQIRKSLGLCPQ 639
Cdd:cd03213 20 SGKQLLKNVSGKA--------KPGELTAIMGPSGAGKSTLLNALAGRrtGLGVSGEVLINGRPLDKR--SFRKIIGYVPQ 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779783 640 DDLLFPMLTVSEHLHFYCVIKGIplqnqsretnrmltsfgllqqsntmskdlSGGMKRKLSIIIALIGDTKVVILDEPTS 719
Cdd:cd03213 90 DDILHPTLTVRETLMFAAKLRGL-----------------------------SGGERKRVSIALELVSNPSLLFLDEPTS 140
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1039779783 720 GMDPVSRRATWDLLQHYKKD-RTILLTTHH-MDEADVLGDRIAILVMG 765
Cdd:cd03213 141 GLDSSSALQVMSLLRRLADTgRTIICSIHQpSSEIFELFDKLLLLSQG 188
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
574-765 |
1.60e-28 |
|
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: 121.16 E-value: 1.60e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779783 574 AVNDLSLNLYEGQITVLLGHNGAGKTTTLSILTGLyLP----TRGKVYISGYDISSDMVQIR-KSLGLCPQD-DLLFPML 647
Cdd:COG1123 21 AVDGVSLTIAPGETVALVGESGSGKSTLALALMGL-LPhggrISGEVLLDGRDLLELSEALRgRRIGMVFQDpMTQLNPV 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779783 648 TVSEHLHFYCVIKGIPLQNQSRETNRMLTSFGLLQQSNTMSKDLSGGMKRKLSIIIALIGDTKVVILDEPTSGMDPVSRR 727
Cdd:COG1123 100 TVGDQIAEALENLGLSRAEARARVLELLEAVGLERRLDRYPHQLSGGQRQRVAIAMALALDPDLLIADEPTTALDVTTQA 179
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1039779783 728 ATWDLLQHYKKDR--TILLTTHHMDEADVLGDRIAILVMG 765
Cdd:COG1123 180 EILDLLRELQRERgtTVLLITHDLGVVAEIADRVVVMDDG 219
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
545-764 |
2.10e-28 |
|
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: 122.64 E-value: 2.10e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779783 545 MEPEPVGLVAGIRIQHLYKEFILKN-------STLMAVNDLSLNLYEGQITVLLGHNGAGKTTTLSILTGLYLPTRGKVY 617
Cdd:COG2274 454 LPPEREEGRSKLSLPRLKGDIELENvsfrypgDSPPVLDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEPTSGRIL 533
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779783 618 ISGYDISS-DMVQIRKSLGLCPQDDLLFPMlTVSEHLHFYCviKGIPLQnQSRETNRM--LTSF------GLLQQSNTMS 688
Cdd:COG2274 534 IDGIDLRQiDPASLRRQIGVVLQDVFLFSG-TIRENITLGD--PDATDE-EIIEAARLagLHDFiealpmGYDTVVGEGG 609
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1039779783 689 KDLSGGMKRKLSIIIALIGDTKVVILDEPTSGMDPVSRRATWDLLQHYKKDRTILLTTH---HMDEADVlgdriaILVM 764
Cdd:COG2274 610 SNLSGGQRQRLAIARALLRNPRILILDEATSALDAETEAIILENLRRLLKGRTVIIIAHrlsTIRLADR------IIVL 682
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
556-767 |
2.41e-28 |
|
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) proteins function from bacteria to human, mediating the translocation of substances into and out of cells or organelles. ABC transporters contain two transmembrane-spanning domains (TMDs) or subunits and two nucleotide binding domains (NBDs) or subunits that couple transport to the hydrolysis of ATP. In the maltose transport system, the periplasmic maltose binding protein (MBP) stimulates the ATPase activity of the membrane-associated transporter, which consists of two transmembrane subunits, MalF and MalG, and two copies of the ATP binding subunit, MalK, and becomes tightly bound to the transporter in the catalytic transition state, ensuring that maltose is passed to the transporter as ATP is hydrolyzed.
Pssm-ID: 213268 [Multi-domain] Cd Length: 213 Bit Score: 113.89 E-value: 2.41e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779783 556 IRIQHLYKEFilKNSTlmAVNDLSLNLYEGQITVLLGHNGAGKTTTLSILTGLYLPTRGKVYISGYDIsSDMVQIRKSLG 635
Cdd:cd03301 1 VELENVTKRF--GNVT--ALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGRDV-TDLPPKDRDIA 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779783 636 LCPQDDLLFPMLTVSEHLHFYCVIKGIP---LQNQSRETNRMLTSFGLLqqsNTMSKDLSGGMKRKLSIIIALIGDTKVV 712
Cdd:cd03301 76 MVFQNYALYPHMTVYDNIAFGLKLRKVPkdeIDERVREVAELLQIEHLL---DRKPKQLSGGQRQRVALGRAIVREPKVF 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1039779783 713 ILDEPTSGMDPVSRRATWDLLQ--HYKKDRTILLTTHHMDEADVLGDRIAILVMGIL 767
Cdd:cd03301 153 LMDEPLSNLDAKLRVQMRAELKrlQQRLGTTTIYVTHDQVEAMTMADRIAVMNDGQI 209
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
546-786 |
3.32e-28 |
|
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: 121.03 E-value: 3.32e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779783 546 EPEPVGLVAGIRIQHLYkeFILKNSTLMAVNDLSLNLYEGQITVLLGHNGAGKTTTLSILTGLYLPTRGKVYISGYDISS 625
Cdd:COG4987 324 EPAPAPGGPSLELEDVS--FRYPGAGRPVLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFLDPQSGSITLGGVDLRD 401
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779783 626 -DMVQIRKSLGLCPQDDLLFPMlTVSEHLHFycvikGIPlqNQSRET-NRMLTSFGLLQQSNTMSKDL-----------S 692
Cdd:COG4987 402 lDEDDLRRRIAVVPQRPHLFDT-TLRENLRL-----ARP--DATDEElWAALERVGLGDWLAALPDGLdtwlgeggrrlS 473
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779783 693 GGMKRKLSIIIALIGDTKVVILDEPTSGMDPVSRRATWDLLQHYKKDRTILLTTHHMDEADvLGDRIAILVMGILKCCGS 772
Cdd:COG4987 474 GGERRRLALARALLRDAPILLLDEPTEGLDAATEQALLADLLEALAGRTVLLITHRLAGLE-RMDRILVLEDGRIVEQGT 552
|
250
....*....|....
gi 1039779783 773 SLFLKKLYGVGYHL 786
Cdd:COG4987 553 HEELLAQNGRYRQL 566
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
556-747 |
4.04e-28 |
|
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where FtsE is the ATPase and the membrane subunit FtsX resembles a permease subunit. But rather than transporting any substrate, the complex acts in cell division by undergoing conformational changes that alter the activity of cell wall hydrolases located outside the plasma membrane. The complex is widely conserved in bacteria, but also extremely divergent in sequence between different lineages
Pssm-ID: 213259 [Multi-domain] Cd Length: 214 Bit Score: 113.27 E-value: 4.04e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779783 556 IRIQHLYKEFilkNSTLMAVNDLSLNLYEGQITVLLGHNGAGKTTTLSILTGLYLPTRGKVYISGYDIS----SDMVQIR 631
Cdd:cd03292 1 IEFINVTKTY---PNGTAALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQDVSdlrgRAIPYLR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779783 632 KSLGLCPQDDLLFPMLTVSEHLHFYCVIKGIPLQNQSRETNRMLTSFGLLQQSNTMSKDLSGGMKRKLSIIIALIGDTKV 711
Cdd:cd03292 78 RKIGVVFQDFRLLPDRNVYENVAFALEVTGVPPREIRKRVPAALELVGLSHKHRALPAELSGGEQQRVAIARAIVNSPTI 157
|
170 180 190
....*....|....*....|....*....|....*..
gi 1039779783 712 VILDEPTSGMDPVSRRATWDLLQHY-KKDRTILLTTH 747
Cdd:cd03292 158 LIADEPTGNLDPDTTWEIMNLLKKInKAGTTVVVATH 194
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
556-772 |
7.82e-28 |
|
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: 112.72 E-value: 7.82e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779783 556 IRIQHLYKEFilknSTLMAVNDLSLNLYEGQITVLLGHNGAGKTTTLSILTGLYLPTRGKVYISGYDISsDMVQIRKSLG 635
Cdd:cd03300 1 IELENVSKFY----GGFVALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGKDIT-NLPPHKRPVN 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779783 636 LCPQDDLLFPMLTVSEHLHFYCVIKGIPLQNQSRETNRMLTSFGLLQQSNTMSKDLSGGMKRKLSIIIALIGDTKVVILD 715
Cdd:cd03300 76 TVFQNYALFPHLTVFENIAFGLRLKKLPKAEIKERVAEALDLVQLEGYANRKPSQLSGGQQQRVAIARALVNEPKVLLLD 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1039779783 716 EPTSGMDPVSRRATWDLLQ--HYKKDRTILLTTHHMDEADVLGDRIAILVMGILKCCGS 772
Cdd:cd03300 156 EPLGALDLKLRKDMQLELKrlQKELGITFVFVTHDQEEALTMSDRIAVMNKGKIQQIGT 214
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
564-762 |
8.23e-28 |
|
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: 112.30 E-value: 8.23e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779783 564 EFILKNSTLMAVNDLSLNLYEGQITVLLGHNGAGKTTTLSILTGLYLPTRGKVYISGYDISS-DMVQIRKSLGLCPQDdl 642
Cdd:cd03245 9 SFSYPNQEIPALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGTDIRQlDPADLRRNIGYVPQD-- 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779783 643 lfPMLtvsehlhFYCVIK-GIPLQNQSRETNRML--------TSF------GLLQQSNTMSKDLSGGMKRKLSIIIALIG 707
Cdd:cd03245 87 --VTL-------FYGTLRdNITLGAPLADDERILraaelagvTDFvnkhpnGLDLQIGERGRGLSGGQRQAVALARALLN 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1039779783 708 DTKVVILDEPTSGMDPVSRRATWDLLQHYKKDRTILLTTHHMdEADVLGDRIAIL 762
Cdd:cd03245 158 DPPILLLDEPTSAMDMNSEERLKERLRQLLGDKTLIIITHRP-SLLDLVDRIIVM 211
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
556-762 |
9.80e-28 |
|
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid transport and metabolism, Inorganic ion transport and metabolism];
Pssm-ID: 440741 [Multi-domain] Cd Length: 248 Bit Score: 112.97 E-value: 9.80e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779783 556 IRIQHLYKEFILKNSTLMAVNDLSLNLYEGQITVLLGHNGAGKTTTLSILTGLYLPTRGKVYISGYDIS-SDMVQIRKSL 634
Cdd:COG1124 2 LEVRNLSVSYGQGGRRVPVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVTFDGRPVTrRRRKAFRRRV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779783 635 GLCPQDDL--LFPMLTVSEHLHFYCVIKGIPlqNQSRETNRMLTSFGLlqQSNTMSK---DLSGGMKRKLSIIIALIGDT 709
Cdd:COG1124 82 QMVFQDPYasLHPRHTVDRILAEPLRIHGLP--DREERIAELLEQVGL--PPSFLDRyphQLSGGQRQRVAIARALILEP 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1039779783 710 KVVILDEPTSGMDPVSRRATWDLLQHYKKDR--TILLTTHHMDEADVLGDRIAIL 762
Cdd:COG1124 158 ELLLLDEPTSALDVSVQAEILNLLKDLREERglTYLFVSHDLAVVAHLCDRVAVM 212
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
556-762 |
1.07e-27 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 115.18 E-value: 1.07e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779783 556 IRIQHLYKEFI-------LKNS----------TLMAVNDLSLNLYEGQITVLLGHNGAGKTTTLSILTGLYLPTRGKVYI 618
Cdd:COG4586 2 IEVENLSKTYRvyekepgLKGAlkglfrreyrEVEAVDDISFTIEPGEIVGFIGPNGAGKSTTIKMLTGILVPTSGEVRV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779783 619 SGYDISSDMVQIRKSLGLC-PQDDLLFPMLTVSEHLHFYCVIKGIPlQNQSRETNRMLTsfGLLQQSNTMSKDLsggmkR 697
Cdd:COG4586 82 LGYVPFKRRKEFARRIGVVfGQRSQLWWDLPAIDSFRLLKAIYRIP-DAEYKKRLDELV--ELLDLGELLDTPV-----R 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1039779783 698 KLS--------IIIALIGDTKVVILDEPTSGMDPVSRRATWDLLQHYKKDR--TILLTTHHMDEADVLGDRIAIL 762
Cdd:COG4586 154 QLSlgqrmrceLAAALLHRPKILFLDEPTIGLDVVSKEAIREFLKEYNRERgtTILLTSHDMDDIEALCDRVIVI 228
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
561-765 |
1.55e-27 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 116.29 E-value: 1.55e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779783 561 LYKEFILKNSTL-MAVNDLSLNLYEGQITVLLGHNGAGKTTTLSILTGLYLPTRGKVYISGYDIS----SDMVQI-RKSL 634
Cdd:PRK10070 29 LSKEQILEKTGLsLGVKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAkisdAELREVrRKKI 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779783 635 GLCPQDDLLFPMLTVSEHLHFYCVIKGIPLQNQSRETNRMLTSFGLLQQSNTMSKDLSGGMKRKLSIIIALIGDTKVVIL 714
Cdd:PRK10070 109 AMVFQSFALMPHMTVLDNTAFGMELAGINAEERREKALDALRQVGLENYAHSYPDELSGGMRQRVGLARALAINPDILLM 188
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1039779783 715 DEPTSGMDPVSRRATWDLL--QHYKKDRTILLTTHHMDEADVLGDRIAILVMG 765
Cdd:PRK10070 189 DEAFSALDPLIRTEMQDELvkLQAKHQRTIVFISHDLDEAMRIGDRIAIMQNG 241
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
574-762 |
1.71e-27 |
|
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: 111.47 E-value: 1.71e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779783 574 AVNDLSLNLYEGQITVLLGHNGAGKTTTLSILTGLYLPTRGKVYISGYDISSDmvqiRKSLGLCPQD---DLLFPmLTVS 650
Cdd:cd03235 14 VLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFGKPLEKE----RKRIGYVPQRrsiDRDFP-ISVR 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779783 651 EHLHFYCVIKGIPLQNQSRET----NRMLTSFGLLQQSNTMSKDLSGGMKRKLSIIIALIGDTKVVILDEPTSGMDPVSR 726
Cdd:cd03235 89 DVVLMGLYGHKGLFRRLSKADkakvDEALERVGLSELADRQIGELSGGQQQRVLLARALVQDPDLLLLDEPFAGVDPKTQ 168
|
170 180 190
....*....|....*....|....*....|....*..
gi 1039779783 727 RATWDLLQHYKKD-RTILLTTHHMDEADVLGDRIAIL 762
Cdd:cd03235 169 EDIYELLRELRREgMTILVVTHDLGLVLEYFDRVLLL 205
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
574-765 |
3.01e-27 |
|
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: 111.23 E-value: 3.01e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779783 574 AVNDLSLNLYEGQITVLLGHNGAGKTTTLSILTGLYLPTRGKVYISGYDISS----DMVqiRKSLGLCPQDDLLFPMLTV 649
Cdd:COG0410 18 VLHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRSGSIRFDGEDITGlpphRIA--RLGIGYVPEGRRIFPSLTV 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779783 650 SEHLH--FYCViKGIPLQNQSREtnRMLTSFGLLQQ-SNTMSKDLSGGMKRKLSIIIALIGDTKVVILDEPTSGMDPVSR 726
Cdd:COG0410 96 EENLLlgAYAR-RDRAEVRADLE--RVYELFPRLKErRRQRAGTLSGGEQQMLAIGRALMSRPKLLLLDEPSLGLAPLIV 172
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1039779783 727 RATWDLLQHYKKD-RTILLTTHHMDEADVLGDRIAILVMG 765
Cdd:COG0410 173 EEIFEIIRRLNREgVTILLVEQNARFALEIADRAYVLERG 212
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
557-762 |
3.11e-27 |
|
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: 110.42 E-value: 3.11e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779783 557 RIQHLYkeFILKNSTLmAVNDLSLNLYEGQITVLLGHNGAGKTTTLSILTGLYLPTRGKVYISGYDISSDMVqiRKSLGL 636
Cdd:cd03226 1 RIENIS--FSYKKGTE-ILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLNGKPIKAKER--RKSIGY 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779783 637 CPQD--DLLFpMLTVSEHLhfYCVIKGIPLQNQSRETnrMLTSFGLLQQSNTMSKDLSGGMKRKLSIIIALIGDTKVVIL 714
Cdd:cd03226 76 VMQDvdYQLF-TDSVREEL--LLGLKELDAGNEQAET--VLKDLDLYALKERHPLSLSGGQKQRLAIAAALLSGKDLLIF 150
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1039779783 715 DEPTSGMDPVSRRATWDLLQH-YKKDRTILLTTHHMDEADVLGDRIAIL 762
Cdd:cd03226 151 DEPTSGLDYKNMERVGELIRElAAQGKAVIVITHDYEFLAKVCDRVLLL 199
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
562-797 |
4.38e-27 |
|
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: 110.89 E-value: 4.38e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779783 562 YKEFILKNstlmavndLSLNLYEGQITVLLGHNGAGKTTTLSILTGLYLPTRGKVYISGYDISsDMVQIRKSLGLCPQDD 641
Cdd:cd03299 10 WKEFKLKN--------VSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNGKDIT-NLPPEKRDISYVPQNY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779783 642 LLFPMLTVSEHLHFYCVIKGIPLQNQSRETNRMLTSFGLLQQSNTMSKDLSGGMKRKLSIIIALIGDTKVVILDEPTSGM 721
Cdd:cd03299 81 ALFPHMTVYKNIAYGLKKRKVDKKEIERKVLEIAEMLGIDHLLNRKPETLSGGEQQRVAIARALVVNPKILLLDEPFSAL 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1039779783 722 DPVSRRATWDLLQ--HYKKDRTILLTTHHMDEADVLGDRIAILVMGilkccgsslflkKLYGVGYHLVIVKTPdSNDE 797
Cdd:cd03299 161 DVRTKEKLREELKkiRKEFGVTVLHVTHDFEEAWALADKVAIMLNG------------KLIQVGKPEEVFKKP-KNEF 225
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
554-762 |
9.03e-27 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 110.12 E-value: 9.03e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779783 554 AGIRIQHLYKEFilKNSTlmAVNDLSLNLYEGQITVLLGHNGAGKTTTLSILTGLYLPTRGKVYISGYDISSD-MVQ-IR 631
Cdd:COG1137 2 MTLEAENLVKSY--GKRT--VVKDVSLEVNQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGRIFLDGEDITHLpMHKrAR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779783 632 KSLGLCPQDDLLFPMLTVSEHLhfYCV--IKGIPLQNQSRETNRMLTSFGLLQQSNTMSKDLSGGMKRKLSIIIALIGDT 709
Cdd:COG1137 78 LGIGYLPQEASIFRKLTVEDNI--LAVleLRKLSKKEREERLEELLEEFGITHLRKSKAYSLSGGERRRVEIARALATNP 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1039779783 710 KVVILDEPTSGMDPVS----RRATWDLlqhykKDRTI--LLTTHHMDEAdvLG--DRIAIL 762
Cdd:COG1137 156 KFILLDEPFAGVDPIAvadiQKIIRHL-----KERGIgvLITDHNVRET--LGicDRAYII 209
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
575-795 |
1.05e-26 |
|
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: 110.13 E-value: 1.05e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779783 575 VNDLSLNLYEGQITVLLGHNGAGKTTTLSILTGLYLPTRGKVYISGYDISS-DMVQIRKSLGLCPQD-DLLFPmLTVSE- 651
Cdd:COG1120 17 LDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDGRDLASlSRRELARRIAYVPQEpPAPFG-LTVREl 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779783 652 -------HLHFycvikgipLQNQSRE----TNRMLTSFGLLQQSNTMSKDLSGGMKRKLSIIIALIGDTKVVILDEPTSG 720
Cdd:COG1120 96 valgrypHLGL--------FGRPSAEdreaVEEALERTGLEHLADRPVDELSGGERQRVLIARALAQEPPLLLLDEPTSH 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779783 721 MDPVSRRATWDLLQHYKKD--RTILLTTHHMDEADVLGDRIAILVMGILKCCGS--SLF----LKKLYGVgyHLVIVKTP 792
Cdd:COG1120 168 LDLAHQLEVLELLRRLARErgRTVVMVLHDLNLAARYADRLVLLKDGRIVAQGPpeEVLtpelLEEVYGV--EARVIEDP 245
|
...
gi 1039779783 793 DSN 795
Cdd:COG1120 246 VTG 248
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
556-762 |
3.16e-26 |
|
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: 108.42 E-value: 3.16e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779783 556 IRIQHLYKEFilkNSTLMAVNDLSLNLYEGQITVLLGHNGAGKTTTLSILTGLYLPTRGKVYISGYDISS----DMVQIR 631
Cdd:cd03256 1 IEVENLSKTY---PNGKKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGTDINKlkgkALRQLR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779783 632 KSLGLCPQDDLLFPMLTVSE--------HLHFYCVIKGIPLQNQSRETNRMLTSFGLLQQSNTMSKDLSGGMKRKLSIII 703
Cdd:cd03256 78 RQIGMIFQQFNLIERLSVLEnvlsgrlgRRSTWRSLFGLFPKEEKQRALAALERVGLLDKAYQRADQLSGGQQQRVAIAR 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1039779783 704 ALIGDTKVVILDEPTSGMDPVSRRATWDLLQ--HYKKDRTILLTTHHMDEADVLGDRIAIL 762
Cdd:cd03256 158 ALMQQPKLILADEPVASLDPASSRQVMDLLKriNREEGITVIVSLHQVDLAREYADRIVGL 218
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
556-762 |
5.03e-26 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 109.12 E-value: 5.03e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779783 556 IRIQHLykEFILKNSTLMAVNDLSLNLYEGQITVLLGHNGAGKTTTLSILTGLYLP---TRGKVYISGYDISSDMV-QIR 631
Cdd:PRK13640 6 VEFKHV--SFTYPDSKKPALNDISFSIPRGSWTALIGHNGSGKSTISKLINGLLLPddnPNSKITVDGITLTAKTVwDIR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779783 632 KSLGLCPQD-DLLFPMLTVSEHLHFYCVIKGIPLQNQSRETNRMLTSFGLLQQSNTMSKDLSGGMKRKLSIIIALIGDTK 710
Cdd:PRK13640 84 EKVGIVFQNpDNQFVGATVGDDVAFGLENRAVPRPEMIKIVRDVLADVGMLDYIDSEPANLSGGQKQRVAIAGILAVEPK 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1039779783 711 VVILDEPTSGMDPVSRRATWDLLQHYKKDR--TILLTTHHMDEAdVLGDRIAIL 762
Cdd:PRK13640 164 IIILDESTSMLDPAGKEQILKLIRKLKKKNnlTVISITHDIDEA-NMADQVLVL 216
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
575-762 |
8.30e-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: 105.21 E-value: 8.30e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779783 575 VNDLSLNLYEGQITVLLGHNGAGKTTTLSILTGLYLPTRGKVYISGYDISS-DMVQIRKSLGLCPQddllfpmltvsehl 653
Cdd:cd03214 15 LDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDGKDLASlSPKELARKIAYVPQ-------------- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779783 654 hfycvikgiplqnqsretnrMLTSFGLLQQSNTMSKDLSGGMKRKLSIIIALIGDTKVVILDEPTSGMDPVSRRATWDLL 733
Cdd:cd03214 81 --------------------ALELLGLAHLADRPFNELSGGERQRVLLARALAQEPPILLLDEPTSHLDIAHQIELLELL 140
|
170 180 190
....*....|....*....|....*....|.
gi 1039779783 734 QHYKKDR--TILLTTHHMDEADVLGDRIAIL 762
Cdd:cd03214 141 RRLARERgkTVVMVLHDLNLAARYADRVILL 171
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
574-772 |
2.23e-25 |
|
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: 112.16 E-value: 2.23e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779783 574 AVNDLSLNLYEGQITVLLGHNGAGKTTTLSILTGLYLPTRGKVYISGYDISS-DMVQIRKSLGLCPQDDLLFPMlTVSEH 652
Cdd:COG4988 352 ALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPPYSGSILINGVDLSDlDPASWRRQIAWVPQNPYLFAG-TIREN 430
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779783 653 LHFYCvikgiP------LQNQSRETNrmLTSF--GLLQQSNTM----SKDLSGGMKRKLSIIIALIGDTKVVILDEPTSG 720
Cdd:COG4988 431 LRLGR-----PdasdeeLEAALEAAG--LDEFvaALPDGLDTPlgegGRGLSGGQAQRLALARALLRDAPLLLLDEPTAH 503
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1039779783 721 MDPVSRRATWDLLQHYKKDRTILLTTHHMDEAdVLGDRiaILVM--GILKCCGS 772
Cdd:COG4988 504 LDAETEAEILQALRRLAKGRTVILITHRLALL-AQADR--ILVLddGRIVEQGT 554
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
556-764 |
4.45e-25 |
|
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: 107.45 E-value: 4.45e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779783 556 IRIQHLYKEFILKNSTLMAVNDLSLNLYEGQITVLLGHNGAGKTTTLSILTGLYLP---TRGKVYISGYDISS----DMV 628
Cdd:COG0444 2 LEVRNLKVYFPTRRGVVKAVDGVSFDVRRGETLGLVGESGSGKSTLARAILGLLPPpgiTSGEILFDGEDLLKlsekELR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779783 629 QIR-KSLGLCPQDDL--LFPMLTVSEHL------HfycviKGIPLQNQSRETNRMLTSFGLLQQSNTMSK---DLSGGMK 696
Cdd:COG0444 82 KIRgREIQMIFQDPMtsLNPVMTVGDQIaeplriH-----GGLSKAEARERAIELLERVGLPDPERRLDRyphELSGGMR 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779783 697 RKLSIIIALIGDTKVVILDEPTSGMDPVSRRATWDLLQHYKKDR--TILLTTHHMDEADVLGDRIAilVM 764
Cdd:COG0444 157 QRVMIARALALEPKLLIADEPTTALDVTIQAQILNLLKDLQRELglAILFITHDLGVVAEIADRVA--VM 224
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
574-768 |
5.15e-25 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 105.93 E-value: 5.15e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779783 574 AVNDLSLNLYEGQITVLLGHNGAGKTTTLSILTGLYLPTRGKVYISGYDISSD---MVQIRKSLGLCPQ--DDLLF-Pml 647
Cdd:PRK13639 17 ALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIKGEPIKYDkksLLEVRKTVGIVFQnpDDQLFaP-- 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779783 648 TVSEHLHFYCVIKGIPLQNQSRETNRMLTSFGLLQQSNTMSKDLSGGMKRKLSIIIALIGDTKVVILDEPTSGMDPVSRR 727
Cdd:PRK13639 95 TVEEDVAFGPLNLGLSKEEVEKRVKEALKAVGMEGFENKPPHHLSGGQKKRVAIAGILAMKPEIIVLDEPTSGLDPMGAS 174
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1039779783 728 ATWDLLQHY-KKDRTILLTTHHMDEADVLGDRIAILVMG-ILK 768
Cdd:PRK13639 175 QIMKLLYDLnKEGITIIISTHDVDLVPVYADKVYVMSDGkIIK 217
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
556-765 |
5.97e-25 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 105.97 E-value: 5.97e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779783 556 IRIQHLYkeFILKNSTlMAVNDLSLNLYEGQITVLLGHNGAGKTTTLSILTGLYLPTRGKVYISGYDISSDMVQ-IRKSL 634
Cdd:PRK13647 5 IEVEDLH--FRYKDGT-KALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGREVNAENEKwVRSKV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779783 635 GLCPQ--DDLLFPMlTVSEHLHFYCVIKGIPLQNQSRETNRMLTSFGLLQQSNTMSKDLSGGMKRKLSIIIALIGDTKVV 712
Cdd:PRK13647 82 GLVFQdpDDQVFSS-TVWDDVAFGPVNMGLDKDEVERRVEEALKAVRMWDFRDKPPYHLSYGQKKRVAIAGVLAMDPDVI 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1039779783 713 ILDEPTSGMDPVSRRATWDLLQH-YKKDRTILLTTHHMDEADVLGDRIAILVMG 765
Cdd:PRK13647 161 VLDEPMAYLDPRGQETLMEILDRlHNQGKTVIVATHDVDLAAEWADQVIVLKEG 214
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
556-762 |
7.77e-25 |
|
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: 102.12 E-value: 7.77e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779783 556 IRIQHLYKEFilknSTLMAVNDLSLNLYEGQITVLLGHNGAGKTTTLSILTGLYLPTRGKVYISGYDISSdmvqirkslg 635
Cdd:cd03216 1 LELRGITKRF----GGVKALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVDGKEVSF---------- 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779783 636 LCPQDdllfpmltvSEHLhfycvikGIplqnqsretnrmltsfGLLQQsntmskdLSGGMKRKLSIIIALIGDTKVVILD 715
Cdd:cd03216 67 ASPRD---------ARRA-------GI----------------AMVYQ-------LSVGERQMVEIARALARNARLLILD 107
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1039779783 716 EPTSGMDPVSRRATWDLLQHYKKD-RTILLTTHHMDEADVLGDRIAIL 762
Cdd:cd03216 108 EPTAALTPAEVERLFKVIRRLRAQgVAVIFISHRLDEVFEIADRVTVL 155
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
575-751 |
8.69e-25 |
|
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: 104.78 E-value: 8.69e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779783 575 VNDLSLNLYEGQITVLLGHNGAGKTTTLSILTGLYLPTRGK-VYISGYDI-SSDMVQIRKSLGLcpqddllfpmltVSEH 652
Cdd:COG1119 19 LDDISWTVKPGEHWAILGPNGAGKSTLLSLITGDLPPTYGNdVRLFGERRgGEDVWELRKRIGL------------VSPA 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779783 653 LH----------------FYCVIkGI---PLQNQSRETNRMLTSFGLLQQSNTMSKDLSGGMKRKLSIIIALIGDTKVVI 713
Cdd:COG1119 87 LQlrfprdetvldvvlsgFFDSI-GLyrePTDEQRERARELLELLGLAHLADRPFGTLSQGEQRRVLIARALVKDPELLI 165
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1039779783 714 LDEPTSGMDPVSRRATWDLLQHY--KKDRTILLTTHHMDE 751
Cdd:COG1119 166 LDEPTAGLDLGARELLLALLDKLaaEGAPTLVLVTHHVEE 205
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
574-760 |
5.83e-24 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 109.06 E-value: 5.83e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779783 574 AVNDLSLNLYEGQITVLLGHNGAGKTTTLSILTGLYLPTRGKVYISGYDI-SSDMvQIRKSLGLCPQDDLLFPMLTVSE- 651
Cdd:NF033858 281 AVDHVSFRIRRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGEAWLFGQPVdAGDI-ATRRRVGYMSQAFSLYGELTVRQn 359
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779783 652 ---HLHFYcvikGIPLQNQSRETNRMLTSFGLLQQSNTMSKDLSGGMKRKLSIIIALIGDTKVVILDEPTSGMDPVSRRA 728
Cdd:NF033858 360 lelHARLF----HLPAAEIAARVAEMLERFDLADVADALPDSLPLGIRQRLSLAVAVIHKPELLILDEPTSGVDPVARDM 435
|
170 180 190
....*....|....*....|....*....|....
gi 1039779783 729 TWDLLQHY-KKDR-TILLTTHHMDEADvLGDRIA 760
Cdd:NF033858 436 FWRLLIELsREDGvTIFISTHFMNEAE-RCDRIS 468
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
556-759 |
9.17e-24 |
|
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: 100.68 E-value: 9.17e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779783 556 IRIQHLYKEFilknSTLMAVNDLSLNLYEGQITVLLGHNGAGKTTTLSILTGLYLPTRGKVYISGYDI---SSDMVQIRK 632
Cdd:cd03262 1 IEIKNLHKSF----GDFHVLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIDGLKLtddKKNINELRQ 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779783 633 SLGLCPQDDLLFPMLTVSEHLHFYCV-IKGIPLQNQSRETNRMLTSFGLLQQSNTMSKDLSGGMKRKLSIIIALIGDTKV 711
Cdd:cd03262 77 KVGMVFQQFNLFPHLTVLENITLAPIkVKGMSKAEAEERALELLEKVGLADKADAYPAQLSGGQQQRVAIARALAMNPKV 156
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1039779783 712 VILDEPTSGMDPVSRRATWDLLQHYKKD-RTILLTTHHMDEADVLGDRI 759
Cdd:cd03262 157 MLFDEPTSALDPELVGEVLDVMKDLAEEgMTMVVVTHEMGFAREVADRV 205
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
555-772 |
9.46e-24 |
|
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: 101.26 E-value: 9.46e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779783 555 GIRIQHLYKEFilknSTLMAVNDLSLNLYEGQITVLLGHNGAGKTTTLSILTGLYLPTRGKVYISGYDISSDMVQIRKsL 634
Cdd:cd03296 2 SIEVRNVSKRF----GDFVALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGGEDATDVPVQERN-V 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779783 635 GLCPQDDLLFPMLTVSEHLHFYCVIKGI----PLQNQSRETNRMLTSFGLLQQSNTMSKDLSGGMKRKLSIIIALIGDTK 710
Cdd:cd03296 77 GFVFQHYALFRHMTVFDNVAFGLRVKPRserpPEAEIRAKVHELLKLVQLDWLADRYPAQLSGGQRQRVALARALAVEPK 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1039779783 711 VVILDEPTSGMDPVSRRA--TWDLLQHYKKDRTILLTTHHMDEADVLGDRIAILVMGILKCCGS 772
Cdd:cd03296 157 VLLLDEPFGALDAKVRKElrRWLRRLHDELHVTTVFVTHDQEEALEVADRVVVMNKGRIEQVGT 220
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
556-764 |
1.53e-23 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 101.63 E-value: 1.53e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779783 556 IRIQHLYkeFILKNSTLMAVNDLSLNLYEGQITVLLGHNGAGKTTTLSILTGLYLPTRGKVYISGYDISSDMV-QIRKSL 634
Cdd:PRK13635 6 IRVEHIS--FRYPDAATYALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGGMVLSEETVwDVRRQV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779783 635 GLCPQD-DLLFPMLTVSEHLHFYCVIKGIPLQNQSRETNRMLTSFGLLQQSNTMSKDLSGGMKRKLSI--IIALIGDtkV 711
Cdd:PRK13635 84 GMVFQNpDNQFVGATVQDDVAFGLENIGVPREEMVERVDQALRQVGMEDFLNREPHRLSGGQKQRVAIagVLALQPD--I 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1039779783 712 VILDEPTSGMDPVSRRATWDLLQHYKKDR--TILLTTHHMDEAdVLGDRiaILVM 764
Cdd:PRK13635 162 IILDEATSMLDPRGRREVLETVRQLKEQKgiTVLSITHDLDEA-AQADR--VIVM 213
|
|
| COG4674 |
COG4674 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
574-772 |
1.92e-23 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443710 [Multi-domain] Cd Length: 250 Bit Score: 100.58 E-value: 1.92e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779783 574 AVNDLSLNLYEGQITVLLGHNGAGKTTTLSILTGLYLPTRGKVYISGYDISS-DMVQI------RKSlglcpQDDLLFPM 646
Cdd:COG4674 25 ALNDLSLYVDPGELRVIIGPNGAGKTTLMDVITGKTRPDSGSVLFGGTDLTGlDEHEIarlgigRKF-----QKPTVFEE 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779783 647 LTVSEHL--------HFYCVIKGIPLQNQSRETNRMLTSFGLLQQSNTMSKDLSGGMKRKLSIIIALIGDTKVVILDEPT 718
Cdd:COG4674 100 LTVFENLelalkgdrGVFASLFARLTAEERDRIEEVLETIGLTDKADRLAGLLSHGQKQWLEIGMLLAQDPKLLLLDEPV 179
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1039779783 719 SGMDPVSRRATWDLLQHYKKDRTILLTTHHMDEADVLGDRIAILVMGILKCCGS 772
Cdd:COG4674 180 AGMTDAETERTAELLKSLAGKHSVVVVEHDMEFVRQIARKVTVLHQGSVLAEGS 233
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
575-765 |
3.74e-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: 99.46 E-value: 3.74e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779783 575 VNDLSLNLYEGQITVLLGHNGAGKTTTLSILTGLYLPTRGKVYISGYDISSD----MVQIrkslglcpQDDLLFPMLTVS 650
Cdd:TIGR01184 1 LKGVNLTIQQGEFISLIGHSGCGKSTLLNLISGLAQPTSGGVILEGKQITEPgpdrMVVF--------QNYSLLPWLTVR 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779783 651 EH--LHFYCVIKGIPLQNQSRETNRMLTSFGLLQQSNTMSKDLSGGMKRKLSIIIALIGDTKVVILDEPTSGMDPVSRRA 728
Cdd:TIGR01184 73 ENiaLAVDRVLPDLSKSERRAIVEEHIALVGLTEAADKRPGQLSGGMKQRVAIARALSIRPKVLLLDEPFGALDALTRGN 152
|
170 180 190
....*....|....*....|....*....|....*....
gi 1039779783 729 TWD-LLQHYKKDR-TILLTTHHMDEADVLGDRIAILVMG 765
Cdd:TIGR01184 153 LQEeLMQIWEEHRvTVLMVTHDVDEALLLSDRVVMLTNG 191
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
554-764 |
4.12e-23 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 99.94 E-value: 4.12e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779783 554 AGIRIQHLYKEFILKNSTLMAVNDLSLNLYEGQITVLLGHNGAGKTTTLSILTGLYLPTRGKVYISGYDI---SSDmvqi 630
Cdd:COG4525 2 SMLTVRHVSVRYPGGGQPQPALQDVSLTIESGEFVVALGASGCGKTTLLNLIAGFLAPSSGEITLDGVPVtgpGAD---- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779783 631 RkslGLCPQDDLLFPMLTVSEHLHFYCVIKGIPLQNQSRETNRMLTSFGLLQQSNTMSKDLSGGMKRKLSIIIALIGDTK 710
Cdd:COG4525 78 R---GVVFQKDALLPWLNVLDNVAFGLRLRGVPKAERRARAEELLALVGLADFARRRIWQLSGGMRQRVGIARALAADPR 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1039779783 711 VVILDEPTSGMDPVSRRATWDLLQHYKKD--RTILLTTHHMDEADVLGDRiaILVM 764
Cdd:COG4525 155 FLLMDEPFGALDALTREQMQELLLDVWQRtgKGVFLITHSVEEALFLATR--LVVM 208
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
556-762 |
4.86e-23 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 104.34 E-value: 4.86e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779783 556 IRIQHLYKEFilknSTLMAVNDLSLNLYEGQITVLLGHNGAGKTTTLSILTGLYLPTRGKVYISG--YDISSDMVQIRKS 633
Cdd:COG3845 6 LELRGITKRF----GGVVANDDVSLTVRPGEIHALLGENGAGKSTLMKILYGLYQPDSGEILIDGkpVRIRSPRDAIALG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779783 634 LGLCPQDDLLFPMLTVSEHLHFYCVIKGIPLQNQSRETNRMLT---SFGLLQQSNTMSKDLSGGMKRKLSIIIALIGDTK 710
Cdd:COG3845 82 IGMVHQHFMLVPNLTVAENIVLGLEPTKGGRLDRKAARARIRElseRYGLDVDPDAKVEDLSVGEQQRVEILKALYRGAR 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1039779783 711 VVILDEPTSGMDPVSRRATWDLLQHYKKD-RTILLTTHHMDEADVLGDRIAIL 762
Cdd:COG3845 162 ILILDEPTAVLTPQEADELFEILRRLAAEgKSIIFITHKLREVMAIADRVTVL 214
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
574-764 |
5.13e-23 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 100.16 E-value: 5.13e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779783 574 AVNDLSLNLYEGQITVLLGHNGAGKTTTLSILTGLYLPTRGKVYISGYDIS--SDMVQIRKSLGLCPQ--DDLLFPMLtV 649
Cdd:PRK13633 25 ALDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVYVDGLDTSdeENLWDIRNKAGMVFQnpDNQIVATI-V 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779783 650 SEHLHFYCVIKGIPLQNQSRETNRMLTSFGLLQQSNTMSKDLSGGMKRKLSIIIALIGDTKVVILDEPTSGMDPVSRRAT 729
Cdd:PRK13633 104 EEDVAFGPENLGIPPEEIRERVDESLKKVGMYEYRRHAPHLLSGGQKQRVAIAGILAMRPECIIFDEPTAMLDPSGRREV 183
|
170 180 190
....*....|....*....|....*....|....*..
gi 1039779783 730 WDLLQHYKKDR--TILLTTHHMDEAdVLGDRiaILVM 764
Cdd:PRK13633 184 VNTIKELNKKYgiTIILITHYMEEA-VEADR--IIVM 217
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
554-762 |
6.71e-23 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 101.69 E-value: 6.71e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779783 554 AGIRIQHLYKEFilknSTLMAVNDLSLNLYEGQITVLLGHNGAGKTTTLSILTGLYLPTRGKVYISGYDISSDMVQIRkS 633
Cdd:COG3839 2 ASLELENVSKSY----GGVEALKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAGLEDPTSGEILIGGRDVTDLPPKDR-N 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779783 634 LGLCPQDDLLFPMLTVSEHLHFYCVIKGIPLQNQSRETNRMLTSFGLLQQSNTMSKDLSGGMKRKLSIIIALIGDTKVVI 713
Cdd:COG3839 77 IAMVFQSYALYPHMTVYENIAFPLKLRKVPKAEIDRRVREAAELLGLEDLLDRKPKQLSGGQRQRVALGRALVREPKVFL 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1039779783 714 LDEPTSGMDPVSRRATWDLLQ--HYKKDRTILLTTHHMDEADVLGDRIAIL 762
Cdd:COG3839 157 LDEPLSNLDAKLRVEMRAEIKrlHRRLGTTTIYVTHDQVEAMTLADRIAVM 207
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
556-749 |
7.13e-23 |
|
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome bd biogenesis. The CydC and CydD proteins are important for the formation of cytochrome bd terminal oxidase of E. coli and it has been proposed that they were necessary for biosynthesis of the cytochrome bd quinol oxidase and for periplasmic c-type cytochromes. CydCD were proposed to determine a heterooligomeric complex important for heme export into the periplasm or to be involved in the maintenance of the proper redox state of the periplasmic space. In Bacillus subtilis, the absence of CydCD does not affect the presence of halo-cytochrome c in the membrane and this observation suggests that CydCD proteins are not involved in the export of heme in this organism.
Pssm-ID: 213214 [Multi-domain] Cd Length: 178 Bit Score: 97.00 E-value: 7.13e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779783 556 IRIQHLykEFILKNSTLMAVNDLSLNLYEGQITVLLGHNGAGKTTTLSILTGLYLPTRGKVYISGYDISSDMVQIRKSLG 635
Cdd:cd03247 1 LSINNV--SFSYPEQEQQVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDGVPVSDLEKALSSLIS 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779783 636 LCPQDDLLFPmltvsehlhfycvikgiplqnqsretnrmlTSFGllqqsNTMSKDLSGGMKRKLSIIIALIGDTKVVILD 715
Cdd:cd03247 79 VLNQRPYLFD------------------------------TTLR-----NNLGRRFSGGERQRLALARILLQDAPIVLLD 123
|
170 180 190
....*....|....*....|....*....|....
gi 1039779783 716 EPTSGMDPVSRRATWDLLQHYKKDRTILLTTHHM 749
Cdd:cd03247 124 EPTVGLDPITERQLLSLIFEVLKDKTLIWITHHL 157
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
575-772 |
1.05e-22 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 98.43 E-value: 1.05e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779783 575 VNDLSLNLYEGQITVLLGHNGAGKTTTLSILTGLYLPTRGKVYISGYDIS--SDMVQIRKSLGLCPQDDLLFPMLTVSEH 652
Cdd:PRK10895 19 VEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEDISllPLHARARRGIGYLPQEASIFRRLSVYDN 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779783 653 LHFYCVI-KGIPLQNQSRETNRMLTSFGLLQQSNTMSKDLSGGMKRKLSIIIALIGDTKVVILDEPTSGMDPVSRRATWD 731
Cdd:PRK10895 99 LMAVLQIrDDLSAEQREDRANELMEEFHIEHLRDSMGQSLSGGERRRVEIARALAANPKFILLDEPFAGVDPISVIDIKR 178
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1039779783 732 LLQHYKKDRT-ILLTTHHMDEADVLGDRIAILVMGILKCCGS 772
Cdd:PRK10895 179 IIEHLRDSGLgVLITDHNVRETLAVCERAYIVSQGHLIAHGT 220
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
574-769 |
1.05e-22 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 99.74 E-value: 1.05e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779783 574 AVNDLSLNLYEGQITVLLGHNGAGKTTTLSILTGLYLPTRGKVYISGYDISSDMVQ---IRKSLGLCPQ--DDLLFPMlT 648
Cdd:PRK13637 22 ALDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDGVDITDKKVKlsdIRKKVGLVFQypEYQLFEE-T 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779783 649 VSEHLHFYCVIKGIplqNQSRETNRMLTSFGLLQQSNTMSKD-----LSGGMKRKLSI--IIALigDTKVVILDEPTSGM 721
Cdd:PRK13637 101 IEKDIAFGPINLGL---SEEEIENRVKRAMNIVGLDYEDYKDkspfeLSGGQKRRVAIagVVAM--EPKILILDEPTAGL 175
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1039779783 722 DPVSRRATWDLLQ--HYKKDRTILLTTHHMDEADVLGDRiaILVMGILKC 769
Cdd:PRK13637 176 DPKGRDEILNKIKelHKEYNMTIILVSHSMEDVAKLADR--IIVMNKGKC 223
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
574-786 |
1.20e-22 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 99.47 E-value: 1.20e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779783 574 AVNDLSLNLYEGQITVLLGHNGAGKTTTLSILTGLYLPTRGKVYISGYDISSD-----MVQIRKSLGLCPQ--DDLLFPM 646
Cdd:PRK13646 22 AIHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVDDITITHKtkdkyIRPVRKRIGMVFQfpESQLFED 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779783 647 lTVSEHLHFYCVIKGIPLQNQSRETNRMLTSFGLlqQSNTMSKD---LSGGMKRKLSIIIALIGDTKVVILDEPTSGMDP 723
Cdd:PRK13646 102 -TVEREIIFGPKNFKMNLDEVKNYAHRLLMDLGF--SRDVMSQSpfqMSGGQMRKIAIVSILAMNPDIIVLDEPTAGLDP 178
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1039779783 724 VSRRATWDLLQHY--KKDRTILLTTHHMDEADVLGDRIAILVMG--ILKCCGSSLFLKKLYGVGYHL 786
Cdd:PRK13646 179 QSKRQVMRLLKSLqtDENKTIILVSHDMNEVARYADEVIVMKEGsiVSQTSPKELFKDKKKLADWHI 245
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
574-749 |
1.30e-22 |
|
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan exporter ATP-binding protein. In A. tumefaciens cyclic beta-1, 2-glucan must be transported into the periplasmic space to exert its action as a virulence factor. This subfamily belongs to the MRP-like family and is involved in drug, peptide, and lipid export. The MRP-like family, similar to all ABC proteins, have a common four-domain core structure constituted by two membrane-spanning domains each composed of six transmembrane (TM) helices and two nucleotide-binding domains (NBD). ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213221 [Multi-domain] Cd Length: 229 Bit Score: 97.68 E-value: 1.30e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779783 574 AVNDLSLNLYEGQITVLLGHNGAGKTTTLSILTGLYLPTRGKVYISGYDISS-DMVQIRKSLGLCPQDDLLFPMlTVSEH 652
Cdd:cd03254 18 VLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGIDIRDiSRKSLRSMIGVVLQDTFLFSG-TIMEN 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779783 653 LHFycvikgiplqnqSRETNRM-----------LTSF------GLLQQSNTMSKDLSGGMKRKLSIIIALIGDTKVVILD 715
Cdd:cd03254 97 IRL------------GRPNATDeevieaakeagAHDFimklpnGYDTVLGENGGNLSQGERQLLAIARAMLRDPKILILD 164
|
170 180 190
....*....|....*....|....*....|....
gi 1039779783 716 EPTSGMDPVSRRATWDLLQHYKKDRTILLTTHHM 749
Cdd:cd03254 165 EATSNIDTETEKLIQEALEKLMKGRTSIIIAHRL 198
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
574-793 |
1.32e-22 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 99.15 E-value: 1.32e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779783 574 AVNDLSLNLYEGQITVLLGHNGAGKTTTLSILTGLYLPTRGKVYISGYDI---SSDMVQIRKSLGLCPQ--DDLLFPMlT 648
Cdd:PRK13636 21 ALKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGKPIdysRKGLMKLRESVGMVFQdpDNQLFSA-S 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779783 649 VSEHLHFYCVIKGIPLQNQSRETNRMLTSFGLLQQSNTMSKDLSGGMKRKLSIIIALIGDTKVVILDEPTSGMDPVSRRA 728
Cdd:PRK13636 100 VYQDVSFGAVNLKLPEDEVRKRVDNALKRTGIEHLKDKPTHCLSFGQKKRVAIAGVLVMEPKVLVLDEPTAGLDPMGVSE 179
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1039779783 729 TWDLLQHYKK--DRTILLTTHHMDEADVLGDRIAILVMG--ILKCCGSSLFLKK---------LYGVGYHLVIVKTPD 793
Cdd:PRK13636 180 IMKLLVEMQKelGLTIIIATHDIDIVPLYCDNVFVMKEGrvILQGNPKEVFAEKemlrkvnlrLPRIGHLMEILKEKD 257
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
574-765 |
1.40e-22 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 98.67 E-value: 1.40e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779783 574 AVNDLSLNLYEGQITVLLGHNGAGKTTTLSILTGLYLPTRGKVYISGYDISSDMVQ-IRKSLGLCPQD-DLLFPMLTVSE 651
Cdd:PRK13648 24 TLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIFYNNQAITDDNFEkLRKHIGIVFQNpDNQFVGSIVKY 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779783 652 HLHFYCVIKGIPLQNQSRETNRMLTSFGLLQQSNTMSKDLSGGMKRKLSIIIALIGDTKVVILDEPTSGMDPVSRRATWD 731
Cdd:PRK13648 104 DVAFGLENHAVPYDEMHRRVSEALKQVDMLERADYEPNALSGGQKQRVAIAGVLALNPSVIILDEATSMLDPDARQNLLD 183
|
170 180 190
....*....|....*....|....*....|....*.
gi 1039779783 732 LLQHYK--KDRTILLTTHHMDEAdVLGDRIAILVMG 765
Cdd:PRK13648 184 LVRKVKseHNITIISITHDLSEA-MEADHVIVMNKG 218
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
577-767 |
1.74e-22 |
|
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: 96.98 E-value: 1.74e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779783 577 DLSLNL---YEGQITVLLGHNGAGKTTTLSILTGLYLPTRGKVYISG---YDISSDM---VQIRKsLGLCPQDDLLFPML 647
Cdd:cd03297 12 DFTLKIdfdLNEEVTGIFGASGAGKSTLLRCIAGLEKPDGGTIVLNGtvlFDSRKKInlpPQQRK-IGLVFQQYALFPHL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779783 648 TVSEHLHF-YCVIKGIPLQNQSREtnrMLTSFGLLQQSNTMSKDLSGGMKRKLSIIIALIGDTKVVILDEPTSGMDPVSR 726
Cdd:cd03297 91 NVRENLAFgLKRKRNREDRISVDE---LLDLLGLDHLLNRYPAQLSGGEKQRVALARALAAQPELLLLDEPFSALDRALR 167
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1039779783 727 RATWDLLQHYKKDRTI--LLTTHHMDEADVLGDRIAILVMGIL 767
Cdd:cd03297 168 LQLLPELKQIKKNLNIpvIFVTHDLSEAEYLADRIVVMEDGRL 210
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
574-772 |
2.28e-22 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 98.55 E-value: 2.28e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779783 574 AVNDLSLNLYEGQITVLLGHNGAGKTTTLSILTGLYLPTRGKVYISGYDISS-----DMVQIRKSLGLCPQddllFPmlt 648
Cdd:PRK13634 22 ALYDVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVTIGERVITAgkknkKLKPLRKKVGIVFQ----FP--- 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779783 649 vsEHLHF-YCVIK---------GIPLQNQSRETNRMLTSFGLLQQSNTMSK-DLSGGMKRKLSIIIALIGDTKVVILDEP 717
Cdd:PRK13634 95 --EHQLFeETVEKdicfgpmnfGVSEEDAKQKAREMIELVGLPEELLARSPfELSGGQMRRVAIAGVLAMEPEVLVLDEP 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1039779783 718 TSGMDPVSRRATWDLLQ--HYKKDRTILLTTHHMDEADVLGDRIAILVMGILKCCGS 772
Cdd:PRK13634 173 TAGLDPKGRKEMMEMFYklHKEKGLTTVLVTHSMEDAARYADQIVVMHKGTVFLQGT 229
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
574-772 |
2.98e-22 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 97.89 E-value: 2.98e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779783 574 AVNDLSLNLYEGQITVLLGHNGAGKTTTLSILTGLYLPTRGKVYISGYDISS-----DMVQIRKSLGLCPQddllFPMLT 648
Cdd:PRK13649 22 ALFDVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDDTLITStsknkDIKQIRKKVGLVFQ----FPESQ 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779783 649 VSEHlhfyCVIKGIPLQNQ------------SRETNRML-TSFGLLQQSntmSKDLSGGMKRKLSIIIALIGDTKVVILD 715
Cdd:PRK13649 98 LFEE----TVLKDVAFGPQnfgvsqeeaealAREKLALVgISESLFEKN---PFELSGGQMRRVAIAGILAMEPKILVLD 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1039779783 716 EPTSGMDPVSRRATWDLLQH-YKKDRTILLTTHHMDEADVLGDRIAILVMGILKCCGS 772
Cdd:PRK13649 171 EPTAGLDPKGRKELMTLFKKlHQSGMTIVLVTHLMDDVANYADFVYVLEKGKLVLSGK 228
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
574-773 |
3.98e-22 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 97.15 E-value: 3.98e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779783 574 AVNDLSLNLYEGQITVLLGHNGAGKTTTLSILT--GLYLP---TRGKVYISGYDISS---DMVQIRKSLGLCPQDDLLFP 645
Cdd:PRK14239 20 ALNSVSLDFYPNEITALIGPSGSGKSTLLRSINrmNDLNPevtITGSIVYNGHNIYSprtDTVDLRKEIGMVFQQPNPFP 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779783 646 MlTVSEHLHFYCVIKGIplQNQSRETNRMLTSfglLQQSNTMS--KD--------LSGGMKRKLSIIIALIGDTKVVILD 715
Cdd:PRK14239 100 M-SIYENVVYGLRLKGI--KDKQVLDEAVEKS---LKGASIWDevKDrlhdsalgLSGGQQQRVCIARVLATSPKIILLD 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1039779783 716 EPTSGMDPVSRRATWDLLQHYKKDRTILLTTHHMDEADVLGDRIAILVMGILKCCGSS 773
Cdd:PRK14239 174 EPTSALDPISAGKIEETLLGLKDDYTMLLVTRSMQQASRISDRTGFFLDGDLIEYNDT 231
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
574-762 |
4.46e-22 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 101.25 E-value: 4.46e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779783 574 AVNDLSLNLYEGQITVLLGHNGAGKTTTLSILTGLYLPTRGKVYISG--YDISSDMVQIRKSLGLCPQDDLLFPMLTVSE 651
Cdd:COG1129 19 ALDGVSLELRPGEVHALLGENGAGKSTLMKILSGVYQPDSGEILLDGepVRFRSPRDAQAAGIAIIHQELNLVPNLSVAE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779783 652 HLHFYCVIKGIPLQNQS---RETNRMLTSFGLLQQSNTMSKDLSGGMKRKLSIIIALIGDTKVVILDEPTSGMDPVSRRA 728
Cdd:COG1129 99 NIFLGREPRRGGLIDWRamrRRARELLARLGLDIDPDTPVGDLSVAQQQLVEIARALSRDARVLILDEPTASLTEREVER 178
|
170 180 190
....*....|....*....|....*....|....*
gi 1039779783 729 TWDLLQHYKKD-RTILLTTHHMDEADVLGDRIAIL 762
Cdd:COG1129 179 LFRIIRRLKAQgVAIIYISHRLDEVFEIADRVTVL 213
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
556-762 |
1.29e-21 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 97.46 E-value: 1.29e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779783 556 IRIQHLYKEFILKNSTLMAVNDLSLNLYEGQITVLLGHNGAGKTTTLSILTGLYLPTRGKVYISGYDISS----DMVQIR 631
Cdd:COG1135 2 IELENLSKTFPTKGGPVTALDDVSLTIEKGEIFGIIGYSGAGKSTLIRCINLLERPTSGSVLVDGVDLTAlserELRAAR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779783 632 KSLGLCPQDDLLFPMLTVSEHLHFYCVIKGIPLQNQSRETNRMLTSFGLLQQSNTMSKDLSGGMKRKLSIIIALIGDTKV 711
Cdd:COG1135 82 RKIGMIFQHFNLLSSRTVAENVALPLEIAGVPKAEIRKRVAELLELVGLSDKADAYPSQLSGGQKQRVGIARALANNPKV 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1039779783 712 VILDEPTSGMDPVSRRATWDLLQHYKKDR--TILLTTHHMdeaDV---LGDRIAIL 762
Cdd:COG1135 162 LLCDEATSALDPETTRSILDLLKDINRELglTIVLITHEM---DVvrrICDRVAVL 214
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
577-765 |
1.59e-21 |
|
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: 94.10 E-value: 1.59e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779783 577 DLSLNLYEGQITVLLGHNGAGKTTTLSILTGLYLPTRGKVYISGYDISSdMVQIRKSLGLCPQDDLLFPMLTVSEHLHFy 656
Cdd:cd03298 16 HFDLTFAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLINGVDVTA-APPADRPVSMLFQENNLFAHLTVEQNVGL- 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779783 657 CVIKGIPLQNQSRET-NRMLTSFGLLQQSNTMSKDLSGGMKRKLSIIIALIGDTKVVILDEPTSGMDPVSRRATWDLLQ- 734
Cdd:cd03298 94 GLSPGLKLTAEDRQAiEVALARVGLAGLEKRLPGELSGGERQRVALARVLVRDKPVLLLDEPFAALDPALRAEMLDLVLd 173
|
170 180 190
....*....|....*....|....*....|..
gi 1039779783 735 -HYKKDRTILLTTHHMDEADVLGDRIAILVMG 765
Cdd:cd03298 174 lHAETKMTVLMVTHQPEDAKRLAQRVVFLDNG 205
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
575-762 |
2.37e-21 |
|
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: 92.28 E-value: 2.37e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779783 575 VNDLSLNLYEGQITVLLGHNGAGKTTTLSILTGLYLPTRGKVYISGYDISS-DMVQIRKSLGLCPQDDLLFPMlTVSEHL 653
Cdd:cd03246 18 LRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDGADISQwDPNELGDHVGYLPQDDELFSG-SIAENI 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779783 654 hfycvikgiplqnqsretnrmltsfgllqqsntmskdLSGGMKRKLSIIIALIGDTKVVILDEPTSGMDPVSRRATWDLL 733
Cdd:cd03246 97 -------------------------------------LSGGQRQRLGLARALYGNPRILVLDEPNSHLDVEGERALNQAI 139
|
170 180 190
....*....|....*....|....*....|
gi 1039779783 734 QHYKK-DRTILLTTHHMdEADVLGDRIAIL 762
Cdd:cd03246 140 AALKAaGATRIVIAHRP-ETLASADRILVL 168
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
568-764 |
3.71e-21 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 94.80 E-value: 3.71e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779783 568 KNSTLMAVNDLSLNLYEGQITVLLGHNGAGKTTTLSILTGLYLPTRGKVYISGYDISSDMV-QIRKSLGLCPQD-DLLFP 645
Cdd:PRK13650 16 EDQEKYTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIIDGDLLTEENVwDIRHKIGMVFQNpDNQFV 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779783 646 MLTVSEHLHFYCVIKGIPLQNQSRETNRMLTSFGLLQQSNTMSKDLSGGMKRKLSIIIALIGDTKVVILDEPTSGMDPVS 725
Cdd:PRK13650 96 GATVEDDVAFGLENKGIPHEEMKERVNEALELVGMQDFKEREPARLSGGQKQRVAIAGAVAMRPKIIILDEATSMLDPEG 175
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1039779783 726 RRatwDLLQHYKKDR-----TILLTTHHMDEAdVLGDRiaILVM 764
Cdd:PRK13650 176 RL---ELIKTIKGIRddyqmTVISITHDLDEV-ALSDR--VLVM 213
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
556-768 |
4.80e-21 |
|
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in methanogenesis, methyl coenzyme M reductase, contains alpha, beta, and gamma chains. In older literature, the complex of alpha, beta, and gamma chains was termed component C, while this single chain protein was termed methyl coenzyme M reductase system component A2. [Energy metabolism, Methanogenesis]
Pssm-ID: 132313 [Multi-domain] Cd Length: 520 Bit Score: 98.34 E-value: 4.80e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779783 556 IRIQHLYKEFI-LKNSTLMAVNDLSLNLYEGQITVLLGHNGAGKTTTLSILTGLYLPTRGKVYISGYDISSDMVQIR--- 631
Cdd:TIGR03269 280 IKVRNVSKRYIsVDRGVVKAVDNVSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGEVNVRVGDEWVDMTKPGpdg 359
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779783 632 -----KSLGLCPQDDLLFPMLTVSEHLhfycvIKGIPLQnQSRETNRM-----LTSFGLLQQS-----NTMSKDLSGGMK 696
Cdd:TIGR03269 360 rgrakRYIGILHQEYDLYPHRTVLDNL-----TEAIGLE-LPDELARMkavitLKMVGFDEEKaeeilDKYPDELSEGER 433
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1039779783 697 RKLSIIIALIGDTKVVILDEPTSGMDPVSRRATWDLLQHYKKD--RTILLTTHHMDEADVLGDRIAILVMG-ILK 768
Cdd:TIGR03269 434 HRVALAQVLIKEPRIVILDEPTGTMDPITKVDVTHSILKAREEmeQTFIIVSHDMDFVLDVCDRAALMRDGkIVK 508
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
556-765 |
6.07e-21 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 96.06 E-value: 6.07e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779783 556 IRIQHLYKEFilknSTLMAVNDLSLNLYEGQITVLLGHNGAGKTTTLSILTGLYLPTRGKVYISGYDIsSDMVQIRKSLG 635
Cdd:PRK11607 20 LEIRNLTKSF----DGQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVDL-SHVPPYQRPIN 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779783 636 LCPQDDLLFPMLTVSEHLHFYCVIKGIPLQNQSRETNRMLTSFGLLQQSNTMSKDLSGGMKRKLSIIIALIGDTKVVILD 715
Cdd:PRK11607 95 MMFQSYALFPHMTVEQNIAFGLKQDKLPKAEIASRVNEMLGLVHMQEFAKRKPHQLSGGQRQRVALARSLAKRPKLLLLD 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1039779783 716 EPTSGMDPVSRratwDLLQHYKKD------RTILLTTHHMDEADVLGDRIAILVMG 765
Cdd:PRK11607 175 EPMGALDKKLR----DRMQLEVVDilervgVTCVMVTHDQEEAMTMAGRIAIMNRG 226
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
556-749 |
6.23e-21 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 92.63 E-value: 6.23e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779783 556 IRIQHLYKEFILKNSTLMAVNdlsLNLYEGQITVLLGHNGAGKTTTLSILTGLYLPTRGKVYISGYDIS----SDMVQIR 631
Cdd:PRK10908 2 IRFEHVSKAYLGGRQALQGVT---FHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDITrlknREVPFLR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779783 632 KSLGLCPQDDLLFPMLTVSEHLHFYCVIKGIPLQNQSRETNRMLTSFGLLQQSNTMSKDLSGGMKRKLSIIIALIGDTKV 711
Cdd:PRK10908 79 RQIGMIFQDHHLLMDRTVYDNVAIPLIIAGASGDDIRRRVSAALDKVGLLDKAKNFPIQLSGGEQQRVGIARAVVNKPAV 158
|
170 180 190
....*....|....*....|....*....|....*....
gi 1039779783 712 VILDEPTSGMDPVSRRATWDLLQHYKK-DRTILLTTHHM 749
Cdd:PRK10908 159 LLADEPTGNLDDALSEGILRLFEEFNRvGVTVLMATHDI 197
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
572-748 |
6.62e-21 |
|
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein encoded by ccmA in bacteria. An exception is, an arabidopsis protein. Quite likely this is encoded by an organelle. Bacterial c-type cytocromes are located on the periplasmic side of the cytoplasmic membrane. Several gene products encoded in a locus designated as 'ccm' are implicated in the transport and assembly of the functional cytochrome C. This cluster includes genes: ccmA;B;C;D;E;F;G and H. The posttranslational pathway includes the transport of heme moiety, the secretion of the apoprotein and the covalent attachment of the heme with the apoprotein. The proteins ccmA and B represent an ABC transporter; ccmC and D participate in heme transfer to ccmE, which function as a periplasmic heme chaperone. The presence of ccmF, G and H is suggested to be obligatory for the final functional assembly of cytochrome c. [Protein fate, Protein and peptide secretion and trafficking, Transport and binding proteins, Other]
Pssm-ID: 273491 [Multi-domain] Cd Length: 198 Bit Score: 91.65 E-value: 6.62e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779783 572 LMAVNDLSLNLYEGQITVLLGHNGAGKTTTLSILTGLYLPTRGKVYISGYDISSDMVQIRKSLGLCPQDDLLFPMLTVSE 651
Cdd:TIGR01189 13 RMLFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRWNGTPLAEQRDEPHENILYLGHLPGLKPELSALE 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779783 652 HLHFYCVIkgipLQNQSRETNRMLTSFGLLQQSNTMSKDLSGGMKRKLSIIIALIGDTKVVILDEPTSGMDPVS-RRATW 730
Cdd:TIGR01189 93 NLHFWAAI----HGGAQRTIEDALAAVGLTGFEDLPAAQLSAGQQRRLALARLWLSRRPLWILDEPTTALDKAGvALLAG 168
|
170
....*....|....*...
gi 1039779783 731 DLLQHYKKDRTILLTTHH 748
Cdd:TIGR01189 169 LLRAHLARGGIVLLTTHQ 186
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
574-753 |
1.42e-20 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 98.27 E-value: 1.42e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779783 574 AVNDLSLNLYEGQITVLLGHNGAGKTTTLSILTGLYLPTRGKVYISGYDISSdmVQIRKSLglC------PQDdL---LF 644
Cdd:NF033858 16 ALDDVSLDIPAGCMVGLIGPDGVGKSSLLSLIAGARKIQQGRVEVLGGDMAD--ARHRRAV--CpriaymPQG-LgknLY 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779783 645 PMLTVSEHLHFYCVIKGIPLQNQSRETNRMLTSFGLLQQSNTMSKDLSGGMKRKLSIIIALIGDTKVVILDEPTSGMDPV 724
Cdd:NF033858 91 PTLSVFENLDFFGRLFGQDAAERRRRIDELLRATGLAPFADRPAGKLSGGMKQKLGLCCALIHDPDLLILDEPTTGVDPL 170
|
170 180 190
....*....|....*....|....*....|..
gi 1039779783 725 SRRATWDLLQHYKKDR---TILLTTHHMDEAD 753
Cdd:NF033858 171 SRRQFWELIDRIRAERpgmSVLVATAYMEEAE 202
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
575-767 |
3.79e-20 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 92.20 E-value: 3.79e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779783 575 VNDLSLNLYEGQITVLLGHNGAGKTTTLSILTGLYLPTRGKVYISGYDISSD-----MVQIRKSLGLCPQ--DDLLFPMl 647
Cdd:PRK13641 23 LDNISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITIAGYHITPEtgnknLKKLRKKVSLVFQfpEAQLFEN- 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779783 648 TVSEHLHFYCVIKGIPLQNQSRETNRMLTSFGLLQQsnTMSK---DLSGGMKRKLSIIIALIGDTKVVILDEPTSGMDPV 724
Cdd:PRK13641 102 TVLKDVEFGPKNFGFSEDEAKEKALKWLKKVGLSED--LISKspfELSGGQMRRVAIAGVMAYEPEILCLDEPAAGLDPE 179
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1039779783 725 SRRATWDLLQHYKKD-RTILLTTHHMDEADVLGDRIAILVMGIL 767
Cdd:PRK13641 180 GRKEMMQLFKDYQKAgHTVILVTHNMDDVAEYADDVLVLEHGKL 223
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
574-772 |
3.92e-20 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 92.10 E-value: 3.92e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779783 574 AVNDLSLNLYEGQITVLLGHNGAGKTTTLSILTGLYLPTRGKVYISGYDISSDMVQ-----IRKSLGLCPQ--DDLLFPM 646
Cdd:PRK13643 21 ALFDIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVTVGDIVVSSTSKQkeikpVRKKVGVVFQfpESQLFEE 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779783 647 lTVSEHLHFYCVIKGIPLQNQSRETNRMLTSFGLLQQSNTMSK-DLSGGMKRKLSIIIALIGDTKVVILDEPTSGMDPVS 725
Cdd:PRK13643 101 -TVLKDVAFGPQNFGIPKEKAEKIAAEKLEMVGLADEFWEKSPfELSGGQMRRVAIAGILAMEPEVLVLDEPTAGLDPKA 179
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1039779783 726 RRATWDLLQH-YKKDRTILLTTHHMDEADVLGDRIAILVMGILKCCGS 772
Cdd:PRK13643 180 RIEMMQLFESiHQSGQTVVLVTHLMDDVADYADYVYLLEKGHIISCGT 227
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
556-765 |
8.22e-20 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 92.17 E-value: 8.22e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779783 556 IRIQHLYKEFILKNSTLMAVNDLSLNLYEGQITVLLGHNGAGKTTTLSILTGLYLPTRGKVYISGYDISS----DMVQIR 631
Cdd:PRK11153 2 IELKNISKVFPQGGRTIHALNNVSLHIPAGEIFGVIGASGAGKSTLIRCINLLERPTSGRVLVDGQDLTAlsekELRKAR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779783 632 KSLGLCPQDdllFPML---TVSEHLHFYCVIKGIPLQNQSRETNRMLTSFGLLQQSNTMSKDLSGGMKRKLSIIIALIGD 708
Cdd:PRK11153 82 RQIGMIFQH---FNLLssrTVFDNVALPLELAGTPKAEIKARVTELLELVGLSDKADRYPAQLSGGQKQRVAIARALASN 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1039779783 709 TKVVILDEPTSGMDPVSRRATWDLLQhyKKDR----TILLTTHHMDEADVLGDRIAILVMG 765
Cdd:PRK11153 159 PKVLLCDEATSALDPATTRSILELLK--DINRelglTIVLITHEMDVVKRICDRVAVIDAG 217
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
568-775 |
9.54e-20 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 90.54 E-value: 9.54e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779783 568 KNSTLMAVNDLSLNLYEGQITVLLGHNGAGKTTTLSILTGLYLPTRGKVYISGYDISSDMV-QIRKSLGLCPQD-DLLFP 645
Cdd:PRK13642 16 KESDVNQLNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDGELLTAENVwNLRRKIGMVFQNpDNQFV 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779783 646 MLTVSEHLHFYCVIKGIPLQNQSRETNRMLTSFGLLQQSNTMSKDLSGGMKRKLSI--IIALigDTKVVILDEPTSGMDP 723
Cdd:PRK13642 96 GATVEDDVAFGMENQGIPREEMIKRVDEALLAVNMLDFKTREPARLSGGQKQRVAVagIIAL--RPEIIILDESTSMLDP 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1039779783 724 VSRRATWDLLqHYKKDR---TILLTTHHMDEAdVLGDRIAILVMG--ILKCCGSSLF 775
Cdd:PRK13642 174 TGRQEIMRVI-HEIKEKyqlTVLSITHDLDEA-ASSDRILVMKAGeiIKEAAPSELF 228
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
556-771 |
1.53e-19 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 93.70 E-value: 1.53e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779783 556 IRIQHLYKEFilknSTLMAVNDLSLNLYEGQITVLLGHNGAGKTTTLSILTGLYLPTRGKVYISG--YDISSDMVQIRKS 633
Cdd:PRK09700 6 ISMAGIGKSF----GPVHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNinYNKLDHKLAAQLG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779783 634 LGLCPQDDLLFPMLTVSEHL----HFYCVIKGIPLQNQSRETNR---MLTSFGLLQQSNTMSKDLSGGMKRKLSIIIALI 706
Cdd:PRK09700 82 IGIIYQELSVIDELTVLENLyigrHLTKKVCGVNIIDWREMRVRaamMLLRVGLKVDLDEKVANLSISHKQMLEIAKTLM 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1039779783 707 GDTKVVILDEPTSGMDPVSRRATWDLLQHYKKD-RTILLTTHHMDEADVLGDRIAILVMGILKCCG 771
Cdd:PRK09700 162 LDAKVIIMDEPTSSLTNKEVDYLFLIMNQLRKEgTAIVYISHKLAEIRRICDRYTVMKDGSSVCSG 227
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
574-748 |
2.13e-19 |
|
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: 93.19 E-value: 2.13e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779783 574 AVNDLSLNLYEGQITVLLGHNGAGKTTTLSILTGLYLPTRGKVYISGYDISS-DMVQIRKSLGLCPQDDLLFPMlTVSEH 652
Cdd:TIGR02868 350 VLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPLQGEVTLDGVPVSSlDQDEVRRRVSVCAQDAHLFDT-TVREN 428
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779783 653 LHFYC----------VIKGIPLQNQSRETNRML-TSFGllqqsnTMSKDLSGGMKRKLSIIIALIGDTKVVILDEPTSGM 721
Cdd:TIGR02868 429 LRLARpdatdeelwaALERVGLADWLRALPDGLdTVLG------EGGARLSGGERQRLALARALLADAPILLLDEPTEHL 502
|
170 180
....*....|....*....|....*..
gi 1039779783 722 DPVSRRATWDLLQHYKKDRTILLTTHH 748
Cdd:TIGR02868 503 DAETADELLEDLLAALSGRTVVLITHH 529
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
568-747 |
3.33e-19 |
|
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: 86.91 E-value: 3.33e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779783 568 KNSTLMAVNDLSLNLYEGQITVLLGHNGAGKTTTLSIL-----TGLylpTRGKVYISGYDISSDmvqIRKSLGLCPQDDL 642
Cdd:cd03232 16 KGGKRQLLNNISGYVKPGTLTALMGESGAGKTTLLDVLagrktAGV---ITGEILINGRPLDKN---FQRSTGYVEQQDV 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779783 643 LFPMLTVSEHLHFYCVIKGIPLQNqsretnrmltsfgllqqsntmskdlsggmKRKLSIIIALIGDTKVVILDEPTSGMD 722
Cdd:cd03232 90 HSPNLTVREALRFSALLRGLSVEQ-----------------------------RKRLTIGVELAAKPSILFLDEPTSGLD 140
|
170 180
....*....|....*....|....*....
gi 1039779783 723 PvsrRATWDLLQHYKK----DRTILLTTH 747
Cdd:cd03232 141 S---QAAYNIVRFLKKladsGQAILCTIH 166
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
574-764 |
3.35e-19 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 92.92 E-value: 3.35e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779783 574 AVNDLSLNLYEGQITVLLGHNGAGKTTTLSILTGLYLPTRGKVYISGYDISS-DMVQIRKSLGLCPQDDLLFPMlTVSEH 652
Cdd:COG1132 355 VLKDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYDPTSGRILIDGVDIRDlTLESLRRQIGVVPQDTFLFSG-TIREN 433
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779783 653 LHFycvikGIPlqNQSRET----------NRMLTSF--GLlqqsNTM----SKDLSGGMKRKLSIIIALIGDTKVVILDE 716
Cdd:COG1132 434 IRY-----GRP--DATDEEveeaakaaqaHEFIEALpdGY----DTVvgerGVNLSGGQRQRIAIARALLKDPPILILDE 502
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1039779783 717 PTSGMDPVSRRATWDLLQHYKKDRTILLTTH------HMDEadvlgdriaILVM 764
Cdd:COG1132 503 ATSALDTETEALIQEALERLMKGRTTIVIAHrlstirNADR---------ILVL 547
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
556-764 |
3.41e-19 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 88.60 E-value: 3.41e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779783 556 IRIQHLYKEF----ILKNstlMAVNDLSLNLYEGQ-ITVLlGHNGAGKTTTLSILTGLYLPTRGKVYISGYDISSDMVQI 630
Cdd:COG1101 2 LELKNLSKTFnpgtVNEK---RALDGLNLTIEEGDfVTVI-GSNGAGKSTLLNAIAGSLPPDSGSILIDGKDVTKLPEYK 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779783 631 R-KSLGLCPQDDLL--FPMLTVSEHL----------HFycvikGIPLQNQSRETNR-MLTSF--GLLQQSNTMSKDLSGG 694
Cdd:COG1101 78 RaKYIGRVFQDPMMgtAPSMTIEENLalayrrgkrrGL-----RRGLTKKRRELFReLLATLglGLENRLDTKVGLLSGG 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1039779783 695 MKRKLSIIIALIGDTKVVILDEPTSGMDPvsRRA------TWDLLQhyKKDRTILLTTHHMDEADVLGDRiaiLVM 764
Cdd:COG1101 153 QRQALSLLMATLTKPKLLLLDEHTAALDP--KTAalvlelTEKIVE--ENNLTTLMVTHNMEQALDYGNR---LIM 221
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
566-747 |
3.68e-19 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 92.80 E-value: 3.68e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779783 566 ILKNSTLMAvndlslnlYEGQITVLLGHNGAGKTTTLSILTGlYLPT----RGKVYISGYDISSDmvQIRKSLGLCPQDD 641
Cdd:TIGR00955 40 LLKNVSGVA--------KPGELLAVMGSSGAGKTTLMNALAF-RSPKgvkgSGSVLLNGMPIDAK--EMRAISAYVQQDD 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779783 642 LLFPMLTVSEHLHFYCVIKgipLQNQSRETNRM------LTSFGLLQQSNTM------SKDLSGGMKRKLSIIIALIGDT 709
Cdd:TIGR00955 109 LFIPTLTVREHLMFQAHLR---MPRRVTKKEKRervdevLQALGLRKCANTRigvpgrVKGLSGGERKRLAFASELLTDP 185
|
170 180 190
....*....|....*....|....*....|....*....
gi 1039779783 710 KVVILDEPTSGMDPVSRRATWDLLQHY-KKDRTILLTTH 747
Cdd:TIGR00955 186 PLLFCDEPTSGLDSFMAYSVVQVLKGLaQKGKTIICTIH 224
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
575-773 |
4.75e-19 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 88.18 E-value: 4.75e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779783 575 VNDLSLNLYEGQITVLLGHNGAGKTTTLSILTGLY------LPTRGKVYISGYDI-SSDMVQIRKSLGLCPQDDLLFPML 647
Cdd:PRK14246 26 LKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLIeiydskIKVDGKVLYFGKDIfQIDAIKLRKEVGMVFQQPNPFPHL 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779783 648 TVSEHLHFYCVIKGIplqNQSRETNRM----LTSFGLLQQS----NTMSKDLSGGMKRKLSIIIALIGDTKVVILDEPTS 719
Cdd:PRK14246 106 SIYDNIAYPLKSHGI---KEKREIKKIveecLRKVGLWKEVydrlNSPASQLSGGQQQRLTIARALALKPKVLLMDEPTS 182
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1039779783 720 GMDPVSRRATWDLLQHYKKDRTILLTTHHMDEADVLGDRIAILVMGILKCCGSS 773
Cdd:PRK14246 183 MIDIVNSQAIEKLITELKNEIAIVIVSHNPQQVARVADYVAFLYNGELVEWGSS 236
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
577-755 |
4.77e-19 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 86.85 E-value: 4.77e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779783 577 DLSLNLYEGQITVLLGHNGAGKTTTLSILTGLYLPTRGKVYISGYDISSDMVqIRKSLGLCPQDDLLfPMLTVSEHLHFY 656
Cdd:PRK13539 20 GLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDGGDIDDPDV-AEACHYLGHRNAMK-PALTVAENLEFW 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779783 657 CVIKGiplqnqSRETN--RMLTSFGLLQQSNTMSKDLSGGMKRKLSIIIALIGDTKVVILDEPTSGMDPVSRRATWDLLQ 734
Cdd:PRK13539 98 AAFLG------GEELDiaAALEAVGLAPLAHLPFGYLSAGQKRRVALARLLVSNRPIWILDEPTAALDAAAVALFAELIR 171
|
170 180
....*....|....*....|....*
gi 1039779783 735 -HYKKDRTILLTTHH---MDEADVL 755
Cdd:PRK13539 172 aHLAQGGIVIAATHIplgLPGAREL 196
|
|
| nickel_nikD |
TIGR02770 |
nickel import ATP-binding protein NikD; This family represents the NikD subunit of a ... |
574-765 |
5.36e-19 |
|
nickel import ATP-binding protein NikD; This family represents the NikD subunit of a multisubunit nickel import ABC transporter complex. Nickel, once imported, may be used in urease and in certain classes of hydrogenase and superoxide dismutase. NikD and NikE are homologous. [Transport and binding proteins, Cations and iron carrying compounds]
Pssm-ID: 131817 [Multi-domain] Cd Length: 230 Bit Score: 87.42 E-value: 5.36e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779783 574 AVNDLSLNLYEGQITVLLGHNGAGKTTTLSILTGLYLP----TRGKVYISGYDISSDMVQIRKsLGLCPQD--DLLFPML 647
Cdd:TIGR02770 1 LVQDLNLSLKRGEVLALVGESGSGKSLTCLAILGLLPPgltqTSGEILLDGRPLLPLSIRGRH-IATIMQNprTAFNPLF 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779783 648 TVSEHLHFYCVIKGIPLQNQSRETNRMLTSFGLLQQSNTMSK---DLSGGMKRKLSIIIALIGDTKVVILDEPTSGMDPV 724
Cdd:TIGR02770 80 TMGNHAIETLRSLGKLSKQARALILEALEAVGLPDPEEVLKKypfQLSGGMLQRVMIALALLLEPPFLIADEPTTDLDVV 159
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1039779783 725 SRRATWDLLQHYKKDR--TILLTTHHMDEADVLGDRIAILVMG 765
Cdd:TIGR02770 160 NQARVLKLLRELRQLFgtGILLITHDLGVVARIADEVAVMDDG 202
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
545-765 |
6.95e-19 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 87.40 E-value: 6.95e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779783 545 MEPEPVGLVAGIRIQHL---YKEFilknstlMAVNDLSLNLYEGQITVLLGHNGAGKTTTLSILTGLY--LP---TRGKV 616
Cdd:COG1117 1 MTAPASTLEPKIEVRNLnvyYGDK-------QALKDINLDIPENKVTALIGPSGCGKSTLLRCLNRMNdlIPgarVEGEI 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779783 617 YISGYDISS---DMVQIRKSLGLCPQDDLLFPMlTVSEHlhfycVIKGIPLQNQSRETN------RMLTSFGL------- 680
Cdd:COG1117 74 LLDGEDIYDpdvDVVELRRRVGMVFQKPNPFPK-SIYDN-----VAYGLRLHGIKSKSEldeiveESLRKAALwdevkdr 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779783 681 LQQSNTmskDLSGGMKRKLSIIIALIGDTKVVILDEPTSGMDPVSRRATWDLLQHYKKDRTILLTTHHMDEADVLGDRIA 760
Cdd:COG1117 148 LKKSAL---GLSGGQQQRLCIARALAVEPEVLLMDEPTSALDPISTAKIEELILELKKDYTIVIVTHNMQQAARVSDYTA 224
|
....*
gi 1039779783 761 ILVMG 765
Cdd:COG1117 225 FFYLG 229
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
576-747 |
9.89e-19 |
|
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: 86.82 E-value: 9.89e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779783 576 NDLSLNLYEGQITVLLGHNGAGKTTTLSILTGLYLPTRGKVYISGYDISSDMVQ-IRKSLGLCPQDDLLFPMlTVSEHLH 654
Cdd:cd03249 20 KGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEILLDGVDIRDLNLRwLRSQIGLVSQEPVLFDG-TIAENIR 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779783 655 FycvikGIPLQNQ------SRETNrmLTSF--GLLQQSNTMSKD----LSGGMKRKLSIIIALIGDTKVVILDEPTSGMD 722
Cdd:cd03249 99 Y-----GKPDATDeeveeaAKKAN--IHDFimSLPDGYDTLVGErgsqLSGGQKQRIAIARALLRNPKILLLDEATSALD 171
|
170 180
....*....|....*....|....*
gi 1039779783 723 PVSRRATWDLLQHYKKDRTILLTTH 747
Cdd:cd03249 172 AESEKLVQEALDRAMKGRTTIVIAH 196
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
574-747 |
1.50e-18 |
|
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: 86.13 E-value: 1.50e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779783 574 AVNDLSLNLYEGQITVLLGHNGAGKTTTLSILTGLYLPTRGKVYISGYDISS-DMVQIRKSLGLCPQDDLLFPMlTVSEH 652
Cdd:cd03251 17 VLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDGHDVRDyTLASLRRQIGLVSQDVFLFND-TVAEN 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779783 653 LHFycvikGIP--LQNQSRETNRM--LTSF--GLLQQSNTMSKD----LSGGMKRKLSIIIALIGDTKVVILDEPTSGMD 722
Cdd:cd03251 96 IAY-----GRPgaTREEVEEAARAanAHEFimELPEGYDTVIGErgvkLSGGQRQRIAIARALLKDPPILILDEATSALD 170
|
170 180
....*....|....*....|....*
gi 1039779783 723 PVSRRATWDLLQHYKKDRTILLTTH 747
Cdd:cd03251 171 TESERLVQAALERLMKNRTTFVIAH 195
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
575-784 |
1.50e-18 |
|
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: 84.89 E-value: 1.50e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779783 575 VNDLSLNLYEGQITVLLGHNGAGKTTTLSILTGL--YLPTRGKVYISGYDISsDM---VQIRKSLGLCPQDDLLFPMLTV 649
Cdd:cd03217 16 LKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMGHpkYEVTEGEILFKGEDIT-DLppeERARLGIFLAFQYPPEIPGVKN 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779783 650 SEHLhfycvikgiplqnqsRETNrmltsfgllqqsntmsKDLSGGMKRKLSIIIALIGDTKVVILDEPTSGMDPVSRRAT 729
Cdd:cd03217 95 ADFL---------------RYVN----------------EGFSGGEKKRNEILQLLLLEPDLAILDEPDSGLDIDALRLV 143
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1039779783 730 WDLLQHYK-KDRTILLTTHHMDEAD-VLGDRIAILVMGILKCCGSSLFLKKLYGVGY 784
Cdd:cd03217 144 AEVINKLReEGKSVLIITHYQRLLDyIKPDRVHVLYDGRIVKSGDKELALEIEKKGY 200
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
556-759 |
4.57e-18 |
|
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: 84.41 E-value: 4.57e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779783 556 IRIQHLYKEFILKN---STLMAVNDLSLNLYEGQITVLLGHNGAGKTTTLSILTGLYLPTRGKVYI-SGY---DISS--- 625
Cdd:COG4778 5 LEVENLSKTFTLHLqggKRLPVLDGVSFSVAAGECVALTGPSGAGKSTLLKCIYGNYLPDSGSILVrHDGgwvDLAQasp 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779783 626 -DMVQIRKS-LGLcpqddllfpmltVSEHLHfycVI---------------KGIPLQNQSRETNRMLTSFGL---LQQS- 684
Cdd:COG4778 85 rEILALRRRtIGY------------VSQFLR---VIprvsaldvvaeplleRGVDREEARARARELLARLNLperLWDLp 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1039779783 685 -NTmskdLSGGMKRKLSIIIALIGDTKVVILDEPTSGMDPVSRRATWDLLQHYKKDRTILLT-THHMDEADVLGDRI 759
Cdd:COG4778 150 pAT----FSGGEQQRVNIARGFIADPPLLLLDEPTASLDAANRAVVVELIEEAKARGTAIIGiFHDEEVREAVADRV 222
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
575-755 |
4.68e-18 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 84.07 E-value: 4.68e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779783 575 VNDLSLNLYEGQITVLLGHNGAGKTTTLSILTGLYLP---TRGKVYISGYDIssDMVQI-RKSLGLCPQDDLLFPMLTVS 650
Cdd:COG4136 17 LAPLSLTVAPGEILTLMGPSGSGKSTLLAAIAGTLSPafsASGEVLLNGRRL--TALPAeQRRIGILFQDDLLFPHLSVG 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779783 651 EHLHFyCVIKGIPLQNQSRETNRMLTSFGLLQQSNTMSKDLSGGMKRKLSIIIALIGDTKVVILDEPTSGMDPVSR---R 727
Cdd:COG4136 95 ENLAF-ALPPTIGRAQRRARVEQALEEAGLAGFADRDPATLSGGQRARVALLRALLAEPRALLLDEPFSKLDAALRaqfR 173
|
170 180 190
....*....|....*....|....*....|.
gi 1039779783 728 A-TWDLLQhykkDRTI--LLTTHhmDEADVL 755
Cdd:COG4136 174 EfVFEQIR----QRGIpaLLVTH--DEEDAP 198
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
575-751 |
5.22e-18 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 84.38 E-value: 5.22e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779783 575 VNDLSLNLYEGQITVLLGHNGAGKTTTLSILTGLYLPTRGKVYISGYDISS-DMVQIRKSLGLCPQDDLLFPMlTVSEHL 653
Cdd:PRK10247 23 LNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFEGEDISTlKPEIYRQQVSYCAQTPTLFGD-TVYDNL 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779783 654 HFycvikgiPLQ--NQSRETNRM---LTSFGLLQqsNTMSK---DLSGGMKRKLSIIIALIGDTKVVILDEPTSGMDPVS 725
Cdd:PRK10247 102 IF-------PWQirNQQPDPAIFlddLERFALPD--TILTKniaELSGGEKQRISLIRNLQFMPKVLLLDEITSALDESN 172
|
170 180
....*....|....*....|....*...
gi 1039779783 726 RRATWDLLQHYKKDRTI--LLTTHHMDE 751
Cdd:PRK10247 173 KHNVNEIIHRYVREQNIavLWVTHDKDE 200
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
574-772 |
5.55e-18 |
|
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a central component of the secretion machinery that translocates the toxin, hemolysin A, in a Sec-independent fashion across both membranes of E. coli. The hemolysin A (HlyA) transport machinery is composed of the ATP-binding cassette (ABC) transporter HlyB located in the inner membrane, hemolysin D (HlyD), also anchored in the inner membrane, and TolC, which resides in the outer membrane. HlyD apparently forms a continuous channel that bridges the entire periplasm, interacting with TolC and HlyB. This arrangement prevents the appearance of periplasmic intermediates of HlyA during substrate transport. Little is known about the molecular details of HlyA transport, but it is evident that ATP-hydrolysis by the ABC-transporter HlyB is a necessary source of energy.
Pssm-ID: 213219 [Multi-domain] Cd Length: 237 Bit Score: 84.46 E-value: 5.55e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779783 574 AVNDLSLNLYEGQITVLLGHNGAGKTTTLSILTGLYLPTRGKVYISGYDISS-DMVQIRKSLGLCPQDDLLFPMlTVSEH 652
Cdd:cd03252 17 ILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGHDLALaDPAWLRRQVGVVLQENVLFNR-SIRDN 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779783 653 LHFycVIKGIPLQnQSRETNRMLTSFGLLQQ----SNTMSKD----LSGGMKRKLSIIIALIGDTKVVILDEPTSGMDPV 724
Cdd:cd03252 96 IAL--ADPGMSME-RVIEAAKLAGAHDFISElpegYDTIVGEqgagLSGGQRQRIAIARALIHNPRILIFDEATSALDYE 172
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1039779783 725 SRRATWDLLQHYKKDRTILLTTHHMdEADVLGDRIAILVMGILKCCGS 772
Cdd:cd03252 173 SEHAIMRNMHDICAGRTVIIIAHRL-STVKNADRIIVMEKGRIVEQGS 219
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
572-775 |
5.92e-18 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 84.55 E-value: 5.92e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779783 572 LMAVNDLSLNLYEGQITVLLGHNGAGKTTTLSILTGLYLPTRGKVYISGYDISSDMVQ--IRKSLGLCPQDDLLFPMLTV 649
Cdd:PRK11614 18 IQALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDGKDITDWQTAkiMREAVAIVPEGRRVFSRMTV 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779783 650 SEHLHFycvikGIPLQNQSRETNRMLTSFGLL--------QQSNTMskdlSGGMKRKLSIIIALIGDTKVVILDEPTSGM 721
Cdd:PRK11614 98 EENLAM-----GGFFAERDQFQERIKWVYELFprlherriQRAGTM----SGGEQQMLAIGRALMSQPRLLLLDEPSLGL 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1039779783 722 DPVSRRATWDLLQHYKKD-RTILLTTHHMDEADVLGDRIAILVMG--ILKCCGSSLF 775
Cdd:PRK11614 169 APIIIQQIFDTIEQLREQgMTIFLVEQNANQALKLADRGYVLENGhvVLEDTGDALL 225
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
572-766 |
6.47e-18 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 84.66 E-value: 6.47e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779783 572 LMAVNDLSLNLYEGQITVLLGHNGAGKTTTLSILTGLYLPTRGKVYISGYDI---SSDMVQiRKSLGLCPQDDLLFPMLT 648
Cdd:PRK11300 18 LLAVNNVNLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTILLRGQHIeglPGHQIA-RMGVVRTFQHVRLFREMT 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779783 649 VSE------HLHFYC-VIKGI---PLQNQSrETNRM------LTSFGLLQQSNTMSKDLSGGMKRKLSIIIALIGDTKVV 712
Cdd:PRK11300 97 VIEnllvaqHQQLKTgLFSGLlktPAFRRA-ESEALdraatwLERVGLLEHANRQAGNLAYGQQRRLEIARCMVTQPEIL 175
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1039779783 713 ILDEPTSGMDPVSRRATWDLLQHYKKDR--TILLTTHHMDeadvlgdriaiLVMGI 766
Cdd:PRK11300 176 MLDEPAAGLNPKETKELDELIAELRNEHnvTVLLIEHDMK-----------LVMGI 220
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
570-764 |
9.06e-18 |
|
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: 82.09 E-value: 9.06e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779783 570 STLMAVNDLSLNLYEGQITVLLGHNGAGKTTTLSILTGLYLPTRGKVYISGYDISSDMVQ--IRKSLGLCPQD---DLLF 644
Cdd:cd03215 11 SVKGAVRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITLDGKPVTRRSPRdaIRAGIAYVPEDrkrEGLV 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779783 645 PMLTVSEhlhfycvikgiplqnqsretNRMLTSFgllqqsntmskdLSGGMKRKLSIIIALIGDTKVVILDEPTSGMDPV 724
Cdd:cd03215 91 LDLSVAE--------------------NIALSSL------------LSGGNQQKVVLARWLARDPRVLILDEPTRGVDVG 138
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1039779783 725 SRRATWDLLQHYKKD-RTILLTTHHMDEADVLGDRiaILVM 764
Cdd:cd03215 139 AKAEIYRLIRELADAgKAVLLISSELDELLGLCDR--ILVM 177
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
574-772 |
1.09e-17 |
|
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: 83.31 E-value: 1.09e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779783 574 AVNDLSLNLYEGQITVLLGHNGAGKTTTLSILTGLYLPTRGKVYISGYDISS-DMVQIRKSLGLCPQDDLLFP------- 645
Cdd:cd03244 19 VLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSILIDGVDISKiGLHDLRSRISIIPQDPVLFSgtirsnl 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779783 646 ----------MLTVSEHLHFYCVIKGIPLQNQSRETNRmltsfgllqQSNtmskdLSGGMKRKLSIIIALIGDTKVVILD 715
Cdd:cd03244 99 dpfgeysdeeLWQALERVGLKEFVESLPGGLDTVVEEG---------GEN-----LSVGQRQLLCLARALLRKSKILVLD 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1039779783 716 EPTSGMDPVSRRATWDLLQHYKKDRTILLTTHHMDE-ADVlgDRIAILVMGILKCCGS 772
Cdd:cd03244 165 EATASVDPETDALIQKTIREAFKDCTVLTIAHRLDTiIDS--DRILVLDKGRVVEFDS 220
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
576-759 |
4.41e-17 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 82.06 E-value: 4.41e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779783 576 NDLSLNLYEGQITVLLGHNGAGKTTTLSILTGLYLPTRGKVYISGYDI---SSDMVQIRKSLGLCPQDDLLFPMLTVSEH 652
Cdd:PRK09493 18 HNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGLKVndpKVDERLIRQEAGMVFQQFYLFPHLTALEN 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779783 653 LHFYCV-IKGIPLQNQSRETNRMLTSFGLLQQSNTMSKDLSGGMKRKLSIIIALIGDTKVVILDEPTSGMDPVSRRATWD 731
Cdd:PRK09493 98 VMFGPLrVRGASKEEAEKQARELLAKVGLAERAHHYPSELSGGQQQRVAIARALAVKPKLMLFDEPTSALDPELRHEVLK 177
|
170 180
....*....|....*....|....*....
gi 1039779783 732 LLQHYKKD-RTILLTTHHMDEADVLGDRI 759
Cdd:PRK09493 178 VMQDLAEEgMTMVIVTHEIGFAEKVASRL 206
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
556-772 |
4.56e-17 |
|
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding cassette (ABC) protein of the three subunit molybdate ABC transporter. The three proteins of this complex are homologous to proteins of the sulfate ABC transporter. Molybdenum may be used in nitrogenases of nitrogen-fixing bacteria and in molybdopterin cofactors. In some cases, molybdate may be transported by a sulfate transporter rather than by a specific molybdate transporter. [Transport and binding proteins, Anions]
Pssm-ID: 131197 [Multi-domain] Cd Length: 354 Bit Score: 84.01 E-value: 4.56e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779783 556 IRIQHLYKEFILknstlmavnDLSLNLYEGQITVLLGHNGAGKTTTLSILTGLYLPTRGKVYISGYDISSDMVQI----- 630
Cdd:TIGR02142 3 ARFSKRLGDFSL---------DADFTLPGQGVTAIFGRSGSGKTTLIRLIAGLTRPDEGEIVLNGRTLFDSRKGIflppe 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779783 631 RKSLGLCPQDDLLFPMLTVSEHLHfYCVIKGIPLQNQSRETN--RMLTSFGLLQQsntMSKDLSGGMKRKLSIIIALIGD 708
Cdd:TIGR02142 74 KRRIGYVFQEARLFPHLSVRGNLR-YGMKRARPSERRISFERviELLGIGHLLGR---LPGRLSGGEKQRVAIGRALLSS 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1039779783 709 TKVVILDEPTSGMDPVSRRATWDLLQ--HYKKDRTILLTTHHMDEADVLGDRIAILVMGILKCCGS 772
Cdd:TIGR02142 150 PRLLLMDEPLAALDDPRKYEILPYLErlHAEFGIPILYVSHSLQEVLRLADRVVVLEDGRVAAAGP 215
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
577-749 |
5.34e-17 |
|
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: 81.36 E-value: 5.34e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779783 577 DLSLNLYEGQITVLLGHNGAGKTTTLSILTGLYLPTRGKVYISGYDISS-DMVQIRKSLGLCPQDDLLFPMlTVSEHL-- 653
Cdd:cd03248 32 DVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDGKPISQyEHKYLHSKVSLVGQEPVLFAR-SLQDNIay 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779783 654 -----HFYCVIKGIplQNQSRETNRMLTSFGLLQQSNTMSKDLSGGMKRKLSIIIALIGDTKVVILDEPTSGMDPVSRRA 728
Cdd:cd03248 111 glqscSFECVKEAA--QKAHAHSFISELASGYDTEVGEKGSQLSGGQKQRVAIARALIRNPQVLILDEATSALDAESEQQ 188
|
170 180
....*....|....*....|.
gi 1039779783 729 TWDLLQHYKKDRTILLTTHHM 749
Cdd:cd03248 189 VQQALYDWPERRTVLVIAHRL 209
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
574-765 |
5.49e-17 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 82.34 E-value: 5.49e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779783 574 AVNDLSLNLYEGQITVLLGHNGAGKTTTLSILTGLYLPTRGKVYISGYDIS--SDMVQIRKSLGLCPQD-DLLFPMLTVS 650
Cdd:PRK13644 17 ALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLVSGIDTGdfSKLQGIRKLVGIVFQNpETQFVGRTVE 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779783 651 EHLHFYCVIKGIPLQNQSRETNRMLTSFGLLQQSNTMSKDLSGGMKRKLSIIIALIGDTKVVILDEPTSGMDPVSRRATW 730
Cdd:PRK13644 97 EDLAFGPENLCLPPIEIRKRVDRALAEIGLEKYRHRSPKTLSGGQGQCVALAGILTMEPECLIFDEVTSMLDPDSGIAVL 176
|
170 180 190
....*....|....*....|....*....|....*.
gi 1039779783 731 DLLQH-YKKDRTILLTTHHMDEADVlGDRIAILVMG 765
Cdd:PRK13644 177 ERIKKlHEKGKTIVYITHNLEELHD-ADRIIVMDRG 211
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
574-772 |
6.92e-17 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 82.36 E-value: 6.92e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779783 574 AVNDLSLNLYEGQITVLLGHNGAGKTTTLSILTGLYLPTRGKVYISGYDISSDMVQI------RKSLGLCPQddllFPML 647
Cdd:PRK13645 26 ALNNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGLIISETGQTIVGDYAIPANLKKIkevkrlRKEIGLVFQ----FPEY 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779783 648 -----TVSEHLHFYCVIKGIPLQNQSRETNRMLTSFGLLQQSNTMSK-DLSGGMKRKLSI--IIALIGDTkvVILDEPTS 719
Cdd:PRK13645 102 qlfqeTIEKDIAFGPVNLGENKQEAYKKVPELLKLVQLPEDYVKRSPfELSGGQKRRVALagIIAMDGNT--LVLDEPTG 179
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1039779783 720 GMDPVSRRATWDLLQHYKKD--RTILLTTHHMDEADVLGDRIAILVMGILKCCGS 772
Cdd:PRK13645 180 GLDPKGEEDFINLFERLNKEykKRIIMVTHNMDQVLRIADEVIVMHEGKVISIGS 234
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
556-758 |
8.89e-17 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 81.33 E-value: 8.89e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779783 556 IRIQHLYKEFilKNSTLMAVNDLSLNlyEGQITVLLGHNGAGKTTTLSILTGLYLPTRGKVYISGYDISSD--------- 626
Cdd:PRK11264 4 IEVKNLVKKF--HGQTVLHGIDLEVK--PGEVVAIIGPSGSGKTTLLRCINLLEQPEAGTIRVGDITIDTArslsqqkgl 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779783 627 MVQIRKSLGLCPQDDLLFPMLTVSEH-LHFYCVIKGIPLQNQSRETNRMLTSFGLLQQSNTMSKDLSGGMKRKLSIIIAL 705
Cdd:PRK11264 80 IRQLRQHVGFVFQNFNLFPHRTVLENiIEGPVIVKGEPKEEATARARELLAKVGLAGKETSYPRRLSGGQQQRVAIARAL 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1039779783 706 IGDTKVVILDEPTSGMDP--VSR-RATWDLLQHYKkdRTILLTTHHMDEADVLGDR 758
Cdd:PRK11264 160 AMRPEVILFDEPTSALDPelVGEvLNTIRQLAQEK--RTMVIVTHEMSFARDVADR 213
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
577-748 |
9.01e-17 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 79.85 E-value: 9.01e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779783 577 DLSLNLYEGQITVLLGHNGAGKTTTLSILTGLYLPTRGKVYISGYDISsdmvQIRKSLglcpQDDLLF--------PMLT 648
Cdd:PRK13538 19 GLSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVLWQGEPIR----RQRDEY----HQDLLYlghqpgikTELT 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779783 649 VSEHLHFYCVIKGiplqNQSRE-TNRMLTSFGLLQQSNTMSKDLSGGMKRKlsiiIAL----IGDTKVVILDEP-----T 718
Cdd:PRK13538 91 ALENLRFYQRLHG----PGDDEaLWEALAQVGLAGFEDVPVRQLSAGQQRR----VALarlwLTRAPLWILDEPftaidK 162
|
170 180 190
....*....|....*....|....*....|
gi 1039779783 719 SGMDPVSRRatwdLLQHYKKDRTILLTTHH 748
Cdd:PRK13538 163 QGVARLEAL----LAQHAEQGGMVILTTHQ 188
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
574-764 |
9.25e-17 |
|
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide chain transporter in the ATP-binding cassette (ABC) transporter family, MsbA, which exports lipid A. It may also act in multidrug resistance. Lipid A, a part of lipopolysaccharide, is found in the outer leaflet of the outer membrane of most Gram-negative bacteria. Members of this family are restricted to the Proteobacteria (although lipid A is more broadly distributed) and often are clustered with lipid A biosynthesis genes. [Cell envelope, Biosynthesis and degradation of surface polysaccharides and lipopolysaccharides, Transport and binding proteins, Other]
Pssm-ID: 131258 [Multi-domain] Cd Length: 571 Bit Score: 85.15 E-value: 9.25e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779783 574 AVNDLSLNLYEGQITVLLGHNGAGKTTTLSILTGLYLPTRGKVYISGYDISSDMVQ-IRKSLGLCPQDDLLFPMlTVSEH 652
Cdd:TIGR02203 347 ALDSISLVIEPGETVALVGRSGSGKSTLVNLIPRFYEPDSGQILLDGHDLADYTLAsLRRQVALVSQDVVLFND-TIANN 425
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779783 653 LHfYCVIKGIPlQNQSRETNRM--LTSF------GLLQQSNTMSKDLSGGMKRKLSIIIALIGDTKVVILDEPTSGMDPV 724
Cdd:TIGR02203 426 IA-YGRTEQAD-RAEIERALAAayAQDFvdklplGLDTPIGENGVLLSGGQRQRLAIARALLKDAPILILDEATSALDNE 503
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1039779783 725 SRRATWDLLQHYKKDRTILLTTHHM---DEADvlgdriAILVM 764
Cdd:TIGR02203 504 SERLVQAALERLMQGRTTLVIAHRLstiEKAD------RIVVM 540
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
578-765 |
9.68e-17 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 81.11 E-value: 9.68e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779783 578 LSLNLYEGQITVLLGHNGAGKTTTLSI---LTGLYLPTR--GKVYISGYDI-SSDMVQIRKSLGLCPQDDLLFPMLTVSE 651
Cdd:PRK14247 22 VNLEIPDNTITALMGPSGSGKSTLLRVfnrLIELYPEARvsGEVYLDGQDIfKMDVIELRRRVQMVFQIPNPIPNLSIFE 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779783 652 HlhfycVIKGIPLqnqsretNRMLTSFGLLQQS------------------NTMSKDLSGGMKRKLSIIIALIGDTKVVI 713
Cdd:PRK14247 102 N-----VALGLKL-------NRLVKSKKELQERvrwalekaqlwdevkdrlDAPAGKLSGGQQQRLCIARALAFQPEVLL 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1039779783 714 LDEPTSGMDPVSRRATWDLLQHYKKDRTILLTTHHMDEADVLGDRIAILVMG 765
Cdd:PRK14247 170 ADEPTANLDPENTAKIESLFLELKKDMTIVLVTHFPQQAARISDYVAFLYKG 221
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
575-772 |
1.07e-16 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 81.21 E-value: 1.07e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779783 575 VNDLSLNLYEGQITVLLGHNGAGKTTTLSILTGLYLPTRGKVYISGYDISS-DMVQIRKSLGLCPQDDLLFPMLTV---- 649
Cdd:PRK11231 18 LNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDKPISMlSSRQLARRLALLPQHHLTPEGITVrelv 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779783 650 ----SEHLHFYcvikGIPLQNQSRETNRMLTSFGLLQQSNTMSKDLSGGMKRKLSIIIALIGDTKVVILDEPTSGMDpVS 725
Cdd:PRK11231 98 aygrSPWLSLW----GRLSAEDNARVNQAMEQTRINHLADRRLTDLSGGQRQRAFLAMVLAQDTPVVLLDEPTTYLD-IN 172
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1039779783 726 RRAT-WDLLQHYK-KDRTILLTTHHMDEADVLGDRIAILVMGILKCCGS 772
Cdd:PRK11231 173 HQVElMRLMRELNtQGKTVVTVLHDLNQASRYCDHLVVLANGHVMAQGT 221
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
556-762 |
1.26e-16 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 83.07 E-value: 1.26e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779783 556 IRIQHLYKEFilknSTLMAVNDLSLNLYEGQITVLLGHNGAGKTTTLSILTGLYLPTRGKVYISGYDISSDMVQIRKsLG 635
Cdd:PRK09452 15 VELRGISKSF----DGKEVISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLDGQDITHVPAENRH-VN 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779783 636 LCPQDDLLFPMLTVSEHLHFYCVIKGIPLQNQSRETNRMLTSFGLLQQSNTMSKDLSGGMKRKLSIIIALIGDTKVVILD 715
Cdd:PRK09452 90 TVFQSYALFPHMTVFENVAFGLRMQKTPAAEITPRVMEALRMVQLEEFAQRKPHQLSGGQQQRVAIARAVVNKPKVLLLD 169
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1039779783 716 EPTSGMDPVSRRATWDLLQHYKKDR--TILLTTHHMDEADVLGDRIAIL 762
Cdd:PRK09452 170 ESLSALDYKLRKQMQNELKALQRKLgiTFVFVTHDQEEALTMSDRIVVM 218
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
557-765 |
1.36e-16 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 80.18 E-value: 1.36e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779783 557 RIQHLYKEFILKnstlmavndLSLNLYEGQITVLLGHNGAGKTTTLSILTGLYLPTRGKVYISGYDISSDMVQIRkslgl 636
Cdd:COG3840 6 DLTYRYGDFPLR---------FDLTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILWNGQDLTALPPAER----- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779783 637 cP-----QDDLLFPMLTVSEHLhfycvikGIPLQ-------NQSRETNRMLTSFGLLQQSNTMSKDLSGGMKRKLSIIIA 704
Cdd:COG3840 72 -PvsmlfQENNLFPHLTVAQNI-------GLGLRpglkltaEQRAQVEQALERVGLAGLLDRLPGQLSGGQRQRVALARC 143
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1039779783 705 LIGDTKVVILDEPTSGMDPVSRRATWDLLQHYKKDR--TILLTTHHMDEADVLGDRIAILVMG 765
Cdd:COG3840 144 LVRKRPILLLDEPFSALDPALRQEMLDLVDELCRERglTVLMVTHDPEDAARIADRVLLVADG 206
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
574-752 |
1.51e-16 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 80.51 E-value: 1.51e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779783 574 AVNDLSLNLYEGQITVLLGHNGAGKTTTLSILTGLYLPTRGKVYISGYDISSDMVQirksLGLCPQDDLLFPMLTVSEHL 653
Cdd:PRK11248 16 ALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDGKPVEGPGAE----RGVVFQNEGLLPWRNVQDNV 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779783 654 HFYCVIKGIPLQNQSRETNRMLTSFGLLQQSNTMSKDLSGGMKRKLSIIIALIGDTKVVILDEPTSGMDPVSRRATWDLL 733
Cdd:PRK11248 92 AFGLQLAGVEKMQRLEIAHQMLKKVGLEGAEKRYIWQLSGGQRQRVGIARALAANPQLLLLDEPFGALDAFTREQMQTLL 171
|
170 180
....*....|....*....|.
gi 1039779783 734 QHYKKD--RTILLTTHHMDEA 752
Cdd:PRK11248 172 LKLWQEtgKQVLLITHDIEEA 192
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
574-762 |
1.58e-16 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 83.81 E-value: 1.58e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779783 574 AVNDLSLNLYEGQITVLLGHNGAGKTTTLSILTGLYLPTRGKVYISG--YDISSDMVQIRKSLGLCPQDDLLFPMLTVSE 651
Cdd:PRK11288 19 ALDDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSILIDGqeMRFASTTAALAAGVAIIYQELHLVPEMTVAE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779783 652 HL------HFYCVIKGIPLQNQSREtnrMLTSFGLLQQSNTMSKDLSGGMKRKLSIIIALIGDTKVVILDEPTSGMdpvS 725
Cdd:PRK11288 99 NLylgqlpHKGGIVNRRLLNYEARE---QLEHLGVDIDPDTPLKYLSIGQRQMVEIAKALARNARVIAFDEPTSSL---S 172
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1039779783 726 RRATWDLL----QHYKKDRTILLTTHHMDEADVLGDRIAIL 762
Cdd:PRK11288 173 AREIEQLFrvirELRAEGRVILYVSHRMEEIFALCDAITVF 213
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
574-753 |
2.09e-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: 83.88 E-value: 2.09e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779783 574 AVNDLSLNLYEGQITVLLGHNGAGKTTTLSILTGLYLPTRGKVYISGYDISS-DMVQIRKSLGLCPQDDLLFPMlTVSEH 652
Cdd:TIGR02857 337 ALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSIAVNGVPLADaDADSWRDQIAWVPQHPFLFAG-TIAEN 415
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779783 653 LHFYC-VIKGIPLQNQSRETNRMLTSFGLLQQSNTMSKD----LSGGMKRKLSIIIALIGDTKVVILDEPTSGMDPVSRR 727
Cdd:TIGR02857 416 IRLARpDASDAEIREALERAGLDEFVAALPQGLDTPIGEggagLSGGQAQRLALARAFLRDAPLLLLDEPTAHLDAETEA 495
|
170 180
....*....|....*....|....*....
gi 1039779783 728 ATWDLLQHYKKDRTILLTTH---HMDEAD 753
Cdd:TIGR02857 496 EVLEALRALAQGRTVLLVTHrlaLAALAD 524
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
577-756 |
2.22e-16 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 79.86 E-value: 2.22e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779783 577 DLSLNLYEGQITVLLGHNGAGKTTTLSILTGLYLPTRGKVYISGYDI----SSDMVQIR-KSLGLCPQDDLLFPMLTVSE 651
Cdd:PRK11629 27 NVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPMsklsSAAKAELRnQKLGFIYQFHHLLPDFTALE 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779783 652 HLHFYCVIKGIPLQNQSRETNRMLTSFGLLQQSNTMSKDLSGGMKRKLSIIIALIGDTKVVILDEPTSGMDPVSRRATWD 731
Cdd:PRK11629 107 NVAMPLLIGKKKPAEINSRALEMLAAVGLEHRANHRPSELSGGERQRVAIARALVNNPRLVLADEPTGNLDARNADSIFQ 186
|
170 180
....*....|....*....|....*..
gi 1039779783 732 LLQ--HYKKDRTILLTTHHMDEADVLG 756
Cdd:PRK11629 187 LLGelNRLQGTAFLVVTHDLQLAKRMS 213
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
573-767 |
2.73e-16 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 79.89 E-value: 2.73e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779783 573 MAVNDLSLNLYEGQITVLLGHNGAGKTTTLSILTGLY-----LPTRGKVYISGYDISS---DMVQIRKSLGLCPQDDLLF 644
Cdd:PRK14267 18 HVIKGVDLKIPQNGVFALMGPSGCGKSTLLRTFNRLLelneeARVEGEVRLFGRNIYSpdvDPIEVRREVGMVFQYPNPF 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779783 645 PMLTVSEHlhfycVIKGIPLQNQSRETNRM-------LTSFGLLQQSNTMSKD----LSGGMKRKLSIIIALIGDTKVVI 713
Cdd:PRK14267 98 PHLTIYDN-----VAIGVKLNGLVKSKKELdervewaLKKAALWDEVKDRLNDypsnLSGGQRQRLVIARALAMKPKILL 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1039779783 714 LDEPTSGMDPVSRRATWDLLQHYKKDRTILLTTHHMDEADVLGDRIAILVMGIL 767
Cdd:PRK14267 173 MDEPTANIDPVGTAKIEELLFELKKEYTIVLVTHSPAQAARVSDYVAFLYLGKL 226
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
545-762 |
2.81e-16 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 83.18 E-value: 2.81e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779783 545 MEPEPVglvagIRIQHLYKEFilknSTLMAVNDLSLNLYEGQITVLLGHNGAGKTTTLSILTGLYLPTRGKVYISGYDIS 624
Cdd:PRK15439 6 TTAPPL-----LCARSISKQY----SGVEVLKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIGGNPCA 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779783 625 SDMVQIRKSLG--LCPQDDLLFPMLTVSEHLHFycvikGIPlqnQSRETNRMLTSfgLLQQSNT-MSKDLSGGM-----K 696
Cdd:PRK15439 77 RLTPAKAHQLGiyLVPQEPLLFPNLSVKENILF-----GLP---KRQASMQKMKQ--LLAALGCqLDLDSSAGSlevadR 146
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1039779783 697 RKLSIIIALIGDTKVVILDEPTSGMDPVSRRATWDLLQHY-KKDRTILLTTHHMDEADVLGDRIAIL 762
Cdd:PRK15439 147 QIVEILRGLMRDSRILILDEPTASLTPAETERLFSRIRELlAQGVGIVFISHKLPEIRQLADRISVM 213
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
577-787 |
3.61e-16 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 83.62 E-value: 3.61e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779783 577 DLSLNLYEGQITVLLGHNGAGKTTTLSILTGLYLPTRGKVYISGYDISS-DMVQIRKSLGLCPQDDLLFPMlTVSEHLHF 655
Cdd:TIGR00958 499 GLTFTLHPGEVVALVGPSGSGKSTVAALLQNLYQPTGGQVLLDGVPLVQyDHHYLHRQVALVGQEPVLFSG-SVRENIAY 577
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779783 656 ---YCVIKGIplQNQSRETNRMLTSFGLLQQSNTMSKD----LSGGMKRKLSIIIALIGDTKVVILDEPTSGMDPVSRRA 728
Cdd:TIGR00958 578 gltDTPDEEI--MAAAKAANAHDFIMEFPNGYDTEVGEkgsqLSGGQKQRIAIARALVRKPRVLILDEATSALDAECEQL 655
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1039779783 729 TWDLLQhyKKDRTILLTTHHMDEADVlGDRIAILVMGILKCCGSSLFLKKLYGVGYHLV 787
Cdd:TIGR00958 656 LQESRS--RASRTVLLIAHRLSTVER-ADQILVLKKGSVVEMGTHKQLMEDQGCYKHLV 711
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
556-773 |
6.50e-16 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 78.90 E-value: 6.50e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779783 556 IRIQHLYKEFiLKNSTLMAVNdlsLNLYEGQITVLLGHNGAGKTTTLSILTGLYlpTRGKVYISGYDISSDMVQ------ 629
Cdd:PRK09984 5 IRVEKLAKTF-NQHQALHAVD---LNIHHGEMVALLGPSGSGKSTLLRHLSGLI--TGDKSAGSHIELLGRTVQregrla 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779783 630 --IRKS---LGLCPQDDLLFPMLTVSEHL--------HFY--CVIKGIPLQNQsrETNRMLTSFGLLQQSNTMSKDLSGG 694
Cdd:PRK09984 79 rdIRKSranTGYIFQQFNLVNRLSVLENVligalgstPFWrtCFSWFTREQKQ--RALQALTRVGMVHFAHQRVSTLSGG 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779783 695 MKRKLSIIIALIGDTKVVILDEPTSGMDPVSRRATWDLLQHYKKDR--TILLTTHHMDEADVLGDRIAILVMGILKCCGS 772
Cdd:PRK09984 157 QQQRVAIARALMQQAKVILADEPIASLDPESARIVMDTLRDINQNDgiTVVVTLHQVDYALRYCERIVALRQGHVFYDGS 236
|
.
gi 1039779783 773 S 773
Cdd:PRK09984 237 S 237
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
578-748 |
7.68e-16 |
|
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the bacterial CcmAB transporter. The CCM family is involved in bacterial cytochrome c biogenesis. Cytochrome c maturation in E. coli requires the ccm operon, which encodes eight membrane proteins (CcmABCDEFGH). CcmE is a periplasmic heme chaperon that binds heme covalently and transfers it onto apocytochrome c in the presence of CcmF, CcmG, and CcmH. The CcmAB proteins represent an ABC transporter and the CcmCD proteins participate in heme transfer to CcmE.
Pssm-ID: 213198 [Multi-domain] Cd Length: 201 Bit Score: 77.15 E-value: 7.68e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779783 578 LSLNLYEGQITVLLGHNGAGKTTTLSILTGLYLPTRGKVYISGYDISSDMVQIRKSLGLCPQDDLLFPMLTVSEHLHFYC 657
Cdd:cd03231 19 LSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNGGPLDFQRDSIARGLLYLGHAPGIKTTLSVLENLRFWH 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779783 658 VIkgiplqnQSRET-NRMLTSFGLLQQSNTMSKDLSGGMKRKLSIIIALIGDTKVVILDEPTSGMDPVS-RRATWDLLQH 735
Cdd:cd03231 99 AD-------HSDEQvEEALARVGLNGFEDRPVAQLSAGQQRRVALARLLLSGRPLWILDEPTTALDKAGvARFAEAMAGH 171
|
170
....*....|...
gi 1039779783 736 YKKDRTILLTTHH 748
Cdd:cd03231 172 CARGGMVVLTTHQ 184
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
555-723 |
8.67e-16 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 78.13 E-value: 8.67e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779783 555 GIRIQHLYKEFilknSTLMAVNDLSLNLYEGQITVLLGHNGAGKTTTLSILTGLYLPTRGKVYISGYDIS-------SDM 627
Cdd:COG4161 2 SIQLKNINCFY----GSHQALFDINLECPSGETLVLLGPSGAGKSSLLRVLNLLETPDSGQLNIAGHQFDfsqkpseKAI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779783 628 VQIRKSLGLCPQDDLLFPMLTVSEHL-HFYCVIKGIPLQNQSRETNRMLTSFGLLQQSNTMSKDLSGGMKRKLSIIIALI 706
Cdd:COG4161 78 RLLRQKVGMVFQQYNLWPHLTVMENLiEAPCKVLGLSKEQAREKAMKLLARLRLTDKADRFPLHLSGGQQQRVAIARALM 157
|
170
....*....|....*..
gi 1039779783 707 GDTKVVILDEPTSGMDP 723
Cdd:COG4161 158 MEPQVLLFDEPTAALDP 174
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
590-765 |
9.45e-16 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 78.69 E-value: 9.45e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779783 590 LLGHNGAGKTTTLSILTGLYLPTRGKVYISGYDISSDMV-QIRKSLGLCPQ--DDLLFPMlTVSEHLHFYCVIKGIPLQN 666
Cdd:PRK13652 35 VIGPNGAGKSTLFRHFNGILKPTSGSVLIRGEPITKENIrEVRKFVGLVFQnpDDQIFSP-TVEQDIAFGPINLGLDEET 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779783 667 QSRETNRMLTSFGLLQQSNTMSKDLSGGMKRKLSIIIALIGDTKVVILDEPTSGMDPVSRRATWDLLQHYKKD--RTILL 744
Cdd:PRK13652 114 VAHRVSSALHMLGLEELRDRVPHHLSGGEKKRVAIAGVIAMEPQVLVLDEPTAGLDPQGVKELIDFLNDLPETygMTVIF 193
|
170 180
....*....|....*....|.
gi 1039779783 745 TTHHMDEADVLGDRIAILVMG 765
Cdd:PRK13652 194 STHQLDLVPEMADYIYVMDKG 214
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
556-772 |
9.73e-16 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 81.79 E-value: 9.73e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779783 556 IRIQHLykEFILKNSTLMAVNDLSLNLYEGQITVLLGHNGAGKTTTLSILTGLYLPTRGKVYISGYDISS-DMVQIRKSL 634
Cdd:PRK11160 339 LTLNNV--SFTYPDQPQPVLKGLSLQIKAGEKVALLGRTGCGKSTLLQLLTRAWDPQQGEILLNGQPIADySEAALRQAI 416
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779783 635 GLCPQ----------DDLLFPMLTVSEHlHFYCVIKGIPLQNqsretnrmltsfgLLQQSNTMS-------KDLSGGMKR 697
Cdd:PRK11160 417 SVVSQrvhlfsatlrDNLLLAAPNASDE-ALIEVLQQVGLEK-------------LLEDDKGLNawlgeggRQLSGGEQR 482
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779783 698 KLSIIIALIGDTKVVILDEPTSGMDPVSRRATWDLLQHYKKDRTILLTTH------HMdeadvlgDRIAILVMGILKCCG 771
Cdd:PRK11160 483 RLGIARALLHDAPLLLLDEPTEGLDAETERQILELLAEHAQNKTVLMITHrltgleQF-------DRICVMDNGQIIEQG 555
|
.
gi 1039779783 772 S 772
Cdd:PRK11160 556 T 556
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
575-764 |
1.35e-15 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 79.76 E-value: 1.35e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779783 575 VNDLSLNLYEGQITVLLGHNGAGKTTTLSILTGLYLPTRGKVYISGYDISSDMVQIRKslgLCP--QDDLLFPMLTVSEH 652
Cdd:PRK11432 22 IDNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIFIDGEDVTHRSIQQRD---ICMvfQSYALFPHMSLGEN 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779783 653 LHFycvikGIPLQNQSRETNRM----------LTSFGllqqsNTMSKDLSGGMKRKLSIIIALIGDTKVVILDEPTSGMD 722
Cdd:PRK11432 99 VGY-----GLKMLGVPKEERKQrvkealelvdLAGFE-----DRYVDQISGGQQQRVALARALILKPKVLLFDEPLSNLD 168
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1039779783 723 PVSRRATWDLLQHYKK--DRTILLTTHHMDEADVLGDriAILVM 764
Cdd:PRK11432 169 ANLRRSMREKIRELQQqfNITSLYVTHDQSEAFAVSD--TVIVM 210
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
577-725 |
1.52e-15 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 77.88 E-value: 1.52e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779783 577 DLSLNLYEGQITVLLGHNGAGKTTTLSILTGLYLPTRGKVYISGYDI----SSDMVQIRKSLGLCPQDDLLFPMLTVSEH 652
Cdd:PRK11831 25 NISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEILFDGENIpamsRSRLYTVRKRMSMLFQSGALFTDMNVFDN 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779783 653 LHFycvikgiPLQNQS-------RETNRM-LTSFGLLQQSNTMSKDLSGGMKRKLSIIIALIGDTKVVILDEPTSGMDPV 724
Cdd:PRK11831 105 VAY-------PLREHTqlpapllHSTVMMkLEAVGLRGAAKLMPSELSGGMARRAALARAIALEPDLIMFDEPFVGQDPI 177
|
.
gi 1039779783 725 S 725
Cdd:PRK11831 178 T 178
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
573-760 |
1.67e-15 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 77.90 E-value: 1.67e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779783 573 MAVNDLSLNLYEGQITVLLGHNGAGKTTTLSILTGL--YLPT---RGKVYISG---YDISSDMVQIRKSLGLCPQDDLLF 644
Cdd:PRK14243 24 LAVKNVWLDIPKNQITAFIGPSGCGKSTILRCFNRLndLIPGfrvEGKVTFHGknlYAPDVDPVEVRRRIGMVFQKPNPF 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779783 645 PMlTVSEHLHFYCVIKGIPlQNQSRETNRMLTSFGL-------LQQSNTmskDLSGGMKRKLSIIIALIGDTKVVILDEP 717
Cdd:PRK14243 104 PK-SIYDNIAYGARINGYK-GDMDELVERSLRQAALwdevkdkLKQSGL---SLSGGQQQRLCIARAIAVQPEVILMDEP 178
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1039779783 718 TSGMDPVSRRATWDLLQHYKKDRTILLTTHHMDEADVLGDRIA 760
Cdd:PRK14243 179 CSALDPISTLRIEELMHELKEQYTIIIVTHNMQQAARVSDMTA 221
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
574-762 |
1.77e-15 |
|
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: 76.80 E-value: 1.77e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779783 574 AVNDLSLNLYEGQITVLLGHNGAGKTTTLSILTGLYLPTRGKVYISGyDISSdmvqirkslglcpqddLLF------PML 647
Cdd:cd03220 37 ALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVTVRG-RVSS----------------LLGlgggfnPEL 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779783 648 TVSEHLHFYCVIKGIPLQNQSRETNRMLtSFGLLQQSNTMS-KDLSGGMKRKL--SIIIALIGDtkVVILDEPTSGMDPV 724
Cdd:cd03220 100 TGRENIYLNGRLLGLSRKEIDEKIDEII-EFSELGDFIDLPvKTYSSGMKARLafAIATALEPD--ILLIDEVLAVGDAA 176
|
170 180 190
....*....|....*....|....*....|....*....
gi 1039779783 725 SRRATWDLLQHYKKD-RTILLTTHHMDEADVLGDRIAIL 762
Cdd:cd03220 177 FQEKCQRRLRELLKQgKTVILVSHDPSSIKRLCDRALVL 215
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
573-760 |
2.04e-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: 76.89 E-value: 2.04e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779783 573 MAVNDLSLNLYEGQITVLLGHNGAGKTTTLSILTGLYLPTRGKVYISGYDISS-DMVQIRKSLGLCPQDDLLF------- 644
Cdd:cd03253 15 PVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDGQDIREvTLDSLRRAIGVVPQDTVLFndtigyn 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779783 645 -----------PMLTVSEHLHFYCVIKGIPLQNQSRETNRmltsfGLLqqsntmskdLSGGMKRKLSIIIALIGDTKVVI 713
Cdd:cd03253 95 irygrpdatdeEVIEAAKAAQIHDKIMRFPDGYDTIVGER-----GLK---------LSGGEKQRVAIARAILKNPPILL 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1039779783 714 LDEPTSGMDPVSRRATWDLLQHYKKDRTILLTTH------HMDEADVLGD-RIA 760
Cdd:cd03253 161 LDEATSALDTHTEREIQAALRDVSKGRTTIVIAHrlstivNADKIIVLKDgRIV 214
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
556-768 |
2.12e-15 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 78.74 E-value: 2.12e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779783 556 IRIQHLYKEFILK-NSTLMAVNDLSLNLYEGQITVLLGHNGAGKTTTLSILTGLYLPTRGKVYISGYDISSDMV------ 628
Cdd:PRK13631 22 LRVKNLYCVFDEKqENELVALNNISYTFEKNKIYFIIGNSGSGKSTLVTHFNGLIKSKYGTIQVGDIYIGDKKNnhelit 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779783 629 -----------QIRKSLGLCPQddllFPML-----TVSEHLHFYCVIKGIPLQNQSRETNRMLTSFGL----LQQSntmS 688
Cdd:PRK13631 102 npyskkiknfkELRRRVSMVFQ----FPEYqlfkdTIEKDIMFGPVALGVKKSEAKKLAKFYLNKMGLddsyLERS---P 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779783 689 KDLSGGMKRKLSIIIALIGDTKVVILDEPTSGMDPVSRRATWDLLQHYKKD-RTILLTTHHMDEADVLGDRIAILVMG-I 766
Cdd:PRK13631 175 FGLSGGQKRRVAIAGILAIQPEILIFDEPTAGLDPKGEHEMMQLILDAKANnKTVFVITHTMEHVLEVADEVIVMDKGkI 254
|
..
gi 1039779783 767 LK 768
Cdd:PRK13631 255 LK 256
|
|
| COG4559 |
COG4559 |
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism]; |
575-723 |
2.92e-15 |
|
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443620 [Multi-domain] Cd Length: 258 Bit Score: 77.08 E-value: 2.92e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779783 575 VNDLSLNLYEGQITVLLGHNGAGKTTTLSILTGLYLPTRGKVYISGYDISS----DMVQIRkslGLCPQD-DLLFPmLTV 649
Cdd:COG4559 17 LDDVSLTLRPGELTAIIGPNGAGKSTLLKLLTGELTPSSGEVRLNGRPLAAwspwELARRR---AVLPQHsSLAFP-FTV 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779783 650 SEhlhfycVIK------GIPLQNQSRETNRMLTSFGLLQQSNTMSKDLSGGMKRK--LSIIIALI-----GDTKVVILDE 716
Cdd:COG4559 93 EE------VVAlgraphGSSAAQDRQIVREALALVGLAHLAGRSYQTLSGGEQQRvqLARVLAQLwepvdGGPRWLFLDE 166
|
....*..
gi 1039779783 717 PTSGMDP 723
Cdd:COG4559 167 PTSALDL 173
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
575-748 |
2.95e-15 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 75.76 E-value: 2.95e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779783 575 VNDLSLNLYEGQITVLLGHNGAGKTTTLSILTGLYLPTRGKVYISGYDISSDMVQIRKSLGLCPQDDLLFPMLTVSEHLH 654
Cdd:PRK13540 17 LQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEILFERQSIKKDLCTYQKQLCFVGHRSGINPYLTLRENCL 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779783 655 FycvikGIPLQNQSRETNRMLTSFGLLQQSNTMSKDLSGGMKRKLSIIIALIGDTKVVILDEPTSGMDPVSRRATWDLLQ 734
Cdd:PRK13540 97 Y-----DIHFSPGAVGITELCRLFSLEHLIDYPCGLLSSGQKRQVALLRLWMSKAKLWLLDEPLVALDELSLLTIITKIQ 171
|
170
....*....|....*
gi 1039779783 735 -HYKKDRTILLTTHH 748
Cdd:PRK13540 172 eHRAKGGAVLLTSHQ 186
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
575-722 |
4.24e-15 |
|
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: 74.99 E-value: 4.24e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779783 575 VNDLSLNLYEGQITVLLGHNGAGKTTTLSILTGL---YLPTRGKVYISGYDISSDMVQIRKSLGLCPQDDLLFPMLTVSE 651
Cdd:cd03233 23 LKDFSGVVKPGEMVLVLGRPGSGCSTLLKALANRtegNVSVEGDIHYNGIPYKEFAEKYPGEIIYVSEEDVHFPTLTVRE 102
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1039779783 652 HLHFYCVIKGiplqnqsretnrmltsfgllqqsNTMSKDLSGGMKRKLSIIIALIGDTKVVILDEPTSGMD 722
Cdd:cd03233 103 TLDFALRCKG-----------------------NEFVRGISGGERKRVSIAEALVSRASVLCWDNSTRGLD 150
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
556-752 |
5.20e-15 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 77.05 E-value: 5.20e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779783 556 IRIQHLYKEFILKNST-LMAVNDLSLNLYEGQITVLLGHNGAGKTTTLSILTGLYLPTRGKVYISGYDISSDMV------ 628
Cdd:PRK13651 3 IKVKNIVKIFNKKLPTeLKALDNVSVEINQGEFIAIIGQTGSGKTTFIEHLNALLLPDTGTIEWIFKDEKNKKKtkekek 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779783 629 -------------------QIRKSLGLCPQ--DDLLFPMlTVSEHLHFYCVIKGIPLQNQSRETNRMLTSFGL----LQQ 683
Cdd:PRK13651 83 vleklviqktrfkkikkikEIRRRVGVVFQfaEYQLFEQ-TIEKDIIFGPVSMGVSKEEAKKRAAKYIELVGLdesyLQR 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779783 684 SntmSKDLSGGMKRKLSIIIALIGDTKVVILDEPTSGMDPVSRRATWDLLQH-YKKDRTILLTTHHMDEA 752
Cdd:PRK13651 162 S---PFELSGGQKRRVALAGILAMEPDFLVFDEPTAGLDPQGVKEILEIFDNlNKQGKTIILVTHDLDNV 228
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
543-747 |
5.30e-15 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 79.34 E-value: 5.30e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779783 543 DFMEPEPVG-LVagIRIQHLYKEF----ILKnstlmavnDLSLNLYEGQITVLLGHNGAGKTTTLSILTGLYLPTRGKVY 617
Cdd:COG0488 304 RFPPPERLGkKV--LELEGLSKSYgdktLLD--------DLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPDSGTVK 373
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779783 618 IsgydisSDMVQIrkslGLCPQD-DLLFPMLTVSEHLHfycvikgiPLQNQSRETN--RMLTSFGLL-QQSNTMSKDLSG 693
Cdd:COG0488 374 L------GETVKI----GYFDQHqEELDPDKTVLDELR--------DGAPGGTEQEvrGYLGRFLFSgDDAFKPVGVLSG 435
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1039779783 694 GMKRKLSIIIALIGDTKVVILDEPTSGMDPVSRRATWDLLQHYKKdrTILLTTH 747
Cdd:COG0488 436 GEKARLALAKLLLSPPNVLLLDEPTNHLDIETLEALEEALDDFPG--TVLLVSH 487
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
556-750 |
6.65e-15 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 75.50 E-value: 6.65e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779783 556 IRIQHLYKEFIL---KNSTLM---------------AVNDLSLNLYEGQITVLLGHNGAGKTTTLSILTGLYLPTRGKVY 617
Cdd:COG1134 5 IEVENVSKSYRLyhePSRSLKelllrrrrtrreefwALKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTSGRVE 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779783 618 ISGYdISSdmvqirkslglcpqddLL-----F-PMLTVSEHLHFYCVIKGIPLqnqsRETNRML---TSF-GLLQQSNTM 687
Cdd:COG1134 85 VNGR-VSA----------------LLelgagFhPELTGRENIYLNGRLLGLSR----KEIDEKFdeiVEFaELGDFIDQP 143
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1039779783 688 SKDLSGGMKRKL--SIIIALigDTKVVILDEPTSGMDPV-SRRATwDLLQHYKKD-RTILLTTHHMD 750
Cdd:COG1134 144 VKTYSSGMRARLafAVATAV--DPDILLVDEVLAVGDAAfQKKCL-ARIRELRESgRTVIFVSHSMG 207
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
574-723 |
7.45e-15 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 75.44 E-value: 7.45e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779783 574 AVNDLSLNLYEGQITVLLGHNGAGKTTTLSILTGLYLPTRGKVYISG--YDISS-----DMVQIRKSLGLCPQDDLLFPM 646
Cdd:PRK11124 17 ALFDITLDCPQGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLNIAGnhFDFSKtpsdkAIRELRRNVGMVFQQYNLWPH 96
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1039779783 647 LTVSEHL-HFYCVIKGIPLQNQSRETNRMLTSFGLLQQSNTMSKDLSGGMKRKLSIIIALIGDTKVVILDEPTSGMDP 723
Cdd:PRK11124 97 LTVQQNLiEAPCRVLGLSKDQALARAEKLLERLRLKPYADRFPLHLSGGQQQRVAIARALMMEPQVLLFDEPTAALDP 174
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
556-782 |
1.16e-14 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 75.12 E-value: 1.16e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779783 556 IRIQHLYKEFilknSTLMAVNDLSLNLYEGQITVLLGHNGAGKTTTLSILTGLYLPTRGKVYISGYDISS-DMVQIRKSL 634
Cdd:COG4604 2 IEIKNVSKRY----GGKVVLDDVSLTIPKGGITALIGPNGAGKSTLLSMISRLLPPDSGEVLVDGLDVATtPSRELAKRL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779783 635 GLCPQDDLLFPMLTVSEHLHF----YCviKGIPLQNQSRETNRMLTSFGLLQQSNTMSKDLSGGMKRKLSIIIALIGDTK 710
Cdd:COG4604 78 AILRQENHINSRLTVRELVAFgrfpYS--KGRLTAEDREIIDEAIAYLDLEDLADRYLDELSGGQRQRAFIAMVLAQDTD 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779783 711 VVILDEPTSGMDP---VS-----RRATWDLlqhykkDRTILLTTHHMDEADVLGDRIAILVMGILKCCGS------SLFL 776
Cdd:COG4604 156 YVLLDEPLNNLDMkhsVQmmkllRRLADEL------GKTVVIVLHDINFASCYADHIVAMKDGRVVAQGTpeeiitPEVL 229
|
....*.
gi 1039779783 777 KKLYGV 782
Cdd:COG4604 230 SDIYDT 235
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
576-772 |
1.36e-14 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 76.66 E-value: 1.36e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779783 576 NDLSLNLYEGQITVLLGHNGAGKTTTLSILTGLYLPTRGKVYISGYDISSDMVQIRKsLGLCPQDDLLFPMLTVSEHLHF 655
Cdd:PRK10851 19 NDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFHGTDVSRLHARDRK-VGFVFQHYALFRHMTVFDNIAF 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779783 656 YcvIKGIPLQNQ------SRETNRMLTSFGLLQQSNTMSKDLSGGMKRKLSIIIALIGDTKVVILDEPTSGMDPVSRRA- 728
Cdd:PRK10851 98 G--LTVLPRRERpnaaaiKAKVTQLLEMVQLAHLADRYPAQLSGGQKQRVALARALAVEPQILLLDEPFGALDAQVRKEl 175
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1039779783 729 -TWDLLQHYKKDRTILLTTHHMDEADVLGDRIAILVMGILKCCGS 772
Cdd:PRK10851 176 rRWLRQLHEELKFTSVFVTHDQEEAMEVADRVVVMSQGNIEQAGT 220
|
|
| nickel_nikE |
TIGR02769 |
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a ... |
558-762 |
3.25e-14 |
|
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a multisubunit nickel import ABC transporter complex. Nickel, once imported, may be used in urease and in certain classes of hydrogenase and superoxide dismutase. [Transport and binding proteins, Cations and iron carrying compounds]
Pssm-ID: 131816 [Multi-domain] Cd Length: 265 Bit Score: 74.07 E-value: 3.25e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779783 558 IQHLYKE--FILKNSTLMAVNDLSLNLYEGQITVLLGHNGAGKTTTLSILTGLYLPTRGKVYISGYDIS----SDMVQIR 631
Cdd:TIGR02769 8 VTHTYRTggLFGAKQRAPVLTNVSLSIEEGETVGLLGRSGCGKSTLARLLLGLEKPAQGTVSFRGQDLYqldrKQRRAFR 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779783 632 KSLGLCPQDDL--LFPMLTVSEhlhfycvIKGIPLQN--------QSRETNRMLTSFGLlqQSNTMSK---DLSGGMKRK 698
Cdd:TIGR02769 88 RDVQLVFQDSPsaVNPRMTVRQ-------IIGEPLRHltsldeseQKARIAELLDMVGL--RSEDADKlprQLSGGQLQR 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1039779783 699 LSIIIALIGDTKVVILDEPTSGMDPVSRRATWDLLQHYKKDRTI--LLTTHHMDEADVLGDRIAIL 762
Cdd:TIGR02769 159 INIARALAVKPKLIVLDEAVSNLDMVLQAVILELLRKLQQAFGTayLFITHDLRLVQSFCQRVAVM 224
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
576-763 |
4.18e-14 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 73.56 E-value: 4.18e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779783 576 NDLSLNLYEGQITVLLGHNGAGKTTTLSILTGLYLPTRGKVyISGydiSSDMVQIRKSLGLCPQDDLLFPMLTVSEHLhf 655
Cdd:PRK11247 29 NQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAGEL-LAG---TAPLAEAREDTRLMFQDARLLPWKKVIDNV-- 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779783 656 ycvikGIPLQNQSRE-TNRMLTSFGLLQQSNTMSKDLSGGMKRKLSIIIALIGDTKVVILDEPTSGMDPVSRRATWDLL- 733
Cdd:PRK11247 103 -----GLGLKGQWRDaALQALAAVGLADRANEWPAALSGGQKQRVALARALIHRPGLLLLDEPLGALDALTRIEMQDLIe 177
|
170 180 190
....*....|....*....|....*....|....
gi 1039779783 734 ----QHykkDRTILLTTHHMDEADVLGDRIaILV 763
Cdd:PRK11247 178 slwqQH---GFTVLLVTHDVSEAVAMADRV-LLI 207
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
556-747 |
5.30e-14 |
|
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: 70.17 E-value: 5.30e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779783 556 IRIQHLYKEFilKNSTLMavNDLSLNLYEGQITVLLGHNGAGKTTTLSILTGLYLPTrgkvyisgydissdmvqirkslg 635
Cdd:cd03221 1 IELENLSKTY--GGKLLL--KDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPD----------------------- 53
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779783 636 lcpqddllfpmltvsehlhfycviKGIPLQNQSretnrmlTSFGLLQQsntmskdLSGGMKRKLSIIIALIGDTKVVILD 715
Cdd:cd03221 54 ------------------------EGIVTWGST-------VKIGYFEQ-------LSGGEKMRLALAKLLLENPNLLLLD 95
|
170 180 190
....*....|....*....|....*....|..
gi 1039779783 716 EPTSGMDPVSRRATWDLLQHYKkdRTILLTTH 747
Cdd:cd03221 96 EPTNHLDLESIEALEEALKEYP--GTVILVSH 125
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
575-772 |
6.27e-14 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 72.88 E-value: 6.27e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779783 575 VNDLSLNLYEGQITVLLGHNGAGKTTTLSILTGLYLPTRGKVYISGYDISS----DMVQIRKSLglcPQD-DLLFPmLTV 649
Cdd:PRK13548 18 LDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLNGRPLADwspaELARRRAVL---PQHsSLSFP-FTV 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779783 650 SEhlhfycVIK--GIPLQNQSRETNR----MLTSFGLLQQSNTMSKDLSGGMK------RKLSIIIALIGDTKVVILDEP 717
Cdd:PRK13548 94 EE------VVAmgRAPHGLSRAEDDAlvaaALAQVDLAHLAGRDYPQLSGGEQqrvqlaRVLAQLWEPDGPPRWLLLDEP 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1039779783 718 TSGMDPVSRRATWDLLQHYKKDR--TILLTTHHMDEADVLGDRIAILVMGILKCCGS 772
Cdd:PRK13548 168 TSALDLAHQHHVLRLARQLAHERglAVIVVLHDLNLAARYADRIVLLHQGRLVADGT 224
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
551-765 |
7.28e-14 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 74.39 E-value: 7.28e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779783 551 GLVAGIRIQHLYKEFilknSTLMAVNDLSLNLYEGQITVLLGHNGAGKTTTlSILTGLYLPTRGKVYISGYDISSDMVQI 630
Cdd:NF000106 9 GARNAVEVRGLVKHF----GEVKAVDGVDLDVREGTVLGVLGP*GAA**RG-ALPAHV*GPDAGRRPWRF*TWCANRRAL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779783 631 RKSLGLC-PQDDLLFPMLTVSEHLHFYCVIKGIPLQNQSRETNRMLTSFGLLQQSNTMSKDLSGGMKRKLSIIIALIGDT 709
Cdd:NF000106 84 RRTIG*HrPVR*GRRESFSGRENLYMIGR*LDLSRKDARARADELLERFSLTEAAGRAAAKYSGGMRRRLDLAASMIGRP 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1039779783 710 KVVILDEPTSGMDPVSRRATWDLLQHYKKD-RTILLTTHHMDEADVLGDRIAILVMG 765
Cdd:NF000106 164 AVLYLDEPTTGLDPRTRNEVWDEVRSMVRDgATVLLTTQYMEEAEQLAHELTVIDRG 220
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
565-764 |
1.14e-13 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 73.59 E-value: 1.14e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779783 565 FILKNSTLMAVNDLSLNLYEGQITVLLGHNGAGKTTTLSILTGLYLPTRGKVYISGYDI----SSDMVQIRKSLGLCPQD 640
Cdd:PRK15079 27 FWQPPKTLKAVDGVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGEVAWLGKDLlgmkDDEWRAVRSDIQMIFQD 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779783 641 DL--LFPMLTVSEhlhfycvIKGIPLQ----NQSRETNR-----MLTSFGLL-QQSNTMSKDLSGGMKRKLSIIIALIGD 708
Cdd:PRK15079 107 PLasLNPRMTIGE-------IIAEPLRtyhpKLSRQEVKdrvkaMMLKVGLLpNLINRYPHEFSGGQCQRIGIARALILE 179
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1039779783 709 TKVVILDEPTSGMDpVSRRA-TWDLLQHYKKDRTILLTTHHMDEADV--LGDRiaILVM 764
Cdd:PRK15079 180 PKLIICDEPVSALD-VSIQAqVVNLLQQLQREMGLSLIFIAHDLAVVkhISDR--VLVM 235
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
585-748 |
1.18e-13 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 75.30 E-value: 1.18e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779783 585 GQITVLLGHNGAGKTTTLSILTGLYLPT--RGKVYISGYDISSdmvQIRKSLGLCPQDDLLFPMLTVSEHLHFYCVI--- 659
Cdd:PLN03211 94 GEILAVLGPSGSGKSTLLNALAGRIQGNnfTGTILANNRKPTK---QILKRTGFVTQDDILYPHLTVRETLVFCSLLrlp 170
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779783 660 KGIPLQNQSRETNRMLTSFGLLQQSNTMS-----KDLSGGMKRKLSIIIALIGDTKVVILDEPTSGMDPVSR-RATWDLL 733
Cdd:PLN03211 171 KSLTKQEKILVAESVISELGLTKCENTIIgnsfiRGISGGERKRVSIAHEMLINPSLLILDEPTSGLDATAAyRLVLTLG 250
|
170
....*....|....*
gi 1039779783 734 QHYKKDRTILLTTHH 748
Cdd:PLN03211 251 SLAQKGKTIVTSMHQ 265
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
576-762 |
1.70e-13 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 73.53 E-value: 1.70e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779783 576 NDLSLNLYEGQITVLLGHNGAGKTTTLSILTGLYLPTRGKVYISGYDISsDMVQIRKSLGLCPQDDLLFPMLTVSEHLHF 655
Cdd:PRK11000 20 KDINLDIHEGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLFIGEKRMN-DVPPAERGVGMVFQSYALYPHLSVAENMSF 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779783 656 YCVIKGI---PLQNQSRETNRMLTSFGLLQQSntmSKDLSGGMKRKLSIIIALIGDTKVVILDEPTSGMDP---VSRRAT 729
Cdd:PRK11000 99 GLKLAGAkkeEINQRVNQVAEVLQLAHLLDRK---PKALSGGQRQRVAIGRTLVAEPSVFLLDEPLSNLDAalrVQMRIE 175
|
170 180 190
....*....|....*....|....*....|...
gi 1039779783 730 WDLLqHYKKDRTILLTTHHMDEADVLGDRIAIL 762
Cdd:PRK11000 176 ISRL-HKRLGRTMIYVTHDQVEAMTLADKIVVL 207
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
576-747 |
1.71e-13 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 74.33 E-value: 1.71e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779783 576 NDLSLNLYEGQITVLLGHNGAGKTTTLSILTGLYLPTRGKVYISGydissdmvqiRKSLGLCPQDDLLFPMLTVSEHlhf 655
Cdd:COG0488 15 DDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEVSIPK----------GLRIGYLPQEPPLDDDLTVLDT--- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779783 656 ycVIKGIP----------------------------LQNQSRETN---------RMLTSFGL--LQQSNTMSkDLSGGMK 696
Cdd:COG0488 82 --VLDGDAelraleaeleeleaklaepdedlerlaeLQEEFEALGgweaearaeEILSGLGFpeEDLDRPVS-ELSGGWR 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1039779783 697 RKLSIIIALIGDTKVVILDEPTSGMDPVSRRatW--DLLQHYKKdrTILLTTH 747
Cdd:COG0488 159 RRVALARALLSEPDLLLLDEPTNHLDLESIE--WleEFLKNYPG--TVLVVSH 207
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
578-747 |
2.98e-13 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 70.26 E-value: 2.98e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779783 578 LSLNLYEGQITVLLGHNGAGKTTTLSILTGLYLPTRGKVYISGYDIS-SDMVQIRKSLGLCPQddlLFPMLTVSEHLHFY 656
Cdd:PRK13543 30 LDFHVDAGEALLVQGDNGAGKTTLLRVLAGLLHVESGQIQIDGKTATrGDRSRFMAYLGHLPG---LKADLSTLENLHFL 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779783 657 CVIKGiplqnqsRETNRM----LTSFGLLQQSNTMSKDLSGGMKRKLSIIIALIGDTKVVILDEPTSGMDP-----VSRR 727
Cdd:PRK13543 107 CGLHG-------RRAKQMpgsaLAIVGLAGYEDTLVRQLSAGQKKRLALARLWLSPAPLWLLDEPYANLDLegitlVNRM 179
|
170 180
....*....|....*....|
gi 1039779783 728 ATwdllQHYKKDRTILLTTH 747
Cdd:PRK13543 180 IS----AHLRGGGAALVTTH 195
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
577-747 |
4.21e-13 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 73.60 E-value: 4.21e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779783 577 DLSLNLYEGQITVLLGHNGAGKTTTLSILTGLYLPTRGKVYISGYDISS----DMVQIRKS-LGLCPQDDLLFPMLTVSE 651
Cdd:PRK10535 26 GISLDIYAGEMVAIVGASGSGKSTLMNILGCLDKPTSGTYRVAGQDVATldadALAQLRREhFGFIFQRYHLLSHLTAAQ 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779783 652 HLHFYCVIKGIPLQNQSRETNRMLTSFGLLQQSNTMSKDLSGGMKRKLSIIIALIGDTKVVILDEPTSGMDPVSRRATWD 731
Cdd:PRK10535 106 NVEVPAVYAGLERKQRLLRAQELLQRLGLEDRVEYQPSQLSGGQQQRVSIARALMNGGQVILADEPTGALDSHSGEEVMA 185
|
170
....*....|....*..
gi 1039779783 732 LL-QHYKKDRTILLTTH 747
Cdd:PRK10535 186 ILhQLRDRGHTVIIVTH 202
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
556-747 |
4.28e-13 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 69.81 E-value: 4.28e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779783 556 IRIQHLYKEFILKNSTLMAVNDLSLNLYEGQITVLLGHNGAGKTTTLSILTGLYLPTRGKVYISGYDISS----DMVQIR 631
Cdd:PRK10584 7 VEVHHLKKSVGQGEHELSILTGVELVVKRGETIALIGESGSGKSTLLAILAGLDDGSSGEVSLVGQPLHQmdeeARAKLR 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779783 632 -KSLGLCPQDDLLFPMLTVSEHLHFYCVIKGIPlQNQSRETNR-MLTSFGLLQQSNTMSKDLSGGMKRKLSIIIALIGDT 709
Cdd:PRK10584 87 aKHVGFVFQSFMLIPTLNALENVELPALLRGES-SRQSRNGAKaLLEQLGLGKRLDHLPAQLSGGEQQRVALARAFNGRP 165
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1039779783 710 KVVILDEPTSGMDPVSRRATWDLLQHYKKDR--TILLTTH 747
Cdd:PRK10584 166 DVLFADEPTGNLDRQTGDKIADLLFSLNREHgtTLILVTH 205
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
545-728 |
1.12e-12 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 70.53 E-value: 1.12e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779783 545 MEPEPVglvagIRIQHLYKEFILKNSTLM-------AVNDLSLNLYEGQITVLLGHNGAGKTTTLSILTGLYLPTRGKVY 617
Cdd:COG4608 2 AMAEPL-----LEVRDLKKHFPVRGGLFGrtvgvvkAVDGVSFDIRRGETLGLVGESGCGKSTLGRLLLRLEEPTSGEIL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779783 618 ISGYDIS----SDMVQIRKSLGLCPQDDL--LFPMLTVSEHLHFYCVIKGI-PLQNQSRETNRMLTSFGLlqQSNTMSK- 689
Cdd:COG4608 77 FDGQDITglsgRELRPLRRRMQMVFQDPYasLNPRMTVGDIIAEPLRIHGLaSKAERRERVAELLELVGL--RPEHADRy 154
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1039779783 690 --DLSGGMKRKLSIIIALIGDTKVVILDEPTSGMDpVSRRA 728
Cdd:COG4608 155 phEFSGGQRQRIGIARALALNPKLIVCDEPVSALD-VSIQA 194
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
575-775 |
1.40e-12 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 68.96 E-value: 1.40e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779783 575 VNDLSLNLYEGQITVLLGHNGAGKTTTLSILTGLyLP-----TRGKVYISGYDISSDMVQIRKSLGLCPQDDLLF-PMLT 648
Cdd:PRK10418 19 VHGVSLTLQRGRVLALVGGSGSGKSLTCAAALGI-LPagvrqTAGRVLLDGKPVAPCALRGRKIATIMQNPRSAFnPLHT 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779783 649 VSEHLHFYCVIKGIPLQNQS----------RETNRMLTSFGLlqqsntmskDLSGGMKRKLSIIIALIGDTKVVILDEPT 718
Cdd:PRK10418 98 MHTHARETCLALGKPADDATltaaleavglENAARVLKLYPF---------EMSGGMLQRMMIALALLCEAPFIIADEPT 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1039779783 719 SGMDPVSRRATWDLLQHYKKDRT--ILLTTHHMDEADVLGDRIAILVMGILKCCGS--SLF 775
Cdd:PRK10418 169 TDLDVVAQARILDLLESIVQKRAlgMLLVTHDMGVVARLADDVAVMSHGRIVEQGDveTLF 229
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
575-764 |
1.85e-12 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 71.19 E-value: 1.85e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779783 575 VNDLSLNLYEGQITVLLGHNGAGKTTTLSILTGLYLPTRGKVYISGYDISSDmvqirkslglCPQDDL------------ 642
Cdd:PRK10762 268 VNDVSFTLRKGEILGVSGLMGAGRTELMKVLYGALPRTSGYVTLDGHEVVTR----------SPQDGLangivyisedrk 337
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779783 643 ---LFPMLTVSEHLHF----YCVIKGIPLQNQsrETNRMLTSFGLLQQSNTMSKD-----LSGGMKRKLSIIIALIGDTK 710
Cdd:PRK10762 338 rdgLVLGMSVKENMSLtalrYFSRAGGSLKHA--DEQQAVSDFIRLFNIKTPSMEqaiglLSGGNQQKVAIARGLMTRPK 415
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1039779783 711 VVILDEPTSGMDPVSRRATWDLLQHYKKD-RTILLTTHHMDEadVLG--DRiaILVM 764
Cdd:PRK10762 416 VLILDEPTRGVDVGAKKEIYQLINQFKAEgLSIILVSSEMPE--VLGmsDR--ILVM 468
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
579-765 |
1.86e-12 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 68.07 E-value: 1.86e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779783 579 SLNLYEGQITVLLGHNGAGKTTTLSILTGLYLPTRGKVYISGYDiSSDMVQIRKSLGLCPQDDLLFPMLTVSEH----LH 654
Cdd:PRK10771 19 DLTVERGERVAILGPSGAGKSTLLNLIAGFLTPASGSLTLNGQD-HTTTPPSRRPVSMLFQENNLFSHLTVAQNiglgLN 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779783 655 fycviKGIPLQNQSRET-NRMLTSFGLLQQSNTMSKDLSGGMKRKLSIIIALIGDTKVVILDEPTSGMDPVSRRATWDLL 733
Cdd:PRK10771 98 -----PGLKLNAAQREKlHAIARQMGIEDLLARLPGQLSGGQRQRVALARCLVREQPILLLDEPFSALDPALRQEMLTLV 172
|
170 180 190
....*....|....*....|....*....|....
gi 1039779783 734 QHYKKDR--TILLTTHHMDEADVLGDRIAILVMG 765
Cdd:PRK10771 173 SQVCQERqlTLLMVSHSLEDAARIAPRSLVVADG 206
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
574-765 |
1.94e-12 |
|
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The amino terminal domain (pfam03412) processes the N-terminal leader peptide from the bacteriocin while C-terminal domains resemble ABC transporter membrane protein and ATP-binding cassette domain. In general, bacteriocins are agents which are responsible for killing or inhibiting the closely related species or even different strains of the same species. Bacteriocins are usually encoded by bacterial plasmids. Bacteriocins are named after the species and hence in literature one encounters various names e.g., leucocin from Leuconostic geldium; pedicocin from Pedicoccus acidilactici; sakacin from Lactobacillus sake etc. [Protein fate, Protein and peptide secretion and trafficking, Protein fate, Protein modification and repair, Transport and binding proteins, Other]
Pssm-ID: 130261 [Multi-domain] Cd Length: 708 Bit Score: 71.69 E-value: 1.94e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779783 574 AVNDLSLNLYEGQITVLLGHNGAGKTTTLSILTGLYLPTRGKVYISGYDISS-DMVQIRKSLGLCPQDDLLFP------- 645
Cdd:TIGR01193 489 ILSDISLTIKMNSKTTIVGMSGSGKSTLAKLLVGFFQARSGEILLNGFSLKDiDRHTLRQFINYLPQEPYIFSgsilenl 568
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779783 646 MLTVSEHLHFYCVIKGIPLQNQSRETNRMltSFGLLQQSNTMSKDLSGGMKRKLSIIIALIGDTKVVILDEPTSGMDPVS 725
Cdd:TIGR01193 569 LLGAKENVSQDEIWAACEIAEIKDDIENM--PLGYQTELSEEGSSISGGQKQRIALARALLTDSKVLILDESTSNLDTIT 646
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1039779783 726 RRATWDLLQHYkKDRTILLTTHHMDEADvLGDRIAILVMG 765
Cdd:TIGR01193 647 EKKIVNNLLNL-QDKTIIFVAHRLSVAK-QSDKIIVLDHG 684
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
574-764 |
2.81e-12 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 70.43 E-value: 2.81e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779783 574 AVNDLSLNLYEGQITVLLGHNGAGKTTTLSILTGLYLPTRGKVYISG--YDISSDMVQIRKSLGLCPQDDL---LFPMLT 648
Cdd:COG1129 267 VVRDVSFSVRAGEILGIAGLVGAGRTELARALFGADPADSGEIRLDGkpVRIRSPRDAIRAGIAYVPEDRKgegLVLDLS 346
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779783 649 VSE-----HLHFYCVIKGIPLQNQSRETNRMLTSFGLLQQS-NTMSKDLSGGMKRKlsIIIA--LIGDTKVVILDEPTSG 720
Cdd:COG1129 347 IREnitlaSLDRLSRGGLLDRRRERALAEEYIKRLRIKTPSpEQPVGNLSGGNQQK--VVLAkwLATDPKVLILDEPTRG 424
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1039779783 721 MDPVSRRATWDLLQHYKKD-RTILLTTHHMDEadVLG--DRiaILVM 764
Cdd:COG1129 425 IDVGAKAEIYRLIRELAAEgKAVIVISSELPE--LLGlsDR--ILVM 467
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
552-760 |
3.45e-12 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 68.14 E-value: 3.45e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779783 552 LVAGIRIqhlyKEFILKNSTLMAVNDLSLNLYEGQITVLLGHNGAGKTTTLSILTGLY-----LPTRGKVYISGYDISSD 626
Cdd:PRK14258 4 LIPAIKV----NNLSFYYDTQKILEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLNRMNeleseVRVEGRVEFFNQNIYER 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779783 627 MVQI---RKSLGLCPQDDLLFPMlTVSEHLHFYCVIKGI-PLQNQSRETNRMLTSFGLLQQ-SNTMSK---DLSGGMKRK 698
Cdd:PRK14258 80 RVNLnrlRRQVSMVHPKPNLFPM-SVYDNVAYGVKIVGWrPKLEIDDIVESALKDADLWDEiKHKIHKsalDLSGGQQQR 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1039779783 699 LSIIIALIGDTKVVILDEPTSGMDPVSRRATWDLLQHY--KKDRTILLTTHHMDEADVLGDRIA 760
Cdd:PRK14258 159 LCIARALAVKPKVLLMDEPCFGLDPIASMKVESLIQSLrlRSELTMVIVSHNLHQVSRLSDFTA 222
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
574-764 |
3.53e-12 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 70.38 E-value: 3.53e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779783 574 AVNDLSLNLYEGQITVLLGHNGAGKTTTLSILTGLYLPTRGKVYISGYDISSDMVQ-IRKSLGLCPQDDLLFPMlTVSEH 652
Cdd:PRK13657 350 GVEDVSFEAKPGQTVAIVGPTGAGKSTLINLLQRVFDPQSGRILIDGTDIRTVTRAsLRRNIAVVFQDAGLFNR-SIEDN 428
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779783 653 LHFycvikGIPlqNQSREtnRMLTSFGLLQQS----------NTM----SKDLSGGMKRKLSIIIALIGDTKVVILDEPT 718
Cdd:PRK13657 429 IRV-----GRP--DATDE--EMRAAAERAQAHdfierkpdgyDTVvgerGRQLSGGERQRLAIARALLKDPPILILDEAT 499
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1039779783 719 SGMDPVSRRATWDLLQHYKKDRTILLTTHHMD---EADVlgdriaILVM 764
Cdd:PRK13657 500 SALDVETEAKVKAALDELMKGRTTFIIAHRLStvrNADR------ILVF 542
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
575-771 |
4.89e-12 |
|
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular trafficking, secretion, and vesicular transport];
Pssm-ID: 443660 [Multi-domain] Cd Length: 563 Bit Score: 69.78 E-value: 4.89e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779783 575 VNDLSLNLYEGQITVLLGHNGAGKTTTLSILTGLYLPTRGKVYISGYDISS-DMVQIRKSLGLCPQDDLLFPMlTVSEhl 653
Cdd:COG4618 348 LRGVSFSLEPGEVLGVIGPSGSGKSTLARLLVGVWPPTAGSVRLDGADLSQwDREELGRHIGYLPQDVELFDG-TIAE-- 424
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779783 654 hfycvikgiplqNQSR-----------------------------ETnrMLTSFGLLqqsntmskdLSGGMKRKLSIIIA 704
Cdd:COG4618 425 ------------NIARfgdadpekvvaaaklagvhemilrlpdgyDT--RIGEGGAR---------LSGGQRQRIGLARA 481
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779783 705 LIGDTKVVILDEPTSGMDPVSRRATWDLLQHYKKD-RTILLTTHHMdeaDVLG--DRIAILVMGILKCCG 771
Cdd:COG4618 482 LYGDPRLVVLDEPNSNLDDEGEAALAAAIRALKARgATVVVITHRP---SLLAavDKLLVLRDGRVQAFG 548
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
574-718 |
5.53e-12 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 69.65 E-value: 5.53e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779783 574 AVNDLSLNLYEGQITVLLGHNGAGKTTTLSILTGLYLPTRGKVYISGYDISSDmvQIRKS----LGLCPQDDLLFPMLTV 649
Cdd:PRK10762 19 ALSGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSILYLGKEVTFN--GPKSSqeagIGIIHQELNLIPQLTI 96
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1039779783 650 SEHL----HFYCVIKGIPLQNQSRETNRMLTSFGLLQQSNTMSKDLSGGMKRKLSIIIALIGDTKVVILDEPT 718
Cdd:PRK10762 97 AENIflgrEFVNRFGRIDWKKMYAEADKLLARLNLRFSSDKLVGELSIGEQQMVEIAKVLSFESKVIIMDEPT 169
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
546-772 |
9.83e-12 |
|
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: 68.70 E-value: 9.83e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779783 546 EPEPVGLVAgIRIQHLYKEFILkNSTLMAVNDLSLNLYEGQITVLLGHNGAGKTTTLSILTGLYlPTR--GKVYISGY-- 621
Cdd:TIGR02633 249 EPHEIGDVI-LEARNLTCWDVI-NPHRKRVDDVSFSLRRGEILGVAGLVGAGRTELVQALFGAY-PGKfeGNVFINGKpv 325
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779783 622 DISSDMVQIRKSLGLCPQD---DLLFPMLTVSEH-----LHFYCVIKGIplqNQSRETNRMLTSFGLLQqSNTMSKDL-- 691
Cdd:TIGR02633 326 DIRNPAQAIRAGIAMVPEDrkrHGIVPILGVGKNitlsvLKSFCFKMRI---DAAAELQIIGSAIQRLK-VKTASPFLpi 401
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779783 692 ---SGGMKRKLSIIIALIGDTKVVILDEPTSGMDPVSRRATWDLL-QHYKKDRTILLTTHHMDEADVLGDRiaILVMGIL 767
Cdd:TIGR02633 402 grlSGGNQQKAVLAKMLLTNPRVLILDEPTRGVDVGAKYEIYKLInQLAQEGVAIIVVSSELAEVLGLSDR--VLVIGEG 479
|
....*
gi 1039779783 768 KCCGS 772
Cdd:TIGR02633 480 KLKGD 484
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
575-767 |
1.10e-11 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 66.66 E-value: 1.10e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779783 575 VNDLSLNLYEGQITVLLGHNGAGKTTTLSILTGLYLPTRGKVY-----ISGYDISS--DMVQIRKSLGLCPQDDLLFPML 647
Cdd:PRK14271 37 LDQVSMGFPARAVTSLMGPTGSGKTTFLRTLNRMNDKVSGYRYsgdvlLGGRSIFNyrDVLEFRRRVGMLFQRPNPFPMS 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779783 648 TVSEHLHFYCVIKGIPLQNQSRETNRMLTSFGLLQQSNTMSKD----LSGGMKRKLSIIIALIGDTKVVILDEPTSGMDP 723
Cdd:PRK14271 117 IMDNVLAGVRAHKLVPRKEFRGVAQARLTEVGLWDAVKDRLSDspfrLSGGQQQLLCLARTLAVNPEVLLLDEPTSALDP 196
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1039779783 724 VSRRATWDLLQHYKKDRTILLTTHHMDEADVLGDRIAILVMGIL 767
Cdd:PRK14271 197 TTTEKIEEFIRSLADRLTVIIVTHNLAQAARISDRAALFFDGRL 240
|
|
| SufC |
COG0396 |
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, ... |
576-748 |
1.53e-11 |
|
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440165 [Multi-domain] Cd Length: 245 Bit Score: 65.47 E-value: 1.53e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779783 576 NDLSLNLYEGQITVLLGHNGAGKTTTLSILTGL--YLPTRGKVYISGYDISSDMVQIR--KSLGLCPQDDLLFPMLTVSE 651
Cdd:COG0396 17 KGVNLTIKPGEVHAIMGPNGSGKSTLAKVLMGHpkYEVTSGSILLDGEDILELSPDERarAGIFLAFQYPVEIPGVSVSN 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779783 652 HLHfycvikgIPLQNQSRETNRMLTSFGLLQQSNT---MSKD---------LSGGMKRKLSIIIALIGDTKVVILDEPTS 719
Cdd:COG0396 97 FLR-------TALNARRGEELSAREFLKLLKEKMKelgLDEDfldryvnegFSGGEKKRNEILQMLLLEPKLAILDETDS 169
|
170 180 190
....*....|....*....|....*....|....*
gi 1039779783 720 GMD-----PVSrratwDLLQHYK-KDRTILLTTHH 748
Cdd:COG0396 170 GLDidalrIVA-----EGVNKLRsPDRGILIITHY 199
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
577-764 |
1.93e-11 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 67.77 E-value: 1.93e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779783 577 DLSLNLYEGQITVLLGHNGAGKTTTLSILTGLYLPTRGKVYISGYDISSDMVQIRKSLGLC--PQDDL---LF---PM-- 646
Cdd:PRK15439 281 NISLEVRAGEILGLAGVVGAGRTELAETLYGLRPARGGRIMLNGKEINALSTAQRLARGLVylPEDRQssgLYldaPLaw 360
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779783 647 ----LTVSEhLHFYcvikgiplQNQSRET---NRMLTSFGL-LQQSNTMSKDLSGGMKRKLSIIIALIGDTKVVILDEPT 718
Cdd:PRK15439 361 nvcaLTHNR-RGFW--------IKPARENavlERYRRALNIkFNHAEQAARTLSGGNQQKVLIAKCLEASPQLLIVDEPT 431
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1039779783 719 SGMDPVSRRATWDLLQHYKKDRT-ILLTTHHMDEADVLGDRiaILVM 764
Cdd:PRK15439 432 RGVDVSARNDIYQLIRSIAAQNVaVLFISSDLEEIEQMADR--VLVM 476
|
|
| PRK13546 |
PRK13546 |
teichoic acids export ABC transporter ATP-binding subunit TagH; |
568-768 |
2.42e-11 |
|
teichoic acids export ABC transporter ATP-binding subunit TagH;
Pssm-ID: 184131 [Multi-domain] Cd Length: 264 Bit Score: 65.61 E-value: 2.42e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779783 568 KNSTLMAVNDLSLNLYEGQITVLLGHNGAGKTTTLSILTGLYLPTRGKVYISGydissDMVQIRKSLGLCPQddllfpmL 647
Cdd:PRK13546 33 KNKTFFALDDISLKAYEGDVIGLVGINGSGKSTLSNIIGGSLSPTVGKVDRNG-----EVSVIAISAGLSGQ-------L 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779783 648 TVSEHLHFYCVIKGIPLQNQSRETNRMLTSFGLLQQSNTMSKDLSGGMKRKLSIIIALIGDTKVVILDEPTSGMDPVSRR 727
Cdd:PRK13546 101 TGIENIEFKMLCMGFKRKEIKAMTPKIIEFSELGEFIYQPVKKYSSGMRAKLGFSINITVNPDILVIDEALSVGDQTFAQ 180
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1039779783 728 ATWDLLQHYK-KDRTILLTTHHMDEADVLGDRIAILVMGILK 768
Cdd:PRK13546 181 KCLDKIYEFKeQNKTIFFVSHNLGQVRQFCTKIAWIEGGKLK 222
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
574-747 |
2.61e-11 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 67.74 E-value: 2.61e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779783 574 AVNDLSLNLYEGQITVLLGHNGAGKTTTLSILTGLYLPTRGKVYISGYDISS-DMVQIRKSLGLCPQDDLLFPMlTVSEH 652
Cdd:PRK11176 358 ALRNINFKIPAGKTVALVGRSGSGKSTIANLLTRFYDIDEGEILLDGHDLRDyTLASLRNQVALVSQNVHLFND-TIANN 436
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779783 653 LHFYC--------VIKGIPLQNQSRETNRMLTSFGLLQQSNTMSkdLSGGMKRKLSIIIALIGDTKVVILDEPTSGMDPV 724
Cdd:PRK11176 437 IAYARteqysreqIEEAARMAYAMDFINKMDNGLDTVIGENGVL--LSGGQRQRIAIARALLRDSPILILDEATSALDTE 514
|
170 180
....*....|....*....|...
gi 1039779783 725 SRRATWDLLQHYKKDRTILLTTH 747
Cdd:PRK11176 515 SERAIQAALDELQKNRTSLVIAH 537
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
575-765 |
3.13e-11 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 66.79 E-value: 3.13e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779783 575 VNDLSLNLYEGQITVLLGHNGAGKTTTLSILTGLYLPTRGKVYISGYDISS-DMVQIRKSLGLCPQDDLL---FPMLTVS 650
Cdd:PRK09536 19 LDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGDDVEAlSARAASRRVASVPQDTSLsfeFDVRQVV 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779783 651 E-----HLHFYcvikGIPLQNQSRETNRMLTSFGLLQQSNTMSKDLSGGMKRKLSIIIALIGDTKVVILDEPTSGMDPVS 725
Cdd:PRK09536 99 EmgrtpHRSRF----DTWTETDRAAVERAMERTGVAQFADRPVTSLSGGERQRVLLARALAQATPVLLLDEPTASLDINH 174
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1039779783 726 RRATWDLLQHYKKD-RTILLTTHHMDEADVLGDRIAILVMG 765
Cdd:PRK09536 175 QVRTLELVRRLVDDgKTAVAAIHDLDLAARYCDELVLLADG 215
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
578-764 |
3.26e-11 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 67.18 E-value: 3.26e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779783 578 LSLNLYEGQITVLLGHNGAGKTTTLSILTGlYLPTRGKVYISGYDISS-DMVQIRKSLGLCPQDDLLFPMlTVSEHLhfy 656
Cdd:PRK11174 369 LNFTLPAGQRIALVGPSGAGKTSLLNALLG-FLPYQGSLKINGIELRElDPESWRKHLSWVGQNPQLPHG-TLRDNV--- 443
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779783 657 cvikgipLQNQSRETNRMLTSfgLLQQS-------------NTMSKD----LSGGMKRKLSIIIALIGDTKVVILDEPTS 719
Cdd:PRK11174 444 -------LLGNPDASDEQLQQ--ALENAwvseflpllpqglDTPIGDqaagLSVGQAQRLALARALLQPCQLLLLDEPTA 514
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1039779783 720 GMDPVSRRATWDLLQHYKKDRTILLTTHHMDEadvLGDRIAILVM 764
Cdd:PRK11174 515 SLDAHSEQLVMQALNAASRRQTTLMVTHQLED---LAQWDQIWVM 556
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
577-752 |
3.62e-11 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 65.01 E-value: 3.62e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779783 577 DLSLNLYEGQITVLLGHNGAGKTTTLSILTGLYLPTRGKVYISGYDISS-DMVQIRKSLGLCPQDDLLFPMLTVSEhlhf 655
Cdd:PRK10253 25 NLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIQHyASKEVARRIGLLAQNATTPGDITVQE---- 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779783 656 yCVIKG----IPLQNQSRE-----TNRMLTSFGLLQQSNTMSKDLSGGMKRKLSIIIALIGDTKVVILDEPTSGMDPVSR 726
Cdd:PRK10253 101 -LVARGryphQPLFTRWRKedeeaVTKAMQATGITHLADQSVDTLSGGQRQRAWIAMVLAQETAIMLLDEPTTWLDISHQ 179
|
170 180
....*....|....*....|....*...
gi 1039779783 727 RATWDLLQHYKKDR--TILLTTHHMDEA 752
Cdd:PRK10253 180 IDLLELLSELNREKgyTLAAVLHDLNQA 207
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
578-765 |
1.24e-10 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 63.49 E-value: 1.24e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779783 578 LSLNLYEGQITVLLGHNGAGKTTTLSILTGLYLPTRGKVYISG--YDISS-DMVQIRKSLGLCPQD-DLLFPMLTVSEHL 653
Cdd:PRK13638 20 LNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLRPQKGAVLWQGkpLDYSKrGLLALRQQVATVFQDpEQQIFYTDIDSDI 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779783 654 HFYCVIKGIPLQNQSRETNRMLTSFGLLQQSNTMSKDLSGGMKRKLSIIIALIGDTKVVILDEPTSGMDPVSRRATWDLL 733
Cdd:PRK13638 100 AFSLRNLGVPEAEITRRVDEALTLVDAQHFRHQPIQCLSHGQKKRVAIAGALVLQARYLLLDEPTAGLDPAGRTQMIAII 179
|
170 180 190
....*....|....*....|....*....|...
gi 1039779783 734 QH-YKKDRTILLTTHHMDEADVLGDRIAILVMG 765
Cdd:PRK13638 180 RRiVAQGNHVIISSHDIDLIYEISDAVYVLRQG 212
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
568-764 |
2.05e-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: 2.05e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779783 568 KNSTLMAVNDLSLNLYEGQITVLLGHNGAGKTTTLSILTGLYLPTRGKVYISGydissdmvqirkSLGLCPQDDLLFPMl 647
Cdd:cd03250 14 EQETSFTLKDINLEVPKGELVAIVGPVGSGKSSLLSALLGELEKLSGSVSVPG------------SIAYVSQEPWIQNG- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779783 648 TVSEHLHFycvikGIPLQNQsrETNRMLTSFGLLQQSNTMSK-D----------LSGGMKRKLSIIIALIGDTKVVILDE 716
Cdd:cd03250 81 TIRENILF-----GKPFDEE--RYEKVIKACALEPDLEILPDgDlteigekginLSGGQKQRISLARAVYSDADIYLLDD 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1039779783 717 PTSGMDPVSRRATWD--LLQHYKKDRTILLTTHHMD---EADvlgdriAILVM 764
Cdd:cd03250 154 PLSAVDAHVGRHIFEncILGLLLNNKTRILVTHQLQllpHAD------QIVVL 200
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
578-768 |
2.99e-10 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 61.91 E-value: 2.99e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779783 578 LSLNLYEGQITVLLGHNGAGKTTTLSILTGLYLPTRGKVYISGYDIS-----------SDMVQI---RKSLGLCPQDDLL 643
Cdd:PRK10619 24 VSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNGQTINlvrdkdgqlkvADKNQLrllRTRLTMVFQHFNL 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779783 644 FPMLTVSEHLHFYCV-IKGIPLQNQSRETNRMLTSFGLLQQSN-TMSKDLSGGMKRKLSIIIALIGDTKVVILDEPTSGM 721
Cdd:PRK10619 104 WSHMTVLENVMEAPIqVLGLSKQEARERAVKYLAKVGIDERAQgKYPVHLSGGQQQRVSIARALAMEPEVLLFDEPTSAL 183
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1039779783 722 DPVSRRATWDLLQHYKKD-RTILLTTHHMDEADVLGDRIAILVMGILK 768
Cdd:PRK10619 184 DPELVGEVLRIMQQLAEEgKTMVVVTHEMGFARHVSSHVIFLHQGKIE 231
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
575-747 |
3.43e-10 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 61.67 E-value: 3.43e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779783 575 VNDLSLNLYEGQITVLLGHNGAGKTTTLSILTGLYLPTRGKVYISGydissdmvQIRksLGLCPQD---DLLFPmLTVSE 651
Cdd:PRK09544 20 LSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIKRNG--------KLR--IGYVPQKlylDTTLP-LTVNR 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779783 652 HLHFY-CVIKGIPLQNQSRetnrmLTSFGLLQQSntMSKdLSGGMKRKLSIIIALIGDTKVVILDEPTSGMDPVSRRATW 730
Cdd:PRK09544 89 FLRLRpGTKKEDILPALKR-----VQAGHLIDAP--MQK-LSGGETQRVLLARALLNRPQLLVLDEPTQGVDVNGQVALY 160
|
170
....*....|....*....
gi 1039779783 731 DLLQHYKK--DRTILLTTH 747
Cdd:PRK09544 161 DLIDQLRRelDCAVLMVSH 179
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
574-764 |
5.15e-10 |
|
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: 63.16 E-value: 5.15e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779783 574 AVNDLSLNLYEGQITVLLGHNGAGKTTT-LSILtGLyLPTRGKVYISGYDIS----SDMVQIRKSLGLCPQDDL--LFPM 646
Cdd:COG4172 301 AVDGVSLTLRRGETLGLVGESGSGKSTLgLALL-RL-IPSEGEIRFDGQDLDglsrRALRPLRRRMQVVFQDPFgsLSPR 378
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779783 647 LTVSE------HLHfycvikGIPLQNQSRET--NRMLTSFGLlqQSNTMSK---DLSGGMKRKLSIIIALIGDTKVVILD 715
Cdd:COG4172 379 MTVGQiiaeglRVH------GPGLSAAERRArvAEALEEVGL--DPAARHRyphEFSGGQRQRIAIARALILEPKLLVLD 450
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1039779783 716 EPTSGMDpVSRRAT-WDLLQHYKKDR--TILLTTHhmDEADV--LGDRiaILVM 764
Cdd:COG4172 451 EPTSALD-VSVQAQiLDLLRDLQREHglAYLFISH--DLAVVraLAHR--VMVM 499
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
558-764 |
7.55e-10 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 61.66 E-value: 7.55e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779783 558 IQHLYKEFILKNSTLMAVNDLSLNLYEGQITVLLGHNGAGKTTTLSILTGLyLPTRGKVYIS----GYDI----SSDMVQ 629
Cdd:PRK09473 15 VKDLRVTFSTPDGDVTAVNDLNFSLRAGETLGIVGESGSGKSQTAFALMGL-LAANGRIGGSatfnGREIlnlpEKELNK 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779783 630 IR-KSLGLCPQDDL--LFPMLTVSEHL------HfycviKGIPLQNQSRETNRMLTSFGLLQQSNTMS---KDLSGGMKR 697
Cdd:PRK09473 94 LRaEQISMIFQDPMtsLNPYMRVGEQLmevlmlH-----KGMSKAEAFEESVRMLDAVKMPEARKRMKmypHEFSGGMRQ 168
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1039779783 698 KLSIIIALIGDTKVVILDEPTSGMDPVSRRATWDLLQHYKKD--RTILLTTHhmDEADVLG--DRiaILVM 764
Cdd:PRK09473 169 RVMIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKREfnTAIIMITH--DLGVVAGicDK--VLVM 235
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
590-768 |
9.66e-10 |
|
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: 59.73 E-value: 9.66e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779783 590 LLGHNGAGKTTTLSILTGLYLPTRGKVYISGYDISS-DMVQIRKSLGLCPQDDLLFpMLTVSEHLHFYcvikgiplqnqS 668
Cdd:cd03369 39 IVGRTGAGKSTLILALFRFLEAEEGKIEIDGIDISTiPLEDLRSSLTIIPQDPTLF-SGTIRSNLDPF-----------D 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779783 669 RETNRMLtsFGLLQQSNTMSkDLSGGMKRKLSIIIALIGDTKVVILDEPTSGMDPVSRRATWDLLQHYKKDRTILLTTHH 748
Cdd:cd03369 107 EYSDEEI--YGALRVSEGGL-NLSQGQRQLLCLARALLKRPRVLVLDEATASIDYATDALIQKTIREEFTNSTILTIAHR 183
|
170 180
....*....|....*....|.
gi 1039779783 749 MDE-ADVlgDRIAILVMGILK 768
Cdd:cd03369 184 LRTiIDY--DKILVMDAGEVK 202
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
579-764 |
1.04e-09 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 62.24 E-value: 1.04e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779783 579 SLNLYEGQITVLLGHNGAGKTTTLSILTGLYLPTRGKVYISG--YDISSDMVQIRKSLGLCPQD---DLLFPMLTVSE-- 651
Cdd:PRK11288 273 SFSVRAGEIVGLFGLVGAGRSELMKLLYGATRRTAGQVYLDGkpIDIRSPRDAIRAGIMLCPEDrkaEGIIPVHSVADni 352
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779783 652 -------HLHFYCVIkgiplqNQSRETNRMLTSFGLLQqSNTMSKD-----LSGGMKRKlsIIIA--LIGDTKVVILDEP 717
Cdd:PRK11288 353 nisarrhHLRAGCLI------NNRWEAENADRFIRSLN-IKTPSREqlimnLSGGNQQK--AILGrwLSEDMKVILLDEP 423
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1039779783 718 TSGMDPVSRRATWDLLqhY---KKDRTILLTTHhmDEADVLG--DRiaILVM 764
Cdd:PRK11288 424 TRGIDVGAKHEIYNVI--YelaAQGVAVLFVSS--DLPEVLGvaDR--IVVM 469
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
585-722 |
1.66e-09 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 62.43 E-value: 1.66e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779783 585 GQITVLLGHNGAGKTTTLSILT----GLYLPTRGKVYISGYDISSDMVQIRKSLGLCPQDDLLFPMLTVSEHLHFYCVIK 660
Cdd:TIGR00956 87 GELTVVLGRPGSGCSTLLKTIAsntdGFHIGVEGVITYDGITPEEIKKHYRGDVVYNAETDVHFPHLTVGETLDFAARCK 166
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1039779783 661 GIPLQ--NQSRETNR------MLTSFGLLQQSNT-----MSKDLSGGMKRKLSIIIALIGDTKVVILDEPTSGMD 722
Cdd:TIGR00956 167 TPQNRpdGVSREEYAkhiadvYMATYGLSHTRNTkvgndFVRGVSGGERKRVSIAEASLGGAKIQCWDNATRGLD 241
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
577-764 |
2.01e-09 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 61.66 E-value: 2.01e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779783 577 DLSLNLYEGQITVLLGHNGAGKTTTLSILTGLYLPTRGKVYISGYDISSDMVQI-RKSLGLCPQD-----DLLFPMLT-- 648
Cdd:PRK10790 359 NINLSVPSRGFVALVGHTGSGKSTLASLLMGYYPLTEGEIRLDGRPLSSLSHSVlRQGVAMVQQDpvvlaDTFLANVTlg 438
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779783 649 --VSEHlHFYCVIKGIPLQNQSRETNRMLTSFgLLQQSNTmskdLSGGMKRKLSIIIALIGDTKVVILDEPTSGMDPVSR 726
Cdd:PRK10790 439 rdISEE-QVWQALETVQLAELARSLPDGLYTP-LGEQGNN----LSVGQKQLLALARVLVQTPQILILDEATANIDSGTE 512
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1039779783 727 RATWDLLQHYKKDRTILLTTHHMD---EADvlgdriAILVM 764
Cdd:PRK10790 513 QAIQQALAAVREHTTLVVIAHRLStivEAD------TILVL 547
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
570-749 |
2.82e-09 |
|
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The sulfonylurea receptor SUR is an ATP transporter of the ABCC/MRP family with tandem ATPase binding domains. Unlike other ABC proteins, it has no intrinsic transport function, neither active nor passive, but associates with the potassium channel proteins Kir6.1 or Kir6.2 to form the ATP-sensitive potassium (K(ATP)) channel. Within the channel complex, SUR serves as a regulatory subunit that fine-tunes the gating of Kir6.x in response to alterations in cellular metabolism. It constitutes a major pharmaceutical target as it binds numerous drugs, K(ATP) channel openers and blockers, capable of up- or down-regulating channel activity.
Pssm-ID: 213257 [Multi-domain] Cd Length: 218 Bit Score: 58.50 E-value: 2.82e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779783 570 STLMAVNDLSLNLYEGQITVLLGHNGAGKTTTLSILTGLYLPTRGKVYISGYDISSDMVQI-----RKSLGLCPQDDLLF 644
Cdd:cd03290 12 SGLATLSNINIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWSNKNESEPSFEAtrsrnRYSVAYAAQKPWLL 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779783 645 PMlTVSEHLHFycvikGIPLQNQ---------SRETNRMLTSFGLLQQSNTMSKDLSGGMKRKLSIIIALIGDTKVVILD 715
Cdd:cd03290 92 NA-TVEENITF-----GSPFNKQrykavtdacSLQPDIDLLPFGDQTEIGERGINLSGGQRQRICVARALYQNTNIVFLD 165
|
170 180 190
....*....|....*....|....*....|....*....
gi 1039779783 716 EPTSGM-----DPVSRRATWDLLQHYKkdRTILLTTHHM 749
Cdd:cd03290 166 DPFSALdihlsDHLMQEGILKFLQDDK--RTLVLVTHKL 202
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
585-755 |
3.19e-09 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 61.28 E-value: 3.19e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779783 585 GQITVLLGHNGAGKTTTLSIL----TGLYLpTRGKVYISGYDISSdmvQIRKSLGLCPQDDLLFPMLTVSEHLHFYCVI- 659
Cdd:TIGR00956 789 GTLTALMGASGAGKTTLLNVLaervTTGVI-TGGDRLVNGRPLDS---SFQRSIGYVQQQDLHLPTSTVRESLRFSAYLr 864
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779783 660 --KGIPLQNQSRETNRMLTSFGLLQQSNTM----SKDLSGGMKRKLSIIIALIGDTKVVI-LDEPTSGMDPvsrRATWDL 732
Cdd:TIGR00956 865 qpKSVSKSEKMEYVEEVIKLLEMESYADAVvgvpGEGLNVEQRKRLTIGVELVAKPKLLLfLDEPTSGLDS---QTAWSI 941
|
170 180 190
....*....|....*....|....*....|..
gi 1039779783 733 LQHYKK----DRTILLTTHH-----MDEADVL 755
Cdd:TIGR00956 942 CKLMRKladhGQAILCTIHQpsailFEEFDRL 973
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
577-750 |
4.37e-09 |
|
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis fibrosis transmembrane conductor regulator (CFTR) in eukaryotes. The principal role of this protein is chloride ion conductance. The protein is predicted to consist of 12 transmembrane domains. Mutations or lesions in the genetic loci have been linked to the aetiology of asthma, bronchiectasis, chronic obstructive pulmonary disease etc. Disease-causing mutations have been studied by 36Cl efflux assays in vitro cell cultures and electrophysiology, all of which point to the impairment of chloride channel stability and not the biosynthetic processing per se. [Transport and binding proteins, Anions]
Pssm-ID: 273530 [Multi-domain] Cd Length: 1490 Bit Score: 61.08 E-value: 4.37e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779783 577 DLSLNLYEGQITVLLGHNGAGKTTTLSILTGLyLPTRGKVYISGYDISSDMVQI-RKSLGLCPQDDLLFP---------- 645
Cdd:TIGR01271 1237 DLSFSVEGGQRVGLLGRTGSGKSTLLSALLRL-LSTEGEIQIDGVSWNSVTLQTwRKAFGVIPQKVFIFSgtfrknldpy 1315
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779783 646 -------MLTVSEHLHFYCVIKGIPlqnqsRETNRMLTSFGLLqqsntmskdLSGGMKRKLSIIIALIGDTKVVILDEPT 718
Cdd:TIGR01271 1316 eqwsdeeIWKVAEEVGLKSVIEQFP-----DKLDFVLVDGGYV---------LSNGHKQLMCLARSILSKAKILLLDEPS 1381
|
170 180 190
....*....|....*....|....*....|..
gi 1039779783 719 SGMDPVSRRATWDLLQHYKKDRTILLTTHHMD 750
Cdd:TIGR01271 1382 AHLDPVTLQIIRKTLKQSFSNCTVILSEHRVE 1413
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
574-749 |
5.57e-09 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 58.36 E-value: 5.57e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779783 574 AVNDLSLNLYEGQITVLLGHNGAGKTTTLSILTGLYLPTRGKVYISGYDISSdmvQIRKSL-GLCPQD---DLLFPMLTV 649
Cdd:PRK15056 22 ALRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKISILGQPTRQ---ALQKNLvAYVPQSeevDWSFPVLVE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779783 650 SehlhfyCVIKG---------IPLQNQSRETNRMLTSFGLLQQSNTMSKDLSGGMKRKLSIIIALIGDTKVVILDEPTSG 720
Cdd:PRK15056 99 D------VVMMGryghmgwlrRAKKRDRQIVTAALARVDMVEFRHRQIGELSGGQKKRVFLARAIAQQGQVILLDEPFTG 172
|
170 180 190
....*....|....*....|....*....|
gi 1039779783 721 MDPVSRRATWDLLQHYKKD-RTILLTTHHM 749
Cdd:PRK15056 173 VDVKTEARIISLLRELRDEgKTMLVSTHNL 202
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
556-762 |
6.38e-09 |
|
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose isomerase and xylulokinase enzymes for xylose utilization. Members of this protein family are the ATP-binding cassette (ABC) subunit of the known or predicted high-affinity xylose ABC transporter for xylose import. These genes, which closely resemble other sugar transport ABC transporter genes, typically are encoded near xylose utilization enzymes and regulatory proteins. Note that this form of the transporter contains two copies of the ABC transporter domain (pfam00005). [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 131681 [Multi-domain] Cd Length: 500 Bit Score: 59.84 E-value: 6.38e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779783 556 IRIQHLYKEFilknSTLMAVNDLSLNLYEGQITVLLGHNGAGKTTTLSILTGLYlPT---RGKVYISGYDISSDMVQI-- 630
Cdd:TIGR02633 2 LEMKGIVKTF----GGVKALDGIDLEVRPGECVGLCGENGAGKSTLMKILSGVY-PHgtwDGEIYWSGSPLKASNIRDte 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779783 631 RKSLGLCPQDDLLFPMLTVSEHLHFYcviKGIPLQNQSRETNRM-LTSFGLLQQ------SNTMS-KDLSGGMKRKLSII 702
Cdd:TIGR02633 77 RAGIVIIHQELTLVPELSVAENIFLG---NEITLPGGRMAYNAMyLRAKNLLRElqldadNVTRPvGDYGGGQQQLVEIA 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1039779783 703 IALIGDTKVVILDEPTSGMDPVSRRATWDLLQHYK-KDRTILLTTHHMDEADVLGDRIAIL 762
Cdd:TIGR02633 154 KALNKQARLLILDEPSSSLTEKETEILLDIIRDLKaHGVACVYISHKLNEVKAVCDTICVI 214
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
585-747 |
7.97e-09 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 60.24 E-value: 7.97e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779783 585 GQITVLLGHNGAGKTTTLSIL----TGLYLptRGKVYISGYDISSDMVQiRKSlGLCPQDDLLFPMLTVSEHLHFYCVIK 660
Cdd:PLN03140 906 GVLTALMGVSGAGKTTLMDVLagrkTGGYI--EGDIRISGFPKKQETFA-RIS-GYCEQNDIHSPQVTVRESLIYSAFLR 981
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779783 661 gIPLQNQSRETNRMLTSFGLLQQSNTMsKD----------LSGGMKRKLSIIIALIGDTKVVILDEPTSGMDP-----VS 725
Cdd:PLN03140 982 -LPKEVSKEEKMMFVDEVMELVELDNL-KDaivglpgvtgLSTEQRKRLTIAVELVANPSIIFMDEPTSGLDAraaaiVM 1059
|
170 180
....*....|....*....|....
gi 1039779783 726 R--RATWDllqhykKDRTILLTTH 747
Cdd:PLN03140 1060 RtvRNTVD------TGRTVVCTIH 1077
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
524-765 |
1.17e-08 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 59.10 E-value: 1.17e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779783 524 FGEPALSREESQVSDLLSSDFMEPEPVglvagIRIQHLYKEFILKNSTL-------MAVNDLSLNLYEGQITVLLGHNGA 596
Cdd:PRK10261 287 FPLISLEHPAKQEPPIEQDTVVDGEPI-----LQVRNLVTRFPLRSGLLnrvtrevHAVEKVSFDLWPGETLSLVGESGS 361
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779783 597 GKTTTLSILTGLYLPTRGKVYISGYDI----SSDMVQIRKSLGLCPQDDL--LFPMLTVS----EHLHFYCVIKGiplQN 666
Cdd:PRK10261 362 GKSTTGRALLRLVESQGGEIIFNGQRIdtlsPGKLQALRRDIQFIFQDPYasLDPRQTVGdsimEPLRVHGLLPG---KA 438
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779783 667 QSRETNRMLTSFGLL-QQSNTMSKDLSGGMKRKLSIIIALIGDTKVVILDEPTSGMDPVSRRATWDLLQHYKKDRTI--L 743
Cdd:PRK10261 439 AAARVAWLLERVGLLpEHAWRYPHEFSGGQRQRICIARALALNPKVIIADEAVSALDVSIRGQIINLLLDLQRDFGIayL 518
|
250 260
....*....|....*....|..
gi 1039779783 744 LTTHHMDEADVLGDRIAILVMG 765
Cdd:PRK10261 519 FISHDMAVVERISHRVAVMYLG 540
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
559-762 |
1.19e-08 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 58.79 E-value: 1.19e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779783 559 QHLYKEFilknSTLMAVNDLSLNLYEGQITVLLGHNGAGKTTTLSILTGLYlPT---RGKVYISGYDISSDMVQI--RKS 633
Cdd:PRK13549 9 KNITKTF----GGVKALDNVSLKVRAGEIVSLCGENGAGKSTLMKVLSGVY-PHgtyEGEIIFEGEELQASNIRDteRAG 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779783 634 LGLCPQDDLLFPMLTVSEHLHFYCVI--KGIPLQNQ-SRETNRMLTSFGLLQQSNTMSKDLSGGMKRKLSIIIALIGDTK 710
Cdd:PRK13549 84 IAIIHQELALVKELSVLENIFLGNEItpGGIMDYDAmYLRAQKLLAQLKLDINPATPVGNLGLGQQQLVEIAKALNKQAR 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1039779783 711 VVILDEPTSGMDPVSRRATWDLLQHYK-KDRTILLTTHHMDEADVLGDRIAIL 762
Cdd:PRK13549 164 LLILDEPTASLTESETAVLLDIIRDLKaHGIACIYISHKLNEVKAISDTICVI 216
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
575-747 |
1.63e-08 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 57.00 E-value: 1.63e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779783 575 VNDLSLNLYEGQITVLLGHNGAGKTTTLSILTGLYLPTRGKVYISGYDIS----SDMVQIRKSLGLCPQDDL--LFPMLT 648
Cdd:PRK10419 28 LNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWRGEPLAklnrAQRKAFRRDIQMVFQDSIsaVNPRKT 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779783 649 VsehlhfyCVIKGIPLQN--------QSRETNRMLTSFGL-LQQSNTMSKDLSGGMKRKLSIIIALIGDTKVVILDEPTS 719
Cdd:PRK10419 108 V-------REIIREPLRHllsldkaeRLARASEMLRAVDLdDSVLDKRPPQLSGGQLQRVCLARALAVEPKLLILDEAVS 180
|
170 180 190
....*....|....*....|....*....|
gi 1039779783 720 GMDPVSRRATWDLLQHYKKDRTI--LLTTH 747
Cdd:PRK10419 181 NLDLVLQAGVIRLLKKLQQQFGTacLFITH 210
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
584-812 |
1.89e-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: 56.61 E-value: 1.89e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779783 584 EGQITVLLGHNGAGKTTTLSILTGLYLPTRGKV-----------YISGYDISS--------DMVQIRKslglcPQDDLLF 644
Cdd:cd03236 25 EGQVLGLVGPNGIGKSTALKILAGKLKPNLGKFddppdwdeildEFRGSELQNyftkllegDVKVIVK-----PQYVDLI 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779783 645 PMltvsehlhfycVIKG--IPLQNQSRETNRMLTSFGLLQQSNTMSK---DLSGGMKRKLSIIIALIGDTKVVILDEPTS 719
Cdd:cd03236 100 PK-----------AVKGkvGELLKKKDERGKLDELVDQLELRHVLDRnidQLSGGELQRVAIAAALARDADFYFFDEPSS 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779783 720 GMDPVSR----RATWDLLQHykkDRTILLTTHHMDEADVLGDRIailvmgilkCCgsslflkkLYGVGYHLVIVKTPDSN 795
Cdd:cd03236 169 YLDIKQRlnaaRLIRELAED---DNYVLVVEHDLAVLDYLSDYI---------HC--------LYGEPGAYGVVTLPKSV 228
|
250
....*....|....*..
gi 1039779783 796 DEKIFQLIKNYIPTAKM 812
Cdd:cd03236 229 REGINEFLDGYLPTENM 245
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
542-765 |
2.02e-08 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 58.33 E-value: 2.02e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779783 542 SDFMEPEPVGLVAGIRIQhlykeFILKNSTLMAVNDLSLNLYEGQITVLLGHNGAGKTTT-LSIL------------TGL 608
Cdd:PRK10261 4 SDELDARDVLAVENLNIA-----FMQEQQKIAAVRNLSFSLQRGETLAIVGESGSGKSVTaLALMrlleqagglvqcDKM 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779783 609 YLPTRGKVYISGYDIS-SDMVQIRKS-LGLCPQDDL--LFPMLTVSEH------LHfycviKGIPLQNQSRETNRMLTSF 678
Cdd:PRK10261 79 LLRRRSRQVIELSEQSaAQMRHVRGAdMAMIFQEPMtsLNPVFTVGEQiaesirLH-----QGASREEAMVEAKRMLDQV 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779783 679 GLLQQSNTMSK---DLSGGMKRKLSIIIALIGDTKVVILDEPTSGMDPVSRRATWDLLQHYKKDRT--ILLTTHHMDEAD 753
Cdd:PRK10261 154 RIPEAQTILSRyphQLSGGMRQRVMIAMALSCRPAVLIADEPTTALDVTIQAQILQLIKVLQKEMSmgVIFITHDMGVVA 233
|
250
....*....|..
gi 1039779783 754 VLGDRIAILVMG 765
Cdd:PRK10261 234 EIADRVLVMYQG 245
|
|
| CP_lyasePhnK |
TIGR02323 |
phosphonate C-P lyase system protein PhnK; Members of this family are the PhnK protein of C-P ... |
574-764 |
2.27e-08 |
|
phosphonate C-P lyase system protein PhnK; Members of this family are the PhnK protein of C-P lyase systems for utilization of phosphonates. These systems resemble phosphonatase-based systems in having a three component ABC transporter, where TIGR01097 is the permease, TIGR01098 is the phosphonates binding protein, and TIGR02315 is the ATP-binding cassette (ABC) protein. They differ, however, in having, typically, ten or more additional genes, many of which are believed to form a membrane-associated complex. This protein (PhnK) and the adjacent-encoded PhnL resemble transporter ATP-binding proteins but are suggested, based on mutatgenesis studies, to be part of this complex rather than part of a transporter per se. [Central intermediary metabolism, Phosphorus compounds]
Pssm-ID: 188208 [Multi-domain] Cd Length: 253 Bit Score: 56.38 E-value: 2.27e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779783 574 AVNDLSLNLYEGQITVLLGHNGAGKTTTLSILTGLYLPTRGKV-YISGYDISSDMVQI---------RKSLGLC---PQD 640
Cdd:TIGR02323 18 GCRDVSFDLYPGEVLGIVGESGSGKSTLLGCLAGRLAPDHGTAtYIMRSGAELELYQLseaerrrlmRTEWGFVhqnPRD 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779783 641 DLLF-----------PMLTVSEHlhfYCVIKGIP---LQNQSRETNRMltsfgllqqsNTMSKDLSGGMKRKLSIIIALI 706
Cdd:TIGR02323 98 GLRMrvsaganigerLMAIGARH---YGNIRATAqdwLEEVEIDPTRI----------DDLPRAFSGGMQQRLQIARNLV 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1039779783 707 GDTKVVILDEPTSGMDpVSRRATW-DLLQHYKKDRTI--LLTTHHMDEADVLGDRiaILVM 764
Cdd:TIGR02323 165 TRPRLVFMDEPTGGLD-VSVQARLlDLLRGLVRDLGLavIIVTHDLGVARLLAQR--LLVM 222
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
577-750 |
2.79e-08 |
|
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: 56.40 E-value: 2.79e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779783 577 DLSLNLYEGQITVLLGHNGAGKTTTLSILTGLyLPTRGKVYISGYDISS-DMVQIRKSLGLCPQDDLLFP---------- 645
Cdd:cd03289 22 NISFSISPGQRVGLLGRTGSGKSTLLSAFLRL-LNTEGDIQIDGVSWNSvPLQKWRKAFGVIPQKVFIFSgtfrknldpy 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779783 646 -------MLTVSEHLHFYCVIKGIPLQnqsreTNRMLTSFGLLqqsntmskdLSGGMKRKLSIIIALIGDTKVVILDEPT 718
Cdd:cd03289 101 gkwsdeeIWKVAEEVGLKSVIEQFPGQ-----LDFVLVDGGCV---------LSHGHKQLMCLARSVLSKAKILLLDEPS 166
|
170 180 190
....*....|....*....|....*....|..
gi 1039779783 719 SGMDPVSRRATWDLLQHYKKDRTILLTTHHMD 750
Cdd:cd03289 167 AHLDPITYQVIRKTLKQAFADCTVILSEHRIE 198
|
|
| ABC2_membrane_3 |
pfam12698 |
ABC-2 family transporter protein; This family is related to the ABC-2 membrane transporter ... |
323-423 |
4.31e-08 |
|
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: 56.63 E-value: 4.31e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779783 323 EYQLMVGLSNAMLWVSYFITFLLMYFIIICLLCGILFlkitHERVFQHSDPLFIAFYFMcFAVSSVLLGFLISTLFNKAS 402
Cdd:pfam12698 193 ERLLVSGVSPLQYWLGKILGDFLVGLLQLLIILLLLF----GIGIPFGNLGLLLLLFLL-YGLAYIALGYLLGSLFKNSE 267
|
90 100
....*....|....*....|.
gi 1039779783 403 LATSIAGFLHFLTFFPYLILY 423
Cdd:pfam12698 268 DAQSIIGIVILLLSGFFGGLF 288
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
565-782 |
5.50e-08 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 55.18 E-value: 5.50e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779783 565 FILKNSTLMA-----VNDLSLNLYEGQITVLLGHNGAGKTTTLSILTGLYLPTRGKVYISGYDISS-DMVQIRKSLGLCP 638
Cdd:PRK10575 12 FALRNVSFRVpgrtlLHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPLESwSSKAFARKVAYLP 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779783 639 QDDLLFPMLTVSEhlhfYCVIKGIPL--------QNQSRETNRMLTSFGLLQQSNTMSKDLSGGMKRKLSIIIALIGDTK 710
Cdd:PRK10575 92 QQLPAAEGMTVRE----LVAIGRYPWhgalgrfgAADREKVEEAISLVGLKPLAHRLVDSLSGGERQRAWIAMLVAQDSR 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779783 711 VVILDEPTSGMDPVSRRATWDLLQHYKKDR--TILLTTHHMDEADVLGDRIAILVMGILKCCGSSL------FLKKLYGV 782
Cdd:PRK10575 168 CLLLDEPTSALDIAHQVDVLALVHRLSQERglTVIAVLHDINMAARYCDYLVALRGGEMIAQGTPAelmrgeTLEQIYGI 247
|
|
| PRK15093 |
PRK15093 |
peptide ABC transporter ATP-binding protein SapD; |
558-765 |
1.05e-07 |
|
peptide ABC transporter ATP-binding protein SapD;
Pssm-ID: 185049 [Multi-domain] Cd Length: 330 Bit Score: 55.19 E-value: 1.05e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779783 558 IQHLYKEFILKNSTLMAVNDLSLNLYEGQITVLLGHNGAGKTTTLSILTG--------------------LYLPTRGKVY 617
Cdd:PRK15093 6 IRNLTIEFKTSDGWVKAVDRVSMTLTEGEIRGLVGESGSGKSLIAKAICGvtkdnwrvtadrmrfddidlLRLSPRERRK 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779783 618 ISGYDISSDMVQirkslglcPQDdLLFPMLTVSEHLhfycvIKGIP-----------LQNQSRETNRMLTSFGLLQQSNT 686
Cdd:PRK15093 86 LVGHNVSMIFQE--------PQS-CLDPSERVGRQL-----MQNIPgwtykgrwwqrFGWRKRRAIELLHRVGIKDHKDA 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779783 687 MSK---DLSGGMKRKLSIIIALIGDTKVVILDEPTSGMDPVSRRATWDLLQHYKKDR--TILLTTHHMDEADVLGDRIAI 761
Cdd:PRK15093 152 MRSfpyELTEGECQKVMIAIALANQPRLLIADEPTNAMEPTTQAQIFRLLTRLNQNNntTILLISHDLQMLSQWADKINV 231
|
....
gi 1039779783 762 LVMG 765
Cdd:PRK15093 232 LYCG 235
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
562-764 |
1.07e-07 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 54.41 E-value: 1.07e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779783 562 YKEFILKNSTLMAVNDLSLNLYEGQITVLLGHNGAGKTTTLSILTGLYLPTRGKVYISGY-----DISSDMVQIRkslgL 636
Cdd:PRK15112 16 YRTGWFRRQTVEAVKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDHplhfgDYSYRSQRIR----M 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779783 637 CPQD--DLLFPMLTVSEHLHFYCVIKgIPLQNQSRE--TNRMLTSFGLL-QQSNTMSKDLSGGMKRKLSIIIALIGDTKV 711
Cdd:PRK15112 92 IFQDpsTSLNPRQRISQILDFPLRLN-TDLEPEQREkqIIETLRQVGLLpDHASYYPHMLAPGQKQRLGLARALILRPKV 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1039779783 712 VILDEPTSGMDPVSRRATWDLLQHYKKDRTI--LLTTHHMDEADVLGDRiaILVM 764
Cdd:PRK15112 171 IIADEALASLDMSMRSQLINLMLELQEKQGIsyIYVTQHLGMMKHISDQ--VLVM 223
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
576-766 |
1.20e-07 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 53.81 E-value: 1.20e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779783 576 NDLSLNLYEGQITVLLGHNGAGKTTTLSILTGLYL--PTRGKVYISGYDISSDMVQIrkslglcpqDDL--LFPMLTVSE 651
Cdd:COG2401 47 RDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGALKgtPVAGCVDVPDNQFGREASLI---------DAIgrKGDFKDAVE 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779783 652 HLHfYCVIKGIPLqnqsretnrMLTSFgllqqsntmsKDLSGGMKRKLSIIIALIGDTKVVILDEPTSGMDP-VSRRATW 730
Cdd:COG2401 118 LLN-AVGLSDAVL---------WLRRF----------KELSTGQKFRFRLALLLAERPKLLVIDEFCSHLDRqTAKRVAR 177
|
170 180 190
....*....|....*....|....*....|....*...
gi 1039779783 731 DLLQHYKKDR-TILLTTHHMDEADVLG-DRIAILVMGI 766
Cdd:COG2401 178 NLQKLARRAGiTLVVATHHYDVIDDLQpDLLIFVGYGG 215
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
575-767 |
1.22e-07 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 55.56 E-value: 1.22e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779783 575 VNDLSLNLYEGQITVLLGHNGAGKTTTLSILTGLYLPTRGKVYISGYDIS--SDMVQIRKSLGLCPQ---DDLLFPMLTV 649
Cdd:PRK09700 279 VRDISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEIRLNGKDISprSPLDAVKKGMAYITEsrrDNGFFPNFSI 358
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779783 650 SEHLHFYCVIK------GIPLQNQSRETNRMLTSFGLLQ----QSNTMSKDLSGGMKRKLSIIIALIGDTKVVILDEPTS 719
Cdd:PRK09700 359 AQNMAISRSLKdggykgAMGLFHEVDEQRTAENQRELLAlkchSVNQNITELSGGNQQKVLISKWLCCCPEVIIFDEPTR 438
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1039779783 720 GMDPVSRRATWDLLQHYKKD-RTILLTTHHMDEADVLGDRIAILVMGIL 767
Cdd:PRK09700 439 GIDVGAKAEIYKVMRQLADDgKVILMVSSELPEIITVCDRIAVFCEGRL 487
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
574-767 |
1.68e-07 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 55.03 E-value: 1.68e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779783 574 AVNDLSLNLYEGQITVLLGHNGAGKTTTLSILTGLYLPTRGKVYISGYDISSDMVQIRKSLGLC--PQDDL---LFPMLT 648
Cdd:COG3845 273 ALKDVSLEVRAGEILGIAGVAGNGQSELAEALAGLRPPASGSIRLDGEDITGLSPRERRRLGVAyiPEDRLgrgLVPDMS 352
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779783 649 VSEHL---HFY--CVIKGIPLQNQS--RETNRMLTSFGLLQQS-NTMSKDLSGGMKRKLsiIIA--LIGDTKVVILDEPT 718
Cdd:COG3845 353 VAENLilgRYRrpPFSRGGFLDRKAirAFAEELIEEFDVRTPGpDTPARSLSGGNQQKV--ILAreLSRDPKLLIAAQPT 430
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1039779783 719 SGMDPVSRRATWD-LLQHYKKDRTILLTTHHMDEADVLGDRIAIL----VMGIL 767
Cdd:COG3845 431 RGLDVGAIEFIHQrLLELRDAGAAVLLISEDLDEILALSDRIAVMyegrIVGEV 484
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
578-765 |
2.10e-07 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 55.37 E-value: 2.10e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779783 578 LSLNLYEGQITVLLGHNGAGKTTTLSILTGLYLPTRGKVYISGYDISS-DMVQIRKSLGLCPQDDLLFP------MLTVS 650
Cdd:PLN03232 1255 LSFFVSPSEKVGVVGRTGAGKSSMLNALFRIVELEKGRIMIDDCDVAKfGLTDLRRVLSIIPQSPVLFSgtvrfnIDPFS 1334
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779783 651 EH--LHFYCVIKGIPLQNQSRETnrmltSFGLLQQSNTMSKDLSGGMKRKLSIIIALIGDTKVVILDEPTSGMDPVSRRA 728
Cdd:PLN03232 1335 EHndADLWEALERAHIKDVIDRN-----PFGLDAEVSEGGENFSVGQRQLLSLARALLRRSKILVLDEATASVDVRTDSL 1409
|
170 180 190
....*....|....*....|....*....|....*..
gi 1039779783 729 TWDLLQHYKKDRTILLTTHHMDEAdVLGDRIAILVMG 765
Cdd:PLN03232 1410 IQRTIREEFKSCTMLVIAHRLNTI-IDCDKILVLSSG 1445
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
577-749 |
2.27e-07 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 55.42 E-value: 2.27e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779783 577 DLSLNLYEGQITVLLGHNGAGKTTTLSILTGLYLPTRGKVYISGydiSSDMVQI-----RKSLGLCPQDDLLFP------ 645
Cdd:PTZ00265 403 DLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIIIND---SHNLKDInlkwwRSKIGVVSQDPLLFSnsiknn 479
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779783 646 ------MLTVSEHLHFYCVIKGIPLQN--QSRETNRMLTSFGLLQQSNTMSKD--------------------------- 690
Cdd:PTZ00265 480 ikyslySLKDLEALSNYYNEDGNDSQEnkNKRNSCRAKCAGDLNDMSNTTDSNeliemrknyqtikdsevvdvskkvlih 559
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779783 691 --------------------LSGGMKRKLSIIIALIGDTKVVILDEPTSGMDPVSRRATWDLLQHYK--KDRTILLTTHH 748
Cdd:PTZ00265 560 dfvsalpdkyetlvgsnaskLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQKTINNLKgnENRITIIIAHR 639
|
.
gi 1039779783 749 M 749
Cdd:PTZ00265 640 L 640
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
577-760 |
3.86e-07 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 54.78 E-value: 3.86e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779783 577 DLSLNLYEGQITVLLGHNGAGKTTTLSILtglylptrgkvyISGYDISSDMVQIRKSLGLCPQDDLLFPMlTVSEHLHFY 656
Cdd:PTZ00243 678 DVSVSVPRGKLTVVLGATGSGKSTLLQSL------------LSQFEISEGRVWAERSIAYVPQQAWIMNA-TVRGNILFF 744
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779783 657 CVIKGIPLQNQSR----ETNRMLTSFGLLQQSNTMSKDLSGGMKRKLSIIIALIGDTKVVILDEPTSGMDP-VSRRATWD 731
Cdd:PTZ00243 745 DEEDAARLADAVRvsqlEADLAQLGGGLETEIGEKGVNLSGGQKARVSLARAVYANRDVYLLDDPLSALDAhVGERVVEE 824
|
170 180 190
....*....|....*....|....*....|....*.
gi 1039779783 732 LLQHYKKDRTILLTTH------HMDEADVLGD-RIA 760
Cdd:PTZ00243 825 CFLGALAGKTRVLATHqvhvvpRADYVVALGDgRVE 860
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
574-755 |
4.62e-07 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 53.82 E-value: 4.62e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779783 574 AVNDLSLNLYEGQITVLLGHNGAGKTTTLSILTGLYLPTRGKVYISGYDISS-DMVQIRKSLGLCPQDDLLFPMLTVSEh 652
Cdd:PRK10522 338 SVGPINLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKPVTAeQPEDYRKLFSAVFTDFHLFDQLLGPE- 416
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779783 653 lhfycvikGIPLQNQSRET--NRMLTSFGLLQQSNTMSK-DLSGGMKRKLSIIIALIGDTKVVILDEPTSGMDPVSRRAT 729
Cdd:PRK10522 417 --------GKPANPALVEKwlERLKMAHKLELEDGRISNlKLSKGQKKRLALLLALAEERDILLLDEWAADQDPHFRREF 488
|
170 180 190
....*....|....*....|....*....|.
gi 1039779783 730 W-DLLQHYK-KDRTILLTTH---HMDEADVL 755
Cdd:PRK10522 489 YqVLLPLLQeMGKTIFAISHddhYFIHADRL 519
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
584-762 |
5.06e-07 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 53.66 E-value: 5.06e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779783 584 EGQITVLLGHNGAGKTTTLSILTGLYLPTRGKV-----------YISG---YDISSDMVQIRKSLGLCPQD-DLLfPML- 647
Cdd:PRK13409 98 EGKVTGILGPNGIGKTTAVKILSGELIPNLGDYeeepswdevlkRFRGtelQNYFKKLYNGEIKVVHKPQYvDLI-PKVf 176
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779783 648 --TVSEhlhfycVIKGIplqNQSRETNRMLTSFGLlqqSNTMSKD---LSGGMKRKLSIIIALIGDTKVVILDEPTSGMD 722
Cdd:PRK13409 177 kgKVRE------LLKKV---DERGKLDEVVERLGL---ENILDRDiseLSGGELQRVAIAAALLRDADFYFFDEPTSYLD 244
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1039779783 723 PVSRRATWDLLQHYKKDRTILLTTHHMDEADVLGDRIAIL 762
Cdd:PRK13409 245 IRQRLNVARLIRELAEGKYVLVVEHDLAVLDYLADNVHIA 284
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
577-764 |
6.31e-07 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 51.85 E-value: 6.31e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779783 577 DLSLNLYEGQITVLLGHNGAGKTTTLSILTGLYLPTRGKV-YISGYDISSDMVQI---------RKSLGLCPQD--DLLF 644
Cdd:PRK11701 24 DVSFDLYPGEVLGIVGESGSGKTTLLNALSARLAPDAGEVhYRMRDGQLRDLYALseaerrrllRTEWGFVHQHprDGLR 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779783 645 PMLT----VSEHL------HfYCVIKGIPLQNQSR---ETNRM---LTSFgllqqsntmskdlSGGMKRKLSIIIALIGD 708
Cdd:PRK11701 104 MQVSaggnIGERLmavgarH-YGDIRATAGDWLERveiDAARIddlPTTF-------------SGGMQQRLQIARNLVTH 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1039779783 709 TKVVILDEPTSGMDpVSRRATW-DLLQHYKKDR--TILLTTHHMDEADVLGDRiaILVM 764
Cdd:PRK11701 170 PRLVFMDEPTGGLD-VSVQARLlDLLRGLVRELglAVVIVTHDLAVARLLAHR--LLVM 225
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
575-765 |
9.29e-07 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 52.62 E-value: 9.29e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779783 575 VNDLSLNLYEGQITVLLGHNGAGKTTTLSILTGLYlPTR--GKVYISG--YDISSDMVQIRKSLGLCPQD---DLLFPML 647
Cdd:PRK13549 278 VDDVSFSLRRGEILGIAGLVGAGRTELVQCLFGAY-PGRweGEIFIDGkpVKIRNPQQAIAQGIAMVPEDrkrDGIVPVM 356
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779783 648 TvsehlhfycVIKGIPLQNQSRETNRMLTSFGLLQQS----------NTMSKD-----LSGGMKRKLSIIIALIGDTKVV 712
Cdd:PRK13549 357 G---------VGKNITLAALDRFTGGSRIDDAAELKTilesiqrlkvKTASPElaiarLSGGNQQKAVLAKCLLLNPKIL 427
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1039779783 713 ILDEPTSGMDPVSRRATWDLL-QHYKKDRTILLTTHHMDEadVLG--DRiaILVMG 765
Cdd:PRK13549 428 ILDEPTRGIDVGAKYEIYKLInQLVQQGVAIIVISSELPE--VLGlsDR--VLVMH 479
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
575-763 |
1.75e-06 |
|
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding cassette transporter (Pat) is involved in the import of very long-chain fatty acids (VLCFA) into the peroxisome. The peroxisomal membrane forms a permeability barrier for a wide variety of metabolites required for and formed during fatty acid beta-oxidation. To communicate with the cytoplasm and mitochondria, peroxisomes need dedicated proteins to transport such hydrophilic molecules across their membranes. X-linked adrenoleukodystrophy (X-ALD) is caused by mutations in the ALD gene, which encodes ALDP (adrenoleukodystrophy protein ), a peroxisomal integral membrane protein that is a member of the ATP-binding cassette (ABC) transporter protein family. The disease is characterized by a striking and unpredictable variation in phenotypic expression. Phenotypes include the rapidly progressive childhood cerebral form (CCALD), the milder adult form, adrenomyeloneuropathy (AMN), and variants without neurologic involvement (i.e. asymptomatic).
Pssm-ID: 213190 [Multi-domain] Cd Length: 166 Bit Score: 49.07 E-value: 1.75e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779783 575 VNDLSLNLYEGQITVLLGHNGAGKTTTLSILTGLYLPTRGKVYIsgydissdmvqirkslglCPQDDLLFpmltvsehlh 654
Cdd:cd03223 17 LKDLSFEIKPGDRLLITGPSGTGKSSLFRALAGLWPWGSGRIGM------------------PEGEDLLF---------- 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779783 655 fycvikgIPlqnQsretnRMLTSFGLL--QQSNTMSKDLSGGMKRKLSIIIALIGDTKVVILDEPTSGMDPVSRRAtwdL 732
Cdd:cd03223 69 -------LP---Q-----RPYLPLGTLreQLIYPWDDVLSGGEQQRLAFARLLLHKPKFVFLDEATSALDEESEDR---L 130
|
170 180 190
....*....|....*....|....*....|.
gi 1039779783 733 LQHYKKDRTILLTTHHMDEADVLGDRIAILV 763
Cdd:cd03223 131 YQLLKELGITVISVGHRPSLWKFHDRVLDLD 161
|
|
| tagH |
PRK13545 |
teichoic acids export protein ATP-binding subunit; Provisional |
574-751 |
2.86e-06 |
|
teichoic acids export protein ATP-binding subunit; Provisional
Pssm-ID: 184130 [Multi-domain] Cd Length: 549 Bit Score: 51.43 E-value: 2.86e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779783 574 AVNDLSLNLYEGQITVLLGHNGAGKTTTLSILTGLYLPTRGKVYISGydiSSDMVQIrkSLGLCPQddllfpmLTVSEHL 653
Cdd:PRK13545 39 ALNNISFEVPEGEIVGIIGLNGSGKSTLSNLIAGVTMPNKGTVDIKG---SAALIAI--SSGLNGQ-------LTGIENI 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779783 654 HFYCVIKGIPlQNQSRETNRMLTSFGLLQQ-SNTMSKDLSGGMKRKLSIIIALIGDTKVVILDEPTSGMDPVSRRATWDL 732
Cdd:PRK13545 107 ELKGLMMGLT-KEKIKEIIPEIIEFADIGKfIYQPVKTYSSGMKSRLGFAISVHINPDILVIDEALSVGDQTFTKKCLDK 185
|
170 180
....*....|....*....|
gi 1039779783 733 LQHYK-KDRTILLTTHHMDE 751
Cdd:PRK13545 186 MNEFKeQGKTIFFISHSLSQ 205
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
563-807 |
3.06e-06 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 51.27 E-value: 3.06e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779783 563 KEFILKNSTLMAVN-----DLSLNLYEGQITVLLGHNGAGKTTTLSILTGLYLPTRGKVYISGYDI--SSDMVQIRKSLG 635
Cdd:PRK10982 247 GEVILEVRNLTSLRqpsirDVSFDLHKGEILGIAGLVGAKRTDIVETLFGIREKSAGTITLHGKKInnHNANEAINHGFA 326
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779783 636 LCPQDDL---LFPMLTVSehlhFYCVIKGIplqnqsretNRMLTSFGLLQqSNTMSKD---------------------L 691
Cdd:PRK10982 327 LVTEERRstgIYAYLDIG----FNSLISNI---------RNYKNKVGLLD-NSRMKSDtqwvidsmrvktpghrtqigsL 392
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779783 692 SGGMKRKLSIIIALIGDTKVVILDEPTSGMDPVSRRATWDL-LQHYKKDRTILLTTHHMDEADVLGDRiaILVMGILKCC 770
Cdd:PRK10982 393 SGGNQQKVIIGRWLLTQPEILMLDEPTRGIDVGAKFEIYQLiAELAKKDKGIIIISSEMPELLGITDR--ILVMSNGLVA 470
|
250 260 270
....*....|....*....|....*....|....*..
gi 1039779783 771 GsslflkklygvgyhlvIVKTPDSNDEKIFQLIKNYI 807
Cdd:PRK10982 471 G----------------IVDTKTTTQNEILRLASLHL 491
|
|
| PvdE |
COG4615 |
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ... |
578-727 |
3.44e-06 |
|
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: 50.95 E-value: 3.44e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779783 578 LSLNLYEGQITVLLGHNGAGKTTTLSILTGLYLPTRGKVYISGYDIS---------------SDMVQIRKSLGL--CPQD 640
Cdd:COG4615 351 IDLTIRRGELVFIVGGNGSGKSTLAKLLTGLYRPESGEILLDGQPVTadnreayrqlfsavfSDFHLFDRLLGLdgEADP 430
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779783 641 DLLFPMLtvsEHLHfycvikgipLQNQSRETNRMLtsfgllqqSNTmskDLSGGMKRKLSIIIALIGDTKVVILDEPTSG 720
Cdd:COG4615 431 ARARELL---ERLE---------LDHKVSVEDGRF--------STT---DLSQGQRKRLALLVALLEDRPILVFDEWAAD 487
|
....*..
gi 1039779783 721 MDPVSRR 727
Cdd:COG4615 488 QDPEFRR 494
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
525-764 |
4.50e-06 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 50.87 E-value: 4.50e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779783 525 GEPALSREESQVSD-LLSSDFMEPEPVG---LVAGIRiqhlykEFILKNSTLMAVNDLSLNLYEGQITVLLGHNGAGKTT 600
Cdd:PRK10789 283 GSAAYSRIRAMLAEaPVVKDGSEPVPEGrgeLDVNIR------QFTYPQTDHPALENVNFTLKPGQMLGICGPTGSGKST 356
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779783 601 TLSILTGLYLPTRGKvyISGYDISSDMVQI---RKSLGLCPQDDLLFPMlTVSEHLHFycvikGIP--LQNQSRETNRM- 674
Cdd:PRK10789 357 LLSLIQRHFDVSEGD--IRFHDIPLTKLQLdswRSRLAVVSQTPFLFSD-TVANNIAL-----GRPdaTQQEIEHVARLa 428
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779783 675 -------------LTSFGllqQSNTMskdLSGGMKRKLSIIIALIGDTKVVILDEPTSGMDPVSRRATWDLLQHYKKDRT 741
Cdd:PRK10789 429 svhddilrlpqgyDTEVG---ERGVM---LSGGQKQRISIARALLLNAEILILDDALSAVDGRTEHQILHNLRQWGEGRT 502
|
250 260
....*....|....*....|...
gi 1039779783 742 ILLTTHHMdeaDVLGDRIAILVM 764
Cdd:PRK10789 503 VIISAHRL---SALTEASEILVM 522
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
545-764 |
5.30e-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: 50.45 E-value: 5.30e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779783 545 MEPEPVglvagIRIQHLYKEFILKNSTLMAVNDLSLNLYEGQITVLLGHNGAGKT-TTLSILtGLyLP-----TRGKVYI 618
Cdd:COG4172 1 MMSMPL-----LSVEDLSVAFGQGGGTVEAVKGVSFDIAAGETLALVGESGSGKSvTALSIL-RL-LPdpaahPSGSILF 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779783 619 SGYDISS----DMVQIR-KSLGLCPQDDL--LFPMLTV----SE--HLHfycviKGIPLQNQSRETNRMLTSFGLLQQSN 685
Cdd:COG4172 74 DGQDLLGlserELRRIRgNRIAMIFQEPMtsLNPLHTIgkqiAEvlRLH-----RGLSGAAARARALELLERVGIPDPER 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779783 686 TMSK---DLSGGMKRKLSIIIALIGDTKVVILDEPTSGMDPVSRRATWDLLQHYKKDR--TILLTTHhmDEADV--LGDR 758
Cdd:COG4172 149 RLDAyphQLSGGQRQRVMIAMALANEPDLLIADEPTTALDVTVQAQILDLLKDLQRELgmALLLITH--DLGVVrrFADR 226
|
....*.
gi 1039779783 759 IAilVM 764
Cdd:COG4172 227 VA--VM 230
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
691-747 |
6.93e-06 |
|
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems involved in cellular processes other than transport. These families are characterized by the fact that the ABC subunit is made up of duplicated, fused ABC modules (ABC2). No known transmembrane proteins or domains are associated with these proteins.
Pssm-ID: 213194 [Multi-domain] Cd Length: 162 Bit Score: 47.35 E-value: 6.93e-06
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1039779783 691 LSGGMKRKLSIIIAL----IGDTKVVILDEPTSGMDPVSRRA-TWDLLQHYKKDRTILLTTH 747
Cdd:cd03227 78 LSGGEKELSALALILalasLKPRPLYILDEIDRGLDPRDGQAlAEAILEHLVKGAQVIVITH 139
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
590-722 |
7.31e-06 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 50.51 E-value: 7.31e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779783 590 LLGHNGAGKTTTLSILTGLYLPTRGKVYISGYDISS-DMVQIRKSLGLCPQDDLLFPMlTV-------SEH--------- 652
Cdd:PLN03130 1270 IVGRTGAGKSSMLNALFRIVELERGRILIDGCDISKfGLMDLRKVLGIIPQAPVLFSG-TVrfnldpfNEHndadlwesl 1348
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1039779783 653 --LHFYCVIKgiplQNqsretnrmltSFGLLQQSNTMSKDLSGGMKRKLSIIIALIGDTKVVILDEPTSGMD 722
Cdd:PLN03130 1349 erAHLKDVIR----RN----------SLGLDAEVSEAGENFSVGQRQLLSLARALLRRSKILVLDEATAAVD 1406
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
578-733 |
7.36e-06 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 48.78 E-value: 7.36e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779783 578 LSLNLYEGQITVLLGHNGAGKTTTLSILTGLyLPTRGKVYISGYDIS----SDMVQIRKSlgLCPQDDLLFPM-----LT 648
Cdd:PRK03695 15 LSAEVRAGEILHLVGPNGAGKSTLLARMAGL-LPGSGSIQFAGQPLEawsaAELARHRAY--LSQQQTPPFAMpvfqyLT 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779783 649 VSEHlhfycviKGIPLQNQSRETNRMLTSFGLLQQSNTMSKDLSGGMKRK-------LSIIIALIGDTKVVILDEPTSGM 721
Cdd:PRK03695 92 LHQP-------DKTRTEAVASALNEVAEALGLDDKLGRSVNQLSGGEWQRvrlaavvLQVWPDINPAGQLLLLDEPMNSL 164
|
170
....*....|..
gi 1039779783 722 DpVSRRATWDLL 733
Cdd:PRK03695 165 D-VAQQAALDRL 175
|
|
| ABC_Rad50 |
cd03240 |
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ... |
587-748 |
1.20e-05 |
|
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ATP-binding cassette of ABC transporters, but are not associated with membrane-spanning domains. The conserved ATP-binding motifs common to Rad50 and the ABC transporter family include the Walker A and Walker B motifs, the Q loop, a histidine residue in the switch region, a D-loop, and a conserved LSGG sequence. This conserved sequence, LSGG, is the most specific and characteristic motif of this family and is thus known as the ABC signature sequence.
Pssm-ID: 213207 [Multi-domain] Cd Length: 204 Bit Score: 47.60 E-value: 1.20e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779783 587 ITVLLGHNGAGKTTTLS----ILTGLYLP----------------TRGKVYISGYDISSDMVQIRKSLGL------CPQD 640
Cdd:cd03240 24 LTLIVGQNGAGKTTIIEalkyALTGELPPnskggahdpkliregeVRAQVKLAFENANGKKYTITRSLAIlenvifCHQG 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779783 641 DLLFPMLtvsehlhfycvikgiplqnqsretnRMLTSfgllqqsntmskdLSGGMKRKLSIIIAL------IGDTKVVIL 714
Cdd:cd03240 104 ESNWPLL-------------------------DMRGR-------------CSGGEKVLASLIIRLalaetfGSNCGILAL 145
|
170 180 190
....*....|....*....|....*....|....*..
gi 1039779783 715 DEPTSGMDPVSRR-ATWDLLQHYK--KDRTILLTTHH 748
Cdd:cd03240 146 DEPTTNLDEENIEeSLAEIIEERKsqKNFQLIVITHD 182
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
538-728 |
1.79e-05 |
|
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: 48.78 E-value: 1.79e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779783 538 DLLSSDFMEPE-------PVGLVAG---IRIQHLYKEFILKnstlMAVNDLSLNLYEGQITVLLGHNGAGKTTTLSILTG 607
Cdd:TIGR03719 295 ELLSQEFQKRNetaeiyiPPGPRLGdkvIEAENLTKAFGDK----LLIDDLSFKLPPGGIVGVIGPNGAGKSTLFRMITG 370
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779783 608 LYLPTRGKVYIsgydisSDMVQirksLGLCPQD-DLLFPMLTVSEhlhfycVIKG----IPLQNQSRETNRMLTSF---G 679
Cdd:TIGR03719 371 QEQPDSGTIEI------GETVK----LAYVDQSrDALDPNKTVWE------EISGgldiIKLGKREIPSRAYVGRFnfkG 434
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1039779783 680 LLQQSNTmsKDLSGGMKRKLSIIIALIGDTKVVILDEPTSGMDPVSRRA 728
Cdd:TIGR03719 435 SDQQKKV--GQLSGGERNRVHLAKTLKSGGNVLLLDEPTNDLDVETLRA 481
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
556-774 |
2.35e-05 |
|
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: 48.26 E-value: 2.35e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779783 556 IRIQHLYKEFilknSTLMAVNDLSLNLYEGQITVLLGHNGAGKTTTLSILTGL--YLPTRGKV-YISGYDISSDMVQIRK 632
Cdd:TIGR03269 1 IEVKNLTKKF----DGKEVLKNISFTIEEGEVLGILGRSGAGKSVLMHVLRGMdqYEPTSGRIiYHVALCEKCGYVERPS 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779783 633 SLGL-CPQ---------------DDLLFP--------ML----------TVSEHlhfycVIKGIP-LQNQSRET-NRMLT 676
Cdd:TIGR03269 77 KVGEpCPVcggtlepeevdfwnlSDKLRRrirkriaiMLqrtfalygddTVLDN-----VLEALEeIGYEGKEAvGRAVD 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779783 677 SFGLLQQSNTM---SKDLSGGMKRKLSIIIALIGDTKVVILDEPTSGMDPVSRRATWDLLQHYKKDR--TILLTTHHMDE 751
Cdd:TIGR03269 152 LIEMVQLSHRIthiARDLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALEEAVKASgiSMVLTSHWPEV 231
|
250 260
....*....|....*....|...
gi 1039779783 752 ADVLGDRIAILVMGILKCCGSSL 774
Cdd:TIGR03269 232 IEDLSDKAIWLENGEIKEEGTPD 254
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
614-749 |
2.42e-05 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 48.87 E-value: 2.42e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779783 614 GKVYISGYDISS-DMVQIRKSLGLCPQDDLLFPMlTVSEHLHFycvikgiPLQNQSRETNRMLTSFG--------LLQQS 684
Cdd:PTZ00265 1277 GKILLDGVDICDyNLKDLRNLFSIVSQEPMLFNM-SIYENIKF-------GKEDATREDVKRACKFAaidefiesLPNKY 1348
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1039779783 685 NT----MSKDLSGGMKRKLSIIIALIGDTKVVILDEPTSGMDPVSRRATWDLLQHYKK--DRTILLTTHHM 749
Cdd:PTZ00265 1349 DTnvgpYGKSLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDIKDkaDKTIITIAHRI 1419
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
567-802 |
2.60e-05 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 48.43 E-value: 2.60e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779783 567 LKNSTLmavNDLSLNLYEGQITVLLGHNGAGKTTTLSILTGLYLPtrgkvyisgydISSDMVQIRKSLGLCPQDDLLFPM 646
Cdd:PLN03232 628 TSKPTL---SDINLEIPVGSLVAIVGGTGEGKTSLISAMLGELSH-----------AETSSVVIRGSVAYVPQVSWIFNA 693
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779783 647 lTVSEHLHF---------YCVIKGIPLQNQ-SRETNRMLTSFGllqqsnTMSKDLSGGMKRKLSIIIALIGDTKVVILDE 716
Cdd:PLN03232 694 -TVRENILFgsdfeseryWRAIDVTALQHDlDLLPGRDLTEIG------ERGVNISGGQKQRVSMARAVYSNSDIYIFDD 766
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779783 717 PTSGMDP-VSRRATWDLLQHYKKDRTILLTTHHMDEADVLgDRIAILVMGILKCCG-------SSLFLKKLYGVGYHLVI 788
Cdd:PLN03232 767 PLSALDAhVAHQVFDSCMKDELKGKTRVLVTNQLHFLPLM-DRIILVSEGMIKEEGtfaelskSGSLFKKLMENAGKMDA 845
|
250
....*....|....
gi 1039779783 789 VKTPDSNDEKIFQL 802
Cdd:PLN03232 846 TQEVNTNDENILKL 859
|
|
| PRK13541 |
PRK13541 |
cytochrome c biogenesis protein CcmA; Provisional |
577-750 |
2.60e-05 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184128 [Multi-domain] Cd Length: 195 Bit Score: 46.40 E-value: 2.60e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779783 577 DLSLNLYEGQITVLLGHNGAGKTTTLSILTGLYLPTRGKVYISGYDISS----DMVQIRKSLGLCPQddllfpmLTVSEH 652
Cdd:PRK13541 18 DLSITFLPSAITYIKGANGCGKSSLLRMIAGIMQPSSGNIYYKNCNINNiakpYCTYIGHNLGLKLE-------MTVFEN 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779783 653 LHFYCVIkgiplQNQSRETNRMLTSFGLLQQSNTMSKDLSGGMKRKLSIIIALIGDTKVVILDEPTSGMDPVSRRATWDL 732
Cdd:PRK13541 91 LKFWSEI-----YNSAETLYAAIHYFKLHDLLDEKCYSLSSGMQKIVAIARLIACQSDLWLLDEVETNLSKENRDLLNNL 165
|
170
....*....|....*...
gi 1039779783 733 LQHYKKDRTILLTTHHMD 750
Cdd:PRK13541 166 IVMKANSGGIVLLSSHLE 183
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
585-753 |
3.93e-05 |
|
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a variety of cellular activities. This profile/alignment only detects a fraction of this vast family. The poorly conserved N-terminal helix is missing from the alignment.
Pssm-ID: 214640 [Multi-domain] Cd Length: 148 Bit Score: 45.06 E-value: 3.93e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779783 585 GQITVLLGHNGAGKTTTLSILTGLYLPTRGKV-YISGydissdmvqirkslglcpqddllfpmltvsehlhfycvikgip 663
Cdd:smart00382 2 GEVILIVGPPGSGKTTLARALARELGPPGGGViYIDG------------------------------------------- 38
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779783 664 lqnqsrETNRMLTSFGLLQQSNTMSKDLSGGMKRkLSIIIALI--GDTKVVILDEPTSGMDPVSR-------RATWDLLQ 734
Cdd:smart00382 39 ------EDILEEVLDQLLLIIVGGKKASGSGELR-LRLALALArkLKPDVLILDEITSLLDAEQEallllleELRLLLLL 111
|
170
....*....|....*....
gi 1039779783 735 HYKKDRTILLTTHHMDEAD 753
Cdd:smart00382 112 KSEKNLTVILTTNDEKDLG 130
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
574-762 |
6.00e-05 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 47.03 E-value: 6.00e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779783 574 AVNDLSLNLYEGQITVLLGHNGAGKTTTLSILTGLYLPTRGKVYISGYDI--SSDMVQIRKSLGLCPQDDLLFPMLTVSE 651
Cdd:PRK10982 13 ALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEIdfKSSKEALENGISMVHQELNLVLQRSVMD 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779783 652 HLHF--YcVIKGIPLQNQS--RETNRMLTSFGLLQQSNTMSKDLSGGMKRKLSIIIALIGDTKVVILDEPTSGMDPVSRR 727
Cdd:PRK10982 93 NMWLgrY-PTKGMFVDQDKmyRDTKAIFDELDIDIDPRAKVATLSVSQMQMIEIAKAFSYNAKIVIMDEPTSSLTEKEVN 171
|
170 180 190
....*....|....*....|....*....|....*.
gi 1039779783 728 ATWDLLQHYKKDRT-ILLTTHHMDEADVLGDRIAIL 762
Cdd:PRK10982 172 HLFTIIRKLKERGCgIVYISHKMEEIFQLCDEITIL 207
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
575-728 |
6.96e-05 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 47.09 E-value: 6.96e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779783 575 VNDLSLNLYEGQITVLLGHNGAGKTTTLSILTGLYLPTRGKVYISGydissdmvQIRksLGLCPQDDLLFpmLTVSEHlh 654
Cdd:PRK10636 328 LDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELAPVSGEIGLAK--------GIK--LGYFAQHQLEF--LRADES-- 393
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779783 655 fycvikgiPLQNQSR----ETNRMLT----SFGLL-QQSNTMSKDLSGGMKRKLsiIIALI--GDTKVVILDEPTSGMDP 723
Cdd:PRK10636 394 --------PLQHLARlapqELEQKLRdylgGFGFQgDKVTEETRRFSGGEKARL--VLALIvwQRPNLLLLDEPTNHLDL 463
|
....*
gi 1039779783 724 VSRRA 728
Cdd:PRK10636 464 DMRQA 468
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
584-762 |
7.18e-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: 46.70 E-value: 7.18e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779783 584 EGQITVLLGHNGAGKTTTLSILTGLYLPTRGKV-----------YISG-------YDISSDmvQIRKSLGlcPQD-DLLf 644
Cdd:COG1245 98 KGKVTGILGPNGIGKSTALKILSGELKPNLGDYdeepswdevlkRFRGtelqdyfKKLANG--EIKVAHK--PQYvDLI- 172
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779783 645 PML---TVSEhlhfycVIKGIPLQNQSRETNRMLtsfGLlqqSNTMSKD---LSGGMKRKLSIIIALIGDTKVVILDEPT 718
Cdd:COG1245 173 PKVfkgTVRE------LLEKVDERGKLDELAEKL---GL---ENILDRDiseLSGGELQRVAIAAALLRDADFYFFDEPS 240
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1039779783 719 SGMDPVSRRATWDLLQHY-KKDRTILLTTHHMDEADVLGDRIAIL 762
Cdd:COG1245 241 SYLDIYQRLNVARLIRELaEEGKYVLVVEHDLAILDYLADYVHIL 285
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
577-753 |
9.92e-05 |
|
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: 46.83 E-value: 9.92e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779783 577 DLSLNLYEGQITVLLGHNGAGKTTTLSILTGLYLPTRGKVYISGydissdmvqirkSLGLCPQ----------DDLLFPm 646
Cdd:TIGR01271 444 NISFKLEKGQLLAVAGSTGSGKSSLLMMIMGELEPSEGKIKHSG------------RISFSPQtswimpgtikDNIIFG- 510
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779783 647 LTVSEHlHFYCVIKGIPLQNQsretnrmLTSFGllQQSNTMSKD----LSGGMKRKLSIIIALIGDTKVVILDEPTSGMD 722
Cdd:TIGR01271 511 LSYDEY-RYTSVIKACQLEED-------IALFP--EKDKTVLGEggitLSGGQRARISLARAVYKDADLYLLDSPFTHLD 580
|
170 180 190
....*....|....*....|....*....|....*
gi 1039779783 723 PVSRRATWD--LLQHYKKDRTILLTT--HHMDEAD 753
Cdd:TIGR01271 581 VVTEKEIFEscLCKLMSNKTRILVTSklEHLKKAD 615
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
574-764 |
1.31e-04 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 45.50 E-value: 1.31e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779783 574 AVNDLSLNLYEGQITVLLGHNGAGKT-TTLSILTGLYLPTR---GKVYISGYDISSDMVQIRKSL-----GLCPQDDL-- 642
Cdd:PRK11022 22 AVDRISYSVKQGEVVGIVGESGSGKSvSSLAIMGLIDYPGRvmaEKLEFNGQDLQRISEKERRNLvgaevAMIFQDPMts 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779783 643 LFPMLTVSehlhfYCVIKGIPL-QNQSRETNR-----MLTSFGLLQQSNTMS---KDLSGGMKRKLSIIIALIGDTKVVI 713
Cdd:PRK11022 102 LNPCYTVG-----FQIMEAIKVhQGGNKKTRRqraidLLNQVGIPDPASRLDvypHQLSGGMSQRVMIAMAIACRPKLLI 176
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1039779783 714 LDEPTSGMDPVSRRATWDLL--QHYKKDRTILLTTHhmDEADVLGDRIAILVM 764
Cdd:PRK11022 177 ADEPTTALDVTIQAQIIELLleLQQKENMALVLITH--DLALVAEAAHKIIVM 227
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
584-762 |
1.35e-04 |
|
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: 43.71 E-value: 1.35e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779783 584 EGQITVLLGHNGAGKTTTLSILTGLYLPTRGKVYISGYDISSDmvqirkslglcPQddllfpmltvsehlhfycvikgip 663
Cdd:cd03222 24 EGEVIGIVGPNGTGKTTAVKILAGQLIPNGDNDEWDGITPVYK-----------PQ------------------------ 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779783 664 lqnqsretnrmltsfgllqqsntmSKDLSGGMKRKLSIIIALIGDTKVVILDEPTSGMDPVSR----RATWDLLQHYKKd 739
Cdd:cd03222 69 ------------------------YIDLSGGELQRVAIAAALLRNATFYLFDEPSAYLDIEQRlnaaRAIRRLSEEGKK- 123
|
170 180
....*....|....*....|...
gi 1039779783 740 rTILLTTHHMDEADVLGDRIAIL 762
Cdd:cd03222 124 -TALVVEHDLAVLDYLSDRIHVF 145
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
577-765 |
1.35e-04 |
|
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: 45.23 E-value: 1.35e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779783 577 DLSLNLYEGQITVLLGHNGAGKTTTLSILTGLYLPTRGKVYISGydissdmvqirkSLGLCPQDDLLFPMlTVSEHLHF- 655
Cdd:cd03291 55 NINLKIEKGEMLAITGSTGSGKTSLLMLILGELEPSEGKIKHSG------------RISFSSQFSWIMPG-TIKENIIFg 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779783 656 --------YCVIKGIPLQNQsretnrmLTSFGllQQSNTMSKD----LSGGMKRKLSIIIALIGDTKVVILDEPTSGMDP 723
Cdd:cd03291 122 vsydeyryKSVVKACQLEED-------ITKFP--EKDNTVLGEggitLSGGQRARISLARAVYKDADLYLLDSPFGYLDV 192
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1039779783 724 VSRRATWD-LLQHYKKDRTILLTTHHMDEADVlGDRIAILVMG 765
Cdd:cd03291 193 FTEKEIFEsCVCKLMANKTRILVTSKMEHLKK-ADKILILHEG 234
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
529-749 |
6.78e-04 |
|
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: 44.17 E-value: 6.78e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779783 529 LSREEsqvsdlLSSDFMEPEPVGLVAGIRIQHLYKEFILKNSTLMAVNDLSLNLYEGQITVLLGHNGAGKTTTLSILTGL 608
Cdd:TIGR00957 614 LSHEE------LEPDSIERRTIKPGEGNSITVHNATFTWARDLPPTLNGITFSIPEGALVAVVGQVGCGKSSLLSALLAE 687
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779783 609 YLPTRGKVYISGydissdmvqirkSLGLCPQDDLLfPMLTVSEHLHFYCVIKGiPLQNQSRETNRMLTSFGLL---QQSN 685
Cdd:TIGR00957 688 MDKVEGHVHMKG------------SVAYVPQQAWI-QNDSLRENILFGKALNE-KYYQQVLEACALLPDLEILpsgDRTE 753
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1039779783 686 TMSK--DLSGGMKRKLSIIIALIGDTKVVILDEPTSGMDPVSRRATWDLL---QHYKKDRTILLTTHHM 749
Cdd:TIGR00957 754 IGEKgvNLSGGQKQRVSLARAVYSNADIYLFDDPLSAVDAHVGKHIFEHVigpEGVLKNKTRILVTHGI 822
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
575-607 |
1.05e-03 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 42.12 E-value: 1.05e-03
10 20 30
....*....|....*....|....*....|...
gi 1039779783 575 VNDLSLNLYEGQITVLLGHNGAGKTTTLSILTG 607
Cdd:PRK13547 17 LRDLSLRIEPGRVTALLGRNGAGKSTLLKALAG 49
|
|
| YbjD |
COG3593 |
Predicted ATP-dependent endonuclease of the OLD family, contains P-loop ATPase and TOPRIM ... |
575-747 |
2.61e-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: 41.53 E-value: 2.61e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779783 575 VNDLSLNLyEGQITVLLGHNGAGKTTTLSILTgLYLPTRGKVYISGYD--ISSDMVQIRKSLGLC--------------- 637
Cdd:COG3593 14 IKDLSIEL-SDDLTVLVGENNSGKSSILEALR-LLLGPSSSRKFDEEDfyLGDDPDLPEIEIELTfgsllsrllrlllke 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779783 638 -PQDDLLFPMLTVSEHL-------------HFYCVIKG--IPLQNQSRETNRMLTSFGLLQQSNTMS--KDLSGGMKRKL 699
Cdd:COG3593 92 eDKEELEEALEELNEELkealkalnellseYLKELLDGldLELELSLDELEDLLKSLSLRIEDGKELplDRLGSGFQRLI 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1039779783 700 SIIIALI-------GDTKVVILDEPTSGMDPVSRRATWDLLQHY-KKDRTILLTTH 747
Cdd:COG3593 172 LLALLSAlaelkraPANPILLIEEPEAHLHPQAQRRLLKLLKELsEKPNQVIITTH 227
|
|
| |
