|
Name |
Accession |
Description |
Interval |
E-value |
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
5-565 |
7.45e-157 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 471.92 E-value: 7.45e-157
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 5 VIALNGLSRRFpGmDRPAVAPLTCTIRAGYVTGLVGPDGAGKTTLMRMLAGLLKPDEGRASVIGFDpLKDDSALHAVLG- 83
Cdd:NF033858 1 VARLEGVSHRY-G-KTVALDDVSLDIPAGCMVGLIGPDGVGKSSLLSLIAGARKIQQGRVEVLGGD-MADARHRRAVCPr 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 84 --YMPQKFG--LYEDLTVMENLTLYADLRSVTGEARKKIFDRLLEFTSLGPFTERLAGKLSGGMKQKLGLACTLVGDPKV 159
Cdd:NF033858 78 iaYMPQGLGknLYPTLSVFENLDFFGRLFGQDAAERRRRIDELLRATGLAPFADRPAGKLSGGMKQKLGLCCALIHDPDL 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 160 LLLDEPGVGVDPISRRELWQMVHELAGD--GMLILWSTSYLDEAEQCRDVLLMNEGKLLYQGeptaltqtmagrsflvsS 237
Cdd:NF033858 158 LILDEPTTGVDPLSRRQFWELIDRIRAErpGMSVLVATAYMEEAERFDWLVAMDAGRVLATG-----------------T 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 238 PQEnnrrLLQRAlklpqvsdgviqgksvrlilkkdarieevqqhgdmpplqvadTAPRFEDAFIDLLGGAG-TAESPLgA 316
Cdd:NF033858 221 PAE----LLART------------------------------------------GADTLEAAFIALLPEEKrRGHQPV-V 253
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 317 IIHRVDGSKEETVIEAQSLTKKFGDFAATDHVDFQVKRGEIFGLLGPNGAGKSTTFKMMCGLLVPTSGKALVLGMDLKVS 396
Cdd:NF033858 254 IPPRPADDDDEPAIEARGLTMRFGDFTAVDHVSFRIRRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGEAWLFGQPVDAG 333
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 397 SGKARQHLGYMAQKFSLYGNLSVEQNLRFFSGVYGLRGRAQNEKIARMSDAFGLKSIARHAADELPLGYKQRLALACSLM 476
Cdd:NF033858 334 DIATRRRVGYMSQAFSLYGELTVRQNLELHARLFHLPAAEIAARVAEMLERFDLADVADALPDSLPLGIRQRLSLAVAVI 413
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 477 HEPDILFLDEPTSGVDPLTRREFWLHinsMVD----KGVTVMVTTHFMDEAEYCDRIGLVYHGKLIASGTPDALKAQ--A 550
Cdd:NF033858 414 HKPELLILDEPTSGVDPVARDMFWRL---LIElsreDGVTIFISTHFMNEAERCDRISLMHAGRVLASDTPAALVAArgA 490
|
570
....*....|....*
gi 488984955 551 AddsqtdpTMEQAFI 565
Cdd:NF033858 491 A-------TLEEAFI 498
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
330-570 |
1.61e-109 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 327.41 E-value: 1.61e-109
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 330 IEAQSLTKKFGDFAATDHVDFQVKRGEIFGLLGPNGAGKSTTFKMMCGLLVPTSGKALVLGMDLKVSSGKARQHLGYMAQ 409
Cdd:COG1131 1 IEVRGLTKRYGDKTALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRVLGEDVARDPAEVRRRIGYVPQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 410 KFSLYGNLSVEQNLRFFSGVYGLRGRAQNEKIARMSDAFGLKSIARHAADELPLGYKQRLALACSLMHEPDILFLDEPTS 489
Cdd:COG1131 81 EPALYPDLTVRENLRFFARLYGLPRKEARERIDELLELFGLTDAADRKVGTLSGGMKQRLGLALALLHDPELLILDEPTS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 490 GVDPLTRREFWLHINSMVDKGVTVMVTTHFMDEAEY-CDRIGLVYHGKLIASGTPDALKAQaaddsqtdpTMEQAFITLI 568
Cdd:COG1131 161 GLDPEARRELWELLRELAAEGKTVLLSTHYLEEAERlCDRVAIIDKGRIVADGTPDELKAR---------LLEDVFLELT 231
|
..
gi 488984955 569 NR 570
Cdd:COG1131 232 GE 233
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
6-228 |
8.33e-94 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 286.96 E-value: 8.33e-94
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 6 IALNGLSRRFPgmDRPAVAPLTCTIRAGYVTGLVGPDGAGKTTLMRMLAGLLKPDEGRASVIGFDPLKDDSALHAVLGYM 85
Cdd:COG1131 1 IEVRGLTKRYG--DKTALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRVLGEDVARDPAEVRRRIGYV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 86 PQKFGLYEDLTVMENLTLYADLRSVTGEARKKIFDRLLEFTSLGPFTERLAGKLSGGMKQKLGLACTLVGDPKVLLLDEP 165
Cdd:COG1131 79 PQEPALYPDLTVRENLRFFARLYGLPRKEARERIDELLELFGLTDAADRKVGTLSGGMKQRLGLALALLHDPELLILDEP 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 488984955 166 GVGVDPISRRELWQMVHELAGDGMLILWSTSYLDEAEQ-CRDVLLMNEGKLLYQGEPTALTQTM 228
Cdd:COG1131 159 TSGLDPEARRELWELLRELAAEGKTVLLSTHYLEEAERlCDRVAIIDKGRIVADGTPDELKARL 222
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
329-569 |
4.19e-80 |
|
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: 251.70 E-value: 4.19e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 329 VIEAQSLTKKFGDFAATDHVDFQVKRGEIFGLLGPNGAGKSTTFKMMCGLLVPTSGKALVLGMDLKVSSGKARQHLGYMA 408
Cdd:COG4555 1 MIEVENLSKKYGKVPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIDGEDVRKEPREARRQIGVLP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 409 QKFSLYGNLSVEQNLRFFSGVYGLRGRAQNEKIARMSDAFGLKSIARHAADELPLGYKQRLALACSLMHEPDILFLDEPT 488
Cdd:COG4555 81 DERGLYDRLTVRENIRYFAELYGLFDEELKKRIEELIELLGLEEFLDRRVGELSTGMKKKVALARALVHDPKVLLLDEPT 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 489 SGVDPLTRREFWLHINSMVDKGVTVMVTTHFMDEAE-YCDRIGLVYHGKLIASGTPDALKAQAADDSqtdptMEQAFITL 567
Cdd:COG4555 161 NGLDVMARRLLREILRALKKEGKTVLFSSHIMQEVEaLCDRVVILHKGKVVAQGSLDELREEIGEEN-----LEDAFVAL 235
|
..
gi 488984955 568 IN 569
Cdd:COG4555 236 IG 237
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
330-537 |
9.60e-80 |
|
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: 248.47 E-value: 9.60e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 330 IEAQSLTKKFGDFAATDHVDFQVKRGEIFGLLGPNGAGKSTTFKMMCGLLVPTSGKALVLGMDLKVSSGKARQHLGYMAQ 409
Cdd:cd03230 1 IEVRNLSKRYGKKTALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVLGKDIKKEPEEVKRRIGYLPE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 410 KFSLYGNLSVEQNLRfFSGvyglrgraqnekiarmsdafglksiarhaadelplGYKQRLALACSLMHEPDILFLDEPTS 489
Cdd:cd03230 81 EPSLYENLTVRENLK-LSG-----------------------------------GMKQRLALAQALLHDPELLILDEPTS 124
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 488984955 490 GVDPLTRREFWLHINSMVDKGVTVMVTTHFMDEAE-YCDRIGLVYHGKL 537
Cdd:cd03230 125 GLDPESRREFWELLRELKKEGKTILLSSHILEEAErLCDRVAILNNGRI 173
|
|
| drrA |
TIGR01188 |
daunorubicin resistance ABC transporter ATP-binding subunit; This model describes daunorubicin ... |
337-553 |
1.44e-77 |
|
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: 247.30 E-value: 1.44e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 337 KKFGDFAATDHVDFQVKRGEIFGLLGPNGAGKSTTFKMMCGLLVPTSGKALVLGMDLKVSSGKARQHLGYMAQKFSLYGN 416
Cdd:TIGR01188 1 KVYGDFKAVDGVNFKVREGEVFGFLGPNGAGKTTTIRMLTTLLRPTSGTARVAGYDVVREPRKVRRSIGIVPQYASVDED 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 417 LSVEQNLRFFSGVYGLRGRAQNEKIARMSDAFGLKsiarHAADELPLGY----KQRLALACSLMHEPDILFLDEPTSGVD 492
Cdd:TIGR01188 81 LTGRENLEMMGRLYGLPKDEAEERAEELLELFELG----EAADRPVGTYsggmRRRLDIAASLIHQPDVLFLDEPTTGLD 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 488984955 493 PLTRREFWLHINSMVDKGVTVMVTTHFMDEAE-YCDRIGLVYHGKLIASGTPDALKAQAADD 553
Cdd:TIGR01188 157 PRTRRAIWDYIRALKEEGVTILLTTHYMEEADkLCDRIAIIDHGRIIAEGTPEELKRRLGKD 218
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
330-547 |
1.80e-76 |
|
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: 241.51 E-value: 1.80e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 330 IEAQSLTKKFGDFAATDHVDFQVKRGEIFGLLGPNGAGKSTTFKMMCGLLVPTSGKALVLGMDLKVSSGKARQHLGYMAQ 409
Cdd:cd03265 1 IEVENLVKKYGDFEAVRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATVAGHDVVREPREVRRRIGIVFQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 410 KFSLYGNLSVEQNLRFFSGVYGLRGRAQNEKIARMSDAFGLKSIARHAADELPLGYKQRLALACSLMHEPDILFLDEPTS 489
Cdd:cd03265 81 DLSVDDELTGWENLYIHARLYGVPGAERRERIDELLDFVGLLEAADRLVKTYSGGMRRRLEIARSLVHRPEVLFLDEPTI 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 490 GVDPLTRREFWLHINSMVDK-GVTVMVTTHFMDEAE-YCDRIGLVYHGKLIASGTPDALK 547
Cdd:cd03265 161 GLDPQTRAHVWEYIEKLKEEfGMTILLTTHYMEEAEqLCDRVAIIDHGRIIAEGTPEELK 220
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
3-553 |
1.43e-71 |
|
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: 238.65 E-value: 1.43e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 3 ETVIALNGLSRRFPGMDRPAVAPLTCTIRAGYVTGLVGPDGAGKTTLMRMLAGLLKPD---EGRASVIGFDPLKDDSALH 79
Cdd:COG1123 2 TPLLEVRDLSVRYPGGDVPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGLLPHGgriSGEVLLDGRDLLELSEALR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 80 A-VLGYMPQKFGLYED-LTVMENLTLYADLRSVTGEARKKIFDRLLEFTSLGPFTERLAGKLSGGMKQKLGLACTLVGDP 157
Cdd:COG1123 82 GrRIGMVFQDPMTQLNpVTVGDQIAEALENLGLSRAEARARVLELLEAVGLERRLDRYPHQLSGGQRQRVAIAMALALDP 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 158 KVLLLDEPGVGVDPISRRELWQMVHELAGD-GMLILWSTSYLDE-AEQCRDVLLMNEGKLLYQGEPtaltqtmagrsflv 235
Cdd:COG1123 162 DLLIADEPTTALDVTTQAEILDLLRELQRErGTTVLLITHDLGVvAEIADRVVVMDDGRIVEDGPP-------------- 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 236 sspqennRRLLQRALKLPQVsdgviqgksvrlilkkdarieevqqhgdmPPLQVADTAPRfedafidllggagtaesplg 315
Cdd:COG1123 228 -------EEILAAPQALAAV-----------------------------PRLGAARGRAA-------------------- 251
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 316 aiihrVDGSKEETVIEAQSLTKKF-----GDFAATDHVDFQVKRGEIFGLLGPNGAGKSTTFKMMCGLLVPTSGKALVLG 390
Cdd:COG1123 252 -----PAAAAAEPLLEVRNLSKRYpvrgkGGVRAVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRPTSGSILFDG 326
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 391 MDLKVSSGKA----RQHLGYMAQ--KFSLYGNLSVEQNLRFFSGVYGLRGRAQ-NEKIARMSDAFGLksiARHAADELPL 463
Cdd:COG1123 327 KDLTKLSRRSlrelRRRVQMVFQdpYSSLNPRMTVGDIIAEPLRLHGLLSRAErRERVAELLERVGL---PPDLADRYPH 403
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 464 ----GYKQRLALACSLMHEPDILFLDEPTSGVDPLTRREFwlhINSMVD----KGVTVMVTTHFMDEAEY-CDRIGLVYH 534
Cdd:COG1123 404 elsgGQRQRVAIARALALEPKLLILDEPTSALDVSVQAQI---LNLLRDlqreLGLTYLFISHDLAVVRYiADRVAVMYD 480
|
570
....*....|....*....
gi 488984955 535 GKLIASGTPDALKAQAADD 553
Cdd:COG1123 481 GRIVEDGPTEEVFANPQHP 499
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
330-547 |
3.58e-71 |
|
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: 227.77 E-value: 3.58e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 330 IEAQSLTKKFGD--FAATDHVDFQVKRGEIFGLLGPNGAGKSTTFKMMCGLLVPTSGKALVLGMDLKVSSGKARQHLGYM 407
Cdd:cd03263 1 LQIRNLTKTYKKgtKPAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYINGYSIRTDRKAARQSLGYC 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 408 AQKFSLYGNLSVEQNLRFFSGVYGLRGRAQNEKIARMSDAFGLKSIARHAADELPLGYKQRLALACSLMHEPDILFLDEP 487
Cdd:cd03263 81 PQFDALFDELTVREHLRFYARLKGLPKSEIKEEVELLLRVLGLTDKANKRARTLSGGMKRKLSLAIALIGGPSVLLLDEP 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 488984955 488 TSGVDPLTRREFWLHINSMVdKGVTVMVTTHFMDEAEY-CDRIGLVYHGKLIASGTPDALK 547
Cdd:cd03263 161 TSGLDPASRRAIWDLILEVR-KGRSIILTTHSMDEAEAlCDRIAIMSDGKLRCIGSPQELK 220
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
5-226 |
3.03e-69 |
|
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: 223.58 E-value: 3.03e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 5 VIALNGLSRRFPgmDRPAVAPLTCTIRAGYVTGLVGPDGAGKTTLMRMLAGLLKPDEGRASVIGFDPLKDDSALHAVLGY 84
Cdd:COG4555 1 MIEVENLSKKYG--KVPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIDGEDVRKEPREARRQIGV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 85 MPQKFGLYEDLTVMENLTLYADLRSVTGEARKKIFDRLLEFTSLGPFTERLAGKLSGGMKQKLGLACTLVGDPKVLLLDE 164
Cdd:COG4555 79 LPDERGLYDRLTVRENIRYFAELYGLFDEELKKRIEELIELLGLEEFLDRRVGELSTGMKKKVALARALVHDPKVLLLDE 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 488984955 165 PGVGVDPISRRELWQMVHELAGDGMLILWSTSYLDEAEQ-CRDVLLMNEGKLLYQGEPTALTQ 226
Cdd:COG4555 159 PTNGLDVMARRLLREILRALKKEGKTVLFSSHIMQEVEAlCDRVVILHKGKVVAQGSLDELRE 221
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
6-215 |
3.37e-67 |
|
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: 215.72 E-value: 3.37e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 6 IALNGLSRRFPgmDRPAVAPLTCTIRAGYVTGLVGPDGAGKTTLMRMLAGLLKPDEGRASVIGFDPLKDDSALHAVLGYM 85
Cdd:cd03230 1 IEVRNLSKRYG--KKTALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVLGKDIKKEPEEVKRRIGYL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 86 PQKFGLYEDLTVMENLtlyadlrsvtgearkkifdrlleftslgpfterlagKLSGGMKQKLGLACTLVGDPKVLLLDEP 165
Cdd:cd03230 79 PEEPSLYENLTVRENL------------------------------------KLSGGMKQRLALAQALLHDPELLILDEP 122
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 488984955 166 GVGVDPISRRELWQMVHELAGDGMLILWSTSYLDEAEQ-CRDVLLMNEGKL 215
Cdd:cd03230 123 TSGLDPESRREFWELLRELKKEGKTILLSSHILEEAERlCDRVAILNNGRI 173
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
8-225 |
6.15e-64 |
|
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: 208.90 E-value: 6.15e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 8 LNGLSRRFPGMDRPAVAPLTCTIRAGYVTGLVGPDGAGKTTLMRMLAGLLKPDEGRASVIGFDPLKDDSALHAVLGYMPQ 87
Cdd:cd03263 3 IRNLTKTYKKGTKPAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYINGYSIRTDRKAARQSLGYCPQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 88 KFGLYEDLTVMENLTLYADLRSVTGEARKKIFDRLLEFTSLGPFTERLAGKLSGGMKQKLGLACTLVGDPKVLLLDEPGV 167
Cdd:cd03263 83 FDALFDELTVREHLRFYARLKGLPKSEIKEEVELLLRVLGLTDKANKRARTLSGGMKRKLSLAIALIGGPSVLLLDEPTS 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 488984955 168 GVDPISRRELWQMVHELAGDGMLILwSTSYLDEAEQ-CRDVLLMNEGKLLYQGEPTALT 225
Cdd:cd03263 163 GLDPASRRAIWDLILEVRKGRSIIL-TTHSMDEAEAlCDRIAIMSDGKLRCIGSPQELK 220
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
329-551 |
1.12e-62 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 208.42 E-value: 1.12e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 329 VIEAQSLTKKFGDFAATDHVDFQVKRGEIFGLLGPNGAGKSTTFKMMCGLLVPTSGKALVLGMDLKVssgKARQHLGYMA 408
Cdd:COG4152 1 MLELKGLTKRFGDKTAVDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDSGEVLWDGEPLDP---EDRRRIGYLP 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 409 QKFSLYGNLSVEQNLRFFSGVYGLRGRAQNEKIARMSDAFGLKSIARHAADELPLGYKQRLALACSLMHEPDILFLDEPT 488
Cdd:COG4152 78 EERGLYPKMKVGEQLVYLARLKGLSKAEAKRRADEWLERLGLGDRANKKVEELSKGNQQKVQLIAALLHDPELLILDEPF 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 488984955 489 SGVDPLTRREFWLHINSMVDKGVTVMVTTHFMDEAE-YCDRIGLVYHGKLIASGTPDALKAQAA 551
Cdd:COG4152 158 SGLDPVNVELLKDVIRELAAKGTTVIFSSHQMELVEeLCDRIVIINKGRKVLSGSVDEIRRQFG 221
|
|
| drrA |
TIGR01188 |
daunorubicin resistance ABC transporter ATP-binding subunit; This model describes daunorubicin ... |
19-224 |
9.69e-60 |
|
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: 200.69 E-value: 9.69e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 19 DRPAVAPLTCTIRAGYVTGLVGPDGAGKTTLMRMLAGLLKPDEGRASVIGFDPLKDDSALHAVLGYMPQKFGLYEDLTVM 98
Cdd:TIGR01188 5 DFKAVDGVNFKVREGEVFGFLGPNGAGKTTTIRMLTTLLRPTSGTARVAGYDVVREPRKVRRSIGIVPQYASVDEDLTGR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 99 ENLTLYADLRSVTGEARKKIFDRLLEFTSLGPFTERLAGKLSGGMKQKLGLACTLVGDPKVLLLDEPGVGVDPISRRELW 178
Cdd:TIGR01188 85 ENLEMMGRLYGLPKDEAEERAEELLELFELGEAADRPVGTYSGGMRRRLDIAASLIHQPDVLFLDEPTTGLDPRTRRAIW 164
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 488984955 179 QMVHELAGDGMLILWSTSYLDEAEQ-CRDVLLMNEGKLLYQGEPTAL 224
Cdd:TIGR01188 165 DYIRALKEEGVTILLTTHYMEEADKlCDRIAIIDHGRIIAEGTPEEL 211
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
330-541 |
2.32e-57 |
|
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: 191.43 E-value: 2.32e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 330 IEAQSLTKKFGD----FAATDHVDFQVKRGEIFGLLGPNGAGKSTTFKMMCGLLVPTSGKALVLGMDLKVSSGKARQHLG 405
Cdd:cd03266 2 ITADALTKRFRDvkktVQAVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDGFDVVKEPAEARRRLG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 406 YMAQKFSLYGNLSVEQNLRFFSGVYGLRGRAQNEKIARMSDAFGLKSIARHAADELPLGYKQRLALACSLMHEPDILFLD 485
Cdd:cd03266 82 FVSDSTGLYDRLTARENLEYFAGLYGLKGDELTARLEELADRLGMEELLDRRVGGFSTGMRQKVAIARALVHDPPVLLLD 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 488984955 486 EPTSGVDPLTRREFWLHINSMVDKGVTVMVTTHFMDEAE-YCDRIGLVYHGKLIASG 541
Cdd:cd03266 162 EPTTGLDVMATRALREFIRQLRALGKCILFSTHIMQEVErLCDRVVVLHRGRVVYEG 218
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
6-219 |
3.96e-56 |
|
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: 188.17 E-value: 3.96e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 6 IALNGLSRRFPGmdRPAVAPLTCTIRAGyVTGLVGPDGAGKTTLMRMLAGLLKPDEGRASVIGFDPLKDDSALHAVLGYM 85
Cdd:cd03264 1 LQLENLTKRYGK--KRALDGVSLTLGPG-MYGLLGPNGAGKTTLMRILATLTPPSSGTIRIDGQDVLKQPQKLRRRIGYL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 86 PQKFGLYEDLTVMENLTLYADLRSVTGEARKKIFDRLLEFTSLGPFTERLAGKLSGGMKQKLGLACTLVGDPKVLLLDEP 165
Cdd:cd03264 78 PQEFGVYPNFTVREFLDYIAWLKGIPSKEVKARVDEVLELVNLGDRAKKKIGSLSGGMRRRVGIAQALVGDPSILIVDEP 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 488984955 166 GVGVDPISRRELWQMVHELAGDGMLILwSTSYL-DEAEQCRDVLLMNEGKLLYQG 219
Cdd:cd03264 158 TAGLDPEERIRFRNLLSELGEDRIVIL-STHIVeDVESLCNQVAVLNKGKLVFEG 211
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
6-224 |
4.89e-56 |
|
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: 187.96 E-value: 4.89e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 6 IALNGLSRRFPGMDrpAVAPLTCTIRAGYVTGLVGPDGAGKTTLMRMLAGLLKPDEGRASVIGFDPLKDDSALHAVLGYM 85
Cdd:cd03265 1 IEVENLVKKYGDFE--AVRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATVAGHDVVREPREVRRRIGIV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 86 PQKFGLYEDLTVMENLTLYADLRSVTGEARKKIFDRLLEFTSLGPFTERLAGKLSGGMKQKLGLACTLVGDPKVLLLDEP 165
Cdd:cd03265 79 FQDLSVDDELTGWENLYIHARLYGVPGAERRERIDELLDFVGLLEAADRLVKTYSGGMRRRLEIARSLVHRPEVLFLDEP 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 488984955 166 GVGVDPISRRELWQMVHEL-AGDGMLILWSTSYLDEAEQ-CRDVLLMNEGKLLYQGEPTAL 224
Cdd:cd03265 159 TIGLDPQTRAHVWEYIEKLkEEFGMTILLTTHYMEEAEQlCDRVAIIDHGRIIAEGTPEEL 219
|
|
| PQQ_ABC_ATP |
TIGR03864 |
ABC transporter, ATP-binding subunit, PQQ-dependent alcohol dehydrogenase system; Members of ... |
330-567 |
2.42e-54 |
|
ABC transporter, ATP-binding subunit, PQQ-dependent alcohol dehydrogenase system; Members of this protein family are the ATP-binding subunit of an ABC transporter system that is associated with PQQ biosynthesis and PQQ-dependent alcohol dehydrogenases. While this family shows homology to several efflux ABC transporter subunits, the presence of a periplasmic substrate-binding protein and association with systems for catabolism of alcohols suggests a role in import rather than detoxification. [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 274822 [Multi-domain] Cd Length: 236 Bit Score: 184.03 E-value: 2.42e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 330 IEAQSLTKKFGDFAATDHVDFQVKRGEIFGLLGPNGAGKSTTFKMMCGLLVPTSGKALVLGMDLKVSSGKARQHLGYMAQ 409
Cdd:TIGR03864 2 LEVAGLSFRYGARRALDDVSFTVRPGRFVALLGPNGAGKSTLFSLLTRLYVAQSGQISVAGHDLRRAPRAALARLGVVFQ 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 410 KFSLYGNLSVEQNLRFFSGVYGLRGRAQNEKIARMSDAFGLKSIARHAADELPLGYKQRLALACSLMHEPDILFLDEPTS 489
Cdd:TIGR03864 82 QPTLDLDLSVRQNLRYHAALHGLSRAEARARIAELLARLGLAERADDKVRELNGGHRRRVEIARALLHRPALLLLDEPTV 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 488984955 490 GVDPLTRREFWLHINSMV-DKGVTVMVTTHFMDEAEYCDRIGLVYHGKLIASGTPDALKAQAADDsqtdpTMEQAFITL 567
Cdd:TIGR03864 162 GLDPASRAAITAHVRALArDQGLSVLWATHLVDEIEASDRLVVLHRGRVLADGAAAELRGATGGA-----DLEAAFLAL 235
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
5-307 |
5.69e-54 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 185.31 E-value: 5.69e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 5 VIALNGLSRRFpGmDRPAVAPLTCTIRAGYVTGLVGPDGAGKTTLMRMLAGLLKPDEGRASVIGfDPLkdDSALHAVLGY 84
Cdd:COG4152 1 MLELKGLTKRF-G-DKTAVDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDSGEVLWDG-EPL--DPEDRRRIGY 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 85 MPQKFGLYEDLTVMENLTLYADLRSVT-GEARKKIfDRLLEFTSLGPFTERLAGKLSGGMKQKLGLACTLVGDPKVLLLD 163
Cdd:COG4152 76 LPEERGLYPKMKVGEQLVYLARLKGLSkAEAKRRA-DEWLERLGLGDRANKKVEELSKGNQQKVQLIAALLHDPELLILD 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 164 EPGVGVDPISRRELWQMVHELAGDGMLILWSTSYLDEAEQ-CRDVLLMNEGKLLYQGEPTALTQTMAGRSFLVSSpqENN 242
Cdd:COG4152 155 EPFSGLDPVNVELLKDVIRELAAKGTTVIFSSHQMELVEElCDRIVIINKGRKVLSGSVDEIRRQFGRNTLRLEA--DGD 232
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 488984955 243 RRLLQralKLPQVSDGVIQGKSVRLILKKDARIEEV----QQHGDMPPLQVadTAPRFEDAFIDLLGGA 307
Cdd:COG4152 233 AGWLR---ALPGVTVVEEDGDGAELKLEDGADAQELlralLARGPVREFEE--VRPSLNEIFIEVVGEK 296
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
330-541 |
3.15e-53 |
|
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: 180.11 E-value: 3.15e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 330 IEAQSLTKKFGDFAATDHVDFQVKRGEIFGLLGPNGAGKSTTFKMMCGLLVPTSGKALVLGMDlKVSSGKARQHLGYMAQ 409
Cdd:cd03268 1 LKTNDLTKTYGKKRVLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEITFDGKS-YQKNIEALRRIGALIE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 410 KFSLYGNLSVEQNLRFFSGVYGLRgraqNEKIARMSDAFGLKSIARHAADELPLGYKQRLALACSLMHEPDILFLDEPTS 489
Cdd:cd03268 80 APGFYPNLTARENLRLLARLLGIR----KKRIDEVLDVVGLKDSAKKKVKGFSLGMKQRLGIALALLGNPDLLILDEPTN 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 488984955 490 GVDPLTRREFWLHINSMVDKGVTVMVTTHFMDEAE-YCDRIGLVYHGKLIASG 541
Cdd:cd03268 156 GLDPDGIKELRELILSLRDQGITVLISSHLLSEIQkVADRIGIINKGKLIEEG 208
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
327-548 |
4.41e-53 |
|
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: 180.95 E-value: 4.41e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 327 ETVIEAQSLTKKFGDFAATDHVDFQVKRGEIFGLLGPNGAGKSTTFKMMCGLLVPTSGKALVLGMDLKVSSGKA----RQ 402
Cdd:COG1127 3 EPMIEVRNLTKSFGDRVVLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEILVDGQDITGLSEKElyelRR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 403 HLGYMAQKFSLYGNLSVEQNLRFfsgvyGLR-----GRAQNEKIARMS-DAFGLKSIARHAADELPLGYKQRLALACSLM 476
Cdd:COG1127 83 RIGMLFQGGALFDSLTVFENVAF-----PLRehtdlSEAEIRELVLEKlELVGLPGAADKMPSELSGGMRKRVALARALA 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 488984955 477 HEPDILFLDEPTSGVDPLTRREFWLHINSMVDK-GVTVMVTTHFMDEA-EYCDRIGLVYHGKLIASGTPDALKA 548
Cdd:COG1127 158 LDPEILLYDEPTAGLDPITSAVIDELIRELRDElGLTSVVVTHDLDSAfAIADRVAVLADGKIIAEGTPEELLA 231
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
327-548 |
5.50e-52 |
|
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: 178.69 E-value: 5.50e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 327 ETVIEAQSLTKKFGDFAATDHVDFQVKRGEIFGLLGPNGAGKSTTFKMMCGLLVPTSGKALVLGMDLkvsSGKA---RQH 403
Cdd:COG0411 2 DPLLEVRGLTKRFGGLVAVDDVSLEVERGEIVGLIGPNGAGKTTLFNLITGFYRPTSGRILFDGRDI---TGLPphrIAR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 404 LGyMAQKF---SLYGNLSVEQNLR----------FFSGVYGLRGRAQNEKIAR-----MSDAFGLKSIARHAADELPLGY 465
Cdd:COG0411 79 LG-IARTFqnpRLFPELTVLENVLvaaharlgrgLLAALLRLPRARREEREAReraeeLLERVGLADRADEPAGNLSYGQ 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 466 KQRLALACSLMHEPDILFLDEPTSGVDPLTRREFWLHINSMVDK-GVTVMVTTHFMDE-AEYCDRIGLVYHGKLIASGTP 543
Cdd:COG0411 158 QRRLEIARALATEPKLLLLDEPAAGLNPEETEELAELIRRLRDErGITILLIEHDMDLvMGLADRIVVLDFGRVIAEGTP 237
|
....*
gi 488984955 544 DALKA 548
Cdd:COG0411 238 AEVRA 242
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
330-548 |
6.22e-52 |
|
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: 177.73 E-value: 6.22e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 330 IEAQSLTKKFGDFAATDHVDFQVKRGEIFGLLGPNGAGKSTTFKMMCGLLVPTSGKALVLGMDL--KVSSGKARQHLGYM 407
Cdd:cd03218 1 LRAENLSKRYGKRKVVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDGQDItkLPMHKRARLGIGYL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 408 AQKFSLYGNLSVEQNLRFFSGVYGLRGRAQNEKIARMSDAFGLKSIARHAADELPLGYKQRLALACSLMHEPDILFLDEP 487
Cdd:cd03218 81 PQEASIFRKLTVEENILAVLEIRGLSKKEREEKLEELLEEFHITHLRKSKASSLSGGERRRVEIARALATNPKFLLLDEP 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 488984955 488 TSGVDPLTRREFWLHINSMVDKGVTVMVTTHFMDEA-EYCDRIGLVYHGKLIASGTPDALKA 548
Cdd:cd03218 161 FAGVDPIAVQDIQKIIKILKDRGIGVLITDHNVRETlSITDRAYIIYEGKVLAEGTPEEIAA 222
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
330-546 |
1.43e-51 |
|
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: 176.37 E-value: 1.43e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 330 IEAQSLTKKF-GDFAATDHVDFQVKRGEIFGLLGPNGAGKSTTFKMMCGLLVPTSGKALVLGMDLKVSSGKA-RQHLGYM 407
Cdd:COG1122 1 IELENLSFSYpGGTPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVDGKDITKKNLRElRRKVGLV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 408 -----AQKFSLygnlSVEQNLRFfsgvyGLR--GRAQNEKIARMSDA---FGLKSIARHAADELPLGYKQRLALACSLMH 477
Cdd:COG1122 81 fqnpdDQLFAP----TVEEDVAF-----GPEnlGLPREEIRERVEEAlelVGLEHLADRPPHELSGGQKQRVAIAGVLAM 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 478 EPDILFLDEPTSGVDPLTRREFWLHINSMVDKGVTVMVTTHFMDEA-EYCDRIGLVYHGKLIASGTPDAL 546
Cdd:COG1122 152 EPEVLVLDEPTAGLDPRGRRELLELLKRLNKEGKTVIIVTHDLDLVaELADRVIVLDDGRIVADGTPREV 221
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
330-541 |
1.52e-51 |
|
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: 175.93 E-value: 1.52e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 330 IEAQSLTKKFGDFAATDHVDFQVKRGEIFGLLGPNGAGKSTTFKMMCGLLVPTSGKALVLGmdlKVSSGKARQHLGYMAQ 409
Cdd:cd03269 1 LEVENVTKRFGRVTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDG---KPLDIAARNRIGYLPE 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 410 KFSLYGNLSVEQNLRFFSGVYGLRGRAQNEKIARMSDAFGLKSIARHAADELPLGYKQRLALACSLMHEPDILFLDEPTS 489
Cdd:cd03269 78 ERGLYPKMKVIDQLVYLAQLKGLKKEEARRRIDEWLERLELSEYANKRVEELSKGNQQKVQFIAAVIHDPELLILDEPFS 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 488984955 490 GVDPLTRREFWLHINSMVDKGVTVMVTTHFMDEAE-YCDRIGLVYHGKLIASG 541
Cdd:cd03269 158 GLDPVNVELLKDVIRELARAGKTVILSTHQMELVEeLCDRVLLLNKGRAVLYG 210
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
330-548 |
2.47e-51 |
|
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: 176.09 E-value: 2.47e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 330 IEAQSLTKKFGDFAATDHVDFQVKRGEIFGLLGPNGAGKSTTFKMMCGLLVPTSGKALVLGMDlkVSSGKARQ--HLGyM 407
Cdd:cd03219 1 LEVRGLTKRFGGLVALDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFDGED--ITGLPPHEiaRLG-I 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 408 AQKF---SLYGNLSVEQNLR----------FFSGVYGLRGRAQNEKIARMSDAFGLKSIARHAADELPLGYKQRLALACS 474
Cdd:cd03219 78 GRTFqipRLFPELTVLENVMvaaqartgsgLLLARARREEREARERAEELLERVGLADLADRPAGELSYGQQRRLEIARA 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 488984955 475 LMHEPDILFLDEPTSGVDPLTRREFWLHINSMVDKGVTVMVTTHFMDE-AEYCDRIGLVYHGKLIASGTPDALKA 548
Cdd:cd03219 158 LATDPKLLLLDEPAAGLNPEETEELAELIRELRERGITVLLVEHDMDVvMSLADRVTVLDQGRVIAEGTPDEVRN 232
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
329-549 |
5.47e-51 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 177.97 E-value: 5.47e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 329 VIEAQSLTKKF-------GDFA--------------ATDHVDFQVKRGEIFGLLGPNGAGKSTTFKMMCGLLVPTSGKAL 387
Cdd:COG4586 1 IIEVENLSKTYrvyekepGLKGalkglfrreyreveAVDDISFTIEPGEIVGFIGPNGAGKSTTIKMLTGILVPTSGEVR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 388 VLGMDlkvsSGKARQHLGY-----MAQKFSLYGNLSVEQNLRFFSGVYGLRGRAQNEKIARMSDAFGLKSIARHAADELP 462
Cdd:COG4586 81 VLGYV----PFKRRKEFARrigvvFGQRSQLWWDLPAIDSFRLLKAIYRIPDAEYKKRLDELVELLDLGELLDTPVRQLS 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 463 LGYKQRLALACSLMHEPDILFLDEPTSGVDPLTR---REFWLHINSmvDKGVTVMVTTHFMDEAEY-CDRIGLVYHGKLI 538
Cdd:COG4586 157 LGQRMRCELAAALLHRPKILFLDEPTIGLDVVSKeaiREFLKEYNR--ERGTTILLTSHDMDDIEAlCDRVIVIDHGRII 234
|
250
....*....|.
gi 488984955 539 ASGTPDALKAQ 549
Cdd:COG4586 235 YDGSLEELKER 245
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
6-219 |
4.29e-50 |
|
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: 172.17 E-value: 4.29e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 6 IALNGLSRRFPGMDRP--AVAPLTCTIRAGYVTGLVGPDGAGKTTLMRMLAGLLKPDEGRASVIGFDPLKDDSALHAVLG 83
Cdd:cd03266 2 ITADALTKRFRDVKKTvqAVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDGFDVVKEPAEARRRLG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 84 YMPQKFGLYEDLTVMENLTLYADLRSVTGEARKKIFDRLLEFTSLGPFTERLAGKLSGGMKQKLGLACTLVGDPKVLLLD 163
Cdd:cd03266 82 FVSDSTGLYDRLTARENLEYFAGLYGLKGDELTARLEELADRLGMEELLDRRVGGFSTGMRQKVAIARALVHDPPVLLLD 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 488984955 164 EPGVGVDPISRRELWQMVHELAGDGMLILWSTSYLDEAEQ-CRDVLLMNEGKLLYQG 219
Cdd:cd03266 162 EPTTGLDVMATRALREFIRQLRALGKCILFSTHIMQEVERlCDRVVVLHRGRVVYEG 218
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
289-546 |
5.43e-50 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 176.17 E-value: 5.43e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 289 VADTAPRFedafIDLLGGAGTAESPLGAIIHRVdGSKEETVIEAQSLTKKFGDFAATDHVDFQVKRGEIFGLLGPNGAGK 368
Cdd:PRK13536 6 VAEEAPRR----LELSPIERKHQGISEAKASIP-GSMSTVAIDLAGVSKSYGDKAVVNGLSFTVASGECFGLLGPNGAGK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 369 STTFKMMCGLLVPTSGKALVLGMDLKVSSGKARQHLGYMAQKFSLYGNLSVEQNLRFFSGVYGLRGRAQNEKIARMSDAF 448
Cdd:PRK13536 81 STIARMILGMTSPDAGKITVLGVPVPARARLARARIGVVPQFDNLDLEFTVRENLLVFGRYFGMSTREIEAVIPSLLEFA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 449 GLKSIARHAADELPLGYKQRLALACSLMHEPDILFLDEPTSGVDPLTRREFWLHINSMVDKGVTVMVTTHFMDEAE-YCD 527
Cdd:PRK13536 161 RLESKADARVSDLSGGMKRRLTLARALINDPQLLILDEPTTGLDPHARHLIWERLRSLLARGKTILLTTHFMEEAErLCD 240
|
250
....*....|....*....
gi 488984955 528 RIGLVYHGKLIASGTPDAL 546
Cdd:PRK13536 241 RLCVLEAGRKIAEGRPHAL 259
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
329-567 |
1.64e-49 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 184.17 E-value: 1.64e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 329 VIEAQSLTKKFGDFAATDHVDFQVKRGEIFGLLGPNGAGKSTTFKMMCGLLVPTSGKALVLGMDLkvSSGKARQHLG--- 405
Cdd:NF033858 1 VARLEGVSHRYGKTVALDDVSLDIPAGCMVGLIGPDGVGKSSLLSLIAGARKIQQGRVEVLGGDM--ADARHRRAVCpri 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 406 -YMAQ---KfSLYGNLSVEQNLRFFSGVYGLRGRAQNEKIARMSDAFGLKSIARHAADELPLGYKQRLALACSLMHEPDI 481
Cdd:NF033858 79 aYMPQglgK-NLYPTLSVFENLDFFGRLFGQDAAERRRRIDELLRATGLAPFADRPAGKLSGGMKQKLGLCCALIHDPDL 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 482 LFLDEPTSGVDPLTRREFWLHINSMVDK--GVTVMVTTHFMDEAEYCDRIGLVYHGKLIASGTPDALKAQAADDsqtdpT 559
Cdd:NF033858 158 LILDEPTTGVDPLSRRQFWELIDRIRAErpGMSVLVATAYMEEAERFDWLVAMDAGRVLATGTPAELLARTGAD-----T 232
|
....*...
gi 488984955 560 MEQAFITL 567
Cdd:NF033858 233 LEAAFIAL 240
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
5-209 |
1.80e-49 |
|
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: 169.97 E-value: 1.80e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 5 VIALNGLSRRFPgmDRPAVAPLTCTIRAGYVTGLVGPDGAGKTTLMRMLAGLLKPDEGRASVIGFDPLKDDSALHAVLGY 84
Cdd:COG4133 2 MLEAENLSCRRG--ERLLFSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWNGEPIRDAREDYRRRLAY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 85 MPQKFGLYEDLTVMENLTLYADLRSVTGEARKkiFDRLLEFTSLGPFTERLAGKLSGGMKQKLGLACTLVGDPKVLLLDE 164
Cdd:COG4133 80 LGHADGLKPELTVRENLRFWAALYGLRADREA--IDEALEAVGLAGLADLPVRQLSAGQKRRVALARLLLSPAPLWLLDE 157
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 488984955 165 PGVGVDPISRRELWQMVHELAGDGMLILWSTSYLDEAEQCRDVLL 209
Cdd:COG4133 158 PFTALDAAGVALLAELIAAHLARGGAVLLTTHQPLELAAARVLDL 202
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
327-546 |
2.63e-49 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 173.07 E-value: 2.63e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 327 ETVIEAQSLTKKFGDFAATDHVDFQVKRGEIFGLLGPNGAGKSTTFKMMCGLLVPTSGKALVLGMDLKVSSGKARQHLGY 406
Cdd:PRK13537 5 VAPIDFRNVEKRYGDKLVVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCGEPVPSRARHARQRVGV 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 407 MAQKFSLYGNLSVEQNLRFFSGVYGLRGRAQNEKIARMSDAFGLKSIARHAADELPLGYKQRLALACSLMHEPDILFLDE 486
Cdd:PRK13537 85 VPQFDNLDPDFTVRENLLVFGRYFGLSAAAARALVPPLLEFAKLENKADAKVGELSGGMKRRLTLARALVNDPDVLVLDE 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 488984955 487 PTSGVDPLTRREFWLHINSMVDKGVTVMVTTHFMDEAE-YCDRIGLVYHGKLIASGTPDAL 546
Cdd:PRK13537 165 PTTGLDPQARHLMWERLRSLLARGKTILLTTHFMEEAErLCDRLCVIEEGRKIAEGAPHAL 225
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
324-541 |
1.46e-48 |
|
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: 168.66 E-value: 1.46e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 324 SKEETVIEA-QSLTK-KFGDFAATDHVDFQVKRGEIFGLLGPNGAGKSTTFKMMCGLLVPTSGKALVLGMD-LKVSSGKA 400
Cdd:cd03267 14 SKEPGLIGSlKSLFKrKYREVEALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRVAGLVpWKRRKKFL 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 401 RQHLGYMAQKFSLYGNLSVEQNLRFFSGVYGLRGRAQNEKIARMSDAFGLKSIARHAADELPLGYKQRLALACSLMHEPD 480
Cdd:cd03267 94 RRIGVVFGQKTQLWWDLPVIDSFYLLAAIYDLPPARFKKRLDELSELLDLEELLDTPVRQLSLGQRMRAEIAAALLHEPE 173
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 488984955 481 ILFLDEPTSGVDPLTR---REFWLHINSmvDKGVTVMVTTHFMDEAE-YCDRIGLVYHGKLIASG 541
Cdd:cd03267 174 ILFLDEPTIGLDVVAQeniRNFLKEYNR--ERGTTVLLTSHYMKDIEaLARRVLVIDKGRLLYDG 236
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
6-219 |
1.29e-47 |
|
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: 165.08 E-value: 1.29e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 6 IALNGLSRRFPGmdRPAVAPLTCTIRAGYVTGLVGPDGAGKTTLMRMLAGLLKPDEGRASVIGFDPLKDDSALhAVLGYM 85
Cdd:cd03268 1 LKTNDLTKTYGK--KRVLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEITFDGKSYQKNIEAL-RRIGAL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 86 PQKFGLYEDLTVMENLTLYADLRSVtgeaRKKIFDRLLEFTSLGPFTERLAGKLSGGMKQKLGLACTLVGDPKVLLLDEP 165
Cdd:cd03268 78 IEAPGFYPNLTARENLRLLARLLGI----RKKRIDEVLDVVGLKDSAKKKVKGFSLGMKQRLGIALALLGNPDLLILDEP 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 488984955 166 GVGVDPISRRELWQMVHELAGDGMLILWSTSYLDEAEQ-CRDVLLMNEGKLLYQG 219
Cdd:cd03268 154 TNGLDPDGIKELRELILSLRDQGITVLISSHLLSEIQKvADRIGIINKGKLIEEG 208
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
6-219 |
4.89e-47 |
|
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the subfamily A transporters involved in drug resistance, nodulation, lipid transport, and bacteriocin and lantibiotic immunity. In eubacteria and archaea, the typical organization consists of one ABC and one or two integral membranes. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region in addition to the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213236 [Multi-domain] Cd Length: 210 Bit Score: 163.61 E-value: 4.89e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 6 IALNGLSRRFPgmDRPAVAPLTCTIRAGYVTGLVGPDGAGKTTLMRMLAGLLKPDEGrasVIGFDPLKDDSALHAVLGYM 85
Cdd:cd03269 1 LEVENVTKRFG--RVTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSG---EVLFDGKPLDIAARNRIGYL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 86 PQKFGLYEDLTVMENLTLYADLRSVT-GEARKKIfDRLLEFTSLGPFTERLAGKLSGGMKQKLGLACTLVGDPKVLLLDE 164
Cdd:cd03269 76 PEERGLYPKMKVIDQLVYLAQLKGLKkEEARRRI-DEWLERLELSEYANKRVEELSKGNQQKVQFIAAVIHDPELLILDE 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 488984955 165 PGVGVDPISRRELWQMVHELAGDGMLILWSTSYLDEAEQ-CRDVLLMNEGKLLYQG 219
Cdd:cd03269 155 PFSGLDPVNVELLKDVIRELARAGKTVILSTHQMELVEElCDRVLLLNKGRAVLYG 210
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
330-548 |
7.19e-47 |
|
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: 164.21 E-value: 7.19e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 330 IEAQSLTKKFGDFAATDHVDFQVKRGEIFGLLGPNGAGKSTTFKMMCGLLVPTSGKALVLGMDLKVSSGKARQHL----G 405
Cdd:cd03261 1 IELRGLTKSFGGRTVLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGEDISGLSEAELYRLrrrmG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 406 YMAQKFSLYGNLSVEQNLRFFSGVYGLRGRAQNEKIARMS-DAFGLKSIARHAADELPLGYKQRLALACSLMHEPDILFL 484
Cdd:cd03261 81 MLFQSGALFDSLTVFENVAFPLREHTRLSEEEIREIVLEKlEAVGLRGAEDLYPAELSGGMKKRVALARALALDPELLLY 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 488984955 485 DEPTSGVDPLTRREFWLHINSMVD-KGVTVMVTTHFMDEA-EYCDRIGLVYHGKLIASGTPDALKA 548
Cdd:cd03261 161 DEPTAGLDPIASGVIDDLIRSLKKeLGLTSIMVTHDLDTAfAIADRIAVLYDGKIVAEGTPEELRA 226
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
327-546 |
1.06e-46 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 164.05 E-value: 1.06e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 327 ETVIEAQSLTKKFGDFAATDHVDFQVKRGEIFGLLGPNGAGKSTTFKMMCGLLVPTSGKALVLGMDlkVSS----GKARQ 402
Cdd:COG1137 1 MMTLEAENLVKSYGKRTVVKDVSLEVNQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGRIFLDGED--ITHlpmhKRARL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 403 HLGYMAQKFSLYGNLSVEQNLRFFSGVYGLRGRAQNEKIARMSDAFGLKSIARHAADELPLGYKQRLALACSLMHEPDIL 482
Cdd:COG1137 79 GIGYLPQEASIFRKLTVEDNILAVLELRKLSKKEREERLEELLEEFGITHLRKSKAYSLSGGERRRVEIARALATNPKFI 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 488984955 483 FLDEPTSGVDPLTRREfwlhINSMV----DKGVTVMVTTHFMDEA-EYCDRIGLVYHGKLIASGTPDAL 546
Cdd:COG1137 159 LLDEPFAGVDPIAVAD----IQKIIrhlkERGIGVLITDHNVRETlGICDRAYIISEGKVLAEGTPEEI 223
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
6-549 |
5.66e-45 |
|
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: 166.90 E-value: 5.66e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 6 IALNGLSRRFPGMDrpAVAPLTCTIRAGYVTGLVGPDGAGKTTLMRMLAGL--LKPDEGRA----------------SVI 67
Cdd:TIGR03269 1 IEVKNLTKKFDGKE--VLKNISFTIEEGEVLGILGRSGAGKSVLMHVLRGMdqYEPTSGRIiyhvalcekcgyverpSKV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 68 G---------FDPLKDD---------SALHAVLGYMPQK-FGLYEDLTVMEN-LTLYADLRSVTGEARKKIFDrLLEFTS 127
Cdd:TIGR03269 79 GepcpvcggtLEPEEVDfwnlsdklrRRIRKRIAIMLQRtFALYGDDTVLDNvLEALEEIGYEGKEAVGRAVD-LIEMVQ 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 128 LGPFTERLAGKLSGGMKQKLGLACTLVGDPKVLLLDEPGVGVDPISRRELWQMVHELAGDGMLILWSTSYLDE--AEQCR 205
Cdd:TIGR03269 158 LSHRITHIARDLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALEEAVKASGISMVLTSHWPEviEDLSD 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 206 DVLLMNEGKLLYQGEPTALTqtmagrsflvsspqennrrllqrALKLPQVSDgviqgksvrliLKKDariEEVQQHGDmp 285
Cdd:TIGR03269 238 KAIWLENGEIKEEGTPDEVV-----------------------AVFMEGVSE-----------VEKE---CEVEVGEP-- 278
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 286 plqvadtaprfedafidllggagtaesplgaIIHRVDGSKEETVIEAqsltkkfGDFAATDHVDFQVKRGEIFGLLGPNG 365
Cdd:TIGR03269 279 -------------------------------IIKVRNVSKRYISVDR-------GVVKAVDNVSLEVKEGEIFGIVGTSG 320
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 366 AGKSTTFKMMCGLLVPTSGKALVL-----------GMDLKvssGKARQHLGYMAQKFSLYGNLSVEQNLRFFSG------ 428
Cdd:TIGR03269 321 AGKTTLSKIIAGVLEPTSGEVNVRvgdewvdmtkpGPDGR---GRAKRYIGILHQEYDLYPHRTVLDNLTEAIGlelpde 397
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 429 ------VYGLRGRAQNEKIARmsdafglkSIARHAADELPLGYKQRLALACSLMHEPDILFLDEPTSGVDPLTRREFWLH 502
Cdd:TIGR03269 398 larmkaVITLKMVGFDEEKAE--------EILDKYPDELSEGERHRVALAQVLIKEPRIVILDEPTGTMDPITKVDVTHS 469
|
570 580 590 600
....*....|....*....|....*....|....*....|....*....
gi 488984955 503 I-NSMVDKGVTVMVTTHFMDEA-EYCDRIGLVYHGKLIASGTPDALKAQ 549
Cdd:TIGR03269 470 IlKAREEMEQTFIIVSHDMDFVlDVCDRAALMRDGKIVKIGDPEEIVEE 518
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
330-536 |
7.15e-45 |
|
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is comprised of all BPD (Binding Protein Dependent) systems that are largely represented in archaea and eubacteria and are primarily involved in scavenging solutes from the environment. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213196 [Multi-domain] Cd Length: 178 Bit Score: 156.96 E-value: 7.15e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 330 IEAQSLTKKFGDFAATDHVDFQVKRGEIFGLLGPNGAGKSTTFKMMCGLLVPTSGKALVLG---MDLKVSSGKARQHLGY 406
Cdd:cd03229 1 LELKNVSKRYGQKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGedlTDLEDELPPLRRRIGM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 407 MAQKFSLYGNLSVEQNLrffsgVYGLRGraqnekiarmsdafglksiarhaadelplGYKQRLALACSLMHEPDILFLDE 486
Cdd:cd03229 81 VFQDFALFPHLTVLENI-----ALGLSG-----------------------------GQQQRVALARALAMDPDVLLLDE 126
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 488984955 487 PTSGVDPLTRREFWLHINSMVDK-GVTVMVTTHFMDEAEY-CDRIGLVYHGK 536
Cdd:cd03229 127 PTSALDPITRREVRALLKSLQAQlGITVVLVTHDLDEAARlADRVVVLRDGK 178
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
330-537 |
1.21e-44 |
|
ATP-binding cassette domain of the transporters involved in export of lipoprotein and macrolide, and Cell division ATP-binding protein FtsE; This family is comprised of MJ0796 ATP-binding cassette, macrolide-specific ABC-type efflux carrier (MacAB), and proteins involved in cell division (FtsE), and release of lipoproteins from the cytoplasmic membrane (LolCDE). They are clustered together phylogenetically. MacAB is an exporter that confers resistance to macrolides, while the LolCDE system is not a transporter at all. The FtsEX complex resembles an ABC transporter, where FtsE is the ATPase and the membrane subunit FtsX resembles a permease subunit. But rather than transporting any substrate, the complex acts in cell division by undergoing conformational changes that alter the activity of cell wall hydrolases located outside the plasma membrane. The complex is widely conserved in bacteria, but also extremely divergent in sequence between different lineages. The LolCDE complex catalyzes the release of lipoproteins from the cytoplasmic membrane prior to their targeting to the outer membrane.
Pssm-ID: 213222 [Multi-domain] Cd Length: 218 Bit Score: 157.65 E-value: 1.21e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 330 IEAQSLTKKFGD----FAATDHVDFQVKRGEIFGLLGPNGAGKSTTFKMMCGLLVPTSGKALVLGMDLKVSSGKA----- 400
Cdd:cd03255 1 IELKNLSKTYGGggekVQALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRVDGTDISKLSEKElaafr 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 401 RQHLGYMAQKFSLYGNLSVEQNLRFFSGVYGLRGRAQNEKIARMSDAFGLKSIARHAADELPLGYKQRLALACSLMHEPD 480
Cdd:cd03255 81 RRHIGFVFQSFNLLPDLTALENVELPLLLAGVPKKERRERAEELLERVGLGDRLNHYPSELSGGQQQRVAIARALANDPK 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 488984955 481 ILFLDEPTSGVDPLTRREFWLHINSMVDK-GVTVMVTTHFMDEAEYCDRIGLVYHGKL 537
Cdd:cd03255 161 IILADEPTGNLDSETGKEVMELLRELNKEaGTTIVVVTHDPELAEYADRIIELRDGKI 218
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
325-544 |
3.16e-44 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 157.17 E-value: 3.16e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 325 KEETVIEAQSLTKKFGDFAATDHVDFQVKRGEIFGLLGPNGAGKSTTFKMMCGLLVPTSGKALVLGMDLKvssgKARQHL 404
Cdd:COG1121 2 MMMPAIELENLTVSYGGRPVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLFGKPPR----RARRRI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 405 GYMAQKFSLYGN--LSVEQNLRffSGVYGLRG------RAQNEKIARMSDAFGLKSIARHAADELPLGYKQRLALACSLM 476
Cdd:COG1121 78 GYVPQRAEVDWDfpITVRDVVL--MGRYGRRGlfrrpsRADREAVDEALERVGLEDLADRPIGELSGGQQQRVLLARALA 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 488984955 477 HEPDILFLDEPTSGVDPLTRREFWLHINSMVDKGVTVMVTTHFMDEA-EYCDRIGLVyHGKLIASGTPD 544
Cdd:COG1121 156 QDPDLLLLDEPFAGVDAATEEALYELLRELRREGKTILVVTHDLGAVrEYFDRVLLL-NRGLVAHGPPE 223
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
330-541 |
1.83e-43 |
|
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: 154.27 E-value: 1.83e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 330 IEAQSLTKKFGDFAATDHVDFQVKRGeIFGLLGPNGAGKSTTFKMMCGLLVPTSGKALVLGMDLKVSSGKARQHLGYMAQ 409
Cdd:cd03264 1 LQLENLTKRYGKKRALDGVSLTLGPG-MYGLLGPNGAGKTTLMRILATLTPPSSGTIRIDGQDVLKQPQKLRRRIGYLPQ 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 410 KFSLYGNLSVEQNLRFFSGVYGLRGRAQNEKIARMSDAFGLKSIARHAADELPLGYKQRLALACSLMHEPDILFLDEPTS 489
Cdd:cd03264 80 EFGVYPNFTVREFLDYIAWLKGIPSKEVKARVDEVLELVNLGDRAKKKIGSLSGGMRRRVGIAQALVGDPSILIVDEPTA 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 488984955 490 GVDPLTRREFwLHINSMVDKGVTVMVTTHFMDEAEY-CDRIGLVYHGKLIASG 541
Cdd:cd03264 160 GLDPEERIRF-RNLLSELGEDRIVILSTHIVEDVESlCNQVAVLNKGKLVFEG 211
|
|
| galliderm_ABC |
TIGR03740 |
gallidermin-class lantibiotic protection ABC transporter, ATP-binding subunit; Model TIGR03731 ... |
330-538 |
5.83e-43 |
|
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: 153.32 E-value: 5.83e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 330 IEAQSLTKKFGDFAATDHVDFQVKRGEIFGLLGPNGAGKSTTFKMMCGLLVPTSGKALVLGMDLkvsSGKARQHLGYMAQ 409
Cdd:TIGR03740 1 LETKNLSKRFGKQTAVNNISLTVPKNSVYGLLGPNGAGKSTLLKMITGILRPTSGEIIFDGHPW---TRKDLHKIGSLIE 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 410 KFSLYGNLSVEQNLRFFSGVYGLrgraQNEKIARMSDAFGLKSIARHAADELPLGYKQRLALACSLMHEPDILFLDEPTS 489
Cdd:TIGR03740 78 SPPLYENLTARENLKVHTTLLGL----PDSRIDEVLNIVDLTNTGKKKAKQFSLGMKQRLGIAIALLNHPKLLILDEPTN 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 488984955 490 GVDPLTRREFWLHINSMVDKGVTVMVTTHFMDEAEY-CDRIGLVYHGKLI 538
Cdd:TIGR03740 154 GLDPIGIQELRELIRSFPEQGITVILSSHILSEVQQlADHIGIISEGVLG 203
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
1-221 |
6.15e-43 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 153.71 E-value: 6.15e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 1 MSETVIALNGLSRRFPGmdRPAVAPLTCTIRAGYVTGLVGPDGAGKTTLMRMLAGLLKPDEGRASVIGFDPLKDdsalHA 80
Cdd:COG1121 2 MMMPAIELENLTVSYGG--RPVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLFGKPPRRA----RR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 81 VLGYMPQKFGLYED--LTVME--NLTLYAD---LRSVTGEARKKIfDRLLEFTSLGPFTERLAGKLSGGMKQKLGLACTL 153
Cdd:COG1121 76 RIGYVPQRAEVDWDfpITVRDvvLMGRYGRrglFRRPSRADREAV-DEALERVGLEDLADRPIGELSGGQQQRVLLARAL 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 488984955 154 VGDPKVLLLDEPGVGVDPISRRELWQMVHELAGDGMLILWSTSYLDEAEQ-CRDVLLMNEGkLLYQGEP 221
Cdd:COG1121 155 AQDPDLLLLDEPFAGVDAATEEALYELLRELRREGKTILVVTHDLGAVREyFDRVLLLNRG-LVAHGPP 222
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
331-536 |
6.90e-43 |
|
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213179 [Multi-domain] Cd Length: 157 Bit Score: 150.86 E-value: 6.90e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 331 EAQSLTKKFGDFAATDHVDFQVKRGEIFGLLGPNGAGKSTTFKMMCGLLVPTSGKALVLGMDL-KVSSGKARQHLGYMAQ 409
Cdd:cd00267 1 EIENLSFRYGGRTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGKDIaKLPLEELRRRIGYVPQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 410 kfslygnlsveqnlrfFSGvyglrgraqnekiarmsdafglksiarhaadelplGYKQRLALACSLMHEPDILFLDEPTS 489
Cdd:cd00267 81 ----------------LSG-----------------------------------GQRQRVALARALLLNPDLLLLDEPTS 109
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 488984955 490 GVDPLTRREFWLHINSMVDKGVTVMVTTHFMDEAE-YCDRIGLVYHGK 536
Cdd:cd00267 110 GLDPASRERLLELLRELAEEGRTVIIVTHDPELAElAADRVIVLKDGK 157
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
330-546 |
1.44e-42 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 156.03 E-value: 1.44e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 330 IEAQSLTKKFGDFAATDHVDFQVKRGEIFGLLGPNGAGKSTTFKMMCGLLVPTSGKALVLGMDL-KVSSGKaRqHLGYMA 408
Cdd:COG3842 6 LELENVSKRYGDVTALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRILLDGRDVtGLPPEK-R-NVGMVF 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 409 QKFSLYGNLSVEQNLRFfsgvyGLRGR-----AQNEKIARMSDAFGLKSIARHAADELPLGYKQRLALACSLMHEPDILF 483
Cdd:COG3842 84 QDYALFPHLTVAENVAF-----GLRMRgvpkaEIRARVAELLELVGLEGLADRYPHQLSGGQQQRVALARALAPEPRVLL 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 488984955 484 LDEPTSGVDPLTRREFWLHINSMVDK-GVTVMVTTHFMDEA-EYCDRIGLVYHGKLIASGTPDAL 546
Cdd:COG3842 159 LDEPLSALDAKLREEMREELRRLQRElGITFIYVTHDQEEAlALADRIAVMNDGRIEQVGTPEEI 223
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
8-219 |
1.60e-42 |
|
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: 151.53 E-value: 1.60e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 8 LNGLSRRFPGmdRPAVAPLTCTIRAGYVTGLVGPDGAGKTTLMRMLAGLLKPDEGRASVIGFDPLKDDSalhaVLGYMPQ 87
Cdd:cd03235 2 VEDLTVSYGG--HPVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFGKPLEKERK----RIGYVPQ 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 88 KFGLYED--LTVME--NLTLYAD---LRSVTGEARKKIfDRLLEFTSLGPFTERLAGKLSGGMKQKLGLACTLVGDPKVL 160
Cdd:cd03235 76 RRSIDRDfpISVRDvvLMGLYGHkglFRRLSKADKAKV-DEALERVGLSELADRQIGELSGGQQQRVLLARALVQDPDLL 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 161 LLDEPGVGVDPISRRELWQMVHELAGDGMLILWSTSYLDEAEQ-CRDVLLMNeGKLLYQG 219
Cdd:cd03235 155 LLDEPFAGVDPKTQEDIYELLRELRREGMTILVVTHDLGLVLEyFDRVLLLN-RTVVASG 213
|
|
| LPS_export_lptB |
TIGR04406 |
LPS export ABC transporter ATP-binding protein; Members of this fmaily are LptB, the ... |
329-544 |
2.44e-42 |
|
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: 152.04 E-value: 2.44e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 329 VIEAQSLTKKFGDFAATDHVDFQVKRGEIFGLLGPNGAGKSTTFKMMCGLLVPTSGKALVLGMDLKVSS--GKARQHLGY 406
Cdd:TIGR04406 1 TLVAENLIKSYKKRKVVNDVSLSVKSGEIVGLLGPNGAGKTTSFYMIVGLVRPDAGKILIDGQDITHLPmhERARLGIGY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 407 MAQKFSLYGNLSVEQNLRffsGVYGLRGRAQNEKIARMSDA----FGLKSIARHAADELPLGYKQRLALACSLMHEPDIL 482
Cdd:TIGR04406 81 LPQEASIFRKLTVEENIM---AVLEIRKDLDRAEREERLEAlleeFQISHLRDNKAMSLSGGERRRVEIARALATNPKFI 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 488984955 483 FLDEPTSGVDPLTRREFWLHINSMVDKGVTVMVTTHFMDEA-EYCDRIGLVYHGKLIASGTPD 544
Cdd:TIGR04406 158 LLDEPFAGVDPIAVGDIKKIIKHLKERGIGVLITDHNVRETlDICDRAYIISDGKVLAEGTPA 220
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
2-539 |
7.94e-42 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 157.49 E-value: 7.94e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 2 SETVIALNGLSRRFPGmdrpaVAPL---TCTIRAGYVTGLVGPDGAGKTTLMRMLAGLLKPDEGRasvIGFD--PLKDDS 76
Cdd:COG1129 1 AEPLLEMRGISKSFGG-----VKALdgvSLELRPGEVHALLGENGAGKSTLMKILSGVYQPDSGE---ILLDgePVRFRS 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 77 ---ALHAVLGYMPQKFGLYEDLTVMENLTL-----------YADLRSvtgEARKkIFDRL-LEftsLGPftERLAGKLSG 141
Cdd:COG1129 73 prdAQAAGIAIIHQELNLVPNLSVAENIFLgreprrgglidWRAMRR---RARE-LLARLgLD---IDP--DTPVGDLSV 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 142 GMKQKLGLACTLVGDPKVLLLDEPgvgVDPISRRE---LWQMVHELAGDGMLILWSTSYLDEAEQ-CRDVLLMNEGKLLY 217
Cdd:COG1129 144 AQQQLVEIARALSRDARVLILDEP---TASLTEREverLFRIIRRLKAQGVAIIYISHRLDEVFEiADRVTVLRDGRLVG 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 218 QGEPTALT-----QTMAGRSflvsspqennrrllqralklpqvsdgviqgksvrlilkkdarieevqqhgdmpplqvadt 292
Cdd:COG1129 221 TGPVAELTedelvRLMVGRE------------------------------------------------------------ 240
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 293 aprfedafidllggagtaespLGAIIHRVDGSKEETVIEAQSLTKKfGDFaatDHVDFQVKRGEIFGLLGPNGAGKSTTF 372
Cdd:COG1129 241 ---------------------LEDLFPKRAAAPGEVVLEVEGLSVG-GVV---RDVSFSVRAGEILGIAGLVGAGRTELA 295
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 373 KMMCGLLVPTSGKALVLGMDLKVSS-GKARQH-LGYMA---QKFSLYGNLSVEQNL------RFFSGVYgLRGRAQNEKI 441
Cdd:COG1129 296 RALFGADPADSGEIRLDGKPVRIRSpRDAIRAgIAYVPedrKGEGLVLDLSIRENItlasldRLSRGGL-LDRRRERALA 374
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 442 ARMSDAFGLKSiarhAADELPLGY-----KQRLALACSLMHEPDILFLDEPTSGVDPLTRREFWLHINSMVDKGVTVMVT 516
Cdd:COG1129 375 EEYIKRLRIKT----PSPEQPVGNlsggnQQKVVLAKWLATDPKVLILDEPTRGIDVGAKAEIYRLIRELAAEGKAVIVI 450
|
570 580
....*....|....*....|....
gi 488984955 517 THFMDE-AEYCDRIGLVYHGKLIA 539
Cdd:COG1129 451 SSELPElLGLSDRILVMREGRIVG 474
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
346-536 |
8.82e-42 |
|
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: 149.54 E-value: 8.82e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 346 DHVDFQVKRGEIFGLLGPNGAGKSTTFKMMCGLLVPTSGKALVLGMDLKVSSGKA-RQHLGYMAQK----FSlygNLSVE 420
Cdd:cd03225 18 DDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDLTKLSLKElRRKVGLVFQNpddqFF---GPTVE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 421 QNLRFFSGVYGLRGRAQNEKIARMSDAFGLKSIARHAADELPLGYKQRLALACSLMHEPDILFLDEPTSGVDPLTRREFW 500
Cdd:cd03225 95 EEVAFGLENLGLPEEEIEERVEEALELVGLEGLRDRSPFTLSGGQKQRVAIAGVLAMDPDILLLDEPTAGLDPAGRRELL 174
|
170 180 190
....*....|....*....|....*....|....*..
gi 488984955 501 LHINSMVDKGVTVMVTTHFMDE-AEYCDRIGLVYHGK 536
Cdd:cd03225 175 ELLKKLKAEGKTIIIVTHDLDLlLELADRVIVLEDGK 211
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
1-184 |
1.26e-41 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 150.63 E-value: 1.26e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 1 MSETVIALNGLSRRFPGM--DRPAVAPLTCTIRAGYVTGLVGPDGAGKTTLMRMLAGLLKPDEGRASVIGfdplKDDSAL 78
Cdd:COG1116 3 AAAPALELRGVSKRFPTGggGVTALDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPTSGEVLVDG----KPVTGP 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 79 HAVLGYMPQKFGLYEDLTVMENLTLYADLRSVTGEARKKIFDRLLEFTSLGPFTERLAGKLSGGMKQKLGLACTLVGDPK 158
Cdd:COG1116 79 GPDRGVVFQEPALLPWLTVLDNVALGLELRGVPKAERRERARELLELVGLAGFEDAYPHQLSGGMRQRVAIARALANDPE 158
|
170 180
....*....|....*....|....*.
gi 488984955 159 VLLLDEPGVGVDPISRRELWQMVHEL 184
Cdd:COG1116 159 VLLMDEPFGALDALTRERLQDELLRL 184
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
330-541 |
1.68e-41 |
|
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: 148.82 E-value: 1.68e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 330 IEAQSLTKKFGDFAATDHVDFQVKRGEIFGLLGPNGAGKSTTFKMMCGLLVPTSGKALVLGMDlkVSSGKARQ-HLGYMA 408
Cdd:cd03259 1 LELKGLSKTYGSVRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDGRD--VTGVPPERrNIGMVF 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 409 QKFSLYGNLSVEQNLRFFSGVYGLRGRAQNEKIARMSDAFGLKSIARHAADELPLGYKQRLALACSLMHEPDILFLDEPT 488
Cdd:cd03259 79 QDYALFPHLTVAENIAFGLKLRGVPKAEIRARVRELLELVGLEGLLNRYPHELSGGQQQRVALARALAREPSLLLLDEPL 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 488984955 489 SGVDPLTRREFWLHINSMVDK-GVTVMVTTHFMDEA-EYCDRIGLVYHGKLIASG 541
Cdd:cd03259 159 SALDAKLREELREELKELQRElGITTIYVTHDQEEAlALADRIAVMNEGRIVQVG 213
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
329-546 |
3.50e-41 |
|
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: 149.42 E-value: 3.50e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 329 VIEAQSLTKKFGDFAATDHVDFQVKRGEIFGLLGPNGAGKSTTFKMMCGLLVPTSGKALVLGMDLKVSSGKAR-QHLGYM 407
Cdd:COG1120 1 MLEAENLSVGYGGRPVLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDGRDLASLSRRELaRRIAYV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 408 AQKFSLYGNLSVEQNLRF----FSGVYGLRGRAQNEKIARMSDAFGLKSIARHAADELPLGYKQRLALACSLMHEPDILF 483
Cdd:COG1120 81 PQEPPAPFGLTVRELVALgrypHLGLFGRPSAEDREAVEEALERTGLEHLADRPVDELSGGERQRVLIARALAQEPPLLL 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 488984955 484 LDEPTSGVDPLTRREFWLHINSMV-DKGVTVMVTTHFMDEA-EYCDRIGLVYHGKLIASGTPDAL 546
Cdd:COG1120 161 LDEPTSHLDLAHQLEVLELLRRLArERGRTVVMVLHDLNLAaRYADRLVLLKDGRIVAQGPPEEV 225
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
329-531 |
4.16e-41 |
|
ABC-type transport system involved in cytochrome c biogenesis, ATPase component [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 443308 [Multi-domain] Cd Length: 206 Bit Score: 147.63 E-value: 4.16e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 329 VIEAQSLTKKFGDFAATDHVDFQVKRGEIFGLLGPNGAGKSTTFKMMCGLLVPTSGKALVLGMDLKVSSGKARQHLGYMA 408
Cdd:COG4133 2 MLEAENLSCRRGERLLFSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWNGEPIRDAREDYRRRLAYLG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 409 QKFSLYGNLSVEQNLRFFSGVYGLRGRAqnEKIARMSDAFGLKSIARHAADELPLGYKQRLALACSLMHEPDILFLDEPT 488
Cdd:COG4133 82 HADGLKPELTVRENLRFWAALYGLRADR--EAIDEALEAVGLAGLADLPVRQLSAGQKRRVALARLLLSPAPLWLLDEPF 159
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 488984955 489 SGVDPLTRREFWLHINSMVDKGVTVMVTTHFMDEAEYCDRIGL 531
Cdd:COG4133 160 TALDAAGVALLAELIAAHLARGGAVLLTTHQPLELAAARVLDL 202
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
6-221 |
6.14e-41 |
|
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: 147.86 E-value: 6.14e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 6 IALNGLSRRFPGmDRPAVAPLTCTIRAGYVTGLVGPDGAGKTTLMRMLAGLLKPDEGRASVIGFDPLKDD-SALHAVLGY 84
Cdd:COG1122 1 IELENLSFSYPG-GTPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVDGKDITKKNlRELRRKVGL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 85 MPQK-----FG--LYEDLT-VMENLTLYADlrsvtgEARKKIfDRLLEFTSLGPFTERLAGKLSGGMKQKLGLACTLVGD 156
Cdd:COG1122 80 VFQNpddqlFAptVEEDVAfGPENLGLPRE------EIRERV-EEALELVGLEHLADRPPHELSGGQKQRVAIAGVLAME 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 488984955 157 PKVLLLDEPGVGVDPISRRELWQMVHELAGDGMLILWSTSYLDEAEQ-CRDVLLMNEGKLLYQGEP 221
Cdd:COG1122 153 PEVLVLDEPTAGLDPRGRRELLELLKRLNKEGKTVIIVTHDLDLVAElADRVIVLDDGRIVADGTP 218
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
8-538 |
7.55e-41 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 155.22 E-value: 7.55e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 8 LNGLSRRFPGmdRPAVAPLTCTIRAGYVTGLVGPDGAGKTTLMRMLAGLLKPDEGRASVIGfdplkddsalHAVLGYMPQ 87
Cdd:COG0488 1 LENLSKSFGG--RPLLDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEVSIPK----------GLRIGYLPQ 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 88 KFGLYEDLTVMENL---------------TLYADLRSVTGEARK--KIFDRLLEF-------------TSLGpFTE---- 133
Cdd:COG0488 69 EPPLDDDLTVLDTVldgdaelraleaeleELEAKLAEPDEDLERlaELQEEFEALggweaearaeeilSGLG-FPEedld 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 134 RLAGKLSGGMKQKLGLACTLVGDPKVLLLDEP-------GVgvdpisrreLWqmvheLAG-----DGMLILWS--TSYLD 199
Cdd:COG0488 148 RPVSELSGGWRRRVALARALLSEPDLLLLDEPtnhldleSI---------EW-----LEEflknyPGTVLVVShdRYFLD 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 200 EAeqCRDVLLMNEGKL-LYQGEPTAltqtmagrsFLVSSPQENNRRLLQRAL---KLPQVSDGVIQGKS-VRLILKKDAR 274
Cdd:COG0488 214 RV--ATRILELDRGKLtLYPGNYSA---------YLEQRAERLEQEAAAYAKqqkKIAKEEEFIRRFRAkARKAKQAQSR 282
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 275 IEEVQQhgdmppLQVADTAPRFEDAFIDLlggagTAESPLGaiihrvdgskeETVIEAQSLTKKFGDFAATDHVDFQVKR 354
Cdd:COG0488 283 IKALEK------LEREEPPRRDKTVEIRF-----PPPERLG-----------KKVLELEGLSKSYGDKTLLDDLSLRIDR 340
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 355 GEIFGLLGPNGAGKSTTFKMMCGLLVPTSGKaLVLGMDLKVssgkarqhlGYMAQKF-SLYGNLSV------------EQ 421
Cdd:COG0488 341 GDRIGLIGPNGAGKSTLLKLLAGELEPDSGT-VKLGETVKI---------GYFDQHQeELDPDKTVldelrdgapggtEQ 410
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 422 NLRFFSGVYGLRGRAQNEKIARMSdafGlksiarhaadelplGYKQRLALACSLMHEPDILFLDEPTSGVDPLTRREFwl 501
Cdd:COG0488 411 EVRGYLGRFLFSGDDAFKPVGVLS---G--------------GEKARLALAKLLLSPPNVLLLDEPTNHLDIETLEAL-- 471
|
570 580 590 600
....*....|....*....|....*....|....*....|.
gi 488984955 502 hINSMVD-KGvTVMVTTH---FMDEAeyCDRIGLVYHGKLI 538
Cdd:COG0488 472 -EEALDDfPG-TVLLVSHdryFLDRV--ATRILEFEDGGVR 508
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
2-226 |
1.40e-40 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 157.98 E-value: 1.40e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 2 SETVIALNGLSRRFpGmDRPAVAPLTCTIRAGYVTGLVGPDGAGKTTLMRMLAGLLKPDEGRASVIG--FDPlkDDSALH 79
Cdd:NF033858 263 DEPAIEARGLTMRF-G-DFTAVDHVSFRIRRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGEAWLFGqpVDA--GDIATR 338
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 80 AVLGYMPQKFGLYEDLTVMENLTLYADLRSVTGEARKKIFDRLLEFTSLGPFTERLAGKLSGGMKQKLGLACTLVGDPKV 159
Cdd:NF033858 339 RRVGYMSQAFSLYGELTVRQNLELHARLFHLPAAEIAARVAEMLERFDLADVADALPDSLPLGIRQRLSLAVAVIHKPEL 418
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 488984955 160 LLLDEPGVGVDPISRRELWQMVHELA-GDGMLILWSTSYLDEAEQCRDVLLMNEGKLLYQGEPTALTQ 226
Cdd:NF033858 419 LILDEPTSGVDPVARDMFWRLLIELSrEDGVTIFISTHFMNEAERCDRISLMHAGRVLASDTPAALVA 486
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
331-541 |
1.65e-40 |
|
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: 146.14 E-value: 1.65e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 331 EAQSLTKKFGDFAATDHVDFQVKRGEIFGLLGPNGAGKSTTFKMMCGLLVPTSGKALVLGMDLkvssGKARQHLGYMAQK 410
Cdd:cd03235 1 EVEDLTVSYGGHPVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFGKPL----EKERKRIGYVPQR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 411 FSL--YGNLSVEQ----NLRFFSGVYGLRGRAQNEKIARMSDAFGLKSIARHAADELPLGYKQRLALACSLMHEPDILFL 484
Cdd:cd03235 77 RSIdrDFPISVRDvvlmGLYGHKGLFRRLSKADKAKVDEALERVGLSELADRQIGELSGGQQQRVLLARALVQDPDLLLL 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 488984955 485 DEPTSGVDPLTRREFWLHINSMVDKGVTVMVTTHFMDEA-EYCDRIgLVYHGKLIASG 541
Cdd:cd03235 157 DEPFAGVDPKTQEDIYELLRELRREGMTILVVTHDLGLVlEYFDRV-LLLNRTVVASG 213
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
21-219 |
5.52e-40 |
|
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: 145.55 E-value: 5.52e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 21 PAVAPLTCTIRAGYVTGLVGPDGAGKTTLMRMLAGLLKPDEGRASVIGFDPLKDDSALHAVLGY-MPQKFGLYEDLTVME 99
Cdd:cd03267 35 EALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRVAGLVPWKRRKKFLRRIGVvFGQKTQLWWDLPVID 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 100 NLTLYADLRSVTGEARKKIFDRLLEFTSLGPFTERLAGKLSGGMKQKLGLACTLVGDPKVLLLDEPGVGVDPISRRELWQ 179
Cdd:cd03267 115 SFYLLAAIYDLPPARFKKRLDELSELLDLEELLDTPVRQLSLGQRMRAEIAAALLHEPEILFLDEPTIGLDVVAQENIRN 194
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 488984955 180 MVHELAGD-GMLILWSTSYLDEAEQ-CRDVLLMNEGKLLYQG 219
Cdd:cd03267 195 FLKEYNRErGTTVLLTSHYMKDIEAlARRVLVIDKGRLLYDG 236
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
327-539 |
2.34e-39 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 143.65 E-value: 2.34e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 327 ETVIEAQSLTKKFGD----FAATDHVDFQVKRGEIFGLLGPNGAGKSTTFKMMCGLLVPTSGKALVLGMDLKVSSGKA-- 400
Cdd:COG1136 2 SPLLELRNLTKSYGTgegeVTALRGVSLSIEAGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVLIDGQDISSLSEREla 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 401 ---RQHLGYMAQKFSLYGNLSVEQNLRFFSGVYGLRGRAQNEKIARMSDAFGLKSIARHAADELPLGYKQRLALACSLMH 477
Cdd:COG1136 82 rlrRRHIGFVFQFFNLLPELTALENVALPLLLAGVSRKERRERARELLERVGLGDRLDHRPSQLSGGQQQRVAIARALVN 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 488984955 478 EPDILFLDEPTSGVDPLTRREFWLHINSMVDK-GVTVMVTTHFMDEAEYCDRIGLVYHGKLIA 539
Cdd:COG1136 162 RPKLILADEPTGNLDSKTGEEVLELLRELNRElGTTIVMVTHDPELAARADRVIRLRDGRIVS 224
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
8-214 |
2.36e-39 |
|
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: 142.99 E-value: 2.36e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 8 LNGLSRRFPGMDRPAVAPLTCTIRAGYVTGLVGPDGAGKTTLMRMLAGLLKPDEGRASVIGFDPLKDDSA-LHAVLGYMP 86
Cdd:cd03225 2 LKNLSFSYPDGARPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDLTKLSLKeLRRKVGLVF 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 87 QK-----FGL--YEDLT-VMENLTLYADlrsvtgEARKKIfDRLLEFTSLGPFTERLAGKLSGGMKQKLGLACTLVGDPK 158
Cdd:cd03225 82 QNpddqfFGPtvEEEVAfGLENLGLPEE------EIEERV-EEALELVGLEGLRDRSPFTLSGGQKQRVAIAGVLAMDPD 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 488984955 159 VLLLDEPGVGVDPISRRELWQMVHELAGDGMLILWSTSYLDE-AEQCRDVLLMNEGK 214
Cdd:cd03225 155 ILLLDEPTAGLDPAGRRELLELLKKLKAEGKTIIIVTHDLDLlLELADRVIVLEDGK 211
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
6-201 |
4.03e-39 |
|
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: 142.61 E-value: 4.03e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 6 IALNGLSRRFPGMDRP--AVAPLTCTIRAGYVTGLVGPDGAGKTTLMRMLAGLLKPDEGRASVIGfDPLKDdsaLHAVLG 83
Cdd:cd03293 1 LEVRNVSKTYGGGGGAvtALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVDG-EPVTG---PGPDRG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 84 YMPQKFGLYEDLTVMENLTLYADLRSVTGEARKKIFDRLLEFTSLGPFTERLAGKLSGGMKQKLGLACTLVGDPKVLLLD 163
Cdd:cd03293 77 YVFQQDALLPWLTVLDNVALGLELQGVPKAEARERAEELLELVGLSGFENAYPHQLSGGMRQRVALARALAVDPDVLLLD 156
|
170 180 190
....*....|....*....|....*....|....*....
gi 488984955 164 EPGVGVDPISRRELWQMVHEL-AGDGMLILWSTSYLDEA 201
Cdd:cd03293 157 EPFSALDALTREQLQEELLDIwRETGKTVLLVTHDIDEA 195
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
324-529 |
9.86e-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: 142.92 E-value: 9.86e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 324 SKEETVIEAQSLTKKF----GDFAATDHVDFQVKRGEIFGLLGPNGAGKSTTFKMMCGLLVPTSGKALVLGMDLKvssgK 399
Cdd:COG1116 2 SAAAPALELRGVSKRFptggGGVTALDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPTSGEVLVDGKPVT----G 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 400 ARQHLGYMAQKFSLYGNLSVEQNLRFfsgvyGLRGR-----AQNEKIARMSDAFGLKSIARHAADELPLGYKQRLALACS 474
Cdd:COG1116 78 PGPDRGVVFQEPALLPWLTVLDNVAL-----GLELRgvpkaERRERARELLELVGLAGFEDAYPHQLSGGMRQRVAIARA 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 488984955 475 LMHEPDILFLDEPTSGVDPLTRREFWLHINSMVDK-GVTVMVTTHFMDEAEY-CDRI 529
Cdd:COG1116 153 LANDPEVLLMDEPFGALDALTRERLQDELLRLWQEtGKTVLFVTHDVDEAVFlADRV 209
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
330-529 |
1.37e-38 |
|
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: 141.07 E-value: 1.37e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 330 IEAQSLTKKFGD----FAATDHVDFQVKRGEIFGLLGPNGAGKSTTFKMMCGLLVPTSGKALVLGMDLKvssgKARQHLG 405
Cdd:cd03293 1 LEVRNVSKTYGGgggaVTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVDGEPVT----GPGPDRG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 406 YMAQKFSLYGNLSVEQNLRFFSGVYGLRGRAQNEKIARMSDAFGLKSIARHAADELPLGYKQRLALACSLMHEPDILFLD 485
Cdd:cd03293 77 YVFQQDALLPWLTVLDNVALGLELQGVPKAEARERAEELLELVGLSGFENAYPHQLSGGMRQRVALARALAVDPDVLLLD 156
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 488984955 486 EPTSGVDPLTRREFWLHINSMVDK-GVTVMVTTHFMDEAEY-CDRI 529
Cdd:cd03293 157 EPFSALDALTREQLQEELLDIWREtGKTVLLVTHDIDEAVFlADRV 202
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
332-553 |
1.88e-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: 142.40 E-value: 1.88e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 332 AQSLTKKFGDFAATDHVDFQVKRGEIFGLLGPNGAGKSTTFKMMCGLLVPTSGKALVLGMDLKVSSGKA-----RQHLGY 406
Cdd:cd03294 27 KEEILKKTGQTVGVNDVSLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGKVLIDGQDIAAMSRKElrelrRKKISM 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 407 MAQKFSLYGNLSVEQNLrffsgVYGL--RGRAQNEKIARMSDAF---GLKSIARHAADELPLGYKQRLALACSLMHEPDI 481
Cdd:cd03294 107 VFQSFALLPHRTVLENV-----AFGLevQGVPRAEREERAAEALelvGLEGWEHKYPDELSGGMQQRVGLARALAVDPDI 181
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 488984955 482 LFLDEPTSGVDPLTRREFWLHINSMVDK-GVTVMVTTHFMDEA-EYCDRIGLVYHGKLIASGTPDALKAQAADD 553
Cdd:cd03294 182 LLMDEAFSALDPLIRREMQDELLRLQAElQKTIVFITHDLDEAlRLGDRIAIMKDGRLVQVGTPEEILTNPAND 255
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
330-546 |
2.09e-38 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 144.52 E-value: 2.09e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 330 IEAQSLTKKFGDFAATDHVDFQVKRGEIFGLLGPNGAGKSTTFKMMCGLLVPTSGKALVLGMDLKVSSGKARQHLGYMAQ 409
Cdd:COG1118 3 IEVRNISKRFGSFTLLDDVSLEIASGELVALLGPSGSGKTTLLRIIAGLETPDSGRIVLNGRDLFTNLPPRERRVGFVFQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 410 KFSLYGNLSVEQNLRFfsgvyGLRGR-----AQNEKIARMSDAFGLKSIARHAADELPLGYKQRLALACSLMHEPDILFL 484
Cdd:COG1118 83 HYALFPHMTVAENIAF-----GLRVRppskaEIRARVEELLELVQLEGLADRYPSQLSGGQRQRVALARALAVEPEVLLL 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 488984955 485 DEPTSGVDPLTRREF--WLHinSMVDK--GVTVMVtTHFMDEA-EYCDRIGLVYHGKLIASGTPDAL 546
Cdd:COG1118 158 DEPFGALDAKVRKELrrWLR--RLHDElgGTTVFV-THDQEEAlELADRVVVMNQGRIEQVGTPDEV 221
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
329-542 |
4.62e-38 |
|
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: 140.02 E-value: 4.62e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 329 VIEAQSLTKKFGD----FAATDHVDFQVKRGEIFGLLGPNGAGKSTTFKMMCGLLVPTSGKALVLGMDLKVSSGK----A 400
Cdd:cd03258 1 MIELKNVSKVFGDtggkVTALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGSVLVDGTDLTLLSGKelrkA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 401 RQHLGYMAQKFSLYGNLSVEQNLRFFSGVYGLRGRAQNEKIARMSDAFGLKSIARHAADELPLGYKQRLALACSLMHEPD 480
Cdd:cd03258 81 RRRIGMIFQHFNLLSSRTVFENVALPLEIAGVPKAEIEERVLELLELVGLEDKADAYPAQLSGGQKQRVGIARALANNPK 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 488984955 481 ILFLDEPTSGVDPLTRR---EFWLHINSmvDKGVTVMVTTHFMDEA-EYCDRIGLVYHGKLIASGT 542
Cdd:cd03258 161 VLLCDEATSALDPETTQsilALLRDINR--ELGLTIVLITHEMEVVkRICDRVAVMEKGEVVEEGT 224
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
1-230 |
5.28e-38 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 143.43 E-value: 5.28e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 1 MSETVIALNGLSRRFPgmDRPAVAPLTCTIRAGYVTGLVGPDGAGKTTLMRMLAGLLKPDEGRASVIGFDPLKDDSALHA 80
Cdd:PRK13536 37 MSTVAIDLAGVSKSYG--DKAVVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKITVLGVPVPARARLARA 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 81 VLGYMPQKFGLYEDLTVMENLTLYADLRSVTGEARKKIFDRLLEFTSLGPFTERLAGKLSGGMKQKLGLACTLVGDPKVL 160
Cdd:PRK13536 115 RIGVVPQFDNLDLEFTVRENLLVFGRYFGMSTREIEAVIPSLLEFARLESKADARVSDLSGGMKRRLTLARALINDPQLL 194
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 488984955 161 LLDEPGVGVDPISRRELWQMVHELAGDGMLILWSTSYLDEAEQ-CRDVLLMNEGKLLYQGEPTALTQTMAG 230
Cdd:PRK13536 195 ILDEPTTGLDPHARHLIWERLRSLLARGKTILLTTHFMEEAERlCDRLCVLEAGRKIAEGRPHALIDEHIG 265
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
10-224 |
1.06e-37 |
|
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: 139.22 E-value: 1.06e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 10 GLSRRFPGmdRPAVAPLTCTIRAGYVTGLVGPDGAGKTTLMRMLAGLLKPDEGRASVIGFD----PLKDDSALHavLGYM 85
Cdd:cd03218 5 NLSKRYGK--RKVVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDGQDitklPMHKRARLG--IGYL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 86 PQKFGLYEDLTVMENLTLYADLRSVTGEARKKIFDRLLEFTSLGPFTERLAGKLSGGMKQKLGLACTLVGDPKVLLLDEP 165
Cdd:cd03218 81 PQEASIFRKLTVEENILAVLEIRGLSKKEREEKLEELLEEFHITHLRKSKASSLSGGERRRVEIARALATNPKFLLLDEP 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 166 GVGVDPISRRELWQMVHELAGDGMLILWSTSYLDEAEQ-CRDVLLMNEGKLLYQGEPTAL 224
Cdd:cd03218 161 FAGVDPIAVQDIQKIIKILKDRGIGVLITDHNVRETLSiTDRAYIIYEGKVLAEGTPEEI 220
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
1-230 |
1.21e-37 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 141.48 E-value: 1.21e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 1 MSETVIALNGLSRRFPgmDRPAVAPLTCTIRAGYVTGLVGPDGAGKTTLMRMLAGLLKPDEGRASVIGfDPLKDdSALHA 80
Cdd:PRK13537 3 MSVAPIDFRNVEKRYG--DKLVVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCG-EPVPS-RARHA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 81 V--LGYMPQKFGLYEDLTVMENLTLYADLRSVTGEARKKIFDRLLEFTSLGPFTERLAGKLSGGMKQKLGLACTLVGDPK 158
Cdd:PRK13537 79 RqrVGVVPQFDNLDPDFTVRENLLVFGRYFGLSAAAARALVPPLLEFAKLENKADAKVGELSGGMKRRLTLARALVNDPD 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 488984955 159 VLLLDEPGVGVDPISRRELWQMVHELAGDGMLILWSTSYLDEAEQ-CRDVLLMNEGKLLYQGEPTALTQTMAG 230
Cdd:PRK13537 159 VLVLDEPTTGLDPQARHLMWERLRSLLARGKTILLTTHFMEEAERlCDRLCVIEEGRKIAEGAPHALIESEIG 231
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
330-554 |
1.26e-37 |
|
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: 139.36 E-value: 1.26e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 330 IEAQSLTKKFGD-FAATDHVDFQVKRGEIFGLLGPNGAGKSTTFKMMCGLLVPTSGKALVLGMDLK-VSSGKARQHLGYM 407
Cdd:cd03295 1 IEFENVTKRYGGgKKAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGEDIReQDPVELRRKIGYV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 408 AQKFSLYGNLSVEQNLrffSGVYGLRGRAQNEKIARMSDAFGL-----KSIARHAADELPLGYKQRLALACSLMHEPDIL 482
Cdd:cd03295 81 IQQIGLFPHMTVEENI---ALVPKLLKWPKEKIRERADELLALvgldpAEFADRYPHELSGGQQQRVGVARALAADPPLL 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 488984955 483 FLDEPTSGVDPLTR----REFwLHINSMVDKgvTVMVTTHFMDEA-EYCDRIGLVYHGKLIASGTPDALKAQAADDS 554
Cdd:cd03295 158 LMDEPFGALDPITRdqlqEEF-KRLQQELGK--TIVFVTHDIDEAfRLADRIAIMKNGEIVQVGTPDEILRSPANDF 231
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
6-221 |
1.30e-37 |
|
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: 139.36 E-value: 1.30e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 6 IALNGLSRRFPGmDRPAVAPLTCTIRAGYVTGLVGPDGAGKTTLMRMLAGLLKPDEGRASVIGFDPLK-DDSALHAVLGY 84
Cdd:cd03295 1 IEFENVTKRYGG-GKKAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGEDIREqDPVELRRKIGY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 85 MPQKFGLYEDLTVMENLTLYADLRSVTGEARKKIFDRLLEFTSLGP--FTERLAGKLSGGMKQKLGLACTLVGDPKVLLL 162
Cdd:cd03295 80 VIQQIGLFPHMTVEENIALVPKLLKWPKEKIRERADELLALVGLDPaeFADRYPHELSGGQQQRVGVARALAADPPLLLM 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 488984955 163 DEPGVGVDPISRRELWQMVHELAGD-GMLILWSTSYLDEAEQCRD-VLLMNEGKLLYQGEP 221
Cdd:cd03295 160 DEPFGALDPITRDQLQEEFKRLQQElGKTIVFVTHDIDEAFRLADrIAIMKNGEIVQVGTP 220
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
330-553 |
1.59e-37 |
|
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: 138.85 E-value: 1.59e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 330 IEAQSLTKKFGD-FAATDHVDFQVKRGEIFGLLGPNGAGKSTTFKMMCGLLVPTSGKALVLGMDLKVSSGKA----RQHL 404
Cdd:cd03256 1 IEVENLSKTYPNgKKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGTDINKLKGKAlrqlRRQI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 405 GYMAQKFSLYGNLSVEQN--------LRFFSGVYGLRGRAQNEKIARMSDAFGLKSIARHAADELPLGYKQRLALACSLM 476
Cdd:cd03256 81 GMIFQQFNLIERLSVLENvlsgrlgrRSTWRSLFGLFPKEEKQRALAALERVGLLDKAYQRADQLSGGQQQRVAIARALM 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 477 HEPDILFLDEPTSGVDPLTRR---EFWLHINSmvDKGVTVMVTTHFMDEA-EYCDRIGLVYHGKLIASGTPDALKAQAAD 552
Cdd:cd03256 161 QQPKLILADEPVASLDPASSRqvmDLLKRINR--EEGITVIVSLHQVDLArEYADRIVGLKDGRIVFDGPPAELTDEVLD 238
|
.
gi 488984955 553 D 553
Cdd:cd03256 239 E 239
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
329-541 |
3.58e-37 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 137.49 E-value: 3.58e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 329 VIEAQSLTKKF-GDFAATDHVDFQVKRGEIFGLLGPNGAGKSTTFKMMCGLLVPTSGKALVLGMDLKVSSGKA----RQH 403
Cdd:COG2884 1 MIRFENVSKRYpGGREALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLVNGQDLSRLKRREipylRRR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 404 LGYMAQKFSLYGNLSVEQNLRFFSGVYGLRGRAQNEKIARMSDAFGLKSIARHAADELPLGYKQRLALACSLMHEPDILF 483
Cdd:COG2884 81 IGVVFQDFRLLPDRTVYENVALPLRVTGKSRKEIRRRVREVLDLVGLSDKAKALPHELSGGEQQRVAIARALVNRPELLL 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 488984955 484 LDEPTSGVDPLTRREFWLHINSMVDKGVTVMVTTH---FMDEAEYcdRIGLVYHGKLIASG 541
Cdd:COG2884 161 ADEPTGNLDPETSWEIMELLEEINRRGTTVLIATHdleLVDRMPK--RVLELEDGRLVRDE 219
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
326-544 |
2.95e-36 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 141.70 E-value: 2.95e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 326 EETVIEAQSLTKKFGDFAATDHVDFQVKRGEIFGLLGPNGAGKSTTFKMMCGLLVPTSGKALVLGMDLKVSS-GKARQH- 403
Cdd:COG3845 2 MPPALELRGITKRFGGVVANDDVSLTVRPGEIHALLGENGAGKSTLMKILYGLYQPDSGEILIDGKPVRIRSpRDAIALg 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 404 LGYMAQKFSLYGNLSVEQNLrffsgVYGLRGRAQ--------NEKIARMSDAFGLKsIARHA-ADELPLGYKQRLALACS 474
Cdd:COG3845 82 IGMVHQHFMLVPNLTVAENI-----VLGLEPTKGgrldrkaaRARIRELSERYGLD-VDPDAkVEDLSVGEQQRVEILKA 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 488984955 475 LMHEPDILFLDEPTSGVDPLTRREFWLHINSMVDKGVTVMVTTHFMDEA-EYCDRIGLVYHGKLIASGTPD 544
Cdd:COG3845 156 LYRGARILILDEPTAVLTPQEADELFEILRRLAAEGKSIIFITHKLREVmAIADRVTVLRRGKVVGTVDTA 226
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
330-548 |
3.86e-36 |
|
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: 134.48 E-value: 3.86e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 330 IEAQSLTKKFGDFAATDHVDFQVKRGEIFGLLGPNGAGKSTTFKMMCGLLVPTSGKALVLGMDL--KVSSGKARQHLGYM 407
Cdd:cd03224 1 LEVENLNAGYGKSQILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDGRDItgLPPHERARAGIGYV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 408 AQKFSLYGNLSVEQNLRffSGVYGLRGRAQNEKIARMSDAF-GLKSIARHAADELPLGYKQRLALACSLMHEPDILFLDE 486
Cdd:cd03224 81 PEGRRIFPELTVEENLL--LGAYARRRAKRKARLERVYELFpRLKERRKQLAGTLSGGEQQMLAIARALMSRPKLLLLDE 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 488984955 487 PTSGVDPLTRREFWLHINSMVDKGVTVMVTTHFMDEA-EYCDRIGLVYHGKLIASGTPDALKA 548
Cdd:cd03224 159 PSEGLAPKIVEEIFEAIRELRDEGVTILLVEQNARFAlEIADRAYVLERGRVVLEGTAAELLA 221
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
8-219 |
5.69e-36 |
|
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: 133.80 E-value: 5.69e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 8 LNGLSRRFPGMdrPAVAPLTCTIRAGYVTGLVGPDGAGKTTLMRMLAGLLKPDEGRASVIGfdplKDDSALHAV---LGY 84
Cdd:cd03259 3 LKGLSKTYGSV--RALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDG----RDVTGVPPErrnIGM 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 85 MPQKFGLYEDLTVMENLTLYADLRSVTGEARKKIFDRLLEFTSLGPFTERLAGKLSGGMKQKLGLACTLVGDPKVLLLDE 164
Cdd:cd03259 77 VFQDYALFPHLTVAENIAFGLKLRGVPKAEIRARVRELLELVGLEGLLNRYPHELSGGQQQRVALARALAREPSLLLLDE 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 488984955 165 PGVGVDPISRRELWQMVHELAGD-GMLILWSTSYLDEAEQCRD-VLLMNEGKLLYQG 219
Cdd:cd03259 157 PLSALDAKLREELREELKELQRElGITTIYVTHDQEEALALADrIAVMNEGRIVQVG 213
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
8-214 |
1.41e-35 |
|
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: 130.83 E-value: 1.41e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 8 LNGLSRRFPgmDRPAVAPLTCTIRAGYVTGLVGPDGAGKTTLMRMLAGLLKPDEGRASVIGFDPLKDDS-ALHAVLGYMP 86
Cdd:cd00267 2 IENLSFRYG--GRTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGKDIAKLPLeELRRRIGYVP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 87 QkfglyedltvmenltlyadlrsvtgearkkifdrlleftslgpfterlagkLSGGMKQKLGLACTLVGDPKVLLLDEPG 166
Cdd:cd00267 80 Q---------------------------------------------------LSGGQRQRVALARALLLNPDLLLLDEPT 108
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 488984955 167 VGVDPISRRELWQMVHELAGDGMLILWSTSYLDEAEQCRD-VLLMNEGK 214
Cdd:cd00267 109 SGLDPASRERLLELLRELAEEGRTVIIVTHDPELAELAADrVIVLKDGK 157
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
29-226 |
1.58e-35 |
|
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: 132.94 E-value: 1.58e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 29 TIRAGYVTGLVGPDGAGKTTLMRMLAGLLKPDEGRASVIGFD--PLKDDSALHAVLGYMPQKFGLYEDLTVMENLTLYAD 106
Cdd:cd03224 22 TVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDGRDitGLPPHERARAGIGYVPEGRRIFPELTVEENLLLGAY 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 107 LRsvTGEARKKIFDRLLE-FTSLGPFTERLAGKLSGGMKQKLGLACTLVGDPKVLLLDEPGVGVDPISRRELWQMVHELA 185
Cdd:cd03224 102 AR--RRAKRKARLERVYElFPRLKERRKQLAGTLSGGEQQMLAIARALMSRPKLLLLDEPSEGLAPKIVEEIFEAIRELR 179
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 488984955 186 GDGMLILWSTSYLDEAEQCRD-VLLMNEGKLLYQGEPTALTQ 226
Cdd:cd03224 180 DEGVTILLVEQNARFALEIADrAYVLERGRVVLEGTAAELLA 221
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
29-165 |
1.76e-35 |
|
ABC transporter; ABC transporters for a large family of proteins responsible for translocation of a variety of compounds across biological membranes. ABC transporters are the largest family of proteins in many completely sequenced bacteria. ABC transporters are composed of two copies of this domain and two copies of a transmembrane domain pfam00664. These four domains may belong to a single polypeptide or belong in different polypeptide chains.
Pssm-ID: 394964 [Multi-domain] Cd Length: 150 Bit Score: 130.46 E-value: 1.76e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 29 TIRAGYVTGLVGPDGAGKTTLMRMLAGLLKPDEGRASVIGFDPLKDD-SALHAVLGYMPQKFGLYEDLTVMENLTLYADL 107
Cdd:pfam00005 7 TLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDLTDDErKSLRKEIGYVFQDPQLFPRLTVRENLRLGLLL 86
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 488984955 108 RSVTGEARKKIFDRLLEFTSLGPFTERLAGK----LSGGMKQKLGLACTLVGDPKVLLLDEP 165
Cdd:pfam00005 87 KGLSKREKDARAEEALEKLGLGDLADRPVGErpgtLSGGQRQRVAIARALLTKPKLLLLDEP 148
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
346-489 |
2.04e-35 |
|
ABC transporter; ABC transporters for a large family of proteins responsible for translocation of a variety of compounds across biological membranes. ABC transporters are the largest family of proteins in many completely sequenced bacteria. ABC transporters are composed of two copies of this domain and two copies of a transmembrane domain pfam00664. These four domains may belong to a single polypeptide or belong in different polypeptide chains.
Pssm-ID: 394964 [Multi-domain] Cd Length: 150 Bit Score: 130.08 E-value: 2.04e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 346 DHVDFQVKRGEIFGLLGPNGAGKSTTFKMMCGLLVPTSGKALVLGMDLKVSSGKA-RQHLGYMAQKFSLYGNLSVEQNLR 424
Cdd:pfam00005 2 KNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDLTDDERKSlRKEIGYVFQDPQLFPRLTVRENLR 81
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 488984955 425 FFSGVYGLRGRAQNEKIARMSDAFGLKSIARHAADELPL----GYKQRLALACSLMHEPDILFLDEPTS 489
Cdd:pfam00005 82 LGLLLKGLSKREKDARAEEALEKLGLGDLADRPVGERPGtlsgGQRQRVAIARALLTKPKLLLLDEPTA 150
|
|
| galliderm_ABC |
TIGR03740 |
gallidermin-class lantibiotic protection ABC transporter, ATP-binding subunit; Model TIGR03731 ... |
10-220 |
2.46e-35 |
|
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: 132.52 E-value: 2.46e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 10 GLSRRFPGMDrpAVAPLTCTIRAGYVTGLVGPDGAGKTTLMRMLAGLLKPDEGRASVIGFDPLKDDsaLHAVlGYMPQKF 89
Cdd:TIGR03740 5 NLSKRFGKQT--AVNNISLTVPKNSVYGLLGPNGAGKSTLLKMITGILRPTSGEIIFDGHPWTRKD--LHKI-GSLIESP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 90 GLYEDLTVMENLTLYADLRSVTgEARkkiFDRLLEFTSLGPFTERLAGKLSGGMKQKLGLACTLVGDPKVLLLDEPGVGV 169
Cdd:TIGR03740 80 PLYENLTARENLKVHTTLLGLP-DSR---IDEVLNIVDLTNTGKKKAKQFSLGMKQRLGIAIALLNHPKLLILDEPTNGL 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 488984955 170 DPISRRELWQMVHELAGDGMLILWSTSYLDEAEQCRD-VLLMNEGKLLYQGE 220
Cdd:TIGR03740 156 DPIGIQELRELIRSFPEQGITVILSSHILSEVQQLADhIGIISEGVLGYQGK 207
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
330-537 |
4.27e-35 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 131.09 E-value: 4.27e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 330 IEAQSLTKKFGDFAATDHVDFQVKRGEIFGLLGPNGAGKSTTFKMMCGLLVPTSGKALVLGMDLKVSSGKA-RQHLGYMA 408
Cdd:COG4619 1 LELEGLSFRVGGKPILSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIYLDGKPLSAMPPPEwRRQVAYVP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 409 QKFSLYGNlSVEQNLRFfsgVYGLRGRAQN-EKIARMSDAFGL-KSIARHAADELPLGYKQRLALACSLMHEPDILFLDE 486
Cdd:COG4619 81 QEPALWGG-TVRDNLPF---PFQLRERKFDrERALELLERLGLpPDILDKPVERLSGGERQRLALIRALLLQPDVLLLDE 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 488984955 487 PTSGVDPLTRREFWLHINSMV-DKGVTVMVTTHFMDEAE-YCDRIGLVYHGKL 537
Cdd:COG4619 157 PTSALDPENTRRVEELLREYLaEEGRAVLWVSHDPEQIErVADRVLTLEAGRL 209
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
330-544 |
5.90e-35 |
|
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: 131.59 E-value: 5.90e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 330 IEAQSLTKKFGDFAATDHVDFQVKRGEIFGLLGPNGAGKSTTFKMMCGLLVPTSGKALVLGMDLkVSSGKARQHLGYMAQ 409
Cdd:cd03300 1 IELENVSKFYGGFVALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGKDI-TNLPPHKRPVNTVFQ 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 410 KFSLYGNLSVEQNLRFFSGVYGLRGRAQNEKIARMSDAFGLKSIARHAADELPLGYKQRLALACSLMHEPDILFLDEPTS 489
Cdd:cd03300 80 NYALFPHLTVFENIAFGLRLKKLPKAEIKERVAEALDLVQLEGYANRKPSQLSGGQQQRVAIARALVNEPKVLLLDEPLG 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 488984955 490 GVDPLTRREFWLHINSMVDK-GVTVMVTTHFMDEA-EYCDRIGLVYHGKLIASGTPD 544
Cdd:cd03300 160 ALDLKLRKDMQLELKRLQKElGITFVFVTHDQEEAlTMSDRIAVMNKGKIQQIGTPE 216
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
5-221 |
5.95e-35 |
|
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: 132.09 E-value: 5.95e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 5 VIALNGLSRRFPGmdRPAVAPLTCTIRAGYVTGLVGPDGAGKTTLMRMLAGLLKPDEGRASVigfdplkDDSALHA---- 80
Cdd:COG1120 1 MLEAENLSVGYGG--RPVLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLL-------DGRDLASlsrr 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 81 ----VLGYMPQKFGLYEDLTVMENLTL----YADLRSVTGEARKKIFDRLLEFTSLGPFTERLAGKLSGGMKQKLGLACT 152
Cdd:COG1120 72 elarRIAYVPQEPPAPFGLTVRELVALgrypHLGLFGRPSAEDREAVEEALERTGLEHLADRPVDELSGGERQRVLIARA 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 488984955 153 LVGDPKVLLLDEPGVGVDPISRRELWQMVHELAGD-GMLILWSTSYLDEAEQCRD-VLLMNEGKLLYQGEP 221
Cdd:COG1120 152 LAQEPPLLLLDEPTSHLDLAHQLEVLELLRRLARErGRTVVMVLHDLNLAARYADrLVLLKDGRIVAQGPP 222
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
5-369 |
6.45e-35 |
|
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim protein) in eukaryotes. It is the member of ABC transporter superfamily. Rim protein is a membrane glycoprotein which is localized in the photoreceptor outer segment discs. Mutation/s in its genetic loci is implicated in the recessive Stargardt's disease. [Transport and binding proteins, Other]
Pssm-ID: 130324 [Multi-domain] Cd Length: 2272 Bit Score: 141.30 E-value: 6.45e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 5 VIALNGLSRRFPGMDRPAVAPLTCTIRAGYVTGLVGPDGAGKTTLMRMLAGLLKPDEGRASVIGFDPLKDDSALHAVLGY 84
Cdd:TIGR01257 1937 ILRLNELTKVYSGTSSPAVDRLCVGVRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAGKSILTNISDVHQNMGY 2016
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 85 MPQKFGLYEDLTVMENLTLYADLRSVTGEARKKIFDRLLEFTSLGPFTERLAGKLSGGMKQKLGLACTLVGDPKVLLLDE 164
Cdd:TIGR01257 2017 CPQFDAIDDLLTGREHLYLYARLRGVPAEEIEKVANWSIQSLGLSLYADRLAGTYSGGNKRKLSTAIALIGCPPLVLLDE 2096
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 165 PGVGVDPISRRELWQMVHELAGDGMLILWSTSYLDEAEQ-CRDVLLMNEGKLLYQGEPTALtQTMAGRSFLVS----SPQ 239
Cdd:TIGR01257 2097 PTTGMDPQARRMLWNTIVSIIREGRAVVLTSHSMEECEAlCTRLAIMVKGAFQCLGTIQHL-KSKFGDGYIVTmkikSPK 2175
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 240 ENnrrLLQRALKLPQVSDGVIQGKSVRlilkkdarieevQQHGDMPPLQVadtaprfedafidllggagtAESPLGAIIH 319
Cdd:TIGR01257 2176 DD---LLPDLNPVEQFFQGNFPGSVQR------------ERHYNMLQFQV--------------------SSSSLARIFQ 2220
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|.
gi 488984955 320 RVDGSKEETVIEAQSLTKKFGDFAatdHVDFQVKRGEIFGL-LGPNGAGKS 369
Cdd:TIGR01257 2221 LLISHKDSLLIEEYSVTQTTLDQV---FVNFAKQQTETYDLpLHPRAAGAS 2268
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
330-518 |
2.44e-34 |
|
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where FtsE is the ATPase and the membrane subunit FtsX resembles a permease subunit. But rather than transporting any substrate, the complex acts in cell division by undergoing conformational changes that alter the activity of cell wall hydrolases located outside the plasma membrane. The complex is widely conserved in bacteria, but also extremely divergent in sequence between different lineages
Pssm-ID: 213259 [Multi-domain] Cd Length: 214 Bit Score: 129.45 E-value: 2.44e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 330 IEAQSLTKKF-GDFAATDHVDFQVKRGEIFGLLGPNGAGKSTTFKMMCGLLVPTSGKALVLGMDLKVSSGKA----RQHL 404
Cdd:cd03292 1 IEFINVTKTYpNGTAALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQDVSDLRGRAipylRRKI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 405 GYMAQKFSLYGNLSVEQNLRFFSGVYGLRGRAQNEKIARMSDAFGLKSIARHAADELPLGYKQRLALACSLMHEPDILFL 484
Cdd:cd03292 81 GVVFQDFRLLPDRNVYENVAFALEVTGVPPREIRKRVPAALELVGLSHKHRALPAELSGGEQQRVAIARAIVNSPTILIA 160
|
170 180 190
....*....|....*....|....*....|....
gi 488984955 485 DEPTSGVDPLTRREFWLHINSMVDKGVTVMVTTH 518
Cdd:cd03292 161 DEPTGNLDPDTTWEIMNLLKKINKAGTTVVVATH 194
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
6-221 |
2.55e-34 |
|
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ABC transporter subfamily is involved in the transport of the hydrophobic amino acids leucine, isoleucine and valine. MJ1267 is a branched-chain amino acid transporter with 29% similarity to both the LivF and LivG components of the E. coli branched-chain amino acid transporter. MJ1267 contains an insertion from residues 114 to 123 characteristic of LivG (Leucine-Isoleucine-Valine) homologs. The branched-chain amino acid transporter from E. coli comprises a heterodimer of ABCs (LivF and LivG), a heterodimer of six-helix TM domains (LivM and LivH), and one of two alternative soluble periplasmic substrate binding proteins (LivK or LivJ).
Pssm-ID: 213186 [Multi-domain] Cd Length: 236 Bit Score: 129.86 E-value: 2.55e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 6 IALNGLSRRFPGMdrPAVAPLTCTIRAGYVTGLVGPDGAGKTTLMRMLAGLLKPDEGR-----ASVIGFDPlkddsalHA 80
Cdd:cd03219 1 LEVRGLTKRFGGL--VALDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSvlfdgEDITGLPP-------HE 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 81 V----LGYMPQKFGLYEDLTVMENLTLYADLRSVTG-----------EARKKIfDRLLEFTSLGPFTERLAGKLSGGMKQ 145
Cdd:cd03219 72 IarlgIGRTFQIPRLFPELTVLENVMVAAQARTGSGlllararreerEARERA-EELLERVGLADLADRPAGELSYGQQR 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 146 KLGLACTLVGDPKVLLLDEPGVGVDPISRRELWQMVHELAGDGMLILWStsyldE------AEQCRDVLLMNEGKLLYQG 219
Cdd:cd03219 151 RLEIARALATDPKLLLLDEPAAGLNPEETEELAELIRELRERGITVLLV-----EhdmdvvMSLADRVTVLDQGRVIAEG 225
|
..
gi 488984955 220 EP 221
Cdd:cd03219 226 TP 227
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
3-221 |
5.14e-34 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 129.38 E-value: 5.14e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 3 ETVIALNGLSRRFPGmdRPAVAPLTCTIRAGYVTGLVGPDGAGKTTLMRMLAGLLKPDEGRasvIGFDPlKDDSAL---- 78
Cdd:COG1137 1 MMTLEAENLVKSYGK--RTVVKDVSLEVNQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGR---IFLDG-EDITHLpmhk 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 79 --HAVLGYMPQKFGLYEDLTVMENLTLYADLRSVTGEARKKIFDRLLEFTSLGPFTERLAGKLSGGMKQKLGLACTLVGD 156
Cdd:COG1137 75 raRLGIGYLPQEASIFRKLTVEDNILAVLELRKLSKKEREERLEELLEEFGITHLRKSKAYSLSGGERRRVEIARALATN 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 488984955 157 PKVLLLDEPGVGVDPISRRELWQMVHELAGDGMLIL------WST-SYLDEAeqcrdvLLMNEGKLLYQGEP 221
Cdd:COG1137 155 PKFILLDEPFAGVDPIAVADIQKIIRHLKERGIGVLitdhnvRETlGICDRA------YIISEGKVLAEGTP 220
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
331-541 |
1.14e-33 |
|
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: 126.40 E-value: 1.14e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 331 EAQSLTKKFGDFAATDHVDFQVKRGEIFGLLGPNGAGKSTTFKMMCGLLVPTSGKALVLGMDLKVSSGKAR-QHLGYMAQ 409
Cdd:cd03214 1 EVENLSVGYGGRTVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDGKDLASLSPKELaRKIAYVPQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 410 kfslygnlsveqnlrffsgvyglrgraqnekiarMSDAFGLKSIARHAADELPLGYKQRLALACSLMHEPDILFLDEPTS 489
Cdd:cd03214 81 ----------------------------------ALELLGLAHLADRPFNELSGGERQRVLLARALAQEPPILLLDEPTS 126
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 488984955 490 GVDPLTRREFWLHINSMVD-KGVTVMVTTHFMDEA-EYCDRIGLVYHGKLIASG 541
Cdd:cd03214 127 HLDIAHQIELLELLRRLAReRGKTVVMVLHDLNLAaRYADRVILLKDGRIVAQG 180
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
344-547 |
1.27e-33 |
|
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: 137.45 E-value: 1.27e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 344 ATDHVDFQVKRGEIFGLLGPNGAGKSTTFKMMCGLLVPTSGKALVLGMDLKVSSGKARQHLGYMAQKFSLYGNLSVEQNL 423
Cdd:TIGR01257 945 AVDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGKDIETNLDAVRQSLGMCPQHNILFHHLTVAEHI 1024
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 424 RFFSGvygLRGRAQNE---KIARMSDAFGLKSIARHAADELPLGYKQRLALACSLMHEPDILFLDEPTSGVDPLTRREFW 500
Cdd:TIGR01257 1025 LFYAQ---LKGRSWEEaqlEMEAMLEDTGLHHKRNEEAQDLSGGMQRKLSVAIAFVGDAKVVVLDEPTSGVDPYSRRSIW 1101
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 488984955 501 ---LHINSmvdkGVTVMVTTHFMDEAEYC-DRIGLVYHGKLIASGTPDALK 547
Cdd:TIGR01257 1102 dllLKYRS----GRTIIMSTHHMDEADLLgDRIAIISQGRLYCSGTPLFLK 1148
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
330-540 |
1.68e-33 |
|
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: 125.23 E-value: 1.68e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 330 IEAQSLTKKFGDFAATDHVDFQVKRGEIFGLLGPNGAGKSTTFKMMCGLLVPTSGKALVLGMDLKVSSGKARQHLG-YMa 408
Cdd:cd03216 1 LELRGITKRFGGVKALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVDGKEVSFASPRDARRAGiAM- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 409 qkfslygnlsveqnlrffsgVYglrgraqnekiarmsdafglksiarhaadELPLGYKQRLALACSLMHEPDILFLDEPT 488
Cdd:cd03216 80 --------------------VY-----------------------------QLSVGERQMVEIARALARNARLLILDEPT 110
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 488984955 489 SGVDPLTRREFWLHINSMVDKGVTVMVTTHFMDEA-EYCDRIGLVYHGKLIAS 540
Cdd:cd03216 111 AALTPAEVERLFKVIRRLRAQGVAVIFISHRLDEVfEIADRVTVLRDGRVVGT 163
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
22-235 |
3.38e-33 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 129.44 E-value: 3.38e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 22 AVAPLTCTIRAGYVTGLVGPDGAGKTTLMRMLAGLLKPDEGRASVIGFDPLKDDSAL----HAVLGympQKFGLYEDLTV 97
Cdd:COG4586 37 AVDDISFTIEPGEIVGFIGPNGAGKSTTIKMLTGILVPTSGEVRVLGYVPFKRRKEFarriGVVFG---QRSQLWWDLPA 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 98 MENLTLYADLRSVTGEARKKIFDRLLEFTSLGPFTERLAGKLSGGMKQKLGLACTLVGDPKVLLLDEPGVGVDPISRREL 177
Cdd:COG4586 114 IDSFRLLKAIYRIPDAEYKKRLDELVELLDLGELLDTPVRQLSLGQRMRCELAAALLHRPKILFLDEPTIGLDVVSKEAI 193
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 178 WQMVHEL-AGDGMLILWSTSYLDEAEQ-CRDVLLMNEGKLLYQGEPTALTQTMAGRSFLV 235
Cdd:COG4586 194 REFLKEYnRERGTTILLTSHDMDDIEAlCDRVIVIDHGRIIYDGSLEELKERFGPYKTIV 253
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
330-546 |
3.86e-33 |
|
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: 126.68 E-value: 3.86e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 330 IEAQSLTKKFGDFAATDHVDFQVKRGEIFGLLGPNGAGKSTTFKMMCGLLVPTSGKALVLGMDlkVSSGKARQ-HLGYMA 408
Cdd:cd03296 3 IEVRNVSKRFGDFVALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGGED--ATDVPVQErNVGFVF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 409 QKFSLYGNLSVEQNLRFfsgvyGLRGRAQNE---------KIARMSDAFGLKSIARHAADELPLGYKQRLALACSLMHEP 479
Cdd:cd03296 81 QHYALFRHMTVFDNVAF-----GLRVKPRSErppeaeiraKVHELLKLVQLDWLADRYPAQLSGGQRQRVALARALAVEP 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 488984955 480 DILFLDEPTSGVDPLTRREF--WLHinSMVDK-GVTVMVTTHFMDEA-EYCDRIGLVYHGKLIASGTPDAL 546
Cdd:cd03296 156 KVLLLDEPFGALDAKVRKELrrWLR--RLHDElHVTTVFVTHDQEEAlEVADRVVVMNKGRIEQVGTPDEV 224
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
1-546 |
3.90e-33 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 132.84 E-value: 3.90e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 1 MSETVIALNGLSRRFPGM---DRpavapLTCTIRAGYVTGLVGPDGAGKTTLMRMLAGLLKPDEGRASVIGfDPLKDDS- 76
Cdd:COG3845 1 MMPPALELRGITKRFGGVvanDD-----VSLTVRPGEIHALLGENGAGKSTLMKILYGLYQPDSGEILIDG-KPVRIRSp 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 77 --ALHAVLGYMPQKFGLYEDLTVMENLTLYADLRSVTGEARKKIFDRLLEFTSLGPFT---ERLAGKLSGGMKQKLGLAC 151
Cdd:COG3845 75 rdAIALGIGMVHQHFMLVPNLTVAENIVLGLEPTKGGRLDRKAARARIRELSERYGLDvdpDAKVEDLSVGEQQRVEILK 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 152 TLVGDPKVLLLDEPGVGVDPISRRELWQMVHELAGDGMLILWSTSYLDEAEQ-CRDVLLMNEGKLLYQGEPTALTQT--- 227
Cdd:COG3845 155 ALYRGARILILDEPTAVLTPQEADELFEILRRLAAEGKSIIFITHKLREVMAiADRVTVLRRGKVVGTVDTAETSEEela 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 228 --MAGRsflvsspqennrrllqralklpqvsdgviqgkSVRLILKKDARieevqQHGDmPPLQVADtaprfedafidllg 305
Cdd:COG3845 235 elMVGR--------------------------------EVLLRVEKAPA-----EPGE-VVLEVEN-------------- 262
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 306 gagtaesplgaiIHRVDGSKEETVieaqsltkkfgdfaatDHVDFQVKRGEIFGLLGPNGAGKSTTFKMMCGLLVPTSGK 385
Cdd:COG3845 263 ------------LSVRDDRGVPAL----------------KDVSLEVRAGEILGIAGVAGNGQSELAEALAGLRPPASGS 314
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 386 ALVLGMDLKVSSGKARQHLGyMA------QKFSLYGNLSVEQNL---RFFSGVYGLRGRAQNEKIARMS----DAFGLKS 452
Cdd:COG3845 315 IRLDGEDITGLSPRERRRLG-VAyipedrLGRGLVPDMSVAENLilgRYRRPPFSRGGFLDRKAIRAFAeeliEEFDVRT 393
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 453 IARHA-ADELPLGYKQRLALACSLMHEPDILFLDEPTSGVDPLTRREFWLHINSMVDKGVTVMVTTHFMDEA-EYCDRIG 530
Cdd:COG3845 394 PGPDTpARSLSGGNQQKVILARELSRDPKLLIAAQPTRGLDVGAIEFIHQRLLELRDAGAAVLLISEDLDEIlALSDRIA 473
|
570
....*....|....*.
gi 488984955 531 LVYHGKLIASGTPDAL 546
Cdd:COG3845 474 VMYEGRIVGEVPAAEA 489
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
6-224 |
4.53e-33 |
|
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: 135.53 E-value: 4.53e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 6 IALNGLSRRFPGMDRPAVAPLTCTIRAGYVTGLVGPDGAGKTTLMRMLAGLLKPDEGRASVIGFDPLKDDSALHAVLGYM 85
Cdd:TIGR01257 929 VCVKNLVKIFEPSGRPAVDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGKDIETNLDAVRQSLGMC 1008
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 86 PQKFGLYEDLTVMENLTLYADLRSVTGEARKKIFDRLLEFTSLGPFTERLAGKLSGGMKQKLGLACTLVGDPKVLLLDEP 165
Cdd:TIGR01257 1009 PQHNILFHHLTVAEHILFYAQLKGRSWEEAQLEMEAMLEDTGLHHKRNEEAQDLSGGMQRKLSVAIAFVGDAKVVVLDEP 1088
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 166 GVGVDPISRRELWQMVHELAgDGMLILWSTSYLDEAEQCRD-VLLMNEGKLLYQGEPTAL 224
Cdd:TIGR01257 1089 TSGVDPYSRRSIWDLLLKYR-SGRTIIMSTHHMDEADLLGDrIAIISQGRLYCSGTPLFL 1147
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
6-227 |
5.58e-33 |
|
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: 126.08 E-value: 5.58e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 6 IALNGLSRRFpGmDRPAVAPLTCTIRAGYVTGLVGPDGAGKTTLMRMLAGLLKPDEGRASVIGFDPL----KDDSALHAV 81
Cdd:cd03261 1 IELRGLTKSF-G-GRTVLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGEDISglseAELYRLRRR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 82 LGYMPQKFGLYEDLTVMENLTLYadLRSVTGEARKKIFDRL---LEFTSLGPFTERLAGKLSGGMKQKLGLACTLVGDPK 158
Cdd:cd03261 79 MGMLFQSGALFDSLTVFENVAFP--LREHTRLSEEEIREIVlekLEAVGLRGAEDLYPAELSGGMKKRVALARALALDPE 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 488984955 159 VLLLDEPGVGVDPISRRELWQMVHELAGD-GMLILWSTSYLDEAEQCRD-VLLMNEGKLLYQGEPTALTQT 227
Cdd:cd03261 157 LLLYDEPTAGLDPIASGVIDDLIRSLKKElGLTSIMVTHDLDTAFAIADrIAVLYDGKIVAEGTPEELRAS 227
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
1-227 |
6.44e-33 |
|
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: 126.25 E-value: 6.44e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 1 MSETVIALNGLSRRFpGmDRPAVAPLTCTIRAGYVTGLVGPDGAGKTTLMRMLAGLLKPDEGRASVIGFDPLK-DDSALH 79
Cdd:COG1127 1 MSEPMIEVRNLTKSF-G-DRVVLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEILVDGQDITGlSEKELY 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 80 AV---LGYMPQKFGLYEDLTVMENLTLYadLRSVTGEARKKIFDR---LLEFTSLGPFTERLAGKLSGGMKQKLGLACTL 153
Cdd:COG1127 79 ELrrrIGMLFQGGALFDSLTVFENVAFP--LREHTDLSEAEIRELvleKLELVGLPGAADKMPSELSGGMRKRVALARAL 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 154 VGDPKVLLLDEPGVGVDPISRRELWQMVHELAGD-GMlilwsTSY-----LDEAEQCRD-VLLMNEGKLLYQGEPTALTQ 226
Cdd:COG1127 157 ALDPEILLYDEPTAGLDPITSAVIDELIRELRDElGL-----TSVvvthdLDSAFAIADrVAVLADGKIIAEGTPEELLA 231
|
.
gi 488984955 227 T 227
Cdd:COG1127 232 S 232
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
2-221 |
7.27e-33 |
|
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid transport and metabolism];
Pssm-ID: 440180 [Multi-domain] Cd Length: 257 Bit Score: 126.69 E-value: 7.27e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 2 SETVIALNGLSRRFPGMdrPAVAPLTCTIRAGYVTGLVGPDGAGKTTLMRMLAGLLKPDEGR-----ASVIGFDPlkdds 76
Cdd:COG0411 1 SDPLLEVRGLTKRFGGL--VAVDDVSLEVERGEIVGLIGPNGAGKTTLFNLITGFYRPTSGRilfdgRDITGLPP----- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 77 alHAV----LGYMPQKFGLYEDLTVMENLTLYADLRSVTG----------------EARKKIfDRLLEFTSLGPFTERLA 136
Cdd:COG0411 74 --HRIarlgIARTFQNPRLFPELTVLENVLVAAHARLGRGllaallrlprarreerEARERA-EELLERVGLADRADEPA 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 137 GKLSGGMKQKLGLACTLVGDPKVLLLDEPGVGVDPISRRELWQMVHELAGD-GMLILwstsyLDE------AEQCRDVLL 209
Cdd:COG0411 151 GNLSYGQQRRLEIARALATEPKLLLLDEPAAGLNPEETEELAELIRRLRDErGITIL-----LIEhdmdlvMGLADRIVV 225
|
250
....*....|..
gi 488984955 210 MNEGKLLYQGEP 221
Cdd:COG0411 226 LDFGRVIAEGTP 237
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
326-543 |
8.88e-33 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 127.13 E-value: 8.88e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 326 EETVIEAQSLTKKFGD------FAATDHVDFQVKRGEIFGLLGPNGAGKSTTFKMMCGLLVPTSGKALVLGMDLKVSSG- 398
Cdd:PRK13633 1 MNEMIKCKNVSYKYESneesteKLALDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVYVDGLDTSDEENl 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 399 -KARQHLGYMAQK--FSLYGNLsVEQNLRFfsGVYGLrGRAQNEKIARMSDAF---GLKSIARHAADELPLGYKQRLALA 472
Cdd:PRK13633 81 wDIRNKAGMVFQNpdNQIVATI-VEEDVAF--GPENL-GIPPEEIRERVDESLkkvGMYEYRRHAPHLLSGGQKQRVAIA 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 488984955 473 CSLMHEPDILFLDEPTSGVDPLTRREFWLHINSMVDK-GVTVMVTTHFMDEAEYCDRIGLVYHGKLIASGTP 543
Cdd:PRK13633 157 GILAMRPECIIFDEPTAMLDPSGRREVVNTIKELNKKyGITIILITHYMEEAVEADRIIVMDSGKVVMEGTP 228
|
|
| LPS_export_lptB |
TIGR04406 |
LPS export ABC transporter ATP-binding protein; Members of this fmaily are LptB, the ... |
10-222 |
1.06e-32 |
|
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: 125.46 E-value: 1.06e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 10 GLSRRFPGmdRPAVAPLTCTIRAGYVTGLVGPDGAGKTTLMRMLAGLLKPDEGRASVIGFD----PLKDDSALHavLGYM 85
Cdd:TIGR04406 6 NLIKSYKK--RKVVNDVSLSVKSGEIVGLLGPNGAGKTTSFYMIVGLVRPDAGKILIDGQDithlPMHERARLG--IGYL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 86 PQKFGLYEDLTVMENLTLYADLR-SVTGEARKKIFDRLLEFTSLGPFTERLAGKLSGGMKQKLGLACTLVGDPKVLLLDE 164
Cdd:TIGR04406 82 PQEASIFRKLTVEENIMAVLEIRkDLDRAEREERLEALLEEFQISHLRDNKAMSLSGGERRRVEIARALATNPKFILLDE 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 488984955 165 PGVGVDPISRRELWQMVHELAGDGMLILWSTSYLDEA-EQCRDVLLMNEGKLLYQGEPT 222
Cdd:TIGR04406 162 PFAGVDPIAVGDIKKIIKHLKERGIGVLITDHNVRETlDICDRAYIISDGKVLAEGTPA 220
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
330-543 |
1.32e-32 |
|
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely related to ModC. ModC is an ABC-type transporter and the ATPase component of a molybdate transport system that also includes the periplasmic binding protein ModA and the membrane protein ModB. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213266 [Multi-domain] Cd Length: 235 Bit Score: 125.14 E-value: 1.32e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 330 IEAQSLTKKFGDFAATDhVDFQVKRGEIFGLLGPNGAGKSTTFKMMCGLLVPTSGKALVLGMDLKVSSGKARQhLGYMAQ 409
Cdd:cd03299 1 LKVENLSKDWKEFKLKN-VSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNGKDITNLPPEKRD-ISYVPQ 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 410 KFSLYGNLSVEQNLrffsgVYGLRGRAQN-----EKIARMSDAFGLKSIARHAADELPLGYKQRLALACSLMHEPDILFL 484
Cdd:cd03299 79 NYALFPHMTVYKNI-----AYGLKKRKVDkkeieRKVLEIAEMLGIDHLLNRKPETLSGGEQQRVAIARALVVNPKILLL 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 488984955 485 DEPTSGVDPLTRREfwlhINSMVDK-----GVTVMVTTH-FMDEAEYCDRIGLVYHGKLIASGTP 543
Cdd:cd03299 154 DEPFSALDVRTKEK----LREELKKirkefGVTVLHVTHdFEEAWALADKVAIMLNGKLIQVGKP 214
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
346-549 |
2.04e-32 |
|
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: 132.65 E-value: 2.04e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 346 DHVDFQVKRGEIFGLLGPNGAGKSTTFKMMCGLLVPTSGKALVLGMDLK-VSSGKARQHLGYMAQKFSL-YGnlSVEQNL 423
Cdd:COG2274 492 DNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEPTSGRILIDGIDLRqIDPASLRRQIGVVLQDVFLfSG--TIRENI 569
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 424 RFFsgvyglRGRAQNEKIARMSDAFGLKSIARhaadELPLGY---------------KQRLALACSLMHEPDILFLDEPT 488
Cdd:COG2274 570 TLG------DPDATDEEIIEAARLAGLHDFIE----ALPMGYdtvvgeggsnlsggqRQRLAIARALLRNPRILILDEAT 639
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 488984955 489 SGVDPLTRREFWLHINSMvDKGVTVMVTTHFMDEAEYCDRIGLVYHGKLIASGTPDALKAQ 549
Cdd:COG2274 640 SALDAETEAIILENLRRL-LKGRTVIIIAHRLSTIRLADRIIVLDKGRIVEDGTHEELLAR 699
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
1-224 |
2.15e-32 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 127.57 E-value: 2.15e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 1 MSetvIALNGLSRRFPgmDRPAVAPLTCTIRAGYVTGLVGPDGAGKTTLMRMLAGLLKPDEGRASVIGfdplKD-DSALH 79
Cdd:COG1118 1 MS---IEVRNISKRFG--SFTLLDDVSLEIASGELVALLGPSGSGKTTLLRIIAGLETPDSGRIVLNG----RDlFTNLP 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 80 A----VlGYMPQKFGLYEDLTVMENLTLYADLRSVTGEARKKIFDRLLEFTSLGPFTERLAGKLSGGMKQKLGLACTLVG 155
Cdd:COG1118 72 PrerrV-GFVFQHYALFPHMTVAENIAFGLRVRPPSKAEIRARVEELLELVQLEGLADRYPSQLSGGQRQRVALARALAV 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 488984955 156 DPKVLLLDEPGVGVDPISRRELW----QMVHELAGDgmlILWSTSYLDEA-EQCRDVLLMNEGKLLYQGEPTAL 224
Cdd:COG1118 151 EPEVLLLDEPFGALDAKVRKELRrwlrRLHDELGGT---TVFVTHDQEEAlELADRVVVMNQGRIEQVGTPDEV 221
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
346-536 |
2.35e-32 |
|
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: 122.49 E-value: 2.35e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 346 DHVDFQVKRGEIFGLLGPNGAGKSTTFKMMCGLLVPTSGKALVLGMDLK-VSSGKARQHLGYMAQKFSLYgNLSVEQNLr 424
Cdd:cd03228 19 KDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGVDLRdLDLESLRKNIAYVPQDPFLF-SGTIRENI- 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 425 fFSGvyglrgraqnekiarmsdafglksiarhaadelplGYKQRLALACSLMHEPDILFLDEPTSGVDPLTRREFWLHIN 504
Cdd:cd03228 97 -LSG-----------------------------------GQRQRIAIARALLRDPPILILDEATSALDPETEALILEALR 140
|
170 180 190
....*....|....*....|....*....|..
gi 488984955 505 SMvDKGVTVMVTTHFMDEAEYCDRIGLVYHGK 536
Cdd:cd03228 141 AL-AKGKTVIVIAHRLSTIRDADRIIVLDDGR 171
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
6-215 |
2.44e-32 |
|
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: 123.75 E-value: 2.44e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 6 IALNGLSRRFPGMDR--PAVAPLTCTIRAGYVTGLVGPDGAGKTTLMRMLAGLLKPDEGRASVIGFDPLK-DDSALHAV- 81
Cdd:cd03255 1 IELKNLSKTYGGGGEkvQALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRVDGTDISKlSEKELAAFr 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 82 ---LGYMPQKFGLYEDLTVMENLTLYADLRSVTGEARKKIFDRLLEFTSLGPFTERLAGKLSGGMKQKLGLACTLVGDPK 158
Cdd:cd03255 81 rrhIGFVFQSFNLLPDLTALENVELPLLLAGVPKKERRERAEELLERVGLGDRLNHYPSELSGGQQQRVAIARALANDPK 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 488984955 159 VLLLDEPGVGVDPISRRELWQMVHELA-GDGMLILWSTSYLDEAEQCRDVLLMNEGKL 215
Cdd:cd03255 161 IILADEPTGNLDSETGKEVMELLRELNkEAGTTIVVVTHDPELAEYADRIIELRDGKI 218
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
1-537 |
3.69e-32 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 129.90 E-value: 3.69e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 1 MSETVIALNGLSRRFPGMDrpAVAPLTCTIRAGYVTGLVGPDGAGKTTLMRMLAGLLKPDEGRASVIGFDPLKDDSALHA 80
Cdd:PRK09700 1 MATPYISMAGIGKSFGPVH--ALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNINYNKLDHKLAA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 81 VLG--YMPQKFGLYEDLTVMENLTL---------------YADLRSVTGEarkkIFDRLLEFTSLgpftERLAGKLSGGM 143
Cdd:PRK09700 79 QLGigIIYQELSVIDELTVLENLYIgrhltkkvcgvniidWREMRVRAAM----MLLRVGLKVDL----DEKVANLSISH 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 144 KQKLGLACTLVGDPKVLLLDEPGVGVDPISRRELWQMVHELAGDGMLILWSTSYLDEAEQ-CRDVLLMNEGKLLYQGEpt 222
Cdd:PRK09700 151 KQMLEIAKTLMLDAKVIIMDEPTSSLTNKEVDYLFLIMNQLRKEGTAIVYISHKLAEIRRiCDRYTVMKDGSSVCSGM-- 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 223 altqtmagrsflvsspqennrrllqralklpqVSDgVIQGKSVRLILKKDarieevqqhgdmpplqvadtaprFEDAFId 302
Cdd:PRK09700 229 --------------------------------VSD-VSNDDIVRLMVGRE-----------------------LQNRFN- 251
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 303 llggagtaesplgAIIHRVDGSKEETVIEAQSLTKKfgDFAATDHVDFQVKRGEIFGLLGPNGAGKSTTFKMMCGLLVPT 382
Cdd:PRK09700 252 -------------AMKENVSNLAHETVFEVRNVTSR--DRKKVRDISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRA 316
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 383 SGKALVLGMDLKVSS--GKARQHLGYMAQ---KFSLYGNLSVEQNLRF--------FSGVYGLRGRAQNEKIARmsDAFG 449
Cdd:PRK09700 317 GGEIRLNGKDISPRSplDAVKKGMAYITEsrrDNGFFPNFSIAQNMAIsrslkdggYKGAMGLFHEVDEQRTAE--NQRE 394
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 450 LKSIARHAAD----ELPLGYKQRLALACSLMHEPDILFLDEPTSGVDPLTRREFWLHINSMVDKGVTV-MVTTHFMDEAE 524
Cdd:PRK09700 395 LLALKCHSVNqnitELSGGNQQKVLISKWLCCCPEVIIFDEPTRGIDVGAKAEIYKVMRQLADDGKVIlMVSSELPEIIT 474
|
570
....*....|...
gi 488984955 525 YCDRIGLVYHGKL 537
Cdd:PRK09700 475 VCDRIAVFCEGRL 487
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
6-214 |
5.11e-32 |
|
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: 121.53 E-value: 5.11e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 6 IALNGLSRRFPGmdRPAVAPLTCTIRAGYVTGLVGPDGAGKTTLMRMLAGLLKPDEGRASVIG--FDPLKDDSALH-AVL 82
Cdd:cd03229 1 LELKNVSKRYGQ--KTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGedLTDLEDELPPLrRRI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 83 GYMPQKFGLYEDLTVMENLTLyadlrsvtgearkkifdrlleftslgpfterlagKLSGGMKQKLGLACTLVGDPKVLLL 162
Cdd:cd03229 79 GMVFQDFALFPHLTVLENIAL----------------------------------GLSGGQQQRVALARALAMDPDVLLL 124
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 488984955 163 DEPGVGVDPISRRELWQMVHEL-AGDGMLILWSTSYLDEAEQCRD-VLLMNEGK 214
Cdd:cd03229 125 DEPTSALDPITRREVRALLKSLqAQLGITVVLVTHDLDEAARLADrVVVLRDGK 178
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
327-547 |
6.14e-32 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 123.95 E-value: 6.14e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 327 ETVIEAQSLTKKFGDFAATDHVDFQVKRGEIFGLLGPNGAGKSTTFKMMCGLLVPTSGKALVLGMDLKVSSGK--ARQHL 404
Cdd:PRK11300 3 QPLLSVSGLMMRFGGLLAVNNVNLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTILLRGQHIEGLPGHqiARMGV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 405 GYMAQKFSLYGNLSVEQNL----------RFFSGVYGLRG--RAQNEKIARMS---DAFGLKSIARHAADELPLGYKQRL 469
Cdd:PRK11300 83 VRTFQHVRLFREMTVIENLlvaqhqqlktGLFSGLLKTPAfrRAESEALDRAAtwlERVGLLEHANRQAGNLAYGQQRRL 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 470 ALACSLMHEPDILFLDEPTSGVDPLTRREfwlhINSMVDK-----GVTVMVTTHFMDEA-EYCDRIGLVYHGKLIASGTP 543
Cdd:PRK11300 163 EIARCMVTQPEILMLDEPAAGLNPKETKE----LDELIAElrnehNVTVLLIEHDMKLVmGISDRIYVVNQGTPLANGTP 238
|
....
gi 488984955 544 DALK 547
Cdd:PRK11300 239 EEIR 242
|
|
| proV |
TIGR01186 |
glycine betaine/L-proline transport ATP binding subunit; This model describes the glycine ... |
337-553 |
7.27e-32 |
|
glycine betaine/L-proline transport ATP binding subunit; This model describes 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 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. Functionally, this transport system is involved in osmoregulation. Under conditions of stress, the organism recruits these transport system to accumulate glycine betaine and other solutes which offer osmo-protection. It has been demonstrated that glycine betaine uptake is accompanied by symport with sodium ions. The locus has been named variously as proU or opuA. A gene library from L.lactis functionally complements an E.coli proU mutant. The comlementing locus is similar to a opuA locus in B.sutlis. This clarifies the differences in nomenclature. [Transport and binding proteins, Amino acids, peptides and amines]
Pssm-ID: 130254 [Multi-domain] Cd Length: 363 Bit Score: 126.51 E-value: 7.27e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 337 KKFGDFAATDHVDFQVKRGEIFGLLGPNGAGKSTTFKMMCGLLVPTSGKALVLGMDLKVSS-----GKARQHLGYMAQKF 411
Cdd:TIGR01186 1 KKTGGKKGVNDADLAIAKGEIFVIMGLSGSGKSTTVRMLNRLIEPTAGQIFIDGENIMKQSpvelrEVRRKKIGMVFQQF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 412 SLYGNLSVEQNLRFFSGVYGLRGRAQNEKIARMSDAFGLKSIARHAADELPLGYKQRLALACSLMHEPDILFLDEPTSGV 491
Cdd:TIGR01186 81 ALFPHMTILQNTSLGPELLGWPEQERKEKALELLKLVGLEEYEHRYPDELSGGMQQRVGLARALAAEPDILLMDEAFSAL 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 488984955 492 DPLTRREFWLHINSMVDK-GVTVMVTTHFMDEA-EYCDRIGLVYHGKLIASGTPDALKAQAADD 553
Cdd:TIGR01186 161 DPLIRDSMQDELKKLQATlQKTIVFITHDLDEAiRIGDRIVIMKAGEIVQVGTPDEILRNPANE 224
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
327-548 |
8.84e-32 |
|
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: 122.78 E-value: 8.84e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 327 ETVIEAQSLTKKFGDFAATDHVDFQVKRGEIFGLLGPNGAGKSTTFKMMCGLLVPTSGKALVLGMDL-KVSSGK-ARQHL 404
Cdd:COG0410 1 MPMLEVENLHAGYGGIHVLHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRSGSIRFDGEDItGLPPHRiARLGI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 405 GYMAQKFSLYGNLSVEQNLRffSGVYGLRGRAQNEK-IARMSDAF-GLKSIARHAADELPLGYKQRLALACSLMHEPDIL 482
Cdd:COG0410 81 GYVPEGRRIFPSLTVEENLL--LGAYARRDRAEVRAdLERVYELFpRLKERRRQRAGTLSGGEQQMLAIGRALMSRPKLL 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 488984955 483 FLDEPTSGVDPLTRREFWLHINSMVDKGVTVMVTTHFMDEA-EYCDRIGLVYHGKLIASGTPDALKA 548
Cdd:COG0410 159 LLDEPSLGLAPLIVEEIFEIIRRLNREGVTILLVEQNARFAlEIADRAYVLERGRIVLEGTAAELLA 225
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
6-228 |
9.03e-32 |
|
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: 123.06 E-value: 9.03e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 6 IALNGLSRRFPGmDRPAVAPLTCTIRAGYVTGLVGPDGAGKTTLMRMLAGLLKPDEGRASVIGFDPLKD-DSALHAV--- 81
Cdd:cd03256 1 IEVENLSKTYPN-GKKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGTDINKLkGKALRQLrrq 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 82 LGYMPQKFGLYEDLTVMENL---------TLYADLRSVTGEARKKIFdRLLEFTSLGPFTERLAGKLSGGMKQKLGLACT 152
Cdd:cd03256 80 IGMIFQQFNLIERLSVLENVlsgrlgrrsTWRSLFGLFPKEEKQRAL-AALERVGLLDKAYQRADQLSGGQQQRVAIARA 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 488984955 153 LVGDPKVLLLDEPGVGVDPISRRELWQMVHELA-GDGMLILWSTSYLDEA-EQCRDVLLMNEGKLLYQGEPTALTQTM 228
Cdd:cd03256 159 LMQQPKLILADEPVASLDPASSRQVMDLLKRINrEEGITVIVSLHQVDLArEYADRIVGLKDGRIVFDGPPAELTDEV 236
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
330-546 |
1.06e-31 |
|
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: 122.29 E-value: 1.06e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 330 IEAQSLTKKFGDFAATDHVDFQVKRGEIFGLLGPNGAGKSTTFKMMCGLL-----VPTSGKALVLGMDLKVSSGKA---R 401
Cdd:cd03260 1 IELRDLNVYYGDKHALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRLNdlipgAPDEGEVLLDGKDIYDLDVDVlelR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 402 QHLGYMAQKFSLYgNLSVEQNLRFFSGVYGLRGRAQNEKIARMSdafgLKSIA-------RHAADELPLGYKQRLALACS 474
Cdd:cd03260 81 RRVGMVFQKPNPF-PGSIYDNVAYGLRLHGIKLKEELDERVEEA----LRKAAlwdevkdRLHALGLSGGQQQRLCLARA 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 488984955 475 LMHEPDILFLDEPTSGVDPLTRREFWLHINSMvDKGVTVMVTTHFMDEAEYC-DRIGLVYHGKLIASGTPDAL 546
Cdd:cd03260 156 LANEPEVLLLDEPTSALDPISTAKIEELIAEL-KKEYTIVIVTHNMQQAARVaDRTAFLLNGRLVEFGPTEQI 227
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
3-215 |
1.23e-31 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 122.07 E-value: 1.23e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 3 ETVIALNGLSRRFP--GMDRPAVAPLTCTIRAGYVTGLVGPDGAGKTTLMRMLAGLLKPDEGRASVIGFDPLK-DDSALH 79
Cdd:COG1136 2 SPLLELRNLTKSYGtgEGEVTALRGVSLSIEAGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVLIDGQDISSlSERELA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 80 AV----LGYMPQKFGLYEDLTVMENLTLYADLRSVTGEARKKIFDRLLEFTSLGPFTERLAGKLSGGMKQKLGLACTLVG 155
Cdd:COG1136 82 RLrrrhIGFVFQFFNLLPELTALENVALPLLLAGVSRKERRERARELLERVGLGDRLDHRPSQLSGGQQQRVAIARALVN 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 488984955 156 DPKVLLLDEPGVGVDPISRRELWQMVHELAGD-GMLILWSTSYLDEAEQCRDVLLMNEGKL 215
Cdd:COG1136 162 RPKLILADEPTGNLDSKTGEEVLELLRELNRElGTTIVMVTHDPELAARADRVIRLRDGRI 222
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
337-541 |
1.64e-31 |
|
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type transporter and the ATPase component of a molybdate transport system that also includes the periplasmic binding protein ModA and the membrane protein ModB. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213264 [Multi-domain] Cd Length: 214 Bit Score: 121.63 E-value: 1.64e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 337 KKFGDFaaTDHVDFQVKrGEIFGLLGPNGAGKSTTFKMMCGLLVPTSGKaLVLGMDLKVSSGKA------RQHLGYMAQK 410
Cdd:cd03297 8 KRLPDF--TLKIDFDLN-EEVTGIFGASGAGKSTLLRCIAGLEKPDGGT-IVLNGTVLFDSRKKinlppqQRKIGLVFQQ 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 411 FSLYGNLSVEQNLrffsgVYGLRGRAQNEK---IARMSDAFGLKSIARHAADELPLGYKQRLALACSLMHEPDILFLDEP 487
Cdd:cd03297 84 YALFPHLNVRENL-----AFGLKRKRNREDrisVDELLDLLGLDHLLNRYPAQLSGGEKQRVALARALAAQPELLLLDEP 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 488984955 488 TSGVDPLTRREFWLHINSMV-DKGVTVMVTTHFMDEAEY-CDRIGLVYHGKLIASG 541
Cdd:cd03297 159 FSALDRALRLQLLPELKQIKkNLNIPVIFVTHDLSEAEYlADRIVVMEDGRLQYIG 214
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
6-227 |
1.96e-31 |
|
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: 128.34 E-value: 1.96e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 6 IALNGLSRRFPGmDRPAVAPLTCTIRAGYVTGLVGPDGAGKTTLMRMLAGLLKPDEGRASVIGfDPLKDDS--ALHAVLG 83
Cdd:COG4988 337 IELEDVSFSYPG-GRPALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPPYSGSILING-VDLSDLDpaSWRRQIA 414
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 84 YMPQKFGLYEDlTVMENLTLY------ADLRSVTGEArkkifdRLLEF---------TSLGpftERLAGkLSGGMKQKLG 148
Cdd:COG4988 415 WVPQNPYLFAG-TIRENLRLGrpdasdEELEAALEAA------GLDEFvaalpdgldTPLG---EGGRG-LSGGQAQRLA 483
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 488984955 149 LACTLVGDPKVLLLDEPGVGVDPISRRELWQMVHELAGdGMLILWSTSYLDEAEQCRDVLLMNEGKLLYQGEPTALTQT 227
Cdd:COG4988 484 LARALLRDAPLLLLDEPTAHLDAETEAEILQALRRLAK-GRTVILITHRLALLAQADRILVLDDGRIVEQGTHEELLAK 561
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
329-546 |
2.23e-31 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 121.74 E-value: 2.23e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 329 VIEAQSLTKKFGDFAATDHVDFQVKRGEIFGLLGPNGAGKSTTFKMMCGLLVPTSGKALVLGmdLKVSSGKA-----RQH 403
Cdd:PRK09493 1 MIEFKNVSKHFGPTQVLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDG--LKVNDPKVderliRQE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 404 LGYMAQKFSLYGNLSVEQNLRFfsGVYGLRG--RAQNEKIAR-MSDAFGLKSIARHAADELPLGYKQRLALACSLMHEPD 480
Cdd:PRK09493 79 AGMVFQQFYLFPHLTALENVMF--GPLRVRGasKEEAEKQAReLLAKVGLAERAHHYPSELSGGQQQRVAIARALAVKPK 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 488984955 481 ILFLDEPTSGVDPLTRREFWLHINSMVDKGVTVMVTTHFMDEAE-YCDRIGLVYHGKLIASGTPDAL 546
Cdd:PRK09493 157 LMLFDEPTSALDPELRHEVLKVMQDLAEEGMTMVIVTHEIGFAEkVASRLIFIDKGRIAEDGDPQVL 223
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
330-553 |
3.25e-31 |
|
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: 121.83 E-value: 3.25e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 330 IEAQSLTKKFG----DFAATDHVDFQVKRGEIFGLLGPNGAGKSTTFKMMCGLLVPTSGKALVLGMDLKVSSGKA-RQHL 404
Cdd:COG1124 2 LEVRNLSVSYGqggrRVPVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVTFDGRPVTRRRRKAfRRRV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 405 GYMAQ--KFSLYGNLSVEQNLRffSGVYGLRGRAQNEKIARMSDAFGL-KSIARHAADELPLGYKQRLALACSLMHEPDI 481
Cdd:COG1124 82 QMVFQdpYASLHPRHTVDRILA--EPLRIHGLPDREERIAELLEQVGLpPSFLDRYPHQLSGGQRQRVAIARALILEPEL 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 488984955 482 LFLDEPTSGVDPLTRREFWLHINSM-VDKGVTVMVTTHFMDEAEY-CDRIGLVYHGKLIASGTPDALKAQAADD 553
Cdd:COG1124 160 LLLDEPTSALDVSVQAEILNLLKDLrEERGLTYLFVSHDLAVVAHlCDRVAVMQNGRIVEELTVADLLAGPKHP 233
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
330-542 |
3.64e-31 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 124.03 E-value: 3.64e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 330 IEAQSLTKKF----GDFAATDHVDFQVKRGEIFGLLGPNGAGKSTTFKMMCGLLVPTSGKALVLGMDLKVSSGK----AR 401
Cdd:COG1135 2 IELENLSKTFptkgGPVTALDDVSLTIEKGEIFGIIGYSGAGKSTLIRCINLLERPTSGSVLVDGVDLTALSERelraAR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 402 QHLGYMAQKFSLYGNLSVEQN----LRffsgVYGLRGRAQNEKIARMSDAFGLKSIARHAADELPLGYKQRLALACSLMH 477
Cdd:COG1135 82 RKIGMIFQHFNLLSSRTVAENvalpLE----IAGVPKAEIRKRVAELLELVGLSDKADAYPSQLSGGQKQRVGIARALAN 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 488984955 478 EPDILFLDEPTSGVDPLT-----------RREFwlhinsmvdkGVTVMVTTHFMDEA-EYCDRIGLVYHGKLIASGT 542
Cdd:COG1135 158 NPKVLLCDEATSALDPETtrsildllkdiNREL----------GLTIVLITHEMDVVrRICDRVAVLENGRIVEQGP 224
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
6-227 |
8.33e-31 |
|
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: 126.80 E-value: 8.33e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 6 IALNGLSRRFPGMDRPAVAPLTCTIRAGYVTGLVGPDGAGKTTLMRMLAGLLKPDEGRASvIGFDPLK--DDSALHAVLG 83
Cdd:COG4987 334 LELEDVSFRYPGAGRPVLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFLDPQSGSIT-LGGVDLRdlDEDDLRRRIA 412
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 84 YMPQKFGLYEDlTVMENLTLY------ADLRSVTGEARkkifdrlleftsLGPFTERLAG-----------KLSGGMKQK 146
Cdd:COG4987 413 VVPQRPHLFDT-TLRENLRLArpdatdEELWAALERVG------------LGDWLAALPDgldtwlgeggrRLSGGERRR 479
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 147 LGLACTLVGDPKVLLLDEPGVGVDPISRRELWQMVHELAGDGMLIlWSTSYLDEAEQCRDVLLMNEGKLLYQGEPTALTQ 226
Cdd:COG4987 480 LALARALLRDAPILLLDEPTEGLDAATEQALLADLLEALAGRTVL-LITHRLAGLERMDRILVLEDGRIVEQGTHEELLA 558
|
.
gi 488984955 227 T 227
Cdd:COG4987 559 Q 559
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
328-544 |
1.17e-30 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 119.80 E-value: 1.17e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 328 TVIEAQSLTKKF----------------------GDFAATDHVDFQVKRGEIFGLLGPNGAGKSTTFKMMCGLLVPTSGK 385
Cdd:COG1134 3 SMIEVENVSKSYrlyhepsrslkelllrrrrtrrEEFWALKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTSGR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 386 ALVLGmdlKVSSgkarqHLGYMAqkfSLYGNLSVEQNLRFFSGVYGLRGRAQNEKI------ARMSDAFglksiarhaad 459
Cdd:COG1134 83 VEVNG---RVSA-----LLELGA---GFHPELTGRENIYLNGRLLGLSRKEIDEKFdeivefAELGDFI----------- 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 460 ELPL-----GYKQRLALACSLMHEPDILFLDEPTSGVDPLTRREFWLHINSMVDKGVTVMVTTHFMDE-AEYCDRIGLVY 533
Cdd:COG1134 141 DQPVktyssGMRARLAFAVATAVDPDILLVDEVLAVGDAAFQKKCLARIRELRESGRTVIFVSHSMGAvRRLCDRAIWLE 220
|
250
....*....|.
gi 488984955 534 HGKLIASGTPD 544
Cdd:COG1134 221 KGRLVMDGDPE 231
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
321-552 |
1.49e-30 |
|
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: 127.82 E-value: 1.49e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 321 VDGSKEETVIEAQSLTKKFGDFA--ATDHVDFQVKRGEIFGLLGPNGAGKSTTFKMMCGLLVPTSGKALVLGMDLKVSSG 398
Cdd:TIGR01257 1929 ISGGNKTDILRLNELTKVYSGTSspAVDRLCVGVRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAGKSILTNIS 2008
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 399 KARQHLGYMAQKFSLYGNLSVEQNLRFFSGVYGLRGRaQNEKIARMS-DAFGLKSIARHAADELPLGYKQRLALACSLMH 477
Cdd:TIGR01257 2009 DVHQNMGYCPQFDAIDDLLTGREHLYLYARLRGVPAE-EIEKVANWSiQSLGLSLYADRLAGTYSGGNKRKLSTAIALIG 2087
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 488984955 478 EPDILFLDEPTSGVDPLTRREFWLHINSMVDKGVTVMVTTHFMDEAE-YCDRIGLVYHGKLIASGTPDALKAQAAD 552
Cdd:TIGR01257 2088 CPPLVLLDEPTTGMDPQARRMLWNTIVSIIREGRAVVLTSHSMEECEaLCTRLAIMVKGAFQCLGTIQHLKSKFGD 2163
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
340-541 |
2.22e-30 |
|
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: 118.40 E-value: 2.22e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 340 GDFAATDHVDFQVKRGEIFGLLGPNGAGKSTTFKMMCGLLVPTSGKALVLGmdlKVSSgkarqHLGYMAqkfSLYGNLSV 419
Cdd:cd03220 33 GEFWALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVTVRG---RVSS-----LLGLGG---GFNPELTG 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 420 EQNLRFFSGVYGLRGRAQNEKIARMSDAFGLKsiarhAADELPL-----GYKQRLALACSLMHEPDILFLDEPTSGVDPL 494
Cdd:cd03220 102 RENIYLNGRLLGLSRKEIDEKIDEIIEFSELG-----DFIDLPVktyssGMKARLAFAIATALEPDILLIDEVLAVGDAA 176
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 488984955 495 TRREFWLHINSMVDKGVTVMVTTHFMDE-AEYCDRIGLVYHGKLIASG 541
Cdd:cd03220 177 FQEKCQRRLRELLKQGKTVILVSHDPSSiKRLCDRALVLEKGKIRFDG 224
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
332-548 |
2.22e-30 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 119.23 E-value: 2.22e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 332 AQSLTKKFGDFAATDHVDFQVKRGEIFGLLGPNGAGKSTTFKMMCGLLVPTSGKALVLGMDLKVSS--GKARQHLGYMAQ 409
Cdd:PRK10895 6 AKNLAKAYKGRRVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEDISLLPlhARARRGIGYLPQ 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 410 KFSLYGNLSVEQNLRffsGVYGLR----GRAQNEKIARMSDAFGLKSIARHAADELPLGYKQRLALACSLMHEPDILFLD 485
Cdd:PRK10895 86 EASIFRRLSVYDNLM---AVLQIRddlsAEQREDRANELMEEFHIEHLRDSMGQSLSGGERRRVEIARALAANPKFILLD 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 488984955 486 EPTSGVDPLTRREFWLHINSMVDKGVTVMVTTHFMDEA-EYCDRIGLVYHGKLIASGTPDALKA 548
Cdd:PRK10895 163 EPFAGVDPISVIDIKRIIEHLRDSGLGVLITDHNVRETlAVCERAYIVSQGHLIAHGTPTEILQ 226
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
329-543 |
2.65e-30 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 119.80 E-value: 2.65e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 329 VIEAQSLTKKFGD-FAATDHVDFQVKRGEIFGLLGPNGAGKSTTFKMMCGLLVPTSGKALVLGMDLKVSSG---KARQHL 404
Cdd:PRK13639 1 ILETRDLKYSYPDgTEALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIKGEPIKYDKKsllEVRKTV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 405 GYMAQK-----FSlygnLSVEQNLRFFSGVYGLRGRAQNEKIARMSDAFGLKSIARHAADELPLGYKQRLALACSLMHEP 479
Cdd:PRK13639 81 GIVFQNpddqlFA----PTVEEDVAFGPLNLGLSKEEVEKRVKEALKAVGMEGFENKPPHHLSGGQKKRVAIAGILAMKP 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 488984955 480 DILFLDEPTSGVDPLTRREFWLHINSMVDKGVTVMVTTHFMDEAE-YCDRIGLVYHGKLIASGTP 543
Cdd:PRK13639 157 EIIVLDEPTSGLDPMGASQIMKLLYDLNKEGITIIISTHDVDLVPvYADKVYVMSDGKIIKEGTP 221
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
330-529 |
2.66e-30 |
|
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: 118.02 E-value: 2.66e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 330 IEAQSLTKKFGDFAATDHVDFQVKRGEIFGLLGPNGAGKSTTFKMMCGLLVPTSGKALVLGMDL---KVSSGKARQHLGY 406
Cdd:cd03262 1 IEIKNLHKSFGDFHVLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIDGLKLtddKKNINELRQKVGM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 407 MAQKFSLYGNLSVEQNLRFfsGVYGLRGRAQNEKIARMSDAF---GLKSIARHAADELPLGYKQRLALACSLMHEPDILF 483
Cdd:cd03262 81 VFQQFNLFPHLTVLENITL--APIKVKGMSKAEAEERALELLekvGLADKADAYPAQLSGGQQQRVAIARALAMNPKVML 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 488984955 484 LDEPTSGVDPLTRREFwlhINSMVD---KGVTVMVTTHFMDEA-EYCDRI 529
Cdd:cd03262 159 FDEPTSALDPELVGEV---LDVMKDlaeEGMTMVVVTHEMGFArEVADRV 205
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
329-541 |
2.84e-30 |
|
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: 118.38 E-value: 2.84e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 329 VIEAQSLTKKF----GDFAATDHVDFQVKRGEIFGLLGPNGAGKSTTFKMMCGLLVPTSGKALVLGMDLKVSSGKA---- 400
Cdd:cd03257 1 LLEVKNLSVSFptggGSVKALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGKDLLKLSRRLrkir 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 401 RQHLGYMAQK--FSLYGNLSVEQNLRF-FSGVYGLRGRAQ-NEKIARMSDAFGL-KSIARHAADELPLGYKQRLALACSL 475
Cdd:cd03257 81 RKEIQMVFQDpmSSLNPRMTIGEQIAEpLRIHGKLSKKEArKEAVLLLLVGVGLpEEVLNRYPHELSGGQRQRVAIARAL 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 488984955 476 MHEPDILFLDEPTSGVDPLTRREFwlhINSMVD----KGVTVMVTTHFMDEAEY-CDRIGLVYHGKLIASG 541
Cdd:cd03257 161 ALNPKLLIADEPTSALDVSVQAQI---LDLLKKlqeeLGLTLLFITHDLGVVAKiADRVAVMYAGKIVEEG 228
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
6-214 |
4.17e-30 |
|
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: 115.94 E-value: 4.17e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 6 IALNGLSRRFPGMDRPAVAPLTCTIRAGYVTGLVGPDGAGKTTLMRMLAGLLKPDEGRASVIGFDpLK--DDSALHAVLG 83
Cdd:cd03228 1 IEFKNVSFSYPGRPKPVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGVD-LRdlDLESLRKNIA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 84 YMPQKFGLYEDlTVMENLtlyadlrsvtgearkkifdrlleftslgpfterlagkLSGGMKQKLGLACTLVGDPKVLLLD 163
Cdd:cd03228 80 YVPQDPFLFSG-TIRENI-------------------------------------LSGGQRQRIAIARALLRDPPILILD 121
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 488984955 164 EPGVGVDPISRRELWQMVHELAGDGMLILwSTSYLDEAEQCRDVLLMNEGK 214
Cdd:cd03228 122 EATSALDPETEALILEALRALAKGKTVIV-IAHRLSTIRDADRIIVLDDGR 171
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
5-215 |
4.67e-30 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 117.46 E-value: 4.67e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 5 VIALNGLSRRFPGmDRPAVAPLTCTIRAGYVTGLVGPDGAGKTTLMRMLAGLLKPDEGRASVIGFDPLK-DDSALHAV-- 81
Cdd:COG2884 1 MIRFENVSKRYPG-GREALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLVNGQDLSRlKRREIPYLrr 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 82 -LGYMPQKFGLYEDLTVMENLTLYadLRsVTGEARKKIFDR---LLEFTSLGPFTERLAGKLSGGMKQKLGLACTLVGDP 157
Cdd:COG2884 80 rIGVVFQDFRLLPDRTVYENVALP--LR-VTGKSRKEIRRRvreVLDLVGLSDKAKALPHELSGGEQQRVAIARALVNRP 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 488984955 158 KVLLLDEPGVGVDPISRRELWQMVHELAGDGMLILWSTSYLDEAEQCRD-VLLMNEGKL 215
Cdd:COG2884 157 ELLLADEPTGNLDPETSWEIMELLEEINRRGTTVLIATHDLELVDRMPKrVLELEDGRL 215
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
29-224 |
5.16e-30 |
|
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: 117.78 E-value: 5.16e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 29 TIRAGYVTGLVGPDGAGKTTLMRMLAGLLKPDEGRasvIGFD-----PLKDDSALHAVLGYMPQKFGLYEDLTVMENLTL 103
Cdd:COG0410 25 EVEEGEIVALLGRNGAGKTTLLKAISGLLPPRSGS---IRFDgeditGLPPHRIARLGIGYVPEGRRIFPSLTVEENLLL 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 104 YADLRSvTGEARKKIFDRLLE-FTSLGPFTERLAGKLSGGMKQKLGLACTLVGDPKVLLLDEPGVGVDPISRRELWQMVH 182
Cdd:COG0410 102 GAYARR-DRAEVRADLERVYElFPRLKERRRQRAGTLSGGEQQMLAIGRALMSRPKLLLLDEPSLGLAPLIVEEIFEIIR 180
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 488984955 183 ELAGDGMLILWSTSYLDEAEQCRD-VLLMNEGKLLYQGEPTAL 224
Cdd:COG0410 181 RLNREGVTILLVEQNARFALEIADrAYVLERGRIVLEGTAAEL 223
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
328-564 |
5.73e-30 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 118.34 E-value: 5.73e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 328 TVIEAQSLTKKFGDFAATDHVDFQVKRGEIFGLLGPNGAGKSTTFKMMCGLLVPTSGKALVLGMDLKVSSGKAR-QHLGY 406
Cdd:PRK13548 1 AMLEARNLSVRLGGRTLLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLNGRPLADWSPAELaRRRAV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 407 MAQKFSLYGNLSVEQNLRFfsGVYGLRGRAQNEK--IARMSDAFGLKSIARHAADELPLGYKQRLALACSLM------HE 478
Cdd:PRK13548 81 LPQHSSLSFPFTVEEVVAM--GRAPHGLSRAEDDalVAAALAQVDLAHLAGRDYPQLSGGEQQRVQLARVLAqlwepdGP 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 479 PDILFLDEPTSGVDP------------LTRREfwlhinsmvdkGVTVMVTTHfmD---EAEYCDRIGLVYHGKLIASGTP 543
Cdd:PRK13548 159 PRWLLLDEPTSALDLahqhhvlrlarqLAHER-----------GLAVIVVLH--DlnlAARYADRIVLLHQGRLVADGTP 225
|
250 260
....*....|....*....|..
gi 488984955 544 -DALkaqaaddsqTDPTMEQAF 564
Cdd:PRK13548 226 aEVL---------TPETLRRVY 238
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
6-215 |
5.86e-30 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 116.84 E-value: 5.86e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 6 IALNGLSRRFPGmdRPAVAPLTCTIRAGYVTGLVGPDGAGKTTLMRMLAGLLKPDEGRASVIGfdplKDDSALHAV---- 81
Cdd:COG4619 1 LELEGLSFRVGG--KPILSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIYLDG----KPLSAMPPPewrr 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 82 -LGYMPQKFGLYEDlTVMENLTLYADLRSVtgEARKKIFDRLLEFTSLGP-FTERLAGKLSGGMKQKLGLACTLVGDPKV 159
Cdd:COG4619 75 qVAYVPQEPALWGG-TVRDNLPFPFQLRER--KFDRERALELLERLGLPPdILDKPVERLSGGERQRLALIRALLLQPDV 151
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 488984955 160 LLLDEPGVGVDPISRRELWQMVHEL-AGDGMLILWSTSYLDEAEQ-CRDVLLMNEGKL 215
Cdd:COG4619 152 LLLDEPTSALDPENTRRVEELLREYlAEEGRAVLWVSHDPEQIERvADRVLTLEAGRL 209
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
5-220 |
1.03e-29 |
|
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: 116.91 E-value: 1.03e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 5 VIALNGLSRRFPGMDR--PAVAPLTCTIRAGYVTGLVGPDGAGKTTLMRMLAGLLKPDEGRASVIGFD-PLKDDSALHAV 81
Cdd:cd03258 1 MIELKNVSKVFGDTGGkvTALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGSVLVDGTDlTLLSGKELRKA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 82 ---LGYMPQKFGLYEDLTVMENLTLYADLRSVTGEARKKIFDRLLEFTSLGPFTERLAGKLSGGMKQKLGLACTLVGDPK 158
Cdd:cd03258 81 rrrIGMIFQHFNLLSSRTVFENVALPLEIAGVPKAEIEERVLELLELVGLEDKADAYPAQLSGGQKQRVGIARALANNPK 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 488984955 159 VLLLDEPGVGVDPISRRELWQMVHELAGD-GMLILWSTSYLDEAEQ-CRDVLLMNEGKLLYQGE 220
Cdd:cd03258 161 VLLCDEATSALDPETTQSILALLRDINRElGLTIVLITHEMEVVKRiCDRVAVMEKGEVVEEGT 224
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
329-544 |
1.41e-29 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 120.33 E-value: 1.41e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 329 VIEAQSLTKKFGDFAATDHVDFQVKRGEIFGLLGPNGAGKSTTFKMMCGLLVPTSGKALVLGMDLKVSSGKARQhLGYMA 408
Cdd:PRK11607 19 LLEIRNLTKSFDGQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVDLSHVPPYQRP-INMMF 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 409 QKFSLYGNLSVEQNLRFfsgvyGLRGR--AQNEKIARMSDAFGL---KSIARHAADELPLGYKQRLALACSLMHEPDILF 483
Cdd:PRK11607 98 QSYALFPHMTVEQNIAF-----GLKQDklPKAEIASRVNEMLGLvhmQEFAKRKPHQLSGGQRQRVALARSLAKRPKLLL 172
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 488984955 484 LDEPTSGVDPLTRREFWLHINSMVDK-GVTVMVTTHFMDEA-EYCDRIGLVYHGKLIASGTPD 544
Cdd:PRK11607 173 LDEPMGALDKKLRDRMQLEVVDILERvGVTCVMVTHDQEEAmTMAGRIAIMNRGKFVQIGEPE 235
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
29-224 |
2.10e-29 |
|
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: 119.45 E-value: 2.10e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 29 TIRAGYVTGLVGPDGAGKTTLMRMLAGLLKPDEGRASVIG---FDPLK--DDSALHAVLGYMPQKFGLYEDLTVMENLtL 103
Cdd:TIGR02142 19 TLPGQGVTAIFGRSGSGKTTLIRLIAGLTRPDEGEIVLNGrtlFDSRKgiFLPPEKRRIGYVFQEARLFPHLSVRGNL-R 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 104 YAdLRSVTGEARKKIFDRLLEFTSLGPFTERLAGKLSGGMKQKLGLACTLVGDPKVLLLDEPGVGVDPISRRELWQMVHE 183
Cdd:TIGR02142 98 YG-MKRARPSERRISFERVIELLGIGHLLGRLPGRLSGGEKQRVAIGRALLSSPRLLLMDEPLAALDDPRKYEILPYLER 176
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 488984955 184 LAGD-GMLILWSTSYLDEAEQCRD-VLLMNEGKLLYQGEPTAL 224
Cdd:TIGR02142 177 LHAEfGIPILYVSHSLQEVLRLADrVVVLEDGRVAAAGPIAEV 219
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
1-165 |
2.52e-29 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 119.05 E-value: 2.52e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 1 MSETVIALNGLSRRFPgmDRPAVAPLTCTIRAGYVTGLVGPDGAGKTTLMRMLAGLLKPDEGRASVigfdplkDDSALHA 80
Cdd:COG3842 1 MAMPALELENVSKRYG--DVTALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRILL-------DGRDVTG 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 81 V------LGYMPQKFGLYEDLTVMENLTLYADLRSVTGEARKKIFDRLLEFTSLGPFTERLAGKLSGGMKQKLGLACTLV 154
Cdd:COG3842 72 LppekrnVGMVFQDYALFPHLTVAENVAFGLRMRGVPKAEIRARVAELLELVGLEGLADRYPHQLSGGQQQRVALARALA 151
|
170
....*....|.
gi 488984955 155 GDPKVLLLDEP 165
Cdd:COG3842 152 PEPRVLLLDEP 162
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
346-538 |
2.95e-29 |
|
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: 114.66 E-value: 2.95e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 346 DHVDFQVKRGEIFGLLGPNGAGKSTTFKMMCGLLVPTSGKALVLGmdlKVSSGKARQH-LGYMAQ--KFSLYGNlSVEQN 422
Cdd:cd03226 17 DDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLNG---KPIKAKERRKsIGYVMQdvDYQLFTD-SVREE 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 423 LRFFSGVYGlRGRAQNEKIARMSDAFGLKSiaRHAADeLPLGYKQRLALACSLMHEPDILFLDEPTSGVDPLTRREFWLH 502
Cdd:cd03226 93 LLLGLKELD-AGNEQAETVLKDLDLYALKE--RHPLS-LSGGQKQRLAIAAALLSGKDLLIFDEPTSGLDYKNMERVGEL 168
|
170 180 190
....*....|....*....|....*....|....*....
gi 488984955 503 INSMVDKGVTVMVTTH---FMdeAEYCDRIGLVYHGKLI 538
Cdd:cd03226 169 IRELAAQGKAVIVITHdyeFL--AKVCDRVLLLANGAIV 205
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
3-215 |
6.71e-29 |
|
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: 112.91 E-value: 6.71e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 3 ETVIALNGLSRRfpgmdrPAVAPLTCTIRAGYVTGLVGPDGAGKTTLMRMLAGLLKPDEGRASVIGfDPLKDDSALHAV- 81
Cdd:cd03215 2 EPVLEVRGLSVK------GAVRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITLDG-KPVTRRSPRDAIr 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 82 --LGYMP---QKFGLYEDLTVMENLTLyadlrsvtgearkkifdrllefTSLgpfterlagkLSGGMKQKLGLACTLVGD 156
Cdd:cd03215 75 agIAYVPedrKREGLVLDLSVAENIAL----------------------SSL----------LSGGNQQKVVLARWLARD 122
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 157 PKVLLLDEPGVGVDPISRRELWQMVHELAGDGMLILWSTSYLDEAEQCRD-VLLMNEGKL 215
Cdd:cd03215 123 PRVLILDEPTRGVDVGAKAEIYRLIRELADAGKAVLLISSELDELLGLCDrILVMYEGRI 182
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
6-224 |
9.22e-29 |
|
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex cysAWTP involved in sulfate import. Responsible for energy coupling to the transport system. The complex is composed of two ATP-binding proteins (cysA), two transmembrane proteins (cysT and cysW), and a solute-binding protein (cysP). ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213263 [Multi-domain] Cd Length: 239 Bit Score: 114.36 E-value: 9.22e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 6 IALNGLSRRFPGMdrPAVAPLTCTIRAGYVTGLVGPDGAGKTTLMRMLAGLLKPDEGRASVIGfdplKDDSALHAV---L 82
Cdd:cd03296 3 IEVRNVSKRFGDF--VALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGG----EDATDVPVQernV 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 83 GYMPQKFGLYEDLTVMENLTLYADLRSVTG-----EARKKIfDRLLEFTSLGPFTERLAGKLSGGMKQKLGLACTLVGDP 157
Cdd:cd03296 77 GFVFQHYALFRHMTVFDNVAFGLRVKPRSErppeaEIRAKV-HELLKLVQLDWLADRYPAQLSGGQRQRVALARALAVEP 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 488984955 158 KVLLLDEPGVGVDPISRRELWQMVHELAGD-GMLILWSTSYLDEAEQCRD-VLLMNEGKLLYQGEPTAL 224
Cdd:cd03296 156 KVLLLDEPFGALDAKVRKELRRWLRRLHDElHVTTVFVTHDQEEALEVADrVVVMNKGRIEQVGTPDEV 224
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
6-219 |
1.12e-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: 113.84 E-value: 1.12e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 6 IALNGLSRRFPGMDRPAVAPLTCTIRAGYVTGLVGPDGAGKTTLMRMLAGLLKPDEGRASVIGFD-PLKDDSALHAVLGY 84
Cdd:cd03245 3 IEFRNVSFSYPNQEIPALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGTDiRQLDPADLRRNIGY 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 85 MPQKFGLYEDlTVMENLTL---YADLRSVTgearkkifdRLLEFTSLGPFT------------ERLAGkLSGGMKQKLGL 149
Cdd:cd03245 83 VPQDVTLFYG-TLRDNITLgapLADDERIL---------RAAELAGVTDFVnkhpngldlqigERGRG-LSGGQRQAVAL 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 488984955 150 ACTLVGDPKVLLLDEPGVGVDPISRRELWQMVHELAGDGMLILWS--TSYLDEAEQcrdVLLMNEGKLLYQG 219
Cdd:cd03245 152 ARALLNDPPILLLDEPTSAMDMNSEERLKERLRQLLGDKTLIIIThrPSLLDLVDR---IIVMDSGRIVADG 220
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
340-549 |
1.17e-28 |
|
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: 120.25 E-value: 1.17e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 340 GDFAATDHVDFQVKRGEIFGLLGPNGAGKSTTFKMMCGLLVPTSGKALVLGMDLKVSSGKA-RQHLGYMAQKFSLYgNLS 418
Cdd:COG4988 348 GGRPALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPPYSGSILINGVDLSDLDPASwRRQIAWVPQNPYLF-AGT 426
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 419 VEQNLRFFsgvyglRGRAQNEKIARMSDAFGLKSIarhaADELPLGY---------------KQRLALACSLMHEPDILF 483
Cdd:COG4988 427 IRENLRLG------RPDASDEELEAALEAAGLDEF----VAALPDGLdtplgeggrglsggqAQRLALARALLRDAPLLL 496
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 488984955 484 LDEPTSGVDPLTRREFWLHINSMVdKGVTVMVTTHFMDEAEYCDRIGLVYHGKLIASGTPDALKAQ 549
Cdd:COG4988 497 LDEPTAHLDAETEAEILQALRRLA-KGRTVILITHRLALLAQADRILVLDDGRIVEQGTHEELLAK 561
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
330-537 |
2.07e-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: 112.73 E-value: 2.07e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 330 IEAQSLTKKFGDFAATDHVDFQVKRGEIFGLLGPNGAGKSTTFKMMCGLLVPTSGKALVLGMDLKVSSGKARQhLGYMAQ 409
Cdd:cd03301 1 VELENVTKRFGNVTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGRDVTDLPPKDRD-IAMVFQ 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 410 KFSLYGNLSVEQNLRFFSGVYGLRGRAQNEKIARMSDAFGLKSIARHAADELPLGYKQRLALACSLMHEPDILFLDEPTS 489
Cdd:cd03301 80 NYALYPHMTVYDNIAFGLKLRKVPKDEIDERVREVAELLQIEHLLDRKPKQLSGGQRQRVALGRAIVREPKVFLMDEPLS 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 488984955 490 GVDPLTRREFWLHINSMVDK-GVTVMVTTHFMDEAE-YCDRIGLVYHGKL 537
Cdd:cd03301 160 NLDAKLRVQMRAELKRLQQRlGTTTIYVTHDQVEAMtMADRIAVMNDGQI 209
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
2-497 |
2.12e-28 |
|
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: 119.27 E-value: 2.12e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 2 SETVIALNGLSRRFPGmDRPAVAPLTCTIRAGYVTGLVGPDGAGKTTLMRMLAGLLKPDEGRASVigfdplkddsALHAV 81
Cdd:TIGR03719 1 AQYIYTMNRVSKVVPP-KKEILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKDFNGEARP----------QPGIK 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 82 LGYMPQKFGLYEDLTVMENL------------------TLYAD-------LRSVTGEARKKI-------FDRLLEFTSLG 129
Cdd:TIGR03719 70 VGYLPQEPQLDPTKTVRENVeegvaeikdaldrfneisAKYAEpdadfdkLAAEQAELQEIIdaadawdLDSQLEIAMDA 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 130 ---PFTERLAGKLSGGMKQKLGLACTLVGDPKVLLLDEPGVGVDPISRRELWQMVHELAGDGMLILWSTSYLDEAEQCrd 206
Cdd:TIGR03719 150 lrcPPWDADVTKLSGGERRRVALCRLLLSKPDMLLLDEPTNHLDAESVAWLERHLQEYPGTVVAVTHDRYFLDNVAGW-- 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 207 VLLMNEGKLL-YQGEPTALTQTMAGRSFLVSSPQENNRRLLQRALKLPQVSDGVIQGKS-VRLilkkdARIEEvqqhgdm 284
Cdd:TIGR03719 228 ILELDRGRGIpWEGNYSSWLEQKQKRLEQEEKEESARQKTLKRELEWVRQSPKGRQAKSkARL-----ARYEE------- 295
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 285 ppLQVADTAPRFEDAFIDLLGGagtaeSPLGAIihrvdgskeetVIEAQSLTKKFGDFAATDHVDFQVKRGEIFGLLGPN 364
Cdd:TIGR03719 296 --LLSQEFQKRNETAEIYIPPG-----PRLGDK-----------VIEAENLTKAFGDKLLIDDLSFKLPPGGIVGVIGPN 357
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 365 GAGKSTTFKMMCGLLVPTSGkALVLGMDLKvssgkarqhLGYMAQ-KFSLYGNLSV----------------EQNLRFFS 427
Cdd:TIGR03719 358 GAGKSTLFRMITGQEQPDSG-TIEIGETVK---------LAYVDQsRDALDPNKTVweeisggldiiklgkrEIPSRAYV 427
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 428 GVYGLRGRAQNEKIARMSDafglksiarhaadelplGYKQRLALACSLMHEPDILFLDEPTSGVDPLTRR 497
Cdd:TIGR03719 428 GRFNFKGSDQQKKVGQLSG-----------------GERNRVHLAKTLKSGGNVLLLDEPTNDLDVETLR 480
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
326-543 |
2.17e-28 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 114.73 E-value: 2.17e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 326 EETVIEAQSLTKKFGDFA--ATDHVDFQVKRGEIFGLLGPNGAGKSTTFKMMCGLLVPTSGKALVLGMDLKVSS-GKARQ 402
Cdd:PRK13635 2 KEEIIRVEHISFRYPDAAtyALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGGMVLSEETvWDVRR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 403 HLGYMAQ----KFSlygNLSVEQNLRFfsgvyGL--RGRAQNEKIARMSDAF---GLKSIARHAADELPLGYKQRLALAC 473
Cdd:PRK13635 82 QVGMVFQnpdnQFV---GATVQDDVAF-----GLenIGVPREEMVERVDQALrqvGMEDFLNREPHRLSGGQKQRVAIAG 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 488984955 474 SLMHEPDILFLDEPTSGVDPLTRREFWLHINSMVD-KGVTVMVTTHFMDEAEYCDRIGLVYHGKLIASGTP 543
Cdd:PRK13635 154 VLALQPDIIILDEATSMLDPRGRREVLETVRQLKEqKGITVLSITHDLDEAAQADRVIVMNKGEILEEGTP 224
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
330-546 |
2.20e-28 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 116.33 E-value: 2.20e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 330 IEAQSLTKKFGDFAATDHVDFQVKRGEIFGLLGPNGAGKSTTFKMMCGLLVPTSGKALVLGMDlkVSSGKARQ-HLGYMA 408
Cdd:COG3839 4 LELENVSKSYGGVEALKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAGLEDPTSGEILIGGRD--VTDLPPKDrNIAMVF 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 409 QKFSLYGNLSVEQNLRFfsgvyGLRGR-----AQNEKIARMSDAFGLKSIARHAADELPLGYKQRLALACSLMHEPDILF 483
Cdd:COG3839 82 QSYALYPHMTVYENIAF-----PLKLRkvpkaEIDRRVREAAELLGLEDLLDRKPKQLSGGQRQRVALGRALVREPKVFL 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 488984955 484 LDEPTSGVDPLTRREFWLHINSMVDK-GVTVMVTTHfmDEAE---YCDRIGLVYHGKLIASGTPDAL 546
Cdd:COG3839 157 LDEPLSNLDAKLRVEMRAEIKRLHRRlGTTTIYVTH--DQVEamtLADRIAVMNDGRIQQVGTPEEL 221
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
327-546 |
2.51e-28 |
|
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: 113.64 E-value: 2.51e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 327 ETVIEAQSLTKKFGDFAATDHVDFQVKRGEIFGLLGPNGAGKSTTFKMMCGLLVPTSGKAL-VLGMDL-KVSSGKARQHL 404
Cdd:COG1119 1 DPLLELRNVTVRRGGKTILDDISWTVKPGEHWAILGPNGAGKSTLLSLITGDLPPTYGNDVrLFGERRgGEDVWELRKRI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 405 GY----MAQKFslYGNLSVEQNLRffSGVYGLRGR------AQNEKIARMSDAFGLKSIARHAADELPLGYKQRLALACS 474
Cdd:COG1119 81 GLvspaLQLRF--PRDETVLDVVL--SGFFDSIGLyreptdEQRERARELLELLGLAHLADRPFGTLSQGEQRRVLIARA 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 488984955 475 LMHEPDILFLDEPTSGVDPLTRREFWLHINSMVDKGVTVMVT-THFMDEAeycdrIGLVYH------GKLIASGTPDAL 546
Cdd:COG1119 157 LVKDPELLILDEPTAGLDLGARELLLALLDKLAAEGAPTLVLvTHHVEEI-----PPGITHvlllkdGRVVAAGPKEEV 230
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
6-226 |
4.33e-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: 119.17 E-value: 4.33e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 6 IALNGLSRRFPGMDRPAVAPLTCTIRAGYVTGLVGPDGAGKTTLMRMLAGLLKPDEGRASVIGFDpLK--DDSALHAVLG 83
Cdd:COG2274 474 IELENVSFRYPGDSPPVLDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEPTSGRILIDGID-LRqiDPASLRRQIG 552
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 84 YMPQKFGLYEDlTVMENLTLYADLRSvtgearkkiFDRL---LEFTSLGPFTERLAGK-----------LSGGMKQKLGL 149
Cdd:COG2274 553 VVLQDVFLFSG-TIRENITLGDPDAT---------DEEIieaARLAGLHDFIEALPMGydtvvgeggsnLSGGQRQRLAI 622
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 488984955 150 ACTLVGDPKVLLLDEPGVGVDPISRRELWQMVHELAGDGMLILWS--TSYLDEAEQcrdVLLMNEGKLLYQGEPTALTQ 226
Cdd:COG2274 623 ARALLRNPRILILDEATSALDAETEAIILENLRRLLKGRTVIIIAhrLSTIRLADR---IIVLDKGRIVEDGTHEELLA 698
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
35-219 |
9.05e-28 |
|
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: 110.85 E-value: 9.05e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 35 VTGLVGPDGAGKTTLMRMLAGLLKPDEGRASVIGfdPLKDDSALHAVL-------GYMPQKFGLYEDLTVMENLTlYAdL 107
Cdd:cd03297 25 VTGIFGASGAGKSTLLRCIAGLEKPDGGTIVLNG--TVLFDSRKKINLppqqrkiGLVFQQYALFPHLNVRENLA-FG-L 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 108 RSVTGEARKKIFDRLLEFTSLGPFTERLAGKLSGGMKQKLGLACTLVGDPKVLLLDEPGVGVDPISRRELWQMVHELAGD 187
Cdd:cd03297 101 KRKRNREDRISVDELLDLLGLDHLLNRYPAQLSGGEKQRVALARALAAQPELLLLDEPFSALDRALRLQLLPELKQIKKN 180
|
170 180 190
....*....|....*....|....*....|....
gi 488984955 188 -GMLILWSTSYLDEAEQ-CRDVLLMNEGKLLYQG 219
Cdd:cd03297 181 lNIPVIFVTHDLSEAEYlADRIVVMEDGRLQYIG 214
|
|
| COG4559 |
COG4559 |
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism]; |
330-564 |
9.58e-28 |
|
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443620 [Multi-domain] Cd Length: 258 Bit Score: 112.13 E-value: 9.58e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 330 IEAQSLTKKFGDFAATDHVDFQVKRGEIFGLLGPNGAGKSTTFKMMCGLLVPTSGKALVLGMDLKVSSGKAR-QHLGYMA 408
Cdd:COG4559 2 LEAENLSVRLGGRTLLDDVSLTLRPGELTAIIGPNGAGKSTLLKLLTGELTPSSGEVRLNGRPLAAWSPWELaRRRAVLP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 409 QKFSLYGNLSVEQNLRFfsGVY-GLRGRAQNEKIAR--MsDAFGLKSIARHAADELPLGYKQRLALA---CSLMHEPD-- 480
Cdd:COG4559 82 QHSSLAFPFTVEEVVAL--GRApHGSSAAQDRQIVReaL-ALVGLAHLAGRSYQTLSGGEQQRVQLArvlAQLWEPVDgg 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 481 --ILFLDEPTSGVDP--------LTRRefwlhinsMVDKGVTVMVTTHfmD---EAEYCDRIGLVYHGKLIASGTP-DAL 546
Cdd:COG4559 159 prWLFLDEPTSALDLahqhavlrLARQ--------LARRGGGVVAVLH--DlnlAAQYADRILLLHQGRLVAQGTPeEVL 228
|
250
....*....|....*...
gi 488984955 547 kaqaaddsqTDPTMEQAF 564
Cdd:COG4559 229 ---------TDELLERVY 237
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
3-550 |
1.06e-27 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 116.64 E-value: 1.06e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 3 ETVIALNGLSRRFPGMDrpAVAPLTCTIRAGYVTGLVGPDGAGKTTLMRMLAGLLKPDEGRASVIG----FDPLKDDSAl 78
Cdd:PRK10762 2 QALLQLKGIDKAFPGVK--ALSGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSILYLGkevtFNGPKSSQE- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 79 hAVLGYMPQKFGLYEDLTVMENLTLYADLRSVTGEAR-KKIF---DRLLEFTSLGPFTERLAGKLSGGMKQKLGLACTLV 154
Cdd:PRK10762 79 -AGIGIIHQELNLIPQLTIAENIFLGREFVNRFGRIDwKKMYaeaDKLLARLNLRFSSDKLVGELSIGEQQMVEIAKVLS 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 155 GDPKVLLLDEPgvgVDPISRRE---LWQMVHELAGDGMLILWSTSYLDEA-EQCRDVLLMNEGKllyqgeptaltqtmag 230
Cdd:PRK10762 158 FESKVIIMDEP---TDALTDTEtesLFRVIRELKSQGRGIVYISHRLKEIfEICDDVTVFRDGQ---------------- 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 231 rsFLVSSPqennrrllqralklpqVSDgviqgksvrliLKKDARIEevqqhgdmppLQVADtapRFEDAFidllggagta 310
Cdd:PRK10762 219 --FIAERE----------------VAD-----------LTEDSLIE----------MMVGR---KLEDQY---------- 246
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 311 esPlgaiihRVDGSKEETVIEAQSLTKkfgdfAATDHVDFQVKRGEIFGLLGPNGAGKSTTFKMMCGLLVPTSGKALVLG 390
Cdd:PRK10762 247 --P------RLDKAPGEVRLKVDNLSG-----PGVNDVSFTLRKGEILGVSGLMGAGRTELMKVLYGALPRTSGYVTLDG 313
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 391 MDLKVSS---GKA---------RQHLGymaqkfsLYGNLSVEQN-----LRFFSGVYG-LRGRAQNEKIARMSDAFGLKS 452
Cdd:PRK10762 314 HEVVTRSpqdGLAngivyisedRKRDG-------LVLGMSVKENmsltaLRYFSRAGGsLKHADEQQAVSDFIRLFNIKT 386
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 453 IARHAA-DELPLGYKQRLALACSLMHEPDILFLDEPTSGVDPLTRREFWLHINSMVDKGVTVMVTTHFMDEA-EYCDRIg 530
Cdd:PRK10762 387 PSMEQAiGLLSGGNQQKVAIARGLMTRPKVLILDEPTRGVDVGAKKEIYQLINQFKAEGLSIILVSSEMPEVlGMSDRI- 465
|
570 580
....*....|....*....|....*.
gi 488984955 531 LVYH-GKL-----IASGTPDALKAQA 550
Cdd:PRK10762 466 LVMHeGRIsgeftREQATQEKLMAAA 491
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
4-224 |
1.12e-27 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 111.52 E-value: 1.12e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 4 TVIALNgLSRRFPGmdRPAVAPLTCTIRAGYVTGLVGPDGAGKTTLMRMLAGLLKPDEGRASV----IGFDPLKDdSALH 79
Cdd:PRK10895 3 TLTAKN-LAKAYKG--RRVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIddedISLLPLHA-RARR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 80 AVlGYMPQKFGLYEDLTVMENLTLYADLRS-VTGEARKKIFDRLLEFTSLGPFTERLAGKLSGGMKQKLGLACTLVGDPK 158
Cdd:PRK10895 79 GI-GYLPQEASIFRRLSVYDNLMAVLQIRDdLSAEQREDRANELMEEFHIEHLRDSMGQSLSGGERRRVEIARALAANPK 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 488984955 159 VLLLDEPGVGVDPISRRELWQMVHELAGDGMLILWSTSYLDEA-EQCRDVLLMNEGKLLYQGEPTAL 224
Cdd:PRK10895 158 FILLDEPFAGVDPISVIDIKRIIEHLRDSGLGVLITDHNVRETlAVCERAYIVSQGHLIAHGTPTEI 224
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
21-221 |
1.63e-27 |
|
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: 111.97 E-value: 1.63e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 21 PAVAPLTCTIRAGYVTGLVGPDGAGKTTLMRMLAGLLKPDEGRASVIGFDPLK-DDSALHAV----LGYMPQKFGLYEDL 95
Cdd:cd03294 38 VGVNDVSLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGKVLIDGQDIAAmSRKELRELrrkkISMVFQSFALLPHR 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 96 TVMENLTLYADLRSVTGEARKKIFDRLLEFTSLGPFTERLAGKLSGGMKQKLGLACTLVGDPKVLLLDEPGVGVDPISRR 175
Cdd:cd03294 118 TVLENVAFGLEVQGVPRAEREERAAEALELVGLEGWEHKYPDELSGGMQQRVGLARALAVDPDILLMDEAFSALDPLIRR 197
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 488984955 176 ELWQMVHELAGD-GMLILWSTSYLDEAEQCRD-VLLMNEGKLLYQGEP 221
Cdd:cd03294 198 EMQDELLRLQAElQKTIVFITHDLDEALRLGDrIAIMKDGRLVQVGTP 245
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
29-536 |
1.81e-27 |
|
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: 116.81 E-value: 1.81e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 29 TIRAGYVTGLVGPDGAGKTTLMRMLAGLLKPDEGRasvIGFDPLKDDsalhaVLgympQKF---GLYEDLTVMENLTL-- 103
Cdd:COG1245 95 VPKKGKVTGILGPNGIGKSTALKILSGELKPNLGD---YDEEPSWDE-----VL----KRFrgtELQDYFKKLANGEIkv 162
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 104 -----YADL--RSVTGEAR--------KKIFDRLLEFTSLGPFTERLAGKLSGGMKQKLGLACTLVGDPKVLLLDEPGVG 168
Cdd:COG1245 163 ahkpqYVDLipKVFKGTVRellekvdeRGKLDELAEKLGLENILDRDISELSGGELQRVAIAAALLRDADFYFFDEPSSY 242
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 169 VDPISRRELWQMVHELAGDG---MLILWSTSYLDeaeqcrdvLLMNEGKLLYqGEPTA---LTQTMAGRS----FLvssp 238
Cdd:COG1245 243 LDIYQRLNVARLIRELAEEGkyvLVVEHDLAILD--------YLADYVHILY-GEPGVygvVSKPKSVRVginqYL---- 309
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 239 qennrrllqralklpqvsDGVIQGKSVRLilkKDARIE-EVqqhgdmpplqvadTAPRfedafidllggagtaesplgai 317
Cdd:COG1245 310 ------------------DGYLPEENVRI---RDEPIEfEV-------------HAPR---------------------- 333
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 318 ihrvDGSKEETVIEAQSLTKKFGDFAATdhVDF-QVKRGEIFGLLGPNGAGKSTTFKMMCGLLVPTSGKalvLGMDLKVS 396
Cdd:COG1245 334 ----REKEEETLVEYPDLTKSYGGFSLE--VEGgEIREGEVLGIVGPNGIGKTTFAKILAGVLKPDEGE---VDEDLKIS 404
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 397 sgkarqhlgYMAQKFSLYGNLSVEQNLRFFSGVyGLRGRAQNEKIARmsdAFGLKSIARHAADELPLGYKQRLALACSLM 476
Cdd:COG1245 405 ---------YKPQYISPDYDGTVEEFLRSANTD-DFGSSYYKTEIIK---PLGLEKLLDKNVKDLSGGELQRVAIAACLS 471
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 488984955 477 HEPDILFLDEPTSGVDPLTRREFWLHINSMVD-KGVTVMVTTH---FMDeaeY-CDRIgLVYHGK 536
Cdd:COG1245 472 RDADLYLLDEPSAHLDVEQRLAVAKAIRRFAEnRGKTAMVVDHdiyLID---YiSDRL-MVFEGE 532
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
7-219 |
2.00e-27 |
|
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: 108.68 E-value: 2.00e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 7 ALNGLSRRFPGmdRPAVAPLTCTIRAGYVTGLVGPDGAGKTTLMRMLAGLLKPDEGRASVIGFDPLKDDSALHA-VLGYM 85
Cdd:cd03214 1 EVENLSVGYGG--RTVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDGKDLASLSPKELArKIAYV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 86 PQkfglyedltvmenltlyadlrsvtgearkkifdrLLEFTSLGPFTERLAGKLSGGMKQKLGLACTLVGDPKVLLLDEP 165
Cdd:cd03214 79 PQ----------------------------------ALELLGLAHLADRPFNELSGGERQRVLLARALAQEPPILLLDEP 124
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 488984955 166 GVGVDPISRRELWQMVHELAGD-GMLILWSTSYLDEAEQ-CRDVLLMNEGKLLYQG 219
Cdd:cd03214 125 TSHLDIAHQIELLELLRRLARErGKTVVMVLHDLNLAARyADRVILLKDGRIVAQG 180
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
27-226 |
2.62e-27 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 110.23 E-value: 2.62e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 27 TCTIRAGYVTGLVGPDGAGKTTLMRMLAGLLKPDEGRASVIGFDplkddsalhaVLGYMP---------QKFGLYEDLTV 97
Cdd:COG3840 19 DLTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILWNGQD----------LTALPPaerpvsmlfQENNLFPHLTV 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 98 MEN--LTLYADLRsVTGEARKKIfDRLLEFTSLGPFTERLAGKLSGGMKQKLGLACTLVGDPKVLLLDEPGVGVDPISRR 175
Cdd:COG3840 89 AQNigLGLRPGLK-LTAEQRAQV-EQALERVGLAGLLDRLPGQLSGGQRQRVALARCLVRKRPILLLDEPFSALDPALRQ 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 488984955 176 ELWQMVHELAGD-GMLILWSTSYLDEAEQ-CRDVLLMNEGKLLYQGEPTALTQ 226
Cdd:COG3840 167 EMLDLVDELCRErGLTVLMVTHDPEDAARiADRVLLVADGRIAADGPTAALLD 219
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
35-224 |
3.72e-27 |
|
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and metabolism]; ABC-type molybdate transport system, ATPase component ModC is part of the Pathway/BioSystem: Molybdopterin biosynthesis
Pssm-ID: 443319 [Multi-domain] Cd Length: 358 Bit Score: 112.89 E-value: 3.72e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 35 VTGLVGPDGAGKTTLMRMLAGLLKPDEGRASVIGfDPLKDDSALHAV------LGYMPQKFGLYEDLTVMENLtLYADLR 108
Cdd:COG4148 27 VTALFGPSGSGKTTLLRAIAGLERPDSGRIRLGG-EVLQDSARGIFLpphrrrIGYVFQEARLFPHLSVRGNL-LYGRKR 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 109 SVTGEARKKiFDRLLEFTSLGPFTERLAGKLSGGMKQKLGLACTLVGDPKVLLLDEPGVGVDPISRRE----LWQMVHEL 184
Cdd:COG4148 105 APRAERRIS-FDEVVELLGIGHLLDRRPATLSGGERQRVAIGRALLSSPRLLLMDEPLAALDLARKAEilpyLERLRDEL 183
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 488984955 185 agdGMLILWSTSYLDEAEQ-CRDVLLMNEGKLLYQGEPTAL 224
Cdd:COG4148 184 ---DIPILYVSHSLDEVARlADHVVLLEQGRVVASGPLAEV 221
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
2-235 |
4.11e-27 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 112.52 E-value: 4.11e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 2 SETVIALNGLSRRFPgmDRPAVAPLTCTIRAGYVTGLVGPDGAGKTTlMRMLAGLLKPDEGRASVIGFDPLKDDSALHAV 81
Cdd:NF000106 10 ARNAVEVRGLVKHFG--EVKAVDGVDLDVREGTVLGVLGP*GAA**R-GALPAHV*GPDAGRRPWRF*TWCANRRALRRT 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 82 LG-YMPQKFGLYEDLTVMENLTLYADLRSVTGEARKKIFDRLLEFTSLGPFTERLAGKLSGGMKQKLGLACTLVGDPKVL 160
Cdd:NF000106 87 IG*HRPVR*GRRESFSGRENLYMIGR*LDLSRKDARARADELLERFSLTEAAGRAAAKYSGGMRRRLDLAASMIGRPAVL 166
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 488984955 161 LLDEPGVGVDPISRRELWQMVHELAGDGMLILWSTSYLDEAEQ-CRDVLLMNEGKLLYQGEPTALTQTMAGRSFLV 235
Cdd:NF000106 167 YLDEPTTGLDPRTRNEVWDEVRSMVRDGATVLLTTQYMEEAEQlAHELTVIDRGRVIADGKVDELKTKVGGRTLQI 242
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
329-549 |
5.29e-27 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 110.66 E-value: 5.29e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 329 VIEAQSLTKKF-GDFAATDHVDFQVKRGEIFGLLGPNGAGKSTTFKMMCGLLVPTSGKALVLGMDL-KVSSGKARQHLGY 406
Cdd:PRK13652 3 LIETRDLCYSYsGSKEALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIRGEPItKENIREVRKFVGL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 407 MAQK-----FSLygnlSVEQNLRFFSGVYGLRGRAQNEKIARMSDAFGLKSIARHAADELPLGYKQRLALACSLMHEPDI 481
Cdd:PRK13652 83 VFQNpddqiFSP----TVEQDIAFGPINLGLDEETVAHRVSSALHMLGLEELRDRVPHHLSGGEKKRVAIAGVIAMEPQV 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 482 LFLDEPTSGVDPLTRREFWLHINSMVDK-GVTVMVTTHFMD-EAEYCDRIGLVYHGKLIASGTPDALKAQ 549
Cdd:PRK13652 159 LVLDEPTAGLDPQGVKELIDFLNDLPETyGMTVIFSTHQLDlVPEMADYIYVMDKGRIVAYGTVEEIFLQ 228
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
26-219 |
5.37e-27 |
|
ATP-binding cassette domain of the thiamine transport system; Part of the binding-protein-dependent transport system tbpA-thiPQ for thiamine and TPP. Probably responsible for the translocation of thiamine across the membrane. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213265 [Multi-domain] Cd Length: 211 Bit Score: 108.73 E-value: 5.37e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 26 LTCTIRAGYVTGLVGPDGAGKTTLMRMLAGLLKPDEGRASVIGFDPLKDDSALHAVlGYMPQKFGLYEDLTVMEN--LTL 103
Cdd:cd03298 17 FDLTFAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLINGVDVTAAPPADRPV-SMLFQENNLFAHLTVEQNvgLGL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 104 YADLRsVTGEARKKIfDRLLEFTSLGPFTERLAGKLSGGMKQKLGLACTLVGDPKVLLLDEPGVGVDPISRRELWQMVHE 183
Cdd:cd03298 96 SPGLK-LTAEDRQAI-EVALARVGLAGLEKRLPGELSGGERQRVALARVLVRDKPVLLLDEPFAALDPALRAEMLDLVLD 173
|
170 180 190
....*....|....*....|....*....|....*...
gi 488984955 184 L-AGDGMLILWSTSYLDEAEQC-RDVLLMNEGKLLYQG 219
Cdd:cd03298 174 LhAETKMTVLMVTHQPEDAKRLaQRVVFLDNGRIAAQG 211
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
327-545 |
5.46e-27 |
|
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase component [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 443338 [Multi-domain] Cd Length: 233 Bit Score: 109.45 E-value: 5.46e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 327 ETVIEAQSLTKKFGDFAAT----DHVDFQVKRGEIFGLLGPNGAGKSTTFKMMCGLLVPTSGKALVLGMDLKVSS--GKA 400
Cdd:COG4181 6 APIIELRGLTKTVGTGAGEltilKGISLEVEAGESVAIVGASGSGKSTLLGLLAGLDRPTSGTVRLAGQDLFALDedARA 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 401 R---QHLGYMAQKFSLYGNLSVEQN----LRffsgvygLRGRAQNEKIAR-MSDAFGLKSIARHAADELPLGYKQRLALA 472
Cdd:COG4181 86 RlraRHVGFVFQSFQLLPTLTALENvmlpLE-------LAGRRDARARARaLLERVGLGHRLDHYPAQLSGGEQQRVALA 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 488984955 473 CSLMHEPDILFLDEPTSGVDPLTRRE-----FWLHinsmVDKGVTVMVTTHFMDEAEYCDRIGLVYHGKLIASGTPDA 545
Cdd:COG4181 159 RAFATEPAILFADEPTGNLDAATGEQiidllFELN----RERGTTLVLVTHDPALAARCDRVLRLRAGRLVEDTAATA 232
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
1-224 |
5.54e-27 |
|
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: 114.62 E-value: 5.54e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 1 MSETVIALNGLSRRFPGM---DRPAVAPLTCTIRAGYVTGLVGPDGAGKTTLMRMLAGLLKPDEGRASVIGFD----PLK 73
Cdd:COG1123 256 AAEPLLEVRNLSKRYPVRgkgGVRAVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRPTSGSILFDGKDltklSRR 335
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 74 DDSALHAVLGYMPQ--------KFGLYEdlTVMENLTLYadlRSVTGEARKKIFDRLLEFTSLGP-FTERLAGKLSGGMK 144
Cdd:COG1123 336 SLRELRRRVQMVFQdpysslnpRMTVGD--IIAEPLRLH---GLLSRAERRERVAELLERVGLPPdLADRYPHELSGGQR 410
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 145 QKLGLACTLVGDPKVLLLDEPGVGVDPISRRELWQMVHELAGD-GMLILWSTSYLDEAEQ-CRDVLLMNEGKLLYQGEPT 222
Cdd:COG1123 411 QRVAIARALALEPKLLILDEPTSALDVSVQAQILNLLRDLQRElGLTYLFISHDLAVVRYiADRVAVMYDGRIVEDGPTE 490
|
..
gi 488984955 223 AL 224
Cdd:COG1123 491 EV 492
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
14-210 |
8.77e-27 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 107.32 E-value: 8.77e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 14 RFPGmdRPAVAPLTCTIRAGYVTGLVGPDGAGKTTLMRMLAGLLKPDEGRASVigfdplkddsALHAVLGYMPQKFGLYE 93
Cdd:NF040873 1 GYGG--RPVLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTVRR----------AGGARVAYVPQRSEVPD 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 94 DL--TVMENLTL-----YADLRSVTGEARKKIfDRLLEFTSLGPFTERLAGKLSGGMKQKLGLACTLVGDPKVLLLDEPG 166
Cdd:NF040873 69 SLplTVRDLVAMgrwarRGLWRRLTRDDRAAV-DDALERVGLADLAGRQLGELSGGQRQRALLAQGLAQEADLLLLDEPT 147
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 488984955 167 VGVDPISRRELWQMVHELAGDGMLILWSTSYLDEAEQCRDVLLM 210
Cdd:NF040873 148 TGLDAESRERIIALLAEEHARGATVVVVTHDLELVRRADPCVLL 191
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
330-549 |
9.43e-27 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 111.75 E-value: 9.43e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 330 IEAQSLTKKFGDFAATDHVDFQVKRGEIFGLLGPNGAGKSTTfKMMCGLLVPTSGKALVLGMDLKVSSGKARQHLG-YMA 408
Cdd:NF000106 14 VEVRGLVKHFGEVKAVDGVDLDVREGTVLGVLGP*GAA**RG-ALPAHV*GPDAGRRPWRF*TWCANRRALRRTIG*HRP 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 409 QKFSLYGNLSVEQNLRFFSGVYGLRGRAQNEKIARMSDAFGLKSIARHAADELPLGYKQRLALACSLMHEPDILFLDEPT 488
Cdd:NF000106 93 VR*GRRESFSGRENLYMIGR*LDLSRKDARARADELLERFSLTEAAGRAAAKYSGGMRRRLDLAASMIGRPAVLYLDEPT 172
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 488984955 489 SGVDPLTRREFWLHINSMVDKGVTVMVTTHFMDEAE-YCDRIGLVYHGKLIASGTPDALKAQ 549
Cdd:NF000106 173 TGLDPRTRNEVWDEVRSMVRDGATVLLTTQYMEEAEqLAHELTVIDRGRVIADGKVDELKTK 234
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
330-564 |
9.63e-27 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 112.63 E-value: 9.63e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 330 IEAQSLTKKFGDFAATDHVDFQVKRGEIFGLLGPNGAGKSTTFKMMCGLLVPTSGKALVLGMDLKVSSGKA-RQHLGYMA 408
Cdd:PRK09536 4 IDVSDLSVEFGDTTVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGDDVEALSARAaSRRVASVP 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 409 QKFSLYGNLSVEQNLRF----FSGVYGLRGRAQNEKIARMSDAFGLKSIARHAADELPLGYKQRLALACSLMHEPDILFL 484
Cdd:PRK09536 84 QDTSLSFEFDVRQVVEMgrtpHRSRFDTWTETDRAAVERAMERTGVAQFADRPVTSLSGGERQRVLLARALAQATPVLLL 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 485 DEPTSGVD--------PLTRRefwlhinsMVDKGVTVMVTTHFMD-EAEYCDRIGLVYHGKLIASGTPdalkaqaaDDSQ 555
Cdd:PRK09536 164 DEPTASLDinhqvrtlELVRR--------LVDDGKTAVAAIHDLDlAARYCDELVLLADGRVRAAGPP--------ADVL 227
|
....*....
gi 488984955 556 TDPTMEQAF 564
Cdd:PRK09536 228 TADTLRAAF 236
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
327-557 |
2.48e-26 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 108.18 E-value: 2.48e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 327 ETVIEAQSLTKKFGDFAATDHVDFQVKRGEIFGLLGPNGAGKSTTFKMMCGLL----VPTSGKALV---------LGMDL 393
Cdd:PRK09984 2 QTIIRVEKLAKTFNQHQALHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGLItgdkSAGSHIELLgrtvqregrLARDI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 394 KvssgKARQHLGYMAQKFSLYGNLSVEQN---------------LRFFSgvyglrgRAQNEKIARMSDAFGLKSIARHAA 458
Cdd:PRK09984 82 R----KSRANTGYIFQQFNLVNRLSVLENvligalgstpfwrtcFSWFT-------REQKQRALQALTRVGMVHFAHQRV 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 459 DELPLGYKQRLALACSLMHEPDILFLDEPTSGVDPLTRR---EFWLHINSmvDKGVTVMVTTHFMDEA-EYCDRIGLVYH 534
Cdd:PRK09984 151 STLSGGQQQRVAIARALMQQAKVILADEPIASLDPESARivmDTLRDINQ--NDGITVVVTLHQVDYAlRYCERIVALRQ 228
|
250 260
....*....|....*....|...
gi 488984955 535 GKLIASGTpdalkAQAADDSQTD 557
Cdd:PRK09984 229 GHVFYDGS-----SQQFDNERFD 246
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
1-185 |
3.87e-26 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 109.78 E-value: 3.87e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 1 MSEtvIALNGLSRRFpGmDRPAVAPLTCTIRAGYVTGLVGPDGAGKTTLMRMLAGLLKPDEGR-----ASVIGFDPLKDD 75
Cdd:COG3839 1 MAS--LELENVSKSY-G-GVEALKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAGLEDPTSGEiliggRDVTDLPPKDRN 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 76 salhavLGYMPQKFGLYEDLTVMENLTLYADLRSVTGEARKKIFDRLLEFTSLGPFTERLAGKLSGGMKQKLGLACTLVG 155
Cdd:COG3839 77 ------IAMVFQSYALYPHMTVYENIAFPLKLRKVPKAEIDRRVREAAELLGLEDLLDRKPKQLSGGQRQRVALGRALVR 150
|
170 180 190
....*....|....*....|....*....|
gi 488984955 156 DPKVLLLDEPGVGVDPISRrelWQMVHELA 185
Cdd:COG3839 151 EPKVFLLDEPLSNLDAKLR---VEMRAEIK 177
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
6-224 |
4.29e-26 |
|
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: 106.50 E-value: 4.29e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 6 IALNGLSRRFPgmDRPAVAPLTCTIRAGYVTGLVGPDGAGKTTLMRMLAGLLK-----PDEGRASVIG---FDPLKDDSA 77
Cdd:cd03260 1 IELRDLNVYYG--DKHALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRLNDlipgaPDEGEVLLDGkdiYDLDVDVLE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 78 LHAVLGYMPQKFGLYeDLTVMENLTLYADLRsvtGEARKKIFDRLLE--FTSLGPFTE---RL-AGKLSGGMKQKLGLAC 151
Cdd:cd03260 79 LRRRVGMVFQKPNPF-PGSIYDNVAYGLRLH---GIKLKEELDERVEeaLRKAALWDEvkdRLhALGLSGGQQQRLCLAR 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 488984955 152 TLVGDPKVLLLDEPGVGVDPISRRELWQMVHELAGDgMLILWSTSYLDEAEQCRD-VLLMNEGKLLYQGEPTAL 224
Cdd:cd03260 155 ALANEPEVLLLDEPTSALDPISTAKIEELIAELKKE-YTIVIVTHNMQQAARVADrTAFLLNGRLVEFGPTEQI 227
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
344-543 |
4.48e-26 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 108.21 E-value: 4.48e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 344 ATDHVDFQVKRGEIFGLLGPNGAGKSTTFKMMCGLLVPTSGKALVLGMDL---KVSSGKARQHLGYMAQ--KFSLYGNlS 418
Cdd:PRK13637 22 ALDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDGVDItdkKVKLSDIRKKVGLVFQypEYQLFEE-T 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 419 VEQNLRFFSGVYGLRGRAQNEKIARMSDAFGLK--SIARHAADELPLGYKQRLALACSLMHEPDILFLDEPTSGVDPLTR 496
Cdd:PRK13637 101 IEKDIAFGPINLGLSEEEIENRVKRAMNIVGLDyeDYKDKSPFELSGGQKRRVAIAGVVAMEPKILILDEPTAGLDPKGR 180
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 488984955 497 REFWLHINSMVDK-GVTVMVTTHFM-DEAEYCDRIGLVYHGKLIASGTP 543
Cdd:PRK13637 181 DEILNKIKELHKEyNMTIILVSHSMeDVAKLADRIIVMNKGKCELQGTP 229
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
335-552 |
8.28e-26 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 105.99 E-value: 8.28e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 335 LTKKFGDFAAtdHVDFQVKRGEIFGLLGPNGAGKSTTFKMMCGLLVPTSGKALVLGMDL--------KVSSgkarqhlgy 406
Cdd:COG3840 7 LTYRYGDFPL--RFDLTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILWNGQDLtalppaerPVSM--------- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 407 MAQKFSLYGNLSVEQNLRFfsgvyGLR-----GRAQNEKIARMSDAFGLKSIARHAADELPLGYKQRLALA-CSLMHEPd 480
Cdd:COG3840 76 LFQENNLFPHLTVAQNIGL-----GLRpglklTAEQRAQVEQALERVGLAGLLDRLPGQLSGGQRQRVALArCLVRKRP- 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 488984955 481 ILFLDEPTSGVDPLTRREFWLHINSMVDK-GVTVMVTTHFMDEAE-YCDRIGLVYHGKLIASGTPDALKAQAAD 552
Cdd:COG3840 150 ILLLDEPFSALDPALRQEMLDLVDELCRErGLTVLMVTHDPEDAArIADRVLLVADGRIAADGPTAALLDGEPP 223
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
346-549 |
1.24e-25 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 111.02 E-value: 1.24e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 346 DHVDFQVKRGEIFGLLGPNGAGKSTTFKMMCGLLVPTSGKALVLGMDLK-VSSGKARQHLGYMAQKFSLYgNLSVEQNLR 424
Cdd:COG1132 357 KDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYDPTSGRILIDGVDIRdLTLESLRRQIGVVPQDTFLF-SGTIRENIR 435
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 425 FFsgvyglRGRAQNEKIARmsdafglksIARHA-ADE----LPLGY---------------KQRLALACSLMHEPDILFL 484
Cdd:COG1132 436 YG------RPDATDEEVEE---------AAKAAqAHEfieaLPDGYdtvvgergvnlsggqRQRIAIARALLKDPPILIL 500
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 488984955 485 DEPTSGVDPLTRREFWLHINSMVdKGVTVMVTTHFMDEAEYCDRIGLVYHGKLIASGTPDALKAQ 549
Cdd:COG1132 501 DEATSALDTETEALIQEALERLM-KGRTTIVIAHRLSTIRNADRILVLDDGRIVEQGTHEELLAR 564
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
20-195 |
1.57e-25 |
|
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: 103.98 E-value: 1.57e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 20 RPAVAPLTCTIRAGYVTGLVGPDGAGKTTLMRMLAGLLKPDEGRASVIGFDPLKDDSALHAVLGYMPQKFGLYEDLTVME 99
Cdd:TIGR01189 13 RMLFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRWNGTPLAEQRDEPHENILYLGHLPGLKPELSALE 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 100 NLTLYADLrsvTGEARKKIFDrLLEFTSLGPFTERLAGKLSGGMKQKLGLACTLVGDPKVLLLDEPGVGVDPISRRELWQ 179
Cdd:TIGR01189 93 NLHFWAAI---HGGAQRTIED-ALAAVGLTGFEDLPAAQLSAGQQRRLALARLWLSRRPLWILDEPTTALDKAGVALLAG 168
|
170
....*....|....*.
gi 488984955 180 MVHELAGDGMLILWST 195
Cdd:TIGR01189 169 LLRAHLARGGIVLLTT 184
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
344-544 |
1.62e-25 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 106.23 E-value: 1.62e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 344 ATDHVDFQVKRGEIFGLLGPNGAGKSTTFKMMCGLLVPTSGKALVLGMDLKVSS-GKARQHLGYMAQ----KFSlygNLS 418
Cdd:PRK13632 24 ALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIDGITISKENlKEIRKKIGIIFQnpdnQFI---GAT 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 419 VEQNLRFfsgvyGLRGRAQN-----EKIARMSDAFGLKSIARHAADELPLGYKQRLALACSLMHEPDILFLDEPTSGVDP 493
Cdd:PRK13632 101 VEDDIAF-----GLENKKVPpkkmkDIIDDLAKKVGMEDYLDKEPQNLSGGQKQRVAIASVLALNPEIIIFDESTSMLDP 175
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 488984955 494 LTRREFWLHINSMVDKGV-TVMVTTHFMDEAEYCDRIGLVYHGKLIASGTPD 544
Cdd:PRK13632 176 KGKREIKKIMVDLRKTRKkTLISITHDMDEAILADKVIVFSEGKLIAQGKPK 227
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
6-221 |
2.99e-25 |
|
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: 104.24 E-value: 2.99e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 6 IALNGLSRRFPGmdRPAVAPLTCTIRAGYVTGLVGPDGAGKTTLMRMLAGLLKPDEGRAsvigfdpLKDDSALHAV---- 81
Cdd:cd03300 1 IELENVSKFYGG--FVALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEI-------LLDGKDITNLpphk 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 82 --LGYMPQKFGLYEDLTVMENLTLYADLRSVTGEARKKIFDRLLEFTSLGPFTERLAGKLSGGMKQKLGLACTLVGDPKV 159
Cdd:cd03300 72 rpVNTVFQNYALFPHLTVFENIAFGLRLKKLPKAEIKERVAEALDLVQLEGYANRKPSQLSGGQQQRVAIARALVNEPKV 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 488984955 160 LLLDEPGVGVDPISRR----ELWQMVHELagdGMLILWSTSYLDEAEQCRD-VLLMNEGKLLYQGEP 221
Cdd:cd03300 152 LLLDEPLGALDLKLRKdmqlELKRLQKEL---GITFVFVTHDQEEALTMSDrIAVMNKGKIQQIGTP 215
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
347-541 |
3.27e-25 |
|
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: 103.73 E-value: 3.27e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 347 HVDFQVKRGEIFGLLGPNGAGKSTTFKMMCGLLVPTSGKALVLGMDLkVSSGKARQHLGYMAQKFSLYGNLSVEQNLRfF 426
Cdd:cd03298 16 HFDLTFAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLINGVDV-TAAPPADRPVSMLFQENNLFAHLTVEQNVG-L 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 427 SGVYGLRGRA-QNEKIARMSDAFGLKSIARHAADELPLGYKQRLALACSLMHEPDILFLDEPTSGVDPLTRREFW-LHIN 504
Cdd:cd03298 94 GLSPGLKLTAeDRQAIEVALARVGLAGLEKRLPGELSGGERQRVALARVLVRDKPVLLLDEPFAALDPALRAEMLdLVLD 173
|
170 180 190
....*....|....*....|....*....|....*...
gi 488984955 505 SMVDKGVTV-MVTTHFMDEAEYCDRIGLVYHGKLIASG 541
Cdd:cd03298 174 LHAETKMTVlMVTHQPEDAKRLAQRVVFLDNGRIAAQG 211
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
8-196 |
5.47e-25 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 104.17 E-value: 5.47e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 8 LNGLSRRFPGM--DRPAVAPLTCTIRAGYVTGLVGPDGAGKTTLMRMLAGLLKPDEGRASVIGfDPLKDDSALHAVLGym 85
Cdd:COG4525 6 VRHVSVRYPGGgqPQPALQDVSLTIESGEFVVALGASGCGKTTLLNLIAGFLAPSSGEITLDG-VPVTGPGADRGVVF-- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 86 pQKFGLYEDLTVMENLTLYADLRSVTGEARKKIFDRLLEFTSLGPFTERLAGKLSGGMKQKLGLACTLVGDPKVLLLDEP 165
Cdd:COG4525 83 -QKDALLPWLNVLDNVAFGLRLRGVPKAERRARAEELLALVGLADFARRRIWQLSGGMRQRVGIARALAADPRFLLMDEP 161
|
170 180 190
....*....|....*....|....*....|.
gi 488984955 166 GVGVDPISRRelwQMvHELagdgMLILWSTS 196
Cdd:COG4525 162 FGALDALTRE---QM-QEL----LLDVWQRT 184
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
330-544 |
9.31e-25 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 105.94 E-value: 9.31e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 330 IEAQSLTKKFGDFAATDHVDFQVKRGEIFGLLGPNGAGKSTTFKMMCGLLVPTSGKALVLGMDlkVSSGKAR-QHLGYMA 408
Cdd:PRK10851 3 IEIANIKKSFGRTQVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFHGTD--VSRLHARdRKVGFVF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 409 QKFSLYGNLSVEQNLRFFSGVYGLRGR----AQNEKIARMSDAFGLKSIARHAADELPLGYKQRLALACSLMHEPDILFL 484
Cdd:PRK10851 81 QHYALFRHMTVFDNIAFGLTVLPRRERpnaaAIKAKVTQLLEMVQLAHLADRYPAQLSGGQKQRVALARALAVEPQILLL 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 488984955 485 DEPTSGVDPLTRREF--WLHINSMVDKGVTVMVtTHFMDEA-EYCDRIGLVYHGKLIASGTPD 544
Cdd:PRK10851 161 DEPFGALDAQVRKELrrWLRQLHEELKFTSVFV-THDQEEAmEVADRVVVMSQGNIEQAGTPD 222
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
6-219 |
1.17e-24 |
|
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: 100.85 E-value: 1.17e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 6 IALNGLSRRFPGMDRPAVAPLTCTIRAGYVTGLVGPDGAGKTTLMRMLAGLLKPDEGRASVIGFDPLKDDSALHAVLGYM 85
Cdd:cd03247 1 LSINNVSFSYPEQEQQVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDGVPVSDLEKALSSLISVL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 86 PQKFGLYeDLTVMENLTLyadlrsvtgearkkifdrlleftslgpfterlagKLSGGMKQKLGLACTLVGDPKVLLLDEP 165
Cdd:cd03247 81 NQRPYLF-DTTLRNNLGR----------------------------------RFSGGERQRLALARILLQDAPIVLLDEP 125
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 488984955 166 GVGVDPISRRELWQMVHELAGDGMLIlWSTSYLDEAEQCRDVLLMNEGKLLYQG 219
Cdd:cd03247 126 TVGLDPITERQLLSLIFEVLKDKTLI-WITHHLTGIEHMDKILFLENGKIIMQG 178
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
1-221 |
1.24e-24 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 105.55 E-value: 1.24e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 1 MSetvIALNGLSRRFpgmDRPAV-APLTCTIRAGYVTGLVGPDGAGKTTLMRMLAGLLKPDEGRASVIGfdplKDDSALH 79
Cdd:PRK10851 1 MS---IEIANIKKSF---GRTQVlNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFHG----TDVSRLH 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 80 AV---LGYMPQKFGLYEDLTVMEN----LTLYADLRSVTGEARKKIFDRLLEFTSLGPFTERLAGKLSGGMKQKLGLACT 152
Cdd:PRK10851 71 ARdrkVGFVFQHYALFRHMTVFDNiafgLTVLPRRERPNAAAIKAKVTQLLEMVQLAHLADRYPAQLSGGQKQRVALARA 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 488984955 153 LVGDPKVLLLDEPGVGVDPISRREL--W--QMVHELAGDGMLIlwsTSYLDEAEQCRD-VLLMNEGKLLYQGEP 221
Cdd:PRK10851 151 LAVEPQILLLDEPFGALDAQVRKELrrWlrQLHEELKFTSVFV---THDQEEAMEVADrVVVMSQGNIEQAGTP 221
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
330-551 |
1.25e-24 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 105.57 E-value: 1.25e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 330 IEAQSLTKKFGDFAATDHVDFQVKRGEIFGLLGPNGAGKSTTFKMMCGLLVPTSGKALVLGMDLKVSSGKARQhLGYMAQ 409
Cdd:PRK11432 7 VVLKNITKRFGSNTVIDNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIFIDGEDVTHRSIQQRD-ICMVFQ 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 410 KFSLYGNLSVEQNLRffsgvYGLR--GRAQNEKIARMSDAFGLKSIA----RHaADELPLGYKQRLALACSLMHEPDILF 483
Cdd:PRK11432 86 SYALFPHMSLGENVG-----YGLKmlGVPKEERKQRVKEALELVDLAgfedRY-VDQISGGQQQRVALARALILKPKVLL 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 488984955 484 LDEPTSGVDPLTRRefwlhinSMVDK--------GVTVMVTTHFMDEA-EYCDRIGLVYHGKLIASGTPDALKAQAA 551
Cdd:PRK11432 160 FDEPLSNLDANLRR-------SMREKirelqqqfNITSLYVTHDQSEAfAVSDTVIVMNKGKIMQIGSPQELYRQPA 229
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
310-553 |
1.64e-24 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 105.89 E-value: 1.64e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 310 AESPLGAIIHRVDGSKEETVIEAQSLTKKFGDfaatdhVDFQVKRGEIFGLLGPNGAGKSTTFKMMCGLLVPTSGKALVL 389
Cdd:PRK10070 15 GEHPQRAFKYIEQGLSKEQILEKTGLSLGVKD------ASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLID 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 390 GMDL-KVSSGKARQ----HLGYMAQKFSLYGNLSVEQNLRFFSGVYGLRGRAQNEKIARMSDAFGLKSIARHAADELPLG 464
Cdd:PRK10070 89 GVDIaKISDAELREvrrkKIAMVFQSFALMPHMTVLDNTAFGMELAGINAEERREKALDALRQVGLENYAHSYPDELSGG 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 465 YKQRLALACSLMHEPDILFLDEPTSGVDPLTRREFWLHINSMVDKGV-TVMVTTHFMDEA-EYCDRIGLVYHGKLIASGT 542
Cdd:PRK10070 169 MRQRVGLARALAINPDILLMDEAFSALDPLIRTEMQDELVKLQAKHQrTIVFISHDLDEAmRIGDRIAIMQNGEVVQVGT 248
|
250
....*....|.
gi 488984955 543 PDALKAQAADD 553
Cdd:PRK10070 249 PDEILNNPAND 259
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
29-215 |
1.75e-24 |
|
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: 101.18 E-value: 1.75e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 29 TIRAGYVTGLVGPDGAGKTTLMRMLAGLLKPDEGRASVIGfDPLKDDSALHAVlGYMPQ--KFGLYEDlTVMENLTLYAD 106
Cdd:cd03226 22 DLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLNG-KPIKAKERRKSI-GYVMQdvDYQLFTD-SVREELLLGLK 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 107 LRSVTGEARKKIFDRLleftSLGPFTERLAGKLSGGMKQKLGLACTLVGDPKVLLLDEPGVGVDPISRRELWQMVHELAG 186
Cdd:cd03226 99 ELDAGNEQAETVLKDL----DLYALKERHPLSLSGGQKQRLAIAAALLSGKDLLIFDEPTSGLDYKNMERVGELIRELAA 174
|
170 180 190
....*....|....*....|....*....|
gi 488984955 187 DGMLILWSTSYLDEAEQCRD-VLLMNEGKL 215
Cdd:cd03226 175 QGKAVIVITHDYEFLAKVCDrVLLLANGAI 204
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
327-541 |
1.90e-24 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 107.18 E-value: 1.90e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 327 ETVIEAQSLTKKFGDFAATDHVDFQVKRGEIFGLLGPNGAGKSTTFKMMCGLLVPTSGKALVLG-----MDLKVSsgkAR 401
Cdd:PRK09700 3 TPYISMAGIGKSFGPVHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNinynkLDHKLA---AQ 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 402 QHLGYMAQKFSLYGNLSVEQNL-------RFFSGVYGLRGRAQNEKIARMSDAFGLKSIARHAADELPLGYKQRLALACS 474
Cdd:PRK09700 80 LGIGIIYQELSVIDELTVLENLyigrhltKKVCGVNIIDWREMRVRAAMMLLRVGLKVDLDEKVANLSISHKQMLEIAKT 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 488984955 475 LMHEPDILFLDEPTSGvdpLTRRE---FWLHINSMVDKGVTVMVTTHFMDE-AEYCDRIGLVYHGKLIASG 541
Cdd:PRK09700 160 LMLDAKVIIMDEPTSS---LTNKEvdyLFLIMNQLRKEGTAIVYISHKLAEiRRICDRYTVMKDGSSVCSG 227
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
1-222 |
2.42e-24 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 102.96 E-value: 2.42e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 1 MSETVIALNGLSRRFPGMDRPAVAPLTCTIRAGYVTGLVGPDGAGKTTLMRMLAGLLKPDEGRASVIGFDPLKDDSAlha 80
Cdd:PRK13640 1 MKDNIVEFKHVSFTYPDSKKPALNDISFSIPRGSWTALIGHNGSGKSTISKLINGLLLPDDNPNSKITVDGITLTAK--- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 81 VLGYMPQKFGL--------YEDLTVMENLTLYADLRSVTGEARKKIFDRLLEFTSLGPFTERLAGKLSGGMKQKLGLACT 152
Cdd:PRK13640 78 TVWDIREKVGIvfqnpdnqFVGATVGDDVAFGLENRAVPRPEMIKIVRDVLADVGMLDYIDSEPANLSGGQKQRVAIAGI 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 488984955 153 LVGDPKVLLLDEPGVGVDPISRRELWQMVHELAGDGMLILWSTSY-LDEAEQCRDVLLMNEGKLLYQGEPT 222
Cdd:PRK13640 158 LAVEPKIIILDESTSMLDPAGKEQILKLIRKLKKKNNLTVISITHdIDEANMADQVLVLDDGKLLAQGSPV 228
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
29-536 |
3.46e-24 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 106.82 E-value: 3.46e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 29 TIRAGYVTGLVGPDGAGKTTLMRMLAGLLKPDEGRASVigfDPLKDD-------SALHAvlgYMPQkfgLYE-DLTVMEN 100
Cdd:PRK13409 95 IPKEGKVTGILGPNGIGKTTAVKILSGELIPNLGDYEE---EPSWDEvlkrfrgTELQN---YFKK---LYNgEIKVVHK 165
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 101 LTlYADL--RSVTGEAR--------KKIFDRLLEFTSLGPFTERLAGKLSGGMKQKLGLACTLVGDPKVLLLDEPgvgvd 170
Cdd:PRK13409 166 PQ-YVDLipKVFKGKVRellkkvdeRGKLDEVVERLGLENILDRDISELSGGELQRVAIAAALLRDADFYFFDEP----- 239
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 171 pisrrelwqmvhelagdgmlilwsTSYLDEAEQcrdvllMNEGKLLyqgeptaltQTMA-GRSFLVSspqENNRRLLQra 249
Cdd:PRK13409 240 ------------------------TSYLDIRQR------LNVARLI---------RELAeGKYVLVV---EHDLAVLD-- 275
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 250 lklpQVSD------------GVI-QGKSVRL-I---LKKDARIEEVQqhgdmpplqVADTAPRFEdafidllggagtaES 312
Cdd:PRK13409 276 ----YLADnvhiaygepgayGVVsKPKGVRVgIneyLKGYLPEENMR---------IRPEPIEFE-------------ER 329
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 313 PlgaiiHRVDgSKEETVIEAQSLTKKFGDFAATdhVDF-QVKRGEIFGLLGPNGAGKSTTFKMMCGLLVPTSGKALVlgm 391
Cdd:PRK13409 330 P-----PRDE-SERETLVEYPDLTKKLGDFSLE--VEGgEIYEGEVIGIVGPNGIGKTTFAKLLAGVLKPDEGEVDP--- 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 392 DLKVSsgkarqhlgYMAQKFSLYGNLSVEQNLRFFSGVYGlrGRAQNEKIARmsdAFGLKSIARHAADELPLGYKQRLAL 471
Cdd:PRK13409 399 ELKIS---------YKPQYIKPDYDGTVEDLLRSITDDLG--SSYYKSEIIK---PLQLERLLDKNVKDLSGGELQRVAI 464
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 472 ACSLMHEPDILFLDEPTSGVDPLTRREFWLHINSMVD-KGVTVMVTTH---FMDeaeY-CDRIgLVYHGK 536
Cdd:PRK13409 465 AACLSRDADLYLLDEPSAHLDVEQRLAVAKAIRRIAEeREATALVVDHdiyMID---YiSDRL-MVFEGE 530
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
346-535 |
4.00e-24 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 100.94 E-value: 4.00e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 346 DHVDFQVKRGEIFGLLGPNGAGKSTTFKMMCGLLVPTSGKALVLGMDLKVSSGKA-RQHLGYMAQKFSLYGNlSVEQNLR 424
Cdd:PRK10247 24 NNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFEGEDISTLKPEIyRQQVSYCAQTPTLFGD-TVYDNLI 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 425 FfsgVYGLRGRA-QNEKIARMSDAFGL-KSIARHAADELPLGYKQRLALACSLMHEPDILFLDEPTSGVDPLTRRefwlH 502
Cdd:PRK10247 103 F---PWQIRNQQpDPAIFLDDLERFALpDTILTKNIAELSGGEKQRISLIRNLQFMPKVLLLDEITSALDESNKH----N 175
|
170 180 190
....*....|....*....|....*....|....*....
gi 488984955 503 INSMV-----DKGVTVMVTTHFMDEAEYCDR-IGLVYHG 535
Cdd:PRK10247 176 VNEIIhryvrEQNIAVLWVTHDKDEINHADKvITLQPHA 214
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
343-541 |
4.14e-24 |
|
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic bacteriocins of lactic acid bacteria are produced as precursors which have N-terminal leader peptides that share similarities in amino acid sequence and contain a conserved processing site of two glycine residues in positions -1 and -2. A dedicated ATP-binding cassette (ABC) transporter is responsible for the proteolytic cleavage of the leader peptides and subsequent translocation of the bacteriocins across the cytoplasmic membrane.
Pssm-ID: 213212 [Multi-domain] Cd Length: 220 Bit Score: 100.74 E-value: 4.14e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 343 AATDHVDFQVKRGEIFGLLGPNGAGKSTTFKMMCGLLVPTSGKALVLGMDLK-VSSGKARQHLGYMAQKFSL-YGnlSVE 420
Cdd:cd03245 18 PALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGTDIRqLDPADLRRNIGYVPQDVTLfYG--TLR 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 421 QNLRFFSGVyglrgrAQNEKIARMSDAFGLKS-IARHAA----------DELPLGYKQRLALACSLMHEPDILFLDEPTS 489
Cdd:cd03245 96 DNITLGAPL------ADDERILRAAELAGVTDfVNKHPNgldlqigergRGLSGGQRQAVALARALLNDPPILLLDEPTS 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 488984955 490 GVDPLTRREFWLHINSMVdKGVTVMVTTHFMDEAEYCDRIGLVYHGKLIASG 541
Cdd:cd03245 170 AMDMNSEERLKERLRQLL-GDKTLIIITHRPSLLDLVDRIIVMDSGRIVADG 220
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
330-542 |
4.24e-24 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 101.24 E-value: 4.24e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 330 IEAQSLTKKFGDFAATDHVDFQVKRGEIFGLLGPNGAGKSTTFKMMCGLLVPTSGKALVLGMDL----KVSSGKA---RQ 402
Cdd:COG4161 3 IQLKNINCFYGSHQALFDINLECPSGETLVLLGPSGAGKSSLLRVLNLLETPDSGQLNIAGHQFdfsqKPSEKAIrllRQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 403 HLGYMAQKFSLYGNLSVEQNL-----RffsgVYGLRGRAQNEKIARMSDAFGLKSIarhaADELPL----GYKQRLALAC 473
Cdd:COG4161 83 KVGMVFQQYNLWPHLTVMENLieapcK----VLGLSKEQAREKAMKLLARLRLTDK----ADRFPLhlsgGQQQRVAIAR 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 488984955 474 SLMHEPDILFLDEPTSGVDPLTRREFWLHINSMVDKGVTVMVTTHfmdEAEYCDRIG--LVY--HGKLIASGT 542
Cdd:COG4161 155 ALMMEPQVLLFDEPTAALDPEITAQVVEIIRELSQTGITQVIVTH---EVEFARKVAsqVVYmeKGRIIEQGD 224
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
327-537 |
4.43e-24 |
|
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: 99.43 E-value: 4.43e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 327 ETVIEAQSLTKKfgdfAATDHVDFQVKRGEIFGLLGPNGAGKSTTFKMMCGLLVPTSGKALVLGMDLKVSS-GKARQH-L 404
Cdd:cd03215 2 EPVLEVRGLSVK----GAVRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITLDGKPVTRRSpRDAIRAgI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 405 GYMA---QKFSLYGNLSVEQNL---RFFSGvyglrgraqnekiarmsdafglksiarhaadelplGYKQRLALACSLMHE 478
Cdd:cd03215 78 AYVPedrKREGLVLDLSVAENIalsSLLSG-----------------------------------GNQQKVVLARWLARD 122
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 479 PDILFLDEPTSGVDPLTRREFWLHINSMVDKGVTVMVTTHFMDEA-EYCDRIGLVYHGKL 537
Cdd:cd03215 123 PRVLILDEPTRGVDVGAKAEIYRLIRELADAGKAVLLISSELDELlGLCDRILVMYEGRI 182
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
6-192 |
9.86e-24 |
|
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: 105.06 E-value: 9.86e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 6 IALNGLSRRFPGmDRPAVAPLTCTIRAGYVTGLVGPDGAGKTTLMRMLAGLLKPDEGRASVIGFD-PLKDDSALHAVLGY 84
Cdd:TIGR02857 322 LEFSGVSVAYPG-RRPALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSIAVNGVPlADADADSWRDQIAW 400
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 85 MPQKFGLYEDlTVMENLTLYAdlRSVTGEARKKIFDR--LLEFTS-LGPFTERLAGK----LSGGMKQKLGLACTLVGDP 157
Cdd:TIGR02857 401 VPQHPFLFAG-TIAENIRLAR--PDASDAEIREALERagLDEFVAaLPQGLDTPIGEggagLSGGQAQRLALARAFLRDA 477
|
170 180 190
....*....|....*....|....*....|....*
gi 488984955 158 KVLLLDEPGVGVDPISRRELWQMVHELAGDGMLIL 192
Cdd:TIGR02857 478 PLLLLDEPTAHLDAETEAEVLEALRALAQGRTVLL 512
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
30-219 |
1.27e-23 |
|
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette superfamily; ABCG transporters are involved in eye pigment (EP) precursor transport, regulation of lipid-trafficking mechanisms, and pleiotropic drug resistance (DR). DR is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. Compared to other members of the ABC transporter subfamilies, the ABCG transporter family is composed of proteins that have an ATP-binding cassette domain at the N-terminus and a TM (transmembrane) domain at the C-terminus.
Pssm-ID: 213180 [Multi-domain] Cd Length: 194 Bit Score: 98.39 E-value: 1.27e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 30 IRAGYVTGLVGPDGAGKTTLMRMLAGLLKP--DEGRASVIGFDplKDDSALHAVLGYMPQKFGLYEDLTVMENLTLYADL 107
Cdd:cd03213 32 AKPGELTAIMGPSGAGKSTLLNALAGRRTGlgVSGEVLINGRP--LDKRSFRKIIGYVPQDDILHPTLTVRETLMFAAKL 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 108 RSvtgearkkifdrlleftslgpfterlagkLSGGMKQKLGLACTLVGDPKVLLLDEPGVGVDPISRRELWQMVHELAGD 187
Cdd:cd03213 110 RG-----------------------------LSGGERKRVSIALELVSNPSLLFLDEPTSGLDSSSALQVMSLLRRLADT 160
|
170 180 190
....*....|....*....|....*....|....*
gi 488984955 188 GMLILWST---SYLDEaEQCRDVLLMNEGKLLYQG 219
Cdd:cd03213 161 GRTIICSIhqpSSEIF-ELFDKLLLLSQGRVIYFG 194
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
326-549 |
1.36e-23 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 101.08 E-value: 1.36e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 326 EETVIEAQSLTKKFGDFA-ATDHVDFQVKRGEIFGLLGPNGAGKSTTFKMMCGLLVPTSGKALVLGMDLKVSSG---KAR 401
Cdd:PRK13636 2 EDYILKVEELNYNYSDGThALKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGKPIDYSRKglmKLR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 402 QHLGYMAQK-----FSlygnLSVEQNLRFFSGVYGLRGRAQNEKIARMSDAFGLKSIARHAADELPLGYKQRLALACSLM 476
Cdd:PRK13636 82 ESVGMVFQDpdnqlFS----ASVYQDVSFGAVNLKLPEDEVRKRVDNALKRTGIEHLKDKPTHCLSFGQKKRVAIAGVLV 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 488984955 477 HEPDILFLDEPTSGVDPLTRREFWLHINSMVDK-GVTVMVTTHFMDE-AEYCDRIGLVYHGKLIASGTPDALKAQ 549
Cdd:PRK13636 158 MEPKVLVLDEPTAGLDPMGVSEIMKLLVEMQKElGLTIIIATHDIDIvPLYCDNVFVMKEGRVILQGNPKEVFAE 232
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
2-221 |
1.50e-23 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 100.45 E-value: 1.50e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 2 SETVIALNGLSRRFPGMDRPAVAPLTCTIRAGYVTGLVGPDGAGKTTLMRMLAGLLKPDEGRASVIGFDPLKDDsalhav 81
Cdd:PRK13632 4 KSVMIKVENVSFSYPNSENNALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIDGITISKEN------ 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 82 LGYMPQKFGLyedltVMEN-------LTLYADL------RSVTGEARKKIFDRLLEFTSLGPFTERLAGKLSGGMKQKLG 148
Cdd:PRK13632 78 LKEIRKKIGI-----IFQNpdnqfigATVEDDIafglenKKVPPKKMKDIIDDLAKKVGMEDYLDKEPQNLSGGQKQRVA 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 488984955 149 LACTLVGDPKVLLLDEPGVGVDPISRRELWQMVHELAGDGMLILWS-TSYLDEAEQCRDVLLMNEGKLLYQGEP 221
Cdd:PRK13632 153 IASVLALNPEIIIFDESTSMLDPKGKREIKKIMVDLRKTRKKTLISiTHDMDEAILADKVIVFSEGKLIAQGKP 226
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
29-215 |
1.53e-23 |
|
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: 98.76 E-value: 1.53e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 29 TIRAGYVTGLVGPDGAGKTTLMRMLAGLLKPDEGRASVIGFDPLKDDSALHAV---LGYMPQKFGLYEDLTVMENLTLya 105
Cdd:cd03262 22 TVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIDGLKLTDDKKNINELrqkVGMVFQQFNLFPHLTVLENITL-- 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 106 DLRSVTGEARK---KIFDRLLEFTSLGPFTERLAGKLSGGMKQKLGLACTLVGDPKVLLLDEPGVGVDPISRRELWQMVH 182
Cdd:cd03262 100 APIKVKGMSKAeaeERALELLEKVGLADKADAYPAQLSGGQQQRVAIARALAMNPKVMLFDEPTSALDPELVGEVLDVMK 179
|
170 180 190
....*....|....*....|....*....|....
gi 488984955 183 ELAGDGMLILWSTSYLDEAEQCRD-VLLMNEGKL 215
Cdd:cd03262 180 DLAEEGMTMVVVTHEMGFAREVADrVIFMDDGRI 213
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
1-221 |
1.60e-23 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 100.47 E-value: 1.60e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 1 MSETVIALNGLSRRFPGMDRPAVAPLTCTIRAGYVTGLVGPDGAGKTTLMRMLAGLLKPDEGRASVIGFdPLKDDSA--L 78
Cdd:PRK13635 1 MKEEIIRVEHISFRYPDAATYALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGGM-VLSEETVwdV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 79 HAVLGYMPQK---------------FGLyedltvmENltlyadlrsvTGEARKKIFDRL---LEFTSLGPFTERLAGKLS 140
Cdd:PRK13635 80 RRQVGMVFQNpdnqfvgatvqddvaFGL-------EN----------IGVPREEMVERVdqaLRQVGMEDFLNREPHRLS 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 141 GGMKQKLGLACTLVGDPKVLLLDEPGVGVDPISRRELWQMVHELAGDGMLILWS-TSYLDEAEQCRDVLLMNEGKLLYQG 219
Cdd:PRK13635 143 GGQKQRVAIAGVLALQPDIIILDEATSMLDPRGRREVLETVRQLKEQKGITVLSiTHDLDEAAQADRVIVMNKGEILEEG 222
|
..
gi 488984955 220 EP 221
Cdd:PRK13635 223 TP 224
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
3-224 |
2.65e-23 |
|
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: 99.00 E-value: 2.65e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 3 ETVIALNGLSRRFPGmdRPAVAPLTCTIRAGYVTGLVGPDGAGKTTLMRMLAGLLKPDE-----------GRASV----- 66
Cdd:COG1119 1 DPLLELRNVTVRRGG--KTILDDISWTVKPGEHWAILGPNGAGKSTLLSLITGDLPPTYgndvrlfgerrGGEDVwelrk 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 67 -IGF-------DPLKDDSALHAVLGympqkfGLYEdltvmeNLTLYadlRSVTGEARKKIfDRLLEFTSLGPFTERLAGK 138
Cdd:COG1119 79 rIGLvspalqlRFPRDETVLDVVLS------GFFD------SIGLY---REPTDEQRERA-RELLELLGLAHLADRPFGT 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 139 LSGGMKQKLGLACTLVGDPKVLLLDEPGVGVDPISRRELWQMVHELAGDGML-ILWSTSYLDEAEQC-RDVLLMNEGKLL 216
Cdd:COG1119 143 LSQGEQRRVLIARALVKDPELLILDEPTAGLDLGARELLLALLDKLAAEGAPtLVLVTHHVEEIPPGiTHVLLLKDGRVV 222
|
....*...
gi 488984955 217 YQGEPTAL 224
Cdd:COG1119 223 AAGPKEEV 230
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
26-236 |
2.72e-23 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 101.33 E-value: 2.72e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 26 LTCTIRAGYVTGLVGPDGAGKTTLMRMLAGLLKPDEGRASVIGFDpLKDDSALHAVLGYMPQKFGLYEDLTVMENLTLYA 105
Cdd:PRK11432 25 LNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIFIDGED-VTHRSIQQRDICMVFQSYALFPHMSLGENVGYGL 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 106 DLRSVTGEARKKIFDRLLEFTSLGPFTERLAGKLSGGMKQKLGLACTLVGDPKVLLLDEPGVGVDPISRRELWQMVHELA 185
Cdd:PRK11432 104 KMLGVPKEERKQRVKEALELVDLAGFEDRYVDQISGGQQQRVALARALILKPKVLLFDEPLSNLDANLRRSMREKIRELQ 183
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 488984955 186 GD-GMLILWSTSYLDEAEQCRD-VLLMNEGKLLYQGEPTALTQTMAGRsFLVS 236
Cdd:PRK11432 184 QQfNITSLYVTHDQSEAFAVSDtVIVMNKGKIMQIGSPQELYRQPASR-FMAS 235
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
348-537 |
3.37e-23 |
|
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of the protease secretion system PrtD, a 60-kDa integral membrane protein sharing 37% identity with HlyB, the ABC component of the alpha-hemolysin secretion pathway, in the C-terminal domain. They export degradative enzymes by using a type I protein secretion system and lack an N-terminal signal peptide, but contain a C-terminal secretion signal. The Type I secretion apparatus is made up of three components, an ABC transporter, a membrane fusion protein (MFP), and an outer membrane protein (OMP). For the HlyA transporter complex, HlyB (ABC transporter) and HlyD (MFP) reside in the inner membrane of E. coli. The OMP component is TolC, which is thought to interact with the MFP to form a continuous channel across the periplasm from the cytoplasm to the exterior. HlyB belongs to the family of ABC transporters, which are ubiquitous, ATP-dependent transmembrane pumps or channels. The spectrum of transport substrates ranges from inorganic ions, nutrients such as amino acids, sugars, or peptides, hydrophobic drugs, to large polypeptides, such as HlyA.
Pssm-ID: 213213 [Multi-domain] Cd Length: 173 Bit Score: 96.52 E-value: 3.37e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 348 VDFQVKRGEIFGLLGPNGAGKSTTFKMMCGLLVPTSGKALVLGMDL-KVSSGKARQHLGYMAQKFSLYGNlSVEQNLrfF 426
Cdd:cd03246 21 VSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDGADIsQWDPNELGDHVGYLPQDDELFSG-SIAENI--L 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 427 SGvyglrgraqnekiarmsdafglksiarhaadelplGYKQRLALACSLMHEPDILFLDEPTSGVDPLTRREFWLHINSM 506
Cdd:cd03246 98 SG-----------------------------------GQRQRLGLARALYGNPRILVLDEPNSHLDVEGERALNQAIAAL 142
|
170 180 190
....*....|....*....|....*....|.
gi 488984955 507 VDKGVTVMVTTHFMDEAEYCDRIGLVYHGKL 537
Cdd:cd03246 143 KAAGATRIVIAHRPETLASADRILVLEDGRV 173
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
330-544 |
4.25e-23 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 98.62 E-value: 4.25e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 330 IEAQSLTKKFGDFAATDHVDFQVKRGEIFGLLGPNGAGKSTTFKMMCGLLVPTSGKALVLGMDLKVSSGKAR-QHLGYMA 408
Cdd:COG4604 2 IEIKNVSKRYGGKVVLDDVSLTIPKGGITALIGPNGAGKSTLLSMISRLLPPDSGEVLVDGLDVATTPSRELaKRLAILR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 409 QKFSLYGNLSVEQNLRF----FSgvyglRGR---AQNEKIARMSDAFGLKSIARHAADELPLGYKQRLALACSLMHEPDI 481
Cdd:COG4604 82 QENHINSRLTVRELVAFgrfpYS-----KGRltaEDREIIDEAIAYLDLEDLADRYLDELSGGQRQRAFIAMVLAQDTDY 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 488984955 482 LFLDEPTSGVDPLTRREFWLHINSMVD-KGVTVMVTTHfmD---EAEYCDRIGLVYHGKLIASGTPD 544
Cdd:COG4604 157 VLLDEPLNNLDMKHSVQMMKLLRRLADeLGKTVVIVLH--DinfASCYADHIVAMKDGRVVAQGTPE 221
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
346-541 |
5.83e-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: 96.23 E-value: 5.83e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 346 DHVDFQVKRGEIFGLLGPNGAGKSTTFKMMCGLLVPTSGKALVLGMDLKVSSGKARQHLGYMAQKFSLYgNLSVEQNL-R 424
Cdd:cd03247 19 KNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDGVPVSDLEKALSSLISVLNQRPYLF-DTTLRNNLgR 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 425 FFSGvyglrgraqnekiarmsdafglksiarhaadelplGYKQRLALACSLMHEPDILFLDEPTSGVDPLTRREFWLHIN 504
Cdd:cd03247 98 RFSG-----------------------------------GERQRLALARILLQDAPIVLLDEPTVGLDPITERQLLSLIF 142
|
170 180 190
....*....|....*....|....*....|....*..
gi 488984955 505 SMVdKGVTVMVTTHFMDEAEYCDRIGLVYHGKLIASG 541
Cdd:cd03247 143 EVL-KDKTLIWITHHLTGIEHMDKILFLENGKIIMQG 178
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
348-549 |
6.46e-23 |
|
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: 6.46e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 348 VDFQVKRGEIFGLLGPNGAGKSTTFKMMCGLLVPTSGKALVLGMDLKVSSGKA-RQHLGYMAQKFSLYgNLSVEQNLRFF 426
Cdd:cd03254 22 INFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGIDIRDISRKSlRSMIGVVLQDTFLF-SGTIMENIRLG 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 427 sgvyglRGRAQNEKIARMS-----DAF------GLKSIARHAADELPLGYKQRLALACSLMHEPDILFLDEPTSGVDPLT 495
Cdd:cd03254 101 ------RPNATDEEVIEAAkeagaHDFimklpnGYDTVLGENGGNLSQGERQLLAIARAMLRDPKILILDEATSNIDTET 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 488984955 496 RREfwlhINSMVD---KGVTVMVTTHFMDEAEYCDRIGLVYHGKLIASGTPDALKAQ 549
Cdd:cd03254 175 EKL----IQEALEklmKGRTSIIIAHRLSTIKNADKILVLDDGKIIEEGTHDELLAK 227
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
334-569 |
6.76e-23 |
|
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: 100.19 E-value: 6.76e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 334 SLTKKFGDFAATdhVDFQVKRGEIFGLLGPNGAGKSTTFKMMCGLLVPTSGKaLVLGMDLKVSSGKA------RQHLGYM 407
Cdd:TIGR02142 4 RFSKRLGDFSLD--ADFTLPGQGVTAIFGRSGSGKTTLIRLIAGLTRPDEGE-IVLNGRTLFDSRKGiflppeKRRIGYV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 408 AQKFSLYGNLSVEQNLRFfsGVYGLRGRAQNEKIARMSDAFGLKSIARHAADELPLGYKQRLALACSLMHEPDILFLDEP 487
Cdd:TIGR02142 81 FQEARLFPHLSVRGNLRY--GMKRARPSERRISFERVIELLGIGHLLGRLPGRLSGGEKQRVAIGRALLSSPRLLLMDEP 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 488 TSGVDPLTRREFWLHINSMVDK-GVTVMVTTHFMDE-AEYCDRIGLVYHGKLIASGTPDALkaQAADDSQTDPTMEQAFI 565
Cdd:TIGR02142 159 LAALDDPRKYEILPYLERLHAEfGIPILYVSHSLQEvLRLADRVVVLEDGRVAAAGPIAEV--WASPDLPWLAREDQGSL 236
|
....
gi 488984955 566 TLIN 569
Cdd:TIGR02142 237 IEGV 240
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
347-554 |
8.01e-23 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 97.35 E-value: 8.01e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 347 HVDFQVKRGEIFGLLGPNGAGKSTTFKMMCGLLVPTSGKALVLGMDlKVSSGKARQHLGYMAQKFSLYGNLSVEQNLRFf 426
Cdd:PRK10771 17 RFDLTVERGERVAILGPSGAGKSTLLNLIAGFLTPASGSLTLNGQD-HTTTPPSRRPVSMLFQENNLFSHLTVAQNIGL- 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 427 sGVY-GLR-GRAQNEKIARMSDAFGLKSIARHAADELPLGYKQRLALACSLMHEPDILFLDEPTSGVDPLTRREFwLHIN 504
Cdd:PRK10771 95 -GLNpGLKlNAAQREKLHAIARQMGIEDLLARLPGQLSGGQRQRVALARCLVREQPILLLDEPFSALDPALRQEM-LTLV 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 488984955 505 SMV--DKGVT-VMVTTHFMDEAEYCDRIGLVYHGKLIASGTPDALKAQAADDS 554
Cdd:PRK10771 173 SQVcqERQLTlLMVSHSLEDAARIAPRSLVVADGRIAWDGPTDELLSGKASAS 225
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
339-529 |
8.62e-23 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 96.15 E-value: 8.62e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 339 FGDFAATDHVDFQVKRGEIFGLLGPNGAGKSTTFKMMCGLLVPTSGKALVlgmdlkvsSGKARqhLGYMAQKFSLYGNL- 417
Cdd:NF040873 2 YGGRPVLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTVRR--------AGGAR--VAYVPQRSEVPDSLp 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 418 -SVEQNLRFfsGVYGLRG------RAQNEKIARMSDAFGLKSIARHAADELPLGYKQRLALACSLMHEPDILFLDEPTSG 490
Cdd:NF040873 72 lTVRDLVAM--GRWARRGlwrrltRDDRAAVDDALERVGLADLAGRQLGELSGGQRQRALLAQGLAQEADLLLLDEPTTG 149
|
170 180 190
....*....|....*....|....*....|....*....
gi 488984955 491 VDPLTRREFWLHINSMVDKGVTVMVTTHFMDEAEYCDRI 529
Cdd:NF040873 150 LDAESRERIIALLAEEHARGATVVVVTHDLELVRRADPC 188
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
327-552 |
1.00e-22 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 98.27 E-value: 1.00e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 327 ETVIEAQSLTKKFG---DFAATDHVDFQVKRGEIFGLLGPNGAGKSTTFKMMCGLLVPTSGKALVLGMDLKVSS-GKARQ 402
Cdd:PRK13650 2 SNIIEVKNLTFKYKedqEKYTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIIDGDLLTEENvWDIRH 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 403 HLGYMAQK-FSLYGNLSVEQNLRFfsgvyGL--RGRAQNEKIARMSDAF---GLKSIARHAADELPLGYKQRLALACSLM 476
Cdd:PRK13650 82 KIGMVFQNpDNQFVGATVEDDVAF-----GLenKGIPHEEMKERVNEALelvGMQDFKEREPARLSGGQKQRVAIAGAVA 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 488984955 477 HEPDILFLDEPTSGVDPLTRREFWLHINSMVDK-GVTVMVTTHFMDEAEYCDRIGLVYHGKLIASGTPDALKAQAAD 552
Cdd:PRK13650 157 MRPKIIILDEATSMLDPEGRLELIKTIKGIRDDyQMTVISITHDLDEVALSDRVLVMKNGQVESTSTPRELFSRGND 233
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
5-564 |
1.06e-22 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 101.67 E-value: 1.06e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 5 VIALNGLSRRFPGMdrPAVAPLTCTIRAGYVTGLVGPDGAGKTTLMRMLAGLLKPDEGRASVIG--FDPLKDDSAlHAVL 82
Cdd:PRK15439 11 LLCARSISKQYSGV--EVLKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIGGnpCARLTPAKA-HQLG 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 83 GYM-PQKFGLYEDLTVMENLTLyadlRSVTGEARKKIFDRLLEFTSLGPFTERLAGKLSGGMKQKLGLACTLVGDPKVLL 161
Cdd:PRK15439 88 IYLvPQEPLLFPNLSVKENILF----GLPKRQASMQKMKQLLAALGCQLDLDSSAGSLEVADRQIVEILRGLMRDSRILI 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 162 LDEPGVGVDPISRRELWQMVHELAGDGMLILWSTSYLDEAEQCRD-VLLMNEGKLLYQGEPTALTqtmagrsflvsspqe 240
Cdd:PRK15439 164 LDEPTASLTPAETERLFSRIRELLAQGVGIVFISHKLPEIRQLADrISVMRDGTIALSGKTADLS--------------- 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 241 nnrrllqralklpqvSDGVIQGksvrlilkkdarieevqqhgdMPPLQVADTAPRFEDAFIDLLGgagtaesplgaiiHR 320
Cdd:PRK15439 229 ---------------TDDIIQA---------------------ITPAAREKSLSASQKLWLELPG-------------NR 259
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 321 VDGSKEETVIEAQSLTKKfgDFAatdHVDFQVKRGEIFGLLGPNGAGKSTTFKMMCGLLVPTSGKALVLGMDLKVSSGKA 400
Cdd:PRK15439 260 RQQAAGAPVLTVEDLTGE--GFR---NISLEVRAGEILGLAGVVGAGRTELAETLYGLRPARGGRIMLNGKEINALSTAQ 334
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 401 RQHLG--YMAQKFSLYGnLSVEQNLRF--FSGVYG-----LRGRAQNEKIARMSDAFGLK-SIARHAADELPLGYKQRLA 470
Cdd:PRK15439 335 RLARGlvYLPEDRQSSG-LYLDAPLAWnvCALTHNrrgfwIKPARENAVLERYRRALNIKfNHAEQAARTLSGGNQQKVL 413
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 471 LACSLMHEPDILFLDEPTSGVDPLTRREFWLHINSMVDKGVTVMVTTHFMDEAE-YCDRIgLVYHGKLIAsgtpDALKAQ 549
Cdd:PRK15439 414 IAKCLEASPQLLIVDEPTRGVDVSARNDIYQLIRSIAAQNVAVLFISSDLEEIEqMADRV-LVMHQGEIS----GALTGA 488
|
570
....*....|....*
gi 488984955 550 AADdsqTDPTMEQAF 564
Cdd:PRK15439 489 AIN---VDTIMRLAF 500
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
328-544 |
1.10e-22 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 97.39 E-value: 1.10e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 328 TVIEAQSLTKKFGDFAATDHVDFQVKRGEIFGLLGPNGAGKSTTFKMMCGLLVPTSGKALVLGMDLKVSSGKA-RQHLGY 406
Cdd:PRK11231 1 MTLRTENLTVGYGTKRILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDKPISMLSSRQlARRLAL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 407 MAQKFSLYGNLSVEQNLRF----FSGVYGLRGRAQNEKIARMSDAFGLKSIARHAADELPLGYKQRLALACSLMHEPDIL 482
Cdd:PRK11231 81 LPQHHLTPEGITVRELVAYgrspWLSLWGRLSAEDNARVNQAMEQTRINHLADRRLTDLSGGQRQRAFLAMVLAQDTPVV 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 488984955 483 FLDEPTSGVDPLTRREFWLHINSMVDKGVTVMVTTHFMDEA-EYCDRIGLVYHGKLIASGTPD 544
Cdd:PRK11231 161 LLDEPTTYLDINHQVELMRLMRELNTQGKTVVTVLHDLNQAsRYCDHLVVLANGHVMAQGTPE 223
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
348-543 |
1.29e-22 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 98.27 E-value: 1.29e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 348 VDFQVKRGEIFGLLGPNGAGKSTTFKMMCGLLVPTSGKALVlgMDLKVSSGKARQHLGYMAQKFSLYGNL--------SV 419
Cdd:PRK13643 25 IDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVTV--GDIVVSSTSKQKEIKPVRKKVGVVFQFpesqlfeeTV 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 420 EQNLRFFSGVYGLrGRAQNEKIARMS-DAFGL-KSIARHAADELPLGYKQRLALACSLMHEPDILFLDEPTSGVDPLTRR 497
Cdd:PRK13643 103 LKDVAFGPQNFGI-PKEKAEKIAAEKlEMVGLaDEFWEKSPFELSGGQMRRVAIAGILAMEPEVLVLDEPTAGLDPKARI 181
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 488984955 498 EFWLHINSMVDKGVTVMVTTHFMDE-AEYCDRIGLVYHGKLIASGTP 543
Cdd:PRK13643 182 EMMQLFESIHQSGQTVVLVTHLMDDvADYADYVYLLEKGHIISCGTP 228
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
346-546 |
1.41e-22 |
|
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a central component of the secretion machinery that translocates the toxin, hemolysin A, in a Sec-independent fashion across both membranes of E. coli. The hemolysin A (HlyA) transport machinery is composed of the ATP-binding cassette (ABC) transporter HlyB located in the inner membrane, hemolysin D (HlyD), also anchored in the inner membrane, and TolC, which resides in the outer membrane. HlyD apparently forms a continuous channel that bridges the entire periplasm, interacting with TolC and HlyB. This arrangement prevents the appearance of periplasmic intermediates of HlyA during substrate transport. Little is known about the molecular details of HlyA transport, but it is evident that ATP-hydrolysis by the ABC-transporter HlyB is a necessary source of energy.
Pssm-ID: 213219 [Multi-domain] Cd Length: 237 Bit Score: 96.79 E-value: 1.41e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 346 DHVDFQVKRGEIFGLLGPNGAGKSTTFKMMCGLLVPTSGKALVLGMDLK-VSSGKARQHLGYMAQKFSLYgNLSVEQNLR 424
Cdd:cd03252 19 DNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGHDLAlADPAWLRRQVGVVLQENVLF-NRSIRDNIA 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 425 FFSGVYGLRgraQNEKIARMSDAFGLKSiarhaadELPLGY---------------KQRLALACSLMHEPDILFLDEPTS 489
Cdd:cd03252 98 LADPGMSME---RVIEAAKLAGAHDFIS-------ELPEGYdtivgeqgaglsggqRQRIAIARALIHNPRILIFDEATS 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 488984955 490 GVDPLTRREFwlhINSMVD--KGVTVMVTTHFMDEAEYCDRIGLVYHGKLIASGTPDAL 546
Cdd:cd03252 168 ALDYESEHAI---MRNMHDicAGRTVIIIAHRLSTVKNADRIIVMEKGRIVEQGSHDEL 223
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
343-549 |
2.03e-22 |
|
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: 96.15 E-value: 2.03e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 343 AATDHVDFQVKRGEIFGLLGPNGAGKSTTFKMMCGLLVPTSGKALVLGMDLK-VSSGKARQHLGYMAQKFSLYgNLSVEQ 421
Cdd:cd03251 16 PVLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDGHDVRdYTLASLRRQIGLVSQDVFLF-NDTVAE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 422 NLRffsgvYGLRG--RAQNEKIARMSDAFGLksiarhaADELPLGY---------------KQRLALACSLMHEPDILFL 484
Cdd:cd03251 95 NIA-----YGRPGatREEVEEAARAANAHEF-------IMELPEGYdtvigergvklsggqRQRIAIARALLKDPPILIL 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 488984955 485 DEPTSGVDPLTRREFWLHINSMVdKGVTVMVTTHFMDEAEYCDRIGLVYHGKLIASGTPDALKAQ 549
Cdd:cd03251 163 DEATSALDTESERLVQAALERLM-KNRTTFVIAHRLSTIENADRIVVLEDGKIVERGTHEELLAQ 226
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
329-542 |
2.32e-22 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 98.33 E-value: 2.32e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 329 VIEAQSLTKKF----GDFAATDHVDFQVKRGEIFGLLGPNGAGKSTTFKMMCGLLVPTSGKALVLGMDLKVSSGK----A 400
Cdd:PRK11153 1 MIELKNISKVFpqggRTIHALNNVSLHIPAGEIFGVIGASGAGKSTLIRCINLLERPTSGRVLVDGQDLTALSEKelrkA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 401 RQHLGYMAQKFSLYGNLSVEQNLRFFSGVYGLRGRAQNEKIARMSDAFGLKSIARHAADELPLGYKQRLALACSLMHEPD 480
Cdd:PRK11153 81 RRQIGMIFQHFNLLSSRTVFDNVALPLELAGTPKAEIKARVTELLELVGLSDKADRYPAQLSGGQKQRVAIARALASNPK 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 488984955 481 ILFLDEPTSGVDPLTRR---EFWLHINSmvDKGVTVMVTTHFMDEA-EYCDRIGLVYHGKLIASGT 542
Cdd:PRK11153 161 VLLCDEATSALDPATTRsilELLKDINR--ELGLTIVLITHEMDVVkRICDRVAVIDAGRLVEQGT 224
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
6-215 |
2.33e-22 |
|
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: 94.21 E-value: 2.33e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 6 IALNGLSRRFPGMDRPAVAPLTCTIRAGYVTGLVGPDGAGKTTLMRMLAGLLKPDEGRASVIGFDPLK-DDSALHAVLGY 84
Cdd:cd03246 1 LEVENVSFRYPGAEPPVLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDGADISQwDPNELGDHVGY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 85 MPQKFGLYEDlTVMENLtlyadlrsvtgearkkifdrlleftslgpfterlagkLSGGMKQKLGLACTLVGDPKVLLLDE 164
Cdd:cd03246 81 LPQDDELFSG-SIAENI-------------------------------------LSGGQRQRLGLARALYGNPRILVLDE 122
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 488984955 165 PGVGVDPISRRELWQMVHELAGDGMLILWSTSYLDEAEQCRDVLLMNEGKL 215
Cdd:cd03246 123 PNSHLDVEGERALNQAIAALKAAGATRIVIAHRPETLASADRILVLEDGRV 173
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
2-226 |
2.34e-22 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 96.78 E-value: 2.34e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 2 SETVIALNGLSRRFPGmdRPAVAPLTCTIRAGYVTGLVGPDGAGKTTLMRMLAGLLKPDEGRAsVIGFDPLK--DDSALH 79
Cdd:PRK10575 8 SDTTFALRNVSFRVPG--RTLLHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEI-LLDAQPLEswSSKAFA 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 80 AVLGYMPQKFGLYEDLTVMENLTL-----YADLRSVTGEARKKIfDRLLEFTSLGPFTERLAGKLSGGMKQKLGLACTLV 154
Cdd:PRK10575 85 RKVAYLPQQLPAAEGMTVRELVAIgrypwHGALGRFGAADREKV-EEAISLVGLKPLAHRLVDSLSGGERQRAWIAMLVA 163
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 488984955 155 GDPKVLLLDEPGVGVDPISRRELWQMVHELAGD-GMLILWSTSYLDEAEQ-CRDVLLMNEGKLLYQGEPTALTQ 226
Cdd:PRK10575 164 QDSRCLLLDEPTSALDIAHQVDVLALVHRLSQErGLTVIAVLHDINMAARyCDYLVALRGGEMIAQGTPAELMR 237
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
5-221 |
5.24e-22 |
|
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440743 [Multi-domain] Cd Length: 239 Bit Score: 95.06 E-value: 5.24e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 5 VIALNGLSRRFpGmDRPAVAPLTCTIRAGYVTGLVGPDGAGKTTLMRMLAGLLKPDEGRASVIGFDPLKDDSALHAV--- 81
Cdd:COG1126 1 MIEIENLHKSF-G-DLEVLKGISLDVEKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTITVDGEDLTDSKKDINKLrrk 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 82 LGYMPQKFGLYEDLTVMENLTLyaDLRSVTGEARKKIFDR---LLEFTSLGPFTERLAGKLSGGMKQKLGLACTLVGDPK 158
Cdd:COG1126 79 VGMVFQQFNLFPHLTVLENVTL--APIKVKKMSKAEAEERameLLERVGLADKADAYPAQLSGGQQQRVAIARALAMEPK 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 488984955 159 VLLLDEPGVGVDPISRRELWQMVHELAGDGMLILWSTSYLDEAEQCRD-VLLMNEGKLLYQGEP 221
Cdd:COG1126 157 VMLFDEPTSALDPELVGEVLDVMRDLAKEGMTMVVVTHEMGFAREVADrVVFMDGGRIVEEGPP 220
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
9-219 |
6.00e-22 |
|
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ABC transporters homologous to the Drosophila white gene, which acts as a dimeric importer for eye pigment precursors. The eye pigmentation of Drosophila is developed from the synthesis and deposition in the cells of red pigments, which are synthesized from guanine, and brown pigments, which are synthesized from tryptophan. The pigment precursors are encoded by the white, brown, and scarlet genes, respectively. Evidence from genetic and biochemical studies suggest that the White and Brown proteins function as heterodimers to import guanine, while the White and Scarlet proteins function to import tryptophan. However, a recent study also suggests that White may be involved in the transport of a metabolite, such as 3-hydroxykynurenine, across intracellular membranes. Mammalian ABC transporters belonging to the White subfamily (ABCG1, ABCG5, and ABCG8) have been shown to be involved in the regulation of lipid-trafficking mechanisms in macrophages, hepatocytes, and intestinal mucosa cells. ABCG1 (ABC8), the human homolog of the Drosophila white gene is induced in monocyte-derived macrophages during cholesterol influx mediated by acetylated low-density lipoprotein. It is possible that human ABCG1 forms heterodimers with several heterologous partners.
Pssm-ID: 213201 [Multi-domain] Cd Length: 226 Bit Score: 94.65 E-value: 6.00e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 9 NGLSRRFPGMDRPAVAPLTCTIRAGYVTGLVGPDGAGKTTLMRMLAGLLKPDEGRASVIGFD--PLKDDSALHAVlGYMP 86
Cdd:cd03234 9 VGLKAKNWNKYARILNDVSLHVESGQVMAILGSSGSGKTTLLDAISGRVEGGGTTSGQILFNgqPRKPDQFQKCV-AYVR 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 87 QKFGLYEDLTVMENLTLYADLRSvTGEARKKIFDRLLEFTSLGPFT-ERLAGK----LSGGMKQKLGLACTLVGDPKVLL 161
Cdd:cd03234 88 QDDILLPGLTVRETLTYTAILRL-PRKSSDAIRKKRVEDVLLRDLAlTRIGGNlvkgISGGERRRVSIAVQLLWDPKVLI 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 488984955 162 LDEPGVGVDPISRRELWQMVHELAGDGMLILWSTsyldeaEQCR--------DVLLMNEGKLLYQG 219
Cdd:cd03234 167 LDEPTSGLDSFTALNLVSTLSQLARRNRIVILTI------HQPRsdlfrlfdRILLLSSGEIVYSG 226
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
348-543 |
6.41e-22 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 95.97 E-value: 6.41e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 348 VDFQVKRGEIFGLLGPNGAGKSTTFKMMCGLLVPTSGKALVLGMDLKVSS-----GKARQHLGYMAQkF--SLYGNLSVE 420
Cdd:PRK13649 26 VNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDDTLITSTSknkdiKQIRKKVGLVFQ-FpeSQLFEETVL 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 421 QNLRFFSGVYGLrGRAQNEKIARmsDAFGLKSIARHAAD----ELPLGYKQRLALACSLMHEPDILFLDEPTSGVDPLTR 496
Cdd:PRK13649 105 KDVAFGPQNFGV-SQEEAEALAR--EKLALVGISESLFEknpfELSGGQMRRVAIAGILAMEPKILVLDEPTAGLDPKGR 181
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 488984955 497 REFWLHINSMVDKGVTVMVTTHFMDE-AEYCDRIGLVYHGKLIASGTP 543
Cdd:PRK13649 182 KELMTLFKKLHQSGMTIVLVTHLMDDvANYADFVYVLEKGKLVLSGKP 229
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
6-171 |
6.73e-22 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 97.07 E-value: 6.73e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 6 IALNGLSRRFPGMDRP--AVAPLTCTIRAGYVTGLVGPDGAGKTTLMRMLAGLLKPDEGRASVIGFDPLK-DDSALHAV- 81
Cdd:COG1135 2 IELENLSKTFPTKGGPvtALDDVSLTIEKGEIFGIIGYSGAGKSTLIRCINLLERPTSGSVLVDGVDLTAlSERELRAAr 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 82 --LGYMPQKFGLYEDLTVMENLTLYADLRSVTGEARKKIFDRLLEFTSLGPFTERLAGKLSGGMKQKLGLACTLVGDPKV 159
Cdd:COG1135 82 rkIGMIFQHFNLLSSRTVAENVALPLEIAGVPKAEIRKRVAELLELVGLSDKADAYPSQLSGGQKQRVGIARALANNPKV 161
|
170
....*....|..
gi 488984955 160 LLLDEPGVGVDP 171
Cdd:COG1135 162 LLCDEATSALDP 173
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
29-219 |
7.22e-22 |
|
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: 94.52 E-value: 7.22e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 29 TIRAGYVTGLVGPDGAGKTTLMRMLAGLLKPDEGRASVIGfdplkDDSALHAvLGYmpqkfGLYEDLTVMENLTLYADLR 108
Cdd:cd03220 44 EVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVTVRG-----RVSSLLG-LGG-----GFNPELTGRENIYLNGRLL 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 109 SVTGEARKKIFDRLLEFTSLGPFTERLAGKLSGGMKQKLGLACTLVGDPKVLLLDEP-GVGvDPISRRELWQMVHEL-AG 186
Cdd:cd03220 113 GLSRKEIDEKIDEIIEFSELGDFIDLPVKTYSSGMKARLAFAIATALEPDILLIDEVlAVG-DAAFQEKCQRRLRELlKQ 191
|
170 180 190
....*....|....*....|....*....|...
gi 488984955 187 DGMLILWSTSYLDEAEQCRDVLLMNEGKLLYQG 219
Cdd:cd03220 192 GKTVILVSHDPSSIKRLCDRALVLEKGKIRFDG 224
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
38-221 |
7.75e-22 |
|
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: 94.71 E-value: 7.75e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 38 LVGPDGAGKTTLMRMLAGLLKPDEGRASVIGFD-----PLKDDsalhavLGYMPQKFGLYEDLTVMENLTLYADLRSVTG 112
Cdd:cd03299 30 ILGPTGSGKSVLLETIAGFIKPDSGKILLNGKDitnlpPEKRD------ISYVPQNYALFPHMTVYKNIAYGLKKRKVDK 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 113 EARKKIFDRLLEFTSLGPFTERLAGKLSGGMKQKLGLACTLVGDPKVLLLDEPGVGVDP---ISRRELWQMVHELAgdGM 189
Cdd:cd03299 104 KEIERKVLEIAEMLGIDHLLNRKPETLSGGEQQRVAIARALVVNPKILLLDEPFSALDVrtkEKLREELKKIRKEF--GV 181
|
170 180 190
....*....|....*....|....*....|...
gi 488984955 190 LILWSTSYLDEAEQCRD-VLLMNEGKLLYQGEP 221
Cdd:cd03299 182 TVLHVTHDFEEAWALADkVAIMLNGKLIQVGKP 214
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
6-215 |
9.23e-22 |
|
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: 93.86 E-value: 9.23e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 6 IALNGLSRRFPgmDRPAVAPLTCTIRAGYVTGLVGPDGAGKTTLMRMLAGLLKPDEGRASVIGFDpLKDDSALHAVLGYM 85
Cdd:cd03301 1 VELENVTKRFG--NVTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGRD-VTDLPPKDRDIAMV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 86 PQKFGLYEDLTVMENLTLYADLRSVTGEARKKIFDRLLEFTSLGPFTERLAGKLSGGMKQKLGLACTLVGDPKVLLLDEP 165
Cdd:cd03301 78 FQNYALYPHMTVYDNIAFGLKLRKVPKDEIDERVREVAELLQIEHLLDRKPKQLSGGQRQRVALGRAIVREPKVFLMDEP 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 488984955 166 GVGVDPI----SRRELWQMVHELagdGMLILWSTSYLDEAEQCRD-VLLMNEGKL 215
Cdd:cd03301 158 LSNLDAKlrvqMRAELKRLQQRL---GTTTIYVTHDQVEAMTMADrIAVMNDGQI 209
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
328-548 |
1.10e-21 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 94.43 E-value: 1.10e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 328 TVIEAQSLTKKFGDFAATDHVDFQVKRGEIFGLLGPNGAGKSTTFKMMCGLLVPTSGKALVlgMDLKVSSGKA------- 400
Cdd:PRK11264 2 SAIEVKNLVKKFHGQTVLHGIDLEVKPGEVVAIIGPSGSGKTTLLRCINLLEQPEAGTIRV--GDITIDTARSlsqqkgl 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 401 ----RQHLGYMAQKFSLYGNLSVEQNLrfFSGVYGLRGRAQNEKIARMSDAF---GLKSIARHAADELPLGYKQRLALAC 473
Cdd:PRK11264 80 irqlRQHVGFVFQNFNLFPHRTVLENI--IEGPVIVKGEPKEEATARARELLakvGLAGKETSYPRRLSGGQQQRVAIAR 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 488984955 474 SLMHEPDILFLDEPTSGVDPLTRREFWLHINSMVDKGVTVMVTTHFMDEA-EYCDRIGLVYHGKLIASGTPDALKA 548
Cdd:PRK11264 158 ALAMRPEVILFDEPTSALDPELVGEVLNTIRQLAQEKRTMVIVTHEMSFArDVADRAIFMDQGRIVEQGPAKALFA 233
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
6-239 |
1.11e-21 |
|
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: 94.48 E-value: 1.11e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 6 IALNGLSRRFP--GMDRPAVAPLTCTIRAGYVTGLVGPDGAGKTTLMRMLAGLLKPDEGRASVIGfDPL--KDDSALHAV 81
Cdd:COG1124 2 LEVRNLSVSYGqgGRRVPVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVTFDG-RPVtrRRRKAFRRR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 82 LGYMPQ--------KFGLYEdlTVMENLTLYadlrsVTGEARKKIfDRLLEFTSLGP-FTERLAGKLSGGMKQKLGLACT 152
Cdd:COG1124 81 VQMVFQdpyaslhpRHTVDR--ILAEPLRIH-----GLPDREERI-AELLEQVGLPPsFLDRYPHQLSGGQRQRVAIARA 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 153 LVGDPKVLLLDEPGVGVDPISRRELWQMVHEL-AGDGMLILWST------SYLdeaeqCRDVLLMNEGKLLYQGEPTAL- 224
Cdd:COG1124 153 LILEPELLLLDEPTSALDVSVQAEILNLLKDLrEERGLTYLFVShdlavvAHL-----CDRVAVMQNGRIVEELTVADLl 227
|
250
....*....|....*..
gi 488984955 225 --TQTMAGRSFLVSSPQ 239
Cdd:COG1124 228 agPKHPYTRELLAASLA 244
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
5-238 |
1.16e-21 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 95.05 E-value: 1.16e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 5 VIALNGLSRRFPGmDRPAVAPLTCTIRAGYVTGLVGPDGAGKTTLMRMLAGLLKPDEGRASVIGFDPlKDDSALHAV--- 81
Cdd:PRK13644 1 MIRLENVSYSYPD-GTPALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLVSGIDT-GDFSKLQGIrkl 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 82 LGYMPQ----KF---GLYEDLTV-MENLTLYADlrsvtgEARKKIfDRLLEFTSLGPFTERLAGKLSGGMKQKLGLACTL 153
Cdd:PRK13644 79 VGIVFQnpetQFvgrTVEEDLAFgPENLCLPPI------EIRKRV-DRALAEIGLEKYRHRSPKTLSGGQGQCVALAGIL 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 154 VGDPKVLLLDEPGVGVDPISRRELWQMVHELAGDGMLILWSTSYLDEAEQCRDVLLMNEGKLLYQGEPTALTQTMAGRSF 233
Cdd:PRK13644 152 TMEPECLIFDEVTSMLDPDSGIAVLERIKKLHEKGKTIVYITHNLEELHDADRIIVMDRGKIVLEGEPENVLSDVSLQTL 231
|
....*
gi 488984955 234 LVSSP 238
Cdd:PRK13644 232 GLTPP 236
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
5-219 |
1.24e-21 |
|
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: 93.72 E-value: 1.24e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 5 VIALNGLSRRFP--GMDRPAVAPLTCTIRAGYVTGLVGPDGAGKTTLMRMLAGLLKPDEGRASVIGFDPLKDDSALHAVL 82
Cdd:cd03257 1 LLEVKNLSVSFPtgGGSVKALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGKDLLKLSRRLRKIR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 83 G----YMPQkfglyeD--------LTVMENL--TLYADLRSVTGEARKKIFDRLLEFTSLGP-FTERLAGKLSGGMKQKL 147
Cdd:cd03257 81 RkeiqMVFQ------DpmsslnprMTIGEQIaePLRIHGKLSKKEARKEAVLLLLVGVGLPEeVLNRYPHELSGGQRQRV 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 488984955 148 GLACTLVGDPKVLLLDEPGVGVDPISRRELWQMVHELAGD-GMLILWSTSYLDEAEQ-CRDVLLMNEGKLLYQG 219
Cdd:cd03257 155 AIARALALNPKLLIADEPTSALDVSVQAQILDLLKKLQEElGLTLLFITHDLGVVAKiADRVAVMYAGKIVEEG 228
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
346-546 |
1.37e-21 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 95.28 E-value: 1.37e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 346 DHVDFQVKRGEIFGLLGPNGAGKSTTFKMMCGLLVPTSGKALVLGMDLKVSSG-----KARQHLGYMAQ--KFSLYGNlS 418
Cdd:PRK13641 24 DNISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITIAGYHITPETGnknlkKLRKKVSLVFQfpEAQLFEN-T 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 419 VEQNLRFFSGVYGLRGRAQNEKIARMSDAFGLK-SIARHAADELPLGYKQRLALACSLMHEPDILFLDEPTSGVDPLTRR 497
Cdd:PRK13641 103 VLKDVEFGPKNFGFSEDEAKEKALKWLKKVGLSeDLISKSPFELSGGQMRRVAIAGVMAYEPEILCLDEPAAGLDPEGRK 182
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 488984955 498 EFWLHINSMVDKGVTVMVTTHFMDE-AEYCDRIGLVYHGKLIASGTPDAL 546
Cdd:PRK13641 183 EMMQLFKDYQKAGHTVILVTHNMDDvAEYADDVLVLEHGKLIKHASPKEI 232
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
330-529 |
1.55e-21 |
|
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is a cytosolic protein required by fungal ribosomes for in vitro protein synthesis and for in vivo growth. EF-3 stimulates the binding of the EF-1: GTP: aa-tRNA ternary complex to the ribosomal A site by facilitated release of the deacylated tRNA from the E site. The reaction requires ATP hydrolysis. EF-3 contains two ATP nucleotide binding sequence (NBS) motifs. NBSI is sufficient for the intrinsic ATPase activity. NBSII is essential for the ribosome-stimulated functions.
Pssm-ID: 213188 [Multi-domain] Cd Length: 144 Bit Score: 90.97 E-value: 1.55e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 330 IEAQSLTKKFGDFAATDHVDFQVKRGEIFGLLGPNGAGKSTTFKMMCGLLVPTSGKaLVLGMDLKVssgkarqhlGYMAQ 409
Cdd:cd03221 1 IELENLSKTYGGKLLLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGI-VTWGSTVKI---------GYFEQ 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 410 kfslygnlsveqnlrfFSGvyglrgraqnekiarmsdafglksiarhaadelplGYKQRLALACSLMHEPDILFLDEPTS 489
Cdd:cd03221 71 ----------------LSG-----------------------------------GEKMRLALAKLLLENPNLLLLDEPTN 99
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 488984955 490 GVDPLTRRefWLhINSMVDKGVTVMVTTH---FMDEAeyCDRI 529
Cdd:cd03221 100 HLDLESIE--AL-EEALKEYPGTVILVSHdryFLDQV--ATKI 137
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
2-554 |
2.27e-21 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 97.67 E-value: 2.27e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 2 SETVIALNGLSRRFPGMDrpAVAPLTCTIRAGYVTGLVGPDGAGKTTLMRMLAGLLKPDEGRASVIG----FDPLKDdsA 77
Cdd:PRK11288 1 SSPYLSFDGIGKTFPGVK--ALDDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSILIDGqemrFASTTA--A 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 78 LHAVLGYMPQKFGLYEDLTVMENLTL-----------YADLRSVTGEARKKIFDRLLEFTSLgpfterlaGKLSGGMKQK 146
Cdd:PRK11288 77 LAAGVAIIYQELHLVPEMTVAENLYLgqlphkggivnRRLLNYEAREQLEHLGVDIDPDTPL--------KYLSIGQRQM 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 147 LGLACTLVGDPKVLLLDEPgvgVDPISRRE---LWQMVHELAGDGMLILWSTSYLDEA-EQCRDVLLMNEGKLLYQGEPT 222
Cdd:PRK11288 149 VEIAKALARNARVIAFDEP---TSSLSAREieqLFRVIRELRAEGRVILYVSHRMEEIfALCDAITVFKDGRYVATFDDM 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 223 A------LTQTMAGRsflvsspqennrrllqralklpQVSDgviqgksvrlilkkdarieevqqhgdmpplqVADTAPRf 296
Cdd:PRK11288 226 AqvdrdqLVQAMVGR----------------------EIGD-------------------------------IYGYRPR- 251
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 297 edafidllggagtaesPLGAIIHRVDGskeetvIEAQSLTKKfgdfaatdhVDFQVKRGEIFGLLGPNGAGKSTTFKMMC 376
Cdd:PRK11288 252 ----------------PLGEVRLRLDG------LKGPGLREP---------ISFSVRAGEIVGLFGLVGAGRSELMKLLY 300
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 377 GLLVPTSGKALVLGMDLKVSSGKARQHLGYMA----QKF-SLYGNLSVEQNL-----RFFSGVYGLRGRAQNEKIA-RMS 445
Cdd:PRK11288 301 GATRRTAGQVYLDGKPIDIRSPRDAIRAGIMLcpedRKAeGIIPVHSVADNInisarRHHLRAGCLINNRWEAENAdRFI 380
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 446 DAFGLKSIARHAA-DELPLGYKQRLALACSLMHEPDILFLDEPTSGVDPLTRREFWLHINSMVDKGVTV-MVTTHFMDEA 523
Cdd:PRK11288 381 RSLNIKTPSREQLiMNLSGGNQQKAILGRWLSEDMKVILLDEPTRGIDVGAKHEIYNVIYELAAQGVAVlFVSSDLPEVL 460
|
570 580 590
....*....|....*....|....*....|.
gi 488984955 524 EYCDRIGLVYHGKLIAsgtpDALKAQAADDS 554
Cdd:PRK11288 461 GVADRIVVMREGRIAG----ELAREQATERQ 487
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
328-543 |
2.54e-21 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 96.17 E-value: 2.54e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 328 TVIEAQSLTKKFGDFAATDHVDFQVKRGEIFGLLGPNGAGKSTTFKMMCGLLVPTSGKALVLGMDLKVSSGKARqHLGYM 407
Cdd:PRK09452 13 PLVELRGISKSFDGKEVISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLDGQDITHVPAENR-HVNTV 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 408 AQKFSLYGNLSVEQNLRFfsgvyGLR-GRAQNEKIA-RMSDAFG---LKSIARHAADELPLGYKQRLALACSLMHEPDIL 482
Cdd:PRK09452 92 FQSYALFPHMTVFENVAF-----GLRmQKTPAAEITpRVMEALRmvqLEEFAQRKPHQLSGGQQQRVAIARAVVNKPKVL 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 488984955 483 FLDEPTSGVDPLTRREFWLHINSMVDK-GVTVMVTTHFMDEA-EYCDRIGLVYHGKLIASGTP 543
Cdd:PRK09452 167 LLDESLSALDYKLRKQMQNELKALQRKlGITFVFVTHDQEEAlTMSDRIVVMRDGRIEQDGTP 229
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
26-226 |
2.73e-21 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 93.16 E-value: 2.73e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 26 LTCTirAGYVTGLVGPDGAGKTTLMRMLAGLLKPDEGRASVIG--FD-----PLKDDSALHAVLGYMPQKFGLYEDLTVM 98
Cdd:PRK11124 23 LDCP--QGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLNIAGnhFDfsktpSDKAIRELRRNVGMVFQQYNLWPHLTVQ 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 99 ENLTlYADLRsVTG----EARKKIfDRLLEFTSLGPFTERLAGKLSGGMKQKLGLACTLVGDPKVLLLDEPGVGVDPISR 174
Cdd:PRK11124 101 QNLI-EAPCR-VLGlskdQALARA-EKLLERLRLKPYADRFPLHLSGGQQQRVAIARALMMEPQVLLFDEPTAALDPEIT 177
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 488984955 175 RELWQMVHELAGDGMLILWSTSYLDEAEQ-CRDVLLMNEGKLLYQGEPTALTQ 226
Cdd:PRK11124 178 AQIVSIIRELAETGITQVIVTHEVEVARKtASRVVYMENGHIVEQGDASCFTQ 230
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
344-546 |
2.95e-21 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 93.90 E-value: 2.95e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 344 ATDHVDFQVKRGEIFGLLGPNGAGKSTTFKMMCGLLVPTSGKALVLGMDLKVSSG--KARQHLGYMAQK-FSLYGNLSVE 420
Cdd:PRK13644 17 ALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLVSGIDTGDFSKlqGIRKLVGIVFQNpETQFVGRTVE 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 421 QNLRFFSGVYGLRGRAQNEKIARMSDAFGLKSIARHAADELPLGYKQRLALACSLMHEPDILFLDEPTSGVDPLTRREFW 500
Cdd:PRK13644 97 EDLAFGPENLCLPPIEIRKRVDRALAEIGLEKYRHRSPKTLSGGQGQCVALAGILTMEPECLIFDEVTSMLDPDSGIAVL 176
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 488984955 501 LHINSMVDKGVTVMVTTHFMDEAEYCDRIGLVYHGKLIASGTPDAL 546
Cdd:PRK13644 177 ERIKKLHEKGKTIVYITHNLEELHDADRIIVMDRGKIVLEGEPENV 222
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
32-192 |
3.58e-21 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 91.86 E-value: 3.58e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 32 AGYVTGLVGPDGAGKTTLMRMLAGLLKPDEGRASVIGFDPlkDDSALHAVLGYMPQKFGLYEDLTVMENLTLYADLRsvt 111
Cdd:PRK13539 27 AGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDGGDI--DDPDVAEACHYLGHRNAMKPALTVAENLEFWAAFL--- 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 112 GEARKKIfDRLLEFTSLGPFTERLAGKLSGGMKQKLGLACTLVGDPKVLLLDEPGVGVDPISRRELWQMVHE-LAGDGML 190
Cdd:PRK13539 102 GGEELDI-AAALEAVGLAPLAHLPFGYLSAGQKRRVALARLLVSNRPIWILDEPTAALDAAAVALFAELIRAhLAQGGIV 180
|
..
gi 488984955 191 IL 192
Cdd:PRK13539 181 IA 182
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
327-546 |
3.90e-21 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 93.65 E-value: 3.90e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 327 ETVIEAQSLTKKFGD-FAATDHVDFQVKRGEIFGLLGPNGAGKSTTFKMMCGLLVPTSGKALVLGMDLKVSSGK-ARQHL 404
Cdd:PRK13647 2 DNIIEVEDLHFRYKDgTKALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGREVNAENEKwVRSKV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 405 GYMAQK-----FSLygnlSVEQNLRFFSGVYGLRGRAQNEKIARMSDAFGLKSIARHAADELPLGYKQRLALACSLMHEP 479
Cdd:PRK13647 82 GLVFQDpddqvFSS----TVWDDVAFGPVNMGLDKDEVERRVEEALKAVRMWDFRDKPPYHLSYGQKKRVAIAGVLAMDP 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 488984955 480 DILFLDEPTSGVDPLTRREFWLHINSMVDKGVTVMVTTHFMD-EAEYCDRIGLVYHGKLIASGTPDAL 546
Cdd:PRK13647 158 DVIVLDEPMAYLDPRGQETLMEILDRLHNQGKTVIVATHDVDlAAEWADQVIVLKEGRVLAEGDKSLL 225
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
334-543 |
4.96e-21 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 93.33 E-value: 4.96e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 334 SLTKKFGDFAATDHVDFQVKRGEIFGLLGPNGAGKSTTFKMMCGLLVPTS---GKALVLGMDLKVSS-GKARQHLGYMAQ 409
Cdd:PRK13640 12 SFTYPDSKKPALNDISFSIPRGSWTALIGHNGSGKSTISKLINGLLLPDDnpnSKITVDGITLTAKTvWDIREKVGIVFQ 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 410 K-FSLYGNLSVEQNLRFfsgvyGLRGRA--QNEKIARMSDAF---GLKSIARHAADELPLGYKQRLALACSLMHEPDILF 483
Cdd:PRK13640 92 NpDNQFVGATVGDDVAF-----GLENRAvpRPEMIKIVRDVLadvGMLDYIDSEPANLSGGQKQRVAIAGILAVEPKIII 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 488984955 484 LDEPTSGVDPLTRREFW-LHINSMVDKGVTVMVTTHFMDEAEYCDRIGLVYHGKLIASGTP 543
Cdd:PRK13640 167 LDESTSMLDPAGKEQILkLIRKLKKKNNLTVISITHDIDEANMADQVLVLDDGKLLAQGSP 227
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
8-198 |
5.29e-21 |
|
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: 96.66 E-value: 5.29e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 8 LNGLSRRFPGmDRPAVAPLTCTIRAGYVTGLVGPDGAGKTTLMRMLAGLLKPDEGRASVIGFDPLK-DDSALHAVLGYMP 86
Cdd:TIGR02868 337 LRDLSAGYPG-APPVLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPLQGEVTLDGVPVSSlDQDEVRRRVSVCA 415
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 87 QKFGLYeDLTVMENLTLYAdlrsvtGEARKKIFDRLLEFTSLGPFTERL-----------AGKLSGGMKQKLGLACTLVG 155
Cdd:TIGR02868 416 QDAHLF-DTTVRENLRLAR------PDATDEELWAALERVGLADWLRALpdgldtvlgegGARLSGGERQRLALARALLA 488
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 488984955 156 DPKVLLLDEPGVGVDPISRRElwqMVHEL--AGDGMLILWSTSYL 198
Cdd:TIGR02868 489 DAPILLLDEPTEHLDAETADE---LLEDLlaALSGRTVVLITHHL 530
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
26-192 |
5.75e-21 |
|
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: 91.02 E-value: 5.75e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 26 LTCTIRAGYVTGLVGPDGAGKTTLMRMLAGLLKPDEGRASVIGFDPLKDDSALHAVLGYMPQKFGLYEDLTVMENLTLYA 105
Cdd:cd03231 19 LSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNGGPLDFQRDSIARGLLYLGHAPGIKTTLSVLENLRFWH 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 106 DLRSvtgeaRKKIFDRLLEfTSLGPFTERLAGKLSGGMKQKLGLACTLVGDPKVLLLDEPGVGVDPISRRELWQ-MVHEL 184
Cdd:cd03231 99 ADHS-----DEQVEEALAR-VGLNGFEDRPVAQLSAGQQRRVALARLLLSGRPLWILDEPTTALDKAGVARFAEaMAGHC 172
|
....*...
gi 488984955 185 AGDGMLIL 192
Cdd:cd03231 173 ARGGMVVL 180
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
29-221 |
9.75e-21 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 91.68 E-value: 9.75e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 29 TIRAGYVTGLVGPDGAGKTTLMRMLAGLLKPDEGRASVIGfdplkddsALHAVLGYMpqkFGLYEDLTVMENLTLYADLR 108
Cdd:COG1134 48 EVERGESVGIIGRNGAGKSTLLKLIAGILEPTSGRVEVNG--------RVSALLELG---AGFHPELTGRENIYLNGRLL 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 109 SVTGEARKKIFDRLLEFTSLGPFTERLAGKLSGGMKQKLGLACTLVGDPKVLLLDEP-GVGvDPISRRELWQMVHELAGD 187
Cdd:COG1134 117 GLSRKEIDEKFDEIVEFAELGDFIDQPVKTYSSGMRARLAFAVATAVDPDILLVDEVlAVG-DAAFQKKCLARIRELRES 195
|
170 180 190
....*....|....*....|....*....|....*
gi 488984955 188 GMLILWSTSYLDEAEQ-CRDVLLMNEGKLLYQGEP 221
Cdd:COG1134 196 GRTVIFVSHSMGAVRRlCDRAIWLEKGRLVMDGDP 230
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
1-221 |
1.00e-20 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 92.60 E-value: 1.00e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 1 MSETVIALNGLSRRFPGMDRpAVAPLTCTIRAGYVTGLVGPDGAGKTTLMRMLAGLLKPDEGRAsVIGFDPLkDDSA--- 77
Cdd:PRK13636 1 MEDYILKVEELNYNYSDGTH-ALKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRI-LFDGKPI-DYSRkgl 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 78 --LHAVLGYMPQ-------KFGLYEDLTV-MENLTLYADlrsvtgEARKKIfDRLLEFTSLGPFTERLAGKLSGGMKQKL 147
Cdd:PRK13636 78 mkLRESVGMVFQdpdnqlfSASVYQDVSFgAVNLKLPED------EVRKRV-DNALKRTGIEHLKDKPTHCLSFGQKKRV 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 488984955 148 GLACTLVGDPKVLLLDEPGVGVDPISRRELWQMVHELA-GDGMLILWSTSYLDE-AEQCRDVLLMNEGKLLYQGEP 221
Cdd:PRK13636 151 AIAGVLVMEPKVLVLDEPTAGLDPMGVSEIMKLLVEMQkELGLTIIIATHDIDIvPLYCDNVFVMKEGRVILQGNP 226
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
288-549 |
1.19e-20 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 95.80 E-value: 1.19e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 288 QVADTAPRFEDaFIDLLGGAGTAESPLGAI-IHRVDGSkeetvIEAQSLTKKFGDFA-ATDHVDFQVKRGEIFGLLGPNG 365
Cdd:PRK13657 298 QVFMAAPKLEE-FFEVEDAVPDVRDPPGAIdLGRVKGA-----VEFDDVSFSYDNSRqGVEDVSFEAKPGQTVAIVGPTG 371
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 366 AGKSTTFKMMCGLLVPTSGKALVLGMDL-KVSSGKARQHLGYMAQKFSLYgNLSVEQNLRFfsG--------VYGLRGRA 436
Cdd:PRK13657 372 AGKSTLINLLQRVFDPQSGRILIDGTDIrTVTRASLRRNIAVVFQDAGLF-NRSIEDNIRV--GrpdatdeeMRAAAERA 448
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 437 Q-NEKIARMSDafGLKSIARHAADELPLGYKQRLALACSLMHEPDILFLDEPTSGVDPLTRREfwlhINSMVD---KGVT 512
Cdd:PRK13657 449 QaHDFIERKPD--GYDTVVGERGRQLSGGERQRLAIARALLKDPPILILDEATSALDVETEAK----VKAALDelmKGRT 522
|
250 260 270
....*....|....*....|....*....|....*..
gi 488984955 513 VMVTTHFMDEAEYCDRIGLVYHGKLIASGTPDALKAQ 549
Cdd:PRK13657 523 TFIIAHRLSTVRNADRILVFDNGRVVESGSFDELVAR 559
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
348-549 |
1.23e-20 |
|
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: 91.14 E-value: 1.23e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 348 VDFQVKRGEIFGLLGPNGAGKSTTFKMMCGLLVPTSGKALVLGMDLK-VSSGKARQHLGYMAQKFSLYgNLSVEQNLRFf 426
Cdd:cd03253 20 VSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDGQDIReVTLDSLRRAIGVVPQDTVLF-NDTIGYNIRY- 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 427 sG--------VYGLRGRAQ-NEKIARMSDAF-------GLKsiarhaadeLPLGYKQRLALACSLMHEPDILFLDEPTSG 490
Cdd:cd03253 98 -GrpdatdeeVIEAAKAAQiHDKIMRFPDGYdtivgerGLK---------LSGGEKQRVAIARAILKNPPILLLDEATSA 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 488984955 491 VDPLTRREFWLHINSmVDKGVTVMVTTHFMDEAEYCDRIGLVYHGKLIASGTPDALKAQ 549
Cdd:cd03253 168 LDTHTEREIQAALRD-VSKGRTTIVIAHRLSTIVNADKIIVLKDGRIVERGTHEELLAK 225
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
329-546 |
1.23e-20 |
|
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: 92.81 E-value: 1.23e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 329 VIEAQSLTKKF----GDFAATDHVDFQVKRGEIFGLLGPNGAGKSTTFKMMCGLLVP---TSGKALVLGMDLKVSSGKAR 401
Cdd:COG0444 1 LLEVRNLKVYFptrrGVVKAVDGVSFDVRRGETLGLVGESGSGKSTLARAILGLLPPpgiTSGEILFDGEDLLKLSEKEL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 402 QHlgYMAQKFSL-----YGNL--------SVEQNLRFFsgvYGLRGRAQNEKIARMSDAFGLKSIARHAAD---ELPLGY 465
Cdd:COG0444 81 RK--IRGREIQMifqdpMTSLnpvmtvgdQIAEPLRIH---GGLSKAEARERAIELLERVGLPDPERRLDRyphELSGGM 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 466 KQRLALACSLMHEPDILFLDEPTSGVDPLTRREFwlhINSMVD----KGVTVMVTTHFMDEAEY-CDRIGLVYHGKLIAS 540
Cdd:COG0444 156 RQRVMIARALALEPKLLIADEPTTALDVTIQAQI---LNLLKDlqreLGLAILFITHDLGVVAEiADRVAVMYAGRIVEE 232
|
....*.
gi 488984955 541 GTPDAL 546
Cdd:COG0444 233 GPVEEL 238
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
29-228 |
1.37e-20 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 91.37 E-value: 1.37e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 29 TIRAGYVTGLVGPDGAGKTTLMRMLAGLLKPDEGRASVIGfDPLKDDSA--LHAVLGYMPQKFGLYEDLTVMENLTLYAD 106
Cdd:PRK13548 24 TLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLNG-RPLADWSPaeLARRRAVLPQHSSLSFPFTVEEVVAMGRA 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 107 LRSVTGEARKKIFDRLLEFTSLGPFTERLAGKLSGGMKQKLGLACTLV------GDPKVLLLDEPGVGVDPISRRELWQM 180
Cdd:PRK13548 103 PHGLSRAEDDALVAAALAQVDLAHLAGRDYPQLSGGEQQRVQLARVLAqlwepdGPPRWLLLDEPTSALDLAHQHHVLRL 182
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 488984955 181 VHELA---GDGMLI---------LWstsyldeaeqCRDVLLMNEGKLLYQGEPT-ALTQTM 228
Cdd:PRK13548 183 ARQLAherGLAVIVvlhdlnlaaRY----------ADRIVLLHQGRLVADGTPAeVLTPET 233
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
27-224 |
2.08e-20 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 90.41 E-value: 2.08e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 27 TCTIRAGYVTGLVGPDGAGKTTLMRMLAGLLKPDEGRASVIGFDPLKDDSALHAVlGYMPQKFGLYEDLTVMEN--LTLY 104
Cdd:PRK10771 19 DLTVERGERVAILGPSGAGKSTLLNLIAGFLTPASGSLTLNGQDHTTTPPSRRPV-SMLFQENNLFSHLTVAQNigLGLN 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 105 ADLRsVTGEARKKIfDRLLEFTSLGPFTERLAGKLSGGMKQKLGLACTLVGDPKVLLLDEPGVGVDPISRRELWQMVHEL 184
Cdd:PRK10771 98 PGLK-LNAAQREKL-HAIARQMGIEDLLARLPGQLSGGQRQRVALARCLVREQPILLLDEPFSALDPALRQEMLTLVSQV 175
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 488984955 185 AGDGMLILWSTSY-LDEAEQCRD-VLLMNEGKLLYQGEPTAL 224
Cdd:PRK10771 176 CQERQLTLLMVSHsLEDAARIAPrSLVVADGRIAWDGPTDEL 217
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
4-165 |
2.15e-20 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 94.75 E-value: 2.15e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 4 TVIALNGLSRRFPgmDRPAVAPLTCTIRAGYVTGLVGPDGAGKTTLMRMLAGLLKPDEGRASVigfdplkddsALHAVLG 83
Cdd:COG0488 314 KVLELEGLSKSYG--DKTLLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPDSGTVKL----------GETVKIG 381
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 84 YMPQKF-GLYEDLTVMENLTLYAD------LRSVTGearkkifdRLLeFTslGPFTERLAGKLSGGMKQKLGLACTLVGD 156
Cdd:COG0488 382 YFDQHQeELDPDKTVLDELRDGAPggteqeVRGYLG--------RFL-FS--GDDAFKPVGVLSGGEKARLALAKLLLSP 450
|
....*....
gi 488984955 157 PKVLLLDEP 165
Cdd:COG0488 451 PNVLLLDEP 459
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
26-226 |
2.50e-20 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 90.46 E-value: 2.50e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 26 LTCTirAGYVTGLVGPDGAGKTTLMRMLAGLLKPDEGRASVIG--FD-----PLKDDSALHAVLGYMPQKFGLYEDLTVM 98
Cdd:COG4161 23 LECP--SGETLVLLGPSGAGKSSLLRVLNLLETPDSGQLNIAGhqFDfsqkpSEKAIRLLRQKVGMVFQQYNLWPHLTVM 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 99 ENLTlYADLRsVTG----EARKKIfDRLLEFTSLGPFTERLAGKLSGGMKQKLGLACTLVGDPKVLLLDEPGVGVDPISR 174
Cdd:COG4161 101 ENLI-EAPCK-VLGlskeQAREKA-MKLLARLRLTDKADRFPLHLSGGQQQRVAIARALMMEPQVLLFDEPTAALDPEIT 177
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 488984955 175 RELWQMVHELAGDGMLILWSTSYLDEAEQ-CRDVLLMNEGKLLYQGEPTALTQ 226
Cdd:COG4161 178 AQVVEIIRELSQTGITQVIVTHEVEFARKvASQVVYMEKGRIIEQGDASHFTQ 230
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
3-221 |
3.48e-20 |
|
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in methanogenesis, methyl coenzyme M reductase, contains alpha, beta, and gamma chains. In older literature, the complex of alpha, beta, and gamma chains was termed component C, while this single chain protein was termed methyl coenzyme M reductase system component A2. [Energy metabolism, Methanogenesis]
Pssm-ID: 132313 [Multi-domain] Cd Length: 520 Bit Score: 94.10 E-value: 3.48e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 3 ETVIALNGLSRRFPGMDR---PAVAPLTCTIRAGYVTGLVGPDGAGKTTLMRMLAGLLKPDEGRASVIGFDPLKDDSALH 79
Cdd:TIGR03269 277 EPIIKVRNVSKRYISVDRgvvKAVDNVSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGEVNVRVGDEWVDMTKPG 356
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 80 AV--------LGYMPQKFGLYEDLTVMENLTLYADLRSVTGEARKKIFDRLlefTSLGpFTE--------RLAGKLSGGM 143
Cdd:TIGR03269 357 PDgrgrakryIGILHQEYDLYPHRTVLDNLTEAIGLELPDELARMKAVITL---KMVG-FDEekaeeildKYPDELSEGE 432
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 144 KQKLGLACTLVGDPKVLLLDEPGVGVDPISRRELWQMVH----ELAGDGMLILWSTSYLDEAeqCRDVLLMNEGKLLYQG 219
Cdd:TIGR03269 433 RHRVALAQVLIKEPRIVILDEPTGTMDPITKVDVTHSILkareEMEQTFIIVSHDMDFVLDV--CDRAALMRDGKIVKIG 510
|
..
gi 488984955 220 EP 221
Cdd:TIGR03269 511 DP 512
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
8-191 |
3.51e-20 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 90.14 E-value: 3.51e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 8 LNGLSRRFPGmdRPAVAPLTCTIRAGYVTGLVGPDGAGKTTLMRMLAGLLKPDEGRASVIGfDPLKDDSALHAVLGympQ 87
Cdd:PRK11248 4 ISHLYADYGG--KPALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDG-KPVEGPGAERGVVF---Q 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 88 KFGLYEDLTVMENLTLYADLRSVTGEARKKIFDRLLEFTSLGPFTERLAGKLSGGMKQKLGLACTLVGDPKVLLLDEPGV 167
Cdd:PRK11248 78 NEGLLPWRNVQDNVAFGLQLAGVEKMQRLEIAHQMLKKVGLEGAEKRYIWQLSGGQRQRVGIARALAANPQLLLLDEPFG 157
|
170 180
....*....|....*....|....*...
gi 488984955 168 GVDPISRRE----LWQMVHELAGDGMLI 191
Cdd:PRK11248 158 ALDAFTREQmqtlLLKLWQETGKQVLLI 185
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
19-221 |
5.92e-20 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 89.69 E-value: 5.92e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 19 DRPAVAPLTCTIRAGYVTGLVGPDGAGKTTLMRMLAGLLKPDEGRASVIGfDPLKDDSA--LHAVLGYMPQKFGLYEDLT 96
Cdd:PRK11231 14 TKRILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGD-KPISMLSSrqLARRLALLPQHHLTPEGIT 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 97 VME--------NLTLYADLrsvtGEARKKIFDRLLEFTSLGPFTERLAGKLSGGMKQKLGLACTLVGDPKVLLLDEPGVG 168
Cdd:PRK11231 93 VRElvaygrspWLSLWGRL----SAEDNARVNQAMEQTRINHLADRRLTDLSGGQRQRAFLAMVLAQDTPVVLLDEPTTY 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 488984955 169 VDpISRR-ELWQMVHELAGDGMLILWSTSYLDEAEQ-CRDVLLMNEGKLLYQGEP 221
Cdd:PRK11231 169 LD-INHQvELMRLMRELNTQGKTVVTVLHDLNQASRyCDHLVVLANGHVMAQGTP 222
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
6-187 |
6.95e-20 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 93.31 E-value: 6.95e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 6 IALNGLSRRFPGmDRPAVAPLTCTIRAGYVTGLVGPDGAGKTTLMRMLAGLLKPDEGRasvIGFD--PLKD--DSALHAV 81
Cdd:COG1132 340 IEFENVSFSYPG-DRPVLKDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYDPTSGR---ILIDgvDIRDltLESLRRQ 415
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 82 LGYMPQKFGLYEDlTVMENLTLY------ADLRSVTGEArkkifdRLLEF---------TSLGpftERlAGKLSGGMKQK 146
Cdd:COG1132 416 IGVVPQDTFLFSG-TIRENIRYGrpdatdEEVEEAAKAA------QAHEFiealpdgydTVVG---ER-GVNLSGGQRQR 484
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 488984955 147 LGLACTLVGDPKVLLLDEPGVGVDPISRRELWQMVHELAGD 187
Cdd:COG1132 485 IAIARALLKDPPILILDEATSALDTETEALIQEALERLMKG 525
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
330-545 |
6.99e-20 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 88.92 E-value: 6.99e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 330 IEAQSLTKKFGDFAATDHVDFQVKRGEIFGLLGPNGAGKSTTFKMMCGLLVPTSGKALVLG--MDLKVSSG-KA----RQ 402
Cdd:PRK11124 3 IQLNGINCFYGAHQALFDITLDCPQGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLNIAGnhFDFSKTPSdKAirelRR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 403 HLGYMAQKFSLYGNLSVEQNL-----RffsgVYGLrgrAQNEKIARmsdAFGLKSIARHA--ADELPL----GYKQRLAL 471
Cdd:PRK11124 83 NVGMVFQQYNLWPHLTVQQNLieapcR----VLGL---SKDQALAR---AEKLLERLRLKpyADRFPLhlsgGQQQRVAI 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 488984955 472 ACSLMHEPDILFLDEPTSGVDPLTRREFWLHINSMVDKGVTVMVTTHfmdEAEYCDRIG--LVY--HGKLIASGTPDA 545
Cdd:PRK11124 153 ARALMMEPQVLLFDEPTAALDPEITAQIVSIIRELAETGITQVIVTH---EVEVARKTAsrVVYmeNGHIVEQGDASC 227
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
330-546 |
7.04e-20 |
|
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and metabolism]; ABC-type molybdate transport system, ATPase component ModC is part of the Pathway/BioSystem: Molybdopterin biosynthesis
Pssm-ID: 443319 [Multi-domain] Cd Length: 358 Bit Score: 91.32 E-value: 7.04e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 330 IEAQsLTKKFGDFAAtdHVDFQVKRGEIFGLLGPNGAGKSTTFKMMCGLLVPTSGKALVLGMDLkVSSGKA------RQH 403
Cdd:COG4148 3 LEVD-FRLRRGGFTL--DVDFTLPGRGVTALFGPSGSGKTTLLRAIAGLERPDSGRIRLGGEVL-QDSARGiflpphRRR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 404 LGYMAQKFSLYGNLSVEQNLRffsgvYGLRGRAQNEKIARMSDA---FGLKSIARHAADELPLGYKQRLALACSLMHEPD 480
Cdd:COG4148 79 IGYVFQEARLFPHLSVRGNLL-----YGRKRAPRAERRISFDEVvelLGIGHLLDRRPATLSGGERQRVAIGRALLSSPR 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 488984955 481 ILFLDEPTSGVDPLTRREFWLHINSMVDK-GVTVMVTTHFMDEAEY-CDRIGLVYHGKLIASGTPDAL 546
Cdd:COG4148 154 LLLMDEPLAALDLARKAEILPYLERLRDElDIPILYVSHSLDEVARlADHVVLLEQGRVVASGPLAEV 221
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
30-226 |
8.31e-20 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 93.19 E-value: 8.31e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 30 IRAGYVTGLVGPDGAGKTTLMRMLAGLLKPDEGRASVIGFDPLK-DDSALHAVLGYMPQKFGLYEDLTVMENLTLYADLR 108
Cdd:TIGR00955 48 AKPGELLAVMGSSGAGKTTLMNALAFRSPKGVKGSGSVLLNGMPiDAKEMRAISAYVQQDDLFIPTLTVREHLMFQAHLR 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 109 ---SVTGEARKKIFDRLLEFTSLGPFTERLAGK------LSGGMKQKLGLACTLVGDPKVLLLDEPGVGVDPISRRELWQ 179
Cdd:TIGR00955 128 mprRVTKKEKRERVDEVLQALGLRKCANTRIGVpgrvkgLSGGERKRLAFASELLTDPPLLFCDEPTSGLDSFMAYSVVQ 207
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 488984955 180 MVHELAGDGMLILWS----TSYLdeAEQCRDVLLMNEGKLLYQGEPTALTQ 226
Cdd:TIGR00955 208 VLKGLAQKGKTIICTihqpSSEL--FELFDKIILMAEGRVAYLGSPDQAVP 256
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
3-219 |
8.63e-20 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 89.30 E-value: 8.63e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 3 ETVIALNGLSRRFpgMDRPAVAPLTCTIRAGYVTGLVGPDGAGKTTLMRMLAGLLKPD---EGRASVIGFDP------LK 73
Cdd:PRK09984 2 QTIIRVEKLAKTF--NQHQALHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGLITGDksaGSHIELLGRTVqregrlAR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 74 DDSALHAVLGYMPQKFGLYEDLTVMENLTLYA---------DLRSVTGEARKKIFdRLLEFTSLGPFTERLAGKLSGGMK 144
Cdd:PRK09984 80 DIRKSRANTGYIFQQFNLVNRLSVLENVLIGAlgstpfwrtCFSWFTREQKQRAL-QALTRVGMVHFAHQRVSTLSGGQQ 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 488984955 145 QKLGLACTLVGDPKVLLLDEPGVGVDPISRRELWQMVHEL-AGDGMLILWSTSYLDEA-EQCRDVLLMNEGKLLYQG 219
Cdd:PRK09984 159 QRVAIARALMQQAKVILADEPIASLDPESARIVMDTLRDInQNDGITVVVTLHQVDYAlRYCERIVALRQGHVFYDG 235
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
330-547 |
1.25e-19 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 89.76 E-value: 1.25e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 330 IEAQSLTKKFG-----DFAATDHVDFQVKRGEIFGLLGPNGAGKSTTFKMMCGLLVPTSGK------------------- 385
Cdd:PRK13651 3 IKVKNIVKIFNkklptELKALDNVSVEINQGEFIAIIGQTGSGKTTFIEHLNALLLPDTGTiewifkdeknkkktkekek 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 386 ---ALVLGMDL--KVSSGKA-RQHLGYMAQkFSLYG--NLSVEQNLRFFSGVYGLRGRAQNEKIARMSDAFGL-KSIARH 456
Cdd:PRK13651 83 vleKLVIQKTRfkKIKKIKEiRRRVGVVFQ-FAEYQlfEQTIEKDIIFGPVSMGVSKEEAKKRAAKYIELVGLdESYLQR 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 457 AADELPLGYKQRLALACSLMHEPDILFLDEPTSGVDPLTRREFWLHINSMVDKGVTVMVTTHFMDEA-EYCDRIGLVYHG 535
Cdd:PRK13651 162 SPFELSGGQKRRVALAGILAMEPDFLVFDEPTAGLDPQGVKEILEIFDNLNKQGKTIILVTHDLDNVlEWTKRTIFFKDG 241
|
250
....*....|...
gi 488984955 536 KLIASG-TPDALK 547
Cdd:PRK13651 242 KIIKDGdTYDILS 254
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
348-535 |
1.43e-19 |
|
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: 86.84 E-value: 1.43e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 348 VDFQVKRGEIFGLLGPNGAGKSTTFKMMCGLLVP--TSGKALVLGMDLKVSSGKARqhLGYMAQKFSLYGNLSVEQNLRF 425
Cdd:cd03213 28 VSGKAKPGELTAIMGPSGAGKSTLLNALAGRRTGlgVSGEVLINGRPLDKRSFRKI--IGYVPQDDILHPTLTVRETLMF 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 426 FSGVYGLRGraqnekiarmsdafglksiarhaadelplGYKQRLALACSLMHEPDILFLDEPTSGVDPLTRREFWLHINS 505
Cdd:cd03213 106 AAKLRGLSG-----------------------------GERKRVSIALELVSNPSLLFLDEPTSGLDSSSALQVMSLLRR 156
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 488984955 506 MVDKGVTVMVTTH------FmdeaEYCDRI------GLVYHG 535
Cdd:cd03213 157 LADTGRTIICSIHqpsseiF----ELFDKLlllsqgRVIYFG 194
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
330-549 |
1.55e-19 |
|
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The amino terminal domain (pfam03412) processes the N-terminal leader peptide from the bacteriocin while C-terminal domains resemble ABC transporter membrane protein and ATP-binding cassette domain. In general, bacteriocins are agents which are responsible for killing or inhibiting the closely related species or even different strains of the same species. Bacteriocins are usually encoded by bacterial plasmids. Bacteriocins are named after the species and hence in literature one encounters various names e.g., leucocin from Leuconostic geldium; pedicocin from Pedicoccus acidilactici; sakacin from Lactobacillus sake etc. [Protein fate, Protein and peptide secretion and trafficking, Protein fate, Protein modification and repair, Transport and binding proteins, Other]
Pssm-ID: 130261 [Multi-domain] Cd Length: 708 Bit Score: 92.50 E-value: 1.55e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 330 IEAQSLTKKFGDFA-ATDHVDFQVKRGEIFGLLGPNGAGKSTTFKMMCGLLVPTSGKALVLGMDLK-VSSGKARQHLGYM 407
Cdd:TIGR01193 474 IVINDVSYSYGYGSnILSDISLTIKMNSKTTIVGMSGSGKSTLAKLLVGFFQARSGEILLNGFSLKdIDRHTLRQFINYL 553
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 408 AQKFSLYGNlSVEQNLrffsgVYGLRGRAQNEKIARMSDafglksIARHAAD--ELPLGY---------------KQRLA 470
Cdd:TIGR01193 554 PQEPYIFSG-SILENL-----LLGAKENVSQDEIWAACE------IAEIKDDieNMPLGYqtelseegssisggqKQRIA 621
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 488984955 471 LACSLMHEPDILFLDEPTSGVDPLTRREFWLHINSMVDKgvTVMVTTHFMDEAEYCDRIGLVYHGKLIASGTPDALKAQ 549
Cdd:TIGR01193 622 LARALLTDSKVLILDESTSNLDTITEKKIVNNLLNLQDK--TIIFVAHRLSVAKQSDKIIVLDHGKIIEQGSHDELLDR 698
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
330-518 |
2.11e-19 |
|
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: 86.64 E-value: 2.11e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 330 IEAQSLTKKFGDFAATDHVDFQVKRGEIFGLLGPNGAGKSTTFKMMCGLLVPTSGKALVLGMDLKVSSGKARQHLGYMAQ 409
Cdd:TIGR01189 1 LAARNLACSRGERMLFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRWNGTPLAEQRDEPHENILYLGH 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 410 KFSLYGNLSVEQNLRFFSGVYGLRGRAQNEKIARMsdafGLKSIARHAADELPLGYKQRLALACSLMHEPDILFLDEPTS 489
Cdd:TIGR01189 81 LPGLKPELSALENLHFWAAIHGGAQRTIEDALAAV----GLTGFEDLPAAQLSAGQQRRLALARLWLSRRPLWILDEPTT 156
|
170 180
....*....|....*....|....*....
gi 488984955 490 GVDPLTRREFWLHINSMVDKGVTVMVTTH 518
Cdd:TIGR01189 157 ALDKAGVALLAGLLRAHLARGGIVLLTTH 185
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
330-518 |
2.24e-19 |
|
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: 86.39 E-value: 2.24e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 330 IEAQSLTKKFGDFAATDHVDFQVKRGEIFGLLGPNGAGKSTTFKMMCGLLVPTSGKALVLGMDLKVSSGKARQHLGYMAQ 409
Cdd:cd03231 1 LEADELTCERDGRALFSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNGGPLDFQRDSIARGLLYLGH 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 410 KFSLYGNLSVEQNLRFFSGVYGlrgraqNEKIARMSDAFGLKSIARHAADELPLGYKQRLALACSLMHEPDILFLDEPTS 489
Cdd:cd03231 81 APGIKTTLSVLENLRFWHADHS------DEQVEEALARVGLNGFEDRPVAQLSAGQQRRVALARLLLSGRPLWILDEPTT 154
|
170 180
....*....|....*....|....*....
gi 488984955 490 GVDPLTRREFWLHINSMVDKGVTVMVTTH 518
Cdd:cd03231 155 ALDKAGVARFAEAMAGHCARGGMVVLTTH 183
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
29-247 |
2.61e-19 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 87.46 E-value: 2.61e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 29 TIRAGYVTGLVGPDGAGKTTLMRMLAGLLKPDEGRASVIGF---DPLKDDSALHAVLGYMPQKFGLYEDLTVMENLTLYA 105
Cdd:PRK09493 23 NIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGLkvnDPKVDERLIRQEAGMVFQQFYLFPHLTALENVMFGP 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 106 -DLRSVTGEARKKIFDRLLEFTSLGPFTERLAGKLSGGMKQKLGLACTLVGDPKVLLLDEPGVGVDPISRRELWQMVHEL 184
Cdd:PRK09493 103 lRVRGASKEEAEKQARELLAKVGLAERAHHYPSELSGGQQQRVAIARALAVKPKLMLFDEPTSALDPELRHEVLKVMQDL 182
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 488984955 185 AGDGMLILWSTSYLDEAEQCRDVLL-MNEGKLLYQGEPTALTQTmagrsflvsSPQENNRRLLQ 247
Cdd:PRK09493 183 AEEGMTMVIVTHEIGFAEKVASRLIfIDKGRIAEDGDPQVLIKN---------PPSQRLQEFLQ 237
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
16-221 |
3.28e-19 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 88.18 E-value: 3.28e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 16 PGM--DRPAVAPLTCTIRAGYVTGLVGPDGAGKTTLMRMLAGLLKPDEGRASVIGFDPLKDDSALHAVlgymPQKFGL-- 91
Cdd:PRK13637 14 EGTpfEKKALDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDGVDITDKKVKLSDI----RKKVGLvf 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 92 -YEDLTVMENlTLYADLR---SVTGEARKKIFDRLLEFTSL-GPFTERLAGK----LSGGMKQKLGLACTLVGDPKVLLL 162
Cdd:PRK13637 90 qYPEYQLFEE-TIEKDIAfgpINLGLSEEEIENRVKRAMNIvGLDYEDYKDKspfeLSGGQKRRVAIAGVVAMEPKILIL 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 488984955 163 DEPGVGVDPISRRELWQMVHELAGD-GM-LILWSTSYLDEAEQCRDVLLMNEGKLLYQGEP 221
Cdd:PRK13637 169 DEPTAGLDPKGRDEILNKIKELHKEyNMtIILVSHSMEDVAKLADRIIVMNKGKCELQGTP 229
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
1-165 |
4.15e-19 |
|
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase component [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 443338 [Multi-domain] Cd Length: 233 Bit Score: 86.72 E-value: 4.15e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 1 MSETVIALNGLSRRFPGMDRPAVA--PLTCTIRAGYVTGLVGPDGAGKTTLMRMLAGLLKPDEGRASVIG--FDPLKDDs 76
Cdd:COG4181 4 SSAPIIELRGLTKTVGTGAGELTIlkGISLEVEAGESVAIVGASGSGKSTLLGLLAGLDRPTSGTVRLAGqdLFALDED- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 77 ALHAV----LGYMPQKFGLYEDLTVMENLTLYADLRSVtGEARKKIfDRLLEFTSLGpftERLA---GKLSGGMKQKLGL 149
Cdd:COG4181 83 ARARLrarhVGFVFQSFQLLPTLTALENVMLPLELAGR-RDARARA-RALLERVGLG---HRLDhypAQLSGGEQQRVAL 157
|
170
....*....|....*.
gi 488984955 150 ACTLVGDPKVLLLDEP 165
Cdd:COG4181 158 ARAFATEPAILFADEP 173
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
29-210 |
4.17e-19 |
|
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: 86.37 E-value: 4.17e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 29 TIRAGYVTGLVGPDGAGKTTLMRMLAGLLKPDEGRASVIGFDPLKDDSALHAVLgympQKFGLYEDLTVMENLTLYAD-- 106
Cdd:TIGR01184 7 TIQQGEFISLIGHSGCGKSTLLNLISGLAQPTSGGVILEGKQITEPGPDRMVVF----QNYSLLPWLTVRENIALAVDrv 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 107 LRSVTGEARKKIFDRLLEFTSLGPFTERLAGKLSGGMKQKLGLACTLVGDPKVLLLDEPGVGVDPISRRELWQMVHELAG 186
Cdd:TIGR01184 83 LPDLSKSERRAIVEEHIALVGLTEAADKRPGQLSGGMKQRVAIARALSIRPKVLLLDEPFGALDALTRGNLQEELMQIWE 162
|
170 180
....*....|....*....|....*
gi 488984955 187 D-GMLILWSTSYLDEAEQCRDVLLM 210
Cdd:TIGR01184 163 EhRVTVLMVTHDVDEALLLSDRVVM 187
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
1-184 |
5.60e-19 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 86.58 E-value: 5.60e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 1 MSETVIALNGLSRRFPGMdrPAVAPLTCTIRAGYVTGLVGPDGAGKTTLMRMLAGLLKPDEGRAsvigfdpLKDDSALHA 80
Cdd:PRK11300 1 MSQPLLSVSGLMMRFGGL--LAVNNVNLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTI-------LLRGQHIEG 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 81 VLGYMPQKFG---------LYEDLTVMENLtLYADLRSV-TG------------EARKKIFDRL---LEFTSLGPFTERL 135
Cdd:PRK11300 72 LPGHQIARMGvvrtfqhvrLFREMTVIENL-LVAQHQQLkTGlfsgllktpafrRAESEALDRAatwLERVGLLEHANRQ 150
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 488984955 136 AGKLSGGMKQKLGLACTLVGDPKVLLLDEPGVGVDPISRRELWQMVHEL 184
Cdd:PRK11300 151 AGNLAYGQQRRLEIARCMVTQPEILMLDEPAAGLNPKETKELDELIAEL 199
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
11-221 |
6.18e-19 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 88.74 E-value: 6.18e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 11 LSRRFPGmdRPAVAPLTCTIRAGYVTGLVGPDGAGKTTLMRMLAGLLKPDEGRASVIGFDpLKDDSALHAVLGYMPQKFG 90
Cdd:PRK11607 25 LTKSFDG--QHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVD-LSHVPPYQRPINMMFQSYA 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 91 LYEDLTVMENLT--LYADlRSVTGEARKKIfDRLLEFTSLGPFTERLAGKLSGGMKQKLGLACTLVGDPKVLLLDEPGVG 168
Cdd:PRK11607 102 LFPHMTVEQNIAfgLKQD-KLPKAEIASRV-NEMLGLVHMQEFAKRKPHQLSGGQRQRVALARSLAKRPKLLLLDEPMGA 179
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 488984955 169 VDPISR-RELWQMVHELAGDGMLILWSTSYLDEA-EQCRDVLLMNEGKLLYQGEP 221
Cdd:PRK11607 180 LDKKLRdRMQLEVVDILERVGVTCVMVTHDQEEAmTMAGRIAIMNRGKFVQIGEP 234
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
323-546 |
6.19e-19 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 86.64 E-value: 6.19e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 323 GSKEETVIEAQSLTKKFGDFAATDHVDFQVKRGEIFGLLGPNGAGKSTTFKMMCGLL------VPTSGKALVLGMDL-KV 395
Cdd:PRK14246 4 GKSAEDVFNISRLYLYINDKAILKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLIeiydskIKVDGKVLYFGKDIfQI 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 396 SSGKARQHLGYMAQKFSLYGNLSVEQNLRFFSGVYGLRGRAQNEKIARMS-DAFGL-KSI---ARHAADELPLGYKQRLA 470
Cdd:PRK14246 84 DAIKLRKEVGMVFQQPNPFPHLSIYDNIAYPLKSHGIKEKREIKKIVEEClRKVGLwKEVydrLNSPASQLSGGQQQRLT 163
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 488984955 471 LACSLMHEPDILFLDEPTSGVDPLTRREFWLHINSMVDKGVTVMVTTHFMDEAEYCDRIGLVYHGKLIASGTPDAL 546
Cdd:PRK14246 164 IARALALKPKVLLMDEPTSMIDIVNSQAIEKLITELKNEIAIVIVSHNPQQVARVADYVAFLYNGELVEWGSSNEI 239
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
340-518 |
7.26e-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: 90.11 E-value: 7.26e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 340 GDFAATDHVDFQVKRGEIFGLLGPNGAGKSTTFKMMCGLLVPTSGKALVLGMDL-KVSSGKARQHLGYMAQKFSLYGNlS 418
Cdd:TIGR02868 346 GAPPVLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPLQGEVTLDGVPVsSLDQDEVRRRVSVCAQDAHLFDT-T 424
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 419 VEQNLRFfsgvygLRGRAQNEKIARMSDAFGLKSIARhaadELPLGY---------------KQRLALACSLMHEPDILF 483
Cdd:TIGR02868 425 VRENLRL------ARPDATDEELWAALERVGLADWLR----ALPDGLdtvlgeggarlsggeRQRLALARALLADAPILL 494
|
170 180 190
....*....|....*....|....*....|....*
gi 488984955 484 LDEPTSGVDPLTRREFwLHINSMVDKGVTVMVTTH 518
Cdd:TIGR02868 495 LDEPTEHLDAETADEL-LEDLLAALSGRTVVLITH 528
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
6-195 |
8.40e-19 |
|
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where FtsE is the ATPase and the membrane subunit FtsX resembles a permease subunit. But rather than transporting any substrate, the complex acts in cell division by undergoing conformational changes that alter the activity of cell wall hydrolases located outside the plasma membrane. The complex is widely conserved in bacteria, but also extremely divergent in sequence between different lineages
Pssm-ID: 213259 [Multi-domain] Cd Length: 214 Bit Score: 85.15 E-value: 8.40e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 6 IALNGLSRRFPGMdRPAVAPLTCTIRAGYVTGLVGPDGAGKTTLMRMLAGLLKPDEGRASVIGFD--PLKDDSA--LHAV 81
Cdd:cd03292 1 IEFINVTKTYPNG-TAALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQDvsDLRGRAIpyLRRK 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 82 LGYMPQKFGLYEDLTVMENLTLyaDLRsVTGEARKKIFDR---LLEFTSLGPFTERLAGKLSGGMKQKLGLACTLVGDPK 158
Cdd:cd03292 80 IGVVFQDFRLLPDRNVYENVAF--ALE-VTGVPPREIRKRvpaALELVGLSHKHRALPAELSGGEQQRVAIARAIVNSPT 156
|
170 180 190
....*....|....*....|....*....|....*..
gi 488984955 159 VLLLDEPGVGVDPISRRELWQMVHELAGDGMLILWST 195
Cdd:cd03292 157 ILIADEPTGNLDPDTTWEIMNLLKKINKAGTTVVVAT 193
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
330-543 |
8.66e-19 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 86.58 E-value: 8.66e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 330 IEAQSLTKKFGDFAATDHVDFQVKRGEIFGLLGPNGAGKSTTFKMMCGLLVPTSGKALVLGMDLK-VSSGKARQHLGYMA 408
Cdd:PRK10253 8 LRGEQLTLGYGKYTVAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIQhYASKEVARRIGLLA 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 409 QKFSLYGNLSVEQNL---RFFSGVYGLRGRAQNEK-IARMSDAFGLKSIARHAADELPLGYKQRLALACSLMHEPDILFL 484
Cdd:PRK10253 88 QNATTPGDITVQELVargRYPHQPLFTRWRKEDEEaVTKAMQATGITHLADQSVDTLSGGQRQRAWIAMVLAQETAIMLL 167
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 488984955 485 DEPTSgvdpltrrefWLHINSMVD-----------KGVTVMVTTHFMDEA-EYCDRIGLVYHGKLIASGTP 543
Cdd:PRK10253 168 DEPTT----------WLDISHQIDllellselnreKGYTLAAVLHDLNQAcRYASHLIALREGKIVAQGAP 228
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
19-224 |
1.13e-18 |
|
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: 85.36 E-value: 1.13e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 19 DRPAVAPLTCTIRAGYVTGLVGPDGAGKTTLMRMLAGLLKPDEGRASVIGFDpLK--DDSALHAVLGYMPQKFGLYEDlT 96
Cdd:cd03253 13 GRPVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDGQD-IRevTLDSLRRAIGVVPQDTVLFND-T 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 97 VMENLtLYADLrSVTGE----ARKK--IFDRLLEF-----TSLGpftERlaG-KLSGGMKQKLGLACTLVGDPKVLLLDE 164
Cdd:cd03253 91 IGYNI-RYGRP-DATDEevieAAKAaqIHDKIMRFpdgydTIVG---ER--GlKLSGGEKQRVAIARAILKNPPILLLDE 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 165 PGVGVDPISRRELWQMVHELAGDGMLILwSTSYLDEAEQCRDVLLMNEGKLLYQGEPTAL 224
Cdd:cd03253 164 ATSALDTHTEREIQAALRDVSKGRTTIV-IAHRLSTIVNADKIIVLKDGRIVERGTHEEL 222
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
355-546 |
1.38e-18 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 85.99 E-value: 1.38e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 355 GEIFGLLGPNGAGKSTTFKMMCGLLVPTSGKALVLGMDLKVSSGK--ARQhLGYMAQKFSLYGNLSVEQNL---RF-FSG 428
Cdd:PRK10575 37 GKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPLESWSSKafARK-VAYLPQQLPAAEGMTVRELVaigRYpWHG 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 429 VYGLRGRAQNEKIARMSDAFGLKSIARHAADELPLGYKQRLALACSLMHEPDILFLDEPTSGVDPLTRREFWLHINSMV- 507
Cdd:PRK10575 116 ALGRFGAADREKVEEAISLVGLKPLAHRLVDSLSGGERQRAWIAMLVAQDSRCLLLDEPTSALDIAHQVDVLALVHRLSq 195
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 488984955 508 DKGVTVMVTTHFMD-EAEYCDRIGLVYHGKLIASGTPDAL 546
Cdd:PRK10575 196 ERGLTVIAVLHDINmAARYCDYLVALRGGEMIAQGTPAEL 235
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
346-549 |
1.46e-18 |
|
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: 85.28 E-value: 1.46e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 346 DHVDFQVKRGEIFGLLGPNGAGKSTTFKMMCGLLVPTSGKALVLGMDLK-VSSGKARQHLGYMAQKFSLYgNLSVEQNLR 424
Cdd:cd03249 20 KGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEILLDGVDIRdLNLRWLRSQIGLVSQEPVLF-DGTIAENIR 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 425 ffsgvYGLRGRAQNEKIARMSDAFGLKSIArhaadELPLGY---------------KQRLALACSLMHEPDILFLDEPTS 489
Cdd:cd03249 99 -----YGKPDATDEEVEEAAKKANIHDFIM-----SLPDGYdtlvgergsqlsggqKQRIAIARALLRNPKILLLDEATS 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 488984955 490 GVDPLTRREfwlhINSMVD---KGVTVMVTTHFMDEAEYCDRIGLVYHGKLIASGTPDALKAQ 549
Cdd:cd03249 169 ALDAESEKL----VQEALDramKGRTTIVIAHRLSTIRNADLIAVLQNGQVVEQGTHDELMAQ 227
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
348-566 |
1.46e-18 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 85.83 E-value: 1.46e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 348 VDFQvkRGEIFGLLGPNGAGKSTTFKMMCGLLVPTSGKALVLGMDLKVSSgkaRQHLGYMAQKFSLYGNlsVEQNLrFFS 427
Cdd:PRK13638 22 LDFS--LSPVTGLVGANGCGKSTLFMNLSGLLRPQKGAVLWQGKPLDYSK---RGLLALRQQVATVFQD--PEQQI-FYT 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 428 GV-----YGLR--GRAQNEKIARMSDAFGLKSiARHAADE----LPLGYKQRLALACSLMHEPDILFLDEPTSGVDPLTR 496
Cdd:PRK13638 94 DIdsdiaFSLRnlGVPEAEITRRVDEALTLVD-AQHFRHQpiqcLSHGQKKRVAIAGALVLQARYLLLDEPTAGLDPAGR 172
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 488984955 497 REFWLHINSMVDKGVTVMVTTHFMDEA-EYCDRIGLVYHGKLIASGTPDALKAQAAddsqtdpTMEQAFIT 566
Cdd:PRK13638 173 TQMIAIIRRIVAQGNHVIISSHDIDLIyEISDAVYVLRQGQILTHGAPGEVFACTE-------AMEQAGLT 236
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
347-552 |
1.55e-18 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 86.23 E-value: 1.55e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 347 HVDFQVKRGEIFGLLGPNGAGKSTTFKMMCGLLVPTSGKaLVLGmDLKVSSGKARQHLGYMAQKFSLYGNL--------S 418
Cdd:PRK13634 25 DVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGT-VTIG-ERVITAGKKNKKLKPLRKKVGIVFQFpehqlfeeT 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 419 VEQNLRFFSGVYGLRGRAQNEKIARMSDAFGL-KSIARHAADELPLGYKQRLALACSLMHEPDILFLDEPTSGVDPLTRR 497
Cdd:PRK13634 103 VEKDICFGPMNFGVSEEDAKQKAREMIELVGLpEELLARSPFELSGGQMRRVAIAGVLAMEPEVLVLDEPTAGLDPKGRK 182
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 488984955 498 E----FW-LHinsmVDKGVTVMVTTHFMDE-AEYCDRIGLVYHGKLIASGTPDALKAQAAD 552
Cdd:PRK13634 183 EmmemFYkLH----KEKGLTTVLVTHSMEDaARYADQIVVMHKGTVFLQGTPREIFADPDE 239
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
348-499 |
1.84e-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: 1.84e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 348 VDFQVKRGEIFGLLGPNGAGKSTTFKMMCGLLVP---TSGKALVLGMDLkvSSGKARQ-HLGYMAQKFSLYGNLSVEQNL 423
Cdd:COG4136 20 LSLTVAPGEILTLMGPSGSGKSTLLAAIAGTLSPafsASGEVLLNGRRL--TALPAEQrRIGILFQDDLLFPHLSVGENL 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 424 RFfsgvyGL----RGRAQNEKIARMSDAFGLKSIARHAADELPLGYKQRLALACSLMHEPDILFLDEPTSGVDPLTRREF 499
Cdd:COG4136 98 AF-----ALpptiGRAQRRARVEQALEEAGLAGFADRDPATLSGGQRARVALLRALLAEPRALLLDEPFSKLDAALRAQF 172
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
322-544 |
2.35e-18 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 85.09 E-value: 2.35e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 322 DGSKEETVIEAQSLTKKFGDFAATDHVDFQVKRGEIFGLLGPNGAGKSTTFKMMCGL--LVP---TSGKALVLGMDL--- 393
Cdd:COG1117 4 PASTLEPKIEVRNLNVYYGDKQALKDINLDIPENKVTALIGPSGCGKSTLLRCLNRMndLIPgarVEGEILLDGEDIydp 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 394 KVSSGKARQHLGYMAQK-----FSLYGNlsVEQNLRffsgVYGLRGRAQNEKIARMSdafgLksiaRHAA--DE------ 460
Cdd:COG1117 84 DVDVVELRRRVGMVFQKpnpfpKSIYDN--VAYGLR----LHGIKSKSELDEIVEES----L----RKAAlwDEvkdrlk 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 461 -----LPLGYKQRLALACSLMHEPDILFLDEPTSGVDPL-TRR--EFwlhINSMVDKgVTVMVTTHFMDEAEYC-DRIGL 531
Cdd:COG1117 150 ksalgLSGGQQQRLCIARALAVEPEVLLMDEPTSALDPIsTAKieEL---ILELKKD-YTIVIVTHNMQQAARVsDYTAF 225
|
250
....*....|...
gi 488984955 532 VYHGKLIASGTPD 544
Cdd:COG1117 226 FYLGELVEFGPTE 238
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
329-552 |
3.11e-18 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 85.14 E-value: 3.11e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 329 VIEAQSLTKKF---GDFAATDHVDFQVKRGEIFGLLGPNGAGKSTTFKMMCGLLVPTSGKALVLGMDLKVSS-GKARQHL 404
Cdd:PRK13642 4 ILEVENLVFKYekeSDVNQLNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDGELLTAENvWNLRRKI 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 405 GYMAQK-FSLYGNLSVEQNLRFfsgvyGL--RGRAQNEKIARMSDAF---GLKSIARHAADELPLGYKQRLALACSLMHE 478
Cdd:PRK13642 84 GMVFQNpDNQFVGATVEDDVAF-----GMenQGIPREEMIKRVDEALlavNMLDFKTREPARLSGGQKQRVAVAGIIALR 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 488984955 479 PDILFLDEPTSGVDPLTRREFWLHINSMVDK-GVTVMVTTHFMDEAEYCDRIGLVYHGKLIASGTPDALKAQAAD 552
Cdd:PRK13642 159 PEIIILDESTSMLDPTGRQEIMRVIHEIKEKyQLTVLSITHDLDEAASSDRILVMKAGEIIKEAAPSELFATSED 233
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
346-535 |
3.17e-18 |
|
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: 84.05 E-value: 3.17e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 346 DHVDFQVKRGEIFGLLGPNGAGKSTTFKMMCGLLVPTSGKALVLGMDLKvSSGKARQhlgYMAQKFSLYGNLSVEQNLRF 425
Cdd:TIGR01184 2 KGVNLTIQQGEFISLIGHSGCGKSTLLNLISGLAQPTSGGVILEGKQIT-EPGPDRM---VVFQNYSLLPWLTVRENIAL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 426 -FSGVYGLRGRAQNEKIARMS-DAFGLKSIARHAADELPLGYKQRLALACSLMHEPDILFLDEPTSGVDPLTRREFWLHI 503
Cdd:TIGR01184 78 aVDRVLPDLSKSERRAIVEEHiALVGLTEAADKRPGQLSGGMKQRVAIARALSIRPKVLLLDEPFGALDALTRGNLQEEL 157
|
170 180 190
....*....|....*....|....*....|....
gi 488984955 504 NSMV-DKGVTVMVTTHFMDEAEY-CDRIGLVYHG 535
Cdd:TIGR01184 158 MQIWeEHRVTVLMVTHDVDEALLlSDRVVMLTNG 191
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
6-215 |
3.66e-18 |
|
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: 81.71 E-value: 3.66e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 6 IALNGLSRRFPGMdrPAVAPLTCTIRAGYVTGLVGPDGAGKTTLMRMLAGLLKPDEGRASVIGfDPLKDDSALHAvlgym 85
Cdd:cd03216 1 LELRGITKRFGGV--KALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVDG-KEVSFASPRDA----- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 86 pQKFGLYedlTVMEnltlyadlrsvtgearkkifdrlleftslgpfterlagkLSGGMKQKLGLACTLVGDPKVLLLDEP 165
Cdd:cd03216 73 -RRAGIA---MVYQ---------------------------------------LSVGERQMVEIARALARNARLLILDEP 109
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 488984955 166 GVGVDPISRRELWQMVHELAGDGMLILWSTSYLDEAEQ-CRDVLLMNEGKL 215
Cdd:cd03216 110 TAALTPAEVERLFKVIRRLRAQGVAVIFISHRLDEVFEiADRVTVLRDGRV 160
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
5-221 |
4.00e-18 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 84.67 E-value: 4.00e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 5 VIALNGLSRRFpgMDRPAVAPLTCTIRAGYVTGLVGPDGAGKTTLMRMLAGLLKPDEGRASVIGfDPLkdDSALHAVLGY 84
Cdd:PRK13638 1 MLATSDLWFRY--QDEPVLKGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLRPQKGAVLWQG-KPL--DYSKRGLLAL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 85 MPQKFGLYEDltvMENLTLYADLRSVT-------GEARKKIFDRLLEFTSL---GPFTERLAGKLSGGMKQKLGLACTLV 154
Cdd:PRK13638 76 RQQVATVFQD---PEQQIFYTDIDSDIafslrnlGVPEAEITRRVDEALTLvdaQHFRHQPIQCLSHGQKKRVAIAGALV 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 488984955 155 GDPKVLLLDEPGVGVDPISRRELWQMVHELAGDGMLILWSTSYLDEAEQCRD-VLLMNEGKLLYQGEP 221
Cdd:PRK13638 153 LQARYLLLDEPTAGLDPAGRTQMIAIIRRIVAQGNHVIISSHDIDLIYEISDaVYVLRQGQILTHGAP 220
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
19-226 |
4.39e-18 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 84.80 E-value: 4.39e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 19 DRPAVAPLTCTIRAGYVTGLVGPDGAGKTTLMRMLAGLLKPDEGRASVIGFDPL-----KDDSALHAVLGYMPQ--KFGL 91
Cdd:PRK13649 19 EGRALFDVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDDTLITstsknKDIKQIRKKVGLVFQfpESQL 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 92 YEDlTVMENLTLYADLRSVTGE-----ARKKIfdRLL----EFTSLGPFterlagKLSGGMKQKLGLACTLVGDPKVLLL 162
Cdd:PRK13649 99 FEE-TVLKDVAFGPQNFGVSQEeaealAREKL--ALVgiseSLFEKNPF------ELSGGQMRRVAIAGILAMEPKILVL 169
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 488984955 163 DEPGVGVDPISRRELWQMVHELAGDGMLILWSTSYLDEAEQCRD-VLLMNEGKLLYQGEPTALTQ 226
Cdd:PRK13649 170 DEPTAGLDPKGRKELMTLFKKLHQSGMTIVLVTHLMDDVANYADfVYVLEKGKLVLSGKPKDIFQ 234
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
327-546 |
4.42e-18 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 84.25 E-value: 4.42e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 327 ETVIEAQSLTKKFGDFAATDHVDFQVKRGEIFGLLGPNGAGKSTTFKMMCGLLVPTSGKALVLGMD----------LKVS 396
Cdd:PRK10619 3 ENKLNVIDLHKRYGEHEVLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNGQTinlvrdkdgqLKVA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 397 SGKA----RQHLGYMAQKFSLYGNLSVEQN-LRFFSGVYGLRGRAQNEKIARMSDAFGLKSIARHA-ADELPLGYKQRLA 470
Cdd:PRK10619 83 DKNQlrllRTRLTMVFQHFNLWSHMTVLENvMEAPIQVLGLSKQEARERAVKYLAKVGIDERAQGKyPVHLSGGQQQRVS 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 488984955 471 LACSLMHEPDILFLDEPTSGVDPLTRREFWLHINSMVDKGVTVMVTTHFMDEAEYC-DRIGLVYHGKLIASGTPDAL 546
Cdd:PRK10619 163 IARALAMEPEVLLFDEPTSALDPELVGEVLRIMQQLAEEGKTMVVVTHEMGFARHVsSHVIFLHQGKIEEEGAPEQL 239
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
343-529 |
4.53e-18 |
|
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: 87.34 E-value: 4.53e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 343 AATDHVDFQVKRGEIFGLLGPNGAGKSTTFKMMCGLLVPTSGKALVLGMDLKVSSGKA-RQHLGYMAQKFSLYgNLSVEQ 421
Cdd:TIGR02857 336 PALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSIAVNGVPLADADADSwRDQIAWVPQHPFLF-AGTIAE 414
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 422 NLRFFsgvyglRGRAQNEKIARMSDAFGLKSIARhaadELPLGY---------------KQRLALACSLMHEPDILFLDE 486
Cdd:TIGR02857 415 NIRLA------RPDASDAEIREALERAGLDEFVA----ALPQGLdtpigeggaglsggqAQRLALARAFLRDAPLLLLDE 484
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 488984955 487 PTSGVDPLTRREFwlhINSMVD--KGVTVMVTTHFMDEAEYCDRI 529
Cdd:TIGR02857 485 PTAHLDAETEAEV---LEALRAlaQGRTVLLVTHRLALAALADRI 526
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
2-184 |
5.08e-18 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 84.43 E-value: 5.08e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 2 SETVIALNGLSrrFPGMDRPAVAPLTCTIRAGYVTGLVGPDGAGKTTLMRMLAGLLKPDEGRasvIGFD----PLKDDSA 77
Cdd:PRK11831 4 VANLVDMRGVS--FTRGNRCIFDNISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGE---ILFDgeniPAMSRSR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 78 LHAVLGYMPQKF---GLYEDLTVMENLTLyaDLRSVT---GEARKKIFDRLLEFTSLGPFTERLAGKLSGGMKQKLGLAC 151
Cdd:PRK11831 79 LYTVRKRMSMLFqsgALFTDMNVFDNVAY--PLREHTqlpAPLLHSTVMMKLEAVGLRGAAKLMPSELSGGMARRAALAR 156
|
170 180 190
....*....|....*....|....*....|...
gi 488984955 152 TLVGDPKVLLLDEPGVGVDPISRRELWQMVHEL 184
Cdd:PRK11831 157 AIALEPDLIMFDEPFVGQDPITMGVLVKLISEL 189
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
37-492 |
5.31e-18 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 87.48 E-value: 5.31e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 37 GLVGPDGAGKTTLMRMLAGLLKPDEGRASVigfdplkddsALHAVLGYMPQKFGLYEDLTVMENL--------------- 101
Cdd:PRK11819 37 GVLGLNGAGKSTLLRIMAGVDKEFEGEARP----------APGIKVGYLPQEPQLDPEKTVRENVeegvaevkaaldrfn 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 102 ---TLYAD-------LRSVTGEARKKI-------FDRLLEFT--SLG-PFTERLAGKLSGGMKQKLGLACTLVGDPKVLL 161
Cdd:PRK11819 107 eiyAAYAEpdadfdaLAAEQGELQEIIdaadawdLDSQLEIAmdALRcPPWDAKVTKLSGGERRRVALCRLLLEKPDMLL 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 162 LDEPGVGVDPISRRELWQMVHELAG-------D----------------GMLILWS---TSYLdEAEQCRdvlLMNEGKl 215
Cdd:PRK11819 187 LDEPTNHLDAESVAWLEQFLHDYPGtvvavthDryfldnvagwileldrGRGIPWEgnySSWL-EQKAKR---LAQEEK- 261
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 216 lyqgeptaltqtmagrsflvsspQENNRrllQRALK--LPQVSDG--VIQGKS-VRLilkkdARIEEVQQhgdmpplQVA 290
Cdd:PRK11819 262 -----------------------QEAAR---QKALKreLEWVRQSpkARQAKSkARL-----ARYEELLS-------EEY 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 291 DTAPRFEDAFIdllggagtaesPLGAiihRVdGSKeetVIEAQSLTKKFGDFAATDHVDFQVKRGEIFGLLGPNGAGKST 370
Cdd:PRK11819 304 QKRNETNEIFI-----------PPGP---RL-GDK---VIEAENLSKSFGDRLLIDDLSFSLPPGGIVGIIGPNGAGKST 365
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 371 TFKMMCGLLVPTSGkALVLGMDLKVSSgkARQHLGYMAQKFSLYGNLS----------VEQNLRFFSGVYGLRGRAQNEK 440
Cdd:PRK11819 366 LFKMITGQEQPDSG-TIKIGETVKLAY--VDQSRDALDPNKTVWEEISggldiikvgnREIPSRAYVGRFNFKGGDQQKK 442
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|..
gi 488984955 441 IARMSdafGlksiarhaadelplGYKQRLALACSLMHEPDILFLDEPTSGVD 492
Cdd:PRK11819 443 VGVLS---G--------------GERNRLHLAKTLKQGGNVLLLDEPTNDLD 477
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
333-537 |
5.51e-18 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 83.96 E-value: 5.51e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 333 QSLTKKFGDFAATDHVDFQVKRGEIFGLLGPNGAGKSTTFKMMCGLLVPTSGKALVLGMDLkvssGKARQHLGYMAQKFS 412
Cdd:PRK11247 16 NAVSKRYGERTVLNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAGELLAGTAPL----AEAREDTRLMFQDAR 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 413 LYGNLSVEQNLRFfsgvyGLRGRAQnEKIARMSDAFGLKSIARHAADELPLGYKQRLALACSLMHEPDILFLDEPTSGVD 492
Cdd:PRK11247 92 LLPWKKVIDNVGL-----GLKGQWR-DAALQALAAVGLADRANEWPAALSGGQKQRVALARALIHRPGLLLLDEPLGALD 165
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 488984955 493 PLTRREFWLHINSMVDK-GVTVMVTTHFMDEA-EYCDRIGLVYHGKL 537
Cdd:PRK11247 166 ALTRIEMQDLIESLWQQhGFTVLLVTHDVSEAvAMADRVLLIEEGKI 212
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
6-230 |
5.65e-18 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 86.43 E-value: 5.65e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 6 IALNGLSRRFPgmDRPAVAPLTCTIRAGYVTGLVGPDGAGKTTLMRMLAGLLKPDEGRASVIGfDPLKDDSALHA--VLG 83
Cdd:PRK09536 4 IDVSDLSVEFG--DTTVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAG-DDVEALSARAAsrRVA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 84 YMPQKFGLYEDLTVMENL----TLYADLRSVTGEARKKIFDRLLEFTSLGPFTERLAGKLSGGMKQKLGLACTLVGDPKV 159
Cdd:PRK09536 81 SVPQDTSLSFEFDVRQVVemgrTPHRSRFDTWTETDRAAVERAMERTGVAQFADRPVTSLSGGERQRVLLARALAQATPV 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 488984955 160 LLLDEPGVGVDPISRRELWQMVHELAGDGMLILWSTSYLDEAEQ-CRDVLLMNEGKLLYQGEPTAL--TQTMAG 230
Cdd:PRK09536 161 LLLDEPTASLDINHQVRTLELVRRLVDDGKTAVAAIHDLDLAARyCDELVLLADGRVRAAGPPADVltADTLRA 234
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
30-226 |
6.62e-18 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 84.40 E-value: 6.62e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 30 IRAGYVTGLVGPDGAGKTTLMRMLAGLLKPDEGRASV-----IGFDPLKDDSALHAVLGYMPQ--KFGLYEDlTVMENLT 102
Cdd:PRK13643 29 VKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVTVgdivvSSTSKQKEIKPVRKKVGVVFQfpESQLFEE-TVLKDVA 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 103 LYADLRSVTGEARKKIFDRLLEFTSLGP-FTERLAGKLSGGMKQKLGLACTLVGDPKVLLLDEPGVGVDPISRRELWQMV 181
Cdd:PRK13643 108 FGPQNFGIPKEKAEKIAAEKLEMVGLADeFWEKSPFELSGGQMRRVAIAGILAMEPEVLVLDEPTAGLDPKARIEMMQLF 187
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 488984955 182 HELAGDGMLILWSTSYLDEAEQCRD-VLLMNEGKLLYQGEPTALTQ 226
Cdd:PRK13643 188 ESIHQSGQTVVLVTHLMDDVADYADyVYLLEKGHIISCGTPSDVFQ 233
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
327-540 |
6.84e-18 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 86.91 E-value: 6.84e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 327 ETVIEAQSLTKKFGDFAATDHVDFQVKRGEIFGLLGPNGAGKSTTFKMMCGLLvPT---SGKALVLGMDLKVSSGKARQH 403
Cdd:PRK13549 3 EYLLEMKNITKTFGGVKALDNVSLKVRAGEIVSLCGENGAGKSTLMKVLSGVY-PHgtyEGEIIFEGEELQASNIRDTER 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 404 LG--YMAQKFSLYGNLSVEQNLrfFSGVYGLRG-----RAQNEKIARMSDAFGLKSIARHAADELPLGYKQRLALACSLM 476
Cdd:PRK13549 82 AGiaIIHQELALVKELSVLENI--FLGNEITPGgimdyDAMYLRAQKLLAQLKLDINPATPVGNLGLGQQQLVEIAKALN 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 488984955 477 HEPDILFLDEPTSgvdPLTRRE--FWLHI-NSMVDKGVTVMVTTHFMDE-AEYCDRIGLVYHGKLIAS 540
Cdd:PRK13549 160 KQARLLILDEPTA---SLTESEtaVLLDIiRDLKAHGIACIYISHKLNEvKAISDTICVIRDGRHIGT 224
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
6-219 |
6.84e-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: 83.30 E-value: 6.84e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 6 IALNGLSRRFPGMDRPAVAPLTCTIRAGYVTGLVGPDGAGKTTLMRMLAGLLKPDEGRASVIGFD-PLKDDSALHAVLGY 84
Cdd:cd03252 1 ITFEHVRFRYKPDGPVILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGHDlALADPAWLRRQVGV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 85 MPQKFGLYeDLTVMENLTLY---ADLRSVTGEAR-KKIFDRLLEF-----TSLGpftERLAGkLSGGMKQKLGLACTLVG 155
Cdd:cd03252 81 VLQENVLF-NRSIRDNIALAdpgMSMERVIEAAKlAGAHDFISELpegydTIVG---EQGAG-LSGGQRQRIAIARALIH 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 488984955 156 DPKVLLLDEPGVGVDPISRRELWQMVHELAgDGMLILWSTSYLDEAEQCRDVLLMNEGKLLYQG 219
Cdd:cd03252 156 NPRILIFDEATSALDYESEHAIMRNMHDIC-AGRTVIIIAHRLSTVKNADRIIVMEKGRIVEQG 218
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
318-549 |
7.10e-18 |
|
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: 87.08 E-value: 7.10e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 318 IHRVDGSkeetvIEAQSLTKKFG--DFAATDHVDFQVKRGEIFGLLGPNGAGKSTTFKMMCGLLVPTSGKALVLGMDLK- 394
Cdd:TIGR02203 324 IERARGD-----VEFRNVTFRYPgrDRPALDSISLVIEPGETVALVGRSGSGKSTLVNLIPRFYEPDSGQILLDGHDLAd 398
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 395 VSSGKARQHLGYMAQKFSLYgNLSVEQNLRffsgvYGLRGRAQNEKIARMSDAFGLKSIArhaaDELPLGY--------- 465
Cdd:TIGR02203 399 YTLASLRRQVALVSQDVVLF-NDTIANNIA-----YGRTEQADRAEIERALAAAYAQDFV----DKLPLGLdtpigengv 468
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 466 ------KQRLALACSLMHEPDILFLDEPTSGVDPLTRRefwlHINSMVD---KGVTVMVTTHFMDEAEYCDRIGLVYHGK 536
Cdd:TIGR02203 469 llsggqRQRLAIARALLKDAPILILDEATSALDNESER----LVQAALErlmQGRTTLVIAHRLSTIEKADRIVVMDDGR 544
|
250
....*....|...
gi 488984955 537 LIASGTPDALKAQ 549
Cdd:TIGR02203 545 IVERGTHNELLAR 557
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
326-551 |
7.80e-18 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 83.00 E-value: 7.80e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 326 EETVIEAQSLTKKFGDFAATDHVDFQVKRGEIFGLLGPNGAGKSTTFKMMCGLLVPTSGKALVLGMDLK--VSSGKARQH 403
Cdd:PRK11614 2 EKVMLSFDKVSAHYGKIQALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDGKDITdwQTAKIMREA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 404 LGYMAQKFSLYGNLSVEQNLRfFSGVYGLRGRAQnEKIARMSDAFGLKSIARHA-ADELPLGYKQRLALACSLMHEPDIL 482
Cdd:PRK11614 82 VAIVPEGRRVFSRMTVEENLA-MGGFFAERDQFQ-ERIKWVYELFPRLHERRIQrAGTMSGGEQQMLAIGRALMSQPRLL 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 483 FLDEPTSGVDPLTRREFWLHINSMVDKGVTVMVTTHFMDEA-EYCDRIGLVYHGKLIASGTPDALKAQAA 551
Cdd:PRK11614 160 LLDEPSLGLAPIIIQQIFDTIEQLREQGMTIFLVEQNANQAlKLADRGYVLENGHVVLEDTGDALLANEA 229
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
327-537 |
8.02e-18 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 82.90 E-value: 8.02e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 327 ETVIEAQSLTKKFGD----FAATDHVDFQVKRGEIFGLLGPNGAGKSTTFKMMCGLLVPTSGKALVLGMDLKVSSGKAR- 401
Cdd:PRK10584 4 ENIVEVHHLKKSVGQgeheLSILTGVELVVKRGETIALIGESGSGKSTLLAILAGLDDGSSGEVSLVGQPLHQMDEEARa 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 402 ----QHLGYMAQKFSLYGNLSVEQNLRFFSGVYGLRGRAQNEKIARMSDAFGLKSIARHAADELPLGYKQRLALACSLMH 477
Cdd:PRK10584 84 klraKHVGFVFQSFMLIPTLNALENVELPALLRGESSRQSRNGAKALLEQLGLGKRLDHLPAQLSGGEQQRVALARAFNG 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 488984955 478 EPDILFLDEPTSGVDPLTRREFWLHINSM-VDKGVTVMVTTHFMDEAEYCDRIGLVYHGKL 537
Cdd:PRK10584 164 RPDVLFADEPTGNLDRQTGDKIADLLFSLnREHGTTLILVTHDLQLAARCDRRLRLVNGQL 224
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
325-543 |
8.52e-18 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 84.52 E-value: 8.52e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 325 KEETVIEAQSLTKKFGD-----FAATDHVDFQVKRGEIFGLLGPNGAGKSTTFKMMCGLLVPTSG----KALVLGMDLKV 395
Cdd:PRK13631 17 SDDIILRVKNLYCVFDEkqeneLVALNNISYTFEKNKIYFIIGNSGSGKSTLVTHFNGLIKSKYGtiqvGDIYIGDKKNN 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 396 SSG-------------KARQHLGYMAQ--KFSLYGNlSVEQNLRFFSGVYGLRGRAQNEKIARMSDAFGLK-SIARHAAD 459
Cdd:PRK13631 97 HELitnpyskkiknfkELRRRVSMVFQfpEYQLFKD-TIEKDIMFGPVALGVKKSEAKKLAKFYLNKMGLDdSYLERSPF 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 460 ELPLGYKQRLALACSLMHEPDILFLDEPTSGVDPLTRREFWLHINSMVDKGVTVMVTTHFMDEA-EYCDRIGLVYHGKLI 538
Cdd:PRK13631 176 GLSGGQKRRVAIAGILAIQPEILIFDEPTAGLDPKGEHEMMQLILDAKANNKTVFVITHTMEHVlEVADEVIVMDKGKIL 255
|
....*
gi 488984955 539 ASGTP 543
Cdd:PRK13631 256 KTGTP 260
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
5-171 |
1.19e-17 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 84.47 E-value: 1.19e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 5 VIALNGLSRRFPGMDRP--AVAPLTCTIRAGYVTGLVGPDGAGKTTLMRMLAGLLKPDEGRASVIGFDPLK-DDSALHAV 81
Cdd:PRK11153 1 MIELKNISKVFPQGGRTihALNNVSLHIPAGEIFGVIGASGAGKSTLIRCINLLERPTSGRVLVDGQDLTAlSEKELRKA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 82 ---LGYMPQKFGLYEDLTVMENLTLYADLRSVTGEARKKIFDRLLEFTSLGPFTERLAGKLSGGMKQKLGLACTLVGDPK 158
Cdd:PRK11153 81 rrqIGMIFQHFNLLSSRTVFDNVALPLELAGTPKAEIKARVTELLELVGLSDKADRYPAQLSGGQKQRVAIARALASNPK 160
|
170
....*....|...
gi 488984955 159 VLLLDEPGVGVDP 171
Cdd:PRK11153 161 VLLCDEATSALDP 173
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
26-192 |
1.30e-17 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 81.39 E-value: 1.30e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 26 LTCTIRAGYVTGLVGPDGAGKTTLMRMLAGLLKPDEGRASVIGFDPLKDDSALHAVLGYMPQKFGLYEDLTVMENLTLYA 105
Cdd:PRK13538 20 LSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVLWQGEPIRRQRDEYHQDLLYLGHQPGIKTELTALENLRFYQ 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 106 DLRSVTGEARkkIFDrLLEFTSLGPFTERLAGKLSGGMKQKLGLACTLVGDPKVLLLDEPGV-----GVDPISRRelwqM 180
Cdd:PRK13538 100 RLHGPGDDEA--LWE-ALAQVGLAGFEDVPVRQLSAGQQRRVALARLWLTRAPLWILDEPFTaidkqGVARLEAL----L 172
|
170
....*....|..
gi 488984955 181 VHELAGDGMLIL 192
Cdd:PRK13538 173 AQHAEQGGMVIL 184
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
348-518 |
1.38e-17 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 81.46 E-value: 1.38e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 348 VDFQVKRGEIFGLLGPNGAGKSTTFKMMCGLLVPTSGKALVLGMDLKVSSGKARQHlgYMAQKFSLYGNLSVEQNLRFFS 427
Cdd:PRK13539 21 LSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDGGDIDDPDVAEACH--YLGHRNAMKPALTVAENLEFWA 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 428 GVYGlrgrAQNEKIARMSDAFGLKSIARHAADELPLGYKQRLALACSLMHEPDILFLDEPTSGVDPLTRREFWLHINSMV 507
Cdd:PRK13539 99 AFLG----GEELDIAAALEAVGLAPLAHLPFGYLSAGQKRRVALARLLVSNRPIWILDEPTAALDAAAVALFAELIRAHL 174
|
170
....*....|.
gi 488984955 508 DKGVTVMVTTH 518
Cdd:PRK13539 175 AQGGIVIAATH 185
|
|
| BtuD |
COG4138 |
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ... |
23-221 |
1.38e-17 |
|
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism];
Pssm-ID: 443313 [Multi-domain] Cd Length: 248 Bit Score: 82.58 E-value: 1.38e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 23 VAPLTCTIRAGYVTGLVGPDGAGKTTLMRMLAGLLkPDEGRASVIGfDPLKDDSALH-AVL-GYMPQKFGLYEDLTVMEN 100
Cdd:COG4138 12 LGPISAQVNAGELIHLIGPNGAGKSTLLARMAGLL-PGQGEILLNG-RPLSDWSAAElARHrAYLSQQQSPPFAMPVFQY 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 101 LTLYADlRSVTGEARKKIFDRLLEFTSLGPFTERLAGKLSGGMKQKLGLACTLV-------GDPKVLLLDEPGVGVDPIS 173
Cdd:COG4138 90 LALHQP-AGASSEAVEQLLAQLAEALGLEDKLSRPLTQLSGGEWQRVRLAAVLLqvwptinPEGQLLLLDEPMNSLDVAQ 168
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 488984955 174 RRELWQMVHELAGDGMLILWSTSYLDEA-EQCRDVLLMNEGKLLYQGEP 221
Cdd:COG4138 169 QAALDRLLRELCQQGITVVMSSHDLNHTlRHADRVWLLKQGKLVASGET 217
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
341-543 |
1.53e-17 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 83.13 E-value: 1.53e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 341 DFAATDHVDFQVKRGEIFGLLGPNGAGKSTTFKMMCGLLVPTSGKALVlgMDLKVSSG--------KARQHLGYMAQ--K 410
Cdd:PRK13645 23 EFKALNNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGLIISETGQTIV--GDYAIPANlkkikevkRLRKEIGLVFQfpE 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 411 FSLYGNlSVEQNLRFFSGVYGLRGRAQNEKIARMSDAFGL-KSIARHAADELPLGYKQRLALACSLMHEPDILFLDEPTS 489
Cdd:PRK13645 101 YQLFQE-TIEKDIAFGPVNLGENKQEAYKKVPELLKLVQLpEDYVKRSPFELSGGQKRRVALAGIIAMDGNTLVLDEPTG 179
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 488984955 490 GVDPLTRREF---WLHINSmvDKGVTVMVTTHFMDEA-EYCDRIGLVYHGKLIASGTP 543
Cdd:PRK13645 180 GLDPKGEEDFinlFERLNK--EYKKRIIMVTHNMDQVlRIADEVIVMHEGKVISIGSP 235
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
6-165 |
1.60e-17 |
|
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: 85.96 E-value: 1.60e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 6 IALNGLSRRFPGMDRPAVAPLTCTIRAGYVTGLVGPDGAGKTTLMRMLAGLLKPDEGRASVIGFDpLK--DDSALHAVLG 83
Cdd:COG4618 331 LSVENLTVVPPGSKRPILRGVSFSLEPGEVLGVIGPSGSGKSTLARLLVGVWPPTAGSVRLDGAD-LSqwDREELGRHIG 409
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 84 YMPQKFGLYEDlTVMENLTLYADLRS--VTGEARK-KIFDRLLEF-----TSLGPfterlAGK-LSGGMKQKLGLACTLV 154
Cdd:COG4618 410 YLPQDVELFDG-TIAENIARFGDADPekVVAAAKLaGVHEMILRLpdgydTRIGE-----GGArLSGGQRQRIGLARALY 483
|
170
....*....|.
gi 488984955 155 GDPKVLLLDEP 165
Cdd:COG4618 484 GDPRLVVLDEP 494
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
6-165 |
1.77e-17 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 82.44 E-value: 1.77e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 6 IALNGLSRRFpGmDRPAVAPLTCTIRAGYVTGLVGPDGAGKTTLMRMLAGLLKPDEGRASVIGFDPLKDDSALHA-VLGY 84
Cdd:COG4604 2 IEIKNVSKRY-G-GKVVLDDVSLTIPKGGITALIGPNGAGKSTLLSMISRLLPPDSGEVLVDGLDVATTPSRELAkRLAI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 85 MPQKFGLYEDLTVmenltlyADLRS----------VTGEARKKIfDRLLEFTSLGPFTERLAGKLSGGMKQKLGLACTLV 154
Cdd:COG4604 80 LRQENHINSRLTV-------RELVAfgrfpyskgrLTAEDREII-DEAIAYLDLEDLADRYLDELSGGQRQRAFIAMVLA 151
|
170
....*....|.
gi 488984955 155 GDPKVLLLDEP 165
Cdd:COG4604 152 QDTDYVLLDEP 162
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
17-220 |
1.91e-17 |
|
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: 85.95 E-value: 1.91e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 17 GMDRPAVAPLTCTIRAGYVTGLVGPDGAGKTTLMRMLAGLLKPDEGRASVIGFdPLK--DDSALHAVLGYMPQKFGLYeD 94
Cdd:TIGR01193 484 GYGSNILSDISLTIKMNSKTTIVGMSGSGKSTLAKLLVGFFQARSGEILLNGF-SLKdiDRHTLRQFINYLPQEPYIF-S 561
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 95 LTVMENLTLYADlRSVTGEARKKI-----FDRLLEFTSLGPFTE--RLAGKLSGGMKQKLGLACTLVGDPKVLLLDEPGV 167
Cdd:TIGR01193 562 GSILENLLLGAK-ENVSQDEIWAAceiaeIKDDIENMPLGYQTElsEEGSSISGGQKQRIALARALLTDSKVLILDESTS 640
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 488984955 168 GVDPISRRE----LWQMVHElagdgmLILWSTSYLDEAEQCRDVLLMNEGKLLYQGE 220
Cdd:TIGR01193 641 NLDTITEKKivnnLLNLQDK------TIIFVAHRLSVAKQSDKIIVLDHGKIIEQGS 691
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
6-224 |
2.33e-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: 85.54 E-value: 2.33e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 6 IALNGLSRRFPGMDRPAVAPLTCTIRAGYVTGLVGPDGAGKTTLMRMLAGLLKPDEGRASVIGfDPLKDDS--ALHAVLG 83
Cdd:TIGR02203 331 VEFRNVTFRYPGRDRPALDSISLVIEPGETVALVGRSGSGKSTLVNLIPRFYEPDSGQILLDG-HDLADYTlaSLRRQVA 409
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 84 YMPQKFGLYEDlTVMENLTlYADLRSVtGEARkkiFDRLLEFTSLGPFTERL-----------AGKLSGGMKQKLGLACT 152
Cdd:TIGR02203 410 LVSQDVVLFND-TIANNIA-YGRTEQA-DRAE---IERALAAAYAQDFVDKLplgldtpigenGVLLSGGQRQRLAIARA 483
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 488984955 153 LVGDPKVLLLDEPGVGVDPISRRELWQMVHELAGD--GMLILWSTSYLDEAEQcrdVLLMNEGKLLYQGEPTAL 224
Cdd:TIGR02203 484 LLKDAPILILDEATSALDNESERLVQAALERLMQGrtTLVIAHRLSTIEKADR---IVVMDDGRIVERGTHNEL 554
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
19-165 |
2.38e-17 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 80.99 E-value: 2.38e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 19 DRPAVAPLTCTIRAGYVTGLVGPDGAGKTTLMRMLAGLLKPD---EGRAsvigfdpLKDDSALHAV------LGYMPQKF 89
Cdd:COG4136 13 GRPLLAPLSLTVAPGEILTLMGPSGSGKSTLLAAIAGTLSPAfsaSGEV-------LLNGRRLTALpaeqrrIGILFQDD 85
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 488984955 90 GLYEDLTVMENLtLYADLRSVTGEARKKIFDRLLEFTSLGPFTERLAGKLSGGMKQKLGLACTLVGDPKVLLLDEP 165
Cdd:COG4136 86 LLFPHLSVGENL-AFALPPTIGRAQRRARVEQALEEAGLAGFADRDPATLSGGQRARVALLRALLAEPRALLLDEP 160
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
350-549 |
2.90e-17 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 85.54 E-value: 2.90e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 350 FQVKRGEIFGLLGPNGAGKSTTFKMMCGLLVPTSGKALVLGMDLKVSSGKA-RQHLGYMAQKFSLYGNlSVEQNLrffsg 428
Cdd:TIGR00958 502 FTLHPGEVVALVGPSGSGKSTVAALLQNLYQPTGGQVLLDGVPLVQYDHHYlHRQVALVGQEPVLFSG-SVRENI----- 575
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 429 VYGLRgRAQNEKI---ARMSDAFGLKSIARHAAD--------ELPLGYKQRLALACSLMHEPDILFLDEPTSGVDPLTRR 497
Cdd:TIGR00958 576 AYGLT-DTPDEEImaaAKAANAHDFIMEFPNGYDtevgekgsQLSGGQKQRIAIARALVRKPRVLILDEATSALDAECEQ 654
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 488984955 498 EFWlhiNSMVDKGVTVMVTTHFMDEAEYCDRIGLVYHGKLIASGTPDALKAQ 549
Cdd:TIGR00958 655 LLQ---ESRSRASRTVLLIAHRLSTVERADQILVLKKGSVVEMGTHKQLMED 703
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
24-221 |
3.78e-17 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 81.13 E-value: 3.78e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 24 APLTCTIRAGYVTGLVGPDGAGKTTLMRMLAGLLkPDEGRASVIGfDPLKDDSA--LHAVLGYMPQKFGLYEDLTVMENL 101
Cdd:PRK03695 13 GPLSAEVRAGEILHLVGPNGAGKSTLLARMAGLL-PGSGSIQFAG-QPLEAWSAaeLARHRAYLSQQQTPPFAMPVFQYL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 102 TLYADLRSVTGEARKKIfDRLLEFTSLGPFTERLAGKLSGGMKQKLGLACTL-----VGDP--KVLLLDEPGVGVDPISR 174
Cdd:PRK03695 91 TLHQPDKTRTEAVASAL-NEVAEALGLDDKLGRSVNQLSGGEWQRVRLAAVVlqvwpDINPagQLLLLDEPMNSLDVAQQ 169
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 488984955 175 RELWQMVHELAGDGMLILWSTSYLDE-AEQCRDVLLMNEGKLLYQGEP 221
Cdd:PRK03695 170 AALDRLLSELCQQGIAVVMSSHDLNHtLRHADRVWLLKQGKLLASGRR 217
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
17-221 |
4.55e-17 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 81.67 E-value: 4.55e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 17 GMDRPAVAPLTCTIRAGYVTGLVGPDGAGKTTLMRMLAGLLKPDEGRASVIGFDPlKDDSALHAVlgymPQKFGLY---- 92
Cdd:PRK13633 20 STEKLALDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVYVDGLDT-SDEENLWDI----RNKAGMVfqnp 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 93 ----------EDLTV-MENLTLYAD-LRSVTGEARKKIfdRLLEFTSLGPFTerlagkLSGGMKQKLGLACTLVGDPKVL 160
Cdd:PRK13633 95 dnqivativeEDVAFgPENLGIPPEeIRERVDESLKKV--GMYEYRRHAPHL------LSGGQKQRVAIAGILAMRPECI 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 488984955 161 LLDEPGVGVDPISRRELWQMVHELAG-DGMLILWSTSYLDEAEQCRDVLLMNEGKLLYQGEP 221
Cdd:PRK13633 167 IFDEPTAMLDPSGRREVVNTIKELNKkYGITIILITHYMEEAVEADRIIVMDSGKVVMEGTP 228
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
19-226 |
4.89e-17 |
|
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: 80.35 E-value: 4.89e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 19 DRPAVAPLTCTIRAGYVTGLVGPDGAGKTTLMRMLAGLLKPDEGRASVIGFDPLK-DDSALHAVLGYMPQKFGLYEDlTV 97
Cdd:cd03254 15 KKPVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGIDIRDiSRKSLRSMIGVVLQDTFLFSG-TI 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 98 MENLTL---YADLRSVTGEARKKIFDRLLEF------TSLGPfterlAGK-LSGGMKQKLGLACTLVGDPKVLLLDEPGV 167
Cdd:cd03254 94 MENIRLgrpNATDEEVIEAAKEAGAHDFIMKlpngydTVLGE-----NGGnLSQGERQLLAIARAMLRDPKILILDEATS 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 488984955 168 GVDPISRRELWQMVHELAGDGMLILWS--TSYLDEAEQcrdVLLMNEGKLLYQGEPTALTQ 226
Cdd:cd03254 169 NIDTETEKLIQEALEKLMKGRTSIIIAhrLSTIKNADK---ILVLDDGKIIEEGTHDELLA 226
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
326-543 |
5.00e-17 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 81.34 E-value: 5.00e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 326 EETVIEAQSLTKKF-GDFAAT-DHVDFQVKRGEIFGLLGPNGAGKSTTFKMMCGLLVPTSGKalVLGMDLKVSSG---KA 400
Cdd:PRK13648 4 KNSIIVFKNVSFQYqSDASFTlKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGE--IFYNNQAITDDnfeKL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 401 RQHLGYMAQKFSlygNLSVEQNLRFfSGVYGLRGRA-----QNEKIARMSDAFGLKSIARHAADELPLGYKQRLALACSL 475
Cdd:PRK13648 82 RKHIGIVFQNPD---NQFVGSIVKY-DVAFGLENHAvpydeMHRRVSEALKQVDMLERADYEPNALSGGQKQRVAIAGVL 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 488984955 476 MHEPDILFLDEPTSGVDPLTRREFWLHINSM-VDKGVTVMVTTHFMDEAEYCDRIGLVYHGKLIASGTP 543
Cdd:PRK13648 158 ALNPSVIILDEATSMLDPDARQNLLDLVRKVkSEHNITIISITHDLSEAMEADHVIVMNKGTVYKEGTP 226
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
1-224 |
6.27e-17 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 80.78 E-value: 6.27e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 1 MSETVIALNGLSRRFPgmDRPAVAPLTCTIRAGYVTGLVGPDGAGKTTLMRMLAGLLKPDEGRASVIG------------ 68
Cdd:PRK10619 1 MSENKLNVIDLHKRYG--EHEVLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNGqtinlvrdkdgq 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 69 ---FDPlKDDSALHAVLGYMPQKFGLYEDLTVMENLtLYADLRsVTGEARKKIFDRLLEFTSLGPFTERLAGK----LSG 141
Cdd:PRK10619 79 lkvADK-NQLRLLRTRLTMVFQHFNLWSHMTVLENV-MEAPIQ-VLGLSKQEARERAVKYLAKVGIDERAQGKypvhLSG 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 142 GMKQKLGLACTLVGDPKVLLLDEPGVGVDPISRRELWQMVHELAGDGMLILWSTSYLDEAEQCRD-VLLMNEGKLLYQGE 220
Cdd:PRK10619 156 GQQQRVSIARALAMEPEVLLFDEPTSALDPELVGEVLRIMQQLAEEGKTMVVVTHEMGFARHVSShVIFLHQGKIEEEGA 235
|
....
gi 488984955 221 PTAL 224
Cdd:PRK10619 236 PEQL 239
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
33-221 |
6.53e-17 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 81.28 E-value: 6.53e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 33 GYVTGLVGPDGAGKTTLMRMLAGLLKPDEGRASVIGfDPLK-DDSALHAVlgymPQKFGLY----EDL----TVME---- 99
Cdd:PRK13639 28 GEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIKG-EPIKyDKKSLLEV----RKTVGIVfqnpDDQlfapTVEEdvaf 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 100 ---NLTLYADlrsvtgEARKKIFDRLLEFTSLGpFTERLAGKLSGGMKQKLGLACTLVGDPKVLLLDEPGVGVDPISRRE 176
Cdd:PRK13639 103 gplNLGLSKE------EVEKRVKEALKAVGMEG-FENKPPHHLSGGQKKRVAIAGILAMKPEIIVLDEPTSGLDPMGASQ 175
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 488984955 177 LWQMVHELAGDGMLILWSTSYLDEAEQCRD-VLLMNEGKLLYQGEP 221
Cdd:PRK13639 176 IMKLLYDLNKEGITIIISTHDVDLVPVYADkVYVMSDGKIIKEGTP 221
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
341-549 |
6.74e-17 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 81.36 E-value: 6.74e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 341 DFAATDHVDFQVKRGEIFGLLGPNGAGKSTTFKMMCGLLVPTSGKALVlgMDLKVSSGKARQHLGYMAQKFSLYGNL--- 417
Cdd:PRK13646 19 EHQAIHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTV--DDITITHKTKDKYIRPVRKRIGMVFQFpes 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 418 -----SVEQNLRFFSGVYGLRGRAQNEKIARMSDAFGL-KSIARHAADELPLGYKQRLALACSLMHEPDILFLDEPTSGV 491
Cdd:PRK13646 97 qlfedTVEREIIFGPKNFKMNLDEVKNYAHRLLMDLGFsRDVMSQSPFQMSGGQMRKIAIVSILAMNPDIIVLDEPTAGL 176
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 492 DPLTRREFWLHINSM-VDKGVTVMVTTHFMDE-AEYCDRIGLVYHGKLIASGTPDALKAQ 549
Cdd:PRK13646 177 DPQSKRQVMRLLKSLqTDENKTIILVSHDMNEvARYADEVIVMKEGSIVSQTSPKELFKD 236
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
22-224 |
7.90e-17 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 80.98 E-value: 7.90e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 22 AVAPLTCTIRAGYVTGLVGPDGAGKTTLMRMLAGLLKPDEGRASVigfdplkDDSALHA-----VLGYMPQKFG------ 90
Cdd:PRK13646 22 AIHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTV-------DDITITHktkdkYIRPVRKRIGmvfqfp 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 91 ---LYEDLTVMENLTLYADLRSVTGEARKKIFDRLLEF------TSLGPFterlagKLSGGMKQKLGLACTLVGDPKVLL 161
Cdd:PRK13646 95 esqLFEDTVEREIIFGPKNFKMNLDEVKNYAHRLLMDLgfsrdvMSQSPF------QMSGGQMRKIAIVSILAMNPDIIV 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 488984955 162 LDEPGVGVDPISRRELWQMVHELAGD--GMLILWSTSYLDEAEQCRDVLLMNEGKLLYQGEPTAL 224
Cdd:PRK13646 169 LDEPTAGLDPQSKRQVMRLLKSLQTDenKTIILVSHDMNEVARYADEVIVMKEGSIVSQTSPKEL 233
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
353-544 |
8.69e-17 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 83.56 E-value: 8.69e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 353 KRGEIFGLLGPNGAGKST-----TFKMMCGLLVptSGKALVLGMdlKVSSGKARQHLGYMAQKFSLYGNLSVEQNLRFFS 427
Cdd:TIGR00955 49 KPGELLAVMGSSGAGKTTlmnalAFRSPKGVKG--SGSVLLNGM--PIDAKEMRAISAYVQQDDLFIPTLTVREHLMFQA 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 428 GVYGLRGRAQNEKIARMSD---AFGLKSIA--------RHAAdeLPLGYKQRLALACSLMHEPDILFLDEPTSGVDPLTR 496
Cdd:TIGR00955 125 HLRMPRRVTKKEKRERVDEvlqALGLRKCAntrigvpgRVKG--LSGGERKRLAFASELLTDPPLLFCDEPTSGLDSFMA 202
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 488984955 497 REFWLHINSMVDKGVTVMVTTHFMDEAEYC--DRIGLVYHGKLIASGTPD 544
Cdd:TIGR00955 203 YSVVQVLKGLAQKGKTIICTIHQPSSELFElfDKIILMAEGRVAYLGSPD 252
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
1-221 |
9.34e-17 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 82.30 E-value: 9.34e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 1 MSETVIALNGLSRRFPgmDRPAVAPLTCTIRAGYVTGLVGPDGAGKTTLMRMLAGLLKPDEGRASVIGFDpLKDDSALHA 80
Cdd:PRK09452 10 SLSPLVELRGISKSFD--GKEVISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLDGQD-ITHVPAENR 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 81 VLGYMPQKFGLYEDLTVMENLTLYADLRSV-TGEARKKIFDrLLEFTSLGPFTERLAGKLSGGMKQKLGLACTLVGDPKV 159
Cdd:PRK09452 87 HVNTVFQSYALFPHMTVFENVAFGLRMQKTpAAEITPRVME-ALRMVQLEEFAQRKPHQLSGGQQQRVAIARAVVNKPKV 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 488984955 160 LLLDEPGVGVDPISRRelwQMVHELAG----DGMLILWSTSYLDEAEQCRD-VLLMNEGKLLYQGEP 221
Cdd:PRK09452 166 LLLDESLSALDYKLRK---QMQNELKAlqrkLGITFVFVTHDQEEALTMSDrIVVMRDGRIEQDGTP 229
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
1-492 |
1.05e-16 |
|
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 443332 [Multi-domain] Cd Length: 533 Bit Score: 83.20 E-value: 1.05e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 1 MSETVIALNGLSRRFPGMDR--PAVAPLTCTIRAGYVTGLVGPDGAGKT----TLMRMLAGLLKPDEGRASVIGFDPLK- 73
Cdd:COG4172 2 MSMPLLSVEDLSVAFGQGGGtvEAVKGVSFDIAAGETLALVGESGSGKSvtalSILRLLPDPAAHPSGSILFDGQDLLGl 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 74 DDSALHAVLGympQKFGLY--EDLT-----------VMENLTLYADLRSvtGEARKKIFDrLLEFTSLgPFTERLAGK-- 138
Cdd:COG4172 82 SERELRRIRG---NRIAMIfqEPMTslnplhtigkqIAEVLRLHRGLSG--AAARARALE-LLERVGI-PDPERRLDAyp 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 139 --LSGGMKQKLGLACTLVGDPKVLLLDEPGVGVDPISRRELWQMVHELAGD-GMLILWST-------SYLDEaeqcrdVL 208
Cdd:COG4172 155 hqLSGGQRQRVMIAMALANEPDLLIADEPTTALDVTVQAQILDLLKDLQRElGMALLLIThdlgvvrRFADR------VA 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 209 LMNEGKLLYQGEPTALtqtmagrsFlvSSPQEN-NRRLLqralklpqvsdgviqgksvrlilkkDARieevqQHGDMPPl 287
Cdd:COG4172 229 VMRQGEIVEQGPTAEL--------F--AAPQHPyTRKLL-------------------------AAE-----PRGDPRP- 267
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 288 qVADTAPrfedafidllggagtaesplgaiihrvdgskeeTVIEAQSLTKKF-----------GDFAATDHVDFQVKRGE 356
Cdd:COG4172 268 -VPPDAP---------------------------------PLLEARDLKVWFpikrglfrrtvGHVKAVDGVSLTLRRGE 313
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 357 IFGLLGPNGAGKSTTFKMMCGlLVPTSGKALVLGMDLKVSSGKARQHLgymAQKFSL-----YGNLS--------VEQNL 423
Cdd:COG4172 314 TLGLVGESGSGKSTLGLALLR-LIPSEGEIRFDGQDLDGLSRRALRPL---RRRMQVvfqdpFGSLSprmtvgqiIAEGL 389
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 424 RFFSGvyGLRGRAQNEKIARMSDAFGLKSIARHA-ADELPLGYKQRLALACSLMHEPDILFLDEPTSGVD 492
Cdd:COG4172 390 RVHGP--GLSAAERRARVAEALEEVGLDPAARHRyPHEFSGGQRQRIAIARALILEPKLLVLDEPTSALD 457
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
5-171 |
1.07e-16 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 79.12 E-value: 1.07e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 5 VIALNGLSrrFPGMDRPAVAPLTCTIRAGYVTGLVGPDGAGKTTLMRMLAGLLKPDEGRASVIGFDPLKDDSALH-AVLG 83
Cdd:PRK13543 11 LLAAHALA--FSRNEEPVFGPLDFHVDAGEALLVQGDNGAGKTTLLRVLAGLLHVESGQIQIDGKTATRGDRSRFmAYLG 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 84 YMPqkfGLYEDLTVMENLTLyadLRSVTGEARKKIFDRLLEFTSLGPFTERLAGKLSGGMKQKLGLACTLVGDPKVLLLD 163
Cdd:PRK13543 89 HLP---GLKADLSTLENLHF---LCGLHGRRAKQMPGSALAIVGLAGYEDTLVRQLSAGQKKRLALARLWLSPAPLWLLD 162
|
....*...
gi 488984955 164 EPGVGVDP 171
Cdd:PRK13543 163 EPYANLDL 170
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
329-540 |
1.11e-16 |
|
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose isomerase and xylulokinase enzymes for xylose utilization. Members of this protein family are the ATP-binding cassette (ABC) subunit of the known or predicted high-affinity xylose ABC transporter for xylose import. These genes, which closely resemble other sugar transport ABC transporter genes, typically are encoded near xylose utilization enzymes and regulatory proteins. Note that this form of the transporter contains two copies of the ABC transporter domain (pfam00005). [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 131681 [Multi-domain] Cd Length: 500 Bit Score: 82.95 E-value: 1.11e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 329 VIEAQSLTKKFGDFAATDHVDFQVKRGEIFGLLGPNGAGKSTTFKMMCGLLvPT---SGKALVLGMDLKVSSGKARQHLG 405
Cdd:TIGR02633 1 LLEMKGIVKTFGGVKALDGIDLEVRPGECVGLCGENGAGKSTLMKILSGVY-PHgtwDGEIYWSGSPLKASNIRDTERAG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 406 --YMAQKFSLYGNLSVEQNLrFFSGVYGLRGR--AQNEKIARMSDAFGLKSI-----ARHAADeLPLGYKQRLALACSLM 476
Cdd:TIGR02633 80 ivIIHQELTLVPELSVAENI-FLGNEITLPGGrmAYNAMYLRAKNLLRELQLdadnvTRPVGD-YGGGQQQLVEIAKALN 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 488984955 477 HEPDILFLDEPTSGvdpLTRREFWLHINSMVD---KGVTVMVTTHFMDEAE-YCDRIGLVYHGKLIAS 540
Cdd:TIGR02633 158 KQARLLILDEPSSS---LTEKETEILLDIIRDlkaHGVACVYISHKLNEVKaVCDTICVIRDGQHVAT 222
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
346-518 |
1.12e-16 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 78.69 E-value: 1.12e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 346 DHVDFQVKRGEIFGLLGPNGAGKSTTFKMMCGLLVPTSGKALVLGMDLKVSSGKARQHLGYMAQKFSLYGNLSVEQNLRF 425
Cdd:PRK13538 18 SGLSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVLWQGEPIRRQRDEYHQDLLYLGHQPGIKTELTALENLRF 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 426 FSgvyGLRGRAQNEKIARMSDAFGLKSIARHAADELPLGYKQRLALACSLMHEPDILFLDEP-----TSGVDPLTRrefw 500
Cdd:PRK13538 98 YQ---RLHGPGDDEALWEALAQVGLAGFEDVPVRQLSAGQQRRVALARLWLTRAPLWILDEPftaidKQGVARLEA---- 170
|
170
....*....|....*...
gi 488984955 501 lHINSMVDKGVTVMVTTH 518
Cdd:PRK13538 171 -LLAQHAEQGGMVILTTH 187
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
19-208 |
1.43e-16 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 78.99 E-value: 1.43e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 19 DRPAVAPLTCTIRAGYVTGLVGPDGAGKTTLMRMLAGLLKPDEGRasvIGFDPlKDDSAL-----HAVLGYMPQKFGLYE 93
Cdd:PRK10247 19 DAKILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGT---LLFEG-EDISTLkpeiyRQQVSYCAQTPTLFG 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 94 DlTVMENLTLYADLRSVTGEaRKKIFDRLLEFTSLGPFTERLAGKLSGGMKQKLGLACTLVGDPKVLLLDEPGVGVDPIS 173
Cdd:PRK10247 95 D-TVYDNLIFPWQIRNQQPD-PAIFLDDLERFALPDTILTKNIAELSGGEKQRISLIRNLQFMPKVLLLDEITSALDESN 172
|
170 180 190
....*....|....*....|....*....|....*.
gi 488984955 174 RRELWQMVHELAGD-GMLILWSTSYLDEAEQCRDVL 208
Cdd:PRK10247 173 KHNVNEIIHRYVREqNIAVLWVTHDKDEINHADKVI 208
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
16-261 |
1.44e-16 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 80.26 E-value: 1.44e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 16 PG--MDRPAVAPLTCTIRAGYVTGLVGPDGAGKTTLMRMLAGLLKPDEGRASVIGF--DPLKDDSALHAV-----LGYMP 86
Cdd:PRK13641 14 PGtpMEKKGLDNISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITIAGYhiTPETGNKNLKKLrkkvsLVFQF 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 87 QKFGLYEDlTVMENLtLYADLRsvTGEARKKIFDRLLEFTSLGPFTERLAGK----LSGGMKQKLGLACTLVGDPKVLLL 162
Cdd:PRK13641 94 PEAQLFEN-TVLKDV-EFGPKN--FGFSEDEAKEKALKWLKKVGLSEDLISKspfeLSGGQMRRVAIAGVMAYEPEILCL 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 163 DEPGVGVDPISRRELWQMVHELAGDG-MLILWSTSYLDEAEQCRDVLLMNEGKLLYQGEPTA------------LTQTMA 229
Cdd:PRK13641 170 DEPAAGLDPEGRKEMMQLFKDYQKAGhTVILVTHNMDDVAEYADDVLVLEHGKLIKHASPKEifsdkewlkkhyLDEPAT 249
|
250 260 270
....*....|....*....|....*....|..
gi 488984955 230 GRsfLVSSPQENNRRLLQRALKLPQVSDGVIQ 261
Cdd:PRK13641 250 SR--FASKLEKGGFKFSEMPLTIDELVDGIKN 279
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
6-219 |
1.49e-16 |
|
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: 79.20 E-value: 1.49e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 6 IALNGLSRRFPGMDRPAVAPLTCTIRAGYVTGLVGPDGAGKTTLMRMLAGLLKPDEGRASVIGFDpLKDDSA--LHAVLG 83
Cdd:cd03251 1 VEFKNVTFRYPGDGPPVLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDGHD-VRDYTLasLRRQIG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 84 YMPQKFGLYEDlTVMENLTlYADlrsvTGEARKKIFD-----RLLEF---------TSLGpftERlAGKLSGGMKQKLGL 149
Cdd:cd03251 80 LVSQDVFLFND-TVAENIA-YGR----PGATREEVEEaaraaNAHEFimelpegydTVIG---ER-GVKLSGGQRQRIAI 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 488984955 150 ACTLVGDPKVLLLDEPGVGVDPISRRELWQMVHELAGD--GMLILWSTSYLDEAEQcrdVLLMNEGKLLYQG 219
Cdd:cd03251 150 ARALLKDPPILILDEATSALDTESERLVQAALERLMKNrtTFVIAHRLSTIENADR---IVVLEDGKIVERG 218
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
348-528 |
1.68e-16 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 79.09 E-value: 1.68e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 348 VDFQVKRGEIFGLLGPNGAGKSTTFKMMCGLLVPTSGKALVLGMDLKVSSGKAR-----QHLGYMAQKFSLYGNLSVEQN 422
Cdd:PRK11629 28 VSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPMSKLSSAAKaelrnQKLGFIYQFHHLLPDFTALEN 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 423 LRFFSGVYGLRGRAQNEKIARMSDAFGLKSIARHAADELPLGYKQRLALACSLMHEPDILFLDEPTSGVDPLTRRE-FWL 501
Cdd:PRK11629 108 VAMPLLIGKKKPAEINSRALEMLAAVGLEHRANHRPSELSGGERQRVAIARALVNNPRLVLADEPTGNLDARNADSiFQL 187
|
170 180
....*....|....*....|....*..
gi 488984955 502 HINSMVDKGVTVMVTTHFMDEAEYCDR 528
Cdd:PRK11629 188 LGELNRLQGTAFLVVTHDLQLAKRMSR 214
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
29-226 |
1.80e-16 |
|
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose isomerase and xylulokinase enzymes for xylose utilization. Members of this protein family are the ATP-binding cassette (ABC) subunit of the known or predicted high-affinity xylose ABC transporter for xylose import. These genes, which closely resemble other sugar transport ABC transporter genes, typically are encoded near xylose utilization enzymes and regulatory proteins. Note that this form of the transporter contains two copies of the ABC transporter domain (pfam00005). [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 131681 [Multi-domain] Cd Length: 500 Bit Score: 82.18 E-value: 1.80e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 29 TIRAGYVTGLVGPDGAGKTTLMRMLAGLLkPDEGRASV-IGFDPLKDDSALHAV---LGYMPQ---KFGLYEDLTVMENL 101
Cdd:TIGR02633 282 SLRRGEILGVAGLVGAGRTELVQALFGAY-PGKFEGNVfINGKPVDIRNPAQAIragIAMVPEdrkRHGIVPILGVGKNI 360
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 102 TL-----YADLRSVTGEARKKIFDRLLEFTSLGPFTERLA-GKLSGGMKQKLGLACTLVGDPKVLLLDEPGVGVDPISRR 175
Cdd:TIGR02633 361 TLsvlksFCFKMRIDAAAELQIIGSAIQRLKVKTASPFLPiGRLSGGNQQKAVLAKMLLTNPRVLILDEPTRGVDVGAKY 440
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 488984955 176 ELWQMVHELAGDGMLILWSTSYLDEAEQCRD-VLLMNEGKLLYQGEPTALTQ 226
Cdd:TIGR02633 441 EIYKLINQLAQEGVAIIVVSSELAEVLGLSDrVLVIGEGKLKGDFVNHALTQ 492
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
346-558 |
2.20e-16 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 82.46 E-value: 2.20e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 346 DHVDFQVKRGEIFGLLGPNGAGKSTTFKMMCGLLVPTSGKALVLGMDLKVSSGKA-----RQHLGYMAQKFSLYGNLSVE 420
Cdd:PRK10535 25 KGISLDIYAGEMVAIVGASGSGKSTLMNILGCLDKPTSGTYRVAGQDVATLDADAlaqlrREHFGFIFQRYHLLSHLTAA 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 421 QNLRfFSGVYGLRGRAQNEKIARM-SDAFGLKSIARHAADELPLGYKQRLALACSLMHEPDILFLDEPTSGVDPLTRREF 499
Cdd:PRK10535 105 QNVE-VPAVYAGLERKQRLLRAQElLQRLGLEDRVEYQPSQLSGGQQQRVSIARALMNGGQVILADEPTGALDSHSGEEV 183
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 500 WLHINSMVDKGVTVMVTTHFMDEAEYCDRIGLVYHGKLIA-SGTPDALKAQAADDSQTDP 558
Cdd:PRK10535 184 MAILHQLRDRGHTVIIVTHDPQVAAQAERVIEIRDGEIVRnPPAQEKVNVAGGTEPVVNT 243
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
323-562 |
2.74e-16 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 79.04 E-value: 2.74e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 323 GSKEETVIEAQSLTKKFGDFAATDHVDFQVKRGEIFGLLGPNGAGKSTTFKMMCGLLVPTSGKALVLGMDLKVSSG---- 398
Cdd:PRK11831 1 EQSVANLVDMRGVSFTRGNRCIFDNISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEILFDGENIPAMSRsrly 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 399 KARQHLGYMAQKFSLYGNLSVEQNLrffsgVYGLRGRAQ-NEKIARMS-----DAFGLKSIARHAADELPLGYKQRLALA 472
Cdd:PRK11831 81 TVRKRMSMLFQSGALFTDMNVFDNV-----AYPLREHTQlPAPLLHSTvmmklEAVGLRGAAKLMPSELSGGMARRAALA 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 473 CSLMHEPDILFLDEPTSGVDPLTRREFWLHINSMVDK-GVTVMVTTHFMDEA-EYCDRIGLVYHGKLIASGTPDALKAqa 550
Cdd:PRK11831 156 RAIALEPDLIMFDEPFVGQDPITMGVLVKLISELNSAlGVTCVVVSHDVPEVlSIADHAYIVADKKIVAHGSAQALQA-- 233
|
250
....*....|..
gi 488984955 551 addsQTDPTMEQ 562
Cdd:PRK11831 234 ----NPDPRVRQ 241
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
22-255 |
2.79e-16 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 81.23 E-value: 2.79e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 22 AVAPLTCTIRAGYVTGLVGPDGAGKTTLMRMLAGLLKPDEGRASVIGFDPLK-DDSALHAV----LGYMPQKFGLYEDLT 96
Cdd:PRK10070 43 GVKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAKiSDAELREVrrkkIAMVFQSFALMPHMT 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 97 VMENLTLYADLRSVTGEARKKIFDRLLEFTSLGPFTERLAGKLSGGMKQKLGLACTLVGDPKVLLLDEPGVGVDPISRRE 176
Cdd:PRK10070 123 VLDNTAFGMELAGINAEERREKALDALRQVGLENYAHSYPDELSGGMRQRVGLARALAINPDILLMDEAFSALDPLIRTE 202
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 177 LW-QMVHELAGDGMLILWSTSYLDEAEQCRD-VLLMNEGKLLYQGEPTAltqtmagrsfLVSSPQENNRRLLQRALKLPQ 254
Cdd:PRK10070 203 MQdELVKLQAKHQRTIVFISHDLDEAMRIGDrIAIMQNGEVVQVGTPDE----------ILNNPANDYVRTFFRGVDISQ 272
|
.
gi 488984955 255 V 255
Cdd:PRK10070 273 V 273
|
|
| BtuD |
COG4138 |
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ... |
348-544 |
3.51e-16 |
|
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism];
Pssm-ID: 443313 [Multi-domain] Cd Length: 248 Bit Score: 78.34 E-value: 3.51e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 348 VDFQVKRGEIFGLLGPNGAGKSTTFKMMCGLLvPTSGKALVLGMDLKVSSGKA-RQHLGYMAQKFSLYGNLSVEQNLRFF 426
Cdd:COG4138 15 ISAQVNAGELIHLIGPNGAGKSTLLARMAGLL-PGQGEILLNGRPLSDWSAAElARHRAYLSQQQSPPFAMPVFQYLALH 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 427 SGVyGLRGRAQNEKIARMSDAFGLKSIARHAADELPLGYKQRLALACSLMH-------EPDILFLDEPTSGVDpltrref 499
Cdd:COG4138 94 QPA-GASSEAVEQLLAQLAEALGLEDKLSRPLTQLSGGEWQRVRLAAVLLQvwptinpEGQLLLLDEPMNSLD------- 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 488984955 500 WLH-------INSMVDKGVTVMVTTHFMDEA-EYCDRIGLVYHGKLIASGTPD 544
Cdd:COG4138 166 VAQqaaldrlLRELCQQGITVVMSSHDLNHTlRHADRVWLLKQGKLVASGETA 218
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
29-215 |
3.51e-16 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 81.51 E-value: 3.51e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 29 TIRAGYVTGLVGPDGAGKTTLMRMLAGLLKpdeGRAS---VIGFDPLKDDSALHAV---LGYMPQ---KFGLYEDLTVME 99
Cdd:PRK13549 284 SLRRGEILGIAGLVGAGRTELVQCLFGAYP---GRWEgeiFIDGKPVKIRNPQQAIaqgIAMVPEdrkRDGIVPVMGVGK 360
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 100 NLTLyADLRSVTGearKKIFDRLLEFTSLGPFTERLA----------GKLSGGMKQKLGLACTLVGDPKVLLLDEPGVGV 169
Cdd:PRK13549 361 NITL-AALDRFTG---GSRIDDAAELKTILESIQRLKvktaspelaiARLSGGNQQKAVLAKCLLLNPKILILDEPTRGI 436
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 488984955 170 DPISRRELWQMVHELAGDGMLILWSTSYLDEAEQCRD-VLLMNEGKL 215
Cdd:PRK13549 437 DVGAKYEIYKLINQLVQQGVAIIVISSELPEVLGLSDrVLVMHEGKL 483
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
29-526 |
4.53e-16 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 80.83 E-value: 4.53e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 29 TIRAGYVTGLVGPDGAGKTTLMRMLAGLLKPDEG-------RASVIGFDPLkddsalhavlgympQKfgLYEDLTVMENL 101
Cdd:PRK10938 25 TLNAGDSWAFVGANGSGKSALARALAGELPLLSGerqsqfsHITRLSFEQL--------------QK--LVSDEWQRNNT 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 102 TLYADLRSVTGE-ARKKIFD---------RLLEFTSLGPFTERLAGKLSGGMKQKLGLACTLVGDPKVLLLDEPGVGVDP 171
Cdd:PRK10938 89 DMLSPGEDDTGRtTAEIIQDevkdparceQLAQQFGITALLDRRFKYLSTGETRKTLLCQALMSEPDLLILDEPFDGLDV 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 172 ISRRELWQMVHELAGDGM-LILWSTSYLDEAEQCRDVLLMNEGKLLYQGEPTALTQTmAGRSFLVSSPQENNrrllqraL 250
Cdd:PRK10938 169 ASRQQLAELLASLHQSGItLVLVLNRFDEIPDFVQFAGVLADCTLAETGEREEILQQ-ALVAQLAHSEQLEG-------V 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 251 KLPQVsdgviqgksvrlilkkdariEEVQQHGDMPPlqvadTAPRFEdafidLLGGagtaesplgaiihrvdgskeetVI 330
Cdd:PRK10938 241 QLPEP--------------------DEPSARHALPA-----NEPRIV-----LNNG----------------------VV 268
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 331 eaqsltkKFGDFAATDHVDFQVKRGEIFGLLGPNGAGKSTTFKMMCGLLVPTSGKALVLgMDLKVSSGKA----RQHLGY 406
Cdd:PRK10938 269 -------SYNDRPILHNLSWQVNPGEHWQIVGPNGAGKSTLLSLITGDHPQGYSNDLTL-FGRRRGSGETiwdiKKHIGY 340
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 407 MAQkfSLYGNLSVEQNLR------FFS--GVYGLRGRAQNEKIARMSDAFGL-KSIARHAADELPLGyKQRLAL-ACSLM 476
Cdd:PRK10938 341 VSS--SLHLDYRVSTSVRnvilsgFFDsiGIYQAVSDRQQKLAQQWLDILGIdKRTADAPFHSLSWG-QQRLALiVRALV 417
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....
gi 488984955 477 HEPDILFLDEPTSGVDPLTR---REFwlhINSMVDKGVT-VMVTTHFMDEAEYC 526
Cdd:PRK10938 418 KHPTLLILDEPLQGLDPLNRqlvRRF---VDVLISEGETqLLFVSHHAEDAPAC 468
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
8-173 |
6.10e-16 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 76.53 E-value: 6.10e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 8 LNGLSRRFPGMDRPAVAPLTCTIRAGYVTGLVGPDGAGKTTLMRMLAGLLKPDEGRASVIGFDPLKDDSALHAVLGYMPQ 87
Cdd:PRK13540 2 LDVIELDFDYHDQPLLQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEILFERQSIKKDLCTYQKQLCFVGH 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 88 KFGLYEDLTVMENltLYADLRSVTGEARkkiFDRLLEFTSLGPFTERLAGKLSGGMKQKLGLACTLVGDPKVLLLDEPGV 167
Cdd:PRK13540 82 RSGINPYLTLREN--CLYDIHFSPGAVG---ITELCRLFSLEHLIDYPCGLLSSGQKRQVALLRLWMSKAKLWLLDEPLV 156
|
....*.
gi 488984955 168 GVDPIS 173
Cdd:PRK13540 157 ALDELS 162
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
348-541 |
6.51e-16 |
|
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: 76.93 E-value: 6.51e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 348 VDFQVKRGEIFGLLGPNGAGKSTTFKMMCGLLVP---TSGKALVLGMDLKvsSGKARQHLGYMAQKFSLYGNLSVEQNLR 424
Cdd:cd03234 26 VSLHVESGQVMAILGSSGSGKTTLLDAISGRVEGggtTSGQILFNGQPRK--PDQFQKCVAYVRQDDILLPGLTVRETLT 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 425 FFSGvygLR-GRAQNEKIARMSDA-FGLKSIA-RHAADE----LPLGYKQRLALACSLMHEPDILFLDEPTSGVDPLTRR 497
Cdd:cd03234 104 YTAI---LRlPRKSSDAIRKKRVEdVLLRDLAlTRIGGNlvkgISGGERRRVSIAVQLLWDPKVLILDEPTSGLDSFTAL 180
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 488984955 498 EFWLHINSMVDKGVTVMVTTH------FmdeaEYCDRIGLVYHGKLIASG 541
Cdd:cd03234 181 NLVSTLSQLARRNRIVILTIHqprsdlF----RLFDRILLLSSGEIVYSG 226
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
350-574 |
6.87e-16 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 77.67 E-value: 6.87e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 350 FQVKRGEIFGLLGPNGAGKSTTFKMMCGLLvPTSGKALVLGMDLKVSSG-KARQHLGYMAQKFSLYGNLSVEQNLRFFSG 428
Cdd:PRK03695 17 AEVRAGEILHLVGPNGAGKSTLLARMAGLL-PGSGSIQFAGQPLEAWSAaELARHRAYLSQQQTPPFAMPVFQYLTLHQP 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 429 VyGLRGRAQNEKIARMSDAFGLKS-IARHaADELPLGYKQRLALACSLMH-EPDI------LFLDEPTSGVDplTRREFW 500
Cdd:PRK03695 96 D-KTRTEAVASALNEVAEALGLDDkLGRS-VNQLSGGEWQRVRLAAVVLQvWPDInpagqlLLLDEPMNSLD--VAQQAA 171
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 488984955 501 LH--INSMVDKGVTVMVTTHFMDE-AEYCDRIGLVYHGKLIASGTPdalkaqaaDDSQTDPTMEQAFITLINRWDKE 574
Cdd:PRK03695 172 LDrlLSELCQQGIAVVMSSHDLNHtLRHADRVWLLKQGKLLASGRR--------DEVLTPENLAQVFGVNFRRLDVE 240
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
4-215 |
7.29e-16 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 77.80 E-value: 7.29e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 4 TVIALNGLSRRFPgmDRPAVAPLTCTIRAGYVTGLVGPDGAGKTTLMRMLAGLLKPDEGrASVIGFDPL---KDDSALha 80
Cdd:PRK11247 11 TPLLLNAVSKRYG--ERTVLNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAG-ELLAGTAPLaeaREDTRL-- 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 81 vlgyMPQKFGLYEDLTVMEN--LTLYADLRSVTGEArkkifdrlLEFTSLGPFTERLAGKLSGGMKQKLGLACTLVGDPK 158
Cdd:PRK11247 86 ----MFQDARLLPWKKVIDNvgLGLKGQWRDAALQA--------LAAVGLADRANEWPAALSGGQKQRVALARALIHRPG 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 488984955 159 VLLLDEPGVGVDPISRRELWQMVHELAGD-GMLILWSTSYLDEAEQCRD-VLLMNEGKL 215
Cdd:PRK11247 154 LLLLDEPLGALDALTRIEMQDLIESLWQQhGFTVLLVTHDVSEAVAMADrVLLIEEGKI 212
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
1-492 |
7.53e-16 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 80.52 E-value: 7.53e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 1 MSETVIALNGLSRRF--PGMDRPAVAPLTCTIRAGYVTGLVGPDGAGKT----TLMRML--------------AG--LLK 58
Cdd:PRK15134 1 MTQPLLAIENLSVAFrqQQTVRTVVNDVSLQIEAGETLALVGESGSGKSvtalSILRLLpsppvvypsgdirfHGesLLH 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 59 PDE--------GRASVIGFDPLKDDSALHAVlgympQKfGLYEDLTVMenltlyadlRSVTGEARKKIFDRLLEFTSLGP 130
Cdd:PRK15134 81 ASEqtlrgvrgNKIAMIFQEPMVSLNPLHTL-----EK-QLYEVLSLH---------RGMRREAARGEILNCLDRVGIRQ 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 131 FTERLAG---KLSGGMKQKLGLACTLVGDPKVLLLDEPGVGVDPISRRELWQMVHELAGD-GMLILWSTSYLDEAEQCRD 206
Cdd:PRK15134 146 AAKRLTDyphQLSGGERQRVMIAMALLTRPELLIADEPTTALDVSVQAQILQLLRELQQElNMGLLFITHNLSIVRKLAD 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 207 -VLLMNEGKLLYQGEPTALtqtmagrsflVSSPQEN-NRRLLqralklpqvsdgviqgksvrlilkkDARIEevqqhGDM 284
Cdd:PRK15134 226 rVAVMQNGRCVEQNRAATL----------FSAPTHPyTQKLL-------------------------NSEPS-----GDP 265
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 285 PPLQvADTAPrfedafidLLggagtaesplgaiihRVDGSKEETVIEAQSLTKKFGDFAATDHVDFQVKRGEIFGLLGPN 364
Cdd:PRK15134 266 VPLP-EPASP--------LL---------------DVEQLQVAFPIRKGILKRTVDHNVVVKNISFTLRPGETLGLVGES 321
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 365 GAGKSTTfkmmcGL----LVPTSGKALVLGMDLKVSSgkARQHLGYMAQ--------KFSLYGNLSVEQ----NLRFFSG 428
Cdd:PRK15134 322 GSGKSTT-----GLallrLINSQGEIWFDGQPLHNLN--RRQLLPVRHRiqvvfqdpNSSLNPRLNVLQiieeGLRVHQP 394
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 488984955 429 VygLRGRAQNEKIARMSDAFGLKSIARHA-ADELPLGYKQRLALACSLMHEPDILFLDEPTSGVD 492
Cdd:PRK15134 395 T--LSAAQREQQVIAVMEEVGLDPETRHRyPAEFSGGQRQRIAIARALILKPSLIILDEPTSSLD 457
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
35-219 |
1.28e-15 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 78.38 E-value: 1.28e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 35 VTGLVGPDGAGKTTLMRMLAGLLKPDEGRASVIG---FD--------PLKDDsalhavLGYMPQKFGLYEDLTVMENLtL 103
Cdd:PRK11144 26 ITAIFGRSGAGKTSLINAISGLTRPQKGRIVLNGrvlFDaekgiclpPEKRR------IGYVFQDARLFPHYKVRGNL-R 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 104 YADLRSVTGEarkkiFDRLLEFTSLGPFTERLAGKLSGGMKQKLGLACTLVGDPKVLLLDEPGVGVDPISRRELWQMVHE 183
Cdd:PRK11144 99 YGMAKSMVAQ-----FDKIVALLGIEPLLDRYPGSLSGGEKQRVAIGRALLTAPELLLMDEPLASLDLPRKRELLPYLER 173
|
170 180 190
....*....|....*....|....*....|....*...
gi 488984955 184 LAGDGML-ILWSTSYLDEAEQCRD-VLLMNEGKLLYQG 219
Cdd:PRK11144 174 LAREINIpILYVSHSLDEILRLADrVVVLEQGKVKAFG 211
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
38-221 |
1.48e-15 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 77.15 E-value: 1.48e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 38 LVGPDGAGKTTLMRMLAGLLKPDEGRASVIGfDPLKDDSaLHAVLGYMPQKFGLYEDL----TVMENLTLYADLRSVTGE 113
Cdd:PRK13652 35 VIGPNGAGKSTLFRHFNGILKPTSGSVLIRG-EPITKEN-IREVRKFVGLVFQNPDDQifspTVEQDIAFGPINLGLDEE 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 114 ARKKIFDRLLEFTSLGPFTERLAGKLSGGMKQKLGLACTLVGDPKVLLLDEPGVGVDPISRRELWQMVHELAGD-GMLIL 192
Cdd:PRK13652 113 TVAHRVSSALHMLGLEELRDRVPHHLSGGEKKRVAIAGVIAMEPQVLVLDEPTAGLDPQGVKELIDFLNDLPETyGMTVI 192
|
170 180 190
....*....|....*....|....*....|
gi 488984955 193 WSTSYLD-EAEQCRDVLLMNEGKLLYQGEP 221
Cdd:PRK13652 193 FSTHQLDlVPEMADYIYVMDKGRIVAYGTV 222
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
29-221 |
1.50e-15 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 77.37 E-value: 1.50e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 29 TIRAGYVTGLVGPDGAGKTTLMRMLAGLLKPDEGRASvIGFDPL------KDDSALHAVLGYMPQ--KFGLYEDlTVMEN 100
Cdd:PRK13634 29 SIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVT-IGERVItagkknKKLKPLRKKVGIVFQfpEHQLFEE-TVEKD 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 101 LTLYADLRSVTGEARKKIFDRLLEFTSLGP-FTERLAGKLSGGMKQKLGLACTLVGDPKVLLLDEPGVGVDPISRRELWQ 179
Cdd:PRK13634 107 ICFGPMNFGVSEEDAKQKAREMIELVGLPEeLLARSPFELSGGQMRRVAIAGVLAMEPEVLVLDEPTAGLDPKGRKEMME 186
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 488984955 180 MVHELAGD-GMLILWSTSYLDEAEQCRD-VLLMNEGKLLYQGEP 221
Cdd:PRK13634 187 MFYKLHKEkGLTTVLVTHSMEDAARYADqIVVMHKGTVFLQGTP 230
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
27-229 |
2.28e-15 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 76.46 E-value: 2.28e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 27 TCTIRAGYVTGLVGPDGAGKTTLMRMLAGLLKPDEGRASVIGfdpLKDDSAL-HAVLGYMPQKFG-------LYEDLTVM 98
Cdd:PRK15056 27 SFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKISILG---QPTRQALqKNLVAYVPQSEEvdwsfpvLVEDVVMM 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 99 ENLTLYADLRSVTGEARKkIFDRLLEFTSLGPFTERLAGKLSGGMKQKLGLACTLVGDPKVLLLDEPGVGVDPISRRELW 178
Cdd:PRK15056 104 GRYGHMGWLRRAKKRDRQ-IVTAALARVDMVEFRHRQIGELSGGQKKRVFLARAIAQQGQVILLDEPFTGVDVKTEARII 182
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 488984955 179 QMVHELAGDGMLILWSTSYLDEAEQCRDVLLMNEGKLLYQGePTALTQTMA 229
Cdd:PRK15056 183 SLLRELRDEGKTMLVSTHNLGSVTEFCDYTVMVKGTVLASG-PTETTFTAE 232
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
21-226 |
2.49e-15 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 79.12 E-value: 2.49e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 21 PAVAPLTCTIRAGYVTGLVGPDGAGKTTLMRMLAGLLkPDEGRASVIGFdPLKDDSALH-----AVLGYMPQKF-Glyed 94
Cdd:PRK11174 364 TLAGPLNFTLPAGQRIALVGPSGAGKTSLLNALLGFL-PYQGSLKINGI-ELRELDPESwrkhlSWVGQNPQLPhG---- 437
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 95 lTVMENLTLyADlrsvtGEARKKIFDRLLEFTSLGPFTERL-----------AGKLSGGMKQKLGLACTLVGDPKVLLLD 163
Cdd:PRK11174 438 -TLRDNVLL-GN-----PDASDEQLQQALENAWVSEFLPLLpqgldtpigdqAAGLSVGQAQRLALARALLQPCQLLLLD 510
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 488984955 164 EPGVGVDPISRRELWQMVHELAGDGMLILwSTSYLDEAEQCRDVLLMNEGKLLYQGEPTALTQ 226
Cdd:PRK11174 511 EPTASLDAHSEQLVMQALNAASRRQTTLM-VTHQLEDLAQWDQIWVMQDGQIVQQGDYAELSQ 572
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
324-564 |
2.55e-15 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 76.46 E-value: 2.55e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 324 SKEETVIEAQSLTKKFGDFAATDhVDFQVKRGEIFGLLGPNGAGKSTTFKMMCGLLVPTSGKALVLGMDLKVSsgkARQH 403
Cdd:PRK15056 3 QQAGIVVNDVTVTWRNGHTALRD-ASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKISILGQPTRQA---LQKN 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 404 L-GYMAQKFSLYGNLSVEQNLRFFSGVYGLRG---RAQNEKIARMSDAFGLKSIA--RH-AADELPLGYKQRLALACSLM 476
Cdd:PRK15056 79 LvAYVPQSEEVDWSFPVLVEDVVMMGRYGHMGwlrRAKKRDRQIVTAALARVDMVefRHrQIGELSGGQKKRVFLARAIA 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 477 HEPDILFLDEPTSGVDPLTRREFWLHINSMVDKGVTVMVTTHFMDE-AEYCDRIGLVyHGKLIASGtpdalkaqAADDSQ 555
Cdd:PRK15056 159 QQGQVILLDEPFTGVDVKTEARIISLLRELRDEGKTMLVSTHNLGSvTEFCDYTVMV-KGTVLASG--------PTETTF 229
|
....*....
gi 488984955 556 TDPTMEQAF 564
Cdd:PRK15056 230 TAENLELAF 238
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
4-224 |
2.79e-15 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 75.94 E-value: 2.79e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 4 TVIALNGLSRRFPGmdRPAVAPLTCTIRAGYVTGLVGPDGAGKTTLMRMLAGLLKPDEGRASV--IGFD---PLKDDSAL 78
Cdd:PRK11264 2 SAIEVKNLVKKFHG--QTVLHGIDLEVKPGEVVAIIGPSGSGKTTLLRCINLLEQPEAGTIRVgdITIDtarSLSQQKGL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 79 HAVL----GYMPQKFGLYEDLTVMENLTLYADLrsVTGEARKKIFDR---LLEFTSLGPFTERLAGKLSGGMKQKLGLAC 151
Cdd:PRK11264 80 IRQLrqhvGFVFQNFNLFPHRTVLENIIEGPVI--VKGEPKEEATARareLLAKVGLAGKETSYPRRLSGGQQQRVAIAR 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 488984955 152 TLVGDPKVLLLDEPGVGVDPISRRELWQMVHELAGDGMLILWSTSYLDEAEQCRD-VLLMNEGKLLYQGEPTAL 224
Cdd:PRK11264 158 ALAMRPEVILFDEPTSALDPELVGEVLNTIRQLAQEKRTMVIVTHEMSFARDVADrAIFMDQGRIVEQGPAKAL 231
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
348-544 |
3.80e-15 |
|
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: 74.10 E-value: 3.80e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 348 VDFQVKRGEIFGLLGPNGAGKSTTFKMMCGL--LVPTSGKALVLGMDLKVSSGKARQHLG-YMA-QKFSLYGNLSVEQNL 423
Cdd:cd03217 19 VNLTIKKGEVHALMGPNGSGKSTLAKTIMGHpkYEVTEGEILFKGEDITDLPPEERARLGiFLAfQYPPEIPGVKNADFL 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 424 RF----FSGvyglrgraqnekiarmsdafglksiarhaadelplGYKQRLALACSLMHEPDILFLDEPTSGVDPLTRREF 499
Cdd:cd03217 99 RYvnegFSG-----------------------------------GEKKRNEILQLLLLEPDLAILDEPDSGLDIDALRLV 143
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 488984955 500 WLHINSMVDKGVTVMVTTHFMDEAEYC--DRIGLVYHGKLIASGTPD 544
Cdd:cd03217 144 AEVINKLREEGKSVLIITHYQRLLDYIkpDRVHVLYDGRIVKSGDKE 190
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
27-256 |
4.56e-15 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 76.28 E-value: 4.56e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 27 TCTIRAGYVTGLVGPDGAGKTTLMRMLAGLLKPDEGRASVIGFD-------------------------PLKDDSALHAV 81
Cdd:PRK13651 27 SVEINQGEFIAIIGQTGSGKTTFIEHLNALLLPDTGTIEWIFKDeknkkktkekekvleklviqktrfkKIKKIKEIRRR 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 82 LGYMPQ--KFGLYEDlTVMENLTLYADLRSVTGEARKKIFDRLLEFTSLG-PFTERLAGKLSGGMKQKLGLACTLVGDPK 158
Cdd:PRK13651 107 VGVVFQfaEYQLFEQ-TIEKDIIFGPVSMGVSKEEAKKRAAKYIELVGLDeSYLQRSPFELSGGQKRRVALAGILAMEPD 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 159 VLLLDEPGVGVDPISRRELWQMVHELAGDGMLILWSTSYLDEA-EQCRDVLLMNEGKLLYQGEPtalTQTMAGRSFLVss 237
Cdd:PRK13651 186 FLVFDEPTAGLDPQGVKEILEIFDNLNKQGKTIILVTHDLDNVlEWTKRTIFFKDGKIIKDGDT---YDILSDNKFLI-- 260
|
250 260
....*....|....*....|....*....
gi 488984955 238 pqENN----------RRLLQRALKLPQVS 256
Cdd:PRK13651 261 --ENNmeppkllnfvNKLEKKGIDVPKVT 287
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
4-184 |
4.97e-15 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 75.15 E-value: 4.97e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 4 TVIALNGLSRRFPgmDRPAVAPLTCTIRAGYVTGLVGPDGAGKTTLMRMLAGLLKPDEGRasvigfdpLKDDSALHavLG 83
Cdd:PRK09544 3 SLVSLENVSVSFG--QRRVLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGV--------IKRNGKLR--IG 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 84 YMPQKfgLYEDLTVmeNLTLYADLRSVTGEARKKIFDrLLEFTSLGPFTERLAGKLSGGMKQKLGLACTLVGDPKVLLLD 163
Cdd:PRK09544 71 YVPQK--LYLDTTL--PLTVNRFLRLRPGTKKEDILP-ALKRVQAGHLIDAPMQKLSGGETQRVLLARALLNRPQLLVLD 145
|
170 180
....*....|....*....|.
gi 488984955 164 EPGVGVDPISRRELWQMVHEL 184
Cdd:PRK09544 146 EPTQGVDVNGQVALYDLIDQL 166
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
3-230 |
5.06e-15 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 77.76 E-value: 5.06e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 3 ETVIALNGLSRRfPGMDRPAVAPLTCTIRAGYVTGLVGPDGAGKTTLMRMLAGLLKPDEGRASVIGFDPLKDDSA--LHA 80
Cdd:COG3845 255 EVVLEVENLSVR-DDRGVPALKDVSLEVRAGEILGIAGVAGNGQSELAEALAGLRPPASGSIRLDGEDITGLSPRerRRL 333
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 81 VLGYMP---QKFGLYEDLTVMENLTLYA------------DLRSVTGEARKKI--FD-RlleftslGPFTERLAGKLSGG 142
Cdd:COG3845 334 GVAYIPedrLGRGLVPDMSVAENLILGRyrrppfsrggflDRKAIRAFAEELIeeFDvR-------TPGPDTPARSLSGG 406
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 143 MKQKLGLACTLVGDPKVLLLDEPGVGVDPISRRELWQMVHELAGDGMLILWSTSYLDEAEQCRD-VLLMNEGKLLYQGEP 221
Cdd:COG3845 407 NQQKVILARELSRDPKLLIAAQPTRGLDVGAIEFIHQRLLELRDAGAAVLLISEDLDEILALSDrIAVMYEGRIVGEVPA 486
|
250
....*....|....
gi 488984955 222 TALTQT-----MAG 230
Cdd:COG3845 487 AEATREeigllMAG 500
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
328-541 |
5.65e-15 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 74.95 E-value: 5.65e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 328 TVIEAQSLTKKFGDFAATDHVDFQVKRGEIFGLLGPNGAGKSTTFKMMCGL--LVP---TSGKALVLGMDL-KVSSGKAR 401
Cdd:PRK14247 2 NKIEIRDLKVSFGQVEVLDGVNLEIPDNTITALMGPSGSGKSTLLRVFNRLieLYPearVSGEVYLDGQDIfKMDVIELR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 402 QHLGYMAQKFSLYGNLSVEQNLRFfsgvyGLR----GRAQNEKIARMSDAF-------GLKSIARHAADELPLGYKQRLA 470
Cdd:PRK14247 82 RRVQMVFQIPNPIPNLSIFENVAL-----GLKlnrlVKSKKELQERVRWALekaqlwdEVKDRLDAPAGKLSGGQQQRLC 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 488984955 471 LACSLMHEPDILFLDEPTSGVDPltrrEFWLHINSM---VDKGVTVMVTTHFMDE-AEYCDRIGLVYHGKLIASG 541
Cdd:PRK14247 157 IARALAFQPEVLLADEPTANLDP----ENTAKIESLfleLKKDMTIVLVTHFPQQaARISDYVAFLYKGQIVEWG 227
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
26-222 |
6.44e-15 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 74.95 E-value: 6.44e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 26 LTCTIRAGYVTGLVGPDGAGKTTLMRMLAGL--LKPD---EGRASVIGFDPLKDD-SALHAVLGYMPQKFGLYEDLTVME 99
Cdd:PRK14247 22 VNLEIPDNTITALMGPSGSGKSTLLRVFNRLieLYPEarvSGEVYLDGQDIFKMDvIELRRRVQMVFQIPNPIPNLSIFE 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 100 NLTLYADLRSVTgEARKKIFDRL---LEFTSL-GPFTERL---AGKLSGGMKQKLGLACTLVGDPKVLLLDEPGVGVDPI 172
Cdd:PRK14247 102 NVALGLKLNRLV-KSKKELQERVrwaLEKAQLwDEVKDRLdapAGKLSGGQQQRLCIARALAFQPEVLLADEPTANLDPE 180
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 488984955 173 SRRELWQMVHELAGDgMLILWSTSYLDEAEQCRD-VLLMNEGKLLYQGePT 222
Cdd:PRK14247 181 NTAKIESLFLELKKD-MTIVLVTHFPQQAARISDyVAFLYKGQIVEWG-PT 229
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
5-546 |
7.59e-15 |
|
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose isomerase and xylulokinase enzymes for xylose utilization. Members of this protein family are the ATP-binding cassette (ABC) subunit of the known or predicted high-affinity xylose ABC transporter for xylose import. These genes, which closely resemble other sugar transport ABC transporter genes, typically are encoded near xylose utilization enzymes and regulatory proteins. Note that this form of the transporter contains two copies of the ABC transporter domain (pfam00005). [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 131681 [Multi-domain] Cd Length: 500 Bit Score: 77.17 E-value: 7.59e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 5 VIALNGLSRRFPGMDrpAVAPLTCTIRAGYVTGLVGPDGAGKTTLMRMLAGLLkPDEGRASVIGFD--PLKDDS---ALH 79
Cdd:TIGR02633 1 LLEMKGIVKTFGGVK--ALDGIDLEVRPGECVGLCGENGAGKSTLMKILSGVY-PHGTWDGEIYWSgsPLKASNirdTER 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 80 AVLGYMPQKFGLYEDLTVMENLTLYADLRSVTGEA-------RKKIFDRLLEFTSLgPFTeRLAGKLSGGMKQKLGLACT 152
Cdd:TIGR02633 78 AGIVIIHQELTLVPELSVAENIFLGNEITLPGGRMaynamylRAKNLLRELQLDAD-NVT-RPVGDYGGGQQQLVEIAKA 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 153 LVGDPKVLLLDEPGVGVDPISRRELWQMVHELAGDGMLILWSTSYLDEAEQ-CRDVLLMNEGKLLYQGEPTALTQ----- 226
Cdd:TIGR02633 156 LNKQARLLILDEPSSSLTEKETEILLDIIRDLKAHGVACVYISHKLNEVKAvCDTICVIRDGQHVATKDMSTMSEddiit 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 227 TMAGRSFLVSSPQEnnrrllqralklpqvsdgviqgksvrlilkkdarieevqqhgdmpPLQVADTAPRFEDAfidllgg 306
Cdd:TIGR02633 236 MMVGREITSLYPHE---------------------------------------------PHEIGDVILEARNL------- 263
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 307 agTAESPLGAIIHRVDgskeetvieaqsltkkfgdfaatdHVDFQVKRGEIFGLLGPNGAGKSTTFKMMCGLLVPT-SGK 385
Cdd:TIGR02633 264 --TCWDVINPHRKRVD------------------------DVSFSLRRGEILGVAGLVGAGRTELVQALFGAYPGKfEGN 317
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 386 ALVLG--MDLKVSSGKARQHLGYMAQKFSLYG---NLSVEQN-----LRFFSGVYGLRGRAQNEKIARMSDAFGLKSiar 455
Cdd:TIGR02633 318 VFINGkpVDIRNPAQAIRAGIAMVPEDRKRHGivpILGVGKNitlsvLKSFCFKMRIDAAAELQIIGSAIQRLKVKT--- 394
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 456 hAADELPL-----GYKQRLALACSLMHEPDILFLDEPTSGVDPLTRREFWLHINSMVDKGVTVMVTTHFMDEA-EYCDRI 529
Cdd:TIGR02633 395 -ASPFLPIgrlsgGNQQKAVLAKMLLTNPRVLILDEPTRGVDVGAKYEIYKLINQLAQEGVAIIVVSSELAEVlGLSDRV 473
|
570
....*....|....*..
gi 488984955 530 GLVYHGKLIASGTPDAL 546
Cdd:TIGR02633 474 LVIGEGKLKGDFVNHAL 490
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
30-232 |
8.78e-15 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 74.15 E-value: 8.78e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 30 IRAGYVTGLVGPDGAGKTTLMRMLAGLLKPDEGRASVIGFDPLKDDSA--LHAVLGYMPQKFGLYEDLTVMENLTL---Y 104
Cdd:PRK11614 28 INQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDGKDITDWQTAkiMREAVAIVPEGRRVFSRMTVEENLAMggfF 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 105 ADLRSVTGEARK--KIFDRLLEFTSlgpfteRLAGKLSGGMKQKLGLACTLVGDPKVLLLDEPGVGVDPISRRELWQMVH 182
Cdd:PRK11614 108 AERDQFQERIKWvyELFPRLHERRI------QRAGTMSGGEQQMLAIGRALMSQPRLLLLDEPSLGLAPIIIQQIFDTIE 181
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 488984955 183 ELAGDGMLILWSTSYLDEAEQCRDV-LLMNEGKLLYQGEPTALTQTMAGRS 232
Cdd:PRK11614 182 QLREQGMTIFLVEQNANQALKLADRgYVLENGHVVLEDTGDALLANEAVRS 232
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
19-224 |
9.75e-15 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 77.45 E-value: 9.75e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 19 DRPAVAPLTCTIRAGYVTGLVGPDGAGKTTLMRMLAGLLKPDEGRASVIGfDPLK--DDSALH---AVLGYMPQKFGlye 93
Cdd:TIGR00958 493 DVPVLKGLTFTLHPGEVVALVGPSGSGKSTVAALLQNLYQPTGGQVLLDG-VPLVqyDHHYLHrqvALVGQEPVLFS--- 568
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 94 dLTVMENLTL---YADLRSVTGEARKKIFDRLLEFTSLGPFTE--RLAGKLSGGMKQKLGLACTLVGDPKVLLLDEPGVG 168
Cdd:TIGR00958 569 -GSVRENIAYgltDTPDEEIMAAAKAANAHDFIMEFPNGYDTEvgEKGSQLSGGQKQRIAIARALVRKPRVLILDEATSA 647
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 488984955 169 VDPISRRELWQMvHELAGDGMLILwsTSYLDEAEQCRDVLLMNEGKLLYQGEPTAL 224
Cdd:TIGR00958 648 LDAECEQLLQES-RSRASRTVLLI--AHRLSTVERADQILVLKKGSVVEMGTHKQL 700
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
328-492 |
1.07e-14 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 73.99 E-value: 1.07e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 328 TVIEAQSLTKKFGDFAATDHVDFQVKRGEIFGLLGPNGAGKSTTFKMMCGLLVPTSGKAlvlgmdlkVSSGKARqhLGYM 407
Cdd:PRK09544 3 SLVSLENVSVSFGQRRVLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVI--------KRNGKLR--IGYV 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 408 AQKFSLYGN--LSVEQNLRFFSGVyglrgraqnekiaRMSDAF-GLKSI-ARHAAD----ELPLGYKQRLALACSLMHEP 479
Cdd:PRK09544 73 PQKLYLDTTlpLTVNRFLRLRPGT-------------KKEDILpALKRVqAGHLIDapmqKLSGGETQRVLLARALLNRP 139
|
170
....*....|...
gi 488984955 480 DILFLDEPTSGVD 492
Cdd:PRK09544 140 QLLVLDEPTQGVD 152
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
29-227 |
1.21e-14 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 74.36 E-value: 1.21e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 29 TIRAGYVTGLVGPDGAGKTTLMRMLAGLLKPDEGRASVIGfDPLKDDSALHavlgyMPQKFGL--------YEDLTVMEN 100
Cdd:PRK13642 29 SITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDG-ELLTAENVWN-----LRRKIGMvfqnpdnqFVGATVEDD 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 101 LTLYADLRSVTGEARKKIFDRLLEFTSLGPFTERLAGKLSGGMKQKLGLACTLVGDPKVLLLDEPGVGVDPISRRELWQM 180
Cdd:PRK13642 103 VAFGMENQGIPREEMIKRVDEALLAVNMLDFKTREPARLSGGQKQRVAVAGIIALRPEIIILDESTSMLDPTGRQEIMRV 182
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 488984955 181 VHELAGDGMLILWSTSY-LDEAEQCRDVLLMNEGKLLYQGEPTALTQT 227
Cdd:PRK13642 183 IHEIKEKYQLTVLSITHdLDEAASSDRILVMKAGEIIKEAAPSELFAT 230
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
19-215 |
1.33e-14 |
|
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; TAP (Transporter Associated with Antigen Processing) is essential for peptide delivery from the cytosol into the lumen of the endoplasmic reticulum (ER), where these peptides are loaded on major histocompatibility complex (MHC) I molecules. Loaded MHC I leave the ER and display their antigenic cargo on the cell surface to cytotoxic T cells. Subsequently, virus-infected or malignantly transformed cells can be eliminated. TAP belongs to the large family of ATP-binding cassette (ABC) transporters, which translocate a vast variety of solutes across membranes.
Pssm-ID: 213215 [Multi-domain] Cd Length: 226 Bit Score: 73.27 E-value: 1.33e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 19 DRPAVAPLTCTIRAGYVTGLVGPDGAGKTTLMRMLAGLLKPDEGRASVIGFD-PLKDDSALH---AVLGYMPQKFGlyed 94
Cdd:cd03248 26 DTLVLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDGKPiSQYEHKYLHskvSLVGQEPVLFA---- 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 95 LTVMENLTlY----ADLRSVTGEARKKIFDRLLEFTSLGPFTE--RLAGKLSGGMKQKLGLACTLVGDPKVLLLDEPGVG 168
Cdd:cd03248 102 RSLQDNIA-YglqsCSFECVKEAAQKAHAHSFISELASGYDTEvgEKGSQLSGGQKQRVAIARALIRNPQVLILDEATSA 180
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 488984955 169 VDPISRrelwQMVHELAGDGM---LILWSTSYLDEAEQCRDVLLMNEGKL 215
Cdd:cd03248 181 LDAESE----QQVQQALYDWPerrTVLVIAHRLSTVERADQILVLDGGRI 226
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
29-170 |
1.42e-14 |
|
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI), is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI's are not transport proteins and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLI's have an N-terminal Fe-S domain and two nucleotide-binding domains which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity of more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213204 [Multi-domain] Cd Length: 246 Bit Score: 73.60 E-value: 1.42e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 29 TIRAGYVTGLVGPDGAGKTTLMRMLAGLLKPDEGRASVIGFDplkddsalhavLGYMPQKFGLYEDLTVmenltlYADLR 108
Cdd:cd03237 21 SISESEVIGILGPNGIGKTTFIKMLAGVLKPDEGDIEIELDT-----------VSYKPQYIKADYEGTV------RDLLS 83
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 488984955 109 SVTGEA------RKKIFDRLleftSLGPFTERLAGKLSGGMKQKLGLACTLVGDPKVLLLDEPGVGVD 170
Cdd:cd03237 84 SITKDFythpyfKTEIAKPL----QIEQILDREVPELSGGELQRVAIAACLSKDADIYLLDEPSAYLD 147
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
329-518 |
1.56e-14 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 72.99 E-value: 1.56e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 329 VIEAQSLTKKF-GDFAATDHVDFQVKRGEIFGLLGPNGAGKSTTFKMMCGLLVPTSGKALVLGMDLKVSSGKA----RQH 403
Cdd:PRK10908 1 MIRFEHVSKAYlGGRQALQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDITRLKNREvpflRRQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 404 LGYMAQKFSLYGNLSVEQNLRFFSGVYGLRGRAQNEKIARMSDAFGLKSIARHAADELPLGYKQRLALACSLMHEPDILF 483
Cdd:PRK10908 81 IGMIFQDHHLLMDRTVYDNVAIPLIIAGASGDDIRRRVSAALDKVGLLDKAKNFPIQLSGGEQQRVGIARAVVNKPAVLL 160
|
170 180 190
....*....|....*....|....*....|....*
gi 488984955 484 LDEPTSGVDPLTRREFWLHINSMVDKGVTVMVTTH 518
Cdd:PRK10908 161 ADEPTGNLDDALSEGILRLFEEFNRVGVTVLMATH 195
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
330-538 |
1.65e-14 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 73.58 E-value: 1.65e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 330 IEAQSLTKKFgdFAAT-------DHVDFQVKRGEIFGLLGPNGAGKSTTFKMMCGLLVPTSGKALVLGMDlkVSSGKARQ 402
Cdd:COG1101 2 LELKNLSKTF--NPGTvnekralDGLNLTIEEGDFVTVIGSNGAGKSTLLNAIAGSLPPDSGSILIDGKD--VTKLPEYK 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 403 HLGYMAQKF--SLYG---NLSVEQNL-----RffSGVYGLRGRAQNEKIA---------------RMSDAFGLksiarha 457
Cdd:COG1101 78 RAKYIGRVFqdPMMGtapSMTIEENLalayrR--GKRRGLRRGLTKKRRElfrellatlglglenRLDTKVGL------- 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 458 adeLPLGYKQRLALACSLMHEPDILFLDEPTSGVDP--------LTRRefwlhinsMV-DKGVTVMVTTHFMDEA-EYCD 527
Cdd:COG1101 149 ---LSGGQRQALSLLMATLTKPKLLLLDEHTAALDPktaalvleLTEK--------IVeENNLTTLMVTHNMEQAlDYGN 217
|
250
....*....|.
gi 488984955 528 RIGLVYHGKLI 538
Cdd:COG1101 218 RLIMMHEGRII 228
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
17-257 |
2.45e-14 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 75.72 E-value: 2.45e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 17 GMDRPAVA-PLTCTIRAGYVTGLVGPDGAGKTTLMRMLAGLLKPDEGRASVIGfDPLKDDSALHAV-LGYM--PQ--KF- 89
Cdd:PRK11288 262 GLKGPGLRePISFSVRAGEIVGLFGLVGAGRSELMKLLYGATRRTAGQVYLDG-KPIDIRSPRDAIrAGIMlcPEdrKAe 340
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 90 GLYEDLTVMENLTLYA-----------DLRSVTGEARKKIfDRLLEFTslgPFTERLAGKLSGGMKQKLGLACTLVGDPK 158
Cdd:PRK11288 341 GIIPVHSVADNINISArrhhlragcliNNRWEAENADRFI-RSLNIKT---PSREQLIMNLSGGNQQKAILGRWLSEDMK 416
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 159 VLLLDEPGVGVDPISRRELWQMVHELAGDGMLILWSTSYLDEAEQCRD-VLLMNEGKLlyQGEptaltqtmagrsflVSS 237
Cdd:PRK11288 417 VILLDEPTRGIDVGAKHEIYNVIYELAAQGVAVLFVSSDLPEVLGVADrIVVMREGRI--AGE--------------LAR 480
|
250 260
....*....|....*....|
gi 488984955 238 PQENNRRLLQraLKLPQVSD 257
Cdd:PRK11288 481 EQATERQALS--LALPRTSA 498
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
5-191 |
2.49e-14 |
|
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of the ABC transporter ATP-binding cassette, but are found outside the common ABC transporter operon structure that features integral membrane permease proteins and substrate-binding proteins encoded next to the ATP-binding cassette (ABC domain) protein. The member protein ChvD from Agrobacterium tumefaciens was identified as both a candidate to interact with VirB8, based on yeast two-hybrid analysis, and as an apparent regulator of VirG. The general function of this protein family is unknown.
Pssm-ID: 274744 [Multi-domain] Cd Length: 552 Bit Score: 75.74 E-value: 2.49e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 5 VIALNGLSRRFPgmDRPAVAPLTCTIRAGYVTGLVGPDGAGKTTLMRMLAGLLKPDEGRASvIGfDPLKddsalhavLGY 84
Cdd:TIGR03719 322 VIEAENLTKAFG--DKLLIDDLSFKLPPGGIVGVIGPNGAGKSTLFRMITGQEQPDSGTIE-IG-ETVK--------LAY 389
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 85 MPQ-KFGLYEDLTVMENLTLYADLRSVTGearKKIFDR--LLEFTSLGPFTERLAGKLSGGMKQKLGLACTLVGDPKVLL 161
Cdd:TIGR03719 390 VDQsRDALDPNKTVWEEISGGLDIIKLGK---REIPSRayVGRFNFKGSDQQKKVGQLSGGERNRVHLAKTLKSGGNVLL 466
|
170 180 190
....*....|....*....|....*....|
gi 488984955 162 LDEPGVGVDPISRRELWQMVHELAGDGMLI 191
Cdd:TIGR03719 467 LDEPTNDLDVETLRALEEALLNFAGCAVVI 496
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
334-546 |
2.96e-14 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 74.68 E-value: 2.96e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 334 SLTKKFGDFAATDHVDFQVKRGEIFGLLGPNGAGKSTTFKMMCGLLVPTSGKaLVLGMDLKVSSGKARQHLGYMAQKFSL 413
Cdd:PRK11000 8 NVTKAYGDVVISKDINLDIHEGEFVVFVGPSGCGKSTLLRMIAGLEDITSGD-LFIGEKRMNDVPPAERGVGMVFQSYAL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 414 YGNLSVEQNLRFfsgvyGLR--GRAQNEKIARMSDAFGLKSIArHAADELPL----GYKQRLALACSLMHEPDILFLDEP 487
Cdd:PRK11000 87 YPHLSVAENMSF-----GLKlaGAKKEEINQRVNQVAEVLQLA-HLLDRKPKalsgGQRQRVAIGRTLVAEPSVFLLDEP 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 488984955 488 TSGVDPLTRREFWLHINSMVDK-GVTVMVTTHFMDEA-EYCDRIGLVYHGKLIASGTPDAL 546
Cdd:PRK11000 161 LSNLDAALRVQMRIEISRLHKRlGRTMIYVTHDQVEAmTLADKIVVLDAGRVAQVGKPLEL 221
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
39-165 |
2.99e-14 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 74.68 E-value: 2.99e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 39 VGPDGAGKTTLMRMLAGLLKPDEGRAsVIGFDPLKDDSALHAVLGYMPQKFGLYEDLTVMENLTLYADLRSVTGEARKKI 118
Cdd:PRK11000 35 VGPSGCGKSTLLRMIAGLEDITSGDL-FIGEKRMNDVPPAERGVGMVFQSYALYPHLSVAENMSFGLKLAGAKKEEINQR 113
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 488984955 119 FDRLLEFTSLGPFTERLAGKLSGGMKQKLGLACTLVGDPKVLLLDEP 165
Cdd:PRK11000 114 VNQVAEVLQLAHLLDRKPKALSGGQRQRVAIGRTLVAEPSVFLLDEP 160
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
1-537 |
3.03e-14 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 75.35 E-value: 3.03e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 1 MSETVIALNGLSRRFPGMdrPAVAPLTCTIRAGYVTGLVGPDGAGKTTLMRMLAG-----------LLKPDEGRASVIgf 69
Cdd:PRK13549 1 MMEYLLEMKNITKTFGGV--KALDNVSLKVRAGEIVSLCGENGAGKSTLMKVLSGvyphgtyegeiIFEGEELQASNI-- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 70 dplKDDSALHAVLGYmpQKFGLYEDLTVMENLTL--------YADLRSVTGEArkkifDRLLEFTSLGPFTERLAGKLSG 141
Cdd:PRK13549 77 ---RDTERAGIAIIH--QELALVKELSVLENIFLgneitpggIMDYDAMYLRA-----QKLLAQLKLDINPATPVGNLGL 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 142 GMKQKLGLACTLVGDPKVLLLDEPgvgVDPISRRE---LWQMVHELAGDGMLILWSTSYLDE-AEQCRDVLLMNEGKLLY 217
Cdd:PRK13549 147 GQQQLVEIAKALNKQARLLILDEP---TASLTESEtavLLDIIRDLKAHGIACIYISHKLNEvKAISDTICVIRDGRHIG 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 218 QGEPTALTQ-----TMAGRSFLVSSPQENNrrllqralklpQVSDGVIQGKSVrlilkkdarieevqqhgdmpplqvadt 292
Cdd:PRK13549 224 TRPAAGMTEddiitMMVGRELTALYPREPH-----------TIGEVILEVRNL--------------------------- 265
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 293 aprfedafidllggagTAESPLGAIIHRVdgskeetvieaqsltkkfgdfaatDHVDFQVKRGEIFGLLGPNGAGKSTTF 372
Cdd:PRK13549 266 ----------------TAWDPVNPHIKRV------------------------DDVSFSLRRGEILGIAGLVGAGRTELV 305
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 373 KMMCGLLV-PTSGKALVLGMDLKVSS-GKA-RQHLGYMAQ---KFSLYGNLSVEQN-----LRFFSGVYGLRGRAQ---- 437
Cdd:PRK13549 306 QCLFGAYPgRWEGEIFIDGKPVKIRNpQQAiAQGIAMVPEdrkRDGIVPVMGVGKNitlaaLDRFTGGSRIDDAAElkti 385
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 438 NEKIARMSdafglksiARHAADELPL-----GYKQRLALACSLMHEPDILFLDEPTSGVDPLTRREFWLHINSMVDKGVT 512
Cdd:PRK13549 386 LESIQRLK--------VKTASPELAIarlsgGNQQKAVLAKCLLLNPKILILDEPTRGIDVGAKYEIYKLINQLVQQGVA 457
|
570 580
....*....|....*....|....*..
gi 488984955 513 VMVTTHFMDEA-EYCDRIgLVYH-GKL 537
Cdd:PRK13549 458 IIVISSELPEVlGLSDRV-LVMHeGKL 483
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
346-543 |
4.87e-14 |
|
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: 71.29 E-value: 4.87e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 346 DHVDFQVKRGEIFGLLGPNGAGKSTTFKMMCGLLVPTSGKALVLGMDL-KVSSGKARQHLGYMAQKFSLYGNlSVEQNLR 424
Cdd:cd03369 25 KNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDGIDIsTIPLEDLRSSLTIIPQDPTLFSG-TIRSNLD 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 425 FFsgvyglrGRAQNEKIarmsdaFGLKSIArHAADELPLGYKQRLALACSLMHEPDILFLDEPTSGVDPLT--------R 496
Cdd:cd03369 104 PF-------DEYSDEEI------YGALRVS-EGGLNLSQGQRQLLCLARALLKRPRVLVLDEATASIDYATdaliqktiR 169
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 488984955 497 REFwlhinsmvdKGVTVMVTTHFMDEAEYCDRIGLVYHGKLIASGTP 543
Cdd:cd03369 170 EEF---------TNSTILTIAHRLRTIIDYDKILVMDAGEVKEYDHP 207
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
334-536 |
6.03e-14 |
|
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI), is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI's are not transport proteins and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLI's have an N-terminal Fe-S domain and two nucleotide-binding domains which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity of more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213204 [Multi-domain] Cd Length: 246 Bit Score: 71.67 E-value: 6.03e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 334 SLTKKFGDFAAT-DHVDFqvKRGEIFGLLGPNGAGKSTTFKMMCGLLVPTSGKALVLGMDlkVSsgkarqhlgYMAQKFS 412
Cdd:cd03237 5 TMKKTLGEFTLEvEGGSI--SESEVIGILGPNGIGKTTFIKMLAGVLKPDEGDIEIELDT--VS---------YKPQYIK 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 413 LYGNLSVEQNLRFFSGVYGLRGRAQNEKIarmsDAFGLKSIARHAADELPLGYKQRLALACSLMHEPDILFLDEPTSGVD 492
Cdd:cd03237 72 ADYEGTVRDLLSSITKDFYTHPYFKTEIA----KPLQIEQILDREVPELSGGELQRVAIAACLSKDADIYLLDEPSAYLD 147
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 488984955 493 PLTR-------REFWLHINSmvdkgvTVMVTTHFMDEAEY-CDRIgLVYHGK 536
Cdd:cd03237 148 VEQRlmaskviRRFAENNEK------TAFVVEHDIIMIDYlADRL-IVFEGE 192
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
29-221 |
6.27e-14 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 72.73 E-value: 6.27e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 29 TIRAGYVTGLVGPDGAGKTTLMRMLAGLLKPDEGRASV------IGFDPLKDDSALHAVLGYMPQ--KFGLYEDlTVMEN 100
Cdd:PRK13645 33 TFKKNKVTCVIGTTGSGKSTMIQLTNGLIISETGQTIVgdyaipANLKKIKEVKRLRKEIGLVFQfpEYQLFQE-TIEKD 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 101 LTL-YADLRSVTGEARKKIfDRLLEFTSLG-PFTERLAGKLSGGMKQKLGLACTLVGDPKVLLLDEPGVGVDPISRRELW 178
Cdd:PRK13645 112 IAFgPVNLGENKQEAYKKV-PELLKLVQLPeDYVKRSPFELSGGQKRRVALAGIIAMDGNTLVLDEPTGGLDPKGEEDFI 190
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 488984955 179 QMVHELAGD-GMLILWSTSYLDEAEQCRD-VLLMNEGKLLYQGEP 221
Cdd:PRK13645 191 NLFERLNKEyKKRIIMVTHNMDQVLRIADeVIVMHEGKVISIGSP 235
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
330-549 |
7.17e-14 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 74.50 E-value: 7.17e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 330 IEAQSLT-KKFGDFAATDHVDFQVKRGEIFGLLGPNGAGKSTTFKMMCGLLvPTSGKALVLGMDLKVSSGKA-RQHLGYM 407
Cdd:PRK11174 350 IEAEDLEiLSPDGKTLAGPLNFTLPAGQRIALVGPSGAGKTSLLNALLGFL-PYQGSLKINGIELRELDPESwRKHLSWV 428
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 408 AQKFSLYGNlSVEQNLRFFSG------VYGLRGRAQ-NEKIARMSDafGLKSIARHAADELPLGYKQRLALACSLMHEPD 480
Cdd:PRK11174 429 GQNPQLPHG-TLRDNVLLGNPdasdeqLQQALENAWvSEFLPLLPQ--GLDTPIGDQAAGLSVGQAQRLALARALLQPCQ 505
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 488984955 481 ILFLDEPTSGVDPLTRREFWLHINSMVDKGVTVMVtTHFMDEAEYCDRIGLVYHGKLIASGTPDALKAQ 549
Cdd:PRK11174 506 LLLLDEPTASLDAHSEQLVMQALNAASRRQTTLMV-THQLEDLAQWDQIWVMQDGQIVQQGDYAELSQA 573
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
329-518 |
8.55e-14 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 70.65 E-value: 8.55e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 329 VIEAQSLTKKFGDFAATDHVDFQVKRGEIFGLLGPNGAGKSTTFKMMCGLLVPTSGKALVLGMdlKVSSGKARQHLGYMA 408
Cdd:PRK13543 11 LLAAHALAFSRNEEPVFGPLDFHVDAGEALLVQGDNGAGKTTLLRVLAGLLHVESGQIQIDGK--TATRGDRSRFMAYLG 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 409 QKFSLYGNLSVEQNLRFFSGVYGLRGRaqnekiaRM-SDAFGLKSIARHA---ADELPLGYKQRLALACSLMHEPDILFL 484
Cdd:PRK13543 89 HLPGLKADLSTLENLHFLCGLHGRRAK-------QMpGSALAIVGLAGYEdtlVRQLSAGQKKRLALARLWLSPAPLWLL 161
|
170 180 190
....*....|....*....|....*....|....*...
gi 488984955 485 DEPTSGVDP----LTRREFWLHINSmvdkGVTVMVTTH 518
Cdd:PRK13543 162 DEPYANLDLegitLVNRMISAHLRG----GGAALVTTH 195
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
3-256 |
9.51e-14 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 71.69 E-value: 9.51e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 3 ETVIALNGLSRRFPGMDRpAVAPLTCTIRAGYVTGLVGPDGAGKTTLMRMLAGLLKPDEGRASVIGfdplkddSALHAVL 82
Cdd:PRK13647 2 DNIIEVEDLHFRYKDGTK-ALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMG-------REVNAEN 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 83 GY-MPQKFGL-YED-------LTVME-------NLTLYAD-LRSVTGEARKKIfdRLLEFTSLGPFterlagKLSGGMKQ 145
Cdd:PRK13647 74 EKwVRSKVGLvFQDpddqvfsSTVWDdvafgpvNMGLDKDeVERRVEEALKAV--RMWDFRDKPPY------HLSYGQKK 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 146 KLGLACTLVGDPKVLLLDEPGVGVDPISRRELWQMVHELAGDGMLILWSTSYLDEAEQCRD-VLLMNEGKLLYQGEPTAL 224
Cdd:PRK13647 146 RVAIAGVLAMDPDVIVLDEPMAYLDPRGQETLMEILDRLHNQGKTVIVATHDVDLAAEWADqVIVLKEGRVLAEGDKSLL 225
|
250 260 270
....*....|....*....|....*....|...
gi 488984955 225 TqtmagrsflvsspqenNRRLLQRA-LKLPQVS 256
Cdd:PRK13647 226 T----------------DEDIVEQAgLRLPLVA 242
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
6-171 |
1.01e-13 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 71.27 E-value: 1.01e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 6 IALNGLSRRF-PGM--DRPAVAPLTCTIRAG-YVTgLVGPDGAGKTTLMRMLAGLLKPDEG----------------RAS 65
Cdd:COG1101 2 LELKNLSKTFnPGTvnEKRALDGLNLTIEEGdFVT-VIGSNGAGKSTLLNAIAGSLPPDSGsilidgkdvtklpeykRAK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 66 VIG--F-DPLKddsalhavlgympqkfGLYEDLTVMENLTLyADLR--------SVTGeARKKIFDRLLEFTSLGpFTER 134
Cdd:COG1101 81 YIGrvFqDPMM----------------GTAPSMTIEENLAL-AYRRgkrrglrrGLTK-KRRELFRELLATLGLG-LENR 141
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 488984955 135 L---AGKLSGGMKQKLGLA-CTLVgDPKVLLLDEPGVGVDP 171
Cdd:COG1101 142 LdtkVGLLSGGQRQALSLLmATLT-KPKLLLLDEHTAALDP 181
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
31-192 |
1.18e-13 |
|
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI), is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI s are not transport proteins and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLIs have an N-terminal Fe-S domain and two nucleotide binding domains which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213203 [Multi-domain] Cd Length: 255 Bit Score: 71.24 E-value: 1.18e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 31 RAGYVTGLVGPDGAGKTTLMRMLAGLLKPDEGRASvigfDPLKDDSALHAVLGYMPQKFglyedLTVMENLTL------- 103
Cdd:cd03236 24 REGQVLGLVGPNGIGKSTALKILAGKLKPNLGKFD----DPPDWDEILDEFRGSELQNY-----FTKLLEGDVkvivkpq 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 104 YADL--RSVTGEARKKI--------FDRLLEFTSLGPFTERLAGKLSGGMKQKLGLACTLVGDPKVLLLDEPGVGVDPIS 173
Cdd:cd03236 95 YVDLipKAVKGKVGELLkkkdergkLDELVDQLELRHVLDRNIDQLSGGELQRVAIAAALARDADFYFFDEPSSYLDIKQ 174
|
170
....*....|....*....
gi 488984955 174 RRELWQMVHELAGDGMLIL 192
Cdd:cd03236 175 RLNAARLIRELAEDDNYVL 193
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
8-240 |
1.64e-13 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 73.22 E-value: 1.64e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 8 LNGLSRRFPGMDRPAVA--PLTCTIRAGYVTGLVGPDGAGKTTLMRMLAGLLKPDEGRASVIGFDPLK-DDSALHAV--- 81
Cdd:PRK10535 7 LKDIRRSYPSGEEQVEVlkGISLDIYAGEMVAIVGASGSGKSTLMNILGCLDKPTSGTYRVAGQDVATlDADALAQLrre 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 82 -LGYMPQKFGLYEDLTVMENLTLYADLRSVTGEARKKIFDRLLEFTSLGPFTERLAGKLSGGMKQKLGLACTLVGDPKVL 160
Cdd:PRK10535 87 hFGFIFQRYHLLSHLTAAQNVEVPAVYAGLERKQRLLRAQELLQRLGLEDRVEYQPSQLSGGQQQRVSIARALMNGGQVI 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 161 LLDEPGVGVDPISRRELWQMVHELAGDGMLILWSTSYLDEAEQCRDVLLMNEGKLLY----------QGEPTALTQTMAG 230
Cdd:PRK10535 167 LADEPTGALDSHSGEEVMAILHQLRDRGHTVIIVTHDPQVAAQAERVIEIRDGEIVRnppaqekvnvAGGTEPVVNTASG 246
|
250
....*....|
gi 488984955 231 RSFLVSSPQE 240
Cdd:PRK10535 247 WRQFVSGFRE 256
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
330-541 |
1.81e-13 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 70.64 E-value: 1.81e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 330 IEAQSLTKKFGDFAATDHVDFQVKRGEIFGLLGPNGAGKSTTFKMMCGLL-----VPTSGKALVLGMDL---KVSSGKAR 401
Cdd:PRK14267 5 IETVNLRVYYGSNHVIKGVDLKIPQNGVFALMGPSGCGKSTLLRTFNRLLelneeARVEGEVRLFGRNIyspDVDPIEVR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 402 QHLGYMAQKFSLYGNLSVEQNLRFFSGVYGL-RGRAQNEKIARmsdaFGLKSIA---------RHAADELPLGYKQRLAL 471
Cdd:PRK14267 85 REVGMVFQYPNPFPHLTIYDNVAIGVKLNGLvKSKKELDERVE----WALKKAAlwdevkdrlNDYPSNLSGGQRQRLVI 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 472 ACSLMHEPDILFLDEPTSGVDPLTRREFWLHINSMVDKGVTVMVTTHFMDEAEYCDRIGLVYHGKLIASG 541
Cdd:PRK14267 161 ARALAMKPKILLMDEPTANIDPVGTAKIEELLFELKKEYTIVLVTHSPAQAARVSDYVAFLYLGKLIEVG 230
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
344-549 |
1.90e-13 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 72.94 E-value: 1.90e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 344 ATDHVDFQVKRGEIFGLLGPNGAGKSTTFKMMCGLLVPTSGKALVLGMDLKVSSGKA-RQHLGYMAQKFSLYgNLSVEQN 422
Cdd:PRK11160 355 VLKGLSLQIKAGEKVALLGRTGCGKSTLLQLLTRAWDPQQGEILLNGQPIADYSEAAlRQAISVVSQRVHLF-SATLRDN 433
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 423 LRFFSGvyglrgRAQNEKIARMSDAFGLksiARHAADELPL-------------GYKQRLALACSLMHEPDILFLDEPTS 489
Cdd:PRK11160 434 LLLAAP------NASDEALIEVLQQVGL---EKLLEDDKGLnawlgeggrqlsgGEQRRLGIARALLHDAPLLLLDEPTE 504
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 488984955 490 GVDPLTRRE-FWLHINSMVDKgvTVMVTTHFMDEAEYCDRIGLVYHGKLIASGTPDALKAQ 549
Cdd:PRK11160 505 GLDAETERQiLELLAEHAQNK--TVLMITHRLTGLEQFDRICVMDNGQIIEQGTHQELLAQ 563
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
6-165 |
2.45e-13 |
|
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: 67.47 E-value: 2.45e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 6 IALNGLSRRFPgmDRPAVAPLTCTIRAGYVTGLVGPDGAGKTTLMRMLAGLLKPDEGRASVIGfdplkddsalHAVLGYM 85
Cdd:cd03221 1 IELENLSKTYG--GKLLLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIVTWGS----------TVKIGYF 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 86 PQkfglyedltvmenltlyadlrsvtgearkkifdrlleftslgpfterlagkLSGGMKQKLGLACTLVGDPKVLLLDEP 165
Cdd:cd03221 69 EQ---------------------------------------------------LSGGEKMRLALAKLLLENPNLLLLDEP 97
|
|
| tagH |
PRK13545 |
teichoic acids export protein ATP-binding subunit; Provisional |
22-164 |
4.26e-13 |
|
teichoic acids export protein ATP-binding subunit; Provisional
Pssm-ID: 184130 [Multi-domain] Cd Length: 549 Bit Score: 71.85 E-value: 4.26e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 22 AVAPLTCTIRAGYVTGLVGPDGAGKTTLMRMLAGLLKPDEGRASVigfdplKDDSALHAVlgympqKFGLYEDLTVMENL 101
Cdd:PRK13545 39 ALNNISFEVPEGEIVGIIGLNGSGKSTLSNLIAGVTMPNKGTVDI------KGSAALIAI------SSGLNGQLTGIENI 106
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 488984955 102 TLYADLRSVTGEARKKIFDRLLEFTSLGPFTERLAGKLSGGMKQKLGLACTLVGDPKVLLLDE 164
Cdd:PRK13545 107 ELKGLMMGLTKEKIKEIIPEIIEFADIGKFIYQPVKTYSSGMKSRLGFAISVHINPDILVIDE 169
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
3-224 |
4.37e-13 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 69.76 E-value: 4.37e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 3 ETVIALNGLSRRF-PGMDRPAVAPLTCTIRAGYVTGLVGPDGAGKTTLMRMLAGLLKPDEGRASVIGfDPLKDDSALHav 81
Cdd:PRK13650 2 SNIIEVKNLTFKYkEDQEKYTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIIDG-DLLTEENVWD-- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 82 lgyMPQKFGL--------YEDLTVMENLTLYADLRSVTGEARKKIFDRLLEFTSLGPFTERLAGKLSGGMKQKLGLACTL 153
Cdd:PRK13650 79 ---IRHKIGMvfqnpdnqFVGATVEDDVAFGLENKGIPHEEMKERVNEALELVGMQDFKEREPARLSGGQKQRVAIAGAV 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 488984955 154 VGDPKVLLLDEPGVGVDPISRRELWQMVHELAGD-GMLILWSTSYLDEAEQCRDVLLMNEGKLLYQGEPTAL 224
Cdd:PRK13650 156 AMRPKIIILDEATSMLDPEGRLELIKTIKGIRDDyQMTVISITHDLDEVALSDRVLVMKNGQVESTSTPREL 227
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
5-165 |
4.50e-13 |
|
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: 70.47 E-value: 4.50e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 5 VIALNGLSRRFPGMDRP--AVAPLTCTIRAGYVTGLVGPDGAGKTTLMRMLAGLLKP---DEGRASVIGFDPLK-DDSAL 78
Cdd:COG0444 1 LLEVRNLKVYFPTRRGVvkAVDGVSFDVRRGETLGLVGESGSGKSTLARAILGLLPPpgiTSGEILFDGEDLLKlSEKEL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 79 HAVLG----YMPQkfglyeD--------LTV----MENLTLYadlRSVTGEARKKIFDRLLEFTSLgPFTERLAGK---- 138
Cdd:COG0444 81 RKIRGreiqMIFQ------DpmtslnpvMTVgdqiAEPLRIH---GGLSKAEARERAIELLERVGL-PDPERRLDRyphe 150
|
170 180
....*....|....*....|....*..
gi 488984955 139 LSGGMKQKLGLACTLVGDPKVLLLDEP 165
Cdd:COG0444 151 LSGGMRQRVMIARALALEPKLLIADEP 177
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
38-221 |
4.80e-13 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 70.26 E-value: 4.80e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 38 LVGPDGAGKTTLMRMLAGLLKPDEGRASVIGFDPLKDDSALHAVLGYMPQK-------------------FGLYEDlTVM 98
Cdd:PRK13631 57 IIGNSGSGKSTLVTHFNGLIKSKYGTIQVGDIYIGDKKNNHELITNPYSKKiknfkelrrrvsmvfqfpeYQLFKD-TIE 135
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 99 ENLTLYADLRSVTGEARKKIFDRLLEFTSLG-PFTERLAGKLSGGMKQKLGLACTLVGDPKVLLLDEPGVGVDPISRREL 177
Cdd:PRK13631 136 KDIMFGPVALGVKKSEAKKLAKFYLNKMGLDdSYLERSPFGLSGGQKRRVAIAGILAIQPEILIFDEPTAGLDPKGEHEM 215
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 488984955 178 WQMVHELAGDGMLILWSTSYLDEAEQCRD-VLLMNEGKLLYQGEP 221
Cdd:PRK13631 216 MQLILDAKANNKTVFVITHTMEHVLEVADeVIVMDKGKILKTGTP 260
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
1-222 |
5.66e-13 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 69.39 E-value: 5.66e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 1 MSETVIALNGLSRRFPGMDRPAVAPLTCTIRAGYVTGLVGPDGAGKTTLMRMLAGLLKPDEGRA----SVIGFDPLKDds 76
Cdd:PRK13648 3 DKNSIIVFKNVSFQYQSDASFTLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIfynnQAITDDNFEK-- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 77 aLHAVLGYMPQK---------------FGLyedltvmENltlyadlRSVTGEARKKIFDRLLEFTSLGPFTERLAGKLSG 141
Cdd:PRK13648 81 -LRKHIGIVFQNpdnqfvgsivkydvaFGL-------EN-------HAVPYDEMHRRVSEALKQVDMLERADYEPNALSG 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 142 GMKQKLGLACTLVGDPKVLLLDEPGVGVDPISRRELWQMVHELAGDGMLILWS-TSYLDEAEQCRDVLLMNEGKLLYQGE 220
Cdd:PRK13648 146 GQKQRVAIAGVLALNPSVIILDEATSMLDPDARQNLLDLVRKVKSEHNITIISiTHDLSEAMEADHVIVMNKGTVYKEGT 225
|
..
gi 488984955 221 PT 222
Cdd:PRK13648 226 PT 227
|
|
| PRK13546 |
PRK13546 |
teichoic acids export ABC transporter ATP-binding subunit TagH; |
22-220 |
5.83e-13 |
|
teichoic acids export ABC transporter ATP-binding subunit TagH;
Pssm-ID: 184131 [Multi-domain] Cd Length: 264 Bit Score: 69.07 E-value: 5.83e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 22 AVAPLTCTIRAGYVTGLVGPDGAGKTTLMRMLAGLLKPDEGR------ASVIgfdplkddsALHAvlgympqkfGLYEDL 95
Cdd:PRK13546 39 ALDDISLKAYEGDVIGLVGINGSGKSTLSNIIGGSLSPTVGKvdrngeVSVI---------AISA---------GLSGQL 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 96 TVMENLTLYADLRSVTGEARKKIFDRLLEFTSLGPFTERLAGKLSGGMKQKLGLACTLVGDPKVLLLDEP-GVGVDPISR 174
Cdd:PRK13546 101 TGIENIEFKMLCMGFKRKEIKAMTPKIIEFSELGEFIYQPVKKYSSGMRAKLGFSINITVNPDILVIDEAlSVGDQTFAQ 180
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 488984955 175 RELWQMvHELAGDGMLILWSTSYLDEAEQ-CRDVLLMNEGKLLYQGE 220
Cdd:PRK13546 181 KCLDKI-YEFKEQNKTIFFVSHNLGQVRQfCTKIAWIEGGKLKDYGE 226
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
38-165 |
5.87e-13 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 68.65 E-value: 5.87e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 38 LVGPDGAGKTTLMRMLAGLLKPDEGRASVIGFDPLKDDSALHAVL-----GYMPQKFGLYEDLTVMENLTLYADLRSVTG 112
Cdd:PRK10584 41 LIGESGSGKSTLLAILAGLDDGSSGEVSLVGQPLHQMDEEARAKLrakhvGFVFQSFMLIPTLNALENVELPALLRGESS 120
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 488984955 113 EARKKIFDRLLEFTSLGPFTERLAGKLSGGMKQKLGLACTLVGDPKVLLLDEP 165
Cdd:PRK10584 121 RQSRNGAKALLEQLGLGKRLDHLPAQLSGGEQQRVALARAFNGRPDVLFADEP 173
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
346-526 |
6.87e-13 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 67.67 E-value: 6.87e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 346 DHVDFQVKRGEIFGLLGPNGAGKSTTFKMMCGLLVPTSGKALVLGMDLKVSSGKARQHLGYMAQKFSLYGNLSVEQNLrf 425
Cdd:PRK13540 18 QQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEILFERQSIKKDLCTYQKQLCFVGHRSGINPYLTLRENC-- 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 426 fsgVYGLRGRAQNEKIARMSDAFGLKSIARHAADELPLGYKQRLALACSLMHEPDILFLDEPTSGVDPLTRREFWLHINS 505
Cdd:PRK13540 96 ---LYDIHFSPGAVGITELCRLFSLEHLIDYPCGLLSSGQKRQVALLRLWMSKAKLWLLDEPLVALDELSLLTIITKIQE 172
|
170 180
....*....|....*....|....*..
gi 488984955 506 MVDKGVTVMVTTH------FMDEAEYC 526
Cdd:PRK13540 173 HRAKGGAVLLTSHqdlplnKADYEEYH 199
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
38-385 |
9.59e-13 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 70.75 E-value: 9.59e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 38 LVGPDGAGKTTLMRMLAGLLKPDEGR--------ASVIGFDPLKDDSAlhAVLGYMPQkfGLYEdltVMENLTLYADL-R 108
Cdd:PRK11147 34 LVGRNGAGKSTLMKILNGEVLLDDGRiiyeqdliVARLQQDPPRNVEG--TVYDFVAE--GIEE---QAEYLKRYHDIsH 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 109 SVTGEARKKIFDRL------LEFTSLGPFTERLA--------------GKLSGGMKQKLGLACTLVGDPKVLLLDEPgvg 168
Cdd:PRK11147 107 LVETDPSEKNLNELaklqeqLDHHNLWQLENRINevlaqlgldpdaalSSLSGGWLRKAALGRALVSNPDVLLLDEP--- 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 169 vdpisrrelwqmvhelagdgmlilwsTSYLD-EA-EQCRDVLLMNEGKLLYQGEPTALTQTMA------GRSFLVSSP-- 238
Cdd:PRK11147 184 --------------------------TNHLDiETiEWLEGFLKTFQGSIIFISHDRSFIRNMAtrivdlDRGKLVSYPgn 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 239 -------QENNRRL--LQRAL---KLPQVSDGVIQG-KS--------VRLIlkKDARIE-----EVQQHGDMpplQVADT 292
Cdd:PRK11147 238 ydqylleKEEALRVeeLQNAEfdrKLAQEEVWIRQGiKArrtrnegrVRAL--KALRRErserrEVMGTAKM---QVEEA 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 293 APRfedafidllggagtaesplGAIihrvdgskeetVIEAQSLTKKFGDFAATDHVDFQVKRGEIFGLLGPNGAGKSTTF 372
Cdd:PRK11147 313 SRS-------------------GKI-----------VFEMENVNYQIDGKQLVKDFSAQVQRGDKIALIGPNGCGKTTLL 362
|
410
....*....|...
gi 488984955 373 KMMCGLLVPTSGK 385
Cdd:PRK11147 363 KLMLGQLQADSGR 375
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
327-538 |
1.39e-12 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 67.88 E-value: 1.39e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 327 ETVIEAQSLTKKFGDFAATDHVDFQVKRGEIFGLLGPNGAGKSTTFKMM--CGLLVP---TSGKALVLGMDL---KVSSG 398
Cdd:PRK14239 3 EPILQVSDLSVYYNKKKALNSVSLDFYPNEITALIGPSGSGKSTLLRSInrMNDLNPevtITGSIVYNGHNIyspRTDTV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 399 KARQHLGYMAQK-----FSLYGNLsveqnlrffsgVYGLRGRAQNEKiARMSDAFG-----------LKSIARHAADELP 462
Cdd:PRK14239 83 DLRKEIGMVFQQpnpfpMSIYENV-----------VYGLRLKGIKDK-QVLDEAVEkslkgasiwdeVKDRLHDSALGLS 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 488984955 463 LGYKQRLALACSLMHEPDILFLDEPTSGVDPLTRREFWLHINSMVDKgVTVMVTTHFMDEA-EYCDRIGLVYHGKLI 538
Cdd:PRK14239 151 GGQQQRVCIARVLATSPKIILLDEPTSALDPISAGKIEETLLGLKDD-YTMLLVTRSMQQAsRISDRTGFFLDGDLI 226
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
27-492 |
1.57e-12 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 70.20 E-value: 1.57e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 27 TCTIRAGYVTGLVGPDGAGKTTLMRMLAGLLKPDEGRASVIGF---------DPLKDDSALHAVLGYMPQKFGLYEDLTV 97
Cdd:PRK10636 21 TATINPGQKVGLVGKNGCGKSTLLALLKNEISADGGSYTFPGNwqlawvnqeTPALPQPALEYVIDGDREYRQLEAQLHD 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 98 MEN-------LTLYADLRSV---TGEARKKIFDRLLEFTSlgPFTERLAGKLSGGMKQKLGLACTLVGDPKVLLLDEPG- 166
Cdd:PRK10636 101 ANErndghaiATIHGKLDAIdawTIRSRAASLLHGLGFSN--EQLERPVSDFSGGWRMRLNLAQALICRSDLLLLDEPTn 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 167 -VGVDPISRRELWQMVHElagdGMLILWSTSyldeaeqcRDVLLMNEGKLLYQGEPTALTQTMAGRSFLVsspqennrrl 245
Cdd:PRK10636 179 hLDLDAVIWLEKWLKSYQ----GTLILISHD--------RDFLDPIVDKIIHIEQQSLFEYTGNYSSFEV---------- 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 246 lQRALKLPQvsdgviqgksvrlilkKDARIEEVQQHgdMPPLQvadtapRFEDAFIDLLGGAGTAES--------PLGAI 317
Cdd:PRK10636 237 -QRATRLAQ----------------QQAMYESQQER--VAHLQ------SYIDRFRAKATKAKQAQSrikmlermELIAP 291
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 318 IH---------RVDGSKEETVIEAQSLTKKFGDFAATDHVDFQVKRGEIFGLLGPNGAGKSTTFKMMCGLLVPTSGK-AL 387
Cdd:PRK10636 292 AHvdnpfhfsfRAPESLPNPLLKMEKVSAGYGDRIILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELAPVSGEiGL 371
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 388 VLGMDLkvssGKARQH-LGYMAQKFSLYGNLS------VEQNLRFFSGVYGLRGRAQNEKIARMSDafglksiarhaade 460
Cdd:PRK10636 372 AKGIKL----GYFAQHqLEFLRADESPLQHLArlapqeLEQKLRDYLGGFGFQGDKVTEETRRFSG-------------- 433
|
490 500 510
....*....|....*....|....*....|..
gi 488984955 461 lplGYKQRLALACSLMHEPDILFLDEPTSGVD 492
Cdd:PRK10636 434 ---GEKARLVLALIVWQRPNLLLLDEPTNHLD 462
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
348-537 |
1.69e-12 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 70.00 E-value: 1.69e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 348 VDFQVKRGEIFGLLGPNGAGKSTTFKMMCGLLVPTSGKALVLGMDLKVSSGKARQHLgymaqkFSlygnlSVEQNLRFFS 427
Cdd:PRK10522 342 INLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKPVTAEQPEDYRKL------FS-----AVFTDFHLFD 410
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 428 GVYGLRGRAQNEKIAR-------MSDAFGLKSiARHAADELPLGYKQRLALACSLMHEPDILFLDEPTSGVDPLTRREFW 500
Cdd:PRK10522 411 QLLGPEGKPANPALVEkwlerlkMAHKLELED-GRISNLKLSKGQKKRLALLLALAEERDILLLDEWAADQDPHFRREFY 489
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 488984955 501 LH-INSMVDKGVTVMVTTHfmDEA--EYCDRIGLVYHGKL 537
Cdd:PRK10522 490 QVlLPLLQEMGKTIFAISH--DDHyfIHADRLLEMRNGQL 527
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
326-523 |
2.55e-12 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 67.50 E-value: 2.55e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 326 EETVIEAQSLTKKFGDFAATDHVDFQVKRGEIFGLLGPNGAGKSTTFKMMCGL--LVPT---SGKALVLGMDL---KVSS 397
Cdd:PRK14243 7 TETVLRTENLNVYYGSFLAVKNVWLDIPKNQITAFIGPSGCGKSTILRCFNRLndLIPGfrvEGKVTFHGKNLyapDVDP 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 398 GKARQHLGYMAQKFSLYGNlSVEQNLRFFSGVYGLRGRAQN--EKIARMSDAFG-LKSIARHAADELPLGYKQRLALACS 474
Cdd:PRK14243 87 VEVRRRIGMVFQKPNPFPK-SIYDNIAYGARINGYKGDMDElvERSLRQAALWDeVKDKLKQSGLSLSGGQQQRLCIARA 165
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 488984955 475 LMHEPDILFLDEPTSGVDPLTRREFWLHINSMVDKgVTVMVTTHFMDEA 523
Cdd:PRK14243 166 IAVQPEVILMDEPCSALDPISTLRIEELMHELKEQ-YTIIIVTHNMQQA 213
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
335-540 |
2.85e-12 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 68.99 E-value: 2.85e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 335 LTKKFGDFAATDHVDFQVKRGEIFGLLGPNGAGKSTTFKMMCGLLVPTSGKALVLGMDLKVSSGK-ARQHLGYMA-QKFS 412
Cdd:PRK10982 4 ISKSFPGVKALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEIDFKSSKeALENGISMVhQELN 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 413 LYGNLSVEQNLrfFSGVYGLRGRAQNEK-----IARMSDAFGLKSIARHAADELPLGYKQRLALACSLMHEPDILFLDEP 487
Cdd:PRK10982 84 LVLQRSVMDNM--WLGRYPTKGMFVDQDkmyrdTKAIFDELDIDIDPRAKVATLSVSQMQMIEIAKAFSYNAKIVIMDEP 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 488984955 488 TSGvdpLTRRE---FWLHINSMVDKGVTVMVTTHFMDEA-EYCDRIGLVYHGKLIAS 540
Cdd:PRK10982 162 TSS---LTEKEvnhLFTIIRKLKERGCGIVYISHKMEEIfQLCDEITILRDGQWIAT 215
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
348-529 |
3.25e-12 |
|
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: 65.95 E-value: 3.25e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 348 VDFQVKRGEIFGLLGPNGAGKSTTFKMMCGLLVPTSGKALVLGmdlkvssgkarqHLGYMAQKFSLYgNLSVEQNLRFfs 427
Cdd:cd03250 24 INLEVPKGELVAIVGPVGSGKSSLLSALLGELEKLSGSVSVPG------------SIAYVSQEPWIQ-NGTIRENILF-- 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 428 gvyglrGRAQNEK--------------IARMSDA----FGLKSIArhaadeLPLGYKQRLALACSLMHEPDILFLDEPTS 489
Cdd:cd03250 89 ------GKPFDEEryekvikacalepdLEILPDGdlteIGEKGIN------LSGGQKQRISLARAVYSDADIYLLDDPLS 156
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 488984955 490 GVDPLTRREFWLH-INSMVDKGVTVMVTTHFMDEAEYCDRI 529
Cdd:cd03250 157 AVDAHVGRHIFENcILGLLLNNKTRILVTHQLQLLPHADQI 197
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
3-188 |
3.35e-12 |
|
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: 66.30 E-value: 3.35e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 3 ETVIALNGLSRRFP-----GMDRPAVAPLTCTIRAGYVTGLVGPDGAGKTTLMRMLAGLLKPDEGRASVI-GFDPLK--- 73
Cdd:COG4778 2 TTLLEVENLSKTFTlhlqgGKRLPVLDGVSFSVAAGECVALTGPSGAGKSTLLKCIYGNYLPDSGSILVRhDGGWVDlaq 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 74 -DDSALHAV----LGY-------MPQKFGLyeDLtVMENLtlyADLRSVTGEAR---KKIFDRL---LEFTSLGPFTerl 135
Cdd:COG4778 82 aSPREILALrrrtIGYvsqflrvIPRVSAL--DV-VAEPL---LERGVDREEARaraRELLARLnlpERLWDLPPAT--- 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 488984955 136 agkLSGGMKQKLGLACTLVGDPKVLLLDEPGVGVDPISRRELWQMVHELAGDG 188
Cdd:COG4778 153 ---FSGGEQQRVNIARGFIADPPLLLLDEPTASLDAANRAVVVELIEEAKARG 202
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
6-226 |
3.74e-12 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 69.08 E-value: 3.74e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 6 IALNGLSRRFPGMDRPAVAPLTCTIRAGYVTGLVGPDGAGKTTLMRMLAGLLKPDEGRASVIGfDPLKD--DSALHAVLG 83
Cdd:PRK11160 339 LTLNNVSFTYPDQPQPVLKGLSLQIKAGEKVALLGRTGCGKSTLLQLLTRAWDPQQGEILLNG-QPIADysEAALRQAIS 417
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 84 YMPQKFGLYEDlTVMENLTLYADlrsvtgEARKKIFDRLLEFTSLGPFTERLAG----------KLSGGMKQKLGLACTL 153
Cdd:PRK11160 418 VVSQRVHLFSA-TLRDNLLLAAP------NASDEALIEVLQQVGLEKLLEDDKGlnawlgeggrQLSGGEQRRLGIARAL 490
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 488984955 154 VGDPKVLLLDEPGVGVDPISRRELWQMVHELAGDGMLILwSTSYLDEAEQCRDVLLMNEGKLLYQGEPTALTQ 226
Cdd:PRK11160 491 LHDAPLLLLDEPTEGLDAETERQILELLAEHAQNKTVLM-ITHRLTGLEQFDRICVMDNGQIIEQGTHQELLA 562
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
330-546 |
4.76e-12 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 66.66 E-value: 4.76e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 330 IEAQSLTKKFGDFAATDHVDFQVKRGEIFGLLGPNGAGKSTTFKMMCGLLVPTSG-----KALVLGMDLKVSSG--KARQ 402
Cdd:PRK14271 22 MAAVNLTLGFAGKTVLDQVSMGFPARAVTSLMGPTGSGKTTFLRTLNRMNDKVSGyrysgDVLLGGRSIFNYRDvlEFRR 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 403 HLGYMAQKFSLYgNLSVEQNLrfFSGVYG--------LRGRAQnekiARMSDAfGLKSIARHAADELPL----GYKQRLA 470
Cdd:PRK14271 102 RVGMLFQRPNPF-PMSIMDNV--LAGVRAhklvprkeFRGVAQ----ARLTEV-GLWDAVKDRLSDSPFrlsgGQQQLLC 173
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 488984955 471 LACSLMHEPDILFLDEPTSGVDPLTRREFWLHINSMVDKGVTVMVTTHFMDEAEYCDRIGLVYHGKLIASGTPDAL 546
Cdd:PRK14271 174 LARTLAVNPEVLLLDEPTSALDPTTTEKIEEFIRSLADRLTVIIVTHNLAQAARISDRAALFFDGRLVEEGPTEQL 249
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
30-219 |
4.80e-12 |
|
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding cassette transporters; The pleiotropic drug resistance (PDR) is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. This PDR subfamily represents domain I of its (ABC-IM)2 organization. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds including sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213199 [Multi-domain] Cd Length: 192 Bit Score: 64.96 E-value: 4.80e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 30 IRAGYVTGLVGPDGAGKTTLMRMLAGllkpdEGRASVIGFDPLKD----DSALHAVLGYMPQKFGLYEDLTVMENLTLYA 105
Cdd:cd03232 30 VKPGTLTALMGESGAGKTTLLDVLAG-----RKTAGVITGEILINgrplDKNFQRSTGYVEQQDVHSPNLTVREALRFSA 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 106 DLRSVTGEARKkifdrlleftslgpfterlagklsggmkqKLGLACTLVGDPKVLLLDEPGVGVDPISRRELWQMVHELA 185
Cdd:cd03232 105 LLRGLSVEQRK-----------------------------RLTIGVELAAKPSILFLDEPTSGLDSQAAYNIVRFLKKLA 155
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 488984955 186 GDGMLILWSTS--------YLDEAeqcrdVLLMNEGKLLYQG 219
Cdd:cd03232 156 DSGQAILCTIHqpsasifeKFDRL-----LLLKRGGKTVYFG 192
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
19-164 |
5.82e-12 |
|
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 (also known as ABCB6) is a mitochondrial ATP-binding cassette protein involved in iron homeostasis and one of four ABC transporters expressed in the mitochondrial inner membrane, the other three being MDL1(ABC7), MDL2, and ATM1. In fact, the yeast MDL1 (multidrug resistance-like protein 1) and MDL2 (multidrug resistance-like protein 2) transporters are also included in this CD. MDL1 is an ATP-dependent permease that acts as a high-copy suppressor of ATM1 and is thought to have a role in resistance to oxidative stress. Interestingly, subfamily B is more closely related to the carboxyl-terminal component of subfamily C than the two halves of ABCC molecules are with one another.
Pssm-ID: 213216 [Multi-domain] Cd Length: 238 Bit Score: 65.64 E-value: 5.82e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 19 DRPAVAPLTCTIRAGYVTGLVGPDGAGKTTLMRMLAGLLKPDEGRASVIGFDpLKD--DSALHAVLGYMPQKFGLYeDLT 96
Cdd:cd03249 15 DVPILKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEILLDGVD-IRDlnLRWLRSQIGLVSQEPVLF-DGT 92
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 488984955 97 VMENLTLYADLRSVTG--EARKK--IFDRLLEF-----TSLGPFterlAGKLSGGMKQKLGLACTLVGDPKVLLLDE 164
Cdd:cd03249 93 IAENIRYGKPDATDEEveEAAKKanIHDFIMSLpdgydTLVGER----GSQLSGGQKQRIAIARALLRNPKILLLDE 165
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
1-192 |
6.14e-12 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 65.95 E-value: 6.14e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 1 MSETVIALNGLSRRFPgmDRPAVAPLTCTIRAGYVTGLVGPDGAGKTTLMRML--AGLLKPDEGRASVIGFD------PL 72
Cdd:PRK14239 1 MTEPILQVSDLSVYYN--KKKALNSVSLDFYPNEITALIGPSGSGKSTLLRSInrMNDLNPEVTITGSIVYNghniysPR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 73 KDDSALHAVLGYM---PQKFglyeDLTVMENLtLYAdLRsVTGEARKKIFDRLLEFTSLGP-----FTERL---AGKLSG 141
Cdd:PRK14239 79 TDTVDLRKEIGMVfqqPNPF----PMSIYENV-VYG-LR-LKGIKDKQVLDEAVEKSLKGAsiwdeVKDRLhdsALGLSG 151
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 488984955 142 GMKQKLGLACTLVGDPKVLLLDEPGVGVDPISRRELWQMVHELAGDGMLIL 192
Cdd:PRK14239 152 GQQQRVCIARVLATSPKIILLDEPTSALDPISAGKIEETLLGLKDDYTMLL 202
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
8-537 |
6.51e-12 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 67.83 E-value: 6.51e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 8 LNGLSRRFPGMDrpAVAPLTCTIRAGYVTGLVGPDGAGKTTLMRMLAGLLKPDEGRASVIG----FDPLKDdsALHAVLG 83
Cdd:PRK10982 1 MSNISKSFPGVK--ALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGkeidFKSSKE--ALENGIS 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 84 YMPQKFGLYEDLTVMENLTL--------YADLRSVTGEArKKIFDRLleFTSLGPfTERLAgKLSGGMKQKLGLACTLVG 155
Cdd:PRK10982 77 MVHQELNLVLQRSVMDNMWLgryptkgmFVDQDKMYRDT-KAIFDEL--DIDIDP-RAKVA-TLSVSQMQMIEIAKAFSY 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 156 DPKVLLLDEPGVGVDPISRRELWQMVHELAGDGMLILWSTSYLDEAEQ-CRDVLLMNEGKLLYQGEPTALT-----QTMA 229
Cdd:PRK10982 152 NAKIVIMDEPTSSLTEKEVNHLFTIIRKLKERGCGIVYISHKMEEIFQlCDEITILRDGQWIATQPLAGLTmdkiiAMMV 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 230 GRSFLVSSPQENNRrllqralklpqvsdgviqgksvrlilkkdarieevqqhgdmpplqvadtaprfedafidllggagt 309
Cdd:PRK10982 232 GRSLTQRFPDKENK------------------------------------------------------------------ 245
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 310 aesplgaiihrvdgsKEETVIEAQSLTKKfgDFAATDHVDFQVKRGEIFGLLGPNGAGKSTTFKMMCGLLVPTSGKALVL 389
Cdd:PRK10982 246 ---------------PGEVILEVRNLTSL--RQPSIRDVSFDLHKGEILGIAGLVGAKRTDIVETLFGIREKSAGTITLH 308
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 390 GMDLKVSSGKARQHLGYM-----AQKFSLYGNLSVE-----QNLRFFSGVYGLrgrAQNEKIAR----MSDAFGLKSIAR 455
Cdd:PRK10982 309 GKKINNHNANEAINHGFAlvteeRRSTGIYAYLDIGfnsliSNIRNYKNKVGL---LDNSRMKSdtqwVIDSMRVKTPGH 385
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 456 HAA-DELPLGYKQRLALACSLMHEPDILFLDEPTSGVDPLTRREFWLHINSMV--DKGVtVMVTTHFMDEAEYCDRIGLV 532
Cdd:PRK10982 386 RTQiGSLSGGNQQKVIIGRWLLTQPEILMLDEPTRGIDVGAKFEIYQLIAELAkkDKGI-IIISSEMPELLGITDRILVM 464
|
....*
gi 488984955 533 YHGKL 537
Cdd:PRK10982 465 SNGLV 469
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
1-221 |
8.53e-12 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 65.78 E-value: 8.53e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 1 MSETVIALNGLSRRFpGMDRPAVAP-LTCTIRAGYVTGLVGPDGAGKTTLMRMLAGLLKPDEGRASVIGFDPLKDDSALH 79
Cdd:PRK10253 1 MTESVARLRGEQLTL-GYGKYTVAEnLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIQHYASKEV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 80 A-VLGYMPQKFGLYEDLTVMENLT--------LYADLRSVTGEArkkiFDRLLEFTSLGPFTERLAGKLSGGMKQKLGLA 150
Cdd:PRK10253 80 ArRIGLLAQNATTPGDITVQELVArgryphqpLFTRWRKEDEEA----VTKAMQATGITHLADQSVDTLSGGQRQRAWIA 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 488984955 151 CTLVGDPKVLLLDEPGVGVDPISRRELWQMVHELAGDGMLILWSTSYlDEAEQCR---DVLLMNEGKLLYQGEP 221
Cdd:PRK10253 156 MVLAQETAIMLLDEPTTWLDISHQIDLLELLSELNREKGYTLAAVLH-DLNQACRyasHLIALREGKIVAQGAP 228
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
19-219 |
8.91e-12 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 65.45 E-value: 8.91e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 19 DRPAVAPLTCTIRAGYVTGLVGPDGAGKTTLMRMLAGLLK------PDEGRASVIGFDPLKDDS-ALHAVLGYMPQKFGL 91
Cdd:PRK14246 22 DKAILKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLIEiydskiKVDGKVLYFGKDIFQIDAiKLRKEVGMVFQQPNP 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 92 YEDLTVMENLTLYADLRSVTGEAR-KKIFDRLLEFTSL-GPFTERL---AGKLSGGMKQKLGLACTLVGDPKVLLLDEPG 166
Cdd:PRK14246 102 FPHLSIYDNIAYPLKSHGIKEKREiKKIVEECLRKVGLwKEVYDRLnspASQLSGGQQQRLTIARALALKPKVLLMDEPT 181
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 488984955 167 VGVDPISRRELWQMVHELAGDGMLILWSTSYLDEAEQCRDVLLMNEGKLLYQG 219
Cdd:PRK14246 182 SMIDIVNSQAIEKLITELKNEIAIVIVSHNPQQVARVADYVAFLYNGELVEWG 234
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
330-495 |
1.44e-11 |
|
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: 65.26 E-value: 1.44e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 330 IEAQSLTKKF--GDFAATDHVDFQVKRGEIFGLLGPNGAGKSTTFKMMCGLLvPTSGKALVLGMDL-KVSSGKARQHLGY 406
Cdd:cd03289 3 MTVKDLTAKYteGGNAVLENISFSISPGQRVGLLGRTGSGKSTLLSAFLRLL-NTEGDIQIDGVSWnSVPLQKWRKAFGV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 407 MAQKFSLYGNlSVEQNLRFFsgvyglrGRAQNEKIARMSDAFGLKSIARHAADELPL-----------GYKQRLALACSL 475
Cdd:cd03289 82 IPQKVFIFSG-TFRKNLDPY-------GKWSDEEIWKVAEEVGLKSVIEQFPGQLDFvlvdggcvlshGHKQLMCLARSV 153
|
170 180
....*....|....*....|
gi 488984955 476 MHEPDILFLDEPTSGVDPLT 495
Cdd:cd03289 154 LSKAKILLLDEPSAHLDPIT 173
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
344-549 |
1.52e-11 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 66.97 E-value: 1.52e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 344 ATDHVDFQVKRGEIFGLLGPNGAGKSTTFKMMCGLLVPTSGKALVLGMDL---KVSSgkARQHLGYMAQKFSLYgNLSVE 420
Cdd:PRK11176 358 ALRNINFKIPAGKTVALVGRSGSGKSTIANLLTRFYDIDEGEILLDGHDLrdyTLAS--LRNQVALVSQNVHLF-NDTIA 434
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 421 QNLRF-FSGVYGlrgRAQNEKIARMSDAF--------GLKSIARHAADELPLGYKQRLALACSLMHEPDILFLDEPTSGV 491
Cdd:PRK11176 435 NNIAYaRTEQYS---REQIEEAARMAYAMdfinkmdnGLDTVIGENGVLLSGGQRQRIAIARALLRDSPILILDEATSAL 511
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 488984955 492 DPLTRREfwlhINSMVD---KGVTVMVTTHFMDEAEYCDRIGLVYHGKLIASGTPDALKAQ 549
Cdd:PRK11176 512 DTESERA----IQAALDelqKNRTSLVIAHRLSTIEKADEILVVEDGEIVERGTHAELLAQ 568
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
333-495 |
1.69e-11 |
|
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis fibrosis transmembrane conductor regulator (CFTR) in eukaryotes. The principal role of this protein is chloride ion conductance. The protein is predicted to consist of 12 transmembrane domains. Mutations or lesions in the genetic loci have been linked to the aetiology of asthma, bronchiectasis, chronic obstructive pulmonary disease etc. Disease-causing mutations have been studied by 36Cl efflux assays in vitro cell cultures and electrophysiology, all of which point to the impairment of chloride channel stability and not the biosynthetic processing per se. [Transport and binding proteins, Anions]
Pssm-ID: 273530 [Multi-domain] Cd Length: 1490 Bit Score: 67.63 E-value: 1.69e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 333 QSLTKKF--GDFAATDHVDFQVKRGEIFGLLGPNGAGKSTTFKMMCGLLvPTSGKALVLGMDL-KVSSGKARQHLGYMAQ 409
Cdd:TIGR01271 1221 QGLTAKYteAGRAVLQDLSFSVEGGQRVGLLGRTGSGKSTLLSALLRLL-STEGEIQIDGVSWnSVTLQTWRKAFGVIPQ 1299
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 410 K-FSLYGnlSVEQNLRFFSgvyglrgRAQNEKIARMSDAFGLKSIARHAADELPL-----------GYKQRLALACSLMH 477
Cdd:TIGR01271 1300 KvFIFSG--TFRKNLDPYE-------QWSDEEIWKVAEEVGLKSVIEQFPDKLDFvlvdggyvlsnGHKQLMCLARSILS 1370
|
170
....*....|....*...
gi 488984955 478 EPDILFLDEPTSGVDPLT 495
Cdd:TIGR01271 1371 KAKILLLDEPSAHLDPVT 1388
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
327-497 |
1.82e-11 |
|
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: 63.99 E-value: 1.82e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 327 ETVIEAQSLTKKF-----GD--FAATDHVDFQVKRGEIFGLLGPNGAGKSTTFKMMCGLLVPTSGKALVLGMDLKVSSGK 399
Cdd:COG4778 2 TTLLEVENLSKTFtlhlqGGkrLPVLDGVSFSVAAGECVALTGPSGAGKSTLLKCIYGNYLPDSGSILVRHDGGWVDLAQ 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 400 A---------RQHLGYMAQkFslygnLS----------VEQNLRffsgvygLRGRAQNEKIARMSDAFGLKSIARHAADE 460
Cdd:COG4778 82 AspreilalrRRTIGYVSQ-F-----LRviprvsaldvVAEPLL-------ERGVDREEARARARELLARLNLPERLWDL 148
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 488984955 461 LPL----GYKQRLALACSLMHEPDILFLDEPTSGVDPLTRR 497
Cdd:COG4778 149 PPAtfsgGEQQRVNIARGFIADPPLLLLDEPTASLDAANRA 189
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
348-537 |
1.82e-11 |
|
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: 64.03 E-value: 1.82e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 348 VDFQVKRGEIFGLLGPNGAGKSTTFKMMCGLLVPTSGKALVLGMDLKVSSGKarqhlgYMAQKFSLygnlsVEQNLRFFS 427
Cdd:cd03248 33 VSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDGKPISQYEHK------YLHSKVSL-----VGQEPVLFA 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 428 G------VYGLRGrAQNEKIARMSDAFglksiarHAAD---ELPLGY---------------KQRLALACSLMHEPDILF 483
Cdd:cd03248 102 RslqdniAYGLQS-CSFECVKEAAQKA-------HAHSfisELASGYdtevgekgsqlsggqKQRVAIARALIRNPQVLI 173
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 488984955 484 LDEPTSGVDPLTRRefwlhinsMVDKGV-------TVMVTTHFMDEAEYCDRIGLVYHGKL 537
Cdd:cd03248 174 LDEATSALDAESEQ--------QVQQALydwperrTVLVIAHRLSTVERADQILVLDGGRI 226
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
2-187 |
1.99e-11 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 64.67 E-value: 1.99e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 2 SETVIALNGLSRRFpGmDRPAVAPLTCTIRAGYVTGLVGPDGAGKTTLMRMLAGL--LKPD---EGRASVIG---FDPLK 73
Cdd:COG1117 8 LEPKIEVRNLNVYY-G-DKQALKDINLDIPENKVTALIGPSGCGKSTLLRCLNRMndLIPGarvEGEILLDGediYDPDV 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 74 DDSALHAVLGYMPQK---FglyeDLTVMENLTlYAdLRsVTGEARKKIFDRLLEfTSL---GPFTE---RL---AGKLSG 141
Cdd:COG1117 86 DVVELRRRVGMVFQKpnpF----PKSIYDNVA-YG-LR-LHGIKSKSELDEIVE-ESLrkaALWDEvkdRLkksALGLSG 157
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 488984955 142 GMKQKLGLACTLVGDPKVLLLDEPGVGVDPISRRELWQMVHELAGD 187
Cdd:COG1117 158 GQQQRLCIARALAVEPEVLLMDEPTSALDPISTAKIEELILELKKD 203
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
35-222 |
2.03e-11 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 64.48 E-value: 2.03e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 35 VTGLVGPDGAGKTTLMRMLAGLLKPD-----EGRASVIG---FDPLKDDSALHAVLGYMPQKFGLYEDLTVMENLTLYAD 106
Cdd:PRK14267 32 VFALMGPSGCGKSTLLRTFNRLLELNeearvEGEVRLFGrniYSPDVDPIEVRREVGMVFQYPNPFPHLTIYDNVAIGVK 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 107 LRSVTgEARKKIFDRL---LEFTSL-GPFTERL---AGKLSGGMKQKLGLACTLVGDPKVLLLDEPGVGVDPISRRELWQ 179
Cdd:PRK14267 112 LNGLV-KSKKELDERVewaLKKAALwDEVKDRLndyPSNLSGGQRQRLVIARALAMKPKILLMDEPTANIDPVGTAKIEE 190
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 488984955 180 MVHELAGDGMLILWSTSYLDEAEQCRDVLLMNEGKLLYQGePT 222
Cdd:PRK14267 191 LLFELKKEYTIVLVTHSPAQAARVSDYVAFLYLGKLIEVG-PT 232
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
6-165 |
2.58e-11 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 65.25 E-value: 2.58e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 6 IALNGLSRRFPGmDRPAVAPLTCTIRAGYVTGLVGPDGAGKTTLMRMLAGLLKPDEGRAS-----VIGFDPLKDDSALha 80
Cdd:PRK11650 4 LKLQAVRKSYDG-KTQVIKGIDLDVADGEFIVLVGPSGCGKSTLLRMVAGLERITSGEIWiggrvVNELEPADRDIAM-- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 81 VLgympQKFGLYEDLTVMENLTLYADLRSVT-GEARKKIFD--RLLEftsLGPFTERLAGKLSGGMKQKLGLACTLVGDP 157
Cdd:PRK11650 81 VF----QNYALYPHMSVRENMAYGLKIRGMPkAEIEERVAEaaRILE---LEPLLDRKPRELSGGQRQRVAMGRAIVREP 153
|
....*...
gi 488984955 158 KVLLLDEP 165
Cdd:PRK11650 154 AVFLFDEP 161
|
|
| PRK13541 |
PRK13541 |
cytochrome c biogenesis protein CcmA; Provisional |
26-195 |
2.88e-11 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184128 [Multi-domain] Cd Length: 195 Bit Score: 62.97 E-value: 2.88e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 26 LTCTIRAGYVTGLVGPDGAGKTTLMRMLAGLLKPDEGRasvIGFDPLKDDSALHAVLGYMPQKFGLYEDLTVMENLTLYA 105
Cdd:PRK13541 19 LSITFLPSAITYIKGANGCGKSSLLRMIAGIMQPSSGN---IYYKNCNINNIAKPYCTYIGHNLGLKLEMTVFENLKFWS 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 106 DLRSVTgearkKIFDRLLEFTSLGPFTERLAGKLSGGMKQKLGLACTLVGDPKVLLLDEPGVGVDPISRRELWQMVHELA 185
Cdd:PRK13541 96 EIYNSA-----ETLYAAIHYFKLHDLLDEKCYSLSSGMQKIVAIARLIACQSDLWLLDEVETNLSKENRDLLNNLIVMKA 170
|
170
....*....|
gi 488984955 186 GDGMLILWST 195
Cdd:PRK13541 171 NSGGIVLLSS 180
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
19-164 |
3.08e-11 |
|
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 444078 [Multi-domain] Cd Length: 605 Bit Score: 66.00 E-value: 3.08e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 19 DRPAVAPLTCTIRAGYVTGLVGPDGAGKTTLMRMLAGLLKPDEGRASVIGFDpLKD--DSALHAVLGYMPQkfglyeDlT 96
Cdd:COG5265 370 ERPILKGVSFEVPAGKTVAIVGPSGAGKSTLARLLFRFYDVTSGRILIDGQD-IRDvtQASLRAAIGIVPQ------D-T 441
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 97 VMENLTLY---------ADLRSVTGEARKKifdRLLEF---------TSLGpftERlaG-KLSGGMKQKLGLACTLVGDP 157
Cdd:COG5265 442 VLFNDTIAyniaygrpdASEEEVEAAARAA---QIHDFieslpdgydTRVG---ER--GlKLSGGEKQRVAIARTLLKNP 513
|
....*..
gi 488984955 158 KVLLLDE 164
Cdd:COG5265 514 PILIFDE 520
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
3-220 |
3.22e-11 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 64.04 E-value: 3.22e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 3 ETVIALNGLSRRF---PGMDR----PAVAPLTCTIRAGYVTGLVGPDGAGKTTLMRMLAGLLKPDEGrasvigfDPLKDD 75
Cdd:PRK15112 2 ETLLEVRNLSKTFryrTGWFRrqtvEAVKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSG-------ELLIDD 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 76 SALH-AVLGYMPQKFGL-YEDLTVMEN------------LTLYADLrsvTGEARKKIFDRLLEFTSLGP-FTERLAGKLS 140
Cdd:PRK15112 75 HPLHfGDYSYRSQRIRMiFQDPSTSLNprqrisqildfpLRLNTDL---EPEQREKQIIETLRQVGLLPdHASYYPHMLA 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 141 GGMKQKLGLACTLVGDPKVLLLDEPGVGVDPISRRELWQMVHEL-AGDGMLILWSTSYLDEAEQCRD-VLLMNEGKLLYQ 218
Cdd:PRK15112 152 PGQKQRLGLARALILRPKVIIADEALASLDMSMRSQLINLMLELqEKQGISYIYVTQHLGMMKHISDqVLVMHQGEVVER 231
|
..
gi 488984955 219 GE 220
Cdd:PRK15112 232 GS 233
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
6-221 |
3.94e-11 |
|
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: 62.81 E-value: 3.94e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 6 IALNGLSRRFPGMDRPAVAPLTCTIRAGYVTGLVGPDGAGKTTLMRMLAGLLKPDEGRASVIGFD----PLKDdsaLHAV 81
Cdd:cd03369 7 IEVENLSVRYAPDLPPVLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDGIDistiPLED---LRSS 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 82 LGYMPQKFGLYeDLTVMENLTLYADLRSVtgearkKIFDrLLEFTSLGpfterlaGKLSGGMKQKLGLACTLVGDPKVLL 161
Cdd:cd03369 84 LTIIPQDPTLF-SGTIRSNLDPFDEYSDE------EIYG-ALRVSEGG-------LNLSQGQRQLLCLARALLKRPRVLV 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 488984955 162 LDEPGVGVDPISRRELWQMVHEL-AGDGMLILwsTSYLDEAEQCRDVLLMNEGKLLYQGEP 221
Cdd:cd03369 149 LDEATASIDYATDALIQKTIREEfTNSTILTI--AHRLRTIIDYDKILVMDAGEVKEYDHP 207
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
30-228 |
4.28e-11 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 66.29 E-value: 4.28e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 30 IRAGYVTGLVGPDGAGKTTLMRMLA-----GLLKPDEgraSVIGFDPLkdDSALHAVLGYMPQKFGLYEDLTVMENLTLY 104
Cdd:TIGR00956 786 VKPGTLTALMGASGAGKTTLLNVLAervttGVITGGD---RLVNGRPL--DSSFQRSIGYVQQQDLHLPTSTVRESLRFS 860
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 105 ADLR---SVTGEARKKIFD---RLLEFTSLGPFTERLAGK-LSGGMKQKLGLACTLVGDPKVLL-LDEPGVGVDPISRRE 176
Cdd:TIGR00956 861 AYLRqpkSVSKSEKMEYVEeviKLLEMESYADAVVGVPGEgLNVEQRKRLTIGVELVAKPKLLLfLDEPTSGLDSQTAWS 940
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 488984955 177 LWQMVHELAGDGMLILWST---SYLDEAEQCRDVLLMNEGKLLYQGEPTALTQTM 228
Cdd:TIGR00956 941 ICKLMRKLADHGQAILCTIhqpSAILFEEFDRLLLLQKGGQTVYFGDLGENSHTI 995
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
346-543 |
4.64e-11 |
|
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: 62.90 E-value: 4.64e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 346 DHVDFQVKRGEIFGLLGPNGAGKSTTFKMMCGLLVPTSGKALVLGMDL-KVSSGKARQHLGYMAQK---FSlyGnlSVEQ 421
Cdd:cd03244 21 KNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSILIDGVDIsKIGLHDLRSRISIIPQDpvlFS--G--TIRS 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 422 NLRFFsgvyglrGRAQNEKIARMSDAFGLKSI---------ARHAADELPL--GYKQRLALACSLMHEPDILFLDEPTSG 490
Cdd:cd03244 97 NLDPF-------GEYSDEELWQALERVGLKEFveslpggldTVVEEGGENLsvGQRQLLCLARALLRKSKILVLDEATAS 169
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 488984955 491 VDPLT--------RREFwlhinsmvdKGVTVMVTTH----FMDeaeyCDRIGLVYHGKLIASGTP 543
Cdd:cd03244 170 VDPETdaliqktiREAF---------KDCTVLTIAHrldtIID----SDRILVLDKGRVVEFDSP 221
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
6-191 |
4.75e-11 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 65.60 E-value: 4.75e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 6 IALNGLSRRFPGmDRPAVAPLTCTIRAGYVTGLVGPDGAGKTTLMRMLAGLLKPDEGRasvIGFDPLKDdsalhaVLgYM 85
Cdd:COG4178 363 LALEDLTLRTPD-GRPLLEDLSLSLKPGERLLITGPSGSGKSTLLRAIAGLWPYGSGR---IARPAGAR------VL-FL 431
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 86 PQKfgLYedL---TVMENLTLYADLRSVTGEARKKIfdrlLEFTSLGPFTERL------AGKLSGGMKQKLGLACTLVGD 156
Cdd:COG4178 432 PQR--PY--LplgTLREALLYPATAEAFSDAELREA----LEAVGLGHLAERLdeeadwDQVLSLGEQQRLAFARLLLHK 503
|
170 180 190
....*....|....*....|....*....|....*
gi 488984955 157 PKVLLLDEPGVGVDPISRRELWQMVHELAGDGMLI 191
Cdd:COG4178 504 PDWLFLDEATSALDEENEAALYQLLREELPGTTVI 538
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
355-518 |
5.16e-11 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 65.29 E-value: 5.16e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 355 GEIFGLLGPNGAGKSTTFKMMCGLLVPTSGKALVLGMDLKVSSGKARQhLGYMAQKFSLYGNLSVEQNLRFFSGVYGLRG 434
Cdd:PLN03211 94 GEILAVLGPSGSGKSTLLNALAGRIQGNNFTGTILANNRKPTKQILKR-TGFVTQDDILYPHLTVRETLVFCSLLRLPKS 172
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 435 RAQNEKIarmsdafglkSIARHAADELPL------------------GYKQRLALACSLMHEPDILFLDEPTSGVDPLTR 496
Cdd:PLN03211 173 LTKQEKI----------LVAESVISELGLtkcentiignsfirgisgGERKRVSIAHEMLINPSLLILDEPTSGLDATAA 242
|
170 180
....*....|....*....|..
gi 488984955 497 REFWLHINSMVDKGVTVMVTTH 518
Cdd:PLN03211 243 YRLVLTLGSLAQKGKTIVTSMH 264
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
326-492 |
5.16e-11 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 64.22 E-value: 5.16e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 326 EETVIEAQSLTK----KFGDFA------ATDHVDFQVKRGEIFGLLGPNGAGKSTTFKMMCGLLVPTSGKALVLGMDLKV 395
Cdd:PRK11308 2 QQPLLQAIDLKKhypvKRGLFKperlvkALDGVSFTLERGKTLAVVGESGCGKSTLARLLTMIETPTGGELYYQGQDLLK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 396 SSGKARQHLgymAQKFSL-----YGNLS----VEQNLRFFSGVYGLRGRAQN-EKIARMSDAFGLKsiARHAaDELPL-- 463
Cdd:PRK11308 82 ADPEAQKLL---RQKIQIvfqnpYGSLNprkkVGQILEEPLLINTSLSAAERrEKALAMMAKVGLR--PEHY-DRYPHmf 155
|
170 180 190
....*....|....*....|....*....|.
gi 488984955 464 --GYKQRLALACSLMHEPDILFLDEPTSGVD 492
Cdd:PRK11308 156 sgGQRQRIAIARALMLDPDVVVADEPVSALD 186
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
346-518 |
5.87e-11 |
|
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding cassette transporter (Pat) is involved in the import of very long-chain fatty acids (VLCFA) into the peroxisome. The peroxisomal membrane forms a permeability barrier for a wide variety of metabolites required for and formed during fatty acid beta-oxidation. To communicate with the cytoplasm and mitochondria, peroxisomes need dedicated proteins to transport such hydrophilic molecules across their membranes. X-linked adrenoleukodystrophy (X-ALD) is caused by mutations in the ALD gene, which encodes ALDP (adrenoleukodystrophy protein ), a peroxisomal integral membrane protein that is a member of the ATP-binding cassette (ABC) transporter protein family. The disease is characterized by a striking and unpredictable variation in phenotypic expression. Phenotypes include the rapidly progressive childhood cerebral form (CCALD), the milder adult form, adrenomyeloneuropathy (AMN), and variants without neurologic involvement (i.e. asymptomatic).
Pssm-ID: 213190 [Multi-domain] Cd Length: 166 Bit Score: 61.40 E-value: 5.87e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 346 DHVDFQVKRGEIFGLLGPNGAGKSTTFKMMCGLLVPTSGKalvLGMdlkvssgKARQHLGYMAQK--FSLyGNLsveqnl 423
Cdd:cd03223 18 KDLSFEIKPGDRLLITGPSGTGKSSLFRALAGLWPWGSGR---IGM-------PEGEDLLFLPQRpyLPL-GTL------ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 424 rffsgvyglrgRAQnekiarmsdafglksIARHAADELPLGYKQRLALACSLMHEPDILFLDEPTSGVDPLTRREFWLHI 503
Cdd:cd03223 81 -----------REQ---------------LIYPWDDVLSGGEQQRLAFARLLLHKPKFVFLDEATSALDEESEDRLYQLL 134
|
170
....*....|....*
gi 488984955 504 NsmvDKGVTVMVTTH 518
Cdd:cd03223 135 K---ELGITVISVGH 146
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
4-165 |
7.96e-11 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 64.75 E-value: 7.96e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 4 TVIALNGLSRRFPgmDRPAVAPLTCTIRAGYVTGLVGPDGAGKTTLMRMLAGLLKPDEGRAsVIGfDPLKddsalhavLG 83
Cdd:PRK11819 323 KVIEAENLSKSFG--DRLLIDDLSFSLPPGGIVGIIGPNGAGKSTLFKMITGQEQPDSGTI-KIG-ETVK--------LA 390
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 84 YMPQ-KFGLYEDLTVMENLTLYADLRSVtgeARKKIFDR--LLEFTSLGPFTERLAGKLSGGMKQKLGLACTLVGDPKVL 160
Cdd:PRK11819 391 YVDQsRDALDPNKTVWEEISGGLDIIKV---GNREIPSRayVGRFNFKGGDQQKKVGVLSGGERNRLHLAKTLKQGGNVL 467
|
....*
gi 488984955 161 LLDEP 165
Cdd:PRK11819 468 LLDEP 472
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
26-170 |
9.39e-11 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 64.87 E-value: 9.39e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 26 LTCTIRAGYVTGLVGPDGAGKTTLMRMLAGLLKPD--EGRASVIGFdPLKDDSaLHAVLGYMPQKFGLYEDLTVMENLTL 103
Cdd:PLN03140 899 VTGAFRPGVLTALMGVSGAGKTTLMDVLAGRKTGGyiEGDIRISGF-PKKQET-FARISGYCEQNDIHSPQVTVRESLIY 976
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 488984955 104 YADLR---SVTGEARKKIFDRLLEFTSLGPFTERLAG-----KLSGGMKQKLGLACTLVGDPKVLLLDEPGVGVD 170
Cdd:PLN03140 977 SAFLRlpkEVSKEEKMMFVDEVMELVELDNLKDAIVGlpgvtGLSTEQRKRLTIAVELVANPSIIFMDEPTSGLD 1051
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
20-215 |
1.29e-10 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 61.43 E-value: 1.29e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 20 RPAVAPLTCTIRAGYVTGLVGPDGAGKTTLMRMLAGLLKPDEGRASVIGFD--PLKDDSA--LHAVLGYMPQKFGLYEDL 95
Cdd:PRK10908 15 RQALQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDitRLKNREVpfLRRQIGMIFQDHHLLMDR 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 96 TVMENLTLYADLRSVTGEARKKIFDRLLEFTSLGPFTERLAGKLSGGMKQKLGLACTLVGDPKVLLLDEPGVGVDPISRR 175
Cdd:PRK10908 95 TVYDNVAIPLIIAGASGDDIRRRVSAALDKVGLLDKAKNFPIQLSGGEQQRVGIARAVVNKPAVLLADEPTGNLDDALSE 174
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 488984955 176 ELWQMVHELAGDGMLILWSTSYLDE-AEQCRDVLLMNEGKL 215
Cdd:PRK10908 175 GILRLFEEFNRVGVTVLMATHDIGLiSRRSYRMLTLSDGHL 215
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
2-541 |
1.69e-10 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 63.72 E-value: 1.69e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 2 SETVIALNGLSRRF--PGMDRPAVAPLTCTIRAGYVTGLVGPDGAGKT----TLMRML---AGLLKPDE-----GRASVI 67
Cdd:PRK10261 9 ARDVLAVENLNIAFmqEQQKIAAVRNLSFSLQRGETLAIVGESGSGKSvtalALMRLLeqaGGLVQCDKmllrrRSRQVI 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 68 GFDPLKDDSALHAVLGYMPQKFglYEDLT-----------VMENLTLYADLRSVTGEARKKifdRLLEFTSLgPFTE--- 133
Cdd:PRK10261 89 ELSEQSAAQMRHVRGADMAMIF--QEPMTslnpvftvgeqIAESIRLHQGASREEAMVEAK---RMLDQVRI-PEAQtil 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 134 -RLAGKLSGGMKQKLGLACTLVGDPKVLLLDEPGVGVDPISRRELWQMVHELAGD-GMLILWSTSYLDEAEQCRD-VLLM 210
Cdd:PRK10261 163 sRYPHQLSGGMRQRVMIAMALSCRPAVLIADEPTTALDVTIQAQILQLIKVLQKEmSMGVIFITHDMGVVAEIADrVLVM 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 211 negkllYQGEptALTQTMAGRSFlvSSPQENNRRLLQRAlkLPQVsdGVIQGKSV----RLILKKDARIEEVQQHGDM-- 284
Cdd:PRK10261 243 ------YQGE--AVETGSVEQIF--HAPQHPYTRALLAA--VPQL--GAMKGLDYprrfPLISLEHPAKQEPPIEQDTvv 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 285 ---PPLQVADTAPRFedafidllggagtaesPL-GAIIHRVdgsKEETvieaqsltkkfgdfAATDHVDFQVKRGEIFGL 360
Cdd:PRK10261 309 dgePILQVRNLVTRF----------------PLrSGLLNRV---TREV--------------HAVEKVSFDLWPGETLSL 355
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 361 LGPNGAGKSTTFKMMCGLLVPTSGKALVLGMDLKVSSGKARQHLGYMAQKF--SLYGNL--------SVEQNLRffsgVY 430
Cdd:PRK10261 356 VGESGSGKSTTGRALLRLVESQGGEIIFNGQRIDTLSPGKLQALRRDIQFIfqDPYASLdprqtvgdSIMEPLR----VH 431
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 431 GL-RGRAQNEKIARMSDAFGLKsiARHA---ADELPLGYKQRLALACSLMHEPDILFLDEPTSGVDPLTRREFwlhINSM 506
Cdd:PRK10261 432 GLlPGKAAAARVAWLLERVGLL--PEHAwryPHEFSGGQRQRICIARALALNPKVIIADEAVSALDVSIRGQI---INLL 506
|
570 580 590 600
....*....|....*....|....*....|....*....|
gi 488984955 507 VD----KGVTVMVTTHFMDEAEYCD-RIGLVYHGKLIASG 541
Cdd:PRK10261 507 LDlqrdFGIAYLFISHDMAVVERIShRVAVMYLGQIVEIG 546
|
|
| sufC |
TIGR01978 |
FeS assembly ATPase SufC; SufC is part of the SUF system, shown in E. coli to consist of six ... |
348-544 |
1.77e-10 |
|
FeS assembly ATPase SufC; SufC is part of the SUF system, shown in E. coli to consist of six proteins and believed to act in Fe-S cluster formation during oxidative stress. SufC forms a complex with SufB and SufD. SufC belongs to the ATP-binding cassette transporter family (pfam00005) but is no longer thought to be part of a transporter. The complex is reported as cytosolic () or associated with the membrane (). The SUF system also includes a cysteine desulfurase (SufS, enhanced by SufE) and a probable iron-sulfur cluster assembly scaffold protein, SufA. [Biosynthesis of cofactors, prosthetic groups, and carriers, Other]
Pssm-ID: 273907 [Multi-domain] Cd Length: 243 Bit Score: 61.51 E-value: 1.77e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 348 VDFQVKRGEIFGLLGPNGAGKSTTFKMMCG---LLVpTSGKALVLGMDLKVSSGKARQHLG-YMAQKFslygnlSVE--- 420
Cdd:TIGR01978 19 VNLTVKKGEIHAIMGPNGSGKSTLSKTIAGhpsYEV-TSGTILFKGQDLLELEPDERARAGlFLAFQY------PEEipg 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 421 -QNLRFFSGVYGLRGRAQNEKIARMSDAFGL--KSIARHAADELPL----------GYKQRLALACSLMHEPDILFLDEP 487
Cdd:TIGR01978 92 vSNLEFLRSALNARRSARGEEPLDLLDFEKLlkEKLALLDMDEEFLnrsvnegfsgGEKKRNEILQMALLEPKLAILDEI 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 488984955 488 TSGVDPLTRREFWLHINSMVDKGVTVMVTTHFMDEAEYC--DRIGLVYHGKLIASGTPD 544
Cdd:TIGR01978 172 DSGLDIDALKIVAEGINRLREPDRSFLIITHYQRLLNYIkpDYVHVLLDGRIVKSGDVE 230
|
|
| SufC |
COG0396 |
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, ... |
348-544 |
1.89e-10 |
|
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440165 [Multi-domain] Cd Length: 245 Bit Score: 61.24 E-value: 1.89e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 348 VDFQVKRGEIFGLLGPNGAGKSTTFKMMCGL--LVPTSGKALVLGMDLKvssgkarqhlgymaqkfslygNLSVEQNLR- 424
Cdd:COG0396 19 VNLTIKPGEVHAIMGPNGSGKSTLAKVLMGHpkYEVTSGSILLDGEDIL---------------------ELSPDERARa 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 425 --FFS--------GV---YGLRgRAQNEKIARMSDAFGLKSIARHAADELPL---------------GYKQRLALACSLM 476
Cdd:COG0396 78 giFLAfqypveipGVsvsNFLR-TALNARRGEELSAREFLKLLKEKMKELGLdedfldryvnegfsgGEKKRNEILQMLL 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 488984955 477 HEPDILFLDEPTSGVD-----PLTRRefwlhINSMVDKGVTVMVTTH---FMDEAEyCDRIGLVYHGKLIASGTPD 544
Cdd:COG0396 157 LEPKLAILDETDSGLDidalrIVAEG-----VNKLRSPDRGILIITHyqrILDYIK-PDFVHVLVDGRIVKSGGKE 226
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
350-546 |
1.98e-10 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 63.84 E-value: 1.98e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 350 FQVKRGEIFGLLGPNGAGKSTTFKMMCGLLVPTSGKALVLGMDL-KVSSGKARQHLGYMAQKFSLYGNlSVEQNLRFFS- 427
Cdd:PLN03232 1257 FFVSPSEKVGVVGRTGAGKSSMLNALFRIVELEKGRIMIDDCDVaKFGLTDLRRVLSIIPQSPVLFSG-TVRFNIDPFSe 1335
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 428 ----GVYGLRGRAQNEKIARMSdAFGLKSIARHAADELPLGYKQRLALACSLMHEPDILFLDEPTSGVDPLT-------- 495
Cdd:PLN03232 1336 hndaDLWEALERAHIKDVIDRN-PFGLDAEVSEGGENFSVGQRQLLSLARALLRRSKILVLDEATASVDVRTdsliqrti 1414
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 488984955 496 RREFwlhinsmvdKGVTVMVTTHFMDEAEYCDRIGLVYHGKLIASGTPDAL 546
Cdd:PLN03232 1415 REEF---------KSCTMLVIAHRLNTIIDCDKILVLSSGQVLEYDSPQEL 1456
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
35-222 |
2.06e-10 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 61.65 E-value: 2.06e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 35 VTGLVGPDGAGKTTLMRML-------AGLLKPDE---GRASVIGFDPLKDDSALHAVLGYMPQKFglyeDLTVMENLtlY 104
Cdd:PRK14271 49 VTSLMGPTGSGKTTFLRTLnrmndkvSGYRYSGDvllGGRSIFNYRDVLEFRRRVGMLFQRPNPF----PMSIMDNV--L 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 105 ADLRSVTGEARKKIFD----RLLEFTSLGPFTERLAG---KLSGGMKQKLGLACTLVGDPKVLLLDEPGVGVDPISRREL 177
Cdd:PRK14271 123 AGVRAHKLVPRKEFRGvaqaRLTEVGLWDAVKDRLSDspfRLSGGQQQLLCLARTLAVNPEVLLLDEPTSALDPTTTEKI 202
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 488984955 178 WQMVHELAgDGMLILWSTSYLDEAEQCRD-VLLMNEGKLLYQGePT 222
Cdd:PRK14271 203 EEFIRSLA-DRLTVIIVTHNLAQAARISDrAALFFDGRLVEEG-PT 246
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
8-165 |
3.20e-10 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 62.60 E-value: 3.20e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 8 LNGLSRRFPgmDRPAVAPLTCTIRAGYVTGLVGPDGAGKTTLMRMLAGLLKPDEGrasVIGFdplkddsALHAVLGYMPQ 87
Cdd:PRK15064 322 VENLTKGFD--NGPLFKNLNLLLEAGERLAIIGENGVGKTTLLRTLVGELEPDSG---TVKW-------SENANIGYYAQ 389
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 88 ----KFGlyEDLTVMENLTLYAD-------LRSVTGearkkifdRLLeftslgpFTERLAGK----LSGGMKQKLGLACT 152
Cdd:PRK15064 390 dhayDFE--NDLTLFDWMSQWRQegddeqaVRGTLG--------RLL-------FSQDDIKKsvkvLSGGEKGRMLFGKL 452
|
170
....*....|...
gi 488984955 153 LVGDPKVLLLDEP 165
Cdd:PRK15064 453 MMQKPNVLVMDEP 465
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
346-549 |
3.79e-10 |
|
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 444078 [Multi-domain] Cd Length: 605 Bit Score: 62.53 E-value: 3.79e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 346 DHVDFQVKRGEIFGLLGPNGAGKSTTFKMMCGLLVPTSGKALVLGMDLK-VSSGKARQHLGYMAQKFSLYgNLSVEQNLR 424
Cdd:COG5265 375 KGVSFEVPAGKTVAIVGPSGAGKSTLARLLFRFYDVTSGRILIDGQDIRdVTQASLRAAIGIVPQDTVLF-NDTIAYNIA 453
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 425 ffsgvYGLRG--RAQNEKIARMS--DAFglksIARhaadeLPLGY---------------KQRLALACSLMHEPDILFLD 485
Cdd:COG5265 454 -----YGRPDasEEEVEAAARAAqiHDF----IES-----LPDGYdtrvgerglklsggeKQRVAIARTLLKNPPILIFD 519
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 488984955 486 EPTSGVDPLTRREFWLHINSmVDKGVTVMVTTHFMDEAEYCDRIgLVY-HGKLIASGTPDALKAQ 549
Cdd:COG5265 520 EATSALDSRTERAIQAALRE-VARGRTTLVIAHRLSTIVDADEI-LVLeAGRIVERGTHAELLAQ 582
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
347-546 |
4.66e-10 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 62.83 E-value: 4.66e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 347 HVDFQVKRGEIFGLLGPNGAGKSTTFKMMCGLLVPTSGKALVLGMDL-KVSSGKARQHLGYMAQKFSLYGNlSVEQNLRF 425
Cdd:PLN03130 1257 GLSFEISPSEKVGIVGRTGAGKSSMLNALFRIVELERGRILIDGCDIsKFGLMDLRKVLGIIPQAPVLFSG-TVRFNLDP 1335
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 426 FS-----GVYGLRGRAQNEKIARmSDAFGLKSIARHAADELPLGYKQRLALACSLMHEPDILFLDEPTSGVDPLT----- 495
Cdd:PLN03130 1336 FNehndaDLWESLERAHLKDVIR-RNSLGLDAEVSEAGENFSVGQRQLLSLARALLRRSKILVLDEATAAVDVRTdaliq 1414
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 488984955 496 ---RREFwlhinsmvdKGVTVMVTTHFMDEAEYCDRIGLVYHGKLIASGTPDAL 546
Cdd:PLN03130 1415 ktiREEF---------KSCTMLIIAHRLNTIIDCDRILVLDAGRVVEFDTPENL 1459
|
|
| nickel_nikE |
TIGR02769 |
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a ... |
29-218 |
5.87e-10 |
|
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: 60.20 E-value: 5.87e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 29 TIRAGYVTGLVGPDGAGKTTLMRMLAGLLKPDEGRASVIGFDPLKDDSA--------LHAVLGYMPQKFGLYEDL--TVM 98
Cdd:TIGR02769 33 SIEEGETVGLLGRSGCGKSTLARLLLGLEKPAQGTVSFRGQDLYQLDRKqrrafrrdVQLVFQDSPSAVNPRMTVrqIIG 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 99 ENLTLYADLRSVTGEARKKifdRLLEFTSLGP-FTERLAGKLSGGMKQKLGLACTLVGDPKVLLLDEPGVGVDPISRREL 177
Cdd:TIGR02769 113 EPLRHLTSLDESEQKARIA---ELLDMVGLRSeDADKLPRQLSGGQLQRINIARALAVKPKLIVLDEAVSNLDMVLQAVI 189
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 488984955 178 WQMVHEL-AGDGMLILWSTSYLDEAEQ-CRDVLLMNEGKLLYQ 218
Cdd:TIGR02769 190 LELLRKLqQAFGTAYLFITHDLRLVQSfCQRVAVMDKGQIVEE 232
|
|
| tagH |
PRK13545 |
teichoic acids export protein ATP-binding subunit; Provisional |
344-537 |
5.93e-10 |
|
teichoic acids export protein ATP-binding subunit; Provisional
Pssm-ID: 184130 [Multi-domain] Cd Length: 549 Bit Score: 61.83 E-value: 5.93e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 344 ATDHVDFQVKRGEIFGLLGPNGAGKSTTFKMMCGLLVPTSGKalvlgMDLKVSSgkarqhlGYMAQKFSLYGNLSVEQNL 423
Cdd:PRK13545 39 ALNNISFEVPEGEIVGIIGLNGSGKSTLSNLIAGVTMPNKGT-----VDIKGSA-------ALIAISSGLNGQLTGIENI 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 424 RFFSGVYGLRGRAQNEKIARMSDAFGLKSIARHAADELPLGYKQRLALACSLMHEPDILFLDEPTSGVDPLTRREFWLHI 503
Cdd:PRK13545 107 ELKGLMMGLTKEKIKEIIPEIIEFADIGKFIYQPVKTYSSGMKSRLGFAISVHINPDILVIDEALSVGDQTFTKKCLDKM 186
|
170 180 190
....*....|....*....|....*....|....*
gi 488984955 504 NSMVDKGVTVMVTTHFMDEAE-YCDRIGLVYHGKL 537
Cdd:PRK13545 187 NEFKEQGKTIFFISHSLSQVKsFCTKALWLHYGQV 221
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
19-220 |
6.41e-10 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 61.82 E-value: 6.41e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 19 DRPAVAPLTCTIRAGYVTGLVGPDGAGKTTLMRMLAGLLKPDEGRASVIGFDPlKDDSALHAVLGYMPQKFGLYEDLTVM 98
Cdd:PLN03211 80 ERTILNGVTGMASPGEILAVLGPSGSGKSTLLNALAGRIQGNNFTGTILANNR-KPTKQILKRTGFVTQDDILYPHLTVR 158
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 99 ENLTLYADLR---SVTGEARKKIFDRLLEFTSLGPFTERLAGK-----LSGGMKQKLGLACTLVGDPKVLLLDEPGVGVD 170
Cdd:PLN03211 159 ETLVFCSLLRlpkSLTKQEKILVAESVISELGLTKCENTIIGNsfirgISGGERKRVSIAHEMLINPSLLILDEPTSGLD 238
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 488984955 171 PISRRELWQMVHELAGDGMLILWSTSYLDEA--EQCRDVLLMNEGKLLYQGE 220
Cdd:PLN03211 239 ATAAYRLVLTLGSLAQKGKTIVTSMHQPSSRvyQMFDSVLVLSEGRCLFFGK 290
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
344-523 |
6.87e-10 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 59.71 E-value: 6.87e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 344 ATDHVDFQVKRGEIFGLLGPNGAGKSTTFKMMCGLLVPTSGKALVLGMdlKVSSGKARQhlGYMAQKFSLYGNLSVEQNL 423
Cdd:PRK11248 16 ALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDGK--PVEGPGAER--GVVFQNEGLLPWRNVQDNV 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 424 RFfsgvyGLR----GRAQNEKIAR-MSDAFGLKSIARHAADELPLGYKQRLALACSLMHEPDILFLDEPTSGVDPLTRRE 498
Cdd:PRK11248 92 AF-----GLQlagvEKMQRLEIAHqMLKKVGLEGAEKRYIWQLSGGQRQRVGIARALAANPQLLLLDEPFGALDAFTREQ 166
|
170 180
....*....|....*....|....*.
gi 488984955 499 FW-LHINSMVDKGVTVMVTTHFMDEA 523
Cdd:PRK11248 167 MQtLLLKLWQETGKQVLLITHDIEEA 192
|
|
| PvdE |
COG4615 |
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ... |
348-529 |
8.02e-10 |
|
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion transport and metabolism];
Pssm-ID: 443659 [Multi-domain] Cd Length: 547 Bit Score: 61.35 E-value: 8.02e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 348 VDFQVKRGEIFGLLGPNGAGKSTTFKMMCGLLVPTSGKALVlgmDLKVSSGKARQHlgYMaQKFSlygnlSVEQNLRFFS 427
Cdd:COG4615 351 IDLTIRRGELVFIVGGNGSGKSTLAKLLTGLYRPESGEILL---DGQPVTADNREA--YR-QLFS-----AVFSDFHLFD 419
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 428 GVYGLRGRAQNEKIARMSDAFGLKSIARHAAD-----ELPLGYKQRLALACSLMHEPDILFLDEPTSGVDPLTRREFWLH 502
Cdd:COG4615 420 RLLGLDGEADPARARELLERLELDHKVSVEDGrfsttDLSQGQRKRLALLVALLEDRPILVFDEWAADQDPEFRRVFYTE 499
|
170 180 190
....*....|....*....|....*....|.
gi 488984955 503 I-NSMVDKGVTVMVTTH---FMDEAeycDRI 529
Cdd:COG4615 500 LlPELKARGKTVIAISHddrYFDLA---DRV 527
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
298-529 |
8.30e-10 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 61.36 E-value: 8.30e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 298 DAFIDLLGGAGTAESPLGAIIHRVDGSkeetvIEAQSLTKKFGDFAA-TDHVDFQVKRGEifGLL--GPNGAGKSTTFKM 374
Cdd:COG4178 336 AGFEEALEAADALPEAASRIETSEDGA-----LALEDLTLRTPDGRPlLEDLSLSLKPGE--RLLitGPSGSGKSTLLRA 408
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 375 MCGL--------LVPTSGKALVLGMDLKVSSGKARQHLGY--MAQKFSlygnlsveqnlrffsgvyglrgraqNEKIARM 444
Cdd:COG4178 409 IAGLwpygsgriARPAGARVLFLPQRPYLPLGTLREALLYpaTAEAFS-------------------------DAELREA 463
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 445 SDAFGLKSIARHAADE------LPLGYKQRLALACSLMHEPDILFLDEPTSGVDPLTRREFWLHINSMVdKGVTVMVTTH 518
Cdd:COG4178 464 LEAVGLGHLAERLDEEadwdqvLSLGEQQRLAFARLLLHKPDWLFLDEATSALDEENEAALYQLLREEL-PGTTVISVGH 542
|
250
....*....|.
gi 488984955 519 FMDEAEYCDRI 529
Cdd:COG4178 543 RSTLAAFHDRV 553
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
326-555 |
8.54e-10 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 59.55 E-value: 8.54e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 326 EETVIEAQSLTKKFGDFAATDHVDFQVKRGEIFGLLGPNGAGKSTTFKMMCGLLVPTSGKALVLG-----MDLKVSSGKA 400
Cdd:PRK11701 3 DQPLLSVRGLTKLYGPRKGCRDVSFDLYPGEVLGIVGESGSGKTTLLNALSARLAPDAGEVHYRMrdgqlRDLYALSEAE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 401 RQHLGYMAQKFslygnlsVEQNLRffsgvYGLRGR------------AQNEK----I-ARMSDAFGLKSIARHAADELPL 463
Cdd:PRK11701 83 RRRLLRTEWGF-------VHQHPR-----DGLRMQvsaggnigerlmAVGARhygdIrATAGDWLERVEIDAARIDDLPT 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 464 ----GYKQRLALACSLMHEPDILFLDEPTSGVD--------PLTRRefwlhinSMVDKGVTVMVTTHFMDEAE-YCDRIG 530
Cdd:PRK11701 151 tfsgGMQQRLQIARNLVTHPRLVFMDEPTGGLDvsvqarllDLLRG-------LVRELGLAVVIVTHDLAVARlLAHRLL 223
|
250 260
....*....|....*....|....*
gi 488984955 531 LVYHGKLIASGTPDalkaQAADDSQ 555
Cdd:PRK11701 224 VMKQGRVVESGLTD----QVLDDPQ 244
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
327-548 |
9.00e-10 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 59.80 E-value: 9.00e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 327 ETVIEAQSLTKKF----GDF-----AATDHVDFQVKRGEIFGLLGPNGAGKSTTFKMMCGLLVPTSGKALVLGMDLKVSS 397
Cdd:PRK15112 2 ETLLEVRNLSKTFryrtGWFrrqtvEAVKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDHPLHFGD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 398 GKAR-QHLGYMAQ--KFSLYGNLSVEQNLRF-FSGVYGLRGRAQNEKIARMSDAFGLksIARHAA---DELPLGYKQRLA 470
Cdd:PRK15112 82 YSYRsQRIRMIFQdpSTSLNPRQRISQILDFpLRLNTDLEPEQREKQIIETLRQVGL--LPDHASyypHMLAPGQKQRLG 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 471 LACSLMHEPDILFLDEPTSGVDPLTRREFwlhINSMVD----KGVT-VMVTTHFMDEAEYCDRIGLVYHGKLIASG-TPD 544
Cdd:PRK15112 160 LARALILRPKVIIADEALASLDMSMRSQL---INLMLElqekQGISyIYVTQHLGMMKHISDQVLVMHQGEVVERGsTAD 236
|
....
gi 488984955 545 ALKA 548
Cdd:PRK15112 237 VLAS 240
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
29-214 |
9.07e-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: 58.63 E-value: 9.07e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 29 TIRAGYVTGLVGPDGAGKTTLMRMLAGLLKPDEGRASVIGfdplkddsalhaVLGYMPQK-------------FGLYED- 94
Cdd:cd03250 27 EVPKGELVAIVGPVGSGKSSLLSALLGELEKLSGSVSVPG------------SIAYVSQEpwiqngtirenilFGKPFDe 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 95 ---LTVMENLTLYADLrsvtgearkKIFDRLLEfTSLGpftERlaG-KLSGGMKQKLGLACTLVGDPKVLLLDEPGVGVD 170
Cdd:cd03250 95 eryEKVIKACALEPDL---------EILPDGDL-TEIG---EK--GiNLSGGQKQRISLARAVYSDADIYLLDDPLSAVD 159
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 488984955 171 PISRRELWQMVheLAGDGML---ILWSTSYLDEAEQCRDVLLMNEGK 214
Cdd:cd03250 160 AHVGRHIFENC--ILGLLLNnktRILVTHQLQLLPHADQIVVLDNGR 204
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
4-219 |
1.04e-09 |
|
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette transporters; The pleiotropic drug resistance (PDR) is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. This PDR subfamily represents domain I of its (ABC-IM)2 organization. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds including sugars, ions, peptides, and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213200 [Multi-domain] Cd Length: 202 Bit Score: 58.43 E-value: 1.04e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 4 TVIALNGLSRRFPGMD-RPAVAPLTCTIRAGYVTGLVGPDGAGKTTLMRMLAGLLKPD---EGRASVIGFDPLKDDSALH 79
Cdd:cd03233 3 TLSWRNISFTTGKGRSkIPILKDFSGVVKPGEMVLVLGRPGSGCSTLLKALANRTEGNvsvEGDIHYNGIPYKEFAEKYP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 80 AVLGYMPQkfglyED-----LTVMENLTLYADLRsvtGEArkkiFDRlleftslgpfterlagKLSGGMKQKLGLACTLV 154
Cdd:cd03233 83 GEIIYVSE-----EDvhfptLTVRETLDFALRCK---GNE----FVR----------------GISGGERKRVSIAEALV 134
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 155 GDPKVLLLDEPGVGVDPISRRE----LWQMVHELAGDGMLILWSTSylDEAEQCRD-VLLMNEGKLLYQG 219
Cdd:cd03233 135 SRASVLCWDNSTRGLDSSTALEilkcIRTMADVLKTTTFVSLYQAS--DEIYDLFDkVLVLYEGRQIYYG 202
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
6-164 |
1.46e-09 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 60.75 E-value: 1.46e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 6 IALNGLSRRFPGmDRPAVAPLTCTIRAGYVTGLVGPDGAGKTTLMRMLAGLLKPDEGRASVIGFDpLKDDS--ALHAVLG 83
Cdd:PRK13657 335 VEFDDVSFSYDN-SRQGVEDVSFEAKPGQTVAIVGPTGAGKSTLINLLQRVFDPQSGRILIDGTD-IRTVTraSLRRNIA 412
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 84 YMPQKFGLYeDLTVMENLTL------YADLR--SVTGEARKKIFDRLLEF-TSLGpftERlAGKLSGGMKQKLGLACTLV 154
Cdd:PRK13657 413 VVFQDAGLF-NRSIEDNIRVgrpdatDEEMRaaAERAQAHDFIERKPDGYdTVVG---ER-GRQLSGGERQRLAIARALL 487
|
170
....*....|
gi 488984955 155 GDPKVLLLDE 164
Cdd:PRK13657 488 KDPPILILDE 497
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
346-541 |
1.74e-09 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 58.56 E-value: 1.74e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 346 DHVDFQVKRGEIFGLLGPNGAGKSTTFKMMCGLLVP----TSGKALVLGMDLKVSSGKARQHLGYMAQKFSLYGNLsveQ 421
Cdd:PRK10418 20 HGVSLTLQRGRVLALVGGSGSGKSLTCAAALGILPAgvrqTAGRVLLDGKPVAPCALRGRKIATIMQNPRSAFNPL---H 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 422 NLRfFSGVYGLRGRAQNEKIARMS---DAFGL---KSIARHAADELPLGYKQRLALACSLMHEPDILFLDEPTSGVDPLT 495
Cdd:PRK10418 97 TMH-THARETCLALGKPADDATLTaalEAVGLenaARVLKLYPFEMSGGMLQRMMIALALLCEAPFIIADEPTTDLDVVA 175
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 488984955 496 RREFWLHINSMV-DKGVTVMVTTHFMD-EAEYCDRIGLVYHGKLIASG 541
Cdd:PRK10418 176 QARILDLLESIVqKRALGMLLVTHDMGvVARLADDVAVMSHGRIVEQG 223
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
6-183 |
1.81e-09 |
|
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: 57.89 E-value: 1.81e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 6 IALNGLSRRFPGMDRPAVAPLTCTIRAGYVTGLVGPDGAGKTTLMRMLAGLLKPDEGRASVIGFD----PLKDdsaLHAV 81
Cdd:cd03244 3 IEFKNVSLRYRPNLPPVLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSILIDGVDiskiGLHD---LRSR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 82 LGYMPQKFGLYEDlTVMENL---TLYADlrsvtgEARKKIfdrlLEFTSLGPFTERLAGKL-----------SGGMKQKL 147
Cdd:cd03244 80 ISIIPQDPVLFSG-TIRSNLdpfGEYSD------EELWQA----LERVGLKEFVESLPGGLdtvveeggenlSVGQRQLL 148
|
170 180 190
....*....|....*....|....*....|....*.
gi 488984955 148 GLACTLVGDPKVLLLDEPGVGVDPISRRELWQMVHE 183
Cdd:cd03244 149 CLARALLRKSKILVLDEATASVDPETDALIQKTIRE 184
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
357-541 |
1.94e-09 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 59.50 E-value: 1.94e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 357 IFGLlgpNGAGKSTTFKMMCGLLVPTSGKaLVLGMDLKVSSGKA------RQHLGYMAQKFSLYGNLSVEQNLRffsgvY 430
Cdd:PRK11144 29 IFGR---SGAGKTSLINAISGLTRPQKGR-IVLNGRVLFDAEKGiclppeKRRIGYVFQDARLFPHYKVRGNLR-----Y 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 431 GLRG--RAQNEKIARMsdaFGLKsiarHAADELPL----GYKQRLALACSLMHEPDILFLDEPTSGVDPLTRREF--WL- 501
Cdd:PRK11144 100 GMAKsmVAQFDKIVAL---LGIE----PLLDRYPGslsgGEKQRVAIGRALLTAPELLLMDEPLASLDLPRKRELlpYLe 172
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 488984955 502 ----HINsmvdkgVTVMVTTHFMDE----AeycDRIGLVYHGKLIASG 541
Cdd:PRK11144 173 rlarEIN------IPILYVSHSLDEilrlA---DRVVVLEQGKVKAFG 211
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
348-535 |
2.00e-09 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 58.51 E-value: 2.00e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 348 VDFQVKRGEIFGLLGPNGAGKSTTFKMMCGL-----LVPTSGKALVLGMDL---KVSSGKARQHLGYMAQKFSLYgNLSV 419
Cdd:PRK14258 26 VSMEIYQSKVTAIIGPSGCGKSTFLKCLNRMnelesEVRVEGRVEFFNQNIyerRVNLNRLRRQVSMVHPKPNLF-PMSV 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 420 EQNLRFFSGVYGLRGRAQNEKI-------ARMSDAfgLKSIARHAADELPLGYKQRLALACSLMHEPDILFLDEPTSGVD 492
Cdd:PRK14258 105 YDNVAYGVKIVGWRPKLEIDDIvesalkdADLWDE--IKHKIHKSALDLSGGQQQRLCIARALAVKPKVLLMDEPCFGLD 182
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 488984955 493 PLT--RREFWLHiNSMVDKGVTVMVTTHFMDEAEYCDRIGLVYHG 535
Cdd:PRK14258 183 PIAsmKVESLIQ-SLRLRSELTMVIVSHNLHQVSRLSDFTAFFKG 226
|
|
| PRK13546 |
PRK13546 |
teichoic acids export ABC transporter ATP-binding subunit TagH; |
319-544 |
2.15e-09 |
|
teichoic acids export ABC transporter ATP-binding subunit TagH;
Pssm-ID: 184131 [Multi-domain] Cd Length: 264 Bit Score: 58.67 E-value: 2.15e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 319 HRVDGSKEETVIEAQSLTKKFGDFAATDHVDFQVKRGEIFGLLGPNGAGKSTTFKMMCGLLVPTSGKALVLGmDLKVssg 398
Cdd:PRK13546 14 YRIYRTNKERMKDALIPKHKNKTFFALDDISLKAYEGDVIGLVGINGSGKSTLSNIIGGSLSPTVGKVDRNG-EVSV--- 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 399 karqhlgyMAQKFSLYGNLSVEQNLRFFSGVYGLRGRAQNEKIARMSDAFGLKSIARHAADELPLGYKQRLALACSLMHE 478
Cdd:PRK13546 90 --------IAISAGLSGQLTGIENIEFKMLCMGFKRKEIKAMTPKIIEFSELGEFIYQPVKKYSSGMRAKLGFSINITVN 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 488984955 479 PDILFLDEPTSGVDPLTRREFWLHINSMVDKGVTVMVTTHFMDEA-EYCDRIGLVYHGKLIASGTPD 544
Cdd:PRK13546 162 PDILVIDEALSVGDQTFAQKCLDKIYEFKEQNKTIFFVSHNLGQVrQFCTKIAWIEGGKLKDYGELD 228
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
29-253 |
2.47e-09 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 58.54 E-value: 2.47e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 29 TIRAGYVTGLVGPDGAGKTTLMRMLAGLLKPDEGRASVIGFDPLKDDSALH-------------AVLGYMPQKfglyedl 95
Cdd:PRK10419 34 SLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWRGEPLAKLNRAQRkafrrdiqmvfqdSISAVNPRK------- 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 96 TVMEnlTLYADLRSVTG---EARKKIFDRLLEFTSLGP-FTERLAGKLSGGMKQKLGLACTLVGDPKVLLLDEPGVGVDP 171
Cdd:PRK10419 107 TVRE--IIREPLRHLLSldkAERLARASEMLRAVDLDDsVLDKRPPQLSGGQLQRVCLARALAVEPKLLILDEAVSNLDL 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 172 ISRRELWQMVHEL-AGDGMLILWSTSYLDEAEQ-CRDVLLMNEGKLLyQGEPTALTQTMagrsflvSSPQEnnrRLLQRA 249
Cdd:PRK10419 185 VLQAGVIRLLKKLqQQFGTACLFITHDLRLVERfCQRVMVMDNGQIV-ETQPVGDKLTF-------SSPAG---RVLQNA 253
|
....
gi 488984955 250 LkLP 253
Cdd:PRK10419 254 V-LP 256
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
344-550 |
2.62e-09 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 59.73 E-value: 2.62e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 344 ATDHVDFQVKRGEIFGLLGPNGAGKSTTFKMMCGLLVPTSGKALVLGM---DLKVSSGKARqhLGYMAQKFSLYGNlSVE 420
Cdd:PRK10789 330 ALENVNFTLKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGDIRFHDIpltKLQLDSWRSR--LAVVSQTPFLFSD-TVA 406
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 421 QNLRFfsgvyglrGR-----AQNEKIARMSDAFglKSIARhaadeLPLGY---------------KQRLALACSLMHEPD 480
Cdd:PRK10789 407 NNIAL--------GRpdatqQEIEHVARLASVH--DDILR-----LPQGYdtevgergvmlsggqKQRISIARALLLNAE 471
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 481 ILFLDEPTSGVDPLTRREFwLHINSMVDKGVTVMVTTHFMDEAEYCDRIGLVYHGKLIASGTPDALKAQA 550
Cdd:PRK10789 472 ILILDDALSAVDGRTEHQI-LHNLRQWGEGRTVIISAHRLSALTEASEILVMQHGHIAQRGNHDQLAQQS 540
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
27-492 |
3.45e-09 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 59.49 E-value: 3.45e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 27 TCTIRAGYVTGLVGPDGAGKTTLMRMLAglLKPDEG----------RASVIGfdplKDDSALHAVL-------------- 82
Cdd:PLN03073 197 SVTLAFGRHYGLVGRNGTGKTTFLRYMA--MHAIDGipkncqilhvEQEVVG----DDTTALQCVLntdiertqlleeea 270
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 83 -----------------GYMPQKFGLYEDLTVMENLTLYADLRSV---TGEARKKIFDRLLEFTSlgPFTERLAGKLSGG 142
Cdd:PLN03073 271 qlvaqqrelefetetgkGKGANKDGVDKDAVSQRLEEIYKRLELIdayTAEARAASILAGLSFTP--EMQVKATKTFSGG 348
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 143 MKQKLGLACTLVGDPKVLLLDEPGVGVDpiSRRELWQMVHELAGDGMLILWSTS--YLDEAeqCRDVLLMNEGKLL-YQG 219
Cdd:PLN03073 349 WRMRIALARALFIEPDLLLLDEPTNHLD--LHAVLWLETYLLKWPKTFIVVSHAreFLNTV--VTDILHLHGQKLVtYKG 424
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 220 EPTALTQTMAGRSFLVSSPQENNRRllQRALKLPQVSDGVIQGKSVRLIlkkDARIEEVQQHGDMPPLqVADTAPRFEDA 299
Cdd:PLN03073 425 DYDTFERTREEQLKNQQKAFESNER--SRSHMQAFIDKFRYNAKRASLV---QSRIKALDRLGHVDAV-VNDPDYKFEFP 498
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 300 FIDllggagtaESPLGAIIHRVDGSkeetvieaqsltkkFGDFAAT---DHVDFQVKRGEIFGLLGPNGAGKSTTFKMMC 376
Cdd:PLN03073 499 TPD--------DRPGPPIISFSDAS--------------FGYPGGPllfKNLNFGIDLDSRIAMVGPNGIGKSTILKLIS 556
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 377 GLLVPTSGKAL--------------VLGMDLKVSSgkarqhLGYMAQKFSlyGNLsvEQNLRFFSGVYGLRGraqnekia 442
Cdd:PLN03073 557 GELQPSSGTVFrsakvrmavfsqhhVDGLDLSSNP------LLYMMRCFP--GVP--EQKLRAHLGSFGVTG-------- 618
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|
gi 488984955 443 rmsdafglkSIARHAADELPLGYKQRLALACSLMHEPDILFLDEPTSGVD 492
Cdd:PLN03073 619 ---------NLALQPMYTLSGGQKSRVAFAKITFKKPHILLLDEPSNHLD 659
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
352-518 |
4.31e-09 |
|
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: 57.38 E-value: 4.31e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 352 VKRGEIFGLLGPNGAGKSTTFKMMCGLLVPTSGK-----------------------ALVLGMDLKVSsgKARQHLGYMA 408
Cdd:cd03236 23 PREGQVLGLVGPNGIGKSTALKILAGKLKPNLGKfddppdwdeildefrgselqnyfTKLLEGDVKVI--VKPQYVDLIP 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 409 QKFSlyGNlsVEQNlrffsgvygLRGRAQNEKIARMSDAFGLKSIARHAADELPLGYKQRLALACSLMHEPDILFLDEPT 488
Cdd:cd03236 101 KAVK--GK--VGEL---------LKKKDERGKLDELVDQLELRHVLDRNIDQLSGGELQRVAIAAALARDADFYFFDEPS 167
|
170 180 190
....*....|....*....|....*....|
gi 488984955 489 SGVDPLTRREFWLHINSMVDKGVTVMVTTH 518
Cdd:cd03236 168 SYLDIKQRLNAARLIRELAEDDNYVLVVEH 197
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
22-184 |
4.86e-09 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 57.48 E-value: 4.86e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 22 AVAPLTCTIRAGYVTGLVGPDGAGKTTLMRMLAGL--LKPD---EGRASVIG---FDPLKDDSALHAVLGYMPQKFGLYE 93
Cdd:PRK14243 25 AVKNVWLDIPKNQITAFIGPSGCGKSTILRCFNRLndLIPGfrvEGKVTFHGknlYAPDVDPVEVRRRIGMVFQKPNPFP 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 94 DlTVMENLTLYADLRSVTGEarkkiFDRLLEfTSL------GPFTERL---AGKLSGGMKQKLGLACTLVGDPKVLLLDE 164
Cdd:PRK14243 105 K-SIYDNIAYGARINGYKGD-----MDELVE-RSLrqaalwDEVKDKLkqsGLSLSGGQQQRLCIARAIAVQPEVILMDE 177
|
170 180
....*....|....*....|
gi 488984955 165 PGVGVDPISRRELWQMVHEL 184
Cdd:PRK14243 178 PCSALDPISTLRIEELMHEL 197
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
26-215 |
6.62e-09 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 56.75 E-value: 6.62e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 26 LTCTIRAGYVTGLVGPDGAGKTTLMRMLAGLLKPDEGRASVIGFDPLKDDSALHAV-----LGYMPQKFGLYEDLTVMEN 100
Cdd:PRK11629 28 VSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPMSKLSSAAKAElrnqkLGFIYQFHHLLPDFTALEN 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 101 LTLYADLRSV-TGEARKKIFDrLLEFTSLGPFTERLAGKLSGGMKQKLGLACTLVGDPKVLLLDEPGVGVDPISRRELWQ 179
Cdd:PRK11629 108 VAMPLLIGKKkPAEINSRALE-MLAAVGLEHRANHRPSELSGGERQRVAIARALVNNPRLVLADEPTGNLDARNADSIFQ 186
|
170 180 190
....*....|....*....|....*....|....*..
gi 488984955 180 MVHEL-AGDGMLILWSTSYLDEAEQCRDVLLMNEGKL 215
Cdd:PRK11629 187 LLGELnRLQGTAFLVVTHDLQLAKRMSRQLEMRDGRL 223
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
29-215 |
7.53e-09 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 58.26 E-value: 7.53e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 29 TIRAGYVTGLVGPDGAGKTTLMRMLAGllkpdegRA--SVIGFDPLKD---------DSALHAVLGYMPQ---KFGLYED 94
Cdd:NF040905 282 NVRRGEIVGIAGLMGAGRTELAMSVFG-------RSygRNISGTVFKDgkevdvstvSDAIDAGLAYVTEdrkGYGLNLI 354
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 95 LTVMENLTLyADLRSVtgeARKKIFDRLLEFTSLGPFTERL----------AGKLSGGMKQKLGLACTLVGDPKVLLLDE 164
Cdd:NF040905 355 DDIKRNITL-ANLGKV---SRRGVIDENEEIKVAEEYRKKMniktpsvfqkVGNLSGGNQQKVVLSKWLFTDPDVLILDE 430
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 488984955 165 PGVGVDPISRRELWQMVHELAGDGMLILWSTSYLDEA-EQCRDVLLMNEGKL 215
Cdd:NF040905 431 PTRGIDVGAKYEIYTIINELAAEGKGVIVISSELPELlGMCDRIYVMNEGRI 482
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
335-533 |
8.63e-09 |
|
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI's are not transport proteins, and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLI's have an N-terminal Fe-S domain and two nucleotide-binding domains, which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213189 [Multi-domain] Cd Length: 177 Bit Score: 55.27 E-value: 8.63e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 335 LTKKFGDFaatdHVDFQ---VKRGEIFGLLGPNGAGKSTTFKMMCGLLVPTSGKalvlgmdlkvsSGKARQHLGYMAQKF 411
Cdd:cd03222 6 CVKRYGVF----FLLVElgvVKEGEVIGIVGPNGTGKTTAVKILAGQLIPNGDN-----------DEWDGITPVYKPQYI 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 412 SLYGnlsveqnlrffsgvyglrgraqnekiarmsdafglksiarhaadelplGYKQRLALACSLMHEPDILFLDEPTSGV 491
Cdd:cd03222 71 DLSG------------------------------------------------GELQRVAIAAALLRNATFYLFDEPSAYL 102
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 488984955 492 DPLTRREFWLHINSMVDKGV-TVMVTTHFMDEAEY-CDRIGLVY 533
Cdd:cd03222 103 DIEQRLNAARAIRRLSEEGKkTALVVEHDLAVLDYlSDRIHVFE 146
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
29-185 |
2.03e-08 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 54.96 E-value: 2.03e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 29 TIRAGYVTGLVGPDGAGKTTLMRMLAGLLKpdegRASVIGFDPLKDDSalhavlgympqkfgLYEDLTVMENLTLYADLR 108
Cdd:COG2401 52 EIEPGEIVLIVGASGSGKSTLLRLLAGALK----GTPVAGCVDVPDNQ--------------FGREASLIDAIGRKGDFK 113
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 488984955 109 SVTGE-ARKKIFDrllEFTSLGPFTErlagkLSGGMKQKLGLACTLVGDPKVLLLDEPGVGVDPISRRELWQMVHELA 185
Cdd:COG2401 114 DAVELlNAVGLSD---AVLWLRRFKE-----LSTGQKFRFRLALLLAERPKLLVIDEFCSHLDRQTAKRVARNLQKLA 183
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
346-518 |
2.54e-08 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 54.58 E-value: 2.54e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 346 DHVDFQVKRGEIFGLLGPNGAGKSTTFKMMCGLLVPTSGKALVLGMDLKVSSGKARQHlgymaqkfSLYGNLSVEQNLRF 425
Cdd:COG2401 47 RDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGALKGTPVAGCVDVPDNQFGREASLID--------AIGRKGDFKDAVEL 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 426 FSGVyGLrgraqnekiarmSDAFGLKsiARHaaDELPLGYKQRLALACSLMHEPDILFLDEPTSGVDPLTRREFWLHINS 505
Cdd:COG2401 119 LNAV-GL------------SDAVLWL--RRF--KELSTGQKFRFRLALLLAERPKLLVIDEFCSHLDRQTAKRVARNLQK 181
|
170
....*....|....
gi 488984955 506 MVDK-GVTVMVTTH 518
Cdd:COG2401 182 LARRaGITLVVATH 195
|
|
| PRK15093 |
PRK15093 |
peptide ABC transporter ATP-binding protein SapD; |
329-546 |
3.21e-08 |
|
peptide ABC transporter ATP-binding protein SapD;
Pssm-ID: 185049 [Multi-domain] Cd Length: 330 Bit Score: 55.58 E-value: 3.21e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 329 VIEAQSLTKKF----GDFAATDHVDFQVKRGEIFGLLGPNGAGKSTTFKMMCGL----LVPTSGKALVLGMD-LKVSSGK 399
Cdd:PRK15093 3 LLDIRNLTIEFktsdGWVKAVDRVSMTLTEGEIRGLVGESGSGKSLIAKAICGVtkdnWRVTADRMRFDDIDlLRLSPRE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 400 ARQHLGY-MAQKFS-----LYGNLSVEQNLRFFSGVYGLRGRAQNEKIARMSDAFGL---------KSIARHAADELPLG 464
Cdd:PRK15093 83 RRKLVGHnVSMIFQepqscLDPSERVGRQLMQNIPGWTYKGRWWQRFGWRKRRAIELlhrvgikdhKDAMRSFPYELTEG 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 465 YKQRLALACSLMHEPDILFLDEPTSGVDPLTRRE-FWLHINSMVDKGVTVMVTTHFMDE-AEYCDRIGLVYHGKLIASGT 542
Cdd:PRK15093 163 ECQKVMIAIALANQPRLLIADEPTNAMEPTTQAQiFRLLTRLNQNNNTTILLISHDLQMlSQWADKINVLYCGQTVETAP 242
|
....
gi 488984955 543 PDAL 546
Cdd:PRK15093 243 SKEL 246
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
325-542 |
4.48e-08 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 54.26 E-value: 4.48e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 325 KEETVIEAQSLTKKFGDFAATDHVDFQVKRGEIFGLLGPNGAGKSTTFKMMCGLlvP----TSGKALVLGMDLKVSSGKA 400
Cdd:CHL00131 3 KNKPILEIKNLHASVNENEILKGLNLSINKGEIHAIMGPNGSGKSTLSKVIAGH--PaykiLEGDILFKGESILDLEPEE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 401 RQHLG-YMAQKFslygnlSVE----QNLRFFSGVYGLRGRAQN----------EKIARMSDAFGLKS--IARHAADELPL 463
Cdd:CHL00131 81 RAHLGiFLAFQY------PIEipgvSNADFLRLAYNSKRKFQGlpeldpleflEIINEKLKLVGMDPsfLSRNVNEGFSG 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 464 GYKQR---LALACSlmhEPDILFLDEPTSGVDPLTRREFWLHINSMVDKGVTVMVTTHFMDEAEYC--DRIGLVYHGKLI 538
Cdd:CHL00131 155 GEKKRneiLQMALL---DSELAILDETDSGLDIDALKIIAEGINKLMTSENSIILITHYQRLLDYIkpDYVHVMQNGKII 231
|
....
gi 488984955 539 ASGT 542
Cdd:CHL00131 232 KTGD 235
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
346-541 |
4.63e-08 |
|
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette transporters; The pleiotropic drug resistance (PDR) is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. This PDR subfamily represents domain I of its (ABC-IM)2 organization. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds including sugars, ions, peptides, and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213200 [Multi-domain] Cd Length: 202 Bit Score: 53.42 E-value: 4.63e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 346 DHVDFQVKRGEIFGLLGPNGAGKSTTFKMMCGLLVPT---SGKALVLGMDLKVSSGKARQHLGYMAQKFSLYGNLSVEQN 422
Cdd:cd03233 24 KDFSGVVKPGEMVLVLGRPGSGCSTLLKALANRTEGNvsvEGDIHYNGIPYKEFAEKYPGEIIYVSEEDVHFPTLTVRET 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 423 LRFfsgvyglRGRAQNEKIARmsdafGLKSiarhaadelplGYKQRLALACSLMHEPDILFLDEPTSGVDPLTRREFWLH 502
Cdd:cd03233 104 LDF-------ALRCKGNEFVR-----GISG-----------GERKRVSIAEALVSRASVLCWDNSTRGLDSSTALEILKC 160
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 488984955 503 INSMVD--KGVTVMVTTHFMDEAEYC-DRIGLVYHGKLIASG 541
Cdd:cd03233 161 IRTMADvlKTTTFVSLYQASDEIYDLfDKVLVLYEGRQIYYG 202
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
347-549 |
4.89e-08 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 55.88 E-value: 4.89e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 347 HVDFQVKRGEIFGLLGPNGAGKSTTFKMMCGLLVPTSGKALVLGMDLKVSSGKA-RQHLGyMAQK------FSLYGNLSV 419
Cdd:PRK10790 359 NINLSVPSRGFVALVGHTGSGKSTLASLLMGYYPLTEGEIRLDGRPLSSLSHSVlRQGVA-MVQQdpvvlaDTFLANVTL 437
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 420 EQNLRFfSGVYGLRGRAQNEKIAR-MSDafGLKSIARHAADELPLGYKQRLALACSLMHEPDILFLDEPTSGVDPLTRRE 498
Cdd:PRK10790 438 GRDISE-EQVWQALETVQLAELARsLPD--GLYTPLGEQGNNLSVGQKQLLALARVLVQTPQILILDEATANIDSGTEQA 514
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 488984955 499 FWlHINSMVDKGVTVMVTTHFMDEAEYCDRIGLVYHGKLIASGTPDALKAQ 549
Cdd:PRK10790 515 IQ-QALAAVREHTTLVVIAHRLSTIVEADTILVLHRGQAVEQGTHQQLLAA 564
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
8-215 |
6.21e-08 |
|
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis fibrosis transmembrane conductor regulator (CFTR) in eukaryotes. The principal role of this protein is chloride ion conductance. The protein is predicted to consist of 12 transmembrane domains. Mutations or lesions in the genetic loci have been linked to the aetiology of asthma, bronchiectasis, chronic obstructive pulmonary disease etc. Disease-causing mutations have been studied by 36Cl efflux assays in vitro cell cultures and electrophysiology, all of which point to the impairment of chloride channel stability and not the biosynthetic processing per se. [Transport and binding proteins, Anions]
Pssm-ID: 273530 [Multi-domain] Cd Length: 1490 Bit Score: 56.07 E-value: 6.21e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 8 LNGLSRRFPGMDRPAVAPLTCTIRAGYVTGLVGPDGAGKTTLMRMLAGLLKPDegraSVIGFDPLKDDSAL----HAVLG 83
Cdd:TIGR01271 1220 VQGLTAKYTEAGRAVLQDLSFSVEGGQRVGLLGRTGSGKSTLLSALLRLLSTE----GEIQIDGVSWNSVTlqtwRKAFG 1295
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 84 YMPQKFGLYEDlTVMENLTLYADLrsvtgeARKKIFdRLLEFTSLGPFTERLAGKL-----------SGGMKQKLGLACT 152
Cdd:TIGR01271 1296 VIPQKVFIFSG-TFRKNLDPYEQW------SDEEIW-KVAEEVGLKSVIEQFPDKLdfvlvdggyvlSNGHKQLMCLARS 1367
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 488984955 153 LVGDPKVLLLDEPGVGVDPISRRELWQMVHELAGDGMLILwSTSYLDEAEQCRDVLLMNEGKL 215
Cdd:TIGR01271 1368 ILSKAKILLLDEPSAHLDPVTLQIIRKTLKQSFSNCTVIL-SEHRVEALLECQQFLVIEGSSV 1429
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
341-492 |
6.89e-08 |
|
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: 53.49 E-value: 6.89e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 341 DFAATDHVDFQVKRGEIFGLLGPNGAGKSTTFKMMCGLLVPTSGK-----ALVLGMDLKVSSGKARQHLGYMAQKFSLYg 415
Cdd:cd03290 13 GLATLSNINIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKvhwsnKNESEPSFEATRSRNRYSVAYAAQKPWLL- 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 416 NLSVEQNLRFFSGVYGLRGRAQNEKIARMSD----AFGLKSIARHAADELPLGYKQRLALACSLMHEPDILFLDEPTSGV 491
Cdd:cd03290 92 NATVEENITFGSPFNKQRYKAVTDACSLQPDidllPFGDQTEIGERGINLSGGQRQRICVARALYQNTNIVFLDDPFSAL 171
|
.
gi 488984955 492 D 492
Cdd:cd03290 172 D 172
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
1-170 |
7.34e-08 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 53.78 E-value: 7.34e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 1 MSETVIALNGLSRRFPGmdRPAVAPLTCTIRAGYVTGLVGPDGAGKTTLMRMLAGLLKPDEGRASVIGFDPLKDDSA--- 77
Cdd:PRK11701 2 MDQPLLSVRGLTKLYGP--RKGCRDVSFDLYPGEVLGIVGESGSGKTTLLNALSARLAPDAGEVHYRMRDGQLRDLYals 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 78 -------LHAVLGYMPQ--KFGLYEDLT----VMENLTL-----YADLRSVTGE--ARKKI-FDRLleftslgpftERLA 136
Cdd:PRK11701 80 eaerrrlLRTEWGFVHQhpRDGLRMQVSaggnIGERLMAvgarhYGDIRATAGDwlERVEIdAARI----------DDLP 149
|
170 180 190
....*....|....*....|....*....|....
gi 488984955 137 GKLSGGMKQKLGLACTLVGDPKVLLLDEPGVGVD 170
Cdd:PRK11701 150 TTFSGGMQQRLQIARNLVTHPRLVFMDEPTGGLD 183
|
|
| CP_lyasePhnK |
TIGR02323 |
phosphonate C-P lyase system protein PhnK; Members of this family are the PhnK protein of C-P ... |
3-170 |
9.85e-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: 53.30 E-value: 9.85e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 3 ETVIALNGLSRRFPGmdRPAVAPLTCTIRAGYVTGLVGPDGAGKTTLMRMLAGLLKPDEGRASVIGFDPLKDD------- 75
Cdd:TIGR02323 1 KPLLQVSGLSKSYGG--GKGCRDVSFDLYPGEVLGIVGESGSGKSTLLGCLAGRLAPDHGTATYIMRSGAELElyqlsea 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 76 ---SALHAVLGYMPQ--KFGLYEDLTVMENLT--LYADLRSVTGEARKKIFDRLLEFTSLGPFTERLAGKLSGGMKQKLG 148
Cdd:TIGR02323 79 errRLMRTEWGFVHQnpRDGLRMRVSAGANIGerLMAIGARHYGNIRATAQDWLEEVEIDPTRIDDLPRAFSGGMQQRLQ 158
|
170 180
....*....|....*....|..
gi 488984955 149 LACTLVGDPKVLLLDEPGVGVD 170
Cdd:TIGR02323 159 IARNLVTRPRLVFMDEPTGGLD 180
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
327-546 |
9.95e-08 |
|
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: 54.69 E-value: 9.95e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 327 ETVIEAQSLTKKFGD----FAATDHVDFQVKRGEIFGLLGPNGAGKSTTFKMMCGLL----VPTSGKALVLGMDLKVSSG 398
Cdd:COG4172 4 MPLLSVEDLSVAFGQgggtVEAVKGVSFDIAAGETLALVGESGSGKSVTALSILRLLpdpaAHPSGSILFDGQDLLGLSE 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 399 KARQHL--GYMAQKF-----SLygN--LSVEQNL-------RffsgvyGLRGRAQNEKIARMSDAFGLKSIARHAAD--- 459
Cdd:COG4172 84 RELRRIrgNRIAMIFqepmtSL--NplHTIGKQIaevlrlhR------GLSGAAARARALELLERVGIPDPERRLDAyph 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 460 ELPLGYKQR----LALACslmhEPDILFLDEPTSGVDPLTRREFWLHINSMVDK-GVTVMVTTHfmD---EAEYCDRIGL 531
Cdd:COG4172 156 QLSGGQRQRvmiaMALAN----EPDLLIADEPTTALDVTVQAQILDLLKDLQRElGMALLLITH--DlgvVRRFADRVAV 229
|
250
....*....|....*
gi 488984955 532 VYHGKLIASGTPDAL 546
Cdd:COG4172 230 MRQGEIVEQGPTAEL 244
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
330-492 |
1.45e-07 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 53.69 E-value: 1.45e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 330 IEAQSLTKKF-GDFAATDHVDFQVKRGEIFGLLGPNGAGKSTTFKMMCGLLVPTSGKaLVLGmDLKVSSGKARQHLGYMA 408
Cdd:PRK11650 4 LKLQAVRKSYdGKTQVIKGIDLDVADGEFIVLVGPSGCGKSTLLRMVAGLERITSGE-IWIG-GRVVNELEPADRDIAMV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 409 -QKFSLYGNLSVEQNLrffsgVYGLrgraqneKIARMSDAfglkSIAR---HAADELPL-------------GYKQRLAL 471
Cdd:PRK11650 82 fQNYALYPHMSVRENM-----AYGL-------KIRGMPKA----EIEErvaEAARILELeplldrkprelsgGQRQRVAM 145
|
170 180
....*....|....*....|.
gi 488984955 472 ACSLMHEPDILFLDEPTSGVD 492
Cdd:PRK11650 146 GRAIVREPAVFLFDEPLSNLD 166
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
329-377 |
1.49e-07 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 54.03 E-value: 1.49e-07
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 488984955 329 VIEAQSLTKKFGDFAATDHVDFQVKRGEIFGLLGPNGAGKSTTFKMMCG 377
Cdd:NF040905 1 ILEMRGITKTFPGVKALDDVNLSVREGEIHALCGENGAGKSTLMKVLSG 49
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
352-518 |
1.70e-07 |
|
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: 51.86 E-value: 1.70e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 352 VKRGEIFGLLGPNGAGKSTTFKMMC-----GLlvpTSGKALVLGMDLKVSsgkARQHLGYMAQKFSLYGNLSVEQNLRFf 426
Cdd:cd03232 30 VKPGTLTALMGESGAGKTTLLDVLAgrktaGV---ITGEILINGRPLDKN---FQRSTGYVEQQDVHSPNLTVREALRF- 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 427 SGVygLRGraqnekiarmsdafglksiarhaadeLPLGYKQRLALACSLMHEPDILFLDEPTSGVDPLTRREFWLHINSM 506
Cdd:cd03232 103 SAL--LRG--------------------------LSVEQRKRLTIGVELAAKPSILFLDEPTSGLDSQAAYNIVRFLKKL 154
|
170
....*....|..
gi 488984955 507 VDKGVTVMVTTH 518
Cdd:cd03232 155 ADSGQAILCTIH 166
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
6-184 |
2.24e-07 |
|
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: 51.00 E-value: 2.24e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 6 IALNGLSRRFPGmDRPAVAPLTCTIRAG---YVTGlvgPDGAGKTTLMRMLAGLLKPDEGRasvIGFdPLKDDSAlhavl 82
Cdd:cd03223 1 IELENLSLATPD-GRVLLKDLSFEIKPGdrlLITG---PSGTGKSSLFRALAGLWPWGSGR---IGM-PEGEDLL----- 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 83 gYMPQKfGLYEDLTVMENLtLYadlrsvtgearkkifdrlleftslgPFTERlagkLSGGMKQKLGLACTLVGDPKVLLL 162
Cdd:cd03223 68 -FLPQR-PYLPLGTLREQL-IY-------------------------PWDDV----LSGGEQQRLAFARLLLHKPKFVFL 115
|
170 180
....*....|....*....|..
gi 488984955 163 DEPGVGVDPISRRELWQMVHEL 184
Cdd:cd03223 116 DEATSALDEESEDRLYQLLKEL 137
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
14-226 |
3.03e-07 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 53.18 E-value: 3.03e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 14 RFPGMDRPAVAPLTCTIRAGYVTGLVGPDGAGKTTLMRMLAGLLKPDEG--RASVIGFDPLKDDS--ALHAVLGYMPqkF 89
Cdd:PRK10789 322 TYPQTDHPALENVNFTLKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGdiRFHDIPLTKLQLDSwrSRLAVVSQTP--F 399
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 90 gLYEDlTVMENLTL---YADLRSVTGEAR-KKIFDRLLEF-----TSLGpftERlAGKLSGGMKQKLGLACTLVGDPKVL 160
Cdd:PRK10789 400 -LFSD-TVANNIALgrpDATQQEIEHVARlASVHDDILRLpqgydTEVG---ER-GVMLSGGQKQRISIARALLLNAEIL 473
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 488984955 161 LLDEPGVGVDpiSRRElWQMVHELA--GDGMLILWSTSYLDEAEQCRDVLLMNEGKLLYQGEPTALTQ 226
Cdd:PRK10789 474 ILDDALSAVD--GRTE-HQILHNLRqwGEGRTVIISAHRLSALTEASEILVMQHGHIAQRGNHDQLAQ 538
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
354-518 |
3.13e-07 |
|
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a variety of cellular activities. This profile/alignment only detects a fraction of this vast family. The poorly conserved N-terminal helix is missing from the alignment.
Pssm-ID: 214640 [Multi-domain] Cd Length: 148 Bit Score: 50.06 E-value: 3.13e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 354 RGEIFGLLGPNGAGKSTTFKMMCGLLVPTSGKALVLGMDlkvssgkarqhlgymaqkFSLYGNLSVEQNLRFFSGVYGLR 433
Cdd:smart00382 1 PGEVILIVGPPGSGKTTLARALARELGPPGGGVIYIDGE------------------DILEEVLDQLLLIIVGGKKASGS 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 434 GRAQNEKIarmsdafglksiarhaadelplgykqrLALACSlmHEPDILFLDEPTSGVDPLTRREFWLHINSMVDK---- 509
Cdd:smart00382 63 GELRLRLA---------------------------LALARK--LKPDVLILDEITSLLDAEQEALLLLLEELRLLLllks 113
|
170
....*....|.
gi 488984955 510 --GVTVMVTTH 518
Cdd:smart00382 114 ekNLTVILTTN 124
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
37-492 |
3.75e-07 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 52.97 E-value: 3.75e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 37 GLVGPDGAGKTTLMRMLAGLLKPDEGRASVigfDPlkddsalHAVLGYMPQ-KFGlYEDLTVM---------------EN 100
Cdd:PRK15064 31 GLIGANGCGKSTFMKILGGDLEPSAGNVSL---DP-------NERLGKLRQdQFA-FEEFTVLdtvimghtelwevkqER 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 101 LTLYAdLRSVTGEARKKIFDRLLEFTSLGPFT-ERLAGKL-----------SGGMKQ-----KLG--LACTLVGDPKVLL 161
Cdd:PRK15064 100 DRIYA-LPEMSEEDGMKVADLEVKFAEMDGYTaEARAGELllgvgipeeqhYGLMSEvapgwKLRvlLAQALFSNPDILL 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 162 LDEPGVGVDPISRRELWQMVHELAGDGMLILWSTSYLDEAeqCRDVLLMNEGKL-LYQGEPTaltqtmagrSFLVSSPQE 240
Cdd:PRK15064 179 LDEPTNNLDINTIRWLEDVLNERNSTMIIISHDRHFLNSV--CTHMADLDYGELrVYPGNYD---------EYMTAATQA 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 241 NNRRLLQRAlklpqvsdgviqgksvrlilKKDARIEEVQQH------------------GDMPPLQVADTAP-------- 294
Cdd:PRK15064 248 RERLLADNA--------------------KKKAQIAELQSFvsrfsanaskakqatsraKQIDKIKLEEVKPssrqnpfi 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 295 RFEDafidllggagtaesplGAIIHRvdgskeeTVIEAQSLTKKFGDFAATDHVDFQVKRGEIFGLLGPNGAGKSTTFKM 374
Cdd:PRK15064 308 RFEQ----------------DKKLHR-------NALEVENLTKGFDNGPLFKNLNLLLEAGERLAIIGENGVGKTTLLRT 364
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 375 MCGLLVPTSGKalvlgmdLKVSSgKARqhLGYMAQKFSLYgnlsVEQNLRFFSGVYGLRGRAQNEK-----IARMsdAFG 449
Cdd:PRK15064 365 LVGELEPDSGT-------VKWSE-NAN--IGYYAQDHAYD----FENDLTLFDWMSQWRQEGDDEQavrgtLGRL--LFS 428
|
490 500 510 520
....*....|....*....|....*....|....*....|...
gi 488984955 450 LKSIaRHAADELPLGYKQRLALACSLMHEPDILFLDEPTSGVD 492
Cdd:PRK15064 429 QDDI-KKSVKVLSGGEKGRMLFGKLMMQKPNVLVMDEPTNHMD 470
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
339-492 |
3.81e-07 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 53.03 E-value: 3.81e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 339 FGDFAATDHVDFQVKRGEIFGLLGPNGAGKSTTFKMMCGLLVPTSGKaLVLGMDLKVSsgKARQH--------------- 403
Cdd:PRK11147 13 FSDAPLLDNAELHIEDNERVCLVGRNGAGKSTLMKILNGEVLLDDGR-IIYEQDLIVA--RLQQDpprnvegtvydfvae 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 404 -LGYMAQKFSLYGNLSV-------EQNLRFFSgvyglrgRAQnEKI---------ARMSDAFGLKSIARHAA-DELPLGY 465
Cdd:PRK11147 90 gIEEQAEYLKRYHDISHlvetdpsEKNLNELA-------KLQ-EQLdhhnlwqleNRINEVLAQLGLDPDAAlSSLSGGW 161
|
170 180
....*....|....*....|....*..
gi 488984955 466 KQRLALACSLMHEPDILFLDEPTSGVD 492
Cdd:PRK11147 162 LRKAALGRALVSNPDVLLLDEPTNHLD 188
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
19-226 |
4.42e-07 |
|
multi drug resistance-associated protein (MRP); This model describes multi drug resistance-associated protein (MRP) in eukaryotes. The multidrug resistance-associated protein is an integral membrane protein that causes multidrug resistance when overexpressed in mammalian cells. It belongs to ABC transporter superfamily. The protein topology and function was experimentally demonstrated by epitope tagging and immunofluorescence. Insertion of tags in the critical regions associated with drug efflux, abrogated its function. The C-terminal domain seem to highly conserved. [Transport and binding proteins, Other]
Pssm-ID: 188098 [Multi-domain] Cd Length: 1522 Bit Score: 53.03 E-value: 4.42e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 19 DRPAVAPLTCTIRAGYVTGLVGPDGAGKTTLMRMLAGLLKPDEGRASVIGfdplkddsalhaVLGYMPQKFGLYEDlTVM 98
Cdd:TIGR00957 650 LPPTLNGITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVHMKG------------SVAYVPQQAWIQND-SLR 716
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 99 ENLTLYADLRsvtgearKKIFDRLLEFTSLGPFTERLAG-----------KLSGGMKQKLGLACTLVGDPKVLLLDEPGV 167
Cdd:TIGR00957 717 ENILFGKALN-------EKYYQQVLEACALLPDLEILPSgdrteigekgvNLSGGQKQRVSLARAVYSNADIYLFDDPLS 789
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 488984955 168 GVDPISRRELWQmvHELAGDGM-------LILWSTSYLdeaEQCRDVLLMNEGKLLYQGEPTALTQ 226
Cdd:TIGR00957 790 AVDAHVGKHIFE--HVIGPEGVlknktriLVTHGISYL---PQVDVIIVMSGGKISEMGSYQELLQ 850
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
322-574 |
5.38e-07 |
|
multi drug resistance-associated protein (MRP); This model describes multi drug resistance-associated protein (MRP) in eukaryotes. The multidrug resistance-associated protein is an integral membrane protein that causes multidrug resistance when overexpressed in mammalian cells. It belongs to ABC transporter superfamily. The protein topology and function was experimentally demonstrated by epitope tagging and immunofluorescence. Insertion of tags in the critical regions associated with drug efflux, abrogated its function. The C-terminal domain seem to highly conserved. [Transport and binding proteins, Other]
Pssm-ID: 188098 [Multi-domain] Cd Length: 1522 Bit Score: 53.03 E-value: 5.38e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 322 DGSKEETVIEAQSLTKKFGDFAATDHVDFQVKRGEIFGLLGPNGAGKSTTFKMMCGLLVPTSGKALVLGmdlkvssgkar 401
Cdd:TIGR00957 631 PGEGNSITVHNATFTWARDLPPTLNGITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVHMKG----------- 699
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 402 qHLGYMAQKfSLYGNLSVEQNLRFFSGVYGLRGRAQNEKIARMSDAFGLKSIARHAADE----LPLGYKQRLALACSLMH 477
Cdd:TIGR00957 700 -SVAYVPQQ-AWIQNDSLRENILFGKALNEKYYQQVLEACALLPDLEILPSGDRTEIGEkgvnLSGGQKQRVSLARAVYS 777
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 478 EPDILFLDEPTSGVDPLTRREFWLH-INSM-VDKGVTVMVTTHFMDEAEYCDRIGLVYHGKLIASGTPDALKAQ------ 549
Cdd:TIGR00957 778 NADIYLFDDPLSAVDAHVGKHIFEHvIGPEgVLKNKTRILVTHGISYLPQVDVIIVMSGGKISEMGSYQELLQRdgafae 857
|
250 260 270
....*....|....*....|....*....|
gi 488984955 550 -----AADDSQTDptMEQAFITLINRWDKE 574
Cdd:TIGR00957 858 flrtyAPDEQQGH--LEDSWTALVSGEGKE 885
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
346-518 |
5.64e-07 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 52.80 E-value: 5.64e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 346 DHVDFQVKRGEIFGLLGPNGAGKSTTFKMMCGLL---VPTSGKALVLGMDLKVSSGKArqhLGYMAQKFSLYGNLSVEQN 422
Cdd:TIGR00956 780 NNVDGWVKPGTLTALMGASGAGKTTLLNVLAERVttgVITGGDRLVNGRPLDSSFQRS---IGYVQQQDLHLPTSTVRES 856
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 423 LRFFSGvygLRGRAQNEKIARMS------DAFGLKSIARH----AADELPLGYKQRLALACSLMHEPD-ILFLDEPTSGV 491
Cdd:TIGR00956 857 LRFSAY---LRQPKSVSKSEKMEyveeviKLLEMESYADAvvgvPGEGLNVEQRKRLTIGVELVAKPKlLLFLDEPTSGL 933
|
170 180
....*....|....*....|....*..
gi 488984955 492 DPLTRREFWLHINSMVDKGVTVMVTTH 518
Cdd:TIGR00956 934 DSQTAWSICKLMRKLADHGQAILCTIH 960
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
333-492 |
6.15e-07 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 51.23 E-value: 6.15e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 333 QSLTKKFGDFAATDHVDFQVKRGEIFGLLGPNGAGKSTTFKMMCGLLVPTSGKALVLGMDLKVSSGKARQ---------- 402
Cdd:PRK10419 16 GGLSGKHQHQTVLNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWRGEPLAKLNRAQRKafrrdiqmvf 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 403 --HLGYMAQKFSLygNLSVEQNLRFFSgvyGLRGRAQNEKIARMSDAFGLK-SIARHAADELPLGYKQRLALACSLMHEP 479
Cdd:PRK10419 96 qdSISAVNPRKTV--REIIREPLRHLL---SLDKAERLARASEMLRAVDLDdSVLDKRPPQLSGGQLQRVCLARALAVEP 170
|
170
....*....|...
gi 488984955 480 DILFLDEPTSGVD 492
Cdd:PRK10419 171 KLLILDEAVSNLD 183
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
349-550 |
6.55e-07 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 51.94 E-value: 6.55e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 349 DFQVKRGEIFGLLGPNGAGKSTTFKMMCGLLVPTSGKalvlgmdlkvssgkaRQHlgymaqKFSLYGNLSVEQ------- 421
Cdd:PRK10938 23 SLTLNAGDSWAFVGANGSGKSALARALAGELPLLSGE---------------RQS------QFSHITRLSFEQlqklvsd 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 422 -----NLRFFSGVYGLRGRAQNEKI----------ARMSDAFGLKSIARHAADELPLGYKQRLALACSLMHEPDILFLDE 486
Cdd:PRK10938 82 ewqrnNTDMLSPGEDDTGRTTAEIIqdevkdparcEQLAQQFGITALLDRRFKYLSTGETRKTLLCQALMSEPDLLILDE 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 488984955 487 PTSGVDPLTRREFWLHINSMVDKGVT-VMVTTHFMDEAEYCDRIGLVYHGKLIASGTPDALKAQA 550
Cdd:PRK10938 162 PFDGLDVASRQQLAELLASLHQSGITlVLVLNRFDEIPDFVQFAGVLADCTLAETGEREEILQQA 226
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
35-184 |
1.47e-06 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 50.04 E-value: 1.47e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 35 VTGLVGPDGAGKTTLMRMLAGLLKPD-----EGRASVIG---FDPLKDDSALHAVLGYMPQKFGLYEdLTVMENLTLYAD 106
Cdd:PRK14258 35 VTAIIGPSGCGKSTFLKCLNRMNELEsevrvEGRVEFFNqniYERRVNLNRLRRQVSMVHPKPNLFP-MSVYDNVAYGVK 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 107 LrsvTGEARKKIFDRLLE--------FTSLGPFTERLAGKLSGGMKQKLGLACTLVGDPKVLLLDEPGVGVDPISRRELW 178
Cdd:PRK14258 114 I---VGWRPKLEIDDIVEsalkdadlWDEIKHKIHKSALDLSGGQQQRLCIARALAVKPKVLLMDEPCFGLDPIASMKVE 190
|
....*.
gi 488984955 179 QMVHEL 184
Cdd:PRK14258 191 SLIQSL 196
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
18-227 |
1.96e-06 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 51.13 E-value: 1.96e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 18 MDRPAVAPLTCTIRAGYVTGLVGPDGAGKTTLMRMLAGLLKPDEGRASVIgfdplkddsalHAVLGYMPQKFGLYeDLTV 97
Cdd:PLN03232 628 TSKPTLSDINLEIPVGSLVAIVGGTGEGKTSLISAMLGELSHAETSSVVI-----------RGSVAYVPQVSWIF-NATV 695
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 98 MENLTLYADLRSvtgearkKIFDRLLEFTSLGPFTERLAGK-----------LSGGMKQKLGLACTLVGDPKVLLLDEPG 166
Cdd:PLN03232 696 RENILFGSDFES-------ERYWRAIDVTALQHDLDLLPGRdlteigergvnISGGQKQRVSMARAVYSNSDIYIFDDPL 768
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 488984955 167 VGVDPISRRELWQ--MVHELAGDGMLILwsTSYLDEAEQCRDVLLMNEGKLLYQGEPTALTQT 227
Cdd:PLN03232 769 SALDAHVAHQVFDscMKDELKGKTRVLV--TNQLHFLPLMDRIILVSEGMIKEEGTFAELSKS 829
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
30-170 |
1.97e-06 |
|
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI's are not transport proteins, and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLI's have an N-terminal Fe-S domain and two nucleotide-binding domains, which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213189 [Multi-domain] Cd Length: 177 Bit Score: 48.34 E-value: 1.97e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 30 IRAGYVTGLVGPDGAGKTTLMRMLAGLLKPDEGRASVIGFDPLkddsalhavlgYMPQKFglyedltvmenltlyadlrs 109
Cdd:cd03222 22 VKEGEVIGIVGPNGTGKTTAVKILAGQLIPNGDNDEWDGITPV-----------YKPQYI-------------------- 70
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 488984955 110 vtgearkkifdrlleftslgpfterlagKLSGGMKQKLGLACTLVGDPKVLLLDEPGVGVD 170
Cdd:cd03222 71 ----------------------------DLSGGELQRVAIAAALLRNATFYLFDEPSAYLD 103
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
338-501 |
2.07e-06 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 50.66 E-value: 2.07e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 338 KFGDfaatdhvdfqvkrGEIFGLLGPNGAGKSTTFKMMCGLLVPTSGKalvLGMDLKVSSGKARQ-HLGY---------- 406
Cdd:PRK15064 23 KFGG-------------GNRYGLIGANGCGKSTFMKILGGDLEPSAGN---VSLDPNERLGKLRQdQFAFeeftvldtvi 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 407 ---------MAQKFSLYGN--LSVEQNLRffsgVYGLRGraqneKIARMSdafGLKSIARhaADELPL------------ 463
Cdd:PRK15064 87 mghtelwevKQERDRIYALpeMSEEDGMK----VADLEV-----KFAEMD---GYTAEAR--AGELLLgvgipeeqhygl 152
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 488984955 464 ------GYKQRLALACSLMHEPDILFLDEPTSGVDPLTRRefWL 501
Cdd:PRK15064 153 msevapGWKLRVLLAQALFSNPDILLLDEPTNNLDINTIR--WL 194
|
|
| PRK13541 |
PRK13541 |
cytochrome c biogenesis protein CcmA; Provisional |
362-518 |
2.42e-06 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184128 [Multi-domain] Cd Length: 195 Bit Score: 48.33 E-value: 2.42e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 362 GPNGAGKSTTFKMMCGLLVPTSGKALVLGMDLkvsSGKARQHLGYMAQKFSLYGNLSVEQNLRFFSGVYGlrgraQNEKI 441
Cdd:PRK13541 33 GANGCGKSSLLRMIAGIMQPSSGNIYYKNCNI---NNIAKPYCTYIGHNLGLKLEMTVFENLKFWSEIYN-----SAETL 104
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 488984955 442 ARMSDAFGLKSIARHAADELPLGYKQRLALACSLMHEPDILFLDEPTSGVDPLTRREFWLHINSMVDKGVTVMVTTH 518
Cdd:PRK13541 105 YAAIHYFKLHDLLDEKCYSLSSGMQKIVAIARLIACQSDLWLLDEVETNLSKENRDLLNNLIVMKANSGGIVLLSSH 181
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
3-215 |
2.80e-06 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 50.11 E-value: 2.80e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 3 ETVIALNGLSrrfpGMDRPAVAPLTCTIRAGYVTGLVGPDGAGKTTLMRMLAGLLKPDEGRASVIGfDPLKDDSALHAVL 82
Cdd:PRK10982 248 EVILEVRNLT----SLRQPSIRDVSFDLHKGEILGIAGLVGAKRTDIVETLFGIREKSAGTITLHG-KKINNHNANEAIN 322
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 83 -GYM-----PQKFGLYEDLTVMENlTLYADLRSVTGE------ARKK-----IFDRLLEFTslgPFTERLAGKLSGGMKQ 145
Cdd:PRK10982 323 hGFAlvteeRRSTGIYAYLDIGFN-SLISNIRNYKNKvglldnSRMKsdtqwVIDSMRVKT---PGHRTQIGSLSGGNQQ 398
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 488984955 146 KLGLACTLVGDPKVLLLDEPGVGVDPISRRELWQMVHELAGDGMLILWSTSYLDEAEQCRD-VLLMNEGKL 215
Cdd:PRK10982 399 KVIIGRWLLTQPEILMLDEPTRGIDVGAKFEIYQLIAELAKKDKGIIIISSEMPELLGITDrILVMSNGLV 469
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
344-492 |
2.83e-06 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 49.70 E-value: 2.83e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 344 ATDHVDFQVKRGEIFGLLGPNGAGKSTTFKMMCGLLVPTSGKALVLGMDLKVSSGK----ARQHLGYMAQK--FSLYGNL 417
Cdd:PRK15079 36 AVDGVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGEVAWLGKDLLGMKDDewraVRSDIQMIFQDplASLNPRM 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 418 SV----EQNLRFFsgvYGLRGRAQ-NEKIARMSDAFGL--KSIARHaADELPLGYKQRLALACSLMHEPDILFLDEPTSG 490
Cdd:PRK15079 116 TIgeiiAEPLRTY---HPKLSRQEvKDRVKAMMLKVGLlpNLINRY-PHEFSGGQCQRIGIARALILEPKLIICDEPVSA 191
|
..
gi 488984955 491 VD 492
Cdd:PRK15079 192 LD 193
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
29-221 |
2.94e-06 |
|
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: 48.29 E-value: 2.94e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 29 TIRAGYVTGLVGPDGAGKTTLMRMLAGLLKPDEGRASVIgfdpLKDdsalhavlgympqkfglyEDLTVMEnltlyadlr 108
Cdd:cd03217 22 TIKKGEVHALMGPNGSGKSTLAKTIMGHPKYEVTEGEIL----FKG------------------EDITDLP--------- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 109 sVTGEARKKI---FDRLLEFT--SLGPFTERLAGKLSGGMKQKLGLACTLVGDPKVLLLDEPGVGVDPISRRELWQMVHE 183
Cdd:cd03217 71 -PEERARLGIflaFQYPPEIPgvKNADFLRYVNEGFSGGEKKRNEILQLLLLEPDLAILDEPDSGLDIDALRLVAEVINK 149
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 488984955 184 LAGDGMLILWSTSYLDEAEQCRD--VLLMNEGKLLYQGEP 221
Cdd:cd03217 150 LREEGKSVLIITHYQRLLDYIKPdrVHVLYDGRIVKSGDK 189
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
26-215 |
4.37e-06 |
|
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: 48.70 E-value: 4.37e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 26 LTCTIRAGYVTGLVGPDGAGKTTLMRMLAGLLKPdEGRASVIGFD----PLKDdsaLHAVLGYMPQKFGLYEDlTVMENL 101
Cdd:cd03289 23 ISFSISPGQRVGLLGRTGSGKSTLLSAFLRLLNT-EGDIQIDGVSwnsvPLQK---WRKAFGVIPQKVFIFSG-TFRKNL 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 102 TLYadlrsvtGEARKKIFDRLLEFTSLGPFTERLAGKL-----------SGGMKQKLGLACTLVGDPKVLLLDEPGVGVD 170
Cdd:cd03289 98 DPY-------GKWSDEEIWKVAEEVGLKSVIEQFPGQLdfvlvdggcvlSHGHKQLMCLARSVLSKAKILLLDEPSAHLD 170
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 488984955 171 PISRRELWQMVHELAGDGMLILwSTSYLDEAEQCRDVLLMNEGKL 215
Cdd:cd03289 171 PITYQVIRKTLKQAFADCTVIL-SEHRIEAMLECQRFLVIEENKV 214
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
26-221 |
4.61e-06 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 48.67 E-value: 4.61e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 26 LTCTIRAGYVTGLVGPDGAGKTTLMRMLAGLL--KPDEGRASVIG-----FDPLKDDSA-----LHAVLGYMPQK-FGLY 92
Cdd:PRK13547 20 LSLRIEPGRVTALLGRNGAGKSTLLKALAGDLtgGGAPRGARVTGdvtlnGEPLAAIDAprlarLRAVLPQAAQPaFAFS 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 93 EDLTVMENLTLYADLRSVTGEARKKIFDRLLEFTSLGPFTERLAGKLSGGMKQKLGLACTL---------VGDPKVLLLD 163
Cdd:PRK13547 100 AREIVLLGRYPHARRAGALTHRDGEIAWQALALAGATALVGRDVTTLSGGELARVQFARVLaqlwpphdaAQPPRYLLLD 179
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 488984955 164 EPGVGVDPISRRELWQMVHELAGD---GMLILWSTSYLdEAEQCRDVLLMNEGKLLYQGEP 221
Cdd:PRK13547 180 EPTAALDLAHQHRLLDTVRRLARDwnlGVLAIVHDPNL-AARHADRIAMLADGAIVAHGAP 239
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
22-165 |
5.40e-06 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 48.55 E-value: 5.40e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 22 AVAPLTCTIRAGYVTGLVGPDGAGKTTLMRMLAGLLKPDEGRASVIGFDPLK-DDSALHAVLGYMPQKF-----GLYEDL 95
Cdd:PRK15079 36 AVDGVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGEVAWLGKDLLGmKDDEWRAVRSDIQMIFqdplaSLNPRM 115
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 488984955 96 TVMENL-----TLYADLRSvtGEARKKIFDRLLEFTSLGPFTERLAGKLSGGMKQKLGLACTLVGDPKVLLLDEP 165
Cdd:PRK15079 116 TIGEIIaeplrTYHPKLSR--QEVKDRVKAMMLKVGLLPNLINRYPHEFSGGQCQRIGIARALILEPKLIICDEP 188
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
348-541 |
6.47e-06 |
|
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins, and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213205 [Multi-domain] Cd Length: 176 Bit Score: 46.93 E-value: 6.47e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 348 VDFQVKRGEIFGLLGPNGAGKSTtfkmmcglLVPTSGKAlvlgmdlkvsSGKARqhLGYMAQKFSLYGNLSVEQnLRFFS 427
Cdd:cd03238 14 LDVSIPLNVLVVVTGVSGSGKST--------LVNEGLYA----------SGKAR--LISFLPKFSRNKLIFIDQ-LQFLI 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 428 GVyGLrgraqnekiarmsdafGLKSIARhAADELPLGYKQRLALACSL-MHEPDILF-LDEPTSGVDPLTRREFWLHINS 505
Cdd:cd03238 73 DV-GL----------------GYLTLGQ-KLSTLSGGELQRVKLASELfSEPPGTLFiLDEPSTGLHQQDINQLLEVIKG 134
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 488984955 506 MVDKGVTVMVTTH---FMDEAEYCDRIGL---VYHGKLIASG 541
Cdd:cd03238 135 LIDLGNTVILIEHnldVLSSADWIIDFGPgsgKSGGKVVFSG 176
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
303-529 |
7.20e-06 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 49.26 E-value: 7.20e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 303 LLGGAGTAESPLGAIIHRVDGSKEETVI----EAQSLTKKFGDFAATDHVDFQVKRGEIFGLLGPNGAGKSTTfkmmcgl 378
Cdd:PTZ00265 1199 IVGETGSGKSTVMSLLMRFYDLKNDHHIvfknEHTNDMTNEQDYQGDEEQNVGMKNVNEFSLTKEGGSGEDST------- 1271
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 379 LVPTSGKALVLGMDLKVSSGKARQHLGYMAQKFSLYGNLSVEQNLRFFsgvyglRGRAQNEKIARMS-----DAFgLKSI 453
Cdd:PTZ00265 1272 VFKNSGKILLDGVDICDYNLKDLRNLFSIVSQEPMLFNMSIYENIKFG------KEDATREDVKRACkfaaiDEF-IESL 1344
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 454 ARHA-------ADELPLGYKQRLALACSLMHEPDILFLDEPTSGVDPLTRREFWLHINSMVDKG-VTVMVTTHFMDEAEY 525
Cdd:PTZ00265 1345 PNKYdtnvgpyGKSLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDIKDKAdKTIITIAHRIASIKR 1424
|
....
gi 488984955 526 CDRI 529
Cdd:PTZ00265 1425 SDKI 1428
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
22-215 |
8.82e-06 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 48.43 E-value: 8.82e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 22 AVAPLTCTIRAGYVTGLVGPDGAGKTTLMRMLAGLLKPDEGrasvigfDPLKDDSALHAvlgympQKFGLYEDL--TVME 99
Cdd:PRK10522 338 SVGPINLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSG-------EILLDGKPVTA------EQPEDYRKLfsAVFT 404
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 100 NLTLYADLRSVTG-EARKKIFDRLLEFTSLGPFTE----RLAG-KLSGGMKQKLGLACTLVGDPKVLLLDEPGVGVDPIS 173
Cdd:PRK10522 405 DFHLFDQLLGPEGkPANPALVEKWLERLKMAHKLEledgRISNlKLSKGQKKRLALLLALAEERDILLLDEWAADQDPHF 484
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 488984955 174 RRELWQM-VHELAGDGMLILWST---SYLDEAEQcrdVLLMNEGKL 215
Cdd:PRK10522 485 RREFYQVlLPLLQEMGKTIFAIShddHYFIHADR---LLEMRNGQL 527
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
38-165 |
1.15e-05 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 48.41 E-value: 1.15e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 38 LVGPDGAGKTTLMRMLAGLLKPDEGRA------SVIGFDPLKDDsalhavlgympqkfgLYEDLTVMENLtlyADLRS-- 109
Cdd:PRK11147 350 LIGPNGCGKTTLLKLMLGQLQADSGRIhcgtklEVAYFDQHRAE---------------LDPEKTVMDNL---AEGKQev 411
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 488984955 110 -VTGEARkKIFDRLLEFTsLGPFTERLAGK-LSGGMKQKLGLACTLVGDPKVLLLDEP 165
Cdd:PRK11147 412 mVNGRPR-HVLGYLQDFL-FHPKRAMTPVKaLSGGERNRLLLARLFLKPSNLLILDEP 467
|
|
| ABC_UvrA_II |
cd03271 |
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair ... |
416-543 |
1.15e-05 |
|
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213238 [Multi-domain] Cd Length: 261 Bit Score: 47.22 E-value: 1.15e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 416 NLSVEQNLRFFSGVYGLRgraqnEKIARMSDAfGLKSIAR-HAADELPLGYKQRLALACSLmHEPD----ILFLDEPTSG 490
Cdd:cd03271 130 DMTVEEALEFFENIPKIA-----RKLQTLCDV-GLGYIKLgQPATTLSGGEAQRIKLAKEL-SKRStgktLYILDEPTTG 202
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 488984955 491 VDPLTRREFWLHINSMVDKGVTVMVTTHFMDEAEYCDRI------GLVYHGKLIASGTP 543
Cdd:cd03271 203 LHFHDVKKLLEVLQRLVDKGNTVVVIEHNLDVIKCADWIidlgpeGGDGGGQVVASGTP 261
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
33-190 |
1.47e-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: 1.47e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 33 GYVTGLVGPDGAGKTTLMRMLAGLLKPDEGRASVIGfdplkddsalhavlgympqkfglyedltvMENLTLYADLRsvtg 112
Cdd:smart00382 2 GEVILIVGPPGSGKTTLARALARELGPPGGGVIYID-----------------------------GEDILEEVLDQ---- 48
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 488984955 113 earkkifdrlleftSLGPFTERLAGKLSGGMKQKLGLACTLVGDPKVLLLDEPGVGVDPISRRELWQMVHELAGDGML 190
Cdd:smart00382 49 --------------LLLIIVGGKKASGSGELRLRLALALARKLKPDVLILDEITSLLDAEQEALLLLLEELRLLLLLK 112
|
|
| AAA_21 |
pfam13304 |
AAA domain, putative AbiEii toxin, Type IV TA system; Several members are annotated as being ... |
423-518 |
1.57e-05 |
|
AAA domain, putative AbiEii toxin, Type IV TA system; Several members are annotated as being of the abortive phage resistance system, in which case the family would be acting as the toxin for a type IV toxin-antitoxin resistance system.
Pssm-ID: 433102 [Multi-domain] Cd Length: 303 Bit Score: 47.00 E-value: 1.57e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 423 LRFFSGVYGLRGRAQNEKIARMSDafGLKSIARHAAdelplgykqrlALAcSLMHEPDILFLDEPTSGVDPLTRREFWLH 502
Cdd:pfam13304 216 LRERGLILLENGGGGELPAFELSD--GTKRLLALLA-----------ALL-SALPKGGLLLIDEPESGLHPKLLRRLLEL 281
|
90
....*....|....*.
gi 488984955 503 INSMVDKGVTVMVTTH 518
Cdd:pfam13304 282 LKELSRNGAQLILTTH 297
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
20-224 |
1.58e-05 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 48.05 E-value: 1.58e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 20 RPAVAP----LTCTIRAGYVTGLVGPDGAGKTTLMRMLAGLLKPDEGRASVIGFDPLKDD-SALHAVLGYMPQKFGLYED 94
Cdd:PLN03232 1245 RPGLPPvlhgLSFFVSPSEKVGVVGRTGAGKSSMLNALFRIVELEKGRIMIDDCDVAKFGlTDLRRVLSIIPQSPVLFSG 1324
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 95 lTVMENLTLY-----ADLRSVTGEAR-KKIFDRllefTSLGPFTERLAG--KLSGGMKQKLGLACTLVGDPKVLLLDEPG 166
Cdd:PLN03232 1325 -TVRFNIDPFsehndADLWEALERAHiKDVIDR----NPFGLDAEVSEGgeNFSVGQRQLLSLARALLRRSKILVLDEAT 1399
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 167 VGVDpISRRELWQ--MVHELAGDGMLILwsTSYLDEAEQCRDVLLMNEGKLLYQGEPTAL 224
Cdd:PLN03232 1400 ASVD-VRTDSLIQrtIREEFKSCTMLVI--AHRLNTIIDCDKILVLSSGQVLEYDSPQEL 1456
|
|
| nickel_nikD |
TIGR02770 |
nickel import ATP-binding protein NikD; This family represents the NikD subunit of a ... |
22-227 |
1.58e-05 |
|
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: 46.59 E-value: 1.58e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 22 AVAPLTCTIRAGYVTGLVGPDGAGKTTLMRMLAGLLKPD--EGRASVigfdpLKDDSALHAvLGYMPQKFGlyedlTVME 99
Cdd:TIGR02770 1 LVQDLNLSLKRGEVLALVGESGSGKSLTCLAILGLLPPGltQTSGEI-----LLDGRPLLP-LSIRGRHIA-----TIMQ 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 100 N-LTLYADLRSVTGEAR----------KKIFDRLLE-FTSLG-PFTERLAGK----LSGGMKQKLGLACTLVGDPKVLLL 162
Cdd:TIGR02770 70 NpRTAFNPLFTMGNHAIetlrslgklsKQARALILEaLEAVGlPDPEEVLKKypfqLSGGMLQRVMIALALLLEPPFLIA 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 488984955 163 DEPGVGVDPISRRELWQMVHELAGD-GMLILWSTSYLDEAEQCRD-VLLMNEGKLLYQGEPTALTQT 227
Cdd:TIGR02770 150 DEPTTDLDVVNQARVLKLLRELRQLfGTGILLITHDLGVVARIADeVAVMDDGRIVERGTVKEIFYN 216
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
6-170 |
2.44e-05 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 47.02 E-value: 2.44e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 6 IALNGLSRRFPGmDRPAVAPLTCTIRAGYVTGLVGPDGAGKTTLMRMLAGLLKPDEGRASVIGfDPLKDDSalHAVLGY- 84
Cdd:PRK10790 341 IDIDNVSFAYRD-DNLVLQNINLSVPSRGFVALVGHTGSGKSTLASLLMGYYPLTEGEIRLDG-RPLSSLS--HSVLRQg 416
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 85 --MPQKFGLYEDLTVMENLTLYADLrsvtgeARKKIFdRLLEFTSLGPFTERLAG-----------KLSGGMKQKLGLAC 151
Cdd:PRK10790 417 vaMVQQDPVVLADTFLANVTLGRDI------SEEQVW-QALETVQLAELARSLPDglytplgeqgnNLSVGQKQLLALAR 489
|
170
....*....|....*....
gi 488984955 152 TLVGDPKVLLLDEPGVGVD 170
Cdd:PRK10790 490 VLVQTPQILILDEATANID 508
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
72-175 |
2.64e-05 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 47.33 E-value: 2.64e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 72 LKDDSALHAVLGYMPQKFglyedltvmeNLTLYADLRSVTGEARKKIFDRLLEFTSLGPFTERLAGK-----------LS 140
Cdd:PTZ00265 1291 LKDLRNLFSIVSQEPMLF----------NMSIYENIKFGKEDATREDVKRACKFAAIDEFIESLPNKydtnvgpygksLS 1360
|
90 100 110
....*....|....*....|....*....|....*
gi 488984955 141 GGMKQKLGLACTLVGDPKVLLLDEPGVGVDPISRR 175
Cdd:PTZ00265 1361 GGQKQRIAIARALLREPKILLLDEATSSLDSNSEK 1395
|
|
| PRK15177 |
PRK15177 |
Vi polysaccharide ABC transporter ATP-binding protein VexC; |
346-537 |
2.72e-05 |
|
Vi polysaccharide ABC transporter ATP-binding protein VexC;
Pssm-ID: 185099 [Multi-domain] Cd Length: 213 Bit Score: 45.44 E-value: 2.72e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 346 DHVDFQVKRGEIFGLLGPNGAGKSTTFKMMCGLLVPTSGKALVLGMDLkvssgkarqhLGYMAQKFSLYGnLSVEQNLRF 425
Cdd:PRK15177 4 DKTDFVMGYHEHIGILAAPGSGKTTLTRLLCGLDAPDEGDFIGLRGDA----------LPLGANSFILPG-LTGEENARM 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 426 FSGVYGLRGRAQNEKIARMSDafgLKSIARHAADELPLGYKQRLALACSLMHEPDILFLDEPTSGVDPLTRREFWLHINS 505
Cdd:PRK15177 73 MASLYGLDGDEFSHFCYQLTQ---LEQCYTDRVSEYSVTMKTHLAFAINLLLPCRLYIADGKLYTGDNATQLRMQAALAC 149
|
170 180 190
....*....|....*....|....*....|..
gi 488984955 506 MVDKGVTVMVTTHFMDEAEYCDRIGLVYHGKL 537
Cdd:PRK15177 150 QLQQKGLIVLTHNPRLIKEHCHAFGVLLHGKI 181
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
346-529 |
3.35e-05 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 46.71 E-value: 3.35e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 346 DHVDFQVKRGEIFGLLGPNGAGKsTTFKMMC-----GllVPTSGKALVLGMDLKVSS-GKARQH-LGYMAQKFSLYGnLS 418
Cdd:NF040905 277 DDVSLNVRRGEIVGIAGLMGAGR-TELAMSVfgrsyG--RNISGTVFKDGKEVDVSTvSDAIDAgLAYVTEDRKGYG-LN 352
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 419 VEQNLRFFSGVYGLRGRA------QNE--KIA-RMSDAFGLKSIA-RHAADELPLGYKQRLALACSLMHEPDILFLDEPT 488
Cdd:NF040905 353 LIDDIKRNITLANLGKVSrrgvidENEeiKVAeEYRKKMNIKTPSvFQKVGNLSGGNQQKVVLSKWLFTDPDVLILDEPT 432
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 488984955 489 SGVDPLTRREFWLHINSMVDKGVTVMVTTHFMDEA-EYCDRI 529
Cdd:NF040905 433 RGIDVGAKYEIYTIINELAAEGKGVIVISSELPELlGMCDRI 474
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
20-248 |
5.32e-05 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 46.27 E-value: 5.32e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 20 RPAVAP----LTCTIRAGYVTGLVGPDGAGKTTLMRMLAGLLKPDEGRASVIGFDPLKDDSA-LHAVLGYMPQKFGLYED 94
Cdd:PLN03130 1248 RPELPPvlhgLSFEISPSEKVGIVGRTGAGKSSMLNALFRIVELERGRILIDGCDISKFGLMdLRKVLGIIPQAPVLFSG 1327
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 95 lTVMENLTLY-----ADLRSVTGEAR-KKIFDRllefTSLGPFTERLAG--KLSGGMKQKLGLACTLVGDPKVLLLDEPG 166
Cdd:PLN03130 1328 -TVRFNLDPFnehndADLWESLERAHlKDVIRR----NSLGLDAEVSEAgeNFSVGQRQLLSLARALLRRSKILVLDEAT 1402
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 167 VGVDpISRRELWQ--MVHELAGDGMLILwsTSYLDEAEQCRDVLLMNEGKLLYQGEPTALTQTmAGRSF--LVSSPQENN 242
Cdd:PLN03130 1403 AAVD-VRTDALIQktIREEFKSCTMLII--AHRLNTIIDCDRILVLDAGRVVEFDTPENLLSN-EGSAFskMVQSTGAAN 1478
|
....*.
gi 488984955 243 RRLLQR 248
Cdd:PLN03130 1479 AQYLRS 1484
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
355-518 |
1.04e-04 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 45.61 E-value: 1.04e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 355 GEIFGLLGPNGAGKSTTFKMMCGLlvPTSGkaLVLGmDLKVSSGKARQHL-----GYMAQK--------------FSLYG 415
Cdd:PLN03140 906 GVLTALMGVSGAGKTTLMDVLAGR--KTGG--YIEG-DIRISGFPKKQETfarisGYCEQNdihspqvtvresliYSAFL 980
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 416 NL----SVEQNLRFFSGVYGLrgraqnEKIARMSDAF-GLKSIARHAADElplgyKQRLALACSLMHEPDILFLDEPTSG 490
Cdd:PLN03140 981 RLpkevSKEEKMMFVDEVMEL------VELDNLKDAIvGLPGVTGLSTEQ-----RKRLTIAVELVANPSIIFMDEPTSG 1049
|
170 180
....*....|....*....|....*...
gi 488984955 491 VDPLTRREFWLHINSMVDKGVTVMVTTH 518
Cdd:PLN03140 1050 LDARAAAIVMRTVRNTVDTGRTVVCTIH 1077
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
348-554 |
1.25e-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: 44.08 E-value: 1.25e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 348 VDFQVKRGEIFGLLGPNGAGKSTTFKMMCGLLVPTSGKAlvlgmdlkvssgKARQHLGYMAQkFSLYGNLSVEQNLRFfs 427
Cdd:cd03291 56 INLKIEKGEMLAITGSTGSGKTSLLMLILGELEPSEGKI------------KHSGRISFSSQ-FSWIMPGTIKENIIF-- 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 428 GV----YGLRGRAQ----NEKIARMSDAFglKSIARHAADELPLGYKQRLALACSLMHEPDILFLDEPTSGVDPLTRREF 499
Cdd:cd03291 121 GVsydeYRYKSVVKacqlEEDITKFPEKD--NTVLGEGGITLSGGQRARISLARAVYKDADLYLLDSPFGYLDVFTEKEI 198
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 488984955 500 WLHINSMVDKGVTVMVTTHFMDEAEYCDRIGLVYHGKLIASGTPDALKAQAADDS 554
Cdd:cd03291 199 FESCVCKLMANKTRILVTSKMEHLKKADKILILHEGSSYFYGTFSELQSLRPDFS 253
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
335-542 |
1.64e-04 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 43.96 E-value: 1.64e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 335 LTKKFGD----FAATDHVDFQVKRGEIFGLLGPNGAGKSTTFKMMCGLL-VPTSGKALVL---GMDLKVSSGKARQHL-- 404
Cdd:PRK11022 9 LSVHFGDesapFRAVDRISYSVKQGEVVGIVGESGSGKSVSSLAIMGLIdYPGRVMAEKLefnGQDLQRISEKERRNLvg 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 405 GYMAQKF-----SLygNLSVEQNLRFFSGVYGLRGRAQNEKIARMSDAFGLKSIARHAA------DELPLGYKQRLALAC 473
Cdd:PRK11022 89 AEVAMIFqdpmtSL--NPCYTVGFQIMEAIKVHQGGNKKTRRQRAIDLLNQVGIPDPASrldvypHQLSGGMSQRVMIAM 166
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 488984955 474 SLMHEPDILFLDEPTSGVDPLTRR---EFWLHINSMVDKGVtVMVTTHFMDEAEYCDRIGLVYHGKLIASGT 542
Cdd:PRK11022 167 AIACRPKLLIADEPTTALDVTIQAqiiELLLELQQKENMAL-VLITHDLALVAEAAHKIIVMYAGQVVETGK 237
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
347-548 |
1.74e-04 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 44.73 E-value: 1.74e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 347 HVDFQVKRGEIFGLLGPNGAGKSTTFKMMCGLLVPTSGKALVLgmdlkvssgkaRQHLGYMAQkFSLYGNLSVEQNLRFF 426
Cdd:PLN03130 635 NINLDVPVGSLVAIVGSTGEGKTSLISAMLGELPPRSDASVVI-----------RGTVAYVPQ-VSWIFNATVRDNILFG 702
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 427 SGVyglrgraQNEKIARMSDAFGLksiaRHAADELPL---------------GYKQRLALACSLMHEPDILFLDEPTSGV 491
Cdd:PLN03130 703 SPF-------DPERYERAIDVTAL----QHDLDLLPGgdlteigergvnisgGQKQRVSMARAVYSNSDVYIFDDPLSAL 771
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 492 DP-LTRREFWLHINSMVDKGVTVMVTT--HFMdeaEYCDRIGLVYHGKLIASGTPDALKA 548
Cdd:PLN03130 772 DAhVGRQVFDKCIKDELRGKTRVLVTNqlHFL---SQVDRIILVHEGMIKEEGTYEELSN 828
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
459-546 |
2.27e-04 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 44.43 E-value: 2.27e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 459 DELPLGYK---------QRLALACSLMH---EPDILFLDEPTSGVDPLTRREFWLHINSMVDKGVTVMVTTHFMDEAEYC 526
Cdd:PRK00635 799 DYLPLGRPlsslsggeiQRLKLAYELLApskKPTLYVLDEPTTGLHTHDIKALIYVLQSLTHQGHTVVIIEHNMHVVKVA 878
|
90 100
....*....|....*....|....*.
gi 488984955 527 DRI------GLVYHGKLIASGTPDAL 546
Cdd:PRK00635 879 DYVlelgpeGGNLGGYLLASCSPEEL 904
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
26-187 |
2.64e-04 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 44.25 E-value: 2.64e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 26 LTCTIRAGYVTGLVGPDGAGKTTLMRMLAGLLKPDEGRASVIGFDPLKDDSA--LHAVLGYMPQ-------------KFG 90
Cdd:PTZ00265 404 LNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIIINDSHNLKDINLkwWRSKIGVVSQdpllfsnsiknniKYS 483
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 91 LY--EDLTVMEN------LTLYADLRSVTG----------------------EARKK-----------IFDRLL--EFTS 127
Cdd:PTZ00265 484 LYslKDLEALSNyynedgNDSQENKNKRNScrakcagdlndmsnttdsneliEMRKNyqtikdsevvdVSKKVLihDFVS 563
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 488984955 128 LGPFT-ERLAG----KLSGGMKQKLGLACTLVGDPKVLLLDEPGVGVDPISRRELWQMVHELAGD 187
Cdd:PTZ00265 564 ALPDKyETLVGsnasKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQKTINNLKGN 628
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
416-546 |
2.82e-04 |
|
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of proteins of which all members for which functions are known except the UvrA proteins are involved in the transport of material through membranes. UvrA orthologs are involved in the recognition of DNA damage as a step in nucleotide excision repair. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 273184 [Multi-domain] Cd Length: 925 Bit Score: 43.85 E-value: 2.82e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 416 NLSVEQNLRFFSGVYGLRgraqnEKIARMSDAfGLKSIAR-HAADELPLGYKQRLALACSLMHE---PDILFLDEPTSGv 491
Cdd:TIGR00630 790 DMTVEEAYEFFEAVPSIS-----RKLQTLCDV-GLGYIRLgQPATTLSGGEAQRIKLAKELSKRstgRTLYILDEPTTG- 862
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 488984955 492 dpltrrefwLH----------INSMVDKGVTVMVTTHFMDEAEYCDRI------GLVYHGKLIASGTPDAL 546
Cdd:TIGR00630 863 ---------LHfddikkllevLQRLVDKGNTVVVIEHNLDVIKTADYIidlgpeGGDGGGTVVASGTPEEV 924
|
|
| COG4928 |
COG4928 |
Predicted P-loop ATPase, KAP-like [General function prediction only]; |
33-146 |
3.08e-04 |
|
Predicted P-loop ATPase, KAP-like [General function prediction only];
Pssm-ID: 443956 Cd Length: 386 Bit Score: 43.36 E-value: 3.08e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 33 GYVTGLVGPDGAGKTTLMRMLAGLLKPDEgRASVIGFDPLK---DDSALHAVLGYMPQKFGLY--EDLTVMENLTLYAdl 107
Cdd:COG4928 29 PLVIGLDGEWGSGKTSFLNLIEKELESNE-KVIVVYFNAWLydgEEDLLAALLSEIAAELEKKkkKDKKAAKKLKKYA-- 105
|
90 100 110
....*....|....*....|....*....|....*....
gi 488984955 108 rsvtgearKKIFDRLLEFTSLGPFTERLAGKLSGGMKQK 146
Cdd:COG4928 106 --------KRLSKLALKAGLLGGPAEAVAEALKALLKKE 136
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
342-548 |
7.05e-04 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 42.79 E-value: 7.05e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 342 FAATDHVDFQVKRGEIFGLLGPNGAGKSTTFKMMC----GLLVPTSGKALVLGMDLKVSSGKARQHLGYMAQKFSLYGNL 417
Cdd:TIGR00956 74 FDILKPMDGLIKPGELTVVLGRPGSGCSTLLKTIAsntdGFHIGVEGVITYDGITPEEIKKHYRGDVVYNAETDVHFPHL 153
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 418 SVEQNLRFFSGVYGLRGRAQN----EKIARMSD----AFGLkSIARHA--ADELPLGY----KQRLALACSLMHEPDILF 483
Cdd:TIGR00956 154 TVGETLDFAARCKTPQNRPDGvsreEYAKHIADvymaTYGL-SHTRNTkvGNDFVRGVsggeRKRVSIAEASLGGAKIQC 232
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 488984955 484 LDEPTSGVDPLTRREFWLHINSMVDkgvtVMVTTHFM-------DEAEYCDRIGLVYHGKLIASGTPDALKA 548
Cdd:TIGR00956 233 WDNATRGLDSATALEFIRALKTSAN----ILDTTPLVaiyqcsqDAYELFDKVIVLYEGYQIYFGPADKAKQ 300
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
348-542 |
7.65e-04 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 42.66 E-value: 7.65e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 348 VDFQVKRGEIFGLLGPNGAGKSTTFKMMCGLLVPTSGKALVLgmdlkvssgkaRQHLGYMAQKFSLYgNLSVEQNLRFFS 427
Cdd:PLN03232 636 INLEIPVGSLVAIVGGTGEGKTSLISAMLGELSHAETSSVVI-----------RGSVAYVPQVSWIF-NATVRENILFGS 703
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 428 gvyglrgRAQNEKIARMSDAFGLKsiarHAADELPL---------------GYKQRLALACSLMHEPDILFLDEPTSGVD 492
Cdd:PLN03232 704 -------DFESERYWRAIDVTALQ----HDLDLLPGrdlteigergvnisgGQKQRVSMARAVYSNSDIYIFDDPLSALD 772
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 488984955 493 PLTRREFWlhiNSMVDKGVT----VMVTT--HFMDEAeycDRIGLVYHGKLIASGT 542
Cdd:PLN03232 773 AHVAHQVF---DSCMKDELKgktrVLVTNqlHFLPLM---DRIILVSEGMIKEEGT 822
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
354-529 |
8.37e-04 |
|
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: 40.42 E-value: 8.37e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 354 RGEIFGLLGPNGAGKSTTFKMMCgllvptsgkaLVLGMDlkvsSGKARQHLGYMAQKFSLYgnlsveQNLRFFSGVYGLR 433
Cdd:cd03227 20 EGSLTIITGPNGSGKSTILDAIG----------LALGGA----QSATRRRSGVKAGCIVAA------VSAELIFTRLQLS 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 434 GraqnekiarmsdafGLKSIARHAadelplgykqrLALACSLMHEPDILFLDEPTSGVDPLTRREFWLHINSMVDKGVTV 513
Cdd:cd03227 80 G--------------GEKELSALA-----------LILALASLKPRPLYILDEIDRGLDPRDGQALAEAILEHLVKGAQV 134
|
170
....*....|....*.
gi 488984955 514 MVTTHFMDEAEYCDRI 529
Cdd:cd03227 135 IVITHLPELAELADKL 150
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
19-204 |
8.59e-04 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 41.92 E-value: 8.59e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 19 DRPAVAPLTCTIRAGYVTGLVGPDGAGKTTLMRMLAG-----------LLKPDEGRASVIGfdplkdDSALHavLGYMPQ 87
Cdd:PRK10938 272 DRPILHNLSWQVNPGEHWQIVGPNGAGKSTLLSLITGdhpqgysndltLFGRRRGSGETIW------DIKKH--IGYVSS 343
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 88 KFGL-YEDLTVMENLTL--YAD----LRSVTGEARKKIFDRLlefTSLGpFTERLAGK----LSGGmKQKLGL-ACTLVG 155
Cdd:PRK10938 344 SLHLdYRVSTSVRNVILsgFFDsigiYQAVSDRQQKLAQQWL---DILG-IDKRTADApfhsLSWG-QQRLALiVRALVK 418
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 488984955 156 DPKVLLLDEPGVGVDPISRRELWQMVHELAGDGMLILWSTSYLDE-AEQC 204
Cdd:PRK10938 419 HPTLLILDEPLQGLDPLNRQLVRRFVDVLISEGETQLLFVSHHAEdAPAC 468
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
17-170 |
9.03e-04 |
|
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: 41.16 E-value: 9.03e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 17 GMDRPAVAPLTCTIRAGYVTGLVGPDGAGKTTLMRMLAGLLKPDEGR---ASVIGFDPLKDDSALHA--VLGYMPQKFGL 91
Cdd:cd03290 11 GSGLATLSNINIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKvhwSNKNESEPSFEATRSRNrySVAYAAQKPWL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 92 YeDLTVMENLTLYADL-----RSVTGEARKKIFDRLLEFTSLGPFTERlAGKLSGGMKQKLGLACTLVGDPKVLLLDEPG 166
Cdd:cd03290 91 L-NATVEENITFGSPFnkqryKAVTDACSLQPDIDLLPFGDQTEIGER-GINLSGGQRQRICVARALYQNTNIVFLDDPF 168
|
....
gi 488984955 167 VGVD 170
Cdd:cd03290 169 SALD 172
|
|
| 3a01203 |
TIGR00954 |
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ... |
23-164 |
1.52e-03 |
|
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 273360 [Multi-domain] Cd Length: 659 Bit Score: 41.27 E-value: 1.52e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 23 VAPLTCTIRAGYVTGLVGPDGAGKTTLMRMLAGL--------LKPDEGRasvigfdplkddsalhavLGYMPQKfgLYED 94
Cdd:TIGR00954 468 IESLSFEVPSGNNLLICGPNGCGKSSLFRILGELwpvyggrlTKPAKGK------------------LFYVPQR--PYMT 527
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 95 LTVMENLTLYADlrSVTGEARKKIFDR----LLEFTSLGPFTERLAG---------KLSGGMKQKLGLACTLVGDPKVLL 161
Cdd:TIGR00954 528 LGTLRDQIIYPD--SSEDMKRRGLSDKdleqILDNVQLTHILEREGGwsavqdwmdVLSGGEKQRIAMARLFYHKPQFAI 605
|
...
gi 488984955 162 LDE 164
Cdd:TIGR00954 606 LDE 608
|
|
| ABC_Rad50 |
cd03240 |
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ... |
339-534 |
1.59e-03 |
|
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ATP-binding cassette of ABC transporters, but are not associated with membrane-spanning domains. The conserved ATP-binding motifs common to Rad50 and the ABC transporter family include the Walker A and Walker B motifs, the Q loop, a histidine residue in the switch region, a D-loop, and a conserved LSGG sequence. This conserved sequence, LSGG, is the most specific and characteristic motif of this family and is thus known as the ABC signature sequence.
Pssm-ID: 213207 [Multi-domain] Cd Length: 204 Bit Score: 39.90 E-value: 1.59e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 339 FGDFAATDHVDFqvkRGEIFGLLGPNGAGKSTTFKmmcGLLVPTSGkalvlgmdLKVSSGKARQHLGYMAQKfslyGNLS 418
Cdd:cd03240 9 IRSFHERSEIEF---FSPLTLIVGQNGAGKTTIIE---ALKYALTG--------ELPPNSKGGAHDPKLIRE----GEVR 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 419 VEQNLRFfsgvyglRGRAQNE-KIARMSDAFgLKSIARHAAD-----ELPLGYKQ-----------RLALACSLMHEPDI 481
Cdd:cd03240 71 AQVKLAF-------ENANGKKyTITRSLAIL-ENVIFCHQGEsnwplLDMRGRCSggekvlasliiRLALAETFGSNCGI 142
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 488984955 482 LFLDEPTSGVDPlTRREFWLH--INSMVDKGV-TVMVTTHfmDEaEYCDRIGLVYH 534
Cdd:cd03240 143 LALDEPTTNLDE-ENIEESLAeiIEERKSQKNfQLIVITH--DE-ELVDAADHIYR 194
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
347-549 |
2.45e-03 |
|
multi drug resistance-associated protein (MRP); This model describes multi drug resistance-associated protein (MRP) in eukaryotes. The multidrug resistance-associated protein is an integral membrane protein that causes multidrug resistance when overexpressed in mammalian cells. It belongs to ABC transporter superfamily. The protein topology and function was experimentally demonstrated by epitope tagging and immunofluorescence. Insertion of tags in the critical regions associated with drug efflux, abrogated its function. The C-terminal domain seem to highly conserved. [Transport and binding proteins, Other]
Pssm-ID: 188098 [Multi-domain] Cd Length: 1522 Bit Score: 41.08 E-value: 2.45e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 347 HVDFQVKRGEIFGLLGPNGAGKSTTFKMMCGLLVPTSGKALVLGMDL-KVSSGKARQHLGYMAQKFSLYGNlSVEQNLRF 425
Cdd:TIGR00957 1304 HINVTIHGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGLNIaKIGLHDLRFKITIIPQDPVLFSG-SLRMNLDP 1382
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 426 FSGvYGLRGRAQNEKIARMSDAF-----GLKSIARHAADELPLGYKQRLALACSLMHEPDILFLDEPTSGVDPLTRREFW 500
Cdd:TIGR00957 1383 FSQ-YSDEEVWWALELAHLKTFVsalpdKLDHECAEGGENLSVGQRQLVCLARALLRKTKILVLDEATAAVDLETDNLIQ 1461
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 488984955 501 LHINSMVDKgVTVMVTTHFMDEAEYCDRIGLVYHGKLIASGTPDALKAQ 549
Cdd:TIGR00957 1462 STIRTQFED-CTVLTIAHRLNTIMDYTRVIVLDKGEVAEFGAPSNLLQQ 1509
|
|
| ABC_sbcCD |
cd03279 |
ATP-binding cassette domain of sbcCD; SbcCD and other Mre11/Rad50 (MR) complexes are ... |
337-399 |
2.85e-03 |
|
ATP-binding cassette domain of sbcCD; SbcCD and other Mre11/Rad50 (MR) complexes are implicated in the metabolism of DNA ends. They cleave ends sealed by hairpin structures and are thought to play a role in removing protein bound to DNA termini.
Pssm-ID: 213246 [Multi-domain] Cd Length: 213 Bit Score: 39.56 E-value: 2.85e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 488984955 337 KKFGDFAATDHVDF-QVKRGEIFGLLGPNGAGKSTTFKMMC-GLLVPTSGKALVLGMDLKVSSGK 399
Cdd:cd03279 9 KNFGPFREEQVIDFtGLDNNGLFLICGPTGAGKSTILDAITyALYGKTPRYGRQENLRSVFAPGE 73
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
275-546 |
7.05e-03 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 39.38 E-value: 7.05e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 275 IEEVQQHgDMPPLQV-ADTAPRFEDAFIDLLGGAGT-AESPLGAIIHRVD-GSkeeTVIEAQSLTKKFGDFAATDHVDFQ 351
Cdd:PTZ00243 1257 TDEVPHE-DMPELDEeVDALERRTGMAADVTGTVVIePASPTSAAPHPVQaGS---LVFEGVQMRYREGLPLVLRGVSFR 1332
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 352 VKRGEIFGLLGPNGAGKST---TFKMM---CGllvptsGKALVLGMDLKvSSG--KARQHLGYMAQKFSLYGNlSVEQNL 423
Cdd:PTZ00243 1333 IAPREKVGIVGRTGSGKSTlllTFMRMvevCG------GEIRVNGREIG-AYGlrELRRQFSMIPQDPVLFDG-TVRQNV 1404
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 424 RFFSG-----------VYGLRGRAQnekiarmSDAFGLKSIARHAADELPLGYKQRLALACSLMHE-PDILFLDEPTSGV 491
Cdd:PTZ00243 1405 DPFLEassaevwaaleLVGLRERVA-------SESEGIDSRVLEGGSNYSVGQRQLMCMARALLKKgSGFILMDEATANI 1477
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 488984955 492 DPLTRREFWLHINSMVdKGVTVMVTTHFMDEAEYCDRIGLVYHGKLIASGTPDAL 546
Cdd:PTZ00243 1478 DPALDRQIQATVMSAF-SAYTVITIAHRLHTVAQYDKIIVMDHGAVAEMGSPREL 1531
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
138-202 |
8.47e-03 |
|
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: 37.34 E-value: 8.47e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984955 138 KLSGGMKQKLGLA-----CTLVGDPkVLLLDEPGVGVDPISRRELWQMVHELAGDGMLILWSTSYLDEAE 202
Cdd:cd03227 77 QLSGGEKELSALAlilalASLKPRP-LYILDEIDRGLDPRDGQALAEAILEHLVKGAQVIVITHLPELAE 145
|
|
| |
