|
Name |
Accession |
Description |
Interval |
E-value |
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
12-913 |
0e+00 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 1911.41 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 12 IALLENVGQQYGATIALRDISLAIPARRMVGLIGPDGVGKSSLLSLIAGARAIEQGNVMVLGGDMRDVHHRRDVCPKIAW 91
Cdd:NF033858 1 VARLEGVSHRYGKTVALDDVSLDIPAGCMVGLIGPDGVGKSSLLSLIAGARKIQQGRVEVLGGDMADARHRRAVCPRIAY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 92 MPQGLGKNLYHTLSVYENVDFFARLFGHDKAERELRINELLQSTGLAPFRDRPAGKLSGGMKQKLGLCCALIHDPQLLIL 171
Cdd:NF033858 81 MPQGLGKNLYPTLSVFENLDFFGRLFGQDAAERRRRIDELLRATGLAPFADRPAGKLSGGMKQKLGLCCALIHDPDLLIL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 172 DEPTTGVDPLSRAQFWELIDSIRQRQPEMSVLVATAYMEEAERFDWLVAMNAGEVLATGSAAELKAQTGSQTLEQAFIAL 251
Cdd:NF033858 161 DEPTTGVDPLSRRQFWELIDRIRAERPGMSVLVATAYMEEAERFDWLVAMDAGRVLATGTPAELLARTGADTLEAAFIAL 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 252 LPEAQRQAHKTVVIPPRDSR-EEEIAIEARGLTMRFGNFVAVDHVNFRIARGEIFGFLGSNGCGKSTTMKMLTGLLPASE 330
Cdd:NF033858 241 LPEEKRRGHQPVVIPPRPADdDDEPAIEARGLTMRFGDFTAVDHVSFRIRRGEIFGFLGSNGCGKSTTMKMLTGLLPASE 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 331 GEAWLFGQPVDPKDIATRQRVGYMSQAFSLYSELSVRQNLELHARLFHIPDDEIAHRVAEMSERFMLTEVKDALPADLPL 410
Cdd:NF033858 321 GEAWLFGQPVDAGDIATRRRVGYMSQAFSLYGELTVRQNLELHARLFHLPAAEIAARVAEMLERFDLADVADALPDSLPL 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 411 GIRQRLSLAVAVIHRPEMLILDEPTSGVDPVARDMFWQLMVDLARQDRVTIFISTHFMNEAERCDRISLMHAGKVLASDT 490
Cdd:NF033858 401 GIRQRLSLAVAVIHKPELLILDEPTSGVDPVARDMFWRLLIELSREDGVTIFISTHFMNEAERCDRISLMHAGRVLASDT 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 491 PQALVEQRGAASLEEAFIAWLKEAQPSSPVPEDPT----SAVASHSEHTAPRQAFSLRRLFSYSRREALELRRDPVRSTL 566
Cdd:NF033858 481 PAALVAARGAATLEEAFIAYLEEAAGAAAAPAAAAapaaAAAAPAAPAPAPRRRFSLRRLLAYARREALELLRDPIRLTF 560
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 567 ALLGTVILMFIMGYGISMDVEDLRFAVLDRDQTLSSQGWSQNIAGSRYFIEQAPLHSYDELDRRMRDGELAVAIEIPPNF 646
Cdd:NF033858 561 ALLGSVILMFVMGYGISLDVENLTFAVLDRDQTPESRAYLLNFAGSRYFIEQPPIADYAELDRRMRSGELSLAIEIPPGF 640
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 647 GRDIARGTPVQIGVWVDGAMPNRAETVRGYVQAMHLAWLQEMAgRQSSPQRDTSLISIETRYRYNPDVKSLPAIVPAVIP 726
Cdd:NF033858 641 GRDLLRGRPPEVGAWIDGAMPFRAETIRGYVQGMHQQWLADLA-RERGGAAAASPATIETRYRYNPDFKSLPAMVPAVIP 719
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 727 LLLMMIPAMLSALSVVREKELGSIINLYVTPTTRSEFLLGKQLPYIVLGMFNFFLLCALSVFVFGVAHKGSFLTLTLAAL 806
Cdd:NF033858 720 LLLMLIPAMLTALSVVREKELGSITNLYVTPVTRLEFLLGKQLPYVALAMLNFLLLVLLAVFVFGVPLKGSFLALALGAL 799
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 807 LYVTIATGLGLLISTFMKSQIAAIFGTAIITLIPATQFSGMIDPVASLEGPGRWIGQIYPTSHFLTIARGTFSKALNLSD 886
Cdd:NF033858 800 LYVTATTGLGLLISTFTRSQIAAIFGTAILTLIPAVQFSGLLDPVSSLEGAGRLIGRIFPATYFLTISRGTFTKGLGFAD 879
|
890 900
....*....|....*....|....*..
gi 1820369315 887 LWGSFIPLLIAVPLVLGLSVLLLKKQE 913
Cdd:NF033858 880 LWPSFLALAAFIPVLLGLSVLLLKKQE 906
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
277-515 |
2.71e-103 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 320.47 E-value: 2.71e-103
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 277 IEARGLTMRFGNFVAVDHVNFRIARGEIFGFLGSNGCGKSTTMKMLTGLLPASEGEAWLFGQPVDPKDIATRQRVGYMSQ 356
Cdd:COG1131 1 IEVRGLTKRYGDKTALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRVLGEDVARDPAEVRRRIGYVPQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 357 AFSLYSELSVRQNLELHARLFHIPDDEIAHRVAEMSERFMLTEVKDALPADLPLGIRQRLSLAVAVIHRPEMLILDEPTS 436
Cdd:COG1131 81 EPALYPDLTVRENLRFFARLYGLPRKEARERIDELLELFGLTDAADRKVGTLSGGMKQRLGLALALLHDPELLILDEPTS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 437 GVDPVARDMFWQLMVDLARQDRvTIFISTHFMNEAER-CDRISLMHAGKVLASDTPQALVEQrgaaSLEEAFIAWLKEAQ 515
Cdd:COG1131 161 GLDPEARRELWELLRELAAEGK-TVLLSTHYLEEAERlCDRVAIIDKGRIVADGTPDELKAR----LLEDVFLELTGEEA 235
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
15-257 |
4.41e-88 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 280.41 E-value: 4.41e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 15 LENVGQQYGATIALRDISLAIPARRMVGLIGPDGVGKSSLLSLIAGARAIEQGNVMVLGGDMRDvhHRRDVCPKIAWMPQ 94
Cdd:COG1131 3 VRGLTKRYGDKTALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRVLGEDVAR--DPAEVRRRIGYVPQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 95 GLgkNLYHTLSVYENVDFFARLFGHDKAERELRINELLQSTGLAPFRDRPAGKLSGGMKQKLGLCCALIHDPQLLILDEP 174
Cdd:COG1131 81 EP--ALYPDLTVRENLRFFARLYGLPRKEARERIDELLELFGLTDAADRKVGTLSGGMKQRLGLALALLHDPELLILDEP 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 175 TTGVDPLSRAQFWELIDSIRQRqpEMSVLVATAYMEEAERF-DWLVAMNAGEVLATGSAAELKAqtgsQTLEQAFIALLP 253
Cdd:COG1131 159 TSGLDPEARRELWELLRELAAE--GKTVLLSTHYLEEAERLcDRVAIIDKGRIVADGTPDELKA----RLLEDVFLELTG 232
|
....
gi 1820369315 254 EAQR 257
Cdd:COG1131 233 EEAR 236
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
11-494 |
1.19e-87 |
|
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: 289.11 E-value: 1.19e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 11 PIALLENVGQQY--GATIALRDISLAIPARRMVGLIGPDGVGKSSLLSLIAG---ARAIEQGNVMVLGGDMRDVHhRRDV 85
Cdd:COG1123 3 PLLEVRDLSVRYpgGDVPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGllpHGGRISGEVLLDGRDLLELS-EALR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 86 CPKIAWMPQGLGKNLyHTLSVYENVDFFARLFGHDKAERELRINELLQSTGLAPFRDRPAGKLSGGMKQKLGLCCALIHD 165
Cdd:COG1123 82 GRRIGMVFQDPMTQL-NPVTVGDQIAEALENLGLSRAEARARVLELLEAVGLERRLDRYPHQLSGGQRQRVAIAMALALD 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 166 PQLLILDEPTTGVDPLSRAQFWELIDSIrQRQPEMSVLVATAYMEE-AERFDWLVAMNAGEVLATGSAAELKAQtgSQTL 244
Cdd:COG1123 161 PDLLIADEPTTALDVTTQAEILDLLREL-QRERGTTVLLITHDLGVvAEIADRVVVMDDGRIVEDGPPEEILAA--PQAL 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 245 eqafiallpEAQRQAHKTVVIPPRDSREEEIAIEARGLTMRF-----GNFVAVDHVNFRIARGEIFGFLGSNGCGKSTTM 319
Cdd:COG1123 238 ---------AAVPRLGAARGRAAPAAAAAEPLLEVRNLSKRYpvrgkGGVRAVDDVSLTLRRGETLGLVGESGSGKSTLA 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 320 KMLTGLLPASEGEAWLFGQPVDPKDIAT----RQRVGYMSQ--AFSLYSELSVRQNLELHARLFHI-PDDEIAHRVAEMS 392
Cdd:COG1123 309 RLLLGLLRPTSGSILFDGKDLTKLSRRSlrelRRRVQMVFQdpYSSLNPRMTVGDIIAEPLRLHGLlSRAERRERVAELL 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 393 ERFML-TEVKDALPADLPLGIRQRLSLAVAVIHRPEMLILDEPTSGVDPVARDMFWQLMVDLARQDRVT-IFIsTHFMNE 470
Cdd:COG1123 389 ERVGLpPDLADRYPHELSGGQRQRVAIARALALEPKLLILDEPTSALDVSVQAQILNLLRDLQRELGLTyLFI-SHDLAV 467
|
490 500
....*....|....*....|....*
gi 1820369315 471 AER-CDRISLMHAGKVLASDTPQAL 494
Cdd:COG1123 468 VRYiADRVAVMYDGRIVEDGPTEEV 492
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
277-517 |
8.60e-75 |
|
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: 245.15 E-value: 8.60e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 277 IEARGLTMRFGNFVAVDHVNFRIARGEIFGFLGSNGCGKSTTMKMLTGLLPASEGEAWLFGQPVDPKDIATRQRVGYMSQ 356
Cdd:COG4555 2 IEVENLSKKYGKVPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIDGEDVRKEPREARRQIGVLPD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 357 AFSLYSELSVRQNLELHARLFHIPDDEIAHRVAEMSERFMLTEVKDALPADLPLGIRQRLSLAVAVIHRPEMLILDEPTS 436
Cdd:COG4555 82 ERGLYDRLTVRENIRYFAELYGLFDEELKKRIEELIELLGLEEFLDRRVGELSTGMKKKVALARALVHDPKVLLLDEPTN 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 437 GVDPVARDMFWQLMVDLARQDRvTIFISTHFMNEAER-CDRISLMHAGKVLASDTPQALVEQRGAASLEEAFIAWLKEAQ 515
Cdd:COG4555 162 GLDVMARRLLREILRALKKEGK-TVLFSSHIMQEVEAlCDRVVILHKGKVVAQGSLDELREEIGEENLEDAFVALIGSEE 240
|
..
gi 1820369315 516 PS 517
Cdd:COG4555 241 GE 242
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
277-485 |
1.11e-73 |
|
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: 239.22 E-value: 1.11e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 277 IEARGLTMRFGNFVAVDHVNFRIARGEIFGFLGSNGCGKSTTMKMLTGLLPASEGEAWLFGQPVDPKDIATRQRVGYMSQ 356
Cdd:cd03230 1 IEVRNLSKRYGKKTALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVLGKDIKKEPEEVKRRIGYLPE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 357 AFSLYSELSVRQNLelharlfhipddeiahrvaemserfmltevkdalpaDLPLGIRQRLSLAVAVIHRPEMLILDEPTS 436
Cdd:cd03230 81 EPSLYENLTVRENL------------------------------------KLSGGMKQRLALAQALLHDPELLILDEPTS 124
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1820369315 437 GVDPVARDMFWQLMVDLARQDRvTIFISTHFMNEAER-CDRISLMHAGKV 485
Cdd:cd03230 125 GLDPESRREFWELLRELKKEGK-TILLSSHILEEAERlCDRVAILNNGRI 173
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
277-494 |
5.44e-72 |
|
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: 236.50 E-value: 5.44e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 277 IEARGLTMRFGNFVAVDHVNFRIARGEIFGFLGSNGCGKSTTMKMLTGLLPASEGEAWLFGQPV--DPKDIatRQRVGYM 354
Cdd:cd03265 1 IEVENLVKKYGDFEAVRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATVAGHDVvrEPREV--RRRIGIV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 355 SQAFSLYSELSVRQNLELHARLFHIPDDEIAHRVAEMSERFMLTEVKDALPADLPLGIRQRLSLAVAVIHRPEMLILDEP 434
Cdd:cd03265 79 FQDLSVDDELTGWENLYIHARLYGVPGAERRERIDELLDFVGLLEAADRLVKTYSGGMRRRLEIARSLVHRPEVLFLDEP 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1820369315 435 TSGVDPVARDMFWQLMVDLARQDRVTIFISTHFMNEAER-CDRISLMHAGKVLASDTPQAL 494
Cdd:cd03265 159 TIGLDPQTRAHVWEYIEKLKEEFGMTILLTTHYMEEAEQlCDRVAIIDHGRIIAEGTPEEL 219
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
276-559 |
1.77e-69 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 232.69 E-value: 1.77e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 276 AIEARGLTMRFGNFVAVDHVNFRIARGEIFGFLGSNGCGKSTTMKMLTGLLPASEGEAWLFGQPVDPKDiatRQRVGYMS 355
Cdd:COG4152 1 MLELKGLTKRFGDKTAVDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDSGEVLWDGEPLDPED---RRRIGYLP 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 356 QAFSLYSELSVRQNLELHARLFHIPDDEIAHRVAEMSERFMLTEVKDALPADLPLGIRQRLSLAVAVIHRPEMLILDEPT 435
Cdd:COG4152 78 EERGLYPKMKVGEQLVYLARLKGLSKAEAKRRADEWLERLGLGDRANKKVEELSKGNQQKVQLIAALLHDPELLILDEPF 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 436 SGVDPVARDMFWQLMVDLARQDrVTIFISTHFMNEAER-CDRISLMHAGKVLASDTPQALVEQRGAASLE---EAFIAWL 511
Cdd:COG4152 158 SGLDPVNVELLKDVIRELAAKG-TTVIFSSHQMELVEElCDRIVIINKGRKVLSGSVDEIRRQFGRNTLRleaDGDAGWL 236
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 1820369315 512 KEAQPSSPVPEDPTSAVASHSEHTAPRQAfsLRRLFSYSRREALELRR 559
Cdd:COG4152 237 RALPGVTVVEEDGDGAELKLEDGADAQEL--LRALLARGPVREFEEVR 282
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
277-494 |
3.03e-68 |
|
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: 226.23 E-value: 3.03e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 277 IEARGLTMRFGN--FVAVDHVNFRIARGEIFGFLGSNGCGKSTTMKMLTGLLPASEGEAWLFGQPVDPKDIATRQRVGYM 354
Cdd:cd03263 1 LQIRNLTKTYKKgtKPAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYINGYSIRTDRKAARQSLGYC 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 355 SQAFSLYSELSVRQNLELHARLFHIPDDEIAHRVAEMSERFMLTEVKDALPADLPLGIRQRLSLAVAVIHRPEMLILDEP 434
Cdd:cd03263 81 PQFDALFDELTVREHLRFYARLKGLPKSEIKEEVELLLRVLGLTDKANKRARTLSGGMKRKLSLAIALIGGPSVLLLDEP 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1820369315 435 TSGVDPVARDMFWQLMVDLaRQDRvTIFISTHFMNEAER-CDRISLMHAGKVLASDTPQAL 494
Cdd:cd03263 161 TSGLDPASRRAIWDLILEV-RKGR-SIILTTHSMDEAEAlCDRIAIMSDGKLRCIGSPQEL 219
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
15-256 |
6.76e-60 |
|
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, Inorganic ion transport and metabolism];
Pssm-ID: 443618 [Multi-domain] Cd Length: 243 Bit Score: 204.32 E-value: 6.76e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 15 LENVGQQYGATIALRDISLAIPARRMVGLIGPDGVGKSSLLSLIAGARAIEQGNVMVLGGDMR--DVHHRRdvcpKIAWM 92
Cdd:COG4555 4 VENLSKKYGKVPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIDGEDVRkePREARR----QIGVL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 93 PQGLGknLYHTLSVYENVDFFARLFGHDKAERELRINELLQSTGLAPFRDRPAGKLSGGMKQKLGLCCALIHDPQLLILD 172
Cdd:COG4555 80 PDERG--LYDRLTVRENIRYFAELYGLFDEELKKRIEELIELLGLEEFLDRRVGELSTGMKKKVALARALVHDPKVLLLD 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 173 EPTTGVDPLSRAQFWELIdsIRQRQPEMSVLVATAYMEEAER-FDWLVAMNAGEVLATGSAAELKAQTGSQTLEQAFIAL 251
Cdd:COG4555 158 EPTNGLDVMARRLLREIL--RALKKEGKTVLFSSHIMQEVEAlCDRVVILHKGKVVAQGSLDELREEIGEENLEDAFVAL 235
|
....*
gi 1820369315 252 LPEAQ 256
Cdd:COG4555 236 IGSEE 240
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
277-487 |
7.79e-58 |
|
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: 197.50 E-value: 7.79e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 277 IEARGLTMRFGNFVAVDHVNFRIARGEIFGFLGSNGCGKSTTMKMLTGLLPASEGEAWLFGQPVDpkdIATRQRVGYMSQ 356
Cdd:cd03269 1 LEVENVTKRFGRVTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDGKPLD---IAARNRIGYLPE 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 357 AFSLYSELSVRQNLELHARLFHIPDDEIAHRVAEMSERFMLTEVKDALPADLPLGIRQRLSLAVAVIHRPEMLILDEPTS 436
Cdd:cd03269 78 ERGLYPKMKVIDQLVYLAQLKGLKKEEARRRIDEWLERLELSEYANKRVEELSKGNQQKVQFIAAVIHDPELLILDEPFS 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1820369315 437 GVDPVARDMFWQLMVDLARQDRvTIFISTHFMNEAER-CDRISLMHAGKVLA 487
Cdd:cd03269 158 GLDPVNVELLKDVIRELARAGK-TVILSTHQMELVEElCDRVLLLNKGRAVL 208
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
15-226 |
1.62e-57 |
|
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: 194.92 E-value: 1.62e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 15 LENVGQQYGATIALRDISLAIPARRMVGLIGPDGVGKSSLLSLIAGARAIEQGNVMVLGGDMRDvhHRRDVCPKIAWMPQ 94
Cdd:cd03230 3 VRNLSKRYGKKTALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVLGKDIKK--EPEEVKRRIGYLPE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 95 GLGknLYHTLSVYENVdffarlfghdkaerelrinellqstglapfrdrpagKLSGGMKQKLGLCCALIHDPQLLILDEP 174
Cdd:cd03230 81 EPS--LYENLTVRENL------------------------------------KLSGGMKQRLALAQALLHDPELLILDEP 122
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1820369315 175 TTGVDPLSRAQFWELIDSIRQRQpeMSVLVATAYMEEAER-FDWLVAMNAGEV 226
Cdd:cd03230 123 TSGLDPESRREFWELLRELKKEG--KTILLSSHILEEAERlCDRVAILNNGRI 173
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
274-494 |
4.96e-55 |
|
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: 190.58 E-value: 4.96e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 274 EIAIEARGLTMRFGNFVAVDHVNFRIARGEIFGFLGSNGCGKSTTMKMLTGLLPASEGEAWLFGQPV---DPKD-IATRQ 349
Cdd:COG1127 3 EPMIEVRNLTKSFGDRVVLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEILVDGQDItglSEKElYELRR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 350 RVGYMSQAFSLYSELSVRQNLEL----HARLfhiPDDEIAHRVAEMSERFMLTEVKDALPADLPLGIRQRLSLAVAVIHR 425
Cdd:COG1127 83 RIGMLFQGGALFDSLTVFENVAFplreHTDL---SEAEIRELVLEKLELVGLPGAADKMPSELSGGMRKRVALARALALD 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 426 PEMLILDEPTSGVDPVARDMFWQLMVDLARQDRVTIFISTHFMNEAER-CDRISLMHAGKVLASDTPQAL 494
Cdd:COG1127 160 PEILLYDEPTAGLDPITSAVIDELIRELRDELGLTSVVVTHDLDSAFAiADRVAVLADGKIIAEGTPEEL 229
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
15-236 |
1.79e-53 |
|
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: 185.40 E-value: 1.79e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 15 LENVGQQYG--ATIALRDISLAIPARRMVGLIGPDGVGKSSLLSLIAGARAIEQGNVMVLGGDMRDvhHRRDVCPKIAWM 92
Cdd:cd03263 3 IRNLTKTYKkgTKPAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYINGYSIRT--DRKAARQSLGYC 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 93 PQGlgKNLYHTLSVYENVDFFARLFGHDKAERELRINELLQSTGLAPFRDRPAGKLSGGMKQKLGLCCALIHDPQLLILD 172
Cdd:cd03263 81 PQF--DALFDELTVREHLRFYARLKGLPKSEIKEEVELLLRVLGLTDKANKRARTLSGGMKRKLSLAIALIGGPSVLLLD 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1820369315 173 EPTTGVDPLSRAQFWELIDSIRQRQpemSVLVATAYMEEAERF-DWLVAMNAGEVLATGSAAELK 236
Cdd:cd03263 159 EPTSGLDPASRRAIWDLILEVRKGR---SIILTTHSMDEAEALcDRIAIMSDGKLRCIGSPQELK 220
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
277-488 |
3.85e-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: 183.96 E-value: 3.85e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 277 IEARGLTMRFGNFVAVDHVNFRIARGEIFGFLGSNGCGKSTTMKMLTGLLPASEGEAWLFGQPVDpKDIATRQRVGYMSQ 356
Cdd:cd03268 1 LKTNDLTKTYGKKRVLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEITFDGKSYQ-KNIEALRRIGALIE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 357 AFSLYSELSVRQNLELHARLFHIPDDEIaHRVAEMSErfmLTEVKDALPADLPLGIRQRLSLAVAVIHRPEMLILDEPTS 436
Cdd:cd03268 80 APGFYPNLTARENLRLLARLLGIRKKRI-DEVLDVVG---LKDSAKKKVKGFSLGMKQRLGIALALLGNPDLLILDEPTN 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1820369315 437 GVDPVARDMFWQLMVDLARQDRvTIFISTHFMNEAER-CDRISLMHAGKVLAS 488
Cdd:cd03268 156 GLDPDGIKELRELILSLRDQGI-TVLISSHLLSEIQKvADRIGIINKGKLIEE 207
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
277-498 |
9.15e-53 |
|
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: 183.69 E-value: 9.15e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 277 IEARGLTMRF-GNFVAVDHVNFRIARGEIFGFLGSNGCGKSTTMKMLTGLLPASEGEAWLFGQPVDPKDIAT-RQRVGYM 354
Cdd:COG1122 1 IELENLSFSYpGGTPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVDGKDITKKNLRElRRKVGLV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 355 -----SQAFslysELSVRQNLELHARLFHIPDDEIAHRVAEMSERFMLTEVKDALPADLPLGIRQRLSLAVAVIHRPEML 429
Cdd:COG1122 81 fqnpdDQLF----APTVEEDVAFGPENLGLPREEIRERVEEALELVGLEHLADRPPHELSGGQKQRVAIAGVLAMEPEVL 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 430 ILDEPTSGVDPVARDMFWQLMVDLARQDrVTIFISTHFMNEAER-CDRISLMHAGKVLASDTPQALVEQR 498
Cdd:COG1122 157 VLDEPTAGLDPRGRRELLELLKRLNKEG-KTVIIVTHDLDLVAElADRVIVLDDGRIVADGTPREVFSDY 225
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
251-504 |
2.78e-50 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 180.80 E-value: 2.78e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 251 LLPEAQRQAHKTVVIPPRDSREEEIAIEARGLTMRFGNFVAVDHVNFRIARGEIFGFLGSNGCGKSTTMKMLTGLLPASE 330
Cdd:PRK13536 16 LSPIERKHQGISEAKASIPGSMSTVAIDLAGVSKSYGDKAVVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDA 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 331 GEAWLFGQPVDPKDIATRQRVGYMSQAFSLYSELSVRQNLELHARLFHIPDDEIAHRVAEMSERFMLTEVKDALPADLPL 410
Cdd:PRK13536 96 GKITVLGVPVPARARLARARIGVVPQFDNLDLEFTVRENLLVFGRYFGMSTREIEAVIPSLLEFARLESKADARVSDLSG 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 411 GIRQRLSLAVAVIHRPEMLILDEPTSGVDPVARDMFWQLMVDLARQDRvTIFISTHFMNEAER-CDRISLMHAGKVLASD 489
Cdd:PRK13536 176 GMKRRLTLARALINDPQLLILDEPTTGLDPHARHLIWERLRSLLARGK-TILLTTHFMEEAERlCDRLCVLEAGRKIAEG 254
|
250
....*....|....*.
gi 1820369315 490 TPQALV-EQRGAASLE 504
Cdd:PRK13536 255 RPHALIdEHIGCQVIE 270
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
277-494 |
3.36e-50 |
|
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: 176.92 E-value: 3.36e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 277 IEARGLTMRFGNFVAVDHVNFRIARGEIFGFLGSNGCGKSTTMKMLTGLLPASEGEAWLFGQPVDP----KDIATRQRVG 352
Cdd:cd03261 1 IELRGLTKSFGGRTVLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGEDISGlseaELYRLRRRMG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 353 YMSQAFSLYSELSVRQNLEL----HARLfhiPDDEIAHRVAEMSERFMLTEVKDALPADLPLGIRQRLSLAVAVIHRPEM 428
Cdd:cd03261 81 MLFQSGALFDSLTVFENVAFplreHTRL---SEEEIREIVLEKLEAVGLRGAEDLYPAELSGGMKKRVALARALALDPEL 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1820369315 429 LILDEPTSGVDPVARDMFWQLMVDLARQDRVTIFISTHFMNEAER-CDRISLMHAGKVLASDTPQAL 494
Cdd:cd03261 158 LLYDEPTAGLDPIASGVIDDLIRSLKKELGLTSIMVTHDLDTAFAiADRIAVLYDGKIVAEGTPEEL 224
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
274-493 |
3.69e-50 |
|
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: 177.54 E-value: 3.69e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 274 EIAIEARGLTMRFGNFVAVDHVNFRIARGEIFGFLGSNGCGKSTTMKMLTGLLPASEGEAWLFGQPVDPKDIATRQRVGy 353
Cdd:COG0411 2 DPLLEVRGLTKRFGGLVAVDDVSLEVERGEIVGLIGPNGAGKTTLFNLITGFYRPTSGRILFDGRDITGLPPHRIARLG- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 354 MSQAF---SLYSELSVRQNLEL--HAR--------LFHIP-----DDEIAHRVAEMSERFMLTEVKDALPADLPLGIRQR 415
Cdd:COG0411 81 IARTFqnpRLFPELTVLENVLVaaHARlgrgllaaLLRLPrarreEREARERAEELLERVGLADRADEPAGNLSYGQQRR 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1820369315 416 LSLAVAVIHRPEMLILDEPTSGVDPVARDMFWQLMVDLARQDRVTIFISTHFMNEAER-CDRISLMHAGKVLASDTPQA 493
Cdd:COG0411 161 LEIARALATEPKLLLLDEPAAGLNPEETEELAELIRRLRDERGITILLIEHDMDLVMGlADRIVVLDFGRVIAEGTPAE 239
|
|
| drrA |
TIGR01188 |
daunorubicin resistance ABC transporter ATP-binding subunit; This model describes daunorubicin ... |
22-245 |
9.77e-50 |
|
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: 177.97 E-value: 9.77e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 22 YGATIALRDISLAIPARRMVGLIGPDGVGKSSLLSLIAGARAIEQGNVMVLGGDMrdVHHRRDVCPKIAWMPQGlgKNLY 101
Cdd:TIGR01188 3 YGDFKAVDGVNFKVREGEVFGFLGPNGAGKTTTIRMLTTLLRPTSGTARVAGYDV--VREPRKVRRSIGIVPQY--ASVD 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 102 HTLSVYENVDFFARLFGHDKAERELRINELLQSTGLAPFRDRPAGKLSGGMKQKLGLCCALIHDPQLLILDEPTTGVDPL 181
Cdd:TIGR01188 79 EDLTGRENLEMMGRLYGLPKDEAEERAEELLELFELGEAADRPVGTYSGGMRRRLDIAASLIHQPDVLFLDEPTTGLDPR 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1820369315 182 SRAQFWELIDSIRQRqpEMSVLVATAYMEEAERF-DWLVAMNAGEVLATGSAAELKAQTGSQTLE 245
Cdd:TIGR01188 159 TRRAIWDYIRALKEE--GVTILLTTHYMEEADKLcDRIAIIDHGRIIAEGTPEELKRRLGKDTLE 221
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
277-488 |
1.18e-49 |
|
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: 174.86 E-value: 1.18e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 277 IEARGLTMRFGN----FVAVDHVNFRIARGEIFGFLGSNGCGKSTTMKMLTGLLPASEGEAWLFGQPVDPKDIATRQRVG 352
Cdd:cd03266 2 ITADALTKRFRDvkktVQAVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDGFDVVKEPAEARRRLG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 353 YMSQAFSLYSELSVRQNLELHARLFHIPDDEIAHRVAEMSERFMLTEVKDALPADLPLGIRQRLSLAVAVIHRPEMLILD 432
Cdd:cd03266 82 FVSDSTGLYDRLTARENLEYFAGLYGLKGDELTARLEELADRLGMEELLDRRVGGFSTGMRQKVAIARALVHDPPVLLLD 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1820369315 433 EPTSGVDPVARDMFWQLMVDLARQDRVTIFiSTHFMNEAER-CDRISLMHAGKVLAS 488
Cdd:cd03266 162 EPTTGLDVMATRALREFIRQLRALGKCILF-STHIMQEVERlCDRVVVLHRGRVVYE 217
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
16-236 |
1.37e-49 |
|
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: 174.48 E-value: 1.37e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 16 ENVGQQYGATIALRDISLAIPARRMVGLIGPDGVGKSSLLSLIAGARAIEQGNVMVLGGDMrdVHHRRDVCPKIAWMPQG 95
Cdd:cd03265 4 ENLVKKYGDFEAVRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATVAGHDV--VREPREVRRRIGIVFQD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 96 LgkNLYHTLSVYENVDFFARLFGHDKAERELRINELLQSTGLAPFRDRPAGKLSGGMKQKLGLCCALIHDPQLLILDEPT 175
Cdd:cd03265 82 L--SVDDELTGWENLYIHARLYGVPGAERRERIDELLDFVGLLEAADRLVKTYSGGMRRRLEIARSLVHRPEVLFLDEPT 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1820369315 176 TGVDPLSRAQFWELIDSIrQRQPEMSVLVATAYMEEAERF-DWLVAMNAGEVLATGSAAELK 236
Cdd:cd03265 160 IGLDPQTRAHVWEYIEKL-KEEFGMTILLTTHYMEEAEQLcDRVAIIDHGRIIAEGTPEELK 220
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
9-485 |
4.40e-49 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 181.76 E-value: 4.40e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 9 SPPIALLENVGQQYGATIALRDISLAIPARRMVGLIGPDGVGKSSLLSLIAGARAIEQGNVMVLGgdmRDVHHRRdvcPK 88
Cdd:COG1129 1 AEPLLEMRGISKSFGGVKALDGVSLELRPGEVHALLGENGAGKSTLMKILSGVYQPDSGEILLDG---EPVRFRS---PR 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 89 ------IAWMPQGLgkNLYHTLSVYENVdFFARLFGH----DKAERELRINELLQSTGLA--PfrDRPAGKLSGGMKQKL 156
Cdd:COG1129 75 daqaagIAIIHQEL--NLVPNLSVAENI-FLGREPRRggliDWRAMRRRARELLARLGLDidP--DTPVGDLSVAQQQLV 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 157 GLCCALIHDPQLLILDEPTTgvdPLSRA---QFWELIDSIRQRQpeMSVLVATAYMEEAERF-DWLVAMNAGEVLATGSA 232
Cdd:COG1129 150 EIARALSRDARVLILDEPTA---SLTEReveRLFRIIRRLKAQG--VAIIYISHRLDEVFEIaDRVTVLRDGRLVGTGPV 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 233 AEL------KAQTGsQTLEQAFiallpeaqrqahktvviPPRDSREEEIAIEARGLTMRfgnfVAVDHVNFRIARGEIFG 306
Cdd:COG1129 225 AELtedelvRLMVG-RELEDLF-----------------PKRAAAPGEVVLEVEGLSVG----GVVRDVSFSVRAGEILG 282
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 307 FLGSNGCGKSTTMKMLTGLLPASEGEAWLFGQPVDPKDI--ATRQRVGYMS---QAFSLYSELSVRQN-----LELHARL 376
Cdd:COG1129 283 IAGLVGAGRTELARALFGADPADSGEIRLDGKPVRIRSPrdAIRAGIAYVPedrKGEGLVLDLSIRENitlasLDRLSRG 362
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 377 FHIPDDEIAHRVAEMSERFmltEVKdalPADLPLGIR-------QRLSLAVAVIHRPEMLILDEPTSGVDPVARDMFWQL 449
Cdd:COG1129 363 GLLDRRRERALAEEYIKRL---RIK---TPSPEQPVGnlsggnqQKVVLAKWLATDPKVLILDEPTRGIDVGAKAEIYRL 436
|
490 500 510
....*....|....*....|....*....|....*..
gi 1820369315 450 MVDLARQDRVTIFISTHfMNEAER-CDRISLMHAGKV 485
Cdd:COG1129 437 IRELAAEGKAVIVISSE-LPELLGlSDRILVMREGRI 472
|
|
| PQQ_ABC_ATP |
TIGR03864 |
ABC transporter, ATP-binding subunit, PQQ-dependent alcohol dehydrogenase system; Members of ... |
276-509 |
2.86e-48 |
|
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: 171.32 E-value: 2.86e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 276 AIEARGLTMRFGNFVAVDHVNFRIARGEIFGFLGSNGCGKSTTMKMLTGLLPASEGEAWLFGQPVDPKDIATRQRVGYMS 355
Cdd:TIGR03864 1 ALEVAGLSFRYGARRALDDVSFTVRPGRFVALLGPNGAGKSTLFSLLTRLYVAQSGQISVAGHDLRRAPRAALARLGVVF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 356 QAFSLYSELSVRQNLELHARLFHIPDDEIAHRVAEMSERFMLTEVKDALPADLPLGIRQRLSLAVAVIHRPEMLILDEPT 435
Cdd:TIGR03864 81 QQPTLDLDLSVRQNLRYHAALHGLSRAEARARIAELLARLGLAERADDKVRELNGGHRRRVEIARALLHRPALLLLDEPT 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1820369315 436 SGVDPVARDMFWQLMVDLARQDRVTIFISTHFMNEAERCDRISLMHAGKVLASDTPQALVEQRGAASLEEAFIA 509
Cdd:TIGR03864 161 VGLDPASRAAITAHVRALARDQGLSVLWATHLVDEIEASDRLVVLHRGRVLADGAAAELRGATGGADLEAAFLA 234
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
277-488 |
4.23e-48 |
|
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: 170.07 E-value: 4.23e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 277 IEARGLTMRFGNFVAVDHVNFRIARGeIFGFLGSNGCGKSTTMKMLTGLLPASEGEAWLFGQPVDPKDIATRQRVGYMSQ 356
Cdd:cd03264 1 LQLENLTKRYGKKRALDGVSLTLGPG-MYGLLGPNGAGKTTLMRILATLTPPSSGTIRIDGQDVLKQPQKLRRRIGYLPQ 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 357 AFSLYSELSVRQNLELHARLFHIPDDEIAHRVAEMSERFMLTEVKDALPADLPLGIRQRLSLAVAVIHRPEMLILDEPTS 436
Cdd:cd03264 80 EFGVYPNFTVREFLDYIAWLKGIPSKEVKARVDEVLELVNLGDRAKKKIGSLSGGMRRRVGIAQALVGDPSILIVDEPTA 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1820369315 437 GVDPVARDMFWQLMVDLArQDRVTIfISTHFMNEAER-CDRISLMHAGKVLAS 488
Cdd:cd03264 160 GLDPEERIRFRNLLSELG-EDRIVI-LSTHIVEDVESlCNQVAVLNKGKLVFE 210
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
277-485 |
5.04e-48 |
|
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: 169.98 E-value: 5.04e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 277 IEARGLTMRFGN----FVAVDHVNFRIARGEIFGFLGSNGCGKSTTMKMLTGLLPASEGEAWLFGQPV---DPKDIAT-- 347
Cdd:cd03255 1 IELKNLSKTYGGggekVQALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRVDGTDIsklSEKELAAfr 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 348 RQRVGYMSQAFSLYSELSVRQNLELHARLFHIPDDEIAHRVAEMSERFMLTEVKDALPADLPLGIRQRLSLAVAVIHRPE 427
Cdd:cd03255 81 RRHIGFVFQSFNLLPDLTALENVELPLLLAGVPKKERRERAEELLERVGLGDRLNHYPSELSGGQQQRVAIARALANDPK 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1820369315 428 MLILDEPTSGVDPVARDMFWQLMVDLARQDRVTIFISTHFMNEAERCDRISLMHAGKV 485
Cdd:cd03255 161 IILADEPTGNLDSETGKEVMELLRELNKEAGTTIVVVTHDPELAEYADRIIELRDGKI 218
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
276-496 |
6.00e-48 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 173.07 E-value: 6.00e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 276 AIEARGLTMRFGNFVAVDHVNFRIARGEIFGFLGSNGCGKSTTMKMLTGLLPASEGEAWLFGQPVDPKDIATRQRVGYMS 355
Cdd:PRK13537 7 PIDFRNVEKRYGDKLVVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCGEPVPSRARHARQRVGVVP 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 356 QAFSLYSELSVRQNLELHARLFHIPDDEIAHRVAEMSERFMLTEVKDALPADLPLGIRQRLSLAVAVIHRPEMLILDEPT 435
Cdd:PRK13537 87 QFDNLDPDFTVRENLLVFGRYFGLSAAAARALVPPLLEFAKLENKADAKVGELSGGMKRRLTLARALVNDPDVLVLDEPT 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1820369315 436 SGVDPVARDMFWQLMVDLARQDRvTIFISTHFMNEAER-CDRISLMHAGKVLASDTPQALVE 496
Cdd:PRK13537 167 TGLDPQARHLMWERLRSLLARGK-TILLTTHFMEEAERlCDRLCVIEEGRKIAEGAPHALIE 227
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
274-483 |
1.95e-47 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 169.89 E-value: 1.95e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 274 EIAIEARGLTMRF----GNFVAVDHVNFRIARGEIFGFLGSNGCGKSTTMKMLTGLLPASEGEAWLFGQPVDpkdiATRQ 349
Cdd:COG1116 5 APALELRGVSKRFptggGGVTALDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPTSGEVLVDGKPVT----GPGP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 350 RVGYMSQAFSLYSELSVRQNLELHARLFHIPDDEIAHRVAEMSERFMLTEVKDALPADLPLGIRQRLSLAVAVIHRPEML 429
Cdd:COG1116 81 DRGVVFQEPALLPWLTVLDNVALGLELRGVPKAERRERARELLELVGLAGFEDAYPHQLSGGMRQRVAIARALANDPEVL 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1820369315 430 ILDEPTSGVDPVARDMFWQLMVDLARQDRVTIFISTHFMNEAER-CDRISLMHAG 483
Cdd:COG1116 161 LMDEPFGALDALTRERLQDELLRLWQETGKTVLFVTHDVDEAVFlADRVVVLSAR 215
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
277-493 |
9.49e-47 |
|
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: 167.23 E-value: 9.49e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 277 IEARGLTMRFGNFVAVDHVNFRIARGEIFGFLGSNGCGKSTTMKMLTGLLPASEGEAWLFGQPVD--PKDIATRQRVGYM 354
Cdd:cd03219 1 LEVRGLTKRFGGLVALDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFDGEDITglPPHEIARLGIGRT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 355 SQAFSLYSELSVRQNLEL--HARLFHIP--------DDEIAHRVAEMSERFMLTEVKDALPADLPLGIRQRLSLAVAVIH 424
Cdd:cd03219 81 FQIPRLFPELTVLENVMVaaQARTGSGLllararreEREARERAEELLERVGLADLADRPAGELSYGQQRRLEIARALAT 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 425 RPEMLILDEPTSGVDPVARDMFWQLMVDLARQDRVTIFIStHFMNEAER-CDRISLMHAGKVLASDTPQA 493
Cdd:cd03219 161 DPKLLLLDEPAAGLNPEETEELAELIRELRERGITVLLVE-HDMDVVMSlADRVTVLDQGRVIAEGTPDE 229
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
274-487 |
1.05e-45 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 163.68 E-value: 1.05e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 274 EIAIEARGLTMRFGN----FVAVDHVNFRIARGEIFGFLGSNGCGKSTTMKMLTGLLPASEGEAWLFGQPV---DPKDIA 346
Cdd:COG1136 2 SPLLELRNLTKSYGTgegeVTALRGVSLSIEAGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVLIDGQDIsslSERELA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 347 T--RQRVGYMSQAFSLYSELSVRQNLELHARLFHIPDDEIAHRVAEMSERFMLTEVKDALPADLPLGIRQRLSLAVAVIH 424
Cdd:COG1136 82 RlrRRHIGFVFQFFNLLPELTALENVALPLLLAGVSRKERRERARELLERVGLGDRLDHRPSQLSGGQQQRVAIARALVN 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1820369315 425 RPEMLILDEPTSGVDPVARDMFWQLMVDLARQDRVTIFISTHFMNEAERCDRISLMHAGKVLA 487
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 ... |
278-484 |
2.03e-45 |
|
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: 162.25 E-value: 2.03e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 278 EARGLTMRFGNF--VAVDHVNFRIARGEIFGFLGSNGCGKSTTMKMLTGLLPASEGEAWLFGQPVDPKDIAT-RQRVGYM 354
Cdd:cd03225 1 ELKNLSFSYPDGarPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDLTKLSLKElRRKVGLV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 355 SQ-AFSLYSELSVRQNLELHARLFHIPDDEIAHRVAEMSERFMLTEVKDALPADLPLGIRQRLSLAVAVIHRPEMLILDE 433
Cdd:cd03225 81 FQnPDDQFFGPTVEEEVAFGLENLGLPEEEIEERVEEALELVGLEGLRDRSPFTLSGGQKQRVAIAGVLAMDPDILLLDE 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1820369315 434 PTSGVDPVARDMFWQLMVDLARQdRVTIFISTHFMNEAER-CDRISLMHAGK 484
Cdd:cd03225 161 PTAGLDPAGRRELLELLKKLKAE-GKTIIIVTHDLDLLLElADRVIVLEDGK 211
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
15-272 |
2.39e-45 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 165.28 E-value: 2.39e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 15 LENVGQQYGATIALRDISLAIPARRMVGLIGPDGVGKSSLLSLIAGARAIEQGNVMVLGGDMRDVHHRRdvcpkIAWMPQ 94
Cdd:COG4152 4 LKGLTKRFGDKTAVDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDSGEVLWDGEPLDPEDRRR-----IGYLPE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 95 GLGknLYHTLSVYENVDFFARLFGHDKAERELRINELLQSTGLAPFRDRPAGKLSGGMKQKLGLCCALIHDPQLLILDEP 174
Cdd:COG4152 79 ERG--LYPKMKVGEQLVYLARLKGLSKAEAKRRADEWLERLGLGDRANKKVEELSKGNQQKVQLIAALLHDPELLILDEP 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 175 TTGVDPLSRAQFWELIdsIRQRQPEMSVLVATAYMEEAERF-DWLVAMNAGEVLATGSAAELKAQTGSQTLEQAFIALLP 253
Cdd:COG4152 157 FSGLDPVNVELLKDVI--RELAAKGTTVIFSSHQMELVEELcDRIVIINKGRKVLSGSVDEIRRQFGRNTLRLEADGDAG 234
|
250
....*....|....*....
gi 1820369315 254 EAQRQAHKTVVIPPRDSRE 272
Cdd:COG4152 235 WLRALPGVTVVEEDGDGAE 253
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
276-497 |
2.68e-45 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 166.81 E-value: 2.68e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 276 AIEARGLTMRFGNFVAVDHVNFRIARGEIFGFLGSNGCGKSTTMKMLTGLLPASEGEAWLFGQPVDpkDIATRQR-VGYM 354
Cdd:COG3842 5 ALELENVSKRYGDVTALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRILLDGRDVT--GLPPEKRnVGMV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 355 SQAFSLYSELSVRQNLELHARLFHIPDDEIAHRVAEMSERFMLTEVKDALPADLPLGIRQRLSLAVAVIHRPEMLILDEP 434
Cdd:COG3842 83 FQDYALFPHLTVAENVAFGLRMRGVPKAEIRARVAELLELVGLEGLADRYPHQLSGGQQQRVALARALAPEPRVLLLDEP 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1820369315 435 TSGVDPVARDmfwQLMVDLAR-QDRV---TIFIsTHFMNEAER-CDRISLMHAGKVLASDTPQALVEQ 497
Cdd:COG3842 163 LSALDAKLRE---EMREELRRlQRELgitFIYV-THDQEEALAlADRIAVMNDGRIEQVGTPEEIYER 226
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
15-235 |
2.93e-45 |
|
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: 162.50 E-value: 2.93e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 15 LENVGQQY-GATIALRDISLAIPARRMVGLIGPDGVGKSSLLSLIAGARAIEQGNVMVLGGDMRDvHHRRDVCPKIAWMP 93
Cdd:COG1122 3 LENLSFSYpGGTPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVDGKDITK-KNLRELRRKVGLVF 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 94 QglgkN----LYHTlSVYENVDFFARLFGHDKAERELRINELLQSTGLAPFRDRPAGKLSGGMKQKLGLCCALIHDPQLL 169
Cdd:COG1122 82 Q----NpddqLFAP-TVEEDVAFGPENLGLPREEIRERVEEALELVGLEHLADRPPHELSGGQKQRVAIAGVLAMEPEVL 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1820369315 170 ILDEPTTGVDPLSRAQFWELIDSIRQRQpeMSVLVATAYMEEAER-FDWLVAMNAGEVLATGSAAEL 235
Cdd:COG1122 157 VLDEPTAGLDPRGRRELLELLKRLNKEG--KTVIIVTHDLDLVAElADRVIVLDDGRIVADGTPREV 221
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
277-487 |
3.32e-45 |
|
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: 162.26 E-value: 3.32e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 277 IEARGLTMRFGN----FVAVDHVNFRIARGEIFGFLGSNGCGKSTTMKMLTGLLPASEGEAWLFGQPVDPkdiaTRQRVG 352
Cdd:cd03293 1 LEVRNVSKTYGGgggaVTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVDGEPVTG----PGPDRG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 353 YMSQAFSLYSELSVRQNLELHARLFHIPDDEIAHRVAEMSERFMLTEVKDALPADLPLGIRQRLSLAVAVIHRPEMLILD 432
Cdd:cd03293 77 YVFQQDALLPWLTVLDNVALGLELQGVPKAEARERAEELLELVGLSGFENAYPHQLSGGMRQRVALARALAVDPDVLLLD 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1820369315 433 EPTSGVDPVARDMFWQLMVDLARQDRVTIFISTHFMNEAER-CDRISLMHA--GKVLA 487
Cdd:cd03293 157 EPFSALDALTREQLQEELLDIWRETGKTVLLVTHDIDEAVFlADRVVVLSArpGRIVA 214
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
272-496 |
5.46e-45 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 169.82 E-value: 5.46e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 272 EEEIAIEARGLTMRFGNFVAVDHVNFRIARGEIFGFLGSNGCGKSTTMKMLTGLLPASEGEAWLFGQPV---DPKDiATR 348
Cdd:COG3845 1 MMPPALELRGITKRFGGVVANDDVSLTVRPGEIHALLGENGAGKSTLMKILYGLYQPDSGEILIDGKPVrirSPRD-AIA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 349 QRVGYMSQAFSLYSELSVRQNLEL---HARLFHIPDDEIAHRVAEMSERFMLtEVK-DALPADLPLGIRQRLSLAVAVIH 424
Cdd:COG3845 80 LGIGMVHQHFMLVPNLTVAENIVLglePTKGGRLDRKAARARIRELSERYGL-DVDpDAKVEDLSVGEQQRVEILKALYR 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1820369315 425 RPEMLILDEPTSGVDPVARDMFWQLMVDLARQDRVTIFIsTHFMNEAER-CDRISLMHAGKV-----LASDTPQALVE 496
Cdd:COG3845 159 GARILILDEPTAVLTPQEADELFEILRRLAAEGKSIIFI-THKLREVMAiADRVTVLRRGKVvgtvdTAETSEEELAE 235
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
15-230 |
1.65e-44 |
|
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: 159.67 E-value: 1.65e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 15 LENVGQQYGATIALRDISLAIPARrMVGLIGPDGVGKSSLLSLIAGARAIEQGNVMVLGGDMRDvhHRRDVCPKIAWMPQ 94
Cdd:cd03264 3 LENLTKRYGKKRALDGVSLTLGPG-MYGLLGPNGAGKTTLMRILATLTPPSSGTIRIDGQDVLK--QPQKLRRRIGYLPQ 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 95 GLGknLYHTLSVYENVDFFARLFGHDKAERELRINELLQSTGLAPFRDRPAGKLSGGMKQKLGLCCALIHDPQLLILDEP 174
Cdd:cd03264 80 EFG--VYPNFTVREFLDYIAWLKGIPSKEVKARVDEVLELVNLGDRAKKKIGSLSGGMRRRVGIAQALVGDPSILIVDEP 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1820369315 175 TTGVDPLSRAQFWELIDSIRQrqpEMSVLVATAYMEEAERF-DWLVAMNAGEVLATG 230
Cdd:cd03264 158 TAGLDPEERIRFRNLLSELGE---DRIVILSTHIVEDVESLcNQVAVLNKGKLVFEG 211
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
277-487 |
2.37e-44 |
|
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: 159.61 E-value: 2.37e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 277 IEARGLTMRFGNFVAVDHVNFRIARGEIFGFLGSNGCGKSTTMKMLTGLLPASEGEAWLFGQPVdpKDIATRQR-VGYMS 355
Cdd:cd03259 1 LELKGLSKTYGSVRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDGRDV--TGVPPERRnIGMVF 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 356 QAFSLYSELSVRQNLELHARLFHIPDDEIAHRVAEMSERFMLTEVKDALPADLPLGIRQRLSLAVAVIHRPEMLILDEPT 435
Cdd:cd03259 79 QDYALFPHLTVAENIAFGLKLRGVPKAEIRARVRELLELVGLEGLLNRYPHELSGGQQQRVALARALAREPSLLLLDEPL 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1820369315 436 SGVDPVARDMFWQLMVDLARQDRVTIFISTHFMNEAER-CDRISLMHAGKVLA 487
Cdd:cd03259 159 SALDAKLREELREELKELQRELGITTIYVTHDQEEALAlADRIAVMNEGRIVQ 211
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
15-435 |
1.57e-43 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 166.01 E-value: 1.57e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 15 LENVGQQYGATIALRDISLAIPARRMVGLIGPDGVGKSSLLSLIAGARAIEQGNVMVlggdmrdvhhRRDVcpKIAWMPQ 94
Cdd:COG0488 1 LENLSKSFGGRPLLDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEVSI----------PKGL--RIGYLPQ 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 95 GLgkNLYHTLSVYENV-----------------------------------DFFARLFGHDkAERelRINELLQSTGLAP 139
Cdd:COG0488 69 EP--PLDDDLTVLDTVldgdaelraleaeleeleaklaepdedlerlaelqEEFEALGGWE-AEA--RAEEILSGLGFPE 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 140 F-RDRPAGKLSGGMKQKLGLCCALIHDPQLLILDEPTTGVDplsraqfwelIDSI-------RQRqpEMSVL-------- 203
Cdd:COG0488 144 EdLDRPVSELSGGWRRRVALARALLSEPDLLLLDEPTNHLD----------LESIewleeflKNY--PGTVLvvshdryf 211
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 204 ---VAT------------------AYMEE-AERFDWLVAMNAgevlatgSAAELKAQtgsqtlEQAFIALLPEAQRQAHK 261
Cdd:COG0488 212 ldrVATrileldrgkltlypgnysAYLEQrAERLEQEAAAYA-------KQQKKIAK------EEEFIRRFRAKARKAKQ 278
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 262 ------------TVVIPPRDSREE----------EIAIEARGLTMRFGNFVAVDHVNFRIARGEIFGFLGSNGCGKSTTM 319
Cdd:COG0488 279 aqsrikalekleREEPPRRDKTVEirfppperlgKKVLELEGLSKSYGDKTLLDDLSLRIDRGDRIGLIGPNGAGKSTLL 358
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 320 KMLTGLLPASEGEAwlfgqpvdpkDIATRQRVGYMSQAF-SLYSELSVRQNLELHArlfhiPDDEIAHrVAEMSERFM-- 396
Cdd:COG0488 359 KLLAGELEPDSGTV----------KLGETVKIGYFDQHQeELDPDKTVLDELRDGA-----PGGTEQE-VRGYLGRFLfs 422
|
490 500 510 520
....*....|....*....|....*....|....*....|....*
gi 1820369315 397 ----LTEVKDalpadlpL--GIRQRLSLAVAVIHRPEMLILDEPT 435
Cdd:COG0488 423 gddaFKPVGV-------LsgGEKARLALAKLLLSPPNVLLLDEPT 460
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
276-507 |
2.59e-43 |
|
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: 157.90 E-value: 2.59e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 276 AIEARGLTMRFGNFVAVDHVNFRIARGEIFGFLGSNGCGKSTTMKMLTGLLPASEGEAWLFGQPV---DPKDIAtrQRVG 352
Cdd:COG1120 1 MLEAENLSVGYGGRPVLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDGRDLaslSRRELA--RRIA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 353 YMSQAFSLYSELSVRQNLEL----HARLFHIPDDEIAHRVAEMSERFMLTEVKDALPADLPLGIRQRLSLAVAVIHRPEM 428
Cdd:COG1120 79 YVPQEPPAPFGLTVRELVALgrypHLGLFGRPSAEDREAVEEALERTGLEHLADRPVDELSGGERQRVLIARALAQEPPL 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 429 LILDEPTSGVDPVARDMFWQLMVDLARQDRVTIFISTHFMNEAER-CDRISLMHAGKVLASDTPQALVEqrgAASLEEAF 507
Cdd:COG1120 159 LLLDEPTSHLDLAHQLEVLELLRRLARERGRTVVMVLHDLNLAARyADRLVLLKDGRIVAQGPPEEVLT---PELLEEVY 235
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
15-225 |
2.92e-43 |
|
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: 156.09 E-value: 2.92e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 15 LENVGQQY--GATIALRDISLAIPARRMVGLIGPDGVGKSSLLSLIAGARAIEQGNVMVLGGDMRDvHHRRDVCPKIAWM 92
Cdd:cd03225 2 LKNLSFSYpdGARPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDLTK-LSLKELRRKVGLV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 93 PQglgkNLYH---TLSVYENVDFFARLFGHDKAERELRINELLQSTGLAPFRDRPAGKLSGGMKQKLGLCCALIHDPQLL 169
Cdd:cd03225 81 FQ----NPDDqffGPTVEEEVAFGLENLGLPEEEIEERVEEALELVGLEGLRDRSPFTLSGGQKQRVAIAGVLAMDPDIL 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1820369315 170 ILDEPTTGVDPLSRAQFWELIDSIRQRQpeMSVLVATAYMEEAERF-DWLVAMNAGE 225
Cdd:cd03225 157 LLDEPTAGLDPAGRRELLELLKKLKAEG--KTIIIVTHDLDLLLELaDRVIVLEDGK 211
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
291-500 |
6.38e-43 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 159.10 E-value: 6.38e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 291 AVDHVNFRIARGEIFGFLGSNGCGKSTTMKMLTGLLPASEGEAWLFGqpVDPkdiaTRQRVGYM----------SQafsL 360
Cdd:COG4586 37 AVDDISFTIEPGEIVGFIGPNGAGKSTTIKMLTGILVPTSGEVRVLG--YVP----FKRRKEFArrigvvfgqrSQ---L 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 361 YSELSVRQNLELHARLFHIPDDEIAHRVAEMSERFmltEVKDAL--PA-DLPLGIRQRLSLAVAVIHRPEMLILDEPTSG 437
Cdd:COG4586 108 WWDLPAIDSFRLLKAIYRIPDAEYKKRLDELVELL---DLGELLdtPVrQLSLGQRMRCELAAALLHRPKILFLDEPTIG 184
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1820369315 438 VDPVARDMFWQLMVDLARQDRVTIFISTHFMNEAER-CDRISLMHAGKVLASDTPQALVEQRGA 500
Cdd:COG4586 185 LDVVSKEAIREFLKEYNRERGTTILLTSHDMDDIEAlCDRVIVIDHGRIIYDGSLEELKERFGP 248
|
|
| YadH |
COG0842 |
ABC-type multidrug transport system, permease component [Defense mechanisms]; |
716-896 |
1.44e-42 |
|
ABC-type multidrug transport system, permease component [Defense mechanisms];
Pssm-ID: 440604 [Multi-domain] Cd Length: 200 Bit Score: 153.82 E-value: 1.44e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 716 SLPAIVPAVIPLLLMMIPAMLSALSVVREKELGSIINLYVTPTTRSEFLLGKQLPYIVLGMFNFFLLCALSVFVFGVAHK 795
Cdd:COG0842 1 YLAFLVPGLLAMSLLFTALMLTALSIAREREQGTLERLLVTPVSRLEILLGKVLAYLLRGLLQALLVLLVALLFFGVPLR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 796 G-SFLTLTLAALLYVTIATGLGLLISTFMKSQIAAIFGTAIItLIPATQFSGMIDPVASLEGPGRWIGQIYPTSHFLTIA 874
Cdd:COG0842 81 GlSLLLLLLVLLLFALAFSGLGLLISTLARSQEQASAISNLV-ILPLTFLSGAFFPIESLPGWLQAIAYLNPLTYFVEAL 159
|
170 180
....*....|....*....|..
gi 1820369315 875 RGTFSKALNLSDLWGSFIPLLI 896
Cdd:COG0842 160 RALFLGGAGLADVWPSLLVLLA 181
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
8-248 |
5.38e-42 |
|
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: 5.38e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 8 TSPPIALLENVGQQYGATIALRDISLAIPARRMVGLIGPDGVGKSSLLSLIAGARAIEQGNVMVLGGDMRDVHHRrdvcp 87
Cdd:COG1121 2 MMMPAIELENLTVSYGGRPVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLFGKPPRRARRR----- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 88 kIAWMPQGLGKNLYHTLSVYENVD--------FFARLfghDKAERElRINELLQSTGLAPFRDRPAGKLSGGMKQKLGLC 159
Cdd:COG1121 77 -IGYVPQRAEVDWDFPITVRDVVLmgrygrrgLFRRP---SRADRE-AVDEALERVGLEDLADRPIGELSGGQQQRVLLA 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 160 CALIHDPQLLILDEPTTGVDPLSRAQFWELIDSIRQRQpeMSVLVATAYMEEAER-FDWLVAMNaGEVLATGSAAELKAq 238
Cdd:COG1121 152 RALAQDPDLLLLDEPFAGVDAATEEALYELLRELRREG--KTILVVTHDLGAVREyFDRVLLLN-RGLVAHGPPEEVLT- 227
|
250
....*....|
gi 1820369315 239 tgSQTLEQAF 248
Cdd:COG1121 228 --PENLSRAY 235
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
277-479 |
5.51e-42 |
|
ABC-type transport system involved in cytochrome c biogenesis, ATPase component [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 443308 [Multi-domain] Cd Length: 206 Bit Score: 152.25 E-value: 5.51e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 277 IEARGLTMRFGNFVAVDHVNFRIARGEIFGFLGSNGCGKSTTMKMLTGLLPASEGEAWLFGQPVDPKDIATRQRVGYMSQ 356
Cdd:COG4133 3 LEAENLSCRRGERLLFSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWNGEPIRDAREDYRRRLAYLGH 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 357 AFSLYSELSVRQNLELHARLFHIPDDEIahRVAEMSERFMLTEVKDALPADLPLGIRQRLSLAVAVIHRPEMLILDEPTS 436
Cdd:COG4133 83 ADGLKPELTVRENLRFWAALYGLRADRE--AIDEALEAVGLAGLADLPVRQLSAGQKRRVALARLLLSPAPLWLLDEPFT 160
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1820369315 437 GVDPVARDMFWQLMVDLARQDRvTIFISTHFMNEAERCDRISL 479
Cdd:COG4133 161 ALDAAGVALLAELIAAHLARGG-AVLLTTHQPLELAAARVLDL 202
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
15-497 |
5.73e-42 |
|
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: 161.51 E-value: 5.73e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 15 LENVGQQYGATIALRDISLAIPARRMVGLIGPDGVGKSSLLSLIAGARAIE--QGNVM---------------------- 70
Cdd:TIGR03269 3 VKNLTKKFDGKEVLKNISFTIEEGEVLGILGRSGAGKSVLMHVLRGMDQYEptSGRIIyhvalcekcgyverpskvgepc 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 71 -VLGGDMR---------DVHHRRDVCPKIAWMPQGLGKnLYHTLSVYENVDFFARLFGHDKAERELRINELLQSTGLAPF 140
Cdd:TIGR03269 83 pVCGGTLEpeevdfwnlSDKLRRRIRKRIAIMLQRTFA-LYGDDTVLDNVLEALEEIGYEGKEAVGRAVDLIEMVQLSHR 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 141 RDRPAGKLSGGMKQKLGLCCALIHDPQLLILDEPTTGVDPlsraQFWELI-DSIRQ--RQPEMSVLVATAYMEEAERF-D 216
Cdd:TIGR03269 162 ITHIARDLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDP----QTAKLVhNALEEavKASGISMVLTSHWPEVIEDLsD 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 217 WLVAMNAGEVLATGSAAELKAQtgsqtleqaFIALLPEAQRQAHKTV---VIPPRDSREEEIAIEaRGLTMrfgnfvAVD 293
Cdd:TIGR03269 238 KAIWLENGEIKEEGTPDEVVAV---------FMEGVSEVEKECEVEVgepIIKVRNVSKRYISVD-RGVVK------AVD 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 294 HVNFRIARGEIFGFLGSNGCGKSTTMKMLTGLLPASEGEAW-LFGQP-VDPKDIATRQR------VGYMSQAFSLYSELS 365
Cdd:TIGR03269 302 NVSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGEVNvRVGDEwVDMTKPGPDGRgrakryIGILHQEYDLYPHRT 381
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 366 VRQNLElHARLFHIPdDEIAHR-------VAEMSERFMlTEVKDALPADLPLGIRQRLSLAVAVIHRPEMLILDEPTSGV 438
Cdd:TIGR03269 382 VLDNLT-EAIGLELP-DELARMkavitlkMVGFDEEKA-EEILDKYPDELSEGERHRVALAQVLIKEPRIVILDEPTGTM 458
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 439 DPVARDMFWQLMVDLARQDRVTIFISTHFMNEA-ERCDRISLMHAGKVLASDTPQALVEQ 497
Cdd:TIGR03269 459 DPITKVDVTHSILKAREEMEQTFIIVSHDMDFVlDVCDRAALMRDGKIVKIGDPEEIVEE 518
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
19-497 |
1.08e-41 |
|
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: 161.01 E-value: 1.08e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 19 GQQYGATIALRDISLAIPARRMVGLIGPDGVGKS----SLLSLIAGARAIEQGNVMVLGGD--------MRDVHHRRdvc 86
Cdd:COG4172 17 GQGGGTVEAVKGVSFDIAAGETLALVGESGSGKSvtalSILRLLPDPAAHPSGSILFDGQDllglsereLRRIRGNR--- 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 87 pkIAwM----------P-QGLGKNLYHTLSVYEnvdffarlfGHDKAERELRINELLQSTGLapfrDRPAGK-------L 148
Cdd:COG4172 94 --IA-MifqepmtslnPlHTIGKQIAEVLRLHR---------GLSGAAARARALELLERVGI----PDPERRldayphqL 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 149 SGGMKQKLGLCCALIHDPQLLILDEPTTGVDPLSRAQFWELIDSIRQRQpEMSVLVATAYMEEAERF-DWLVAMNAGEVL 227
Cdd:COG4172 158 SGGQRQRVMIAMALANEPDLLIADEPTTALDVTVQAQILDLLKDLQREL-GMALLLITHDLGVVRRFaDRVAVMRQGEIV 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 228 ATGSAAELKAQ-----TgsqtleQAFIALLPEAQrqahktvviPPRDSREEEIAIEARGLTMRF-----------GNFVA 291
Cdd:COG4172 237 EQGPTAELFAApqhpyT------RKLLAAEPRGD---------PRPVPPDAPPLLEARDLKVWFpikrglfrrtvGHVKA 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 292 VDHVNFRIARGEIFGFLGSNGCGKSTTMKMLTGLLPaSEGEAWLFGQPVDPKD----IATRQRVgymsQA-F-----SLY 361
Cdd:COG4172 302 VDGVSLTLRRGETLGLVGESGSGKSTLGLALLRLIP-SEGEIRFDGQDLDGLSrralRPLRRRM----QVvFqdpfgSLS 376
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 362 SELSVRQ----NLELHARlfHIPDDEIAHRVAEmserfMLTEVkdALPADLPL--------GIRQRLSLAVAVIHRPEML 429
Cdd:COG4172 377 PRMTVGQiiaeGLRVHGP--GLSAAERRARVAE-----ALEEV--GLDPAARHryphefsgGQRQRIAIARALILEPKLL 447
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 430 ILDEPTSgvdpvARDMFWQ-----LMVDLARQDRVT-IFIStH------FMneaerCDRISLMHAGKVlasdtpqalVEQ 497
Cdd:COG4172 448 VLDEPTS-----ALDVSVQaqildLLRDLQREHGLAyLFIS-HdlavvrAL-----AHRVMVMKDGKV---------VEQ 507
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
276-497 |
1.12e-41 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 156.39 E-value: 1.12e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 276 AIEARGLTMRFGNFVAVDHVNFRIARGEIFGFLGSNGCGKSTTMKMLTGLLPASEGEAWLFGQPVDpkDIATRQR-VGYM 354
Cdd:COG3839 3 SLELENVSKSYGGVEALKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAGLEDPTSGEILIGGRDVT--DLPPKDRnIAMV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 355 SQAFSLYSELSVRQNLELHARLFHIPDDEIAHRVAEMSERFMLTEVKDALPADLPLGIRQRLSLAVAVIHRPEMLILDEP 434
Cdd:COG3839 81 FQSYALYPHMTVYENIAFPLKLRKVPKAEIDRRVREAAELLGLEDLLDRKPKQLSGGQRQRVALGRALVREPKVFLLDEP 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1820369315 435 TSGVDPVARdmfWQLMVDLAR-QDR--VTIFISTHFMNEAER-CDRISLMHAGKVLASDTPQALVEQ 497
Cdd:COG3839 161 LSNLDAKLR---VEMRAEIKRlHRRlgTTTIYVTHDQVEAMTlADRIAVMNDGRIQQVGTPEELYDR 224
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
277-484 |
1.24e-41 |
|
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is comprised of all BPD (Binding Protein Dependent) systems that are largely represented in archaea and eubacteria and are primarily involved in scavenging solutes from the environment. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213196 [Multi-domain] Cd Length: 178 Bit Score: 150.42 E-value: 1.24e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 277 IEARGLTMRFGNFVAVDHVNFRIARGEIFGFLGSNGCGKSTTMKMLTGLLPASEGEAWLFGQPVDPKDIAT---RQRVGY 353
Cdd:cd03229 1 LELKNVSKRYGQKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGEDLTDLEDELpplRRRIGM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 354 MSQAFSLYSELSVRQNLElharlfhipddeiahrvaemserfmltevkdalpadLPL--GIRQRLSLAVAVIHRPEMLIL 431
Cdd:cd03229 81 VFQDFALFPHLTVLENIA------------------------------------LGLsgGQQQRVALARALAMDPDVLLL 124
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1820369315 432 DEPTSGVDPVARDMFWQLMVDLARQDRVTIFISTHFMNEAER-CDRISLMHAGK 484
Cdd:cd03229 125 DEPTSALDPITRREVRALLKSLQAQLGITVVLVTHDLDEAARlADRVVVLRDGK 178
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
15-206 |
2.60e-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: 150.32 E-value: 2.60e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 15 LENVGQQYGATIALRDISLAIPARRMVGLIGPDGVGKSSLLSLIAGARAIEQGNVMVLGGDMRDvhHRRDVCPKIAWMPQ 94
Cdd:COG4133 5 AENLSCRRGERLLFSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWNGEPIRD--AREDYRRRLAYLGH 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 95 GLGknLYHTLSVYENVDFFARLFGHDKAERelRINELLQSTGLAPFRDRPAGKLSGGMKQKLGLCCALIHDPQLLILDEP 174
Cdd:COG4133 83 ADG--LKPELTVRENLRFWAALYGLRADRE--AIDEALEAVGLAGLADLPVRQLSAGQKRRVALARLLLSPAPLWLLDEP 158
|
170 180 190
....*....|....*....|....*....|..
gi 1820369315 175 TTGVDPLSRAQFWELIDSIRQRQpeMSVLVAT 206
Cdd:COG4133 159 FTALDAAGVALLAELIAAHLARG--GAVLLTT 188
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
277-496 |
5.19e-41 |
|
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: 150.39 E-value: 5.19e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 277 IEARGLTMRFGNFVAVDHVNFRIARGEIFGFLGSNGCGKSTTMKMLTGLLPASEGEAWLFGQPVDPKDIATRQR--VGYM 354
Cdd:cd03218 1 LRAENLSKRYGKRKVVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDGQDITKLPMHKRARlgIGYL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 355 SQAFSLYSELSVRQNLELHARLFHIPDDEIAHRVAEMSERFMLTEVKDALPADLPLGIRQRLSLAVAVIHRPEMLILDEP 434
Cdd:cd03218 81 PQEASIFRKLTVEENILAVLEIRGLSKKEREEKLEELLEEFHITHLRKSKASSLSGGERRRVEIARALATNPKFLLLDEP 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1820369315 435 TSGVDPVA-RDMfwQLMVDLARQDRVTIFISTHFMNEA-ERCDRISLMHAGKVLASDTPQALVE 496
Cdd:cd03218 161 FAGVDPIAvQDI--QKIIKILKDRGIGVLITDHNVRETlSITDRAYIIYEGKVLAEGTPEEIAA 222
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
15-230 |
5.96e-41 |
|
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: 149.74 E-value: 5.96e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 15 LENVGQQYGATIALRDISLAIPARRMVGLIGPDGVGKSSLLSLIAGARAIEQGNVMVLGGDMRDVHHRRdvcpkIAWMPQ 94
Cdd:cd03269 3 VENVTKRFGRVTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDGKPLDIAARNR-----IGYLPE 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 95 GLGknLYHTLSVYENVDFFARLFGHDKAERELRINELLQSTGLAPFRDRPAGKLSGGMKQKLGLCCALIHDPQLLILDEP 174
Cdd:cd03269 78 ERG--LYPKMKVIDQLVYLAQLKGLKKEEARRRIDEWLERLELSEYANKRVEELSKGNQQKVQFIAAVIHDPELLILDEP 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1820369315 175 TTGVDPLSRAQFWELIDSIRQRqpEMSVLVATAYMEEAERF-DWLVAMNAGEVLATG 230
Cdd:cd03269 156 FSGLDPVNVELLKDVIRELARA--GKTVILSTHQMELVEELcDRVLLLNKGRAVLYG 210
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
268-489 |
9.10e-41 |
|
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; NatA is the ATPase component of a bacterial ABC-type Na+ transport system called NatAB, which catalyzes ATP-dependent electrogenic Na+ extrusion without mechanically coupled to proton or K+ uptake. NatB possess six putative membrane spanning regions at its C-terminus. In B. subtilis, NatAB is inducible by agents such as ethanol and protonophores, which lower the proton-motive force across the membrane. The closest sequence similarity to NatA is exhibited by DrrA of the two-component daunorubicin- and doxorubicin-efflux system. Hence, the functional NatAB is presumably assembled with two copies of the single ATP-binding protein and the single integral membrane protein.
Pssm-ID: 213234 [Multi-domain] Cd Length: 236 Bit Score: 150.18 E-value: 9.10e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 268 RDSREEEIAIEARGLTMR-FGNFVAVDHVNFRIARGEIFGFLGSNGCGKSTTMKMLTGLLPASEGEAWLFGQ-PVDPKDI 345
Cdd:cd03267 12 VYSKEPGLIGSLKSLFKRkYREVEALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRVAGLvPWKRRKK 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 346 ATRQRVGYMSQAFSLYSELSVRQNLELHARLFHIPDDEIAHRVAEMSERFMLTEVKDALPADLPLGIRQRLSLAVAVIHR 425
Cdd:cd03267 92 FLRRIGVVFGQKTQLWWDLPVIDSFYLLAAIYDLPPARFKKRLDELSELLDLEELLDTPVRQLSLGQRMRAEIAAALLHE 171
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1820369315 426 PEMLILDEPTSGVDPVARDMFWQLMVDLARQDRVTIFISTHFMNEAER-CDRISLMHAGKVLASD 489
Cdd:cd03267 172 PEILFLDEPTIGLDVVAQENIRNFLKEYNRERGTTVLLTSHYMKDIEAlARRVLVIDKGRLLYDG 236
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
15-230 |
9.45e-41 |
|
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: 149.22 E-value: 9.45e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 15 LENVGQQYGATIALRDISLAIPARRMVGLIGPDGVGKSSLLSLIAGARAIEQGNVMVLGGDMRDVHHRrdvcpkIAWMPQ 94
Cdd:cd03235 2 VEDLTVSYGGHPVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFGKPLEKERKR------IGYVPQ 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 95 GLGKNLYHTLSVYENV----DFFARLFGHDKAERELRINELLQSTGLAPFRDRPAGKLSGGMKQKLGLCCALIHDPQLLI 170
Cdd:cd03235 76 RRSIDRDFPISVRDVVlmglYGHKGLFRRLSKADKAKVDEALERVGLSELADRQIGELSGGQQQRVLLARALVQDPDLLL 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1820369315 171 LDEPTTGVDPLSRAQFWELIDSIRQRqpEMSVLVATAYMEEAER-FDWLVAMNaGEVLATG 230
Cdd:cd03235 156 LDEPFAGVDPKTQEDIYELLRELRRE--GMTILVVTHDLGLVLEyFDRVLLLN-RTVVASG 213
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
27-230 |
2.00e-40 |
|
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: 148.28 E-value: 2.00e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 27 ALRDISLAIPARRMVGLIGPDGVGKSSLLSLIAGARAIEQGNVMVLGGDMrdVHHRRDVCPKIAWMPQGLGknLYHTLSV 106
Cdd:cd03266 20 AVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDGFDV--VKEPAEARRRLGFVSDSTG--LYDRLTA 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 107 YENVDFFARLFGHDKAERELRINELLQSTGLAPFRDRPAGKLSGGMKQKLGLCCALIHDPQLLILDEPTTGVDPLSRAQF 186
Cdd:cd03266 96 RENLEYFAGLYGLKGDELTARLEELADRLGMEELLDRRVGGFSTGMRQKVAIARALVHDPPVLLLDEPTTGLDVMATRAL 175
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1820369315 187 WELIDsiRQRQPEMSVLVATAYMEEAERF-DWLVAMNAGEVLATG 230
Cdd:cd03266 176 REFIR--QLRALGKCILFSTHIMQEVERLcDRVVVLHRGRVVYEG 218
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
274-507 |
2.49e-40 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 149.08 E-value: 2.49e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 274 EIAIEARGLTMRFGNFVAVDHVNFRIARGEIFGFLGSNGCGKSTTMKMLTGLLPASEGEAWLFGQPVDPKdiatRQRVGY 353
Cdd:COG1121 4 MPAIELENLTVSYGGRPVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLFGKPPRRA----RRRIGY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 354 MSQAFSLYSE--LSVRQ----NLELHARLFHIPDDEIAHRVAEMSERFMLTEVKDALPADLPLGIRQRLSLAVAVIHRPE 427
Cdd:COG1121 80 VPQRAEVDWDfpITVRDvvlmGRYGRRGLFRRPSRADREAVDEALERVGLEDLADRPIGELSGGQQQRVLLARALAQDPD 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 428 MLILDEPTSGVDPVARDMFWQLMVDLARQDRvTIFISTHFMNEAER-CDRISLMhAGKVLASDTPQALVEQrgaASLEEA 506
Cdd:COG1121 160 LLLLDEPFAGVDAATEEALYELLRELRREGK-TILVVTHDLGAVREyFDRVLLL-NRGLVAHGPPEEVLTP---ENLSRA 234
|
.
gi 1820369315 507 F 507
Cdd:COG1121 235 Y 235
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
15-235 |
2.61e-40 |
|
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: 2.61e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 15 LENVGQQYGATIALRDISLAIPARRMVGLIGPDGVGKSSLLSLIAGARAIEQGNVMVLGgdmRDVHH--RRDVCPKIAWM 92
Cdd:COG1120 4 AENLSVGYGGRPVLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDG---RDLASlsRRELARRIAYV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 93 PQGLGKNLYhtLSVYENVDF----FARLFGHDKAERELRINELLQSTGLAPFRDRPAGKLSGGMKQKLGLCCALIHDPQL 168
Cdd:COG1120 81 PQEPPAPFG--LTVRELVALgrypHLGLFGRPSAEDREAVEEALERTGLEHLADRPVDELSGGERQRVLIARALAQEPPL 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1820369315 169 LILDEPTTGVDPLSRAQFWELIDSIRQRQPeMSVLVATAYMEEAERF-DWLVAMNAGEVLATGSAAEL 235
Cdd:COG1120 159 LLLDEPTSHLDLAHQLEVLELLRRLARERG-RTVVMVLHDLNLAARYaDRLVLLKDGRIVAQGPPEEV 225
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
278-489 |
4.19e-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: 147.29 E-value: 4.19e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 278 EARGLTMRFGNFVAVDHVNFRIARGEIFGFLGSNGCGKSTTMKMLTGLLPASEGEAWLFGQPVDPKdiatRQRVGYMSQA 357
Cdd:cd03235 1 EVEDLTVSYGGHPVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFGKPLEKE----RKRIGYVPQR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 358 FSL--YSELSVRQ----NLELHARLFHIPDDEIAHRVAEMSERFMLTEVKDALPADLPLGIRQRLSLAVAVIHRPEMLIL 431
Cdd:cd03235 77 RSIdrDFPISVRDvvlmGLYGHKGLFRRLSKADKAKVDEALERVGLSELADRQIGELSGGQQQRVLLARALVQDPDLLLL 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1820369315 432 DEPTSGVDPVARDMFWQLMVDLARQDRvTIFISTHFMNEAER-CDRISLMhAGKVLASD 489
Cdd:cd03235 157 DEPFAGVDPKTQEDIYELLRELRREGM-TILVVTHDLGLVLEyFDRVLLL-NRTVVASG 213
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
273-496 |
1.09e-39 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 154.02 E-value: 1.09e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 273 EEIAIEARGLTMRFGNFVAVDHVNFRIARGEIFGFLGSNGCGKSTTMKMLTGLLPASEGEAWLFGQPVDPKDI--ATRQR 350
Cdd:COG1129 1 AEPLLEMRGISKSFGGVKALDGVSLELRPGEVHALLGENGAGKSTLMKILSGVYQPDSGEILLDGEPVRFRSPrdAQAAG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 351 VGYMSQAFSLYSELSVRQNL----ELHARLFhIPDDEIAHRVAEMSERFMLTEVKDALPADLPLGIRQRLSLAVAVIHRP 426
Cdd:COG1129 81 IAIIHQELNLVPNLSVAENIflgrEPRRGGL-IDWRAMRRRARELLARLGLDIDPDTPVGDLSVAQQQLVEIARALSRDA 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1820369315 427 EMLILDEPTSGVDPVARDMFWQLMVDLARQDRVTIFIStHFMNEAER-CDRISLMHAGKVLASD-----TPQALVE 496
Cdd:COG1129 160 RVLILDEPTASLTEREVERLFRIIRRLKAQGVAIIYIS-HRLDEVFEiADRVTVLRDGRLVGTGpvaelTEDELVR 234
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
277-494 |
3.10e-39 |
|
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: 145.91 E-value: 3.10e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 277 IEARGLTMRFGN-FVAVDHVNFRIARGEIFGFLGSNGCGKSTTMKMLTGLLPASEGEAWLFGQPVDPKD-IATRQRVGYM 354
Cdd:cd03295 1 IEFENVTKRYGGgKKAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGEDIREQDpVELRRKIGYV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 355 SQAFSLYSELSVRQNLELHARLFHIPDDEIAHRVAEMSERFML--TEVKDALPADLPLGIRQRLSLAVAVIHRPEMLILD 432
Cdd:cd03295 81 IQQIGLFPHMTVEENIALVPKLLKWPKEKIRERADELLALVGLdpAEFADRYPHELSGGQQQRVGVARALAADPPLLLMD 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1820369315 433 EPTSGVDPVARDMFWQLMVDLARQDRVTIFISTHFMNEAER-CDRISLMHAGKVLASDTPQAL 494
Cdd:cd03295 161 EPFGALDPITRDQLQEEFKRLQQELGKTIVFVTHDIDEAFRlADRIAIMKNGEIVQVGTPDEI 223
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
15-230 |
6.85e-39 |
|
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is comprised of proteins involved in the transport of apparently unrelated solutes and proteins specific for di- and oligosaccharides and polyols. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213226 [Multi-domain] Cd Length: 213 Bit Score: 143.81 E-value: 6.85e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 15 LENVGQQYGATIALRDISLAIPARRMVGLIGPDGVGKSSLLSLIAGARAIEQGNVMVLGGDMRDVH-HRRDvcpkIAWMP 93
Cdd:cd03259 3 LKGLSKTYGSVRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDGRDVTGVPpERRN----IGMVF 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 94 QGLgkNLYHTLSVYENVDFFARLFGHDKAERELRINELLQSTGLAPFRDRPAGKLSGGMKQKLGLCCALIHDPQLLILDE 173
Cdd:cd03259 79 QDY--ALFPHLTVAENIAFGLKLRGVPKAEIRARVRELLELVGLEGLLNRYPHELSGGQQQRVALARALAREPSLLLLDE 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1820369315 174 PTTGVDPLSRAQFWELIDSIrQRQPEMSVLVATAYMEEAERF-DWLVAMNAGEVLATG 230
Cdd:cd03259 157 PLSALDAKLREELREELKEL-QRELGITTIYVTHDQEEALALaDRIAVMNEGRIVQVG 213
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
277-494 |
6.85e-39 |
|
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of fundamental importance in the cell physiology of bacteria because phosphate is required as a nutrient. The Pst system of E. coli comprises four distinct subunits encoded by the pstS, pstA, pstB, and pstC genes. The PstS protein is a phosphate-binding protein located in the periplasmic space. PstA and PstC are hydrophobic and they form the transmembrane portion of the Pst system. PstB is the catalytic subunit, which couples the energy of ATP hydrolysis to the import of phosphate across cellular membranes through the Pst system, often referred as ABC-protein. PstB belongs to one of the largest superfamilies of proteins characterized by a highly conserved adenosine triphosphate (ATP) binding cassette (ABC), which is also a nucleotide binding domain (NBD).
Pssm-ID: 213227 [Multi-domain] Cd Length: 227 Bit Score: 144.25 E-value: 6.85e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 277 IEARGLTMRFGNFVAVDHVNFRIARGEIFGFLGSNGCGKSTTMKMLTGLLPA-----SEGEAWLFGQPVDPKD---IATR 348
Cdd:cd03260 1 IELRDLNVYYGDKHALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRLNDLipgapDEGEVLLDGKDIYDLDvdvLELR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 349 QRVGYMSQAFSLYSeLSVRQNLELHARLFHI-PDDEIAHRVAEMSERFMLT-EVKDALPA-DLPLGIRQRLSLAVAVIHR 425
Cdd:cd03260 81 RRVGMVFQKPNPFP-GSIYDNVAYGLRLHGIkLKEELDERVEEALRKAALWdEVKDRLHAlGLSGGQQQRLCLARALANE 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 426 PEMLILDEPTSGVDPVARDMFWQLMVDLARqdRVTIFISTHFMNEAERC-DRISLMHAGKVLASDTPQAL 494
Cdd:cd03260 160 PEVLLLDEPTSALDPISTAKIEELIAELKK--EYTIVIVTHNMQQAARVaDRTAFLLNGRLVEFGPTEQI 227
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
277-466 |
6.99e-39 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 144.04 E-value: 6.99e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 277 IEARGLTMRFGN-FVAVDHVNFRIARGEiFGFL-GSNGCGKSTTMKMLTGLLPASEGEAWLFGQPV---DPKDIA-TRQR 350
Cdd:COG2884 2 IRFENVSKRYPGgREALSDVSLEIEKGE-FVFLtGPSGAGKSTLLKLLYGEERPTSGQVLVNGQDLsrlKRREIPyLRRR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 351 VGYMSQAFSLYSELSVRQNLELHARLFHIPDDEIAHRVAEMSERFMLTEVKDALPADLPLGIRQRLSLAVAVIHRPEMLI 430
Cdd:COG2884 81 IGVVFQDFRLLPDRTVYENVALPLRVTGKSRKEIRRRVREVLDLVGLSDKAKALPHELSGGEQQRVAIARALVNRPELLL 160
|
170 180 190
....*....|....*....|....*....|....*.
gi 1820369315 431 LDEPTSGVDPVARDMFWQLMVDLARQdRVTIFISTH 466
Cdd:COG2884 161 ADEPTGNLDPETSWEIMELLEEINRR-GTTVLIATH 195
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
276-496 |
7.31e-39 |
|
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid transport and metabolism, Inorganic ion transport and metabolism];
Pssm-ID: 440741 [Multi-domain] Cd Length: 248 Bit Score: 144.95 E-value: 7.31e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 276 AIEARGLTMRFG----NFVAVDHVNFRIARGEIFGFLGSNGCGKSTTMKMLTGLLPASEGEAWLFGQPVDPKDI-ATRQR 350
Cdd:COG1124 1 MLEVRNLSVSYGqggrRVPVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVTFDGRPVTRRRRkAFRRR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 351 VGYMSQ--AFSLYSELSVRQNLELHARLFHIPDDEiaHRVAEMSERFMLT-EVKDALPADLPLGIRQRLSLAVAVIHRPE 427
Cdd:COG1124 81 VQMVFQdpYASLHPRHTVDRILAEPLRIHGLPDRE--ERIAELLEQVGLPpSFLDRYPHQLSGGQRQRVAIARALILEPE 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 428 MLILDEPTSGVDPVARDMFWQLMVDLARQDRVTIFISTHFMNEAER-CDRISLMHAGKVLASDTPQALVE 496
Cdd:COG1124 159 LLLLDEPTSALDVSVQAEILNLLKDLREERGLTYLFVSHDLAVVAHlCDRVAVMQNGRIVEELTVADLLA 228
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
277-485 |
3.76e-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: 142.33 E-value: 3.76e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 277 IEARGLTMRFGN----FVAVDHVNFRIARGEIFGFLGSNGCGKSTTMKMLTGLLPASEGEAWLFGQPV---DPKDI-ATR 348
Cdd:cd03258 2 IELKNVSKVFGDtggkVTALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGSVLVDGTDLtllSGKELrKAR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 349 QRVGYMSQAFSLYSELSVRQNLELHARLFHIPDDEIAHRVAEMSERFMLTEVKDALPADLPLGIRQRLSLAVAVIHRPEM 428
Cdd:cd03258 82 RRIGMIFQHFNLLSSRTVFENVALPLEIAGVPKAEIEERVLELLELVGLEDKADAYPAQLSGGQKQRVGIARALANNPKV 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1820369315 429 LILDEPTSGVDPVARDMFWQLMVDLARQDRVTIFISTHFMNEAER-CDRISLMHAGKV 485
Cdd:cd03258 162 LLCDEATSALDPETTQSILALLRDINRELGLTIVLITHEMEVVKRiCDRVAVMEKGEV 219
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
277-497 |
5.00e-38 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 145.67 E-value: 5.00e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 277 IEARGLTMRFGNFVAVDHVNFRIARGEIFGFLGSNGCGKSTTMKMLTGLLPASEGEAWLFGQPVDpKDIATRQR-VGYMS 355
Cdd:COG1118 3 IEVRNISKRFGSFTLLDDVSLEIASGELVALLGPSGSGKTTLLRIIAGLETPDSGRIVLNGRDLF-TNLPPRERrVGFVF 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 356 QAFSLYSELSVRQNLELHARLFHIPDDEIAHRVAEMSERFMLTEVKDALPADLPLGIRQRLSLAVAVIHRPEMLILDEPT 435
Cdd:COG1118 82 QHYALFPHMTVAENIAFGLRVRPPSKAEIRARVEELLELVQLEGLADRYPSQLSGGQRQRVALARALAVEPEVLLLDEPF 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1820369315 436 SGVDPVARDMFWQLMVDL-ARQDRVTIFIsTHFMNEA-ERCDRISLMHAGKVLASDTPQALVEQ 497
Cdd:COG1118 162 GALDAKVRKELRRWLRRLhDELGGTTVFV-THDQEEAlELADRVVVMNQGRIEQVGTPDEVYDR 224
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
277-485 |
6.69e-38 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 140.72 E-value: 6.69e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 277 IEARGLTMRFGNFVAVDHVNFRIARGEIFGFLGSNGCGKSTTMKMLTGLLPASEGEAWLFGQPVDPKDIAT-RQRVGYMS 355
Cdd:COG4619 1 LELEGLSFRVGGKPILSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIYLDGKPLSAMPPPEwRRQVAYVP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 356 QAFSLYSElSVRQNLELHARLFHIPDDEiaHRVAEMSERFMLTE-VKDALPADLPLGIRQRLSLAVAVIHRPEMLILDEP 434
Cdd:COG4619 81 QEPALWGG-TVRDNLPFPFQLRERKFDR--ERALELLERLGLPPdILDKPVERLSGGERQRLALIRALLLQPDVLLLDEP 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1820369315 435 TSGVDPVARDMFWQLMVDLARQDRVTIFISTHFMNEAER-CDRISLMHAGKV 485
Cdd:COG4619 158 TSALDPENTRRVEELLREYLAEEGRAVLWVSHDPEQIERvADRVLTLEAGRL 209
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
277-496 |
8.58e-38 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 141.71 E-value: 8.58e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 277 IEARGLTMRFGNFVAVDHVNFRIARGEIFGFLGSNGCGKSTTMKMLTGLLPASEGEAWLFGQPVDPKDIATRQR--VGYM 354
Cdd:COG1137 4 LEAENLVKSYGKRTVVKDVSLEVNQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGRIFLDGEDITHLPMHKRARlgIGYL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 355 SQAFSLYSELSVRQNLELHARLFHIPDDEIAHRVAEMSERFMLTEVKDALPADLPLGIRQRLSLAVAVIHRPEMLILDEP 434
Cdd:COG1137 84 PQEASIFRKLTVEDNILAVLELRKLSKKEREERLEELLEEFGITHLRKSKAYSLSGGERRRVEIARALATNPKFILLDEP 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1820369315 435 TSGVDPVA----RDMFWQLmvdlaRQDRVTIFISTHFMNEAER-CDRISLMHAGKVLASDTPQALVE 496
Cdd:COG1137 164 FAGVDPIAvadiQKIIRHL-----KERGIGVLITDHNVRETLGiCDRAYIISEGKVLAEGTPEEILN 225
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
278-484 |
1.43e-37 |
|
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213179 [Multi-domain] Cd Length: 157 Bit Score: 138.15 E-value: 1.43e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 278 EARGLTMRFGNFVAVDHVNFRIARGEIFGFLGSNGCGKSTTMKMLTGLLPASEGEAWLFGQPVDPKDIAT-RQRVGYMSQ 356
Cdd:cd00267 1 EIENLSFRYGGRTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGKDIAKLPLEElRRRIGYVPQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 357 afslyseLSVRQnlelharlfhipddeiahrvaemserfmltevkdalpadlplgiRQRLSLAVAVIHRPEMLILDEPTS 436
Cdd:cd00267 81 -------LSGGQ--------------------------------------------RQRVALARALLLNPDLLLLDEPTS 109
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1820369315 437 GVDPVARDMFWQLMVDLARQDRvTIFISTHFMNEAER-CDRISLMHAGK 484
Cdd:cd00267 110 GLDPASRERLLELLRELAEEGR-TVIIVTHDPELAELaADRVIVLKDGK 157
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
277-488 |
3.75e-37 |
|
First domain of the ATP-binding cassette component of monosaccharide transport system; This family represents the domain I of the carbohydrate uptake proteins that transport only monosaccharides (Monos). The Carb_Monos family is involved in the uptake of monosaccharides, such as pentoses (such as xylose, arabinose, and ribose) and hexoses (such as xylose, arabinose, and ribose), that cannot be broken down to simple sugars by hydrolysis. Pentoses include xylose, arabinose, and ribose. Important hexoses include glucose, galactose, and fructose. In members of the Carb_monos family, the single hydrophobic gene product forms a homodimer while the ABC protein represents a fusion of two nucleotide-binding domains. However, it is assumed that two copies of the ABC domains are present in the assembled transporter.
Pssm-ID: 213183 [Multi-domain] Cd Length: 163 Bit Score: 136.79 E-value: 3.75e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 277 IEARGLTMRFGNFVAVDHVNFRIARGEIFGFLGSNGCGKSTTMKMLTGLLPASEGEAWLFGQPVDPKDI--ATRQRVGYM 354
Cdd:cd03216 1 LELRGITKRFGGVKALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVDGKEVSFASPrdARRAGIAMV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 355 SQafslyselsvrqnlelharlfhipddeiahrvaemserfmltevkdalpadLPLGIRQRLSLAVAVIHRPEMLILDEP 434
Cdd:cd03216 81 YQ---------------------------------------------------LSVGERQMVEIARALARNARLLILDEP 109
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1820369315 435 TSGVDPVARDMFWQLMVDLARQDRVTIFIStHFMNEAER-CDRISLMHAGKVLAS 488
Cdd:cd03216 110 TAALTPAEVERLFKVIRRLRAQGVAVIFIS-HRLDEVFEiADRVTVLRDGRVVGT 163
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
15-237 |
4.62e-37 |
|
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: 140.17 E-value: 4.62e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 15 LENVGQQYGATIALRDISLAIPARRMVGLIGPDGVGKSSLLSLIAGARAIEQGNVMVLGgdmRDVHHRRDvcPKIAWMpq 94
Cdd:COG0411 7 VRGLTKRFGGLVAVDDVSLEVERGEIVGLIGPNGAGKTTLFNLITGFYRPTSGRILFDG---RDITGLPP--HRIARL-- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 95 GLGK-----NLYHTLSVYENV-------------DFFARLFGHDKAERELR--INELLQSTGLAPFRDRPAGKLSGGMKQ 154
Cdd:COG0411 80 GIARtfqnpRLFPELTVLENVlvaaharlgrgllAALLRLPRARREEREARerAEELLERVGLADRADEPAGNLSYGQQR 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 155 KLGLCCALIHDPQLLILDEPTTGVDPLSRAQFWELIDSIRQRQP------E--MSVLVATAymeeaerfDWLVAMNAGEV 226
Cdd:COG0411 160 RLEIARALATEPKLLLLDEPAAGLNPEETEELAELIRRLRDERGitilliEhdMDLVMGLA--------DRIVVLDFGRV 231
|
250
....*....|.
gi 1820369315 227 LATGSAAELKA 237
Cdd:COG0411 232 IAEGTPAEVRA 242
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
15-237 |
4.78e-37 |
|
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: 139.49 E-value: 4.78e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 15 LENVGQQYGATIALRDISLAIPARRMVGLIGPDGVGKSSLLSLIAGARAIEQGNVMVLGgdmRDVHHRRDVcpKIAWMpq 94
Cdd:cd03219 3 VRGLTKRFGGLVALDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFDG---EDITGLPPH--EIARL-- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 95 GLGK-----NLYHTLSVYENV-----------DFFARLFGHDKAERElRINELLQSTGLAPFRDRPAGKLSGGMKQKLGL 158
Cdd:cd03219 76 GIGRtfqipRLFPELTVLENVmvaaqartgsgLLLARARREEREARE-RAEELLERVGLADLADRPAGELSYGQQRRLEI 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 159 CCALIHDPQLLILDEPTTGVDPLSRAQFWELIDSIRQRQpeMSVLVA----TAYMEEAERfdwLVAMNAGEVLATGSAAE 234
Cdd:cd03219 155 ARALATDPKLLLLDEPAAGLNPEETEELAELIRELRERG--ITVLLVehdmDVVMSLADR---VTVLDQGRVIAEGTPDE 229
|
...
gi 1820369315 235 LKA 237
Cdd:cd03219 230 VRN 232
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
8-212 |
6.14e-37 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 139.84 E-value: 6.14e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 8 TSPPIAL-LENVGQQY----GATIALRDISLAIPARRMVGLIGPDGVGKSSLLSLIAGARAIEQGNVMVLGGDMRDVHHR 82
Cdd:COG1116 2 SAAAPALeLRGVSKRFptggGGVTALDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPTSGEVLVDGKPVTGPGPD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 83 RdvcpkiAWMPQGlgknlyHTL----SVYENVDFFARLFGHDKAERELRINELLQSTGLAPFRDRPAGKLSGGMKQKLGL 158
Cdd:COG1116 82 R------GVVFQE------PALlpwlTVLDNVALGLELRGVPKAERRERARELLELVGLAGFEDAYPHQLSGGMRQRVAI 149
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1820369315 159 CCALIHDPQLLILDEPTTGVDPLSRAQFWELIDSIRQRQPeMSVLVATAYMEEA 212
Cdd:COG1116 150 ARALANDPEVLLMDEPFGALDALTRERLQDELLRLWQETG-KTVLFVTHDVDEA 202
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
274-521 |
7.13e-37 |
|
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: 146.20 E-value: 7.13e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 274 EIAIEARGLTMRF--GNFVAVDHVNFRIARGEIFGFLGSNGCGKSTTMKMLTGLLPAS---EGEAWLFGQPVDPKDIATR 348
Cdd:COG1123 2 TPLLEVRDLSVRYpgGDVPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGLLPHGgriSGEVLLDGRDLLELSEALR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 349 -QRVGYMSQ-AFSLYSELSVRQNLELHARLFHIPDDEIAHRVAEMSERFMLTEVKDALPADLPLGIRQRLSLAVAVIHRP 426
Cdd:COG1123 82 gRRIGMVFQdPMTQLNPVTVGDQIAEALENLGLSRAEARARVLELLEAVGLERRLDRYPHQLSGGQRQRVAIAMALALDP 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 427 EMLILDEPTSGVDPVARDMFWQLMVDLARQDRVTIFISTHFMNE-AERCDRISLMHAGKVLASDTPQALVE--QRGAASL 503
Cdd:COG1123 162 DLLIADEPTTALDVTTQAEILDLLRELQRERGTTVLLITHDLGVvAEIADRVVVMDDGRIVEDGPPEEILAapQALAAVP 241
|
250
....*....|....*...
gi 1820369315 504 EEAFIAWLKEAQPSSPVP 521
Cdd:COG1123 242 RLGAARGRAAPAAAAAEP 259
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
277-497 |
1.51e-36 |
|
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: 137.75 E-value: 1.51e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 277 IEARGLTMRFGNFVAVDHVNFRIARGEIFGFLGSNGCGKSTTMKMLTGLLPASEGEAWLFGQPVDPKDIATRQrVGYMSQ 356
Cdd:cd03300 1 IELENVSKFYGGFVALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGKDITNLPPHKRP-VNTVFQ 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 357 AFSLYSELSVRQNLELHARLFHIPDDEIAHRVAEMSERFMLTEVKDALPADLPLGIRQRLSLAVAVIHRPEMLILDEPTS 436
Cdd:cd03300 80 NYALFPHLTVFENIAFGLRLKKLPKAEIKERVAEALDLVQLEGYANRKPSQLSGGQQQRVAIARALVNEPKVLLLDEPLG 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1820369315 437 GVDPVAR-DMFWQLMvDLARQDRVTIFISTHFMNEA-ERCDRISLMHAGKVLASDTPQALVEQ 497
Cdd:cd03300 160 ALDLKLRkDMQLELK-RLQKELGITFVFVTHDQEEAlTMSDRIAVMNKGKIQQIGTPEEIYEE 221
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
276-497 |
1.59e-36 |
|
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: 137.86 E-value: 1.59e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 276 AIEARGLTMRFGNFVAVDHVNFRIARGEIFGFLGSNGCGKSTTMKMLTGLLPASEGEAWLFGQPVDPKDIATRQrVGYMS 355
Cdd:cd03296 2 SIEVRNVSKRFGDFVALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGGEDATDVPVQERN-VGFVF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 356 QAFSLYSELSVRQN----LELHARLFHIPDDEIAHRVAEMSERFMLTEVKDALPADLPLGIRQRLSLAVAVIHRPEMLIL 431
Cdd:cd03296 81 QHYALFRHMTVFDNvafgLRVKPRSERPPEAEIRAKVHELLKLVQLDWLADRYPAQLSGGQRQRVALARALAVEPKVLLL 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1820369315 432 DEPTSGVDPVARDmfwQLMVDLAR-QDRV---TIFIsTHFMNEA-ERCDRISLMHAGKVLASDTPQALVEQ 497
Cdd:cd03296 161 DEPFGALDAKVRK---ELRRWLRRlHDELhvtTVFV-THDQEEAlEVADRVVVMNKGRIEQVGTPDEVYDH 227
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
10-245 |
2.25e-36 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 140.74 E-value: 2.25e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 10 PPIAL-LENVGQQYGATIALRDISLAIPARRMVGLIGPDGVGKSSLLSLIAGARAIEQGNVMVLGGDMRDvhHRRDVCPK 88
Cdd:PRK13536 38 STVAIdLAGVSKSYGDKAVVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKITVLGVPVPA--RARLARAR 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 89 IAWMPQGlgKNLYHTLSVYENVDFFARLFGHDKAERELRINELLQSTGLAPFRDRPAGKLSGGMKQKLGLCCALIHDPQL 168
Cdd:PRK13536 116 IGVVPQF--DNLDLEFTVRENLLVFGRYFGMSTREIEAVIPSLLEFARLESKADARVSDLSGGMKRRLTLARALINDPQL 193
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1820369315 169 LILDEPTTGVDPLSRAQFWELIDSIRQRQpeMSVLVATAYMEEAERF-DWLVAMNAGEVLATGSAAEL-KAQTGSQTLE 245
Cdd:PRK13536 194 LILDEPTTGLDPHARHLIWERLRSLLARG--KTILLTTHFMEEAERLcDRLCVLEAGRKIAEGRPHALiDEHIGCQVIE 270
|
|
| LPS_export_lptB |
TIGR04406 |
LPS export ABC transporter ATP-binding protein; Members of this fmaily are LptB, the ... |
279-496 |
3.63e-36 |
|
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: 137.02 E-value: 3.63e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 279 ARGLTMRFGNFVAVDHVNFRIARGEIFGFLGSNGCGKSTTMKMLTGLLPASEGEAWLFGQPVDPKDIATRQR--VGYMSQ 356
Cdd:TIGR04406 4 AENLIKSYKKRKVVNDVSLSVKSGEIVGLLGPNGAGKTTSFYMIVGLVRPDAGKILIDGQDITHLPMHERARlgIGYLPQ 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 357 AFSLYSELSVRQNLElhARLFHIPD---DEIAHRVAEMSERFMLTEVKDALPADLPLGIRQRLSLAVAVIHRPEMLILDE 433
Cdd:TIGR04406 84 EASIFRKLTVEENIM--AVLEIRKDldrAEREERLEALLEEFQISHLRDNKAMSLSGGERRRVEIARALATNPKFILLDE 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1820369315 434 PTSGVDPVARDMFWQLMVDLaRQDRVTIFISTHFMNEA-ERCDRISLMHAGKVLASDTPQALVE 496
Cdd:TIGR04406 162 PFAGVDPIAVGDIKKIIKHL-KERGIGVLITDHNVRETlDICDRAYIISDGKVLAEGTPAEIVA 224
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
15-237 |
3.90e-36 |
|
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440744 [Multi-domain] Cd Length: 241 Bit Score: 136.65 E-value: 3.90e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 15 LENVGQQYGATIALRDISLAIPARRMVGLIGPDGVGKSSLLSLIAGARAIEQGNVMVLGgdmRDVHH-----RRDVCPKI 89
Cdd:COG1127 8 VRNLTKSFGDRVVLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEILVDG---QDITGlsekeLYELRRRI 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 90 AWMPQGLGknLYHTLSVYENVDFFARLFGH-DKAERELRINELLQSTGLAPFRDRPAGKLSGGMKQKLGLCCALIHDPQL 168
Cdd:COG1127 85 GMLFQGGA--LFDSLTVFENVAFPLREHTDlSEAEIRELVLEKLELVGLPGAADKMPSELSGGMRKRVALARALALDPEI 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 169 LILDEPTTGVDPLSRAQFWELIDSIRQRQPeMSVLVATAYMEEAERF-DWLVAMNAGEVLATGSAAELKA 237
Cdd:COG1127 163 LLYDEPTAGLDPITSAVIDELIRELRDELG-LTSVVVTHDLDSAFAIaDRVAVLADGKIIAEGTPEELLA 231
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
278-488 |
7.04e-36 |
|
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: 134.10 E-value: 7.04e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 278 EARGLTMRFGNFVAVDHVNFRIARGEIFGFLGSNGCGKSTTMKMLTGLLPASEGEAWLFGQPV---DPKDIAtrQRVGYM 354
Cdd:cd03214 1 EVENLSVGYGGRTVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDGKDLaslSPKELA--RKIAYV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 355 SQAfslyselsvrqnLELHarlfhipddeiahRVAEMSERFMLTevkdalpadLPLGIRQRLSLAVAVIHRPEMLILDEP 434
Cdd:cd03214 79 PQA------------LELL-------------GLAHLADRPFNE---------LSGGERQRVLLARALAQEPPILLLDEP 124
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1820369315 435 TSGVDPVARDMFWQLMVDLARQDRVTIFISTHFMNEAER-CDRISLMHAGKVLAS 488
Cdd:cd03214 125 TSHLDIAHQIELLELLRRLARERGKTVVMVLHDLNLAARyADRVILLKDGRIVAQ 179
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
11-510 |
8.02e-36 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 143.00 E-value: 8.02e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 11 PIALLENVGQQYGATIALRDISLAIPARRMVGLIGPDGVGKSSLLSLIAGARAIEQGNVMVLGGDMRDVHHRRDVCPKIA 90
Cdd:PRK09700 4 PYISMAGIGKSFGPVHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNINYNKLDHKLAAQLGIG 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 91 WMPQGLgkNLYHTLSVYENVdFFARL-----FGH---DKAERELRINELLQSTGLAPFRDRPAGKLSGGMKQKLGLCCAL 162
Cdd:PRK09700 84 IIYQEL--SVIDELTVLENL-YIGRHltkkvCGVniiDWREMRVRAAMMLLRVGLKVDLDEKVANLSISHKQMLEIAKTL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 163 IHDPQLLILDEPTTGvdpLSRAQFWELIDSIRQRQPEMSVLVATAY-MEEAERF-DWLVAMNAGEVLATGSAAELKAQ-- 238
Cdd:PRK09700 161 MLDAKVIIMDEPTSS---LTNKEVDYLFLIMNQLRKEGTAIVYISHkLAEIRRIcDRYTVMKDGSSVCSGMVSDVSNDdi 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 239 ----TGSQtLEQAFIALLPEAQRQAHKTVvipprdsreeeiaIEARGLTMRfgNFVAVDHVNFRIARGEIFGFLGSNGCG 314
Cdd:PRK09700 238 vrlmVGRE-LQNRFNAMKENVSNLAHETV-------------FEVRNVTSR--DRKKVRDISFSVCRGEILGFAGLVGSG 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 315 KSTTMKMLTGLLPASEGEAWLFGQPVDPKD--IATRQRVGYMSQA---FSLYSELSVRQNLELHARL--------FHIPD 381
Cdd:PRK09700 302 RTELMNCLFGVDKRAGGEIRLNGKDISPRSplDAVKKGMAYITESrrdNGFFPNFSIAQNMAISRSLkdggykgaMGLFH 381
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 382 DEIAHRVAEMSERFMLTEVK--DALPADLPLGIRQRLSLAVAVIHRPEMLILDEPTSGVDPVARDMFWQLMVDLARQDRV 459
Cdd:PRK09700 382 EVDEQRTAENQRELLALKCHsvNQNITELSGGNQQKVLISKWLCCCPEVIIFDEPTRGIDVGAKAEIYKVMRQLADDGKV 461
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|.
gi 1820369315 460 TIFISTHFMNEAERCDRISLMHAGKVlasdtpQALVEQRGAASlEEAFIAW 510
Cdd:PRK09700 462 ILMVSSELPEIITVCDRIAVFCEGRL------TQILTNRDDMS-EEEIMAW 505
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
277-485 |
9.95e-36 |
|
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: 134.69 E-value: 9.95e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 277 IEARGLTMRFGNFVAVDHVNFRIARGEIFGFLGSNGCGKSTTMKMLTGLLPASEGEAWLFGQPV---DPKDiatrQRVGY 353
Cdd:cd03301 1 VELENVTKRFGNVTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGRDVtdlPPKD----RDIAM 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 354 MSQAFSLYSELSVRQNLELHARLFHIPDDEIAHRVAEMSERFMLTEVKDALPADLPLGIRQRLSLAVAVIHRPEMLILDE 433
Cdd:cd03301 77 VFQNYALYPHMTVYDNIAFGLKLRKVPKDEIDERVREVAELLQIEHLLDRKPKQLSGGQRQRVALGRAIVREPKVFLMDE 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1820369315 434 PTSGVDPVARDMFWQLMVDLARQDRVTIFISTHFMNEAER-CDRISLMHAGKV 485
Cdd:cd03301 157 PLSNLDAKLRVQMRAELKRLQQRLGTTTIYVTHDQVEAMTmADRIAVMNDGQI 209
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
15-226 |
1.08e-35 |
|
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: 134.92 E-value: 1.08e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 15 LENVGQQYGA----TIALRDISLAIPARRMVGLIGPDGVGKSSLLSLIAGARAIEQGNVMVLGGDMRDVHH------RRD 84
Cdd:cd03255 3 LKNLSKTYGGggekVQALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRVDGTDISKLSEkelaafRRR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 85 vcpKIAWMPQGLgkNLYHTLSVYENVDFFARLFGHDKAERELRINELLQSTGLAPFRDRPAGKLSGGMKQKLGLCCALIH 164
Cdd:cd03255 83 ---HIGFVFQSF--NLLPDLTALENVELPLLLAGVPKKERRERAEELLERVGLGDRLNHYPSELSGGQQQRVAIARALAN 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1820369315 165 DPQLLILDEPTTGVDPLSRAQFWELIDSIrQRQPEMSVLVATAYMEEAERFDWLVAMNAGEV 226
Cdd:cd03255 158 DPKIILADEPTGNLDSETGKEVMELLREL-NKEAGTTIVVVTHDPELAEYADRIIELRDGKI 218
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
8-497 |
1.38e-35 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 142.09 E-value: 1.38e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 8 TSPPIALLENVGQQYGATIALRDISLAIPARRMVGLIGPDGVGKSSLLSLIAGARAIEQGNVMVLGgdmRDVHHRRdvcP 87
Cdd:COG3845 1 MMPPALELRGITKRFGGVVANDDVSLTVRPGEIHALLGENGAGKSTLMKILYGLYQPDSGEILIDG---KPVRIRS---P 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 88 KIAwMPQGLGK-----NLYHTLSVYENV-----DFFARLFGHDKAERELRinELLQSTGLA--PfrDRPAGKLSGGMKQK 155
Cdd:COG3845 75 RDA-IALGIGMvhqhfMLVPNLTVAENIvlglePTKGGRLDRKAARARIR--ELSERYGLDvdP--DAKVEDLSVGEQQR 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 156 LGLCCALIHDPQLLILDEPTTG-----VDplsraqfwELIDSIRQ-RQPEMSVLVATAYMEEAERF-DWLVAMNAGEVLA 228
Cdd:COG3845 150 VEILKALYRGARILILDEPTAVltpqeAD--------ELFEILRRlAAEGKSIIFITHKLREVMAIaDRVTVLRRGKVVG 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 229 TGSAAElkaqTGSQTLEQAFIAllpeaqRQAHKTVVIPPRDSREEeiAIEARGLTMR-FGNFVAVDHVNFRIARGEIFGF 307
Cdd:COG3845 222 TVDTAE----TSEEELAELMVG------REVLLRVEKAPAEPGEV--VLEVENLSVRdDRGVPALKDVSLEVRAGEILGI 289
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 308 LGSNGCGKSTTMKMLTGLLPASEGEAWLFGQPVDPKDIATRQR--VGYMS---QAFSLYSELSVRQN--LELH-----AR 375
Cdd:COG3845 290 AGVAGNGQSELAEALAGLRPPASGSIRLDGEDITGLSPRERRRlgVAYIPedrLGRGLVPDMSVAENliLGRYrrppfSR 369
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 376 LFHIPDDEIAHRVAEMSERFmltEVKdalPADLPLGIR-------QRLSLAVAVIHRPEMLILDEPTSGVDPVARDMFWQ 448
Cdd:COG3845 370 GGFLDRKAIRAFAEELIEEF---DVR---TPGPDTPARslsggnqQKVILARELSRDPKLLIAAQPTRGLDVGAIEFIHQ 443
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|.
gi 1820369315 449 LMVDLARQDRVTIFISTHfMNEA-ERCDRISLMHAGKVLAS-DTPQALVEQ 497
Cdd:COG3845 444 RLLELRDAGAAVLLISED-LDEIlALSDRIAVMYEGRIVGEvPAAEATREE 493
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
15-212 |
3.27e-35 |
|
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: 133.37 E-value: 3.27e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 15 LENVGQQYG----ATIALRDISLAIPARRMVGLIGPDGVGKSSLLSLIAGARAIEQGNVMVLGGDMRDVHhrrdvcPKIA 90
Cdd:cd03293 3 VRNVSKTYGggggAVTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVDGEPVTGPG------PDRG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 91 WMPQGlgKNLYHTLSVYENVDFFARLFGHDKAERELRINELLQSTGLAPFRDRPAGKLSGGMKQKLGLCCALIHDPQLLI 170
Cdd:cd03293 77 YVFQQ--DALLPWLTVLDNVALGLELQGVPKAEARERAEELLELVGLSGFENAYPHQLSGGMRQRVALARALAVDPDVLL 154
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1820369315 171 LDEPTTGVDPLSRAQFWELIDSIRQRQPEMSVLVaTAYMEEA 212
Cdd:cd03293 155 LDEPFSALDALTREQLQEELLDIWRETGKTVLLV-THDIDEA 195
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
264-524 |
3.97e-35 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 138.04 E-value: 3.97e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 264 VIPPRDSREEEIA---IEARGLTMRFGNFVAVDHVNFRIARGEIFGFLGSNGCGKSTTMKMLTGLLPASEGEAWLFGQpv 340
Cdd:PRK11607 4 AIPRPQAKTRKALtplLEIRNLTKSFDGQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGV-- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 341 DPKDIATRQR-VGYMSQAFSLYSELSVRQNLELHARLFHIPDDEIAHRVAEMSERFMLTEVKDALPADLPLGIRQRLSLA 419
Cdd:PRK11607 82 DLSHVPPYQRpINMMFQSYALFPHMTVEQNIAFGLKQDKLPKAEIASRVNEMLGLVHMQEFAKRKPHQLSGGQRQRVALA 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 420 VAVIHRPEMLILDEPTSGVDPVARDMFWQLMVDLARQDRVTIFISTHFMNEA-ERCDRISLMHAGKVLASDTPQALVEQ- 497
Cdd:PRK11607 162 RSLAKRPKLLLLDEPMGALDKKLRDRMQLEVVDILERVGVTCVMVTHDQEEAmTMAGRIAIMNRGKFVQIGEPEEIYEHp 241
|
250 260 270
....*....|....*....|....*....|..
gi 1820369315 498 --RGAASL---EEAFIAWLKEAQPSSPVPEDP 524
Cdd:PRK11607 242 ttRYSAEFigsVNVFEGVLKERQEDGLVIDSP 273
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
15-206 |
6.84e-35 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 132.48 E-value: 6.84e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 15 LENVGQQY-GATIALRDISLAIPARRMVGLIGPDGVGKSSLLSLIAGARAIEQGNVMVLGGDMRDVHHRrdvcpKIAWMP 93
Cdd:COG2884 4 FENVSKRYpGGREALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLVNGQDLSRLKRR-----EIPYLR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 94 QGLG------KNLYHtLSVYENVDFFARLFGHDKAERELRINELLQSTGLAPFRDRPAGKLSGGMKQKLGLCCALIHDPQ 167
Cdd:COG2884 79 RRIGvvfqdfRLLPD-RTVYENVALPLRVTGKSRKEIRRRVREVLDLVGLSDKAKALPHELSGGEQQRVAIARALVNRPE 157
|
170 180 190
....*....|....*....|....*....|....*....
gi 1820369315 168 LLILDEPTTGVDPLSRAQFWELIDSIRQRQpeMSVLVAT 206
Cdd:COG2884 158 LLLADEPTGNLDPETSWEIMELLEEINRRG--TTVLIAT 194
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
277-494 |
1.88e-34 |
|
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: 131.40 E-value: 1.88e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 277 IEARGLTMRFGNFVAVDHVNFRIARGEIFGFLGSNGCGKSTTMKMLTGLLPASEGEAWLFGQPVDPKdiATRQRV----G 352
Cdd:cd03224 1 LEVENLNAGYGKSQILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDGRDITGL--PPHERAragiG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 353 YMSQAFSLYSELSVRQNLELHARLFhiPDDEIAHRVAEMSERF-MLTEVKDALPADLPLGIRQRLSLAVAVIHRPEMLIL 431
Cdd:cd03224 79 YVPEGRRIFPELTVEENLLLGAYAR--RRAKRKARLERVYELFpRLKERRKQLAGTLSGGEQQMLAIARALMSRPKLLLL 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1820369315 432 DEPTSGVDPVARDMFWQLMVDLARQDrVTIFISTHFMNEA-ERCDRISLMHAGKVLASDTPQAL 494
Cdd:cd03224 157 DEPSEGLAPKIVEEIFEAIRELRDEG-VTILLVEQNARFAlEIADRAYVLERGRVVLEGTAAEL 219
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
15-230 |
1.92e-34 |
|
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: 130.80 E-value: 1.92e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 15 LENVGQQYGATIALRDISLAIPARRMVGLIGPDGVGKSSLLSLIAGARAIEQGNVMVLGGDMRDVHhrrDVCPKIAWMPQ 94
Cdd:cd03268 3 TNDLTKTYGKKRVLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEITFDGKSYQKNI---EALRRIGALIE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 95 GLGknLYHTLSVYENVDFFARLFGHDKAerelRINELLQSTGLAPFRDRPAGKLSGGMKQKLGLCCALIHDPQLLILDEP 174
Cdd:cd03268 80 APG--FYPNLTARENLRLLARLLGIRKK----RIDEVLDVVGLKDSAKKKVKGFSLGMKQRLGIALALLGNPDLLILDEP 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1820369315 175 TTGVDPLSRAQFWELIDSIRQRqpEMSVLVATAYMEEAERF-DWLVAMNAGEVLATG 230
Cdd:cd03268 154 TNGLDPDGIKELRELILSLRDQ--GITVLISSHLLSEIQKVaDRIGIINKGKLIEEG 208
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
277-520 |
2.35e-34 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 134.82 E-value: 2.35e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 277 IEARGLTMRF----GNFVAVDHVNFRIARGEIFGFLGSNGCGKSTTMKMLTGLLPASEGEAWLFGQPV---DPKDI-ATR 348
Cdd:COG1135 2 IELENLSKTFptkgGPVTALDDVSLTIEKGEIFGIIGYSGAGKSTLIRCINLLERPTSGSVLVDGVDLtalSERELrAAR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 349 QRVGYMSQAFSLYSELSVRQNLELHARLFHIPDDEIAHRVAEMSERFMLTEVKDALPADLPLGIRQRLSLAVAVIHRPEM 428
Cdd:COG1135 82 RKIGMIFQHFNLLSSRTVAENVALPLEIAGVPKAEIRKRVAELLELVGLSDKADAYPSQLSGGQKQRVGIARALANNPKV 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 429 LILDEPTSGVDPVARDMFWQLMVDLARQDRVTIFISTHFMNEAER-CDRISLMHAGKVL------------ASDTPQALV 495
Cdd:COG1135 162 LLCDEATSALDPETTRSILDLLKDINRELGLTIVLITHEMDVVRRiCDRVAVLENGRIVeqgpvldvfanpQSELTRRFL 241
|
250 260
....*....|....*....|....*
gi 1820369315 496 EQRGAASLEEAFIAWLKEAQPSSPV 520
Cdd:COG1135 242 PTVLNDELPEELLARLREAAGGGRL 266
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
292-436 |
2.74e-34 |
|
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: 128.15 E-value: 2.74e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 292 VDHVNFRIARGEIFGFLGSNGCGKSTTMKMLTGLLPASEGEAWLFGQPVDPKDI-ATRQRVGYMSQAFSLYSELSVRQNL 370
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDLTDDERkSLRKEIGYVFQDPQLFPRLTVRENL 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 371 ELHARLFHIPDDEIAHRVAEMSERFMLTEVKD----ALPADLPLGIRQRLSLAVAVIHRPEMLILDEPTS 436
Cdd:pfam00005 81 RLGLLLKGLSKREKDARAEEALEKLGLGDLADrpvgERPGTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
|
|
| GldA_ABC_ATP |
TIGR03522 |
gliding motility-associated ABC transporter ATP-binding subunit GldA; Members of this protein ... |
22-284 |
6.15e-34 |
|
gliding motility-associated ABC transporter ATP-binding subunit GldA; Members of this protein family are exclusive to the Bacteroidetes phylum (previously Cytophaga-Flavobacteria-Bacteroides). GldA is an ABC transporter ATP-binding protein (pfam00005) linked to a type of rapid surface gliding motility found in certain Bacteroidetes, such as Flavobacterium johnsoniae and Cytophaga hutchinsonii. Knockouts of GldA abolish the gliding phenotype. Gliding motility appears closely linked to chitin utilization in the model species Flavobacterium johnsoniae. Bacteroidetes with members of this protein family appear to have all of the genes associated with gliding motility.
Pssm-ID: 132561 [Multi-domain] Cd Length: 301 Bit Score: 132.59 E-value: 6.15e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 22 YGATIALRDISLAIPARRMVGLIGPDGVGKSSLLSLIAGARAIEQGNVMVLGGDMrdVHHRRDVCPKIAWMPQGlgKNLY 101
Cdd:TIGR03522 12 YGTQNALDEVSFEAQKGRIVGFLGPNGAGKSTTMKIITGYLPPDSGSVQVCGEDV--LQNPKEVQRNIGYLPEH--NPLY 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 102 HTLSVYENVDFFARLFGHDKAERELRINELLQSTGLAPFRDRPAGKLSGGMKQKLGLCCALIHDPQLLILDEPTTGVDPL 181
Cdd:TIGR03522 88 LDMYVREYLQFIAGIYGMKGQLLKQRVEEMIELVGLRPEQHKKIGQLSKGYRQRVGLAQALIHDPKVLILDEPTTGLDPN 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 182 SRAQFWELIDSIRQrqpEMSVLVATAYMEEAERF-DWLVAMNAGEVLATGSAAELKAQTGSQTLE---------QAF--- 248
Cdd:TIGR03522 168 QLVEIRNVIKNIGK---DKTIILSTHIMQEVEAIcDRVIIINKGKIVADKKLDELSAANKKQVIEvefeeqidlQLFetl 244
|
250 260 270
....*....|....*....|....*....|....*....
gi 1820369315 249 --IALLPEAQRQAHKTVVIPPRDSREEEI-AIEARGLTM 284
Cdd:TIGR03522 245 eeISSVKNTGGNTWKLTFETPNDTRPEIFkLAQQKGLKL 283
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
277-485 |
7.71e-34 |
|
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: 129.93 E-value: 7.71e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 277 IEARGLTMRFGN----FVAVDHVNFRIARGEIFGFLGSNGCGKSTTMKMLTGLLPASEGEAWLFGQPVDPKDIAT----R 348
Cdd:cd03257 2 LEVKNLSVSFPTgggsVKALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGKDLLKLSRRLrkirR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 349 QRVGYMSQ--AFSLYSELSVRQNLE--LHARLFHIPDDEIAHRVAEMSERFMLTE-VKDALPADLPLGIRQRLSLAVAVI 423
Cdd:cd03257 82 KEIQMVFQdpMSSLNPRMTIGEQIAepLRIHGKLSKKEARKEAVLLLLVGVGLPEeVLNRYPHELSGGQRQRVAIARALA 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1820369315 424 HRPEMLILDEPTSGVDPVARDMFWQLMVDLARQDRVTIFISTHFMNEAER-CDRISLMHAGKV 485
Cdd:cd03257 162 LNPKLLIADEPTSALDVSVQAQILDLLKKLQEELGLTLLFITHDLGVVAKiADRVAVMYAGKI 224
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
15-237 |
8.51e-34 |
|
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: 129.48 E-value: 8.51e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 15 LENVGQQYGATIALRDISLAIPARRMVGLIGPDGVGKSSLLSLIAGARAIEQGNVMVLGGDMRDVH-HRRdVCPKIAWMP 93
Cdd:cd03224 3 VENLNAGYGKSQILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDGRDITGLPpHER-ARAGIGYVP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 94 QGlgKNLYHTLSVYENVDFFARLFGHDKAEREL-RINELLqsTGLAPFRDRPAGKLSGGMKQKLGLCCALIHDPQLLILD 172
Cdd:cd03224 82 EG--RRIFPELTVEENLLLGAYARRRAKRKARLeRVYELF--PRLKERRKQLAGTLSGGEQQMLAIARALMSRPKLLLLD 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1820369315 173 EPTTGVDPLSRAQFWELIDSIRQRqpEMSVLV----ATAYMEEAERFdwlVAMNAGEVLATGSAAELKA 237
Cdd:cd03224 158 EPSEGLAPKIVEEIFEAIRELRDE--GVTILLveqnARFALEIADRA---YVLERGRVVLEGTAAELLA 221
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
10-228 |
8.77e-34 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 129.78 E-value: 8.77e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 10 PPIALLENVGQQYG----ATIALRDISLAIPARRMVGLIGPDGVGKSSLLSLIAGARAIEQGNVMVLGgdmRDVHH---- 81
Cdd:COG1136 2 SPLLELRNLTKSYGtgegEVTALRGVSLSIEAGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVLIDG---QDISSlser 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 82 -----RRDvcpKIAWMPQGLgkNLYHTLSVYENVDFFARLFGHDKAERELRINELLQSTGLAPFRDRPAGKLSGGMKQKL 156
Cdd:COG1136 79 elarlRRR---HIGFVFQFF--NLLPELTALENVALPLLLAGVSRKERRERARELLERVGLGDRLDHRPSQLSGGQQQRV 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1820369315 157 GLCCALIHDPQLLILDEPTTGVDPLSRAQFWELIDSIRqRQPEMSVLVATAYMEEAERFDWLVAMNAGEVLA 228
Cdd:COG1136 154 AIARALVNRPKLILADEPTGNLDSKTGEEVLELLRELN-RELGTTIVMVTHDPELAARADRVIRLRDGRIVS 224
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
9-235 |
1.16e-33 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 131.85 E-value: 1.16e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 9 SPPIALLENVGQQYGATIALRDISLAIPARRMVGLIGPDGVGKSSLLSLIAGARAIEQGNVMVLG----GDMRDVHHRRD 84
Cdd:PRK13537 4 SVAPIDFRNVEKRYGDKLVVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCGepvpSRARHARQRVG 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 85 VCPKIawmpqglgKNLYHTLSVYENVDFFARLFGHDKAERELRINELLQSTGLAPFRDRPAGKLSGGMKQKLGLCCALIH 164
Cdd:PRK13537 84 VVPQF--------DNLDPDFTVRENLLVFGRYFGLSAAAARALVPPLLEFAKLENKADAKVGELSGGMKRRLTLARALVN 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1820369315 165 DPQLLILDEPTTGVDPLSRAQFWELIDSIRQRQPemSVLVATAYMEEAERF-DWLVAMNAGEVLATGSAAEL 235
Cdd:PRK13537 156 DPDVLVLDEPTTGLDPQARHLMWERLRSLLARGK--TILLTTHFMEEAERLcDRLCVIEEGRKIAEGAPHAL 225
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
276-500 |
1.84e-33 |
|
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase domain [Defense mechanisms];
Pssm-ID: 441875 [Multi-domain] Cd Length: 711 Bit Score: 138.04 E-value: 1.84e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 276 AIEARGLTMRFGNFV--AVDHVNFRIARGEIFGFLGSNGCGKSTTMKMLTGLLPASEGEAWLFGQP---VDPKDIatRQR 350
Cdd:COG2274 473 DIELENVSFRYPGDSppVLDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEPTSGRILIDGIDlrqIDPASL--RRQ 550
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 351 VGYMSQAFSLYSElSVRQNLELHARlfHIPDDEIaHRVAEMSErfmLTEVKDALP-----------ADLPLGIRQRLSLA 419
Cdd:COG2274 551 IGVVLQDVFLFSG-TIRENITLGDP--DATDEEI-IEAARLAG---LHDFIEALPmgydtvvgeggSNLSGGQRQRLAIA 623
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 420 VAVIHRPEMLILDEPTSGVDPVARDMFWQLMVDLARQdrVTIFISTHFMNEAERCDRISLMHAGKVLASDTPQALVEQRG 499
Cdd:COG2274 624 RALLRNPRILILDEATSALDAETEAIILENLRRLLKG--RTVIIIAHRLSTIRLADRIIVLDKGRIVEDGTHEELLARKG 701
|
.
gi 1820369315 500 A 500
Cdd:COG2274 702 L 702
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
15-235 |
2.28e-33 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 132.14 E-value: 2.28e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 15 LENVGQQYGATIALRDISLAIPARRMVGLIGPDGVGKSSLLSLIAGARAIEQGNVmVLGGdmRDVH----HRRDvcpkIA 90
Cdd:COG3842 8 LENVSKRYGDVTALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRI-LLDG--RDVTglppEKRN----VG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 91 WMPQGlgknlY----HtLSVYENVDFFARLFGHDKAERELRINELLQSTGLAPFRDRPAGKLSGGMKQKLGLCCALIHDP 166
Cdd:COG3842 81 MVFQD-----YalfpH-LTVAENVAFGLRMRGVPKAEIRARVAELLELVGLEGLADRYPHQLSGGQQQRVALARALAPEP 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 167 QLLILDEPTTGVDPLSRAQFWELIDSIrQRQPEMSVLVATAYMEEAERF-DWLVAMNAGEVLATGSAAEL 235
Cdd:COG3842 155 RVLLLDEPLSALDAKLREEMREELRRL-QRELGITFIYVTHDQEEALALaDRIAVMNDGRIEQVGTPEEI 223
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
15-230 |
3.29e-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: 3.29e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 15 LENVGQQYGATIALRDISLAIPARRMVGLIGPDGVGKSSLLSLIAGARAIEQGNVMVLGGDMRDvHHRRDVCPKIAWMPQ 94
Cdd:cd03214 2 VENLSVGYGGRTVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDGKDLAS-LSPKELARKIAYVPQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 95 glgknlyhtlsvyenvdffarlfghdkaerelrineLLQSTGLAPFRDRPAGKLSGGMKQKLGLCCALIHDPQLLILDEP 174
Cdd:cd03214 81 ------------------------------------ALELLGLAHLADRPFNELSGGERQRVLLARALAQEPPILLLDEP 124
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1820369315 175 TTGVDPlsRAQFwELIDSIRQ--RQPEMSVLVATAYMEEAERF-DWLVAMNAGEVLATG 230
Cdd:cd03214 125 TSHLDI--AHQI-ELLELLRRlaRERGKTVVMVLHDLNLAARYaDRVILLKDGRIVAQG 180
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
277-485 |
4.07e-33 |
|
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: 127.26 E-value: 4.07e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 277 IEARGLTMRFGNFVAVDHVNFRIARGEIFGFLGSNGCGKSTTMKMLTGLLPASEGEAWLFGQPV--DPKDIAT-RQRVGY 353
Cdd:cd03262 1 IEIKNLHKSFGDFHVLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIDGLKLtdDKKNINElRQKVGM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 354 MSQAFSLYSELSVRQNLELHAR-LFHIPDDEIAHRVAEMSERFMLTEVKDALPADLPLGIRQRLSLAVAVIHRPEMLILD 432
Cdd:cd03262 81 VFQQFNLFPHLTVLENITLAPIkVKGMSKAEAEERALELLEKVGLADKADAYPAQLSGGQQQRVAIARALAMNPKVMLFD 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1820369315 433 EPTSGVDPVARDMFWQLMVDLArQDRVTIFISTHFMNEA-ERCDRISLMHAGKV 485
Cdd:cd03262 161 EPTSALDPELVGEVLDVMKDLA-EEGMTMVVVTHEMGFArEVADRVIFMDDGRI 213
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
274-488 |
5.10e-33 |
|
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: 128.28 E-value: 5.10e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 274 EIAIEARGLTMRFGNFVAVDHVNFRIARGEIFGFLGSNGCGKSTTMKMLTGLLPASEG-EAWLFGQP---VDPKDIatRQ 349
Cdd:COG1119 1 DPLLELRNVTVRRGGKTILDDISWTVKPGEHWAILGPNGAGKSTLLSLITGDLPPTYGnDVRLFGERrggEDVWEL--RK 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 350 RVGYMSQAFSLY--SELSVRQ--------NLELHARlfhiPDDEIAHRVAEMSERFMLTEVKDALPADLPLGIRQRLSLA 419
Cdd:COG1119 79 RIGLVSPALQLRfpRDETVLDvvlsgffdSIGLYRE----PTDEQRERARELLELLGLAHLADRPFGTLSQGEQRRVLIA 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 420 VAVIHRPEMLILDEPTSGVDPVARDMFWQLMVDLARQDRVTIFISTHFMNEAERC-DRISLMHAGKVLAS 488
Cdd:COG1119 155 RALVKDPELLILDEPTAGLDLGARELLLALLDKLAAEGAPTLVLVTHHVEEIPPGiTHVLLLKDGRVVAA 224
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
285-497 |
7.54e-33 |
|
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: 128.14 E-value: 7.54e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 285 RFGNFVAVDHVNFRIARGEIFGFLGSNGCGKSTTMKMLTGLLPASEGEAWLFGQPV---DPKDIAT--RQRVGYMSQAFS 359
Cdd:cd03294 33 KTGQTVGVNDVSLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGKVLIDGQDIaamSRKELRElrRKKISMVFQSFA 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 360 LYSELSVRQNLELHARLFHIPDDEIAHRVAEMSERFMLTEVKDALPADLPLGIRQRLSLAVAVIHRPEMLILDEPTSGVD 439
Cdd:cd03294 113 LLPHRTVLENVAFGLEVQGVPRAEREERAAEALELVGLEGWEHKYPDELSGGMQQRVGLARALAVDPDILLMDEAFSALD 192
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 440 PVAR-DMFWQLMVDLARQDRVTIFIsTHFMNEAERC-DRISLMHAGKVLASDTPQALVEQ 497
Cdd:cd03294 193 PLIRrEMQDELLRLQAELQKTIVFI-THDLDEALRLgDRIAIMKDGRLVQVGTPEEILTN 251
|
|
| ABC2_membrane_3 |
pfam12698 |
ABC-2 family transporter protein; This family is related to the ABC-2 membrane transporter ... |
572-896 |
2.28e-32 |
|
ABC-2 family transporter protein; This family is related to the ABC-2 membrane transporter family pfam01061.
Pssm-ID: 463674 [Multi-domain] Cd Length: 345 Bit Score: 129.05 E-value: 2.28e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 572 VILMFIMGYGISMDVEDLRFAVLDRDQTLSSQGWSQNIAGSRYFIEQAPLHSYDELDRRMRDGELAVAIEIPPNFGRDIA 651
Cdd:pfam12698 15 ILLLGLIFSNAVNDPEELPVAVVDEDNSSLSRQLVRALEASPTVNLVQYVDSEEEAKEALKNGKIDGLLVIPKGFSKDLL 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 652 RGTPVQIGVWVDGAMPNRAETVRGYVQAMHLAWLQEMAGRQSSPQRDTSLISIETRYRYNPDVKSLPAIVPaVIPLLLMM 731
Cdd:pfam12698 95 KGESATVTVYINSSNLLVSKLILNALQSLLQQLNASALVLLLEALSTSAPIPVESTPLFNPQSGYAYYLVG-LILMIIIL 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 732 IPAMLSALSVVREKELGSIINLYVTPTTRSEFLLGKQLPYIVLGMFNFFLLCAlsvFVFGVA-HKGSFLTLTLAALLYVT 810
Cdd:pfam12698 174 IGAAIIAVSIVEEKESRIKERLLVSGVSPLQYWLGKILGDFLVGLLQLLIILL---LLFGIGiPFGNLGLLLLLFLLYGL 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 811 IATGLGLLISTFMKSQIAAIFGTAIITLIPATqFSGMIDPVASLEGPGRWIGQIYPTSH----FLTIARGTfskalNLSD 886
Cdd:pfam12698 251 AYIALGYLLGSLFKNSEDAQSIIGIVILLLSG-FFGGLFPLEDPPSFLQWIFSIIPFFSpidgLLRLIYGD-----SLWE 324
|
330
....*....|
gi 1820369315 887 LWGSFIPLLI 896
Cdd:pfam12698 325 IAPSLIILLL 334
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
15-237 |
3.09e-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: 125.48 E-value: 3.09e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 15 LENVGQQYGATIALRDISLAIPARRMVGLIGPDGVGKSSLLSLIAGARAIEQGNVMVLGgdmRDVHHRR--DVCPK-IAW 91
Cdd:COG0410 6 VENLHAGYGGIHVLHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRSGSIRFDG---EDITGLPphRIARLgIGY 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 92 MPQGlgKNLYHTLSVYEN--VDFFARLFGHDKAERELRINELLQStgLAPFRDRPAGKLSGGMKQKLGLCCALIHDPQLL 169
Cdd:COG0410 83 VPEG--RRIFPSLTVEENllLGAYARRDRAEVRADLERVYELFPR--LKERRRQRAGTLSGGEQQMLAIGRALMSRPKLL 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1820369315 170 ILDEPTTGVDPLSRAQFWELIDSIRQRQpeMSVLV----ATAYMEEAERFdwlVAMNAGEVLATGSAAELKA 237
Cdd:COG0410 159 LLDEPSLGLAPLIVEEIFEIIRRLNREG--VTILLveqnARFALEIADRA---YVLERGRIVLEGTAAELLA 225
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
28-176 |
4.93e-32 |
|
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: 121.99 E-value: 4.93e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 28 LRDISLAIPARRMVGLIGPDGVGKSSLLSLIAGARAIEQGNVMVLGGDM--RDVHHRRDvcpKIAWMPQGLgkNLYHTLS 105
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDLtdDERKSLRK---EIGYVFQDP--QLFPRLT 75
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1820369315 106 VYENVDFFARLFGHDKAERELRINELLQSTGLAPFRDRPAGK----LSGGMKQKLGLCCALIHDPQLLILDEPTT 176
Cdd:pfam00005 76 VRENLRLGLLLKGLSKREKDARAEEALEKLGLGDLADRPVGErpgtLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
15-235 |
6.19e-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: 124.60 E-value: 6.19e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 15 LENVGQQYGA-TIALRDISLAIPARRMVGLIGPDGVGKSSLLSLIAGARAIEQGNVMVLGGDMRDVHHR--RDVCPKIAW 91
Cdd:cd03256 3 VENLSKTYPNgKKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGTDINKLKGKalRQLRRQIGM 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 92 MPQGLgkNLYHTLSVYENV--------DFFARLFGH-DKAERELRInELLQSTGLAPFRDRPAGKLSGGMKQKLGLCCAL 162
Cdd:cd03256 83 IFQQF--NLIERLSVLENVlsgrlgrrSTWRSLFGLfPKEEKQRAL-AALERVGLLDKAYQRADQLSGGQQQRVAIARAL 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1820369315 163 IHDPQLLILDEPTTGVDPLSRAQFWELIDSIRQRQpEMSVLVATAYMEEAERF-DWLVAMNAGEVLATGSAAEL 235
Cdd:cd03256 160 MQQPKLILADEPVASLDPASSRQVMDLLKRINREE-GITVIVSLHQVDLAREYaDRIVGLKDGRIVFDGPPAEL 232
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
15-237 |
7.39e-32 |
|
ATP-binding cassette transport system involved in resistance to organic solvents; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213228 [Multi-domain] Cd Length: 235 Bit Score: 124.15 E-value: 7.39e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 15 LENVGQQYGATIALRDISLAIPARRMVGLIGPDGVGKSSLLSLIAGARAIEQGNVMVLGGDMRDV------HHRRdvcpK 88
Cdd:cd03261 3 LRGLTKSFGGRTVLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGEDISGLseaelyRLRR----R 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 89 IAWMPQGLGknLYHTLSVYENVDFFARLFGhDKAERELR--INELLQSTGLAPFRDRPAGKLSGGMKQKLGLCCALIHDP 166
Cdd:cd03261 79 MGMLFQSGA--LFDSLTVFENVAFPLREHT-RLSEEEIReiVLEKLEAVGLRGAEDLYPAELSGGMKKRVALARALALDP 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1820369315 167 QLLILDEPTTGVDPLSRAQFWELIDSIrQRQPEMSVLVATAYMEEAERF-DWLVAMNAGEVLATGSAAELKA 237
Cdd:cd03261 156 ELLLYDEPTAGLDPIASGVIDDLIRSL-KKELGLTSIMVTHDLDTAFAIaDRIAVLYDGKIVAEGTPEELRA 226
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
15-503 |
1.86e-31 |
|
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: 129.56 E-value: 1.86e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 15 LENVGQQYGATIALRDISLAIPARRMVGLIGPDGVGKSSLLSLIAGA--RAIEQGNVMVLGGDMRDVHHRRDVCPKIAWM 92
Cdd:TIGR02633 4 MKGIVKTFGGVKALDGIDLEVRPGECVGLCGENGAGKSTLMKILSGVypHGTWDGEIYWSGSPLKASNIRDTERAGIVII 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 93 PQGLgkNLYHTLSVYENVdFFARLFGH-----DKAERELRINELLQSTGLAPFRD-RPAGKLSGGMKQKLGLCCALIHDP 166
Cdd:TIGR02633 84 HQEL--TLVPELSVAENI-FLGNEITLpggrmAYNAMYLRAKNLLRELQLDADNVtRPVGDYGGGQQQLVEIAKALNKQA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 167 QLLILDEPTTGvdpLSRAQFWELIDSIR--QRQPEMSVLVATAYMEEAERFDWLVAMNAGEVLATGSAAELKA-QTGSQT 243
Cdd:TIGR02633 161 RLLILDEPSSS---LTEKETEILLDIIRdlKAHGVACVYISHKLNEVKAVCDTICVIRDGQHVATKDMSTMSEdDIITMM 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 244 LEQAFIALLPeaqRQAHKTvvipprdsreEEIAIEARGLTMRF---GNFVAVDHVNFRIARGEIFGFLGSNGCGKSTTMK 320
Cdd:TIGR02633 238 VGREITSLYP---HEPHEI----------GDVILEARNLTCWDvinPHRKRVDDVSFSLRRGEILGVAGLVGAGRTELVQ 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 321 MLTGLLP-ASEGEAWLFGQPVDPKDIATRQRVGYM-----SQAFSLYSELSVRQNLELHA--RLFHIPDDEIAHRVAEMS 392
Cdd:TIGR02633 305 ALFGAYPgKFEGNVFINGKPVDIRNPAQAIRAGIAmvpedRKRHGIVPILGVGKNITLSVlkSFCFKMRIDAAAELQIIG 384
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 393 ERFMLTEVKDALPaDLPL-----GIRQRLSLAVAVIHRPEMLILDEPTSGVDPVARDMFWQLMVDLARQDRVTIFISTHF 467
Cdd:TIGR02633 385 SAIQRLKVKTASP-FLPIgrlsgGNQQKAVLAKMLLTNPRVLILDEPTRGVDVGAKYEIYKLINQLAQEGVAIIVVSSEL 463
|
490 500 510
....*....|....*....|....*....|....*..
gi 1820369315 468 MNEAERCDRISLMHAGKVLASDTPQALV-EQRGAASL 503
Cdd:TIGR02633 464 AEVLGLSDRVLVIGEGKLKGDFVNHALTqEQVLAAAL 500
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
15-225 |
2.40e-31 |
|
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213179 [Multi-domain] Cd Length: 157 Bit Score: 120.04 E-value: 2.40e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 15 LENVGQQYGATIALRDISLAIPARRMVGLIGPDGVGKSSLLSLIAGARAIEQGNVMVLGGDM--RDVHHRRDvcpKIAWM 92
Cdd:cd00267 2 IENLSFRYGGRTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGKDIakLPLEELRR---RIGYV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 93 PQglgknlyhtlsvyenvdffarlfghdkaerelrinellqstglapfrdrpagkLSGGMKQKLGLCCALIHDPQLLILD 172
Cdd:cd00267 79 PQ-----------------------------------------------------LSGGQRQRVALARALLLNPDLLLLD 105
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1820369315 173 EPTTGVDPLSRAQFWELIDSIRQRQpeMSVLVATAYMEEAERF-DWLVAMNAGE 225
Cdd:cd00267 106 EPTSGLDPASRERLLELLRELAEEG--RTVIIVTHDPELAELAaDRVIVLKDGK 157
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
15-235 |
3.71e-31 |
|
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ABC-type transporter encoded by metN of the metNPQ operon in Bacillus subtilis that is involved in methionine transport. Other members of this system include the MetP permease and the MetQ substrate binding protein. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213225 [Multi-domain] Cd Length: 233 Bit Score: 122.30 E-value: 3.71e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 15 LENVGQQYGAT----IALRDISLAIPARRMVGLIGPDGVGKSSLLSLIAGARAIEQGNVMVLGGDMRDVHHR--RDVCPK 88
Cdd:cd03258 4 LKNVSKVFGDTggkvTALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGSVLVDGTDLTLLSGKelRKARRR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 89 IAWMPQGLgkNLYHTLSVYENVDFFARLFGHDKAERELRINELLQSTGLAPFRDRPAGKLSGGMKQKLGLCCALIHDPQL 168
Cdd:cd03258 84 IGMIFQHF--NLLSSRTVFENVALPLEIAGVPKAEIEERVLELLELVGLEDKADAYPAQLSGGQKQRVGIARALANNPKV 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1820369315 169 LILDEPTTGVDPLSRAQFWELIDSIRQRQpEMSVLVATAYMEEAERFDWLVA-MNAGEVLATGSAAEL 235
Cdd:cd03258 162 LLCDEATSALDPETTQSILALLRDINREL-GLTIVLITHEMEVVKRICDRVAvMEKGEVVEEGTVEEV 228
|
|
| galliderm_ABC |
TIGR03740 |
gallidermin-class lantibiotic protection ABC transporter, ATP-binding subunit; Model TIGR03731 ... |
16-248 |
4.85e-31 |
|
gallidermin-class lantibiotic protection ABC transporter, ATP-binding subunit; Model TIGR03731 represents the family of all lantibiotics related to gallidermin, including epidermin, mutatin, and nisin. This protein family describes the ATP-binding subunit of a gallidermin/epidermin class lantibiotic protection transporter. It is largely restricted to gallidermin-family lantibiotic biosynthesis and export cassettes, but also occurs in orphan transporter cassettes in species that lack candidate lantibiotic precursor and synthetase genes.
Pssm-ID: 163452 [Multi-domain] Cd Length: 223 Bit Score: 121.74 E-value: 4.85e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 16 ENVGQQYGATIALRDISLAIPARRMVGLIGPDGVGKSSLLSLIAGARAIEQGNVMVLGGDM--RDVHhrrDVCPKIAWMP 93
Cdd:TIGR03740 4 KNLSKRFGKQTAVNNISLTVPKNSVYGLLGPNGAGKSTLLKMITGILRPTSGEIIFDGHPWtrKDLH---KIGSLIESPP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 94 qglgknLYHTLSVYENVDFFARLFGHDKAerelRINELLQSTGLAPFRDRPAGKLSGGMKQKLGLCCALIHDPQLLILDE 173
Cdd:TIGR03740 81 ------LYENLTARENLKVHTTLLGLPDS----RIDEVLNIVDLTNTGKKKAKQFSLGMKQRLGIAIALLNHPKLLILDE 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1820369315 174 PTTGVDPLSRAQFWELIDSIRQRQpeMSVLVATAYMEEAErfdwLVAMNAGeVLATGSAAELKAQTGSQTLEQAF 248
Cdd:TIGR03740 151 PTNGLDPIGIQELRELIRSFPEQG--ITVILSSHILSEVQ----QLADHIG-IISEGVLGYQGKINKSENLEKLF 218
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
292-485 |
7.77e-31 |
|
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: 120.44 E-value: 7.77e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 292 VDHVNFRIARGEIFGFLGSNGCGKSTTMKMLTGLLPASEGEAWLFGQPVDPKDiaTRQRVGYMSQ--AFSLYSElSVRQN 369
Cdd:cd03226 16 LDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLNGKPIKAKE--RRKSIGYVMQdvDYQLFTD-SVREE 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 370 LELHARLfhiPDDEIAhRVAEMSERFMLTEVKDALPADLPLGIRQRLSLAVAVIHRPEMLILDEPTSGVDPVARDMFWQL 449
Cdd:cd03226 93 LLLGLKE---LDAGNE-QAETVLKDLDLYALKERHPLSLSGGQKQRLAIAAALLSGKDLLIFDEPTSGLDYKNMERVGEL 168
|
170 180 190
....*....|....*....|....*....|....*....
gi 1820369315 450 MVDLARQDrVTIFISTH---FMneAERCDRISLMHAGKV 485
Cdd:cd03226 169 IRELAAQG-KAVIVITHdyeFL--AKVCDRVLLLANGAI 204
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
277-484 |
8.28e-31 |
|
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: 119.02 E-value: 8.28e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 277 IEARGLTMRFGNF--VAVDHVNFRIARGEIFGFLGSNGCGKSTTMKMLTGLLPASEGEAWLFGQPVDPKDIAT-RQRVGY 353
Cdd:cd03228 1 IEFKNVSFSYPGRpkPVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGVDLRDLDLESlRKNIAY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 354 MSQAFSLYSElSVRQNLelharlfhipddeiahrvaemserfmltevkdalpadLPLGIRQRLSLAVAVIHRPEMLILDE 433
Cdd:cd03228 81 VPQDPFLFSG-TIRENI-------------------------------------LSGGQRQRIAIARALLRDPPILILDE 122
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1820369315 434 PTSGVDPVARDMFWQLMvdLARQDRVTIFISTHFMNEAERCDRISLMHAGK 484
Cdd:cd03228 123 ATSALDPETEALILEAL--RALAKGKTVIVIAHRLSTIRDADRIIVLDDGR 171
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
8-485 |
1.07e-30 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 127.47 E-value: 1.07e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 8 TSPPIALLENVGQQYGATIALRDISLAIPARRMVGLIGPDGVGKSSLLSLIAGARAIEQGNVMVLGgdmrdvHHRRDVCP 87
Cdd:PRK15439 7 TAPPLLCARSISKQYSGVEVLKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIGG------NPCARLTP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 88 KIAwmpQGLG-------KNLYHTLSVYENVDFfaRLFGHDKAERelRINELLQSTGLAPFRDRPAGKLSGGMKQKLGLCC 160
Cdd:PRK15439 81 AKA---HQLGiylvpqePLLFPNLSVKENILF--GLPKRQASMQ--KMKQLLAALGCQLDLDSSAGSLEVADRQIVEILR 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 161 ALIHDPQLLILDEPTTGVDPLSRAQFWELIDSIRQrQPEMSVLVATAYMEEAERFDWLVAMNAGEVLATGSAAEL----- 235
Cdd:PRK15439 154 GLMRDSRILILDEPTASLTPAETERLFSRIRELLA-QGVGIVFISHKLPEIRQLADRISVMRDGTIALSGKTADLstddi 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 236 ------KAQTGSQTLEQAFIALLPEAQR-QAHKTVVIPPRDSREEeiaieargltmrfgNFVavdHVNFRIARGEIFGFL 308
Cdd:PRK15439 233 iqaitpAAREKSLSASQKLWLELPGNRRqQAAGAPVLTVEDLTGE--------------GFR---NISLEVRAGEILGLA 295
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 309 GSNGCGKSTTMKMLTGLLPASEGEAWLFGQPVDPKDIATRQRVG--YMS---QAFSLYSELSVRQN---LELHARLFHI- 379
Cdd:PRK15439 296 GVVGAGRTELAETLYGLRPARGGRIMLNGKEINALSTAQRLARGlvYLPedrQSSGLYLDAPLAWNvcaLTHNRRGFWIk 375
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 380 PDDEIAhrVAEMSERFMLTEVKDALPA--DLPLGIRQRLSLAVAVIHRPEMLILDEPTSGVDPVARDMFWQLMVDLARQD 457
Cdd:PRK15439 376 PARENA--VLERYRRALNIKFNHAEQAarTLSGGNQQKVLIAKCLEASPQLLIVDEPTRGVDVSARNDIYQLIRSIAAQN 453
|
490 500
....*....|....*....|....*....
gi 1820369315 458 RVTIFISTHFmNEAER-CDRISLMHAGKV 485
Cdd:PRK15439 454 VAVLFISSDL-EEIEQmADRVLVMHQGEI 481
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
285-497 |
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: 121.34 E-value: 1.17e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 285 RFGNFVAVDHVNFRIARGEIFGFLGSNGCGKSTTMKMLTGLLPASEGE-------AWLFGqpvdpkdiatrqrvgyMSQA 357
Cdd:COG1134 35 RREEFWALKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTSGRvevngrvSALLE----------------LGAG 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 358 FSlySELSVRQNLELHARLFHIPDDEIAHRVAEMsERFmlTEVKDALpaDLPL-----GIRQRLSLAVAVIHRPEMLILD 432
Cdd:COG1134 99 FH--PELTGRENIYLNGRLLGLSRKEIDEKFDEI-VEF--AELGDFI--DQPVktyssGMRARLAFAVATAVDPDILLVD 171
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1820369315 433 EPTSGVDPVARDMFWQLMVDLARQDRvTIFISTHFMNEAER-CDRISLMHAGKVLASDTPQALVEQ 497
Cdd:COG1134 172 EVLAVGDAAFQKKCLARIRELRESGR-TVIFVSHSMGAVRRlCDRAIWLEKGRLVMDGDPEEVIAA 236
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
246-499 |
1.28e-30 |
|
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: 127.95 E-value: 1.28e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 246 QAFIALLPEAQRQAHKTVvipprdSREEEIAIEARGLTMRF-GNFVAVDHVNFRIARGEIFGFLGSNGCGKSTTMKMLTG 324
Cdd:COG4988 312 FALLDAPEPAAPAGTAPL------PAAGPPSIELEDVSFSYpGGRPALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLG 385
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 325 LLPASEGEAWLFGQPVDPKDIAT-RQRVGYMSQAFSLYSElSVRQNLELHARlfHIPDDEIaHRVAEMSErfmLTEVKDA 403
Cdd:COG4988 386 FLPPYSGSILINGVDLSDLDPASwRRQIAWVPQNPYLFAG-TIRENLRLGRP--DASDEEL-EAALEAAG---LDEFVAA 458
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 404 LPADL--PL---------GIRQRLSLAVAVIHRPEMLILDEPTSGVDPVARDMFWQLMVDLARQdrVTIFISTHFMNEAE 472
Cdd:COG4988 459 LPDGLdtPLgeggrglsgGQAQRLALARALLRDAPLLLLDEPTAHLDAETEAEILQALRRLAKG--RTVILITHRLALLA 536
|
250 260
....*....|....*....|....*..
gi 1820369315 473 RCDRISLMHAGKVLASDTPQALVEQRG 499
Cdd:COG4988 537 QADRILVLDDGRIVEQGTHEELLAKNG 563
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
15-235 |
1.53e-30 |
|
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of fundamental importance in the cell physiology of bacteria because phosphate is required as a nutrient. The Pst system of E. coli comprises four distinct subunits encoded by the pstS, pstA, pstB, and pstC genes. The PstS protein is a phosphate-binding protein located in the periplasmic space. PstA and PstC are hydrophobic and they form the transmembrane portion of the Pst system. PstB is the catalytic subunit, which couples the energy of ATP hydrolysis to the import of phosphate across cellular membranes through the Pst system, often referred as ABC-protein. PstB belongs to one of the largest superfamilies of proteins characterized by a highly conserved adenosine triphosphate (ATP) binding cassette (ABC), which is also a nucleotide binding domain (NBD).
Pssm-ID: 213227 [Multi-domain] Cd Length: 227 Bit Score: 120.36 E-value: 1.53e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 15 LENVGQQYGATIALRDISLAIPARRMVGLIGPDGVGKSSLLSLIAGARAIEQ-----GNVMVLGGDMRD-----VHHRRd 84
Cdd:cd03260 3 LRDLNVYYGDKHALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRLNDLIPgapdeGEVLLDGKDIYDldvdvLELRR- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 85 vcpKIAWMPQGLgkNLYHtLSVYENVDFFARLFG-HDKAERELRINELLQSTGLAP-FRDRP-AGKLSGGMKQKLGLCCA 161
Cdd:cd03260 82 ---RVGMVFQKP--NPFP-GSIYDNVAYGLRLHGiKLKEELDERVEEALRKAALWDeVKDRLhALGLSGGQQQRLCLARA 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1820369315 162 LIHDPQLLILDEPTTGVDPLSRAQFWELIDSIRQrqpEMSVLVATAYMEEAERF-DWLVAMNAGEVLATGSAAEL 235
Cdd:cd03260 156 LANEPEVLLLDEPTSALDPISTAKIEELIAELKK---EYTIVIVTHNMQQAARVaDRTAFLLNGRLVEFGPTEQI 227
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
268-485 |
1.65e-30 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 121.30 E-value: 1.65e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 268 RDSREEEIAIEARGLTMRFGNFVAVDHVNFRIARGEIFGFLGSNGCGKSTTMKML---TGLLPAS--EGEAWLFGQP--- 339
Cdd:COG1117 3 APASTLEPKIEVRNLNVYYGDKQALKDINLDIPENKVTALIGPSGCGKSTLLRCLnrmNDLIPGArvEGEILLDGEDiyd 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 340 --VDPkdIATRQRVGYMSQ---AFSlyseLSVRQNLELHARLFHIPD-DEIAHRVaEMS-ERFML-TEVKDAL--PA-DL 408
Cdd:COG1117 83 pdVDV--VELRRRVGMVFQkpnPFP----KSIYDNVAYGLRLHGIKSkSELDEIV-EESlRKAALwDEVKDRLkkSAlGL 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1820369315 409 PLGIRQRLSLAVAVIHRPEMLILDEPTSGVDPVARDMFWQLMVDLArqDRVTIFISTHFMNEAERC-DRISLMHAGKV 485
Cdd:COG1117 156 SGGQQQRLCIARALAVEPEVLLMDEPTSALDPISTAKIEELILELK--KDYTIVIVTHNMQQAARVsDYTAFFYLGEL 231
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
276-500 |
1.74e-30 |
|
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: 127.57 E-value: 1.74e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 276 AIEARGLTMRF--GNFVAVDHVNFRIARGEIFGFLGSNGCGKSTTMKMLTGLLPASEGEAWLFGQPVDPKDIAT-RQRVG 352
Cdd:COG4987 333 SLELEDVSFRYpgAGRPVLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFLDPQSGSITLGGVDLRDLDEDDlRRRIA 412
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 353 YMSQAFSLYSElSVRQNLELhARlfhiPD--DEIAHRVAEMSErfmLTEVKDALPA--DLPLGI---------RQRLSLA 419
Cdd:COG4987 413 VVPQRPHLFDT-TLRENLRL-AR----PDatDEELWAALERVG---LGDWLAALPDglDTWLGEggrrlsggeRRRLALA 483
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 420 VAVIHRPEMLILDEPTSGVDPVARDMFWQLMVDLArQDRVTIFIsTHFMNEAERCDRISLMHAGKVLASDTPQALVEQRG 499
Cdd:COG4987 484 RALLRDAPILLLDEPTEGLDAATEQALLADLLEAL-AGRTVLLI-THRLAGLERMDRILVLEDGRIVEQGTHEELLAQNG 561
|
.
gi 1820369315 500 A 500
Cdd:COG4987 562 R 562
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
5-240 |
1.90e-30 |
|
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: 127.57 E-value: 1.90e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 5 PQDTSPPIALlENVGQQY-GATIALRDISLAIPARRMVGLIGPDGVGKSSLLSLIAGARAIEQGNVMVLGGDMRDVHhRR 83
Cdd:COG4988 330 PAAGPPSIEL-EDVSFSYpGGRPALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPPYSGSILINGVDLSDLD-PA 407
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 84 DVCPKIAWMPQglgkN--LYHTlSVYENVdffarLFGHDKAERElRINELLQSTGLAPF-RDRPAG----------KLSG 150
Cdd:COG4988 408 SWRRQIAWVPQ----NpyLFAG-TIRENL-----RLGRPDASDE-ELEAALEAAGLDEFvAALPDGldtplgeggrGLSG 476
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 151 GMKQKLGLCCALIHDPQLLILDEPTTGVDPLSRAQFWELIDSIRQRQpemSVLVATAYMEEAERFDWLVAMNAGEVLATG 230
Cdd:COG4988 477 GQAQRLALARALLRDAPLLLLDEPTAHLDAETEAEILQALRRLAKGR---TVILITHRLALLAQADRILVLDDGRIVEQG 553
|
250
....*....|
gi 1820369315 231 SAAELKAQTG 240
Cdd:COG4988 554 THEELLAKNG 563
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
10-248 |
1.93e-30 |
|
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: 120.57 E-value: 1.93e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 10 PPIALLENVGQQYGATIALRDISLAIPARRMVGLIGPDGVGKSSLLSLIAG-ARAIEQGNVMVLGgdmrdvhHRR----- 83
Cdd:COG1119 1 DPLLELRNVTVRRGGKTILDDISWTVKPGEHWAILGPNGAGKSTLLSLITGdLPPTYGNDVRLFG-------ERRggedv 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 84 -DVCPKIAWMPQGLGKNLYHTLSVYENV--DFFA--RLFGHDKAERELRINELLQSTGLAPFRDRPAGKLSGGMKQKLGL 158
Cdd:COG1119 74 wELRKRIGLVSPALQLRFPRDETVLDVVlsGFFDsiGLYREPTDEQRERARELLELLGLAHLADRPFGTLSQGEQRRVLI 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 159 CCALIHDPQLLILDEPTTGVDPLSRAQFWELIDSIRQrQPEMSVLVATAYMEEA-ERFDWLVAMNAGEVLATGSAAELka 237
Cdd:COG1119 154 ARALVKDPELLILDEPTAGLDLGARELLLALLDKLAA-EGAPTLVLVTHHVEEIpPGITHVLLLKDGRVVAAGPKEEV-- 230
|
250
....*....|.
gi 1820369315 238 qTGSQTLEQAF 248
Cdd:COG1119 231 -LTSENLSEAF 240
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
291-491 |
2.75e-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: 129.75 E-value: 2.75e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 291 AVDHVNFRIARGEIFGFLGSNGCGKSTTMKMLTGLLPASEGEAWLFGQPVDPKDIATRQRVGYMSQAFSLYSELSVRQNL 370
Cdd:TIGR01257 945 AVDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGKDIETNLDAVRQSLGMCPQHNILFHHLTVAEHI 1024
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 371 ELHARLFHIPDDEIAHRVAEMSERFMLTEVKDALPADLPLGIRQRLSLAVAVIHRPEMLILDEPTSGVDPVARDMFWQLM 450
Cdd:TIGR01257 1025 LFYAQLKGRSWEEAQLEMEAMLEDTGLHHKRNEEAQDLSGGMQRKLSVAIAFVGDAKVVVLDEPTSGVDPYSRRSIWDLL 1104
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1820369315 451 VDLaRQDRvTIFISTHFMNEAERC-DRISLMHAGKVLASDTP 491
Cdd:TIGR01257 1105 LKY-RSGR-TIIMSTHHMDEADLLgDRIAIISQGRLYCSGTP 1144
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
291-523 |
3.30e-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: 129.75 E-value: 3.30e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 291 AVDHVNFRIARGEIFGFLGSNGCGKSTTMKMLTGLLPASEGEAWLFGQPVDPKDIATRQRVGYMSQAFSLYSELSVRQNL 370
Cdd:TIGR01257 1954 AVDRLCVGVRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAGKSILTNISDVHQNMGYCPQFDAIDDLLTGREHL 2033
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 371 ELHARLFHIPDDEIaHRVAEMS-ERFMLTEVKDALPADLPLGIRQRLSLAVAVIHRPEMLILDEPTSGVDPVARDMFWQL 449
Cdd:TIGR01257 2034 YLYARLRGVPAEEI-EKVANWSiQSLGLSLYADRLAGTYSGGNKRKLSTAIALIGCPPLVLLDEPTTGMDPQARRMLWNT 2112
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1820369315 450 MVDLARQDRVTIfISTHFMNEAER-CDRISLMHAGKVLASDTPQALVEQRGaasleEAFIAWLKEAQPSSPVPED 523
Cdd:TIGR01257 2113 IVSIIREGRAVV-LTSHSMEECEAlCTRLAIMVKGAFQCLGTIQHLKSKFG-----DGYIVTMKIKSPKDDLLPD 2181
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
15-235 |
3.98e-30 |
|
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: 119.71 E-value: 3.98e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 15 LENVGQQYGA-TIALRDISLAIPARRMVGLIGPDGVGKSSLLSLIAgaRAIE--QGNVMVLGGDMRD---VHHRRdvcpK 88
Cdd:cd03295 3 FENVTKRYGGgKKAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMIN--RLIEptSGEIFIDGEDIREqdpVELRR----K 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 89 IAWMPQGLGknLYHTLSVYENVDFFARLFGHDKAERELRINELLQSTGLAP--FRDRPAGKLSGGMKQKLGLCCALIHDP 166
Cdd:cd03295 77 IGYVIQQIG--LFPHMTVEENIALVPKLLKWPKEKIRERADELLALVGLDPaeFADRYPHELSGGQQQRVGVARALAADP 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 167 QLLILDEPTTGVDPLSRAQFWELIDSIRQRQPEMSVLVaTAYMEEAERF-DWLVAMNAGEVLATGSAAEL 235
Cdd:cd03295 155 PLLLMDEPFGALDPITRDQLQEEFKRLQQELGKTIVFV-THDIDEAFRLaDRIAIMKNGEIVQVGTPDEI 223
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
15-235 |
4.92e-30 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 122.49 E-value: 4.92e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 15 LENVGQQYGATIALRDISLAIPARRMVGLIGPDGVGKSSLLSLIAGARAIEQGNVMvLGGdmRDVHH----RRDvcpkIA 90
Cdd:COG3839 6 LENVSKSYGGVEALKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAGLEDPTSGEIL-IGG--RDVTDlppkDRN----IA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 91 WMPQGLGknLYHTLSVYENVDFFARLFGHDKAERELRINELLQSTGLAPFRDRPAGKLSGGMKQKLGLCCALIHDPQLLI 170
Cdd:COG3839 79 MVFQSYA--LYPHMTVYENIAFPLKLRKVPKAEIDRRVREAAELLGLEDLLDRKPKQLSGGQRQRVALGRALVREPKVFL 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1820369315 171 LDEPTTGVDPLSRaqfWELIDSIR--QRQPEMSVLVATAYMEEAERF-DWLVAMNAGEVLATGSAAEL 235
Cdd:COG3839 157 LDEPLSNLDAKLR---VEMRAEIKrlHRRLGTTTIYVTHDQVEAMTLaDRIAVMNDGRIQQVGTPEEL 221
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
15-212 |
1.29e-29 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 118.81 E-value: 1.29e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 15 LENVGQQYG----ATIALRDISLAIPARRMVGLIGPDGVGKSSLLSLIAGARAIEQGNVMVlggDMRDVHH----RRDVC 86
Cdd:COG4525 6 VRHVSVRYPgggqPQPALQDVSLTIESGEFVVALGASGCGKTTLLNLIAGFLAPSSGEITL---DGVPVTGpgadRGVVF 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 87 PKIAWMPQglgknlyhtLSVYENVDFFARLFGHDKAERELRINELLQSTGLAPFRDRPAGKLSGGMKQKLGLCCALIHDP 166
Cdd:COG4525 83 QKDALLPW---------LNVLDNVAFGLRLRGVPKAERRARAEELLALVGLADFARRRIWQLSGGMRQRVGIARALAADP 153
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1820369315 167 QLLILDEPTTGVDPLSRAQFWELIDSIRQRQPEMsVLVATAYMEEA 212
Cdd:COG4525 154 RFLLMDEPFGALDALTREQMQELLLDVWQRTGKG-VFLITHSVEEA 198
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
15-244 |
1.30e-29 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 117.55 E-value: 1.30e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 15 LENVGQQYGATIAlrDISLAIPARRMVGLIGPDGVGKSSLLSLIAGARAIEQGNVMVLGGDMRDVH-HRRdvcpKIAWMP 93
Cdd:COG3840 4 LDDLTYRYGDFPL--RFDLTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILWNGQDLTALPpAER----PVSMLF 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 94 QglGKNLYHTLSVYENVDF----FARLfghDKAERElRINELLQSTGLAPFRDRPAGKLSGGMKQKLGLCCALIHDPQLL 169
Cdd:COG3840 78 Q--ENNLFPHLTVAQNIGLglrpGLKL---TAEQRA-QVEQALERVGLAGLLDRLPGQLSGGQRQRVALARCLVRKRPIL 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1820369315 170 ILDEPTTGVDPLSRAQFWELIDSIRQRQpEMSVLVATAYMEEAERF-DWLVAMNAGEVLATGSAAELKAQTGSQTL 244
Cdd:COG3840 152 LLDEPFSALDPALRQEMLDLVDELCRER-GLTVLMVTHDPEDAARIaDRVLLVADGRIAADGPTAALLDGEPPPAL 226
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
277-498 |
1.74e-29 |
|
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: 117.67 E-value: 1.74e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 277 IEARGLTMRFGN-FVAVDHVNFRIARGEIFGFLGSNGCGKSTTMKMLTGLLPASEGEAWLFGQPV---DPKDI-ATRQRV 351
Cdd:cd03256 1 IEVENLSKTYPNgKKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGTDInklKGKALrQLRRQI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 352 GYMSQAFSLYSELSVRQNLeLHARL------------FHIPDDEIAhrvAEMSERFMLTEVKDALPADLPLGIRQRLSLA 419
Cdd:cd03256 81 GMIFQQFNLIERLSVLENV-LSGRLgrrstwrslfglFPKEEKQRA---LAALERVGLLDKAYQRADQLSGGQQQRVAIA 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 420 VAVIHRPEMLILDEPTSGVDPVARDMFWQLMVDLARQDRVTIFISTHFMNEAER-CDRISLMHAGKVLASDTPQALVEQR 498
Cdd:cd03256 157 RALMQQPKLILADEPVASLDPASSRQVMDLLKRINREEGITVIVSLHQVDLAREyADRIVGLKDGRIVFDGPPAELTDEV 236
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
15-237 |
1.88e-29 |
|
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: 117.26 E-value: 1.88e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 15 LENVGQQYGATIALRDISLAIPARRMVGLIGPDGVGKSSLLSLIAGARAIEQGNVMVLGGDMRD--VHHRRDVcpKIAWM 92
Cdd:cd03218 3 AENLSKRYGKRKVVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDGQDITKlpMHKRARL--GIGYL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 93 PQGlgKNLYHTLSVYENVDFFARLFGHDKAERELRINELLQSTGLAPFRDRPAGKLSGGMKQKLGLCCALIHDPQLLILD 172
Cdd:cd03218 81 PQE--ASIFRKLTVEENILAVLEIRGLSKKEREEKLEELLEEFHITHLRKSKASSLSGGERRRVEIARALATNPKFLLLD 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1820369315 173 EPTTGVDPLSRAQFWELIDSIRQRQpeMSVL------------VATAYMeeaerfdwlvaMNAGEVLATGSAAELKA 237
Cdd:cd03218 159 EPFAGVDPIAVQDIQKIIKILKDRG--IGVLitdhnvretlsiTDRAYI-----------IYEGKVLAEGTPEEIAA 222
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
291-497 |
2.33e-29 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 118.58 E-value: 2.33e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 291 AVDHVNFRIARGEIFGFLGSNGCGKSTTMKMLTGLLPASEGEAWLFGQPVDPK---DIatRQRVGYMSQ----------- 356
Cdd:PRK13635 22 ALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGGMVLSEEtvwDV--RRQVGMVFQnpdnqfvgatv 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 357 ----AFSLyselsvrqnlELHArlfhIPDDEIAHRVAEMSERFMLTEVKDALPADLPLGIRQRLSLAVAVIHRPEMLILD 432
Cdd:PRK13635 100 qddvAFGL----------ENIG----VPREEMVERVDQALRQVGMEDFLNREPHRLSGGQKQRVAIAGVLALQPDIIILD 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1820369315 433 EPTSGVDPVARDMFWQLMVDLARQDRVTIFISTHFMNEAERCDRISLMHAGKVLASDTPQALVEQ 497
Cdd:PRK13635 166 EATSMLDPRGRREVLETVRQLKEQKGITVLSITHDLDEAAQADRVIVMNKGEILEEGTPEEIFKS 230
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
16-235 |
4.31e-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: 116.67 E-value: 4.31e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 16 ENVGQQYGATIALRDISLAIPARRMVGLIGPDGVGKSSLLSLIAGARAIEQGNVMVLGGDMRDVHHRRDvcpKIAWMPQG 95
Cdd:cd03296 6 RNVSKRFGDFVALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGGEDATDVPVQER---NVGFVFQH 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 96 LGknLYHTLSVYENVDFFARL----FGHDKAERELRINELLQSTGLAPFRDRPAGKLSGGMKQKLGLCCALIHDPQLLIL 171
Cdd:cd03296 83 YA--LFRHMTVFDNVAFGLRVkprsERPPEAEIRAKVHELLKLVQLDWLADRYPAQLSGGQRQRVALARALAVEPKVLLL 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1820369315 172 DEPTTGVDPLSRAqfwELIDSIRQRQPEM---SVLVATAYMEEAERFDWLVAMNAGEVLATGSAAEL 235
Cdd:cd03296 161 DEPFGALDAKVRK---ELRRWLRRLHDELhvtTVFVTHDQEEALEVADRVVVMNKGRIEQVGTPDEV 224
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
290-497 |
6.58e-29 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 117.11 E-value: 6.58e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 290 VAVDHVNFRIARGEIFGFLGSNGCGKSTTMKMLTGLLPASEGEAWLFGqpVDPKDIAT----RQRVGYM-----SQAFSL 360
Cdd:PRK13633 24 LALDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVYVDG--LDTSDEENlwdiRNKAGMVfqnpdNQIVAT 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 361 YSELSVR---QNLelharlfHIPDDEIAHRVAEMSERFMLTEVKDALPADLPLGIRQRLSLAVAVIHRPEMLILDEPTSG 437
Cdd:PRK13633 102 IVEEDVAfgpENL-------GIPPEEIRERVDESLKKVGMYEYRRHAPHLLSGGQKQRVAIAGILAMRPECIIFDEPTAM 174
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 438 VDPVARDMFWQLMVDLARQDRVTIFISTHFMNEAERCDRISLMHAGKVLASDTPQALVEQ 497
Cdd:PRK13633 175 LDPSGRREVVNTIKELNKKYGITIILITHYMEEAVEADRIIVMDSGKVVMEGTPKEIFKE 234
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
302-489 |
7.11e-29 |
|
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: 115.08 E-value: 7.11e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 302 GEIFGFLGSNGCGKSTTMKMLTGLLPASEGEAWLFGQPVDPK----DIATRQR-VGYMSQAFSLYSELSVRQNLELHARL 376
Cdd:cd03297 23 EEVTGIFGASGAGKSTLLRCIAGLEKPDGGTIVLNGTVLFDSrkkiNLPPQQRkIGLVFQQYALFPHLNVRENLAFGLKR 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 377 FHIPDDEIahRVAEMSERFMLTEVKDALPADLPLGIRQRLSLAVAVIHRPEMLILDEPTSGVDPVARDMFWQLMVDLARQ 456
Cdd:cd03297 103 KRNREDRI--SVDELLDLLGLDHLLNRYPAQLSGGEKQRVALARALAAQPELLLLDEPFSALDRALRLQLLPELKQIKKN 180
|
170 180 190
....*....|....*....|....*....|....
gi 1820369315 457 DRVTIFISTHFMNEAER-CDRISLMHAGKVLASD 489
Cdd:cd03297 181 LNIPVIFVTHDLSEAEYlADRIVVMEDGRLQYIG 214
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
19-251 |
8.32e-29 |
|
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: 116.06 E-value: 8.32e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 19 GQQYGATIALRDISLAIPARRMVGLIGPDGVGKSSLLSLIAGARAIEQGNVMVLGgdmRDVHHRRD--VCPKIAWMPQgl 96
Cdd:COG1124 12 GQGGRRVPVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVTFDG---RPVTRRRRkaFRRRVQMVFQ-- 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 97 gkNLYHTL----SVYENVDFFARLFGHDKAERelRINELLQSTGLAP-FRDRPAGKLSGGMKQKLGLCCALIHDPQLLIL 171
Cdd:COG1124 87 --DPYASLhprhTVDRILAEPLRIHGLPDREE--RIAELLEQVGLPPsFLDRYPHQLSGGQRQRVAIARALILEPELLLL 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 172 DEPTTGVDPLSRAQFWELIDSIRQRQpEMSVLVATAYMEEAERF-DWLVAMNAGEVLATGSAAELKAQTGS---QTLEQA 247
Cdd:COG1124 163 DEPTSALDVSVQAEILNLLKDLREER-GLTYLFVSHDLAVVAHLcDRVAVMQNGRIVEELTVADLLAGPKHpytRELLAA 241
|
....
gi 1820369315 248 FIAL 251
Cdd:COG1124 242 SLAF 245
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
15-235 |
1.56e-28 |
|
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and the ATPase component of the spermidine/putrescine-preferential uptake system consisting of PotA, -B, -C, and -D. PotA has two domains with the N-terminal domain containing the ATPase activity and the residues required for homodimerization with PotA and heterdimerization with PotB. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213267 [Multi-domain] Cd Length: 232 Bit Score: 114.64 E-value: 1.56e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 15 LENVGQQYGATIALRDISLAIPARRMVGLIGPDGVGKSSLLSLIAGARAIEQGNVMVLGGDMRDVH-HRRD---VCPKIA 90
Cdd:cd03300 3 LENVSKFYGGFVALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGKDITNLPpHKRPvntVFQNYA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 91 WMPQglgknlyhtLSVYENVDFFARLFGHDKAERELRINELLQSTGLAPFRDRPAGKLSGGMKQKLGLCCALIHDPQLLI 170
Cdd:cd03300 83 LFPH---------LTVFENIAFGLRLKKLPKAEIKERVAEALDLVQLEGYANRKPSQLSGGQQQRVAIARALVNEPKVLL 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1820369315 171 LDEPTTGVDPLSRAQFWELIDSIrQRQPEMSVLVATAYMEEAERF-DWLVAMNAGEVLATGSAAEL 235
Cdd:cd03300 154 LDEPLGALDLKLRKDMQLELKRL-QKELGITFVFVTHDQEEALTMsDRIAVMNKGKIQQIGTPEEI 218
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
290-491 |
1.63e-28 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 116.30 E-value: 1.63e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 290 VAVDHVNFRIARGEIFGFLGSNGCGKSTTMKMLTGLLPASEGEAWLFG-----QPVDPKDIatRQRVGYMSQ--AFSLYS 362
Cdd:PRK13637 21 KALDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDGvditdKKVKLSDI--RKKVGLVFQypEYQLFE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 363 ElSVRQNLELHARLFHIPDDEIAHRVAEMSERFMLT--EVKDALPADLPLGIRQRLSLAVAVIHRPEMLILDEPTSGVDP 440
Cdd:PRK13637 99 E-TIEKDIAFGPINLGLSEEEIENRVKRAMNIVGLDyeDYKDKSPFELSGGQKRRVAIAGVVAMEPKILILDEPTAGLDP 177
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1820369315 441 VARDMFWQLMVDLARQDRVTIFISTHFMNE-AERCDRISLMHAGKVLASDTP 491
Cdd:PRK13637 178 KGRDEILNKIKELHKEYNMTIILVSHSMEDvAKLADRIIVMNKGKCELQGTP 229
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
15-225 |
1.96e-28 |
|
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is comprised of all BPD (Binding Protein Dependent) systems that are largely represented in archaea and eubacteria and are primarily involved in scavenging solutes from the environment. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213196 [Multi-domain] Cd Length: 178 Bit Score: 112.67 E-value: 1.96e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 15 LENVGQQYGATIALRDISLAIPARRMVGLIGPDGVGKSSLLSLIAGARAIEQGNVMVLGGD-MRDVHHRRDVCPKIAWMP 93
Cdd:cd03229 3 LKNVSKRYGQKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGEDlTDLEDELPPLRRRIGMVF 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 94 QGLgkNLYHTLSVYENVDFfarlfghdkaerelrinellqstglapfrdrpagKLSGGMKQKLGLCCALIHDPQLLILDE 173
Cdd:cd03229 83 QDF--ALFPHLTVLENIAL----------------------------------GLSGGQQQRVALARALAMDPDVLLLDE 126
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1820369315 174 PTTGVDPLSRAQFWELIDSIRQRQpEMSVLVATAYMEEAERF-DWLVAMNAGE 225
Cdd:cd03229 127 PTSALDPITRREVRALLKSLQAQL-GITVVLVTHDLDEAARLaDRVVVLRDGK 178
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
285-489 |
2.10e-28 |
|
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: 114.17 E-value: 2.10e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 285 RFGNFVAVDHVNFRIARGEIFGFLGSNGCGKSTTMKMLTGLLPASEGEAWLFGQPVDPKDIATrqrvgymsqafSLYSEL 364
Cdd:cd03220 31 EVGEFWALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVTVRGRVSSLLGLGG-----------GFNPEL 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 365 SVRQNLELHARLFHIPDDEIAHRVAEMSErfmLTEVKDALpaDLPL-----GIRQRLSLAVAVIHRPEMLILDEPTSGVD 439
Cdd:cd03220 100 TGRENIYLNGRLLGLSRKEIDEKIDEIIE---FSELGDFI--DLPVktyssGMKARLAFAIATALEPDILLIDEVLAVGD 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1820369315 440 PVARDMFWQLMVDLARQDRvTIFISTHFMNEAER-CDRISLMHAGKVLASD 489
Cdd:cd03220 175 AAFQEKCQRRLRELLKQGK-TVILVSHDPSSIKRlCDRALVLEKGKIRFDG 224
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
15-241 |
2.33e-28 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 117.51 E-value: 2.33e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 15 LENVGQQYGATIALRDISLAIPARRMVGLIGPDGVGKSSLLSLIAGARAIEQGNVMVlggDMRDVHHR----RDVC---P 87
Cdd:PRK11432 9 LKNITKRFGSNTVIDNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIFI---DGEDVTHRsiqqRDICmvfQ 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 88 KIAWMPQglgknlyhtLSVYENVDFFARLFGHDKAERELRINELLQSTGLAPFRDRPAGKLSGGMKQKLGLCCALIHDPQ 167
Cdd:PRK11432 86 SYALFPH---------MSLGENVGYGLKMLGVPKEERKQRVKEALELVDLAGFEDRYVDQISGGQQQRVALARALILKPK 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1820369315 168 LLILDEPTTGVDPLSRAQFWELIDSIRQRQPEMSVLVAtayMEEAERF---DWLVAMNAGEVLATGSAAELKAQTGS 241
Cdd:PRK11432 157 VLLFDEPLSNLDANLRRSMREKIRELQQQFNITSLYVT---HDQSEAFavsDTVIVMNKGKIMQIGSPQELYRQPAS 230
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
277-492 |
2.46e-28 |
|
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely related to ModC. ModC is an ABC-type transporter and the ATPase component of a molybdate transport system that also includes the periplasmic binding protein ModA and the membrane protein ModB. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213266 [Multi-domain] Cd Length: 235 Bit Score: 114.36 E-value: 2.46e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 277 IEARGLTMRFGNFVaVDHVNFRIARGEIFGFLGSNGCGKSTTMKMLTGLLPASEGEAWLFGqpvdpKDIAT----RQRVG 352
Cdd:cd03299 1 LKVENLSKDWKEFK-LKNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNG-----KDITNlppeKRDIS 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 353 YMSQAFSLYSELSVRQNLELHARLFHIPDDEIAHRVAEMSERFMLTEVKDALPADLPLGIRQRLSLAVAVIHRPEMLILD 432
Cdd:cd03299 75 YVPQNYALFPHMTVYKNIAYGLKKRKVDKKEIERKVLEIAEMLGIDHLLNRKPETLSGGEQQRVAIARALVVNPKILLLD 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1820369315 433 EPTSGVDPVARDMFWQLMVDLARQDRVTIFISTHFMNEAER-CDRISLMHAGKVLASDTPQ 492
Cdd:cd03299 155 EPFSALDVRTKEKLREELKKIRKEFGVTVLHVTHDFEEAWAlADKVAIMLNGKLIQVGKPE 215
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
4-240 |
2.83e-28 |
|
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease components [Energy production and conversion, Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 444011 [Multi-domain] Cd Length: 569 Bit Score: 120.64 E-value: 2.83e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 4 TPQDTSPPIAL-LENVGQQY--GATIALRDISLAIPARRMVGLIGPDGVGKSSLLSLIAGARAIEQGNVMVLGGDMRDVH 80
Cdd:COG4987 324 EPAPAPGGPSLeLEDVSFRYpgAGRPVLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFLDPQSGSITLGGVDLRDLD 403
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 81 hRRDVCPKIAWMPQglgKN-LYHTlSVYENVdffaRLFGHDKAERELRinELLQSTGLAPF-RDRPAG----------KL 148
Cdd:COG4987 404 -EDDLRRRIAVVPQ---RPhLFDT-TLRENL----RLARPDATDEELW--AALERVGLGDWlAALPDGldtwlgeggrRL 472
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 149 SGGMKQKLGLCCALIHDPQLLILDEPTTGVDPLSRAQfweLIDSIRQRQPEMSVLVATAYMEEAERFDWLVAMNAGEVLA 228
Cdd:COG4987 473 SGGERRRLALARALLRDAPILLLDEPTEGLDAATEQA---LLADLLEALAGRTVLLITHRLAGLERMDRILVLEDGRIVE 549
|
250
....*....|..
gi 1820369315 229 TGSAAELKAQTG 240
Cdd:COG4987 550 QGTHEELLAQNG 561
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
27-230 |
3.19e-28 |
|
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter subfamily specific for the transport of dipeptides, oligopeptides (OppD), and nickel (NikDE). The NikABCDE system of E. coli belongs to this family and is composed of the periplasmic binding protein NikA, two integral membrane components (NikB and NikC), and two ATPase (NikD and NikE). The NikABCDE transporter is synthesized under anaerobic conditions to meet the increased demand for nickel resulting from hydrogenase synthesis. The molecular mechanism of nickel uptake in many bacteria and most archaea is not known. Many other members of this ABC family are also involved in the uptake of dipeptides and oligopeptides. The oligopeptide transport system (Opp) is a five-component ABC transport composed of a membrane-anchored substrate binding proteins (SRP), OppA, two transmembrane proteins, OppB and OppC, and two ATP-binding domains, OppD and OppF.
Pssm-ID: 213224 [Multi-domain] Cd Length: 228 Bit Score: 113.75 E-value: 3.19e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 27 ALRDISLAIPARRMVGLIGPDGVGKSSLLSLIAGARAIEQGNVMVLGGDM--RDVHHRRDVCPKIAWMPQGLGKNLYHTL 104
Cdd:cd03257 20 ALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGKDLlkLSRRLRKIRRKEIQMVFQDPMSSLNPRM 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 105 SVYENVD--FFARLFGHDKAERELRINELLQSTGLAP-FRDRPAGKLSGGMKQKLGLCCALIHDPQLLILDEPTTGVDPL 181
Cdd:cd03257 100 TIGEQIAepLRIHGKLSKKEARKEAVLLLLVGVGLPEeVLNRYPHELSGGQRQRVAIARALALNPKLLIADEPTSALDVS 179
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1820369315 182 SRAQFWELIDSIRQRQpEMSVLVAT------AYMeeAERfdwLVAMNAGEVLATG 230
Cdd:cd03257 180 VQAQILDLLKKLQEEL-GLTLLFIThdlgvvAKI--ADR---VAVMYAGKIVEEG 228
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
15-226 |
6.18e-28 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 112.22 E-value: 6.18e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 15 LENVGQQYGATIALRDISLAIPARRMVGLIGPDGVGKSSLLSLIAGARAIEQGNVMVLGGDMRDVH---HRRdvcpKIAW 91
Cdd:COG4619 3 LEGLSFRVGGKPILSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIYLDGKPLSAMPppeWRR----QVAY 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 92 MPQ--GLGKNlyhtlSVYENVDFfARLFGHDKAERElRINELLQSTGLAP-FRDRPAGKLSGGMKQKLGLCCALIHDPQL 168
Cdd:COG4619 79 VPQepALWGG-----TVRDNLPF-PFQLRERKFDRE-RALELLERLGLPPdILDKPVERLSGGERQRLALIRALLLQPDV 151
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1820369315 169 LILDEPTTGVDPLSRAQFWELIDSIRQrQPEMSVLVATAYMEEAERF-DWLVAMNAGEV 226
Cdd:COG4619 152 LLLDEPTSALDPENTRRVEELLREYLA-EEGRAVLWVSHDPEQIERVaDRVLTLEAGRL 209
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
9-485 |
6.87e-28 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 118.88 E-value: 6.87e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 9 SPPIALLENVGQQYGATIALRDISLAIPARRMVGLIGPDGVGKSSLLSLIAGA--RAIEQGNVMVLGGDMRdVHHRRDVC 86
Cdd:PRK13549 2 MEYLLEMKNITKTFGGVKALDNVSLKVRAGEIVSLCGENGAGKSTLMKVLSGVypHGTYEGEIIFEGEELQ-ASNIRDTE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 87 PK-IAWMPQGLGknLYHTLSVYENVdFFARLFGH----DKAERELRINELLQSTGLAPFRDRPAGKLSGGMKQKLGLCCA 161
Cdd:PRK13549 81 RAgIAIIHQELA--LVKELSVLENI-FLGNEITPggimDYDAMYLRAQKLLAQLKLDINPATPVGNLGLGQQQLVEIAKA 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 162 LIHDPQLLILDEPTTgvdPLSRAQFWELIDSIRQRQPEMsvlVATAYM-----EEAERFDWLVAMNAGEVLATGSAAEL- 235
Cdd:PRK13549 158 LNKQARLLILDEPTA---SLTESETAVLLDIIRDLKAHG---IACIYIshklnEVKAISDTICVIRDGRHIGTRPAAGMt 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 236 KAQTGSQTLEQAFIALLPeaqRQAHKTvvipprdsreEEIAIEARGLTM---------RfgnfvaVDHVNFRIARGEIFG 306
Cdd:PRK13549 232 EDDIITMMVGRELTALYP---REPHTI----------GEVILEVRNLTAwdpvnphikR------VDDVSFSLRRGEILG 292
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 307 FLGSNGCGKSTTMKMLTGLLP-ASEGEAWLFGQPVD---PKDiATRQRVGYMSQ---AFSLYSELSVRQNLELHA----R 375
Cdd:PRK13549 293 IAGLVGAGRTELVQCLFGAYPgRWEGEIFIDGKPVKirnPQQ-AIAQGIAMVPEdrkRDGIVPVMGVGKNITLAAldrfT 371
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 376 LFHIPDDEIAHRVAEMSERFMltEVKDALP----ADLPLGIRQRLSLAVAVIHRPEMLILDEPTSGVDPVARDMFWQLMV 451
Cdd:PRK13549 372 GGSRIDDAAELKTILESIQRL--KVKTASPelaiARLSGGNQQKAVLAKCLLLNPKILILDEPTRGIDVGAKYEIYKLIN 449
|
490 500 510
....*....|....*....|....*....|....
gi 1820369315 452 DLARQDRVTIFISTHFMNEAERCDRISLMHAGKV 485
Cdd:PRK13549 450 QLVQQGVAIIVISSELPEVLGLSDRVLVMHEGKL 483
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
15-225 |
1.32e-27 |
|
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: 109.78 E-value: 1.32e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 15 LENVGQQYGATI--ALRDISLAIPARRMVGLIGPDGVGKSSLLSLIAGARAIEQGNVMVLGGDMRDVHhRRDVCPKIAWM 92
Cdd:cd03228 3 FKNVSFSYPGRPkpVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGVDLRDLD-LESLRKNIAYV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 93 PQGLgkNLYHTlSVYENVdffarlfghdkaerelrinellqstglapfrdrpagkLSGGMKQKLGLCCALIHDPQLLILD 172
Cdd:cd03228 82 PQDP--FLFSG-TIRENI-------------------------------------LSGGQRQRIAIARALLRDPPILILD 121
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1820369315 173 EPTTGVDPLSRAQFWELIDSIRQrqpEMSVLVATAYMEEAERFDWLVAMNAGE 225
Cdd:cd03228 122 EATSALDPETEALILEALRALAK---GKTVIVIAHRLSTIRDADRIIVLDDGR 171
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
277-496 |
1.50e-27 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 115.43 E-value: 1.50e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 277 IEARGLTMRFGNFVAVDHVNFRIARGEIFGFLGSNGCGKSTTMKMLTGLLPASEGEAWLFGQPVDpkDIATRQR-VGYMS 355
Cdd:PRK09452 15 VELRGISKSFDGKEVISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLDGQDIT--HVPAENRhVNTVF 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 356 QAFSLYSELSVRQNLELHARLFHIPDDEIAHRVAEMSERFMLTEVKDALPADLPLGIRQRLSLAVAVIHRPEMLILDEPT 435
Cdd:PRK09452 93 QSYALFPHMTVFENVAFGLRMQKTPAAEITPRVMEALRMVQLEEFAQRKPHQLSGGQQQRVAIARAVVNKPKVLLLDESL 172
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1820369315 436 SGVDPVARDMFWQLMVDLARQDRVT-IFIsTHFMNEA-ERCDRISLMHAGKVLASDTPQALVE 496
Cdd:PRK09452 173 SALDYKLRKQMQNELKALQRKLGITfVFV-THDQEEAlTMSDRIVVMRDGRIEQDGTPREIYE 234
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
273-498 |
1.74e-27 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 113.02 E-value: 1.74e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 273 EEIAIEARGLTMRFGNFV-AVDHVNFRIARGEIFGFLGSNGCGKSTTMKMLTGLLPASEGEAWLFGQPVD--PKDIAT-R 348
Cdd:PRK13636 2 EDYILKVEELNYNYSDGThALKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGKPIDysRKGLMKlR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 349 QRVGYMSQA--FSLYSElSVRQNLELHARLFHIPDDEIAHRVAEMSERFMLTEVKDALPADLPLGIRQRLSLAVAVIHRP 426
Cdd:PRK13636 82 ESVGMVFQDpdNQLFSA-SVYQDVSFGAVNLKLPEDEVRKRVDNALKRTGIEHLKDKPTHCLSFGQKKRVAIAGVLVMEP 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1820369315 427 EMLILDEPTSGVDPVARDMFWQLMVDLARQDRVTIFISTHFMNE-AERCDRISLMHAGKVLASDTPQALVEQR 498
Cdd:PRK13636 161 KVLVLDEPTAGLDPMGVSEIMKLLVEMQKELGLTIIIATHDIDIvPLYCDNVFVMKEGRVILQGNPKEVFAEK 233
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
277-494 |
1.88e-27 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 112.39 E-value: 1.88e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 277 IEARGLTMRFGNFVAVDHVNFRIARGEIFGFLGSNGCGKSTTMKMLTGLLPASEGEAWLFGQPVD--PKDIATRQRVGYM 354
Cdd:PRK11300 6 LSVSGLMMRFGGLLAVNNVNLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTILLRGQHIEglPGHQIARMGVVRT 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 355 SQAFSLYSELSVRQNL----------ELHARLFHIP-----DDEIAHRVAEMSERFMLTEVKDALPADLPLGIRQRLSLA 419
Cdd:PRK11300 86 FQHVRLFREMTVIENLlvaqhqqlktGLFSGLLKTPafrraESEALDRAATWLERVGLLEHANRQAGNLAYGQQRRLEIA 165
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1820369315 420 VAVIHRPEMLILDEPTSGVDPVARDMFWQLMVDLARQDRVTIFISTHFMNEA-ERCDRISLMHAGKVLASDTPQAL 494
Cdd:PRK11300 166 RCMVTQPEILMLDEPAAGLNPKETKELDELIAELRNEHNVTVLLIEHDMKLVmGISDRIYVVNQGTPLANGTPEEI 241
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
277-466 |
2.08e-27 |
|
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: 110.96 E-value: 2.08e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 277 IEARGLTMRFGN-FVAVDHVNFRIARGEIFGFLGSNGCGKSTTMKMLTGLLPASEGEAWLFGQPV-DPKDIAT---RQRV 351
Cdd:cd03292 1 IEFINVTKTYPNgTAALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQDVsDLRGRAIpylRRKI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 352 GYMSQAFSLYSELSVRQNLELHARLFHIPDDEIAHRVAEMSERFMLTEVKDALPADLPLGIRQRLSLAVAVIHRPEMLIL 431
Cdd:cd03292 81 GVVFQDFRLLPDRNVYENVAFALEVTGVPPREIRKRVPAALELVGLSHKHRALPAELSGGEQQRVAIARAIVNSPTILIA 160
|
170 180 190
....*....|....*....|....*....|....*..
gi 1820369315 432 DEPTSGVDPvarDMFWQLMVDLARQDR--VTIFISTH 466
Cdd:cd03292 161 DEPTGNLDP---DTTWEIMNLLKKINKagTTVVVATH 194
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
20-496 |
2.68e-27 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 118.42 E-value: 2.68e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 20 QQYGATIALRDISLAIPARRMVGLIGPDGVGKS----SLLSLIAGARAIEQGNVMVLG---------GDMRDVHHRRDVC 86
Cdd:PRK10261 24 QEQQKIAAVRNLSFSLQRGETLAIVGESGSGKSvtalALMRLLEQAGGLVQCDKMLLRrrsrqvielSEQSAAQMRHVRG 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 87 PKIAWMPQGLGKNLYHTLSVYENVDFFARL---FGHDKAEREL-RINELLQSTGLAPFRDRPAGKLSGGMKQKLGLCCAL 162
Cdd:PRK10261 104 ADMAMIFQEPMTSLNPVFTVGEQIAESIRLhqgASREEAMVEAkRMLDQVRIPEAQTILSRYPHQLSGGMRQRVMIAMAL 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 163 IHDPQLLILDEPTTGVDPLSRAQFWELIdSIRQRQPEMSVLVATAYME-EAERFDWLVAMNAGEVLATGSAAE------- 234
Cdd:PRK10261 184 SCRPAVLIADEPTTALDVTIQAQILQLI-KVLQKEMSMGVIFITHDMGvVAEIADRVLVMYQGEAVETGSVEQifhapqh 262
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 235 ------------LKAQTGSQTLEQAFIALLPEAQRQA----HKTVVipprdsrEEEIAIEARGLTMRFG------NFV-- 290
Cdd:PRK10261 263 pytrallaavpqLGAMKGLDYPRRFPLISLEHPAKQEppieQDTVV-------DGEPILQVRNLVTRFPlrsgllNRVtr 335
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 291 ---AVDHVNFRIARGEIFGFLGSNGCGKSTTMKMLTGLLPASEGEAWLFGQPVDP----KDIATRQRVGYMSQafSLYSE 363
Cdd:PRK10261 336 evhAVEKVSFDLWPGETLSLVGESGSGKSTTGRALLRLVESQGGEIIFNGQRIDTlspgKLQALRRDIQFIFQ--DPYAS 413
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 364 LSVRQN--------LELHARLfhiPDDEIAHRVAEMSERF-MLTEVKDALPADLPLGIRQRLSLAVAVIHRPEMLILDEP 434
Cdd:PRK10261 414 LDPRQTvgdsimepLRVHGLL---PGKAAAARVAWLLERVgLLPEHAWRYPHEFSGGQRQRICIARALALNPKVIIADEA 490
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1820369315 435 TSGVDPVARDMFWQLMVDLARQDRVTIFISTHFMNEAERCD-RISLMHAGKVLASDTPQALVE 496
Cdd:PRK10261 491 VSALDVSIRGQIINLLLDLQRDFGIAYLFISHDMAVVERIShRVAVMYLGQIVEIGPRRAVFE 553
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
30-464 |
3.78e-27 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 116.73 E-value: 3.78e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 30 DISLAIPARRMVGLIGPDGVGKS----SLLSLIAGARAI-EQGNVM-----VLGGDMRDVHHRRDvcPKIAWMPQ----- 94
Cdd:PRK15134 27 DVSLQIEAGETLALVGESGSGKSvtalSILRLLPSPPVVyPSGDIRfhgesLLHASEQTLRGVRG--NKIAMIFQepmvs 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 95 -----GLGKNLYHTLSVYenvdffaRLFGHDKAERElrINELLQSTGL--APFR--DRPAgKLSGGMKQKLGLCCALIHD 165
Cdd:PRK15134 105 lnplhTLEKQLYEVLSLH-------RGMRREAARGE--ILNCLDRVGIrqAAKRltDYPH-QLSGGERQRVMIAMALLTR 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 166 PQLLILDEPTTGVDPLSRAQFWELIDSIRQrQPEMSVLVATAYMEEAERF-DWLVAMNAGEVLATGSAAELKAqTGSQTL 244
Cdd:PRK15134 175 PELLIADEPTTALDVSVQAQILQLLRELQQ-ELNMGLLFITHNLSIVRKLaDRVAVMQNGRCVEQNRAATLFS-APTHPY 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 245 EQAFIALLPEAQRQAHKTVVIPPRDSREEEIAIE-ARGLTMR-FGNFVAVDHVNFRIARGEIFGFLGSNGCGKSTTMKML 322
Cdd:PRK15134 253 TQKLLNSEPSGDPVPLPEPASPLLDVEQLQVAFPiRKGILKRtVDHNVVVKNISFTLRPGETLGLVGESGSGKSTTGLAL 332
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 323 TGLLpASEGEAWLFGQPVDPKD----IATRQRVGYMSQ--AFSLYSELSVRQNLELHARLfHIPDDEIAHR----VAEMS 392
Cdd:PRK15134 333 LRLI-NSQGEIWFDGQPLHNLNrrqlLPVRHRIQVVFQdpNSSLNPRLNVLQIIEEGLRV-HQPTLSAAQReqqvIAVME 410
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1820369315 393 ERFMLTEVKDALPADLPLGIRQRLSLAVAVIHRPEMLILDEPTSGVDPVARDMFWQLMVDLARQDRVT-IFIS 464
Cdd:PRK15134 411 EVGLDPETRHRYPAEFSGGQRQRIAIARALILKPSLIILDEPTSSLDKTVQAQILALLKSLQQKHQLAyLFIS 483
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
277-485 |
4.89e-27 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 113.36 E-value: 4.89e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 277 IEARGLTMRF----GNFVAVDHVNFRIARGEIFGFLGSNGCGKSTTMKMLTGLLPASEGEAWLFGQPV---DPKD-IATR 348
Cdd:PRK11153 2 IELKNISKVFpqggRTIHALNNVSLHIPAGEIFGVIGASGAGKSTLIRCINLLERPTSGRVLVDGQDLtalSEKElRKAR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 349 QRVGYMSQAFSLYSELSVRQNLELHARLFHIPDDEIAHRVAEMSERFMLTEVKDALPADLPLGIRQRLSLAVAVIHRPEM 428
Cdd:PRK11153 82 RQIGMIFQHFNLLSSRTVFDNVALPLELAGTPKAEIKARVTELLELVGLSDKADRYPAQLSGGQKQRVAIARALASNPKV 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1820369315 429 LILDEPTSGVDPVARDMFWQLMVDLARQDRVTIFISTHFMNEAER-CDRISLMHAGKV 485
Cdd:PRK11153 162 LLCDEATSALDPATTRSILELLKDINRELGLTIVLITHEMDVVKRiCDRVAVIDAGRL 219
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
15-240 |
5.56e-27 |
|
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: 117.63 E-value: 5.56e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 15 LENVGQQYG--ATIALRDISLAIPARRMVGLIGPDGVGKSSLLSLIAGARAIEQGNVMVLGGDMRDVHH---RRdvcpKI 89
Cdd:COG2274 476 LENVSFRYPgdSPPVLDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEPTSGRILIDGIDLRQIDPaslRR----QI 551
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 90 AWMPQGLgkNLYHTlSVYENVdffarLFGHDKAERElRINELLQSTGLAPF-RDRPAG----------KLSGGMKQKLGL 158
Cdd:COG2274 552 GVVLQDV--FLFSG-TIRENI-----TLGDPDATDE-EIIEAARLAGLHDFiEALPMGydtvvgeggsNLSGGQRQRLAI 622
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 159 CCALIHDPQLLILDEPTTGVDPLSRAQFwelIDSIRQRQPEMSVLVATAYMEEAERFDWLVAMNAGEVLATGSAAELKAQ 238
Cdd:COG2274 623 ARALLRNPRILILDEATSALDAETEAII---LENLRRLLKGRTVIIIAHRLSTIRLADRIIVLDKGRIVEDGTHEELLAR 699
|
..
gi 1820369315 239 TG 240
Cdd:COG2274 700 KG 701
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
275-492 |
5.98e-27 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 111.02 E-value: 5.98e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 275 IAIEARGLTMRFGNFVAVDHVNFRIARGEIFGFLGSNGCGKSTTMKMLTGLLPASEGEAWLFGQPVD---PKDIATRQRV 351
Cdd:PRK13548 1 AMLEARNLSVRLGGRTLLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLNGRPLAdwsPAELARRRAV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 352 gyMSQAFSLYSELSVRQNLELHA---RLFHIPDDEIAHR------VAEMSERFMLTevkdalpadLPLGIRQRLSLA-V- 420
Cdd:PRK13548 81 --LPQHSSLSFPFTVEEVVAMGRaphGLSRAEDDALVAAalaqvdLAHLAGRDYPQ---------LSGGEQQRVQLArVl 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 421 ----AVIHRPEMLILDEPTSgvdpvARDMFWQLMV-----DLARQDRVTIFISTHFMNEAER-CDRISLMHAGKVLASDT 490
Cdd:PRK13548 150 aqlwEPDGPPRWLLLDEPTS-----ALDLAHQHHVlrlarQLAHERGLAVIVVLHDLNLAARyADRIVLLHQGRLVADGT 224
|
..
gi 1820369315 491 PQ 492
Cdd:PRK13548 225 PA 226
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
277-503 |
7.18e-27 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 109.84 E-value: 7.18e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 277 IEARGLTMRFGNFVAvdHVNFRIARGEIFGFLGSNGCGKSTTMKMLTGLLPASEGEAWLFGQPVDPKDIATRQrVGYMSQ 356
Cdd:COG3840 2 LRLDDLTYRYGDFPL--RFDLTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILWNGQDLTALPPAERP-VSMLFQ 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 357 AFSLYSELSVRQN--LELHARLfHIPDDEIAhRVAEMSERFMLTEVKDALPADLPLGIRQRLSLAVAVI-HRPeMLILDE 433
Cdd:COG3840 79 ENNLFPHLTVAQNigLGLRPGL-KLTAEQRA-QVEQALERVGLAGLLDRLPGQLSGGQRQRVALARCLVrKRP-ILLLDE 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1820369315 434 PTSGVDPVARDMFWQLMVDLARQDRVTIFISTHFMNEAER-CDRISLMHAGKVLASDTPQALVEQRGAASL 503
Cdd:COG3840 156 PFSALDPALRQEMLDLVDELCRERGLTVLMVTHDPEDAARiADRVLLVADGRIAADGPTAALLDGEPPPAL 226
|
|
| potA |
TIGR01187 |
spermidine/putrescine ABC transporter ATP-binding subunit; This model describes spermidine ... |
308-497 |
7.89e-27 |
|
spermidine/putrescine ABC transporter ATP-binding subunit; This model describes spermidine/putrescine ABC transporter, 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. Polyamines like spermidine and putrescine play vital role in cell proliferation, differentiation, and ion homeostasis. The concentration of polyamines within the cell are regulated by biosynthesis, degradation and transport (uptake and efflux included). [Transport and binding proteins, Amino acids, peptides and amines]
Pssm-ID: 162242 [Multi-domain] Cd Length: 325 Bit Score: 112.20 E-value: 7.89e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 308 LGSNGCGKSTTMKMLTGLLPASEGEAWLFGQPVDPKDiATRQRVGYMSQAFSLYSELSVRQNLELHARLFHIPDDEIAHR 387
Cdd:TIGR01187 2 LGPSGCGKTTLLRLLAGFEQPDSGSIMLDGEDVTNVP-PHLRHINMVFQSYALFPHMTVEENVAFGLKMRKVPRAEIKPR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 388 VAEMSERFMLTEVKDALPADLPLGIRQRLSLAVAVIHRPEMLILDEPTSGVDPVARDMFWQLMVDLARQDRVTIFISTHF 467
Cdd:TIGR01187 81 VLEALRLVQLEEFADRKPHQLSGGQQQRVALARALVFKPKILLLDEPLSALDKKLRDQMQLELKTIQEQLGITFVFVTHD 160
|
170 180 190
....*....|....*....|....*....|.
gi 1820369315 468 MNEA-ERCDRISLMHAGKVLASDTPQALVEQ 497
Cdd:TIGR01187 161 QEEAmTMSDRIAIMRKGKIAQIGTPEEIYEE 191
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
15-256 |
7.91e-27 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 112.48 E-value: 7.91e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 15 LENVGQQY----GATIALRDISLAIPARRMVGLIGPDGVGKSSLLSLIAGaraIEQ---GNVMVLGGDM--------RDV 79
Cdd:COG1135 4 LENLSKTFptkgGPVTALDDVSLTIEKGEIFGIIGYSGAGKSTLIRCINL---LERptsGSVLVDGVDLtalserelRAA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 80 hhRRdvcpKIAWMPQGLgkNLYHTLSVYENVDFFARLFGHDKAERELRINELLQSTGLAPFRDR-PAgKLSGGMKQKLGL 158
Cdd:COG1135 81 --RR----KIGMIFQHF--NLLSSRTVAENVALPLEIAGVPKAEIRKRVAELLELVGLSDKADAyPS-QLSGGQKQRVGI 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 159 CCALIHDPQLLILDEPTTGVDPLSRAQFWELIDSIRQRQ--------PEMSVL--VAT--AYMEeaerfdwlvamnAGEV 226
Cdd:COG1135 152 ARALANNPKVLLCDEATSALDPETTRSILDLLKDINRELgltivlitHEMDVVrrICDrvAVLE------------NGRI 219
|
250 260 270
....*....|....*....|....*....|
gi 1820369315 227 LATGSAAELKAQTGSQTLeQAFIALLPEAQ 256
Cdd:COG1135 220 VEQGPVLDVFANPQSELT-RRFLPTVLNDE 248
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
277-485 |
1.47e-26 |
|
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: 111.30 E-value: 1.47e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 277 IEARGLTMRF----GNFVAVDHVNFRIARGEIFGFLGSNGCGKSTTMKMLTGLLPA---SEGEAWLFGQPVDP------- 342
Cdd:COG0444 2 LEVRNLKVYFptrrGVVKAVDGVSFDVRRGETLGLVGESGSGKSTLARAILGLLPPpgiTSGEILFDGEDLLKlsekelr 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 343 ----KDIAT-----------RQRVGYmsqafslyselSVRQNLELHARLfhiPDDEIAHRVAEMSERFMLT---EVKDAL 404
Cdd:COG0444 82 kirgREIQMifqdpmtslnpVMTVGD-----------QIAEPLRIHGGL---SKAEARERAIELLERVGLPdpeRRLDRY 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 405 PADLPLGIRQRLSLAVAVIHRPEMLILDEPTSGVDPVARDMFWQLMVDLARQDRVT-IFIsTHFMNE-AERCDRISLMHA 482
Cdd:COG0444 148 PHELSGGMRQRVMIARALALEPKLLIADEPTTALDVTIQAQILNLLKDLQRELGLAiLFI-THDLGVvAEIADRVAVMYA 226
|
...
gi 1820369315 483 GKV 485
Cdd:COG0444 227 GRI 229
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
27-230 |
1.58e-26 |
|
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: 108.96 E-value: 1.58e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 27 ALRDISLAIPARRMVGLIGPDGVGKSSLLSLIAGARAIEQGNVMVLG---GDMRDVHHRRdvcpkIAWMpQGLGKNLYHT 103
Cdd:cd03267 36 ALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRVAGlvpWKRRKKFLRR-----IGVV-FGQKTQLWWD 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 104 LSVYENVDFFARLFGHDKAERELRINELLQSTGLAPFRDRPAGKLSGGMKQKLGLCCALIHDPQLLILDEPTTGVDPLSR 183
Cdd:cd03267 110 LPVIDSFYLLAAIYDLPPARFKKRLDELSELLDLEELLDTPVRQLSLGQRMRAEIAAALLHEPEILFLDEPTIGLDVVAQ 189
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1820369315 184 AQFWELIDsIRQRQPEMSVLVATAYMEEAERF-DWLVAMNAGEVLATG 230
Cdd:cd03267 190 ENIRNFLK-EYNRERGTTVLLTSHYMKDIEALaRRVLVIDKGRLLYDG 236
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
15-235 |
1.62e-26 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 111.78 E-value: 1.62e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 15 LENVGQQYGATIALRDISLAIPARRMVGLIGPDGVGKSSLLSLIAGaraIEQ---GNVMVLGGDM---RDVHHRRdvcpk 88
Cdd:COG1118 5 VRNISKRFGSFTLLDDVSLEIASGELVALLGPSGSGKTTLLRIIAG---LETpdsGRIVLNGRDLftnLPPRERR----- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 89 IAWMPQglgkN--LYHTLSVYENVDFFARLFGHDKAERELRINELLQSTGLAPFRDRPAGKLSGGMKQKLGLCCALIHDP 166
Cdd:COG1118 77 VGFVFQ----HyaLFPHMTVAENIAFGLRVRPPSKAEIRARVEELLELVQLEGLADRYPSQLSGGQRQRVALARALAVEP 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 167 QLLILDEPTTGVDPLSRAQFWELIDSIRQRQPEMSVLVaTAYMEEAERF-DWLVAMNAGEVLATGSAAEL 235
Cdd:COG1118 153 EVLLLDEPFGALDAKVRKELRRWLRRLHDELGGTTVFV-THDQEEALELaDRVVVMNQGRIEQVGTPDEV 221
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
276-487 |
2.17e-26 |
|
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: 108.06 E-value: 2.17e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 276 AIEARGLTMRFGN--FVAVDHVNFRIARGEIFGFLGSNGCGKSTTMKMLTGLLPASEGEAWLFG---QPVDPKDIatRQR 350
Cdd:cd03245 2 RIEFRNVSFSYPNqeIPALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGtdiRQLDPADL--RRN 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 351 VGYMSQAFSLYSElSVRQNLELhARLFHipDDEIAHRVAEMSErfmLTEVKDALPADLPL-----------GIRQRLSLA 419
Cdd:cd03245 80 IGYVPQDVTLFYG-TLRDNITL-GAPLA--DDERILRAAELAG---VTDFVNKHPNGLDLqigergrglsgGQRQAVALA 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1820369315 420 VAVIHRPEMLILDEPTSGVDPVARDMFWQLMVDLARQDrvTIFISTHFMNEAERCDRISLMHAGKVLA 487
Cdd:cd03245 153 RALLNDPPILLLDEPTSAMDMNSEERLKERLRQLLGDK--TLIIITHRPSLLDLVDRIIVMDSGRIVA 218
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
15-230 |
2.39e-26 |
|
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) proteins function from bacteria to human, mediating the translocation of substances into and out of cells or organelles. ABC transporters contain two transmembrane-spanning domains (TMDs) or subunits and two nucleotide binding domains (NBDs) or subunits that couple transport to the hydrolysis of ATP. In the maltose transport system, the periplasmic maltose binding protein (MBP) stimulates the ATPase activity of the membrane-associated transporter, which consists of two transmembrane subunits, MalF and MalG, and two copies of the ATP binding subunit, MalK, and becomes tightly bound to the transporter in the catalytic transition state, ensuring that maltose is passed to the transporter as ATP is hydrolyzed.
Pssm-ID: 213268 [Multi-domain] Cd Length: 213 Bit Score: 107.73 E-value: 2.39e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 15 LENVGQQYGATIALRDISLAIPARRMVGLIGPDGVGKSSLLSLIAGARAIEQGNVMVLGGDMRDVH-HRRDvcpkIAWMP 93
Cdd:cd03301 3 LENVTKRFGNVTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGRDVTDLPpKDRD----IAMVF 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 94 QGLGknLYHTLSVYENVDFFARLFGHDKAERELRINELLQSTGLAPFRDRPAGKLSGGMKQKLGLCCALIHDPQLLILDE 173
Cdd:cd03301 79 QNYA--LYPHMTVYDNIAFGLKLRKVPKDEIDERVREVAELLQIEHLLDRKPKQLSGGQRQRVALGRAIVREPKVFLMDE 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1820369315 174 PTTGVDPLSRAQFWELIDSIRQRQPEMSVLVATAYMEEAERFDWLVAMNAGEVLATG 230
Cdd:cd03301 157 PLSNLDAKLRVQMRAELKRLQQRLGTTTIYVTHDQVEAMTMADRIAVMNDGQIQQIG 213
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
15-206 |
3.00e-26 |
|
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: 107.49 E-value: 3.00e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 15 LENVGQQYGATI-ALRDISLAIPARRMVGLIGPDGVGKSSLLSLIAGARAIEQGNVMVLGGDMRDVHHRRdvcpkIAWMP 93
Cdd:cd03292 3 FINVTKTYPNGTaALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQDVSDLRGRA-----IPYLR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 94 QGLG------KNLYHtLSVYENVDFFARLFGHDKAERELRINELLQSTGLAPFRDRPAGKLSGGMKQKLGLCCALIHDPQ 167
Cdd:cd03292 78 RKIGvvfqdfRLLPD-RNVYENVAFALEVTGVPPREIRKRVPAALELVGLSHKHRALPAELSGGEQQRVAIARAIVNSPT 156
|
170 180 190
....*....|....*....|....*....|....*....
gi 1820369315 168 LLILDEPTTGVDPLSRAQFWELIDSIRQRQpeMSVLVAT 206
Cdd:cd03292 157 ILIADEPTGNLDPDTTWEIMNLLKKINKAG--TTVVVAT 193
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
15-212 |
3.46e-26 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 108.63 E-value: 3.46e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 15 LENVGQQYGATIALRDISLAIPARRMVGLIGPDGVGKSSLLSLIAGARAIEQGNVMVLGGDMRDVHHRRDVcpkiawMPQ 94
Cdd:PRK11248 4 ISHLYADYGGKPALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDGKPVEGPGAERGV------VFQ 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 95 GLGknLYHTLSVYENVDFFARLFGHDKAERELRINELLQSTGLAPFRDRPAGKLSGGMKQKLGLCCALIHDPQLLILDEP 174
Cdd:PRK11248 78 NEG--LLPWRNVQDNVAFGLQLAGVEKMQRLEIAHQMLKKVGLEGAEKRYIWQLSGGQRQRVGIARALAANPQLLLLDEP 155
|
170 180 190
....*....|....*....|....*....|....*...
gi 1820369315 175 TTGVDPLSRAQFWELIDSIRQRQPEmSVLVATAYMEEA 212
Cdd:PRK11248 156 FGALDAFTREQMQTLLLKLWQETGK-QVLLITHDIEEA 192
|
|
| COG4559 |
COG4559 |
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism]; |
277-507 |
4.74e-26 |
|
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443620 [Multi-domain] Cd Length: 258 Bit Score: 108.28 E-value: 4.74e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 277 IEARGLTMRFGNFVAVDHVNFRIARGEIFGFLGSNGCGKSTTMKMLTGLLPASEGEAWLFGQPVD---PKDIATRQRVgy 353
Cdd:COG4559 2 LEAENLSVRLGGRTLLDDVSLTLRPGELTAIIGPNGAGKSTLLKLLTGELTPSSGEVRLNGRPLAawsPWELARRRAV-- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 354 MSQAFSLYSELSVRQNLEL----HARLfHIPDDEIAHRV------AEMSERFMLTevkdalpadLPLGIRQRLSLA--VA 421
Cdd:COG4559 80 LPQHSSLAFPFTVEEVVALgrapHGSS-AAQDRQIVREAlalvglAHLAGRSYQT---------LSGGEQQRVQLArvLA 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 422 VIHRPEM-----LILDEPTSGVDPvardmFWQLMV-DLARQ---DRVTIFISTHFMNEAER-CDRISLMHAGKVLASDTP 491
Cdd:COG4559 150 QLWEPVDggprwLFLDEPTSALDL-----AHQHAVlRLARQlarRGGGVVAVLHDLNLAAQyADRILLLHQGRLVAQGTP 224
|
250
....*....|....*.
gi 1820369315 492 QALVEqrgAASLEEAF 507
Cdd:COG4559 225 EEVLT---DELLERVY 237
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
16-235 |
1.03e-25 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 106.65 E-value: 1.03e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 16 ENVGQQYGATIALRDISLAIPARRMVGLIGPDGVGKSSLLSLIAGARAIEQGNVMvLGGdmRDVH----HRRdvcpkiAW 91
Cdd:COG1137 7 ENLVKSYGKRTVVKDVSLEVNQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGRIF-LDG--EDIThlpmHKR------AR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 92 MpqGLGknlY--------HTLSVYENVDFFARLFGHDKAERELRINELLQSTGLAPFRDRPAGKLSGGMKQKLGLCCALI 163
Cdd:COG1137 78 L--GIG---YlpqeasifRKLTVEDNILAVLELRKLSKKEREERLEELLEEFGITHLRKSKAYSLSGGERRRVEIARALA 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 164 HDPQLLILDEPTTGVDPLSRAQFWELIDSIRQRQpeMSVLVA------------TAYMeeaerfdwlvaMNAGEVLATGS 231
Cdd:COG1137 153 TNPKFILLDEPFAGVDPIAVADIQKIIRHLKERG--IGVLITdhnvretlgicdRAYI-----------ISEGKVLAEGT 219
|
....
gi 1820369315 232 AAEL 235
Cdd:COG1137 220 PEEI 223
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
277-492 |
1.21e-25 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 107.47 E-value: 1.21e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 277 IEARGLTMRFGN-FVAVDHVNFRIARGEIFGFLGSNGCGKSTTMKMLTGLLPASEGEAWLFGQPV--DPKD-IATRQRVG 352
Cdd:PRK13639 2 LETRDLKYSYPDgTEALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIKGEPIkyDKKSlLEVRKTVG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 353 YM-----SQAFSLyselSVRQNLELHARLFHIPDDEIAHRVAEMSERFMLTEVKDALPADLPLGIRQRLSLAVAVIHRPE 427
Cdd:PRK13639 82 IVfqnpdDQLFAP----TVEEDVAFGPLNLGLSKEEVEKRVKEALKAVGMEGFENKPPHHLSGGQKKRVAIAGILAMKPE 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1820369315 428 MLILDEPTSGVDPVARDMFWQLMVDLARQDrVTIFISTHFMNEAER-CDRISLMHAGKVLASDTPQ 492
Cdd:PRK13639 158 IIVLDEPTSGLDPMGASQIMKLLYDLNKEG-ITIIISTHDVDLVPVyADKVYVMSDGKIIKEGTPK 222
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
4-235 |
1.23e-25 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 107.04 E-value: 1.23e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 4 TPQDTSPPIALLENVGQQYGATIALRDISLAIPARRMVGLIGPDGVGKSSLLS-------LIAGARAieQGNVMVLGGDM 76
Cdd:COG1117 3 APASTLEPKIEVRNLNVYYGDKQALKDINLDIPENKVTALIGPSGCGKSTLLRclnrmndLIPGARV--EGEILLDGEDI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 77 RD-----VHHRRdvcpKIAWMPQglgK-NLYhTLSVYENVDFFARLFG-HDKAERELRINELLQSTGLAP-FRDR---PA 145
Cdd:COG1117 81 YDpdvdvVELRR----RVGMVFQ---KpNPF-PKSIYDNVAYGLRLHGiKSKSELDEIVEESLRKAALWDeVKDRlkkSA 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 146 GKLSGGMKQKLglcC---ALIHDPQLLILDEPTTGVDPLSRAQFWELIDSIRQrqpEMSVLVATAYMEEAERF-DWLVAM 221
Cdd:COG1117 153 LGLSGGQQQRL---CiarALAVEPEVLLMDEPTSALDPISTAKIEELILELKK---DYTIVIVTHNMQQAARVsDYTAFF 226
|
250
....*....|....
gi 1820369315 222 NAGEVLATGSAAEL 235
Cdd:COG1117 227 YLGELVEFGPTEQI 240
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
291-499 |
1.46e-25 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 112.57 E-value: 1.46e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 291 AVDHVNFRIARGEIFGFLGSNGCGKSTTMKMLTGLLPASEGEAWLFGQPVdpKDIAT---RQRVGYMSQAFSLYSElSVR 367
Cdd:COG1132 355 VLKDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYDPTSGRILIDGVDI--RDLTLeslRRQIGVVPQDTFLFSG-TIR 431
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 368 QNLELhARLfHIPDDEIaHRVAEMSErfmLTEVKDALP-----------ADLPLGIRQRLSLAVAVIHRPEMLILDEPTS 436
Cdd:COG1132 432 ENIRY-GRP-DATDEEV-EEAAKAAQ---AHEFIEALPdgydtvvgergVNLSGGQRQRIAIARALLKDPPILILDEATS 505
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1820369315 437 GVDPVA----RDMFWQLMvdlarQDRVTIFIStHFMNEAERCDRISLMHAGKVLASDTPQALVEQRG 499
Cdd:COG1132 506 ALDTETealiQEALERLM-----KGRTTIVIA-HRLSTIRNADRILVLDDGRIVEQGTHEELLARGG 566
|
|
| LPS_export_lptB |
TIGR04406 |
LPS export ABC transporter ATP-binding protein; Members of this fmaily are LptB, the ... |
16-235 |
3.38e-25 |
|
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: 105.05 E-value: 3.38e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 16 ENVGQQYGATIALRDISLAIPARRMVGLIGPDGVGKSSLLSLIAGARAIEQGNVMVLGGDMRD--VHHRRDVcpKIAWMP 93
Cdd:TIGR04406 5 ENLIKSYKKRKVVNDVSLSVKSGEIVGLLGPNGAGKTTSFYMIVGLVRPDAGKILIDGQDITHlpMHERARL--GIGYLP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 94 QGlgKNLYHTLSVYENVDFFARLFGH-DKAERELRINELLQSTGLAPFRDRPAGKLSGGMKQKLGLCCALIHDPQLLILD 172
Cdd:TIGR04406 83 QE--ASIFRKLTVEENIMAVLEIRKDlDRAEREERLEALLEEFQISHLRDNKAMSLSGGERRRVEIARALATNPKFILLD 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1820369315 173 EPTTGVDPLSRAQFWELIDSIRQRQpeMSVLVA------------TAYMeeaerfdwlvaMNAGEVLATGSAAEL 235
Cdd:TIGR04406 161 EPFAGVDPIAVGDIKKIIKHLKERG--IGVLITdhnvretldicdRAYI-----------ISDGKVLAEGTPAEI 222
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
274-486 |
4.45e-25 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 105.31 E-value: 4.45e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 274 EIAIEARGLTMRFGNFVAVDHVNFRIARGEIFGFLGSNGCGKSTTMKMLTGLLPAS-----EGEAWLFGQPVDPKD---I 345
Cdd:PRK14267 2 KFAIETVNLRVYYGSNHVIKGVDLKIPQNGVFALMGPSGCGKSTLLRTFNRLLELNeearvEGEVRLFGRNIYSPDvdpI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 346 ATRQRVGYMSQAFSLYSELSVRQNLELHARLFHI--PDDEIAHRVA-EMSERFMLTEVKDAL---PADLPLGIRQRLSLA 419
Cdd:PRK14267 82 EVRREVGMVFQYPNPFPHLTIYDNVAIGVKLNGLvkSKKELDERVEwALKKAALWDEVKDRLndyPSNLSGGQRQRLVIA 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1820369315 420 VAVIHRPEMLILDEPTSGVDPVARDMFWQLMVDLarQDRVTIFISTHFMNEAER-CDRISLMHAGKVL 486
Cdd:PRK14267 162 RALAMKPKILLMDEPTANIDPVGTAKIEELLFEL--KKEYTIVLVTHSPAQAARvSDYVAFLYLGKLI 227
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
291-499 |
4.84e-25 |
|
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: 104.61 E-value: 4.84e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 291 AVDHVNFRIARGEIFGFLGSNGCGKSTTMKMLTGLLPASEGEAWLFGQPVDPKDIAT-RQRVGYMSQAFSLYSElSVRQN 369
Cdd:cd03254 18 VLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGIDIRDISRKSlRSMIGVVLQDTFLFSG-TIMEN 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 370 LelhaRLFH--IPDDEI--------AHRVAEMSERFMLTEVKDAlPADLPLGIRQRLSLAVAVIHRPEMLILDEPTSGVD 439
Cdd:cd03254 97 I----RLGRpnATDEEVieaakeagAHDFIMKLPNGYDTVLGEN-GGNLSQGERQLLAIARAMLRDPKILILDEATSNID 171
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 440 PVARDMFWQLMVDLaRQDRVTIFIStHFMNEAERCDRISLMHAGKVLASDTPQALVEQRG 499
Cdd:cd03254 172 TETEKLIQEALEKL-MKGRTSIIIA-HRLSTIKNADKILVLDDGKIIEEGTHDELLAKKG 229
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
274-492 |
5.09e-25 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 105.46 E-value: 5.09e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 274 EIAIEARGLTMRFGNFV--AVDHVNFRIARGEIFGFLGSNGCGKSTTMKMLTGLLPASEGEAWLFGQPVDPKDIA-TRQR 350
Cdd:PRK13632 5 SVMIKVENVSFSYPNSEnnALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIDGITISKENLKeIRKK 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 351 VGYMSQ---------------AFSLYSELsvrqnlelharlfhIPDDEIAHRVAEMSERFMLTEVKDALPADLPLGIRQR 415
Cdd:PRK13632 85 IGIIFQnpdnqfigatveddiAFGLENKK--------------VPPKKMKDIIDDLAKKVGMEDYLDKEPQNLSGGQKQR 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1820369315 416 LSLAVAVIHRPEMLILDEPTSGVDPVARDMFWQLMVDLARQDRVTIFISTHFMNEAERCDRISLMHAGKVLASDTPQ 492
Cdd:PRK13632 151 VAIASVLALNPEIIIFDESTSMLDPKGKREIKKIMVDLRKTRKKTLISITHDMDEAILADKVIVFSEGKLIAQGKPK 227
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
277-486 |
5.22e-25 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 104.99 E-value: 5.22e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 277 IEARGLTMRFGNFVAVDHVNFRIARGEIFGFLGSNGCGKSTTMKMLTGLL-----PASEGEAWLFGQPVDPKD-IATRQR 350
Cdd:PRK14247 4 IEIRDLKVSFGQVEVLDGVNLEIPDNTITALMGPSGSGKSTLLRVFNRLIelypeARVSGEVYLDGQDIFKMDvIELRRR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 351 VGYMSQAFSLYSELSVRQNLELHARLFHIPDD--EIAHRVAEMSERFML-TEVKDALPA---DLPLGIRQRLSLAVAVIH 424
Cdd:PRK14247 84 VQMVFQIPNPIPNLSIFENVALGLKLNRLVKSkkELQERVRWALEKAQLwDEVKDRLDApagKLSGGQQQRLCIARALAF 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1820369315 425 RPEMLILDEPTSGVDPVARDMFWQLMVDLARQdrVTIFISTHFMNEAERC-DRISLMHAGKVL 486
Cdd:PRK14247 164 QPEVLLADEPTANLDPENTAKIESLFLELKKD--MTIVLVTHFPQQAARIsDYVAFLYKGQIV 224
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
277-497 |
6.17e-25 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 107.50 E-value: 6.17e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 277 IEARGLTMRFGNFVAVDHVNFRIARGEIFGFLGSNGCGKSTTMKMLTGLLPASEGEAWLFGQPVDPKDIATRQrVGYMSQ 356
Cdd:PRK11432 7 VVLKNITKRFGSNTVIDNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIFIDGEDVTHRSIQQRD-ICMVFQ 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 357 AFSLYSELSVRQNLELHARLFHIPDDEIAHRVAEMSERFMLTEVKDALPADLPLGIRQRLSLAVAVIHRPEMLILDEPTS 436
Cdd:PRK11432 86 SYALFPHMSLGENVGYGLKMLGVPKEERKQRVKEALELVDLAGFEDRYVDQISGGQQQRVALARALILKPKVLLFDEPLS 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1820369315 437 GVDPVARDMFWQLMVDLARQDRVTIFISTHFMNEA-ERCDRISLMHAGKVLASDTPQALVEQ 497
Cdd:PRK11432 166 NLDANLRRSMREKIRELQQQFNITSLYVTHDQSEAfAVSDTVIVMNKGKIMQIGSPQELYRQ 227
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
25-259 |
7.05e-25 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 105.20 E-value: 7.05e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 25 TIALRDISLAIPARRMVGLIGPDGVGKSSLLSLIAGARAIEQGNVMVLGgdmRDVHHR--RDVCPKIAWMPQGLGKNLYh 102
Cdd:PRK13647 18 TKALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMG---REVNAEneKWVRSKVGLVFQDPDDQVF- 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 103 TLSVYENVDFFARLFGHDKAERELRINELLQSTGLAPFRDRPAGKLSGGMKQKLGLCCALIHDPQLLILDEPTTGVDPLS 182
Cdd:PRK13647 94 SSTVWDDVAFGPVNMGLDKDEVERRVEEALKAVRMWDFRDKPPYHLSYGQKKRVAIAGVLAMDPDVIVLDEPMAYLDPRG 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 183 RAQFWELIDSIRQRQPemSVLVATAYME-EAERFDWLVAMNAGEVLATG-----------SAAELKAQTGSQTLEQafia 250
Cdd:PRK13647 174 QETLMEILDRLHNQGK--TVIVATHDVDlAAEWADQVIVLKEGRVLAEGdkslltdedivEQAGLRLPLVAQIFED---- 247
|
....*....
gi 1820369315 251 lLPEAQRQA 259
Cdd:PRK13647 248 -LPELGQSK 255
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
39-241 |
8.16e-25 |
|
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: 112.03 E-value: 8.16e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 39 RMVGLIGPDGVGKSSLLSLIAGARAIEQGNVMVLGgdmRDVHHRRDVCPKIAWM-PQGlgKNLYHTLSVYENVDFFARLF 117
Cdd:TIGR01257 957 QITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGG---KDIETNLDAVRQSLGMcPQH--NILFHHLTVAEHILFYAQLK 1031
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 118 GHDKAERELRINELLQSTGLAPFRDRPAGKLSGGMKQKLGLCCALIHDPQLLILDEPTTGVDPLSRAQFWELIDSIRQRQ 197
Cdd:TIGR01257 1032 GRSWEEAQLEMEAMLEDTGLHHKRNEEAQDLSGGMQRKLSVAIAFVGDAKVVVLDEPTSGVDPYSRRSIWDLLLKYRSGR 1111
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1820369315 198 pemSVLVATAYMEEAERF-DWLVAMNAGEVLATGSAAELKAQTGS 241
Cdd:TIGR01257 1112 ---TIIMSTHHMDEADLLgDRIAIISQGRLYCSGTPLFLKNCFGT 1153
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
27-242 |
1.09e-24 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 105.94 E-value: 1.09e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 27 ALRDISLAIPARRMVGLIGPDGVGKSSLLSLIAGaraI---EQGNVMVLGgdMRDVHHRRDVCPKIAW-MPQglgKN-LY 101
Cdd:COG4586 37 AVDDISFTIEPGEIVGFIGPNGAGKSTTIKMLTG---IlvpTSGEVRVLG--YVPFKRRKEFARRIGVvFGQ---RSqLW 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 102 HTLSVYENVDFFARLFGHDKAERELRINELLQSTGLAPFRDRPAGKLSGGMKQKLGLCCALIHDPQLLILDEPTTGVDPL 181
Cdd:COG4586 109 WDLPAIDSFRLLKAIYRIPDAEYKKRLDELVELLDLGELLDTPVRQLSLGQRMRCELAAALLHRPKILFLDEPTIGLDVV 188
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1820369315 182 SRAQFWELIDSIRQRQpEMSVLVATAYMEEAERF-DWLVAMNAGEVLATGSAAELKAQTGSQ 242
Cdd:COG4586 189 SKEAIREFLKEYNRER-GTTILLTSHDMDDIEALcDRVIVIDHGRIIYDGSLEELKERFGPY 249
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
277-498 |
1.47e-24 |
|
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: 108.76 E-value: 1.47e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 277 IEARGLTMRFGNFVAVDHVNFRIARGEIFGFLGSNGCGKSTTMKMLTGLLPAS--EGEAWLFGQPVDPKDIATRQRVG-- 352
Cdd:TIGR02633 2 LEMKGIVKTFGGVKALDGIDLEVRPGECVGLCGENGAGKSTLMKILSGVYPHGtwDGEIYWSGSPLKASNIRDTERAGiv 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 353 YMSQAFSLYSELSVRQNLELHARLFH----IPDDEIAHRVAEMSERFMLTEVKDALP-ADLPLGIRQRLSLAVAVIHRPE 427
Cdd:TIGR02633 82 IIHQELTLVPELSVAENIFLGNEITLpggrMAYNAMYLRAKNLLRELQLDADNVTRPvGDYGGGQQQLVEIAKALNKQAR 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1820369315 428 MLILDEPTSGVDPVARDMFWQLMVDLARQDRVTIFIStHFMNEAER-CDRISLMHAGKVLASDTPQALVEQR 498
Cdd:TIGR02633 162 LLILDEPSSSLTEKETEILLDIIRDLKAHGVACVYIS-HKLNEVKAvCDTICVIRDGQHVATKDMSTMSEDD 232
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
20-235 |
1.60e-24 |
|
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: 104.26 E-value: 1.60e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 20 QQYGATIALRDISLAIPARRMVGLIGPDGVGKSSLLSLIAGARAIEQGNVMVLGGDMRDVHH------RRDvcpKIAWMP 93
Cdd:cd03294 32 KKTGQTVGVNDVSLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGKVLIDGQDIAAMSRkelrelRRK---KISMVF 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 94 QGLGknLYHTLSVYENVDFFARLFGHDKAERELRINELLQSTGLAPFRDRPAGKLSGGMKQKLGLCCALIHDPQLLILDE 173
Cdd:cd03294 109 QSFA--LLPHRTVLENVAFGLEVQGVPRAEREERAAEALELVGLEGWEHKYPDELSGGMQQRVGLARALAVDPDILLMDE 186
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1820369315 174 PTTGVDPLSRAQFWELIDSIRQRQPEMSVLVaTAYMEEAERF-DWLVAMNAGEVLATGSAAEL 235
Cdd:cd03294 187 AFSALDPLIRREMQDELLRLQAELQKTIVFI-THDLDEALRLgDRIAIMKDGRLVQVGTPEEI 248
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
295-486 |
1.92e-24 |
|
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: 102.73 E-value: 1.92e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 295 VNFRIARGEIFGFLGSNGCGKSTTMKMLTGLLP---ASEGEAWLFGQPVDPKdiATRQRVGYMSQAFSLYSELSVRQNLE 371
Cdd:cd03234 26 VSLHVESGQVMAILGSSGSGKTTLLDAISGRVEgggTTSGQILFNGQPRKPD--QFQKCVAYVRQDDILLPGLTVRETLT 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 372 LHARL---FHIPDDEIAHRVAEMSERFM-LTEVKDALPADLPLGIRQRLSLAVAVIHRPEMLILDEPTSGVDPVARDMFW 447
Cdd:cd03234 104 YTAILrlpRKSSDAIRKKRVEDVLLRDLaLTRIGGNLVKGISGGERRRVSIAVQLLWDPKVLILDEPTSGLDSFTALNLV 183
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1820369315 448 QLMVDLARQDRvTIFISTH------FmneaERCDRISLMHAGKVL 486
Cdd:cd03234 184 STLSQLARRNR-IVILTIHqprsdlF----RLFDRILLLSSGEIV 223
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
30-230 |
2.21e-24 |
|
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: 101.99 E-value: 2.21e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 30 DISLAIPARRmVGLIGPDGVGKSSLLSLIAGARAIEQGNVMVLGGDMRDVHHRRDVCP---KIAWMPQGLGknLYHTLSV 106
Cdd:cd03297 16 KIDFDLNEEV-TGIFGASGAGKSTLLRCIAGLEKPDGGTIVLNGTVLFDSRKKINLPPqqrKIGLVFQQYA--LFPHLNV 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 107 YENVDFFARlfGHDKAERELRINELLQSTGLAPFRDRPAGKLSGGMKQKLGLCCALIHDPQLLILDEPTTGVDPLSRAQf 186
Cdd:cd03297 93 RENLAFGLK--RKRNREDRISVDELLDLLGLDHLLNRYPAQLSGGEKQRVALARALAAQPELLLLDEPFSALDRALRLQ- 169
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1820369315 187 weLIDSIRQRQPE--MSVLVATAYMEEAERF-DWLVAMNAGEVLATG 230
Cdd:cd03297 170 --LLPELKQIKKNlnIPVIFVTHDLSEAEYLaDRIVVMEDGRLQYIG 214
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
277-497 |
2.37e-24 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 103.73 E-value: 2.37e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 277 IEARGLTMRF-GNFVAVDHVNFRIARGEIFGFLGSNGCGKSTTMKMLTGLLPASEGEAWLFGQPVDPKDI-ATRQRVGYM 354
Cdd:PRK13652 4 IETRDLCYSYsGSKEALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIRGEPITKENIrEVRKFVGLV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 355 -----SQAFSLyselSVRQNLELHARLFHIPDDEIAHRVAEMSERFMLTEVKDALPADLPLGIRQRLSLAVAVIHRPEML 429
Cdd:PRK13652 84 fqnpdDQIFSP----TVEQDIAFGPINLGLDEETVAHRVSSALHMLGLEELRDRVPHHLSGGEKKRVAIAGVIAMEPQVL 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1820369315 430 ILDEPTSGVDPVARDMFWQLMVDLARQDRVTIFISTHFMN-EAERCDRISLMHAGKVLASDTPQALVEQ 497
Cdd:PRK13652 160 VLDEPTAGLDPQGVKELIDFLNDLPETYGMTVIFSTHQLDlVPEMADYIYVMDKGRIVAYGTVEEIFLQ 228
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
15-234 |
2.76e-24 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 103.17 E-value: 2.76e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 15 LENVGQQYGATIALRDISLAIPARRMVGLIGPDGVGKSSLLSLIAGARAIEQGNVMVLGGDMRDVHHRRdVCPKIAWMPQ 94
Cdd:PRK11231 5 TENLTVGYGTKRILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDKPISMLSSRQ-LARRLALLPQ 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 95 glgknlYHT----LSVYENV--------DFFARLFGHDKAerelRINELLQSTGLAPFRDRPAGKLSGGMKQKLGLCCAL 162
Cdd:PRK11231 84 ------HHLtpegITVRELVaygrspwlSLWGRLSAEDNA----RVNQAMEQTRINHLADRRLTDLSGGQRQRAFLAMVL 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1820369315 163 IHDPQLLILDEPTTGVDpLSRAQfwELIDSIRQRQPEMSVLVATAY-MEEAERF-DWLVAMNAGEVLATGSAAE 234
Cdd:PRK11231 154 AQDTPVVLLDEPTTYLD-INHQV--ELMRLMRELNTQGKTVVTVLHdLNQASRYcDHLVVLANGHVMAQGTPEE 224
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
276-504 |
3.20e-24 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 105.20 E-value: 3.20e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 276 AIEARGLTMRFGNFVAVDHVNFRIARGEIFGFLGSNGCGKSTtmkmltGLLPA------SEGEAWLFGQPVDPKDiATRQ 349
Cdd:NF000106 13 AVEVRGLVKHFGEVKAVDGVDLDVREGTVLGVLGP*GAA**R------GALPAhv*gpdAGRRPWRF*TWCANRR-ALRR 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 350 RVG-YMSQAFSLYSELSVRQNLELHARLFHIPDDEIAHRVAEMSERFMLTEVKDALPADLPLGIRQRLSLAVAVIHRPEM 428
Cdd:NF000106 86 TIG*HRPVR*GRRESFSGRENLYMIGR*LDLSRKDARARADELLERFSLTEAAGRAAAKYSGGMRRRLDLAASMIGRPAV 165
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1820369315 429 LILDEPTSGVDPVARDMFWQLMVDLARqDRVTIFISTHFMNEAER-CDRISLMHAGKVLASDTPQALVEQRGAASLE 504
Cdd:NF000106 166 LYLDEPTTGLDPRTRNEVWDEVRSMVR-DGATVLLTTQYMEEAEQlAHELTVIDRGRVIADGKVDELKTKVGGRTLQ 241
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
11-485 |
3.46e-24 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 107.40 E-value: 3.46e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 11 PIALLENVGQQYGATIALRDISLAIPARRMVGLIGPDGVGKSSLLSLIAGARAIEQGNVMVLGgdmRDVHHRRdvcPK-- 88
Cdd:PRK10762 3 ALLQLKGIDKAFPGVKALSGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSILYLG---KEVTFNG---PKss 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 89 ----IAWMPQGLgkNLYHTLSVYENVdFFARLFGH-------DKAERElrINELLQSTGLAPFRDRPAGKLSGGMKQKLG 157
Cdd:PRK10762 77 qeagIGIIHQEL--NLIPQLTIAENI-FLGREFVNrfgridwKKMYAE--ADKLLARLNLRFSSDKLVGELSIGEQQMVE 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 158 LCCALIHDPQLLILDEPTtgvDPLSRAQFWELIDSIRQRQPEMSVLVATAY-MEEA-ERFDWLVAMNAGEVLATGSAAEL 235
Cdd:PRK10762 152 IAKVLSFESKVIIMDEPT---DALTDTETESLFRVIRELKSQGRGIVYISHrLKEIfEICDDVTVFRDGQFIAEREVADL 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 236 KaqtgsqtlEQAFIALLP----EAQRqahktvvipPR-DSREEEIAIEARGLTmrfGNfvAVDHVNFRIARGEIFGFLGS 310
Cdd:PRK10762 229 T--------EDSLIEMMVgrklEDQY---------PRlDKAPGEVRLKVDNLS---GP--GVNDVSFTLRKGEILGVSGL 286
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 311 NGCGKSTTMKMLTGLLPASEGEAWLFGQPVD---PKDiATRQRVGYMSQ---AFSLYSELSVRQNLELHA-RLFHIPDDE 383
Cdd:PRK10762 287 MGAGRTELMKVLYGALPRTSGYVTLDGHEVVtrsPQD-GLANGIVYISEdrkRDGLVLGMSVKENMSLTAlRYFSRAGGS 365
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 384 IAHR--VAEMSERFMLTEVK----DALPADLPLGIRQRLSLAVAVIHRPEMLILDEPTSGVDPVARDMFWQLmVDLARQD 457
Cdd:PRK10762 366 LKHAdeQQAVSDFIRLFNIKtpsmEQAIGLLSGGNQQKVAIARGLMTRPKVLILDEPTRGVDVGAKKEIYQL-INQFKAE 444
|
490 500
....*....|....*....|....*....
gi 1820369315 458 RVTIFISTHFMNEA-ERCDRISLMHAGKV 485
Cdd:PRK10762 445 GLSIILVSSEMPEVlGMSDRILVMHEGRI 473
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
274-485 |
4.00e-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: 100.20 E-value: 4.00e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 274 EIAIEARGLTMRfgnfVAVDHVNFRIARGEIFGFLGSNGCGKSTTMKMLTGLLPASEGEAWLFGQPVDPKDIATRQRVGy 353
Cdd:cd03215 2 EPVLEVRGLSVK----GAVRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITLDGKPVTRRSPRDAIRAG- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 354 msqafslyselsvrqnlelharLFHIPDDEIAHR-VAEMSERFMLtevkdALPADLPLGIRQRLSLAVAVIHRPEMLILD 432
Cdd:cd03215 77 ----------------------IAYVPEDRKREGlVLDLSVAENI-----ALSSLLSGGNQQKVVLARWLARDPRVLILD 129
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1820369315 433 EPTSGVDPVARDMFWQLMVDLARQDRVTIFISTHfMNEAER-CDRISLMHAGKV 485
Cdd:cd03215 130 EPTRGVDVGAKAEIYRLIRELADAGKAVLLISSE-LDELLGlCDRILVMYEGRI 182
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
292-507 |
4.34e-24 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 102.28 E-value: 4.34e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 292 VDHVNFRIARGEIFGFLGSNGCGKSTTMKMLTGLLPASEGEAwlfgqPVDPKDIA-------TRQRVGYMSQAFSLYSEL 364
Cdd:PRK10895 19 VEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNI-----IIDDEDISllplharARRGIGYLPQEASIFRRL 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 365 SVRQNLelhARLFHIPDD----EIAHRVAEMSERFMLTEVKDALPADLPLGIRQRLSLAVAVIHRPEMLILDEPTSGVDP 440
Cdd:PRK10895 94 SVYDNL---MAVLQIRDDlsaeQREDRANELMEEFHIEHLRDSMGQSLSGGERRRVEIARALAANPKFILLDEPFAGVDP 170
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 441 VARDMFWQLMVDLaRQDRVTIFISTHFMNEA-ERCDRISLMHAGKVLASDTPQALV--EQRGAASLEEAF 507
Cdd:PRK10895 171 ISVIDIKRIIEHL-RDSGLGVLITDHNVRETlAVCERAYIVSQGHLIAHGTPTEILqdEHVKRVYLGEDF 239
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
20-206 |
4.65e-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: 100.79 E-value: 4.65e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 20 QQYGATIALRDISLAIPARRMVGLIGPDGVGKSSLLSLIAGARAIEQGNVmVLGGDMRdvhHRRDVCPKIAWMPQGLGKN 99
Cdd:cd03226 8 SYKKGTEILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSI-LLNGKPI---KAKERRKSIGYVMQDVDYQ 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 100 LYhTLSVYENVDFFARlfghDKAERELRINELLQSTGLAPFRDRPAGKLSGGMKQKLGLCCALIHDPQLLILDEPTTGVD 179
Cdd:cd03226 84 LF-TDSVREELLLGLK----ELDAGNEQAETVLKDLDLYALKERHPLSLSGGQKQRLAIAAALLSGKDLLIFDEPTSGLD 158
|
170 180
....*....|....*....|....*..
gi 1820369315 180 PLSRAQFWELIDSIrQRQpEMSVLVAT 206
Cdd:cd03226 159 YKNMERVGELIREL-AAQ-GKAVIVIT 183
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
21-235 |
4.73e-24 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 102.30 E-value: 4.73e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 21 QYGATIALRDISLAIPARRMVGLIGPDGVGKSSLLSLIAgaRAIE-------QGNVMVLGGDM--RDVHHRRDVCPKIAW 91
Cdd:PRK14247 12 SFGQVEVLDGVNLEIPDNTITALMGPSGSGKSTLLRVFN--RLIElypearvSGEVYLDGQDIfkMDVIELRRRVQMVFQ 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 92 MPqglgkNLYHTLSVYENVDFFARL--FGHDKAERELRINELLQSTGL-APFRDR---PAGKLSGGMKQKLGLCCALIHD 165
Cdd:PRK14247 90 IP-----NPIPNLSIFENVALGLKLnrLVKSKKELQERVRWALEKAQLwDEVKDRldaPAGKLSGGQQQRLCIARALAFQ 164
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1820369315 166 PQLLILDEPTTGVDPLSRAQFWELIDSIRQrqpEMSVLVATAYMEEAERF-DWLVAMNAGEVLATGSAAEL 235
Cdd:PRK14247 165 PEVLLADEPTANLDPENTAKIESLFLELKK---DMTIVLVTHFPQQAARIsDYVAFLYKGQIVEWGPTREV 232
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
277-494 |
7.43e-24 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 102.50 E-value: 7.43e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 277 IEARGLTMRFG---NFVAVDHVNFRIARGEIFGFLGSNGCGKSTTMKMLTGLLPASEGEAWLFGQPVDPKDI-ATRQRVG 352
Cdd:PRK13650 5 IEVKNLTFKYKedqEKYTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIIDGDLLTEENVwDIRHKIG 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 353 YM-----SQAFSLYSELSVRQNLELHArlfhIPDDEIAHRVAEMSERFMLTEVKDALPADLPLGIRQRLSLAVAVIHRPE 427
Cdd:PRK13650 85 MVfqnpdNQFVGATVEDDVAFGLENKG----IPHEEMKERVNEALELVGMQDFKEREPARLSGGQKQRVAIAGAVAMRPK 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1820369315 428 MLILDEPTSGVDPVARDMFWQLMVDLARQDRVTIFISTHFMNEAERCDRISLMHAGKVLASDTPQAL 494
Cdd:PRK13650 161 IIILDEATSMLDPEGRLELIKTIKGIRDDYQMTVISITHDLDEVALSDRVLVMKNGQVESTSTPREL 227
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
277-505 |
1.25e-23 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 100.55 E-value: 1.25e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 277 IEARGLTMRFGNFVAVDHVNFRIARGEIFGFLGSNGCGKSTTMKMLTGLLPASEGEAWLFGQPV-DPK--DIATRQRVGY 353
Cdd:PRK09493 2 IEFKNVSKHFGPTQVLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGLKVnDPKvdERLIRQEAGM 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 354 MSQAFSLYSELSVRQNLELHARLFHIPDDEIAHRVA-EMSERFMLTEVKDALPADLPLGIRQRLSLAVAVIHRPEMLILD 432
Cdd:PRK09493 82 VFQQFYLFPHLTALENVMFGPLRVRGASKEEAEKQArELLAKVGLAERAHHYPSELSGGQQQRVAIARALAVKPKLMLFD 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1820369315 433 EPTSGVDPVARDMFWQLMVDLArQDRVTIFISTHFMNEAERC-DRISLMHAGKVLASDTPQALVEQRGAASLEE 505
Cdd:PRK09493 162 EPTSALDPELRHEVLKVMQDLA-EEGMTMVIVTHEIGFAEKVaSRLIFIDKGRIAEDGDPQVLIKNPPSQRLQE 234
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
13-485 |
1.49e-23 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 105.38 E-value: 1.49e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 13 ALLE--NVGQQYGATIALRDISLAIPARRMVGLIGPDGVGKSSLLSLIAGARAIEQGNVMVLGGDMRDVHHRRDVCPKIA 90
Cdd:PRK11288 3 PYLSfdGIGKTFPGVKALDDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSILIDGQEMRFASTTAALAAGVA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 91 WMPQGLgkNLYHTLSVYENVdFFARL---FGH-DKAERELRINELLQSTGLAPFRDRPAGKLSGGMKQKLGLCCALIHDP 166
Cdd:PRK11288 83 IIYQEL--HLVPEMTVAENL-YLGQLphkGGIvNRRLLNYEAREQLEHLGVDIDPDTPLKYLSIGQRQMVEIAKALARNA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 167 QLLILDEPTTGVDPLSRAQFWELIDSIRQRQpeMSVLVATAYMEEAERF-DWLVAMNAGEVLATGSAAelkAQTGSQTLE 245
Cdd:PRK11288 160 RVIAFDEPTSSLSAREIEQLFRVIRELRAEG--RVILYVSHRMEEIFALcDAITVFKDGRYVATFDDM---AQVDRDQLV 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 246 QAFIAllpeaqRQAHKTVVIPPR---DSREEEIAIEARGLTmrfgnfvavDHVNFRIARGEIFGFLGSNGCGKSTTMKML 322
Cdd:PRK11288 235 QAMVG------REIGDIYGYRPRplgEVRLRLDGLKGPGLR---------EPISFSVRAGEIVGLFGLVGAGRSELMKLL 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 323 TGLLPASEGEAWLFGQPVDPKDIATRQRVGYM-----SQAFSLYSELSVRQNLELHARLFHIPDDEIAH--RVAEMSERF 395
Cdd:PRK11288 300 YGATRRTAGQVYLDGKPIDIRSPRDAIRAGIMlcpedRKAEGIIPVHSVADNINISARRHHLRAGCLINnrWEAENADRF 379
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 396 ML-----TEVKDALPADLPLGIRQRLSLAVAVIHRPEMLILDEPTSGVDPVARDMFWQLMVDLARQDRVTIFISTHFMNE 470
Cdd:PRK11288 380 IRslnikTPSREQLIMNLSGGNQQKAILGRWLSEDMKVILLDEPTRGIDVGAKHEIYNVIYELAAQGVAVLFVSSDLPEV 459
|
490
....*....|....*
gi 1820369315 471 AERCDRISLMHAGKV 485
Cdd:PRK11288 460 LGVADRIVVMREGRI 474
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
277-498 |
1.79e-23 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 105.40 E-value: 1.79e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 277 IEARGLTMRFGNFVAVDHVNFRIARGEIFGFLGSNGCGKSTTMKMLTGLLPAS--EGEAWLFGQPVDPKDIATRQRVG-- 352
Cdd:PRK13549 6 LEMKNITKTFGGVKALDNVSLKVRAGEIVSLCGENGAGKSTLMKVLSGVYPHGtyEGEIIFEGEELQASNIRDTERAGia 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 353 YMSQAFSLYSELSVRQNLELHARLFH---IPDDEIAHRVAEMSERFMLtEVKDALP-ADLPLGIRQRLSLAVAVIHRPEM 428
Cdd:PRK13549 86 IIHQELALVKELSVLENIFLGNEITPggiMDYDAMYLRAQKLLAQLKL-DINPATPvGNLGLGQQQLVEIAKALNKQARL 164
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1820369315 429 LILDEPTSGVDPVARDMFWQLMVDLARQDRVTIFIStHFMNE-AERCDRISLMHAGKVLASDTPQALVEQR 498
Cdd:PRK13549 165 LILDEPTASLTESETAVLLDIIRDLKAHGIACIYIS-HKLNEvKAISDTICVIRDGRHIGTRPAAGMTEDD 234
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
4-221 |
2.16e-23 |
|
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: 105.45 E-value: 2.16e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 4 TPQDTSPPIAL-LENVGQQY-GATIALRDISLAIPARRMVGLIGPDGVGKSSLLSLIAGARAIEQGNVMVLGGDMR--DV 79
Cdd:TIGR02857 312 APVTAAPASSLeFSGVSVAYpGRRPALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSIAVNGVPLAdaDA 391
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 80 HHRRDvcpKIAWMPQGLGknLYHTlSVYENVdffaRLFGHDKAERELRinELLQSTGLAPF-RDRPAG----------KL 148
Cdd:TIGR02857 392 DSWRD---QIAWVPQHPF--LFAG-TIAENI----RLARPDASDAEIR--EALERAGLDEFvAALPQGldtpigeggaGL 459
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1820369315 149 SGGMKQKLGLCCALIHDPQLLILDEPTTGVDPLSRAQFWELIDSIRQRQpemSVLVATAYMEEAERFDWLVAM 221
Cdd:TIGR02857 460 SGGQAQRLALARAFLRDAPLLLLDEPTAHLDAETEAEVLEALRALAQGR---TVLLVTHRLALAALADRIVVL 529
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
28-230 |
2.39e-23 |
|
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: 99.72 E-value: 2.39e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 28 LRDISLAIPARRMVGLIGPDGVGKSSLLSLIAGARAIEQGNVMVLGGDMRDVH-HRRDvcpkIAWMPQGlgKNLYHTLSV 106
Cdd:cd03299 15 LKNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNGKDITNLPpEKRD----ISYVPQN--YALFPHMTV 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 107 YENVDFFARLFGHDKAERELRINELLQSTGLAPFRDRPAGKLSGGMKQKLGLCCALIHDPQLLILDEPTTGVDPLSRAQF 186
Cdd:cd03299 89 YKNIAYGLKKRKVDKKEIERKVLEIAEMLGIDHLLNRKPETLSGGEQQRVAIARALVVNPKILLLDEPFSALDVRTKEKL 168
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1820369315 187 WELIDSIRqRQPEMSVLVATAYMEEAERF-DWLVAMNAGEVLATG 230
Cdd:cd03299 169 REELKKIR-KEFGVTVLHVTHDFEEAWALaDKVAIMLNGKLIQVG 212
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
291-492 |
4.76e-23 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 99.83 E-value: 4.76e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 291 AVDHVNFRIARGEIFGFLGSNGCGKSTTMKMLTGLLPASEGEAWLFGQPVDPKDIA-TRQRVGYM-----SQAFSLYSEL 364
Cdd:PRK13648 24 TLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIFYNNQAITDDNFEkLRKHIGIVfqnpdNQFVGSIVKY 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 365 SVRQNLELHArlfhIPDDEIAHRVAEMSERFMLTEVKDALPADLPLGIRQRLSLAVAVIHRPEMLILDEPTSGVDPVARD 444
Cdd:PRK13648 104 DVAFGLENHA----VPYDEMHRRVSEALKQVDMLERADYEPNALSGGQKQRVAIAGVLALNPSVIILDEATSMLDPDARQ 179
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1820369315 445 MFWQLMVDLARQDRVTIFISTHFMNEAERCDRISLMHAGKVLASDTPQ 492
Cdd:PRK13648 180 NLLDLVRKVKSEHNITIISITHDLSEAMEADHVIVMNKGTVYKEGTPT 227
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
27-230 |
6.04e-23 |
|
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: 98.37 E-value: 6.04e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 27 ALRDISLAIPARRMVGLIGPDGVGKSSLLSLIAGARAIEQGNVMVLGgdmrdvhhrrdvcpKIAWMPqGLGKNLYHTLSV 106
Cdd:cd03220 37 ALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVTVRG--------------RVSSLL-GLGGGFNPELTG 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 107 YENVDFFARLFGHDKAERELRINELLQSTGLAPFRDRPAGKLSGGMKQKLGLCCALIHDPQLLILDEPTTGVDPLSRAQF 186
Cdd:cd03220 102 RENIYLNGRLLGLSRKEIDEKIDEIIEFSELGDFIDLPVKTYSSGMKARLAFAIATALEPDILLIDEVLAVGDAAFQEKC 181
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1820369315 187 WELIDSIRQRqpEMSVLVATAYMEEAERF-DWLVAMNAGEVLATG 230
Cdd:cd03220 182 QRRLRELLKQ--GKTVILVSHDPSSIKRLcDRALVLEKGKIRFDG 224
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
277-494 |
1.04e-22 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 99.01 E-value: 1.04e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 277 IEARGLTMRFGNFVAVDHVN---FRIARGEIFGFLGSNGCGKSTTMKMLTGLLPASEGEAWLFGQPVDPKDIAT-RQRVG 352
Cdd:PRK13642 5 LEVENLVFKYEKESDVNQLNgvsFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDGELLTAENVWNlRRKIG 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 353 YMSQ-AFSLYSELSVRQNLELHARLFHIPDDEIAHRVAEMSERFMLTEVKDALPADLPLGIRQRLSLAVAVIHRPEMLIL 431
Cdd:PRK13642 85 MVFQnPDNQFVGATVEDDVAFGMENQGIPREEMIKRVDEALLAVNMLDFKTREPARLSGGQKQRVAVAGIIALRPEIIIL 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1820369315 432 DEPTSGVDPVARDMFWQLMVDLARQDRVTIFISTHFMNEAERCDRISLMHAGKVLASDTPQAL 494
Cdd:PRK13642 165 DESTSMLDPTGRQEIMRVIHEIKEKYQLTVLSITHDLDEAASSDRILVMKAGEIIKEAAPSEL 227
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
30-230 |
1.29e-22 |
|
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: 96.79 E-value: 1.29e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 30 DISLAIPARRMVGLIGPDGVGKSSLLSLIAGARAIEQGNVMVLGGDMR--DVHHRrdvcpKIAWMPQGlgKNLYHTLSVY 107
Cdd:cd03298 16 HFDLTFAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLINGVDVTaaPPADR-----PVSMLFQE--NNLFAHLTVE 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 108 ENVDFFARLFGHDKAERELRINELLQSTGLAPFRDRPAGKLSGGMKQKLGLCCALIHDPQLLILDEPTTGVDPLSRAQFW 187
Cdd:cd03298 89 QNVGLGLSPGLKLTAEDRQAIEVALARVGLAGLEKRLPGELSGGERQRVALARVLVRDKPVLLLDEPFAALDPALRAEML 168
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1820369315 188 ELIDSIRqRQPEMSVLVATAYMEEAER-FDWLVAMNAGEVLATG 230
Cdd:cd03298 169 DLVLDLH-AETKMTVLMVTHQPEDAKRlAQRVVFLDNGRIAAQG 211
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
22-216 |
1.36e-22 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 96.15 E-value: 1.36e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 22 YGATIALRDISLAIPARRMVGLIGPDGVGKSSLLSLIAGARAieqgnvmVLGGDMRDVHHRRdvcpkIAWMPQGLGKNLY 101
Cdd:NF040873 2 YGGRPVLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLR-------PTSGTVRRAGGAR-----VAYVPQRSEVPDS 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 102 HTLSVYENVD--FFAR--LFGHDKAERELRINELLQSTGLAPFRDRPAGKLSGGMKQKLGLCCALIHDPQLLILDEPTTG 177
Cdd:NF040873 70 LPLTVRDLVAmgRWARrgLWRRLTRDDRAAVDDALERVGLADLAGRQLGELSGGQRQRALLAQGLAQEADLLLLDEPTTG 149
|
170 180 190
....*....|....*....|....*....|....*....
gi 1820369315 178 VDPLSRAQFWELIDSIRQRQpeMSVLVATAYMEEAERFD 216
Cdd:NF040873 150 LDAESRERIIALLAEEHARG--ATVVVVTHDLELVRRAD 186
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
295-476 |
1.46e-22 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 97.16 E-value: 1.46e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 295 VNFRIARGEIFGFLGSNGCGKSTTMKMLTGLLPASEGEAWLFGQPVDPKDIATR-----QRVGYMSQAFSLYSELSVRQN 369
Cdd:PRK10584 29 VELVVKRGETIALIGESGSGKSTLLAILAGLDDGSSGEVSLVGQPLHQMDEEARaklraKHVGFVFQSFMLIPTLNALEN 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 370 LELHARLFHIPDDEIAHRVAEMSERFMLTEVKDALPADLPLGIRQRLSLAVAVIHRPEMLILDEPTSGVDPVARDMFWQL 449
Cdd:PRK10584 109 VELPALLRGESSRQSRNGAKALLEQLGLGKRLDHLPAQLSGGEQQRVALARAFNGRPDVLFADEPTGNLDRQTGDKIADL 188
|
170 180
....*....|....*....|....*..
gi 1820369315 450 MVDLARQDRVTIFISTHFMNEAERCDR 476
Cdd:PRK10584 189 LFSLNREHGTTLILVTHDLQLAARCDR 215
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
15-235 |
1.77e-22 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 100.49 E-value: 1.77e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 15 LENVGQQYGATIALRDISLAIPARRMVGLIGPDGVGKSSLLSLIAGARAIEQGNVMVlgGDMRdvhhRRDVCPKiawmPQ 94
Cdd:PRK11000 6 LRNVTKAYGDVVISKDINLDIHEGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLFI--GEKR----MNDVPPA----ER 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 95 GLGK-----NLYHTLSVYENVDFFARLFGHDKAERELRIN---ELLQstgLAPFRDRPAGKLSGGMKQKLGLCCALIHDP 166
Cdd:PRK11000 76 GVGMvfqsyALYPHLSVAENMSFGLKLAGAKKEEINQRVNqvaEVLQ---LAHLLDRKPKALSGGQRQRVAIGRTLVAEP 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1820369315 167 QLLILDEPTTGVDPLSRAQFWELIDSIRQRQPEMSVLVATAYMEEAERFDWLVAMNAGEVLATGSAAEL 235
Cdd:PRK11000 153 SVFLLDEPLSNLDAALRVQMRIEISRLHKRLGRTMIYVTHDQVEAMTLADKIVVLDAGRVAQVGKPLEL 221
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
282-502 |
2.00e-22 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 96.96 E-value: 2.00e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 282 LTMRFgnfvavdhvNFRIARGEIFGFLGSNGCGKSTTMKMLTGLLPASEGEAWLFGQpvDPKDIATRQR-VGYMSQAFSL 360
Cdd:PRK10771 14 LPMRF---------DLTVERGERVAILGPSGAGKSTLLNLIAGFLTPASGSLTLNGQ--DHTTTPPSRRpVSMLFQENNL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 361 YSELSVRQN--LELHA--RLfhipDDEIAHRVAEMSERFMLTEVKDALPADLPLGIRQRLSLAVAVIHRPEMLILDEPTS 436
Cdd:PRK10771 83 FSHLTVAQNigLGLNPglKL----NAAQREKLHAIARQMGIEDLLARLPGQLSGGQRQRVALARCLVREQPILLLDEPFS 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1820369315 437 GVDPVARDMFWQLMVDLARQDRVTIFISTHFMNEAERCDRISLMHAGKVLASDTP-QALVEQRGAAS 502
Cdd:PRK10771 159 ALDPALRQEMLTLVSQVCQERQLTLLMVSHSLEDAARIAPRSLVVADGRIAWDGPtDELLSGKASAS 225
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
42-240 |
2.28e-22 |
|
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: 104.33 E-value: 2.28e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 42 GLIGPDGVGKSSLLSLIAGARAIEQGNVMVLGG----DMRDVHHRRDVCPKIAWMPQglgknlyhTLSVYENVDFFARLF 117
Cdd:TIGR01257 1969 GLLGVNGAGKTTTFKMLTGDTTVTSGDATVAGKsiltNISDVHQNMGYCPQFDAIDD--------LLTGREHLYLYARLR 2040
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 118 GHDKAERELRINELLQSTGLAPFRDRPAGKLSGGMKQKLGLCCALIHDPQLLILDEPTTGVDPLSRAQFWELIDSIRQRq 197
Cdd:TIGR01257 2041 GVPAEEIEKVANWSIQSLGLSLYADRLAGTYSGGNKRKLSTAIALIGCPPLVLLDEPTTGMDPQARRMLWNTIVSIIRE- 2119
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1820369315 198 pEMSVLVATAYMEEAERF-DWLVAMNAGEVLATGSAAELKAQTG 240
Cdd:TIGR01257 2120 -GRAVVLTSHSMEECEALcTRLAIMVKGAFQCLGTIQHLKSKFG 2162
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
17-244 |
2.32e-22 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 97.09 E-value: 2.32e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 17 NVGQQYGATIALRDISLAIPARRMVGLIGPDGVGKSSLLSLIAGARAIEQGNVMVLGGDMRDVHHRRDVCPKIAWMP-QG 95
Cdd:PRK09493 6 NVSKHFGPTQVLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGLKVNDPKVDERLIRQEAGMVfQQ 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 96 LgkNLYHTLSVYENVDFFA-RLFGHDKAERELRINELLQSTGLAPFRDRPAGKLSGGMKQKLGLCCALIHDPQLLILDEP 174
Cdd:PRK09493 86 F--YLFPHLTALENVMFGPlRVRGASKEEAEKQARELLAKVGLAERAHHYPSELSGGQQQRVAIARALAVKPKLMLFDEP 163
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1820369315 175 TTGVDPLSRAqfwELIDSIRQRQPE-MSVLVATAYMEEAERF-DWLVAMNAGEVLATGSAAELKAQTGSQTL 244
Cdd:PRK09493 164 TSALDPELRH---EVLKVMQDLAEEgMTMVIVTHEIGFAEKVaSRLIFIDKGRIAEDGDPQVLIKNPPSQRL 232
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
27-230 |
2.47e-22 |
|
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic bacteriocins of lactic acid bacteria are produced as precursors which have N-terminal leader peptides that share similarities in amino acid sequence and contain a conserved processing site of two glycine residues in positions -1 and -2. A dedicated ATP-binding cassette (ABC) transporter is responsible for the proteolytic cleavage of the leader peptides and subsequent translocation of the bacteriocins across the cytoplasmic membrane.
Pssm-ID: 213212 [Multi-domain] Cd Length: 220 Bit Score: 96.50 E-value: 2.47e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 27 ALRDISLAIPARRMVGLIGPDGVGKSSLLSLIAGARAIEQGNVMVLGGDMRDVHH---RRDvcpkIAWMPQGLgknlyhT 103
Cdd:cd03245 19 ALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGTDIRQLDPadlRRN----IGYVPQDV------T 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 104 L---SVYENVDFfARLFGHDkaERELRINELlqsTGLAPF-RDRPAG----------KLSGGMKQKLGLCCALIHDPQLL 169
Cdd:cd03245 89 LfygTLRDNITL-GAPLADD--ERILRAAEL---AGVTDFvNKHPNGldlqigergrGLSGGQRQAVALARALLNDPPIL 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1820369315 170 ILDEPTTGVDPLSRAQFwelIDSIRQRQPEMSVLVATAYMEEAERFDWLVAMNAGEVLATG 230
Cdd:cd03245 163 LLDEPTSAMDMNSEERL---KERLRQLLGDKTLIIITHRPSLLDLVDRIIVMDSGRIVADG 220
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
267-473 |
3.05e-22 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 97.16 E-value: 3.05e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 267 PRDSREEEIAIEARGLTMRFGNFVAVDHVNFRIARGEIFGFLGSNGCGKSTTMK---MLTGLLPA--SEGEAW-----LF 336
Cdd:PRK14243 1 TSTLNGTETVLRTENLNVYYGSFLAVKNVWLDIPKNQITAFIGPSGCGKSTILRcfnRLNDLIPGfrVEGKVTfhgknLY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 337 GQPVDPkdIATRQRVGYMSQAFSLYSElSVRQNLELHARL--FHIPDDEIAHRvaEMSERFMLTEVKDALPAD---LPLG 411
Cdd:PRK14243 81 APDVDP--VEVRRRIGMVFQKPNPFPK-SIYDNIAYGARIngYKGDMDELVER--SLRQAALWDEVKDKLKQSglsLSGG 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1820369315 412 IRQRLSLAVAVIHRPEMLILDEPTSGVDPVARDMFWQLMVDLARQdrVTIFISTHFMNEAER 473
Cdd:PRK14243 156 QQQRLCIARAIAVQPEVILMDEPCSALDPISTLRIEELMHELKEQ--YTIIIVTHNMQQAAR 215
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
15-235 |
3.54e-22 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 99.00 E-value: 3.54e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 15 LENVGQQYGATIALRDISLAIPARRMVGLIGPDGVGKSSLLSLIAGARAIEQGNVMVLGGDMRDVHHRRDvcpKIAWMPQ 94
Cdd:PRK10851 5 IANIKKSFGRTQVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFHGTDVSRLHARDR---KVGFVFQ 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 95 GLGknLYHTLSVYENVDFFARLFGH----DKAERELRINELLQSTGLAPFRDRPAGKLSGGMKQKLGLCCALIHDPQLLI 170
Cdd:PRK10851 82 HYA--LFRHMTVFDNIAFGLTVLPRrerpNAAAIKAKVTQLLEMVQLAHLADRYPAQLSGGQKQRVALARALAVEPQILL 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1820369315 171 LDEPTTGVDPLSRAqfwELIDSIRQRQPEM---SVLVaTAYMEEA-ERFDWLVAMNAGEVLATGSAAEL 235
Cdd:PRK10851 160 LDEPFGALDAQVRK---ELRRWLRQLHEELkftSVFV-THDQEEAmEVADRVVVMSQGNIEQAGTPDQV 224
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
277-499 |
3.99e-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: 96.40 E-value: 3.99e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 277 IEARGLTMRFG--NFVAVDHVNFRIARGEIFGFLGSNGCGKSTTMKMLTGLLPASEGEAWlfgqpVDPKDIAT------R 348
Cdd:cd03252 1 ITFEHVRFRYKpdGPVILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVL-----VDGHDLALadpawlR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 349 QRVGYMSQAFSLYSElSVRQNLELHARLFHIPDDEIAHRVAEMSERFM-LTEVKDAL----PADLPLGIRQRLSLAVAVI 423
Cdd:cd03252 76 RQVGVVLQENVLFNR-SIRDNIALADPGMSMERVIEAAKLAGAHDFISeLPEGYDTIvgeqGAGLSGGQRQRIAIARALI 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1820369315 424 HRPEMLILDEPTSGVDPVARDMFWQLMVDLArqDRVTIFISTHFMNEAERCDRISLMHAGKVLASDTPQALVEQRG 499
Cdd:cd03252 155 HNPRILIFDEATSALDYESEHAIMRNMHDIC--AGRTVIIIAHRLSTVKNADRIIVMEKGRIVEQGSHDELLAENG 228
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
291-494 |
4.41e-22 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 97.40 E-value: 4.41e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 291 AVDHVNFRIARGEIFGFLGSNGCGKSTTMKMLTGLLPASEGEAWLfGQPV-----DPKDIAT-RQRVGYM-----SQAFs 359
Cdd:PRK13634 22 ALYDVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVTI-GERVitagkKNKKLKPlRKKVGIVfqfpeHQLF- 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 360 lysELSVRQNLELHARLFHIPDDEIAHRVAEMSERFMLTE-VKDALPADLPLGIRQRLSLAVAVIHRPEMLILDEPTSGV 438
Cdd:PRK13634 100 ---EETVEKDICFGPMNFGVSEEDAKQKAREMIELVGLPEeLLARSPFELSGGQMRRVAIAGVLAMEPEVLVLDEPTAGL 176
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1820369315 439 DPVAR----DMFWQLMvdlaRQDRVTIFISTHFMNEAER-CDRISLMHAGKVLASDTPQAL 494
Cdd:PRK13634 177 DPKGRkemmEMFYKLH----KEKGLTTVLVTHSMEDAARyADQIVVMHKGTVFLQGTPREI 233
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
15-234 |
4.50e-22 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 98.72 E-value: 4.50e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 15 LENVGQQY----GATIALRDISLAIPARRMVGLIGPDGVGKSSLLSLIAGARAIEQGNVMVLGGDM-----RDVHHRRDv 85
Cdd:PRK11153 4 LKNISKVFpqggRTIHALNNVSLHIPAGEIFGVIGASGAGKSTLIRCINLLERPTSGRVLVDGQDLtalseKELRKARR- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 86 cpKIAWMPQGLgkNLYHTLSVYENVDFFARLFGHDKAERELRINELLQSTGLAPFRDR-PAgKLSGGMKQKLGLCCALIH 164
Cdd:PRK11153 83 --QIGMIFQHF--NLLSSRTVFDNVALPLELAGTPKAEIKARVTELLELVGLSDKADRyPA-QLSGGQKQRVAIARALAS 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1820369315 165 DPQLLILDEPTTGVDPLSRAQFWELIDSIrQRQPEMSVLVATAYMEEAERF-DWLVAMNAGEVLATGSAAE 234
Cdd:PRK11153 158 NPKVLLCDEATSALDPATTRSILELLKDI-NRELGLTIVLITHEMDVVKRIcDRVAVIDAGRLVEQGTVSE 227
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
17-235 |
4.74e-22 |
|
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: 99.02 E-value: 4.74e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 17 NVGQQYGAtIALrDISLAIPARRMVGLIGPDGVGKSSLLSLIAGARAIEQGNVMVLG--------GDMRDVHHRRdvcpk 88
Cdd:COG4148 6 DFRLRRGG-FTL-DVDFTLPGRGVTALFGPSGSGKTTLLRAIAGLERPDSGRIRLGGevlqdsarGIFLPPHRRR----- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 89 IAWMPQGlgKNLYHTLSVYENVdffarLFGH---DKAERELRINELLQSTGLAPFRDRPAGKLSGGMKQKLGLCCALIHD 165
Cdd:COG4148 79 IGYVFQE--ARLFPHLSVRGNL-----LYGRkraPRAERRISFDEVVELLGIGHLLDRRPATLSGGERQRVAIGRALLSS 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1820369315 166 PQLLILDEPTTGVDPLSRAQFWELIDSIRQRQpEMSVLVATAYMEEAERF-DWLVAMNAGEVLATGSAAEL 235
Cdd:COG4148 152 PRLLLMDEPLAALDLARKAEILPYLERLRDEL-DIPILYVSHSLDEVARLaDHVVLLEQGRVVASGPLAEV 221
|
|
| anch_rpt_ABC |
TIGR03771 |
anchored repeat-type ABC transporter, ATP-binding subunit; This protein family is the ... |
297-520 |
5.14e-22 |
|
anchored repeat-type ABC transporter, ATP-binding subunit; This protein family is the ATP-binding cassette subunit of binding protein-dependent ABC transporter complex that strictly co-occurs with TIGR03769. TIGRFAMs model TIGR03769 describes a protein domain that occurs singly or as one of up to three repeats in proteins of a number of Actinobacteria, including Propionibacterium acnes KPA171202. The TIGR03769 domain occurs both in an adjacent gene for the substrate-binding protein and in additional (often nearby) proteins, often with LPXTG-like sortase recognition signals. Homologous ATP-binding subunits outside the scope of this family include manganese transporter MntA in Synechocystis sp. PCC 6803 and chelated iron transporter subunits. The function of this transporter complex is unknown. [Transport and binding proteins, Unknown substrate]
Pssm-ID: 163483 [Multi-domain] Cd Length: 223 Bit Score: 95.69 E-value: 5.14e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 297 FRIARGEIFGFLGSNGCGKSTTMKMLTGLLPASEGEAWLFGQPVDPkdiaTRQRVGYMSQ--AFSLYSELSVRQNLeLHA 374
Cdd:TIGR03771 1 LSADKGELLGLLGPNGAGKTTLLRAILGLIPPAKGTVKVAGASPGK----GWRHIGYVPQrhEFAWDFPISVAHTV-MSG 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 375 RLFHI-------PDDEIAhrVAEMSERFMLTEVKDALPADLPLGIRQRLSLAVAVIHRPEMLILDEPTSGVDPVARDMFW 447
Cdd:TIGR03771 76 RTGHIgwlrrpcVADFAA--VRDALRRVGLTELADRPVGELSGGQRQRVLVARALATRPSVLLLDEPFTGLDMPTQELLT 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1820369315 448 QLMVDLArQDRVTIFISTHFMNEA-ERCDRISLMHaGKVLASDTPQALveqRGAASLEEAFiawlkEAQPSSPV 520
Cdd:TIGR03771 154 ELFIELA-GAGTAILMTTHDLAQAmATCDRVVLLN-GRVIADGTPQQL---QDPAPWMTTF-----GVSDSSPL 217
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
292-492 |
6.94e-22 |
|
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: 95.23 E-value: 6.94e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 292 VDHVNFRIARGEIFGFLGSNGCGKSTTMKMLTGLLPASEGEAWLFGQPVDPKDiATRQRVgymSQAFSLYSELSVRQNLE 371
Cdd:TIGR01184 1 LKGVNLTIQQGEFISLIGHSGCGKSTLLNLISGLAQPTSGGVILEGKQITEPG-PDRMVV---FQNYSLLPWLTVRENIA 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 372 L--HARLFHIPDDEIAHRVAEMSERFMLTEVKDALPADLPLGIRQRLSLAVAVIHRPEMLILDEPTSGVDPVARDMFWQL 449
Cdd:TIGR01184 77 LavDRVLPDLSKSERRAIVEEHIALVGLTEAADKRPGQLSGGMKQRVAIARALSIRPKVLLLDEPFGALDALTRGNLQEE 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1820369315 450 MVDLARQDRVTIFISTHFMNEAE-RCDRISLM------HAGKVLASDTPQ 492
Cdd:TIGR01184 157 LMQIWEEHRVTVLMVTHDVDEALlLSDRVVMLtngpaaNIGQILEVPFPR 206
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
291-491 |
8.36e-22 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 96.41 E-value: 8.36e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 291 AVDHVNFRIARGEIFGFLGSNGCGKSTTMKMLTGLL---PASEGEAWLFGQPVDPKDI-ATRQRVGYM-----SQAFSLY 361
Cdd:PRK13640 22 ALNDISFSIPRGSWTALIGHNGSGKSTISKLINGLLlpdDNPNSKITVDGITLTAKTVwDIREKVGIVfqnpdNQFVGAT 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 362 SELSVRQNLELHArlfhIPDDEIAHRVAEMSERFMLTEVKDALPADLPLGIRQRLSLAVAVIHRPEMLILDEPTSGVDPV 441
Cdd:PRK13640 102 VGDDVAFGLENRA----VPRPEMIKIVRDVLADVGMLDYIDSEPANLSGGQKQRVAIAGILAVEPKIIILDESTSMLDPA 177
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1820369315 442 ARDMFWQLMVDLARQDRVTIFISTHFMNEAERCDRISLMHAGKVLASDTP 491
Cdd:PRK13640 178 GKEQILKLIRKLKKKNNLTVISITHDIDEANMADQVLVLDDGKLLAQGSP 227
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
277-485 |
1.01e-21 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 97.11 E-value: 1.01e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 277 IEARGLTMRF---GNFV--------AVDHVNFRIARGEIFGFLGSNGCGKSTTMKMLTGLLPASEGEAWLFGQPV---DP 342
Cdd:COG4608 8 LEVRDLKKHFpvrGGLFgrtvgvvkAVDGVSFDIRRGETLGLVGESGCGKSTLGRLLLRLEEPTSGEILFDGQDItglSG 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 343 KDI-ATRQRVGYMSQ---AfSLYSELSVRQNLELHARLFHI-PDDEIAHRVAEMSERFML-TEVKDALPADLPLGIRQRL 416
Cdd:COG4608 88 RELrPLRRRMQMVFQdpyA-SLNPRMTVGDIIAEPLRIHGLaSKAERRERVAELLELVGLrPEHADRYPHEFSGGQRQRI 166
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1820369315 417 SLAVAVIHRPEMLILDEPTSgvdpvARDMFWQ-----LMVDLARQDRVT-IFIStHFMNEAER-CDRISLMHAGKV 485
Cdd:COG4608 167 GIARALALNPKLIVCDEPVS-----ALDVSIQaqvlnLLEDLQDELGLTyLFIS-HDLSVVRHiSDRVAVMYLGKI 236
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
295-486 |
1.03e-21 |
|
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette superfamily; ABCG transporters are involved in eye pigment (EP) precursor transport, regulation of lipid-trafficking mechanisms, and pleiotropic drug resistance (DR). DR is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. Compared to other members of the ABC transporter subfamilies, the ABCG transporter family is composed of proteins that have an ATP-binding cassette domain at the N-terminus and a TM (transmembrane) domain at the C-terminus.
Pssm-ID: 213180 [Multi-domain] Cd Length: 194 Bit Score: 93.77 E-value: 1.03e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 295 VNFRIARGEIFGFLGSNGCGKSTTMKMLTGLL--PASEGEAWLFGQPVDPKDIatRQRVGYMSQAFSLYSELSVRQNLEL 372
Cdd:cd03213 28 VSGKAKPGELTAIMGPSGAGKSTLLNALAGRRtgLGVSGEVLINGRPLDKRSF--RKIIGYVPQDDILHPTLTVRETLMF 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 373 HARLfhipddeiahRVaemserfmltevkdalpadLPLGIRQRLSLAVAVIHRPEMLILDEPTSGVDPV-ARDMFwQLMV 451
Cdd:cd03213 106 AAKL----------RG-------------------LSGGERKRVSIALELVSNPSLLFLDEPTSGLDSSsALQVM-SLLR 155
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1820369315 452 DLARQDRvTIFISTH------FmneaERCDRISLMHAGKVL 486
Cdd:cd03213 156 RLADTGR-TIICSIHqpsseiF----ELFDKLLLLSQGRVI 191
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
127-474 |
1.32e-21 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 99.32 E-value: 1.32e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 127 RINELLQSTGLAPFRDRPAGKLSGGMKQKLGLCCALIHDPQLLILDEPTTGVDPLSRAQFWELIDSIRQRQPEMsVLVAT 206
Cdd:PRK10938 115 RCEQLAQQFGITALLDRRFKYLSTGETRKTLLCQALMSEPDLLILDEPFDGLDVASRQQLAELLASLHQSGITL-VLVLN 193
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 207 aymeeaeRFDWL--VAMNAGeVLA------TGSAAELKAQTGSQTL---EQAFIALLPEAQRQAHKTvVIPPRDSReeei 275
Cdd:PRK10938 194 -------RFDEIpdFVQFAG-VLAdctlaeTGEREEILQQALVAQLahsEQLEGVQLPEPDEPSARH-ALPANEPR---- 260
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 276 aIEARGLTMRFGNFVAVDHVNFRIARGEIFGFLGSNGCGKSTTMKMLTGLLPAS-EGEAWLFGQPVDPK----DIatRQR 350
Cdd:PRK10938 261 -IVLNNGVVSYNDRPILHNLSWQVNPGEHWQIVGPNGAGKSTLLSLITGDHPQGySNDLTLFGRRRGSGetiwDI--KKH 337
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 351 VGYMSQAFSL----------------------YSELSVRQNL---ELHARLfhipddEIAHRVAEMSERfmltevkdalp 405
Cdd:PRK10938 338 IGYVSSSLHLdyrvstsvrnvilsgffdsigiYQAVSDRQQKlaqQWLDIL------GIDKRTADAPFH----------- 400
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 406 aDLPLGiRQRLSLAV-AVIHRPEMLILDEPTSGVDPVARDMFWQLMVDLARQDRVTIFISTHFMNEAERC 474
Cdd:PRK10938 401 -SLSWG-QQRLALIVrALVKHPTLLILDEPLQGLDPLNRQLVRRFVDVLISEGETQLLFVSHHAEDAPAC 468
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
276-471 |
1.47e-21 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 95.31 E-value: 1.47e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 276 AIEARGLTMRFGNFV----AVDHVNFRIARGEIFGFLGSNGCGKSTTMKMLTGLLPASEGEAWLFGQPVDPKDiATRqrv 351
Cdd:COG4525 3 MLTVRHVSVRYPGGGqpqpALQDVSLTIESGEFVVALGASGCGKTTLLNLIAGFLAPSSGEITLDGVPVTGPG-ADR--- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 352 GYMSQAFSLYSELSVRQNLELHARLFHIPDDEIAHRVAEMSERFMLTEVKDALPADLPLGIRQRLSLAVAVIHRPEMLIL 431
Cdd:COG4525 79 GVVFQKDALLPWLNVLDNVAFGLRLRGVPKAERRARAEELLALVGLADFARRRIWQLSGGMRQRVGIARALAADPRFLLM 158
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1820369315 432 DEPTSGVDPVARDMFWQLMVDLARQDRVTIFISTHFMNEA 471
Cdd:COG4525 159 DEPFGALDALTREQMQELLLDVWQRTGKGVFLITHSVEEA 198
|
|
| LolD_lipo_ex |
TIGR02211 |
lipoprotein releasing system, ATP-binding protein; This model represents LolD, a member of the ... |
277-485 |
4.02e-21 |
|
lipoprotein releasing system, ATP-binding protein; This model represents LolD, a member of the ABC transporter family (pfam00005). LolD is involved in localization of lipoproteins in some bacteria. It works with a transmembrane protein LolC, which in some species is a paralogous pair LolC and LolE. Depending on whether the residue immediately following the new, modified N-terminal Cys residue, the nascent lipoprotein may be carried further by LolA and LolB to the outer membrane, or remain at the inner membrane. The top scoring proteins excluded by this model include homologs from the archaeal genus Methanosarcina. [Protein fate, Protein and peptide secretion and trafficking]
Pssm-ID: 131266 [Multi-domain] Cd Length: 221 Bit Score: 92.80 E-value: 4.02e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 277 IEARGLTMRF--GNF--VAVDHVNFRIARGEIFGFLGSNGCGKSTTMKMLTGLLPASEGEAWLFGQPV----DPKDIATR 348
Cdd:TIGR02211 2 LKCENLGKRYqeGKLdtRVLKGVSLSIGKGEIVAIVGSSGSGKSTLLHLLGGLDNPTSGEVLFNGQSLsklsSNERAKLR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 349 QR-VGYMSQAFSLYSELSVRQNLELHARLFHIPDDEIAHRVAEMSERFMLTEVKDALPADLPLGIRQRLSLAVAVIHRPE 427
Cdd:TIGR02211 82 NKkLGFIYQFHHLLPDFTALENVAMPLLIGKKSVKEAKERAYEMLEKVGLEHRINHRPSELSGGERQRVAIARALVNQPS 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1820369315 428 MLILDEPTSGVDPVARDMFWQLMVDLARQDRVTIFISTHFMNEAERCDRISLMHAGKV 485
Cdd:TIGR02211 162 LVLADEPTGNLDNNNAKIIFDLMLELNRELNTSFLVVTHDLELAKKLDRVLEMKDGQL 219
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
292-521 |
4.52e-21 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 94.51 E-value: 4.52e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 292 VDHVNFRIARGEIFGFLGSNGCGKSTTMKMLTGLLPASEGEAWLFGQPVDP-------KDIatRQRVGYM-----SQAFs 359
Cdd:PRK13641 23 LDNISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITIAGYHITPetgnknlKKL--RKKVSLVfqfpeAQLF- 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 360 lysELSVRQNLELHARLFHIPDDEIAHRVAEMSERFMLTE-VKDALPADLPLGIRQRLSLAVAVIHRPEMLILDEPTSGV 438
Cdd:PRK13641 100 ---ENTVLKDVEFGPKNFGFSEDEAKEKALKWLKKVGLSEdLISKSPFELSGGQMRRVAIAGVMAYEPEILCLDEPAAGL 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 439 DPVARDMFWQLMVDLARQDRVTIFIsTHFMNE-AERCDRISLMHAGKVLASDTPQALVEQRgaasleeafiAWLKEAQPS 517
Cdd:PRK13641 177 DPEGRKEMMQLFKDYQKAGHTVILV-THNMDDvAEYADDVLVLEHGKLIKHASPKEIFSDK----------EWLKKHYLD 245
|
....
gi 1820369315 518 SPVP 521
Cdd:PRK13641 246 EPAT 249
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
275-480 |
4.91e-21 |
|
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: 98.13 E-value: 4.91e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 275 IAIEARGLTMRF-GNFVAVDHVNFRIARGEIFGFLGSNGCGKSTTMKMLTGLLPASEGEAWLFGQPVDPKDIAT-RQRVG 352
Cdd:TIGR02857 320 SSLEFSGVSVAYpGRRPALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSIAVNGVPLADADADSwRDQIA 399
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 353 YMSQAFSLYsELSVRQNLELHARlfhipdDEIAHRVAEMSERFMLTEVKDALPA--DLPL---------GIRQRLSLAVA 421
Cdd:TIGR02857 400 WVPQHPFLF-AGTIAENIRLARP------DASDAEIREALERAGLDEFVAALPQglDTPIgeggaglsgGQAQRLALARA 472
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1820369315 422 VIHRPEMLILDEPTSGVDPVARDMFWQLMVDLARqdRVTIFISTHFMNEAERCDRISLM 480
Cdd:TIGR02857 473 FLRDAPLLLLDEPTAHLDAETEAEVLEALRALAQ--GRTVLLVTHRLALAALADRIVVL 529
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
15-240 |
5.07e-21 |
|
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: 93.06 E-value: 5.07e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 15 LENVGQQYGATI--ALRDISLAIPARRMVGLIGPDGVGKSSLLSLIAGARAIEQGNVMVLGGDMRDV---HHRRdvcpKI 89
Cdd:cd03251 3 FKNVTFRYPGDGppVLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDGHDVRDYtlaSLRR----QI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 90 AWMPQGLgkNLYHTlSVYENVdffarLFGHDKAERElRINELLQSTGLAPFRDR-PAG----------KLSGGMKQKLGL 158
Cdd:cd03251 79 GLVSQDV--FLFND-TVAENI-----AYGRPGATRE-EVEEAARAANAHEFIMElPEGydtvigergvKLSGGQRQRIAI 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 159 CCALIHDPQLLILDEPTTGVDPLSRaqfwELI-DSIRQRQPEMSVLVATAYMEEAERFDWLVAMNAGEVLATGSAAELKA 237
Cdd:cd03251 150 ARALLKDPPILILDEATSALDTESE----RLVqAALERLMKNRTTFVIAHRLSTIENADRIVVLEDGKIVERGTHEELLA 225
|
...
gi 1820369315 238 QTG 240
Cdd:cd03251 226 QGG 228
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
16-214 |
5.14e-21 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 93.69 E-value: 5.14e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 16 ENVGQQYGATIALRDISLAIPARRMVGLIGPDGVGKSSLL-------SLIAGARAieQGNVMVLGGDMRD-----VHHRR 83
Cdd:PRK14243 14 ENLNVYYGSFLAVKNVWLDIPKNQITAFIGPSGCGKSTILrcfnrlnDLIPGFRV--EGKVTFHGKNLYApdvdpVEVRR 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 84 DVcPKIAWMPQGLGKnlyhtlSVYENVDFFARLFGH-----DKAERELR-------INELLQSTGLApfrdrpagkLSGG 151
Cdd:PRK14243 92 RI-GMVFQKPNPFPK------SIYDNIAYGARINGYkgdmdELVERSLRqaalwdeVKDKLKQSGLS---------LSGG 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1820369315 152 MKQKLGLCCALIHDPQLLILDEPTTGVDPLSRAQFWELIDSIRQRqpeMSVLVATAYMEEAER 214
Cdd:PRK14243 156 QQQRLCIARAIAVQPEVILMDEPCSALDPISTLRIEELMHELKEQ---YTIIIVTHNMQQAAR 215
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
285-494 |
5.28e-21 |
|
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: 95.56 E-value: 5.28e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 285 RFGNFvAVDhVNFRIARGEIFGFLGSNGCGKSTTMKMLTGLLPASEGEAWLFGQPVDP--KDIAT---RQRVGYMSQAFS 359
Cdd:TIGR02142 8 RLGDF-SLD-ADFTLPGQGVTAIFGRSGSGKTTLIRLIAGLTRPDEGEIVLNGRTLFDsrKGIFLppeKRRIGYVFQEAR 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 360 LYSELSVRQNLElHARLFHIPDDEIAhRVAEMSERFMLTEVKDALPADLPLGIRQRLSLAVAVIHRPEMLILDEPTSGVD 439
Cdd:TIGR02142 86 LFPHLSVRGNLR-YGMKRARPSERRI-SFERVIELLGIGHLLGRLPGRLSGGEKQRVAIGRALLSSPRLLLMDEPLAALD 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1820369315 440 PVARDMFWQLMVDLARQDRVTIFISTHFMNEAER-CDRISLMHAGKVLASDTPQAL 494
Cdd:TIGR02142 164 DPRKYEILPYLERLHAEFGIPILYVSHSLQEVLRlADRVVVLEDGRVAAAGPIAEV 219
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
276-512 |
5.40e-21 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 93.16 E-value: 5.40e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 276 AIEARGLTMRFGNFVAVDHVNFRIARGEIFGFLGSNGCGKSTTMKMLTGL-LPAS-----EGEAWLFGQPVDPKDIAT-R 348
Cdd:PRK11124 2 SIQLNGINCFYGAHQALFDITLDCPQGETLVLLGPSGAGKSSLLRVLNLLeMPRSgtlniAGNHFDFSKTPSDKAIRElR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 349 QRVGYMSQAFSLYSELSVRQNL-ELHARLFHIPDDEIAHRVAEMSERFMLTEVKDALPADLPLGIRQRLSLAVAVIHRPE 427
Cdd:PRK11124 82 RNVGMVFQQYNLWPHLTVQQNLiEAPCRVLGLSKDQALARAEKLLERLRLKPYADRFPLHLSGGQQQRVAIARALMMEPQ 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 428 MLILDEPTSGVDPVARDMFWQLMVDLArQDRVTIFISTHFMNEAER-CDRISLMHAGKVlasdtpqalVEQRGAASLE-- 504
Cdd:PRK11124 162 VLLFDEPTAALDPEITAQIVSIIRELA-ETGITQVIVTHEVEVARKtASRVVYMENGHI---------VEQGDASCFTqp 231
|
250
....*....|
gi 1820369315 505 --EAFIAWLK 512
Cdd:PRK11124 232 qtEAFKNYLS 241
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
277-507 |
6.42e-21 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 96.06 E-value: 6.42e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 277 IEARGLTMRFGNFVAVDHVNFRIARGEIFGFLGSNGCGKSTTMKMLTGLLPASEGEAWLFGQPVDPKDIAT-RQRVGYMS 355
Cdd:PRK09536 4 IDVSDLSVEFGDTTVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGDDVEALSARAaSRRVASVP 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 356 QAFSLYSELSVRQNLEL----HARLF--HIPDDEIAhrVAEMSERFMLTEVKDALPADLPLGIRQRLSLAVAVIHRPEML 429
Cdd:PRK09536 84 QDTSLSFEFDVRQVVEMgrtpHRSRFdtWTETDRAA--VERAMERTGVAQFADRPVTSLSGGERQRVLLARALAQATPVL 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1820369315 430 ILDEPTSGVDPVARDMFWQLMVDLARQDRvTIFISTHFMNEAER-CDRISLMHAGKVLASDTPQALVEqrgAASLEEAF 507
Cdd:PRK09536 162 LLDEPTASLDINHQVRTLELVRRLVDDGK-TAVAAIHDLDLAARyCDELVLLADGRVRAAGPPADVLT---ADTLRAAF 236
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
103-245 |
7.17e-21 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 95.19 E-value: 7.17e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 103 TLSVYENVDFFARLFGHDKAERELRINELLQSTGLAPFRDRPAGKLSGGMKQKLGLCCALIHDPQLLILDEPTTGVDPLS 182
Cdd:NF000106 100 SFSGRENLYMIGR*LDLSRKDARARADELLERFSLTEAAGRAAAKYSGGMRRRLDLAASMIGRPAVLYLDEPTTGLDPRT 179
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1820369315 183 RAQFWELIDSIRQRQPemSVLVATAYMEEAERF-DWLVAMNAGEVLATGSAAELKAQTGSQTLE 245
Cdd:NF000106 180 RNEVWDEVRSMVRDGA--TVLLTTQYMEEAEQLaHELTVIDRGRVIADGKVDELKTKVGGRTLQ 241
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
280-477 |
8.10e-21 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 91.77 E-value: 8.10e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 280 RGLTMRFGNFVAVDHVNFRIARGEIFGFLGSNGCGKSTTMKMLTGLLPA---SEGEAWLFGQPVDPKDIATRqRVGYMSQ 356
Cdd:COG4136 5 ENLTITLGGRPLLAPLSLTVAPGEILTLMGPSGSGKSTLLAAIAGTLSPafsASGEVLLNGRRLTALPAEQR-RIGILFQ 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 357 AFSLYSELSVRQNLelharLFHIPDD----EIAHRVAEMSERFMLTEVKDALPADLPLGIRQRLSLAVAVIHRPEMLILD 432
Cdd:COG4136 84 DDLLFPHLSVGENL-----AFALPPTigraQRRARVEQALEEAGLAGFADRDPATLSGGQRARVALLRALLAEPRALLLD 158
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1820369315 433 EPTSGVDPVARDMFWQLMVDLARQDRVTIFISTHFMNEAERCDRI 477
Cdd:COG4136 159 EPFSKLDAALRAQFREFVFEQIRQRGIPALLVTHDEEDAPAAGRV 203
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
280-485 |
1.28e-20 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 94.71 E-value: 1.28e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 280 RGLTMRFGNFVAVDHVNFRIARGEIFGFLGSNGCGKSTTMKMLTGLLPASEGEAWLFGQPVDpkDIATRQR-VGYMSQAF 358
Cdd:PRK11000 7 RNVTKAYGDVVISKDINLDIHEGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLFIGEKRMN--DVPPAERgVGMVFQSY 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 359 SLYSELSVRQNLELHARLFHIPDDEIAHRVAEMSERFMLTEVKDALPADLPLGIRQRLSLAVAVIHRPEMLILDEPTSGV 438
Cdd:PRK11000 85 ALYPHLSVAENMSFGLKLAGAKKEEINQRVNQVAEVLQLAHLLDRKPKALSGGQRQRVAIGRTLVAEPSVFLLDEPLSNL 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1820369315 439 DPVARdmfWQLMVDLAR---QDRVTIFISTHFMNEA-ERCDRISLMHAGKV 485
Cdd:PRK11000 165 DAALR---VQMRIEISRlhkRLGRTMIYVTHDQVEAmTLADKIVVLDAGRV 212
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
15-235 |
1.77e-20 |
|
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440743 [Multi-domain] Cd Length: 239 Bit Score: 91.59 E-value: 1.77e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 15 LENVGQQYGATIALRDISLAIPARRMVGLIGPDGVGKSSLLSLIAGARAIEQGNVMV----LGGDMRDVHHRRDvcpKIA 90
Cdd:COG1126 4 IENLHKSFGDLEVLKGISLDVEKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTITVdgedLTDSKKDINKLRR---KVG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 91 WMPQGLgkNLYHTLSVYENVdFFA--RLFGHDKAERELRINELLQSTGLAPFRDRPAGKLSGGMKQKLGLCCALIHDPQL 168
Cdd:COG1126 81 MVFQQF--NLFPHLTVLENV-TLApiKVKKMSKAEAEERAMELLERVGLADKADAYPAQLSGGQQQRVAIARALAMEPKV 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1820369315 169 LILDEPTTGVDPlsraqfwELI----DSIRQ-RQPEMSVLVATAYMEEAER-FDWLVAMNAGEVLATGSAAEL 235
Cdd:COG1126 158 MLFDEPTSALDP-------ELVgevlDVMRDlAKEGMTMVVVTHEMGFAREvADRVVFMDGGRIVEEGPPEEF 223
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
276-494 |
1.87e-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: 94.01 E-value: 1.87e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 276 AIEARgLTMRFGNFvAVDhVNFRIARGEIFGFLGSNGCGKSTTMKMLTGLLPASEGEAWLFGQP-VDPK---DIATRQR- 350
Cdd:COG4148 2 MLEVD-FRLRRGGF-TLD-VDFTLPGRGVTALFGPSGSGKTTLLRAIAGLERPDSGRIRLGGEVlQDSArgiFLPPHRRr 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 351 VGYMSQAFSLYSELSVRQNLELHARlfHIPDDEIAHRVAEMSERFMLTEVKDALPADLPLGIRQRLSLAVAVIHRPEMLI 430
Cdd:COG4148 79 IGYVFQEARLFPHLSVRGNLLYGRK--RAPRAERRISFDEVVELLGIGHLLDRRPATLSGGERQRVAIGRALLSSPRLLL 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1820369315 431 LDEPTSGVDPVARDmfwQLM---VDLARQDRVTIFISTHFMNEAER-CDRISLMHAGKVLASDTPQAL 494
Cdd:COG4148 157 MDEPLAALDLARKA---EILpylERLRDELDIPILYVSHSLDEVARlADHVVLLEQGRVVASGPLAEV 221
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
278-484 |
1.91e-20 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 96.01 E-value: 1.91e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 278 EARGLTMRFGNFVAVDHVNFRIARGEIFGFLGSNGCGKSTTMKMLTGLLPAS--EGEAWLFGQPVDPKDIATRQRVG--Y 353
Cdd:NF040905 3 EMRGITKTFPGVKALDDVNLSVREGEIHALCGENGAGKSTLMKVLSGVYPHGsyEGEILFDGEVCRFKDIRDSEALGivI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 354 MSQAFSLYSELSVRQNLEL---HARLFHIPDDEIAHRVAEMSERFMLTEVKDALPADLPLGIRQRLSLAVAVIHRPEMLI 430
Cdd:NF040905 83 IHQELALIPYLSIAENIFLgneRAKRGVIDWNETNRRARELLAKVGLDESPDTLVTDIGVGKQQLVEIAKALSKDVKLLI 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1820369315 431 LDEPTSGVDPVARDMFWQLMVDLARQDRVTIFIStHFMNEAER-CDRISLMHAGK 484
Cdd:NF040905 163 LDEPTAALNEEDSAALLDLLLELKAQGITSIIIS-HKLNEIRRvADSITVLRDGR 216
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
285-480 |
2.22e-20 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 89.99 E-value: 2.22e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 285 RFGNFVAVDHVNFRIARGEIFGFLGSNGCGKSTTMKMLTGLLPASEGEAwlfgqpvdpkDIATRQRVGYMSQAFSLYSEL 364
Cdd:NF040873 1 GYGGRPVLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTV----------RRAGGARVAYVPQRSEVPDSL 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 365 --SVRQNLEL----HARLFHIPDDEIAHRVAEMSERFMLTEVKDALPADLPLGIRQRLSLAVAVIHRPEMLILDEPTSGV 438
Cdd:NF040873 71 plTVRDLVAMgrwaRRGLWRRLTRDDRAAVDDALERVGLADLAGRQLGELSGGQRQRALLAQGLAQEADLLLLDEPTTGL 150
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1820369315 439 DPVARDMFWQLMVDLARQDRvTIFISTHFMNEAERCDRISLM 480
Cdd:NF040873 151 DAESRERIIALLAEEHARGA-TVVVVTHDLELVRRADPCVLL 191
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
30-237 |
2.32e-20 |
|
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding cassette (ABC) protein of the three subunit molybdate ABC transporter. The three proteins of this complex are homologous to proteins of the sulfate ABC transporter. Molybdenum may be used in nitrogenases of nitrogen-fixing bacteria and in molybdopterin cofactors. In some cases, molybdate may be transported by a sulfate transporter rather than by a specific molybdate transporter. [Transport and binding proteins, Anions]
Pssm-ID: 131197 [Multi-domain] Cd Length: 354 Bit Score: 93.64 E-value: 2.32e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 30 DISLAIPARRMVGLIGPDGVGKSSLLSLIAGARAIEQGNVMVLGGDMRDVHHRRDVCP---KIAWMPQGlgKNLYHTLSV 106
Cdd:TIGR02142 15 DADFTLPGQGVTAIFGRSGSGKTTLIRLIAGLTRPDEGEIVLNGRTLFDSRKGIFLPPekrRIGYVFQE--ARLFPHLSV 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 107 YENVDF-FARLFGHDKAERELRINELLqstGLAPFRDRPAGKLSGGMKQKLGLCCALIHDPQLLILDEPTTGVDPLSRAQ 185
Cdd:TIGR02142 93 RGNLRYgMKRARPSERRISFERVIELL---GIGHLLGRLPGRLSGGEKQRVAIGRALLSSPRLLLMDEPLAALDDPRKYE 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1820369315 186 FWELIDSIRQrQPEMSVLVATAYMEEAERF-DWLVAMNAGEVLATGSAAELKA 237
Cdd:TIGR02142 170 ILPYLERLHA-EFGIPILYVSHSLQEVLRLaDRVVVLEDGRVAAAGPIAEVWA 221
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
277-485 |
2.59e-20 |
|
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: 89.20 E-value: 2.59e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 277 IEARGLTMRFGNFVA--VDHVNFRIARGEIFGFLGSNGCGKSTTMKMLTGLLPASEGEAWLFGQPVDPKDIAT-RQRVGY 353
Cdd:cd03246 1 LEVENVSFRYPGAEPpvLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDGADISQWDPNElGDHVGY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 354 MSQAFSLYSElSVRQNLelharlfhipddeiahrvaemserfmltevkdalpadLPLGIRQRLSLAVAVIHRPEMLILDE 433
Cdd:cd03246 81 LPQDDELFSG-SIAENI-------------------------------------LSGGQRQRLGLARALYGNPRILVLDE 122
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1820369315 434 PTSGVDPVARDMFWQLMVDLaRQDRVTIFISTHFMNEAERCDRISLMHAGKV 485
Cdd:cd03246 123 PNSHLDVEGERALNQAIAAL-KAAGATRIVIAHRPETLASADRILVLEDGRV 173
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
14-227 |
2.67e-20 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 91.28 E-value: 2.67e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 14 LLENVGQQYGATIALRDISLAIPARRMVGLIGPDGVGKSSLLSLIAGARAIEQGNVmvLGGDMRDVHHRRDvcpkIAWMP 93
Cdd:PRK11247 14 LLNAVSKRYGERTVLNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAGEL--LAGTAPLAEARED----TRLMF 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 94 QGlgKNLYHTLSVYENVDFfaRLFGHDKAERElrinELLQSTGLApfrDR----PAGkLSGGMKQKLGLCCALIHDPQLL 169
Cdd:PRK11247 88 QD--ARLLPWKKVIDNVGL--GLKGQWRDAAL----QALAAVGLA---DRanewPAA-LSGGQKQRVALARALIHRPGLL 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1820369315 170 ILDEPTTGVDPLSRAQFWELIDSIRQrQPEMSVLVATAYMEEAerfdwlVAMnAGEVL 227
Cdd:PRK11247 156 LLDEPLGALDALTRIEMQDLIESLWQ-QHGFTVLLVTHDVSEA------VAM-ADRVL 205
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
276-529 |
2.77e-20 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 91.72 E-value: 2.77e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 276 AIEARGLTMRF--GNfVAVDHVNFRIARGEIFGFLGSNGCGKSTTMKMLTGLLPASEGEAWLFGQPVDPKDIA-TRQRVG 352
Cdd:PRK13647 4 IIEVEDLHFRYkdGT-KALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGREVNAENEKwVRSKVG 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 353 YM-----SQAFSLYSELSVR---QNLELHArlfhipdDEIAHRVAEMSERFMLTEVKDALPADLPLGIRQRLSLAVAVIH 424
Cdd:PRK13647 83 LVfqdpdDQVFSSTVWDDVAfgpVNMGLDK-------DEVERRVEEALKAVRMWDFRDKPPYHLSYGQKKRVAIAGVLAM 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 425 RPEMLILDEPTSGVDPVARDMFWQLMVDLARQDRvTIFISTHFMN-EAERCDRISLMHAGKVLASDTPQALVEQR--GAA 501
Cdd:PRK13647 156 DPDVIVLDEPMAYLDPRGQETLMEILDRLHNQGK-TVIVATHDVDlAAEWADQVIVLKEGRVLAEGDKSLLTDEDivEQA 234
|
250 260 270
....*....|....*....|....*....|.
gi 1820369315 502 SLEEAFIAWLKEAQPS---SPVPEDPTSAVA 529
Cdd:PRK13647 235 GLRLPLVAQIFEDLPElgqSKLPLTVKEAVQ 265
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
25-238 |
3.16e-20 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 91.69 E-value: 3.16e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 25 TIALRDISLAIPARRMVGLIGPDGVGKSSLLSLIAGARAIEQGNVMVLGGDMRDVHHRRDVCPKIAWMPQGLGKNLYHTL 104
Cdd:PRK13633 23 KLALDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVYVDGLDTSDEENLWDIRNKAGMVFQNPDNQIVATI 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 105 sVYENVDFFARLFGHDKAERELRINELLQSTGLAPFRDRPAGKLSGGMKQKLGLCCALIHDPQLLILDEPTTGVDPLSRA 184
Cdd:PRK13633 103 -VEEDVAFGPENLGIPPEEIRERVDESLKKVGMYEYRRHAPHLLSGGQKQRVAIAGILAMRPECIIFDEPTAMLDPSGRR 181
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1820369315 185 qfwELIDSIRQ--RQPEMSVLVATAYMEEAERFDWLVAMNAGEVLATGSAAELKAQ 238
Cdd:PRK13633 182 ---EVVNTIKElnKKYGITIILITHYMEEAVEADRIIVMDSGKVVMEGTPKEIFKE 234
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
277-492 |
4.22e-20 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 90.84 E-value: 4.22e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 277 IEARGLTMRFGNFVAVDHVNFRIARGEIFGFLGSNGCGKSTTMKMLTGLLPASEGEAWLFGQP----------------- 339
Cdd:PRK11231 3 LRTENLTVGYGTKRILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDKPismlssrqlarrlallp 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 340 ---VDPKDIATRQRVGY-MSQAFSLYSELSvrqnlelharlfhiPDDEiaHRVAEMSERFMLTEVKDALPADLPLGIRQR 415
Cdd:PRK11231 83 qhhLTPEGITVRELVAYgRSPWLSLWGRLS--------------AEDN--ARVNQAMEQTRINHLADRRLTDLSGGQRQR 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1820369315 416 LSLAVAVIHRPEMLILDEPTSGVDPVARDMFWQLMVDLARQDRvTIFISTHFMNEAER-CDRISLMHAGKVLASDTPQ 492
Cdd:PRK11231 147 AFLAMVLAQDTPVVLLDEPTTYLDINHQVELMRLMRELNTQGK-TVVTVLHDLNQASRyCDHLVVLANGHVMAQGTPE 223
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
16-206 |
4.68e-20 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 89.55 E-value: 4.68e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 16 ENVGQQYGATIALRDISLAIPARRMVGLIGPDGVGKSSLLSLIAGARAIEQGNVMVLGGDMRDVHHR--------RDVCp 87
Cdd:PRK13539 6 EDLACVRGGRVLFSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDGGDIDDPDVAeachylghRNAM- 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 88 kiawmpqglgKNlyhTLSVYENVDFFARLFGhdkaERELRINELLQSTGLAPFRDRPAGKLSGGMKQKLGLCCALIHDPQ 167
Cdd:PRK13539 85 ----------KP---ALTVAENLEFWAAFLG----GEELDIAAALEAVGLAPLAHLPFGYLSAGQKRRVALARLLVSNRP 147
|
170 180 190
....*....|....*....|....*....|....*....
gi 1820369315 168 LLILDEPTTGVDPLSRAQFWELIdSIRQRQPEMsVLVAT 206
Cdd:PRK13539 148 IWILDEPTAALDAAAVALFAELI-RAHLAQGGI-VIAAT 184
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
273-495 |
4.74e-20 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 93.56 E-value: 4.74e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 273 EEIAIEARGLTMrfgnfvAVDHVNFRIARGEIFGFLGSNGCGKSTTMKMLTGLLPASEGEAWLFGqpVDPKDIAT----- 347
Cdd:PRK10070 31 KEQILEKTGLSL------GVKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDG--VDIAKISDaelre 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 348 --RQRVGYMSQAFSLYSELSVRQNLELHARLFHIPDDEIAHRVAEMSERFMLTEVKDALPADLPLGIRQRLSLAVAVIHR 425
Cdd:PRK10070 103 vrRKKIAMVFQSFALMPHMTVLDNTAFGMELAGINAEERREKALDALRQVGLENYAHSYPDELSGGMRQRVGLARALAIN 182
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1820369315 426 PEMLILDEPTSGVDPVARDMFWQLMVDL-ARQDRVTIFIStHFMNEAERC-DRISLMHAGKVLASDTPQALV 495
Cdd:PRK10070 183 PDILLMDEAFSALDPLIRTEMQDELVKLqAKHQRTIVFIS-HDLDEAMRIgDRIAIMQNGEVVQVGTPDEIL 253
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
16-278 |
6.97e-20 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 90.63 E-value: 6.97e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 16 ENVGQQYGATI-ALRDISLAIPARRMVGLIGPDGVGKSSLLSLIAGARAIEQGNVMVLGGDMRDvHHRRDVCPKIAWMPQ 94
Cdd:PRK13652 7 RDLCYSYSGSKeALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIRGEPITK-ENIREVRKFVGLVFQ 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 95 GLGKNLYHTlSVYENVDFFARLFGHDKAERELRINELLQSTGLAPFRDRPAGKLSGGMKQKLGLCCALIHDPQLLILDEP 174
Cdd:PRK13652 86 NPDDQIFSP-TVEQDIAFGPINLGLDEETVAHRVSSALHMLGLEELRDRVPHHLSGGEKKRVAIAGVIAMEPQVLVLDEP 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 175 TTGVDPLSRAqfwELIDSIRqRQPE---MSVLVATAYME-EAERFDWLVAMNAGEVLATGSAAElkaqtgsqtleqafIA 250
Cdd:PRK13652 165 TAGLDPQGVK---ELIDFLN-DLPEtygMTVIFSTHQLDlVPEMADYIYVMDKGRIVAYGTVEE--------------IF 226
|
250 260 270
....*....|....*....|....*....|.
gi 1820369315 251 LLPEAQRQAHKTVVIPP---RDSREEEIAIE 278
Cdd:PRK13652 227 LQPDLLARVHLDLPSLPkliRSLQAQGIAID 257
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
24-246 |
7.76e-20 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 90.88 E-value: 7.76e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 24 ATIALRDISLAIPARRMVGLIGPDGVGKSSLLSLIAGARAIEQGNVMVLGGDMRDVHHR-RDVCPKIAWMPQGLGKNLYH 102
Cdd:PRK13637 19 EKKALDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDGVDITDKKVKlSDIRKKVGLVFQYPEYQLFE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 103 TlSVYENVDFFARLFGHDKAERELRINELLQSTGLA--PFRDRPAGKLSGGMKQKLGLCCALIHDPQLLILDEPTTGVDP 180
Cdd:PRK13637 99 E-TIEKDIAFGPINLGLSEEEIENRVKRAMNIVGLDyeDYKDKSPFELSGGQKRRVAIAGVVAMEPKILILDEPTAGLDP 177
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1820369315 181 LSRAQFWELIDSIRQRQpEMSVLVATAYMEEAERF-DWLVAMNAGEVLATGSAAELKAQTgsQTLEQ 246
Cdd:PRK13637 178 KGRDEILNKIKELHKEY-NMTIILVSHSMEDVAKLaDRIIVMNKGKCELQGTPREVFKEV--ETLES 241
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
28-324 |
8.09e-20 |
|
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: 94.23 E-value: 8.09e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 28 LRDISLAIPARRMVGLIGPDGVGKSSLLSLIAGARAIEQGNVMVLGGdmrdvhhrrdvcPKIAWMPQGlgKNLYHTLSVY 107
Cdd:TIGR03719 21 LKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKDFNGEARPQPG------------IKVGYLPQE--PQLDPTKTVR 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 108 ENV--------DFFARL------FG-----HDK-AERELRINELLQSTGL---------------APFRDRPAGKLSGGM 152
Cdd:TIGR03719 87 ENVeegvaeikDALDRFneisakYAepdadFDKlAAEQAELQEIIDAADAwdldsqleiamdalrCPPWDADVTKLSGGE 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 153 KQKLGLCCALIHDPQLLILDEPTTGVDPLSRAqfWelIDSIRQRQPEMSVLV---------ATAYMEEAER--------- 214
Cdd:TIGR03719 167 RRRVALCRLLLSKPDMLLLDEPTNHLDAESVA--W--LERHLQEYPGTVVAVthdryfldnVAGWILELDRgrgipwegn 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 215 -FDWLVAMNAG-EVLATGSAAELKA---------------QTGSQTLEQAFIALLPEAQRQAHKT--VVIPPRDsREEEI 275
Cdd:TIGR03719 243 ySSWLEQKQKRlEQEEKEESARQKTlkrelewvrqspkgrQAKSKARLARYEELLSQEFQKRNETaeIYIPPGP-RLGDK 321
|
330 340 350 360
....*....|....*....|....*....|....*....|....*....
gi 1820369315 276 AIEARGLTMRFGNFVAVDHVNFRIARGEIFGFLGSNGCGKSTTMKMLTG 324
Cdd:TIGR03719 322 VIEAENLTKAFGDKLLIDDLSFKLPPGGIVGVIGPNGAGKSTLFRMITG 370
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
15-197 |
8.13e-20 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 88.69 E-value: 8.13e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 15 LENVGQQYGATIALRDISLAIPARRMVGLIGPDGVGKSSLLSLIAGARAIE---QGNVMVLGGDMRD--VHHRRdvcpkI 89
Cdd:COG4136 4 LENLTITLGGRPLLAPLSLTVAPGEILTLMGPSGSGKSTLLAAIAGTLSPAfsaSGEVLLNGRRLTAlpAEQRR-----I 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 90 AWMPQ-GLgknLYHTLSVYENVdffarLFG----HDKAERELRINELLQSTGLAPFRDRPAGKLSGGMKQKLGLCCALIH 164
Cdd:COG4136 79 GILFQdDL---LFPHLSVGENL-----AFAlpptIGRAQRRARVEQALEEAGLAGFADRDPATLSGGQRARVALLRALLA 150
|
170 180 190
....*....|....*....|....*....|....
gi 1820369315 165 DPQLLILDEPTTGVDPLSRAQFWELI-DSIRQRQ 197
Cdd:COG4136 151 EPRALLLDEPFSKLDAALRAQFREFVfEQIRQRG 184
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
11-195 |
9.09e-20 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 89.55 E-value: 9.09e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 11 PIALLENVGQQYGATIALRDISLAIPARRMVGLIGPDGVGKSSLLSLIAGARAIEQGNVMVLGGDMRDVHHRRDVCPKIA 90
Cdd:PRK11614 4 VMLSFDKVSAHYGKIQALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDGKDITDWQTAKIMREAVA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 91 WMPQglGKNLYHTLSVYENV---DFFArlfghDKAERELRINELLQ-STGLAPFRDRPAGKLSGGMKQKLGLCCALIHDP 166
Cdd:PRK11614 84 IVPE--GRRVFSRMTVEENLamgGFFA-----ERDQFQERIKWVYElFPRLHERRIQRAGTMSGGEQQMLAIGRALMSQP 156
|
170 180
....*....|....*....|....*....
gi 1820369315 167 QLLILDEPTTGVDPLSRAQFWELIDSIRQ 195
Cdd:PRK11614 157 RLLLLDEPSLGLAPIIIQQIFDTIEQLRE 185
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
15-235 |
9.43e-20 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 89.76 E-value: 9.43e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 15 LENVGQQYGATIALRDISLAIPARRMVGLIGPDGVGKSSLLSLIAGARAIEQGNVMVLGgdmRDVHH--RRDVCPKIAWM 92
Cdd:COG4604 4 IKNVSKRYGGKVVLDDVSLTIPKGGITALIGPNGAGKSTLLSMISRLLPPDSGEVLVDG---LDVATtpSRELAKRLAIL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 93 PQGLGKNLyhTLSVYENVdFFARlFGHDK----AERELRINELLQSTGLAPFRDRPAGKLSGGMKQKlglccALI----- 163
Cdd:COG4604 81 RQENHINS--RLTVRELV-AFGR-FPYSKgrltAEDREIIDEAIAYLDLEDLADRYLDELSGGQRQR-----AFIamvla 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 164 HDPQLLILDEPTTGVDPL-SRaqfwELIDSIRQRQPEMS---VLV------ATAYMeeaerfDWLVAMNAGEVLATGSAA 233
Cdd:COG4604 152 QDTDYVLLDEPLNNLDMKhSV----QMMKLLRRLADELGktvVIVlhdinfASCYA------DHIVAMKDGRVVAQGTPE 221
|
..
gi 1820369315 234 EL 235
Cdd:COG4604 222 EI 223
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
294-487 |
1.28e-19 |
|
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: 88.32 E-value: 1.28e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 294 HVNFRIARGEIFGFLGSNGCGKSTTMKMLTGLLPASEGEAWLFGQPVDPKDIATRQrVGYMSQAFSLYSELSVRQN--LE 371
Cdd:cd03298 16 HFDLTFAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLINGVDVTAAPPADRP-VSMLFQENNLFAHLTVEQNvgLG 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 372 LHARLFHIPDDEiaHRVAEMSERFMLTEVKDALPADLPLGIRQRLSLAVAVIHRPEMLILDEPTSGVDPVARDMFWQLMV 451
Cdd:cd03298 95 LSPGLKLTAEDR--QAIEVALARVGLAGLEKRLPGELSGGERQRVALARVLVRDKPVLLLDEPFAALDPALRAEMLDLVL 172
|
170 180 190
....*....|....*....|....*....|....*..
gi 1820369315 452 DLARQDRVTIFISTHFMNEAERC-DRISLMHAGKVLA 487
Cdd:cd03298 173 DLHAETKMTVLMVTHQPEDAKRLaQRVVFLDNGRIAA 209
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
15-206 |
1.30e-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: 87.80 E-value: 1.30e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 15 LENVGQQYGATIALRDISLAIPARRMVGLIGPDGVGKSSLLSLIAGARAIEQGNVMVLGGDM---RDVHHRrdvcpKIAW 91
Cdd:TIGR01189 3 ARNLACSRGERMLFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRWNGTPLaeqRDEPHE-----NILY 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 92 MpqGLGKNLYHTLSVYENVDFFARLFGHDkaerELRINELLQSTGLAPFRDRPAGKLSGGMKQKLGLCCALIHDPQLLIL 171
Cdd:TIGR01189 78 L--GHLPGLKPELSALENLHFWAAIHGGA----QRTIEDALAAVGLTGFEDLPAAQLSAGQQRRLALARLWLSRRPLWIL 151
|
170 180 190
....*....|....*....|....*....|....*
gi 1820369315 172 DEPTTGVDPLSRAQFWELIDSIRQRQPemSVLVAT 206
Cdd:TIGR01189 152 DEPTTALDKAGVALLAGLLRAHLARGG--IVLLTT 184
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
27-173 |
1.46e-19 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 88.99 E-value: 1.46e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 27 ALRDISLAIPARRMVGLIGPDGVGKSSLLSLIAGARAIEQGNVMVLGgdmrdvhhrrdvcpKIAWmPQGLGKNLYHTLSV 106
Cdd:COG1134 41 ALKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTSGRVEVNG--------------RVSA-LLELGAGFHPELTG 105
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1820369315 107 YENVDFFARLFGHDKAERELRINELLQSTGLAPFRDRPAGKLSGGMKQKLGLCCALIHDPQLLILDE 173
Cdd:COG1134 106 RENIYLNGRLLGLSRKEIDEKFDEIVEFAELGDFIDQPVKTYSSGMRARLAFAVATAVDPDILLVDE 172
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
27-235 |
1.59e-19 |
|
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid transport and metabolism, Inorganic ion transport and metabolism];
Pssm-ID: 440213 [Multi-domain] Cd Length: 320 Bit Score: 90.50 E-value: 1.59e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 27 ALRDISLAIPARRMVGLIGPDGVGKSSLLSLIAG---ARAIEQGNVMVLGGD--------MRDVHHRRdvcpkIAWMPQG 95
Cdd:COG0444 20 AVDGVSFDVRRGETLGLVGESGSGKSTLARAILGllpPPGITSGEILFDGEDllklsekeLRKIRGRE-----IQMIFQD 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 96 LGKNLYHTLSVYENVDFFARLFGH-DKAERELRINELLQSTGLAPFRDRpAGK----LSGGMKQKLGLCCALIHDPQLLI 170
Cdd:COG0444 95 PMTSLNPVMTVGDQIAEPLRIHGGlSKAEARERAIELLERVGLPDPERR-LDRypheLSGGMRQRVMIARALALEPKLLI 173
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1820369315 171 LDEPTTGVDPLSRAQFWELIDSIrQRQPEMSVLVAT------AYMeeAERfdwlVA-MNAGEVLATGSAAEL 235
Cdd:COG0444 174 ADEPTTALDVTIQAQILNLLKDL-QRELGLAILFIThdlgvvAEI--ADR----VAvMYAGRIVEEGPVEEL 238
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
25-238 |
1.97e-19 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 89.52 E-value: 1.97e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 25 TIALRDISLAIPARRMVGLIGPDGVGKSSLLSLIAGARAIEQGNVMvLGGDMRDVHHRrdvcpKIAWMPQGLG------K 98
Cdd:PRK13636 19 THALKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRIL-FDGKPIDYSRK-----GLMKLRESVGmvfqdpD 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 99 NLYHTLSVYENVDFFARLFGHDKAERELRINELLQSTGLAPFRDRPAGKLSGGMKQKLGLCCALIHDPQLLILDEPTTGV 178
Cdd:PRK13636 93 NQLFSASVYQDVSFGAVNLKLPEDEVRKRVDNALKRTGIEHLKDKPTHCLSFGQKKRVAIAGVLVMEPKVLVLDEPTAGL 172
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1820369315 179 DPLSRAQFWELIDSIrQRQPEMSVLVATAYMEEAERF-DWLVAMNAGEVLATGSAAELKAQ 238
Cdd:PRK13636 173 DPMGVSEIMKLLVEM-QKELGLTIIIATHDIDIVPLYcDNVFVMKEGRVILQGNPKEVFAE 232
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
15-226 |
2.34e-19 |
|
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: 87.59 E-value: 2.34e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 15 LENVGQQYGATIALRDISLAIPARRMVGLIGPDGVGKSSLLSLIAGARAIEQGNVMV----LGGDMRDVHHRRDvcpKIA 90
Cdd:cd03262 3 IKNLHKSFGDFHVLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIdglkLTDDKKNINELRQ---KVG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 91 WMPQGLgkNLYHTLSVYENVDFFAR-LFGHDKAERELRINELLQSTGLAPFRDRPAGKLSGGMKQKLGLCCALIHDPQLL 169
Cdd:cd03262 80 MVFQQF--NLFPHLTVLENITLAPIkVKGMSKAEAEERALELLEKVGLADKADAYPAQLSGGQQQRVAIARALAMNPKVM 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1820369315 170 ILDEPTTGVDPlsraqfwELI----DSIRQRQPE-MSVLVATAYMEEA-ERFDWLVAMNAGEV 226
Cdd:cd03262 158 LFDEPTSALDP-------ELVgevlDVMKDLAEEgMTMVVVTHEMGFArEVADRVIFMDDGRI 213
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
11-235 |
3.38e-19 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 88.92 E-value: 3.38e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 11 PIALLENVGQQY--GATIALRDISLAIPARRMVGLIGPDGVGKSSLLSLIAGARAIEQGNVMVlGGDMRDVHHRRDVCPK 88
Cdd:PRK13635 4 EIIRVEHISFRYpdAATYALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITV-GGMVLSEETVWDVRRQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 89 IAWMPQGlGKNLYHTLSVYENVDFFARLFGHDKAERELRINELLQSTGLAPFRDRPAGKLSGGMKQKLGLCCALIHDPQL 168
Cdd:PRK13635 83 VGMVFQN-PDNQFVGATVQDDVAFGLENIGVPREEMVERVDQALRQVGMEDFLNREPHRLSGGQKQRVAIAGVLALQPDI 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1820369315 169 LILDEPTTGVDPLSRAqfwELIDSIRQ--RQPEMSVLVATAYMEEAERFDWLVAMNAGEVLATGSAAEL 235
Cdd:PRK13635 162 IILDEATSMLDPRGRR---EVLETVRQlkEQKGITVLSITHDLDEAAQADRVIVMNKGEILEEGTPEEI 227
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
277-488 |
3.53e-19 |
|
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome bd biogenesis. The CydC and CydD proteins are important for the formation of cytochrome bd terminal oxidase of E. coli and it has been proposed that they were necessary for biosynthesis of the cytochrome bd quinol oxidase and for periplasmic c-type cytochromes. CydCD were proposed to determine a heterooligomeric complex important for heme export into the periplasm or to be involved in the maintenance of the proper redox state of the periplasmic space. In Bacillus subtilis, the absence of CydCD does not affect the presence of halo-cytochrome c in the membrane and this observation suggests that CydCD proteins are not involved in the export of heme in this organism.
Pssm-ID: 213214 [Multi-domain] Cd Length: 178 Bit Score: 85.83 E-value: 3.53e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 277 IEARGLTMRFG--NFVAVDHVNFRIARGEIFGFLGSNGCGKSTTMKMLTGLLPASEGEAWLFGQPVDPKDIATRQRVGYM 354
Cdd:cd03247 1 LSINNVSFSYPeqEQQVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDGVPVSDLEKALSSLISVL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 355 SQAFSLYSElSVRQNLelharlfhipddeiahrvaemSERFMLTEvkdalpadlplgiRQRLSLAVAVIHRPEMLILDEP 434
Cdd:cd03247 81 NQRPYLFDT-TLRNNL---------------------GRRFSGGE-------------RQRLALARILLQDAPIVLLDEP 125
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1820369315 435 TSGVDPVARDMFWQLMVDLARqDRVTIFIsTHFMNEAERCDRISLMHAGKVLAS 488
Cdd:cd03247 126 TVGLDPITERQLLSLIFEVLK-DKTLIWI-THHLTGIEHMDKILFLENGKIIMQ 177
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
266-505 |
4.04e-19 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 88.20 E-value: 4.04e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 266 PPRDSREEEIAIEarGLTMRFGNFVAVDHVNFRIARGEIFGFLGSNGCGKSTTMKMLTGLLPASEGEAWLFGQPVDpkdi 345
Cdd:PRK11247 4 TARLNQGTPLLLN--AVSKRYGERTVLNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAGELLAGTAPLA---- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 346 ATRQRVGYMSQAFSLYSELSVRQNLELHARLFHIPDDEIAHRVAEMSERfmltevKDALPADLPLGIRQRLSLAVAVIHR 425
Cdd:PRK11247 78 EAREDTRLMFQDARLLPWKKVIDNVGLGLKGQWRDAALQALAAVGLADR------ANEWPAALSGGQKQRVALARALIHR 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 426 PEMLILDEPTSGVDPVARDMFWQLMVDLARQDRVTIFISTHFMNEA-ERCDRISLMHAGKV---LASDTPQAlvEQRGAA 501
Cdd:PRK11247 152 PGLLLLDEPLGALDALTRIEMQDLIESLWQQHGFTVLLVTHDVSEAvAMADRVLLIEEGKIgldLTVDLPRP--RRRGSA 229
|
....
gi 1820369315 502 SLEE 505
Cdd:PRK11247 230 RLAE 233
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
23-206 |
5.25e-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: 91.65 E-value: 5.25e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 23 GATIALRDISLAIPARRMVGLIGPDGVGKSSLLSLIAGARAIEQGNVMVLGGDMRDVHHRrDVCPKIAWMPQGlgKNLYH 102
Cdd:TIGR02868 346 GAPPVLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPLQGEVTLDGVPVSSLDQD-EVRRRVSVCAQD--AHLFD 422
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 103 TlSVYENVdffaRLFGHDKAERELRinELLQSTGLAPF-RDRPAG----------KLSGGMKQKLGLCCALIHDPQLLIL 171
Cdd:TIGR02868 423 T-TVRENL----RLARPDATDEELW--AALERVGLADWlRALPDGldtvlgeggaRLSGGERQRLALARALLADAPILLL 495
|
170 180 190
....*....|....*....|....*....|....*
gi 1820369315 172 DEPTTGVDPLSRAqfwELIDSIRQRQPEMSVLVAT 206
Cdd:TIGR02868 496 DEPTEHLDAETAD---ELLEDLLAALSGRTVVLIT 527
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
27-226 |
5.79e-19 |
|
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: 85.56 E-value: 5.79e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 27 ALRDISLAIPARRMVGLIGPDGVGKSSLLSLIAGARAIEQGNVMVLGGDMRDVHHRRDVCPKIAWMP---QGLGknLYHT 103
Cdd:cd03215 15 AVRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITLDGKPVTRRSPRDAIRAGIAYVPedrKREG--LVLD 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 104 LSVYENVdFFARLfghdkaerelrinellqstglapfrdrpagkLSGGMKQKLGLCCALIHDPQLLILDEPTTGVDPLSR 183
Cdd:cd03215 93 LSVAENI-ALSSL-------------------------------LSGGNQQKVVLARWLARDPRVLILDEPTRGVDVGAK 140
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1820369315 184 AQFWELIDSIRQRQpeMSVLVATAYMEEAERF-DWLVAMNAGEV 226
Cdd:cd03215 141 AEIYRLIRELADAG--KAVLLISSELDELLGLcDRILVMYEGRI 182
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
277-450 |
6.89e-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: 86.01 E-value: 6.89e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 277 IEARGLTMRFGNFVAVDHVNFRIARGEIFGFLGSNGCGKSTTMKMLTGLLPASEGEAWLFGQPVDPKDIATRQRVGYMSQ 356
Cdd:cd03231 1 LEADELTCERDGRALFSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNGGPLDFQRDSIARGLLYLGH 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 357 AFSLYSELSVRQNLELHARlFHiPDDEIAHRVAEMSerfmLTEVKDALPADLPLGIRQRLSLAVAVIHRPEMLILDEPTS 436
Cdd:cd03231 81 APGIKTTLSVLENLRFWHA-DH-SDEQVEEALARVG----LNGFEDRPVAQLSAGQQRRVALARLLLSGRPLWILDEPTT 154
|
170
....*....|....
gi 1820369315 437 GVDPVARDMFWQLM 450
Cdd:cd03231 155 ALDKAGVARFAEAM 168
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
28-250 |
7.98e-19 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 87.02 E-value: 7.98e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 28 LRDISLAIPARRMVGLIGPDGVGKSSLLSLIAgaRAIE--------QGNVMVLGGDMR--DVHHRRDVCPKIAWMPqglg 97
Cdd:PRK14246 26 LKDITIKIPNNSIFGIMGPSGSGKSTLLKVLN--RLIEiydskikvDGKVLYFGKDIFqiDAIKLRKEVGMVFQQP---- 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 98 kNLYHTLSVYENVDFFARLFG-HDKAERELRINELLQSTGL-APFRDR---PAGKLSGGMKQKLGLCCALIHDPQLLILD 172
Cdd:PRK14246 100 -NPFPHLSIYDNIAYPLKSHGiKEKREIKKIVEECLRKVGLwKEVYDRlnsPASQLSGGQQQRLTIARALALKPKVLLMD 178
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1820369315 173 EPTTGVDPLSRAQFWELIDSIRQrqpEMSVLVATAYMEEAERF-DWLVAMNAGEVLATGSAAELKAQTGSQTLEQAFIA 250
Cdd:PRK14246 179 EPTSMIDIVNSQAIEKLITELKN---EIAIVIVSHNPQQVARVaDYVAFLYNGELVEWGSSNEIFTSPKNELTEKYVIG 254
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
277-491 |
8.03e-19 |
|
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C is also known as MRP (multidrug resistance-associated protein). Some of the MRP members have five additional transmembrane segments in their N-terminus, but the function of these additional membrane-spanning domains is not clear. The MRP was found in the multidrug-resistance lung cancer cell in which p-glycoprotein was not overexpressed. MRP exports glutathione by drug stimulation, as well as, certain substrates in conjugated forms with anions, such as glutathione, glucuronate, and sulfate.
Pssm-ID: 213211 [Multi-domain] Cd Length: 221 Bit Score: 86.01 E-value: 8.03e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 277 IEARGLTMRFGN--FVAVDHVNFRIARGEIFGFLGSNGCGKSTTMKMLTGLLPASEGEAWLFGQP---VDPKDIatRQRV 351
Cdd:cd03244 3 IEFKNVSLRYRPnlPPVLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSILIDGVDiskIGLHDL--RSRI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 352 GYMSQAFSLYSElSVRQNLELHARLfhiPDDEIAHRVAEMSERFMLTEVKDALPAD-------LPLGIRQRLSLAVAVIH 424
Cdd:cd03244 81 SIIPQDPVLFSG-TIRSNLDPFGEY---SDEELWQALERVGLKEFVESLPGGLDTVveeggenLSVGQRQLLCLARALLR 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1820369315 425 RPEMLILDEPTSGVDPvARDMFWQLMVDLARQDRvTIFISTHFMNEAERCDRISLMHAGKVLASDTP 491
Cdd:cd03244 157 KSKILVLDEATASVDP-ETDALIQKTIREAFKDC-TVLTIAHRLDTIIDSDRILVLDKGRVVEFDSP 221
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
15-240 |
8.49e-19 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 90.99 E-value: 8.49e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 15 LENVGQQY-GATIALRDISLAIPARRMVGLIGPDGVGKSSLLSLIAGARAIEQGNVMVLGGDMRDV---HHRRdvcpKIA 90
Cdd:COG1132 342 FENVSFSYpGDRPVLKDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYDPTSGRILIDGVDIRDLtleSLRR----QIG 417
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 91 WMPQglgKN-LYHTlSVYENVdffarLFGHDKAERElRINELLQSTGLAPF-RDRPAG----------KLSGGMKQKLGL 158
Cdd:COG1132 418 VVPQ---DTfLFSG-TIRENI-----RYGRPDATDE-EVEEAAKAAQAHEFiEALPDGydtvvgergvNLSGGQRQRIAI 487
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 159 CCALIHDPQLLILDEPTTGVDPLSRAqfwELIDSIRQRQPEMSVLV-----ATaymeeAERFDWLVAMNAGEVLATGSAA 233
Cdd:COG1132 488 ARALLKDPPILILDEATSALDTETEA---LIQEALERLMKGRTTIViahrlST-----IRNADRILVLDDGRIVEQGTHE 559
|
....*..
gi 1820369315 234 ELKAQTG 240
Cdd:COG1132 560 ELLARGG 566
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
8-234 |
8.78e-19 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 89.24 E-value: 8.78e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 8 TSPPIALLENVGQQYGATIALRDISLAIPARRMVGLIGPDGVGKSSLLSLIAGARAIEQGNVMVLGGDMRDV-HHRRDVc 86
Cdd:PRK09452 10 SLSPLVELRGISKSFDGKEVISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLDGQDITHVpAENRHV- 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 87 pkiawmpqglgkN-------LYHTLSVYENVDFFARLFGHDKAERELRINELLQSTGLAPFRDRPAGKLSGGMKQKLGLC 159
Cdd:PRK09452 89 ------------NtvfqsyaLFPHMTVFENVAFGLRMQKTPAAEITPRVMEALRMVQLEEFAQRKPHQLSGGQQQRVAIA 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1820369315 160 CALIHDPQLLILDEPTTGVDPLSRAQFWELIDSIrQRQPEMSVLVATAYMEEAERF-DWLVAMNAGEVLATGSAAE 234
Cdd:PRK09452 157 RAVVNKPKVLLLDESLSALDYKLRKQMQNELKAL-QRKLGITFVFVTHDQEEALTMsDRIVVMRDGRIEQDGTPRE 231
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
15-195 |
1.05e-18 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 86.71 E-value: 1.05e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 15 LENVGQQYGATIALRDISLAIPARRMVGLIGPDGVGKSSLLSLIAGARAIEQGNVmvlggdmrdvhhRRDVCPKIAWMPQ 94
Cdd:PRK09544 7 LENVSVSFGQRRVLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVI------------KRNGKLRIGYVPQ 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 95 GLgkNLYHTLSVyeNVDFFARLFGHDKAERELRINELLQSTGLApfrDRPAGKLSGGMKQKLGLCCALIHDPQLLILDEP 174
Cdd:PRK09544 75 KL--YLDTTLPL--TVNRFLRLRPGTKKEDILPALKRVQAGHLI---DAPMQKLSGGETQRVLLARALLNRPQLLVLDEP 147
|
170 180
....*....|....*....|.
gi 1820369315 175 TTGVDPLSRAQFWELIDSIRQ 195
Cdd:PRK09544 148 TQGVDVNGQVALYDLIDQLRR 168
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
15-195 |
1.11e-18 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 86.22 E-value: 1.11e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 15 LENVGQQYGATIALRDISLAIPARRMVGLIGPDGVGKSSL---LSLIAGARAIEqgnvMVLGGDMRDVHHRRDvcPK-IA 90
Cdd:PRK11124 5 LNGINCFYGAHQALFDITLDCPQGETLVLLGPSGAGKSSLlrvLNLLEMPRSGT----LNIAGNHFDFSKTPS--DKaIR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 91 WMPQGLGK-----NLYHTLSVYEN-VDFFARLFGHDKAERELRINELLQSTGLAPFRDRPAGKLSGGMKQKLGLCCALIH 164
Cdd:PRK11124 79 ELRRNVGMvfqqyNLWPHLTVQQNlIEAPCRVLGLSKDQALARAEKLLERLRLKPYADRFPLHLSGGQQQRVAIARALMM 158
|
170 180 190
....*....|....*....|....*....|.
gi 1820369315 165 DPQLLILDEPTTGVDPLSRAQFWELIDSIRQ 195
Cdd:PRK11124 159 EPQVLLFDEPTAALDPEITAQIVSIIRELAE 189
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
24-235 |
1.11e-18 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 87.48 E-value: 1.11e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 24 ATIALRDISLAIPARRMVGLIGPDGVGKSSLLSLIAGARAIEQGNVMVlgGDM--RDVHHRRDVCP---KIAWMPQGLGK 98
Cdd:PRK13643 18 ASRALFDIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVTV--GDIvvSSTSKQKEIKPvrkKVGVVFQFPES 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 99 NLYHTlSVYENVDFFARLFGHDKAERELRINELLQSTGLAP-FRDRPAGKLSGGMKQKLGLCCALIHDPQLLILDEPTTG 177
Cdd:PRK13643 96 QLFEE-TVLKDVAFGPQNFGIPKEKAEKIAAEKLEMVGLADeFWEKSPFELSGGQMRRVAIAGILAMEPEVLVLDEPTAG 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1820369315 178 VDPLSRAQFWELIDSIRQRQpeMSVLVATAYMEE-AERFDWLVAMNAGEVLATGSAAEL 235
Cdd:PRK13643 175 LDPKARIEMMQLFESIHQSG--QTVVLVTHLMDDvADYADYVYLLEKGHIISCGTPSDV 231
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
277-511 |
1.45e-18 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 90.11 E-value: 1.45e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 277 IEARGLTMRFGNFVAVDHVNFRIARGEIFGFLGSNGCGKSTTMKMLTGLLPASEGEAWLFGQPVDPKDIATRQRVG-YM- 354
Cdd:PRK15439 12 LCARSISKQYSGVEVLKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIGGNPCARLTPAKAHQLGiYLv 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 355 SQAFSLYSELSVRQNLelharLFHIPDDEIAHR-----VAEMSERFMLtevkDALPADLPLGIRQRLSLAVAVIHRPEML 429
Cdd:PRK15439 92 PQEPLLFPNLSVKENI-----LFGLPKRQASMQkmkqlLAALGCQLDL----DSSAGSLEVADRQIVEILRGLMRDSRIL 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 430 ILDEPTSGVDPVARDMFWQLMVDLARQDRVTIFIStHFMNEA-ERCDRISLMHAGKVLAS---------DTPQALVEQRG 499
Cdd:PRK15439 163 ILDEPTASLTPAETERLFSRIRELLAQGVGIVFIS-HKLPEIrQLADRISVMRDGTIALSgktadlstdDIIQAITPAAR 241
|
250
....*....|..
gi 1820369315 500 AASLEEAFIAWL 511
Cdd:PRK15439 242 EKSLSASQKLWL 253
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
15-266 |
1.57e-18 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 86.58 E-value: 1.57e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 15 LENVGQQY-GATIALRDISLAIPARRMVGLIGPDGVGKSSLLSLIAGARAIEQGNVMVLG---GDMRDVHHRRDVCPKIA 90
Cdd:PRK13644 4 LENVSYSYpDGTPALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLVSGidtGDFSKLQGIRKLVGIVF 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 91 WMP--QGLGKnlyhtlSVYENVDFFARLFGHDKAERELRINELLQSTGLAPFRDRPAGKLSGGMKQKLGLCCALIHDPQL 168
Cdd:PRK13644 84 QNPetQFVGR------TVEEDLAFGPENLCLPPIEIRKRVDRALAEIGLEKYRHRSPKTLSGGQGQCVALAGILTMEPEC 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 169 LILDEPTTGVDPLSRAQFWELIDSIRQRQPemSVLVATAYMEEAERFDWLVAMNAGEVLATGSAAELKAQTGSQTLEQAF 248
Cdd:PRK13644 158 LIFDEVTSMLDPDSGIAVLERIKKLHEKGK--TIVYITHNLEELHDADRIIVMDRGKIVLEGEPENVLSDVSLQTLGLTP 235
|
250
....*....|....*...
gi 1820369315 249 IALLPEAQRQAHKTVVIP 266
Cdd:PRK13644 236 PSLIELAENLKMHGVVIP 253
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
281-499 |
1.80e-18 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 86.60 E-value: 1.80e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 281 GLTMRFGNFVAVDHVNFRIARGEIFGFLGSNGCGKSTTMKMLTGLLPASEGEAWLFGQPVDPKD---IATRQRVGYMSQA 357
Cdd:PRK13638 6 DLWFRYQDEPVLKGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLRPQKGAVLWQGKPLDYSKrglLALRQQVATVFQD 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 358 FS---LYSELSvrQNLELHARLFHIPDDEIAHRVAEM-----SERFMLTEVKdalpaDLPLGIRQRLSLAVAVIHRPEML 429
Cdd:PRK13638 86 PEqqiFYTDID--SDIAFSLRNLGVPEAEITRRVDEAltlvdAQHFRHQPIQ-----CLSHGQKKRVAIAGALVLQARYL 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1820369315 430 ILDEPTSGVDPVARDMFWQLMVDLARQDRvTIFISTHFMNEA-ERCDRISLMHAGKVLASDTP------QALVEQRG 499
Cdd:PRK13638 159 LLDEPTAGLDPAGRTQMIAIIRRIVAQGN-HVIISSHDIDLIyEISDAVYVLRQGQILTHGAPgevfacTEAMEQAG 234
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
293-500 |
1.91e-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: 85.67 E-value: 1.91e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 293 DHVNFRIARGEIFGFLGSNGCGKSTTMKMLTGLLPASEGEAWLFGQpvDPKDIA---TRQRVGYMSQAFSLYSeLSVRQN 369
Cdd:cd03249 20 KGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEILLDGV--DIRDLNlrwLRSQIGLVSQEPVLFD-GTIAEN 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 370 LELHARLFHIPDDEIAHRVAEMSERFML------TEVKDAlPADLPLGIRQRLSLAVAVIHRPEMLILDEPTSGVDpVAR 443
Cdd:cd03249 97 IRYGKPDATDEEVEEAAKKANIHDFIMSlpdgydTLVGER-GSQLSGGQKQRIAIARALLRNPKILLLDEATSALD-AES 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1820369315 444 DMFWQLMVDLARQDRVTIFIStHFMNEAERCDRISLMHAGKVLASDTPQALVEQRGA 500
Cdd:cd03249 175 EKLVQEALDRAMKGRTTIVIA-HRLSTIRNADLIAVLQNGQVVEQGTHDELMAQKGV 230
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
277-466 |
2.00e-18 |
|
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: 84.33 E-value: 2.00e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 277 IEARGLTMRFGNFVAVDHVNFRIARGEIFGFLGSNGCGKSTTMKMLTGLLPASEGEAWLFGQPVDPKDIATRQRVGYMSQ 356
Cdd:TIGR01189 1 LAARNLACSRGERMLFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRWNGTPLAEQRDEPHENILYLGH 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 357 AFSLYSELSVRQNLELHARLFHIPDDEIAHRVAEMSerfmLTEVKDALPADLPLGIRQRLSLAVAVIHRPEMLILDEPTS 436
Cdd:TIGR01189 81 LPGLKPELSALENLHFWAAIHGGAQRTIEDALAAVG----LTGFEDLPAAQLSAGQQRRLALARLWLSRRPLWILDEPTT 156
|
170 180 190
....*....|....*....|....*....|.
gi 1820369315 437 GVDPVARDMFWQLMVD-LARQDRVtiFISTH 466
Cdd:TIGR01189 157 ALDKAGVALLAGLLRAhLARGGIV--LLTTH 185
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
8-234 |
2.08e-18 |
|
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: 85.18 E-value: 2.08e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 8 TSPPIALLENVGQQYGA-----TIaLRDISLAIPARRMVGLIGPDGVGKSSLLSLIAGARAIEQGNVMVLGgdmRDVHH- 81
Cdd:COG4181 4 SSAPIIELRGLTKTVGTgagelTI-LKGISLEVEAGESVAIVGASGSGKSTLLGLLAGLDRPTSGTVRLAG---QDLFAl 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 82 --------RRDvcpKIAWMPQGLgkNLYHTLSVYENVDFFARLFGHDKAERELRinELLQSTGLAPFRD-RPAGkLSGGM 152
Cdd:COG4181 80 dedararlRAR---HVGFVFQSF--QLLPTLTALENVMLPLELAGRRDARARAR--ALLERVGLGHRLDhYPAQ-LSGGE 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 153 KQKLGLCCALIHDPQLLILDEPTTGVDPLSRAQFWELIDSIRQRQPEMSVLVaTAYMEEAERFDWLVAMNAGEVLATGSA 232
Cdd:COG4181 152 QQRVALARAFATEPAILFADEPTGNLDAATGEQIIDLLFELNRERGTTLVLV-THDPALAARCDRVLRLRAGRLVEDTAA 230
|
..
gi 1820369315 233 AE 234
Cdd:COG4181 231 TA 232
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
27-252 |
2.18e-18 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 86.09 E-value: 2.18e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 27 ALRDISLAIPARRMVGLIGPDGVGKSSLLSLIAGARAIEQGNVMVLGGDMRDVHHRRdvcpKIAWMPQGLGKNLYHTLSV 106
Cdd:PRK15056 22 ALRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKISILGQPTRQALQKN----LVAYVPQSEEVDWSFPVLV 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 107 yENVDFFARlFGH------DKAERELRINELLQSTGLAPFRDRPAGKLSGGMKQKLGLCCALIHDPQLLILDEPTTGVDP 180
Cdd:PRK15056 98 -EDVVMMGR-YGHmgwlrrAKKRDRQIVTAALARVDMVEFRHRQIGELSGGQKKRVFLARAIAQQGQVILLDEPFTGVDV 175
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1820369315 181 LSRAQFWELIDSIRQRQPEMsvLVATAYMEEAERFDWLVAMNAGEVLATGSAaelKAQTGSQTLEQAFIALL 252
Cdd:PRK15056 176 KTEARIISLLRELRDEGKTM--LVSTHNLGSVTEFCDYTVMVKGTVLASGPT---ETTFTAENLELAFSGVL 242
|
|
| thiQ |
TIGR01277 |
thiamine ABC transporter, ATP-binding protein; This model describes the energy-transducing ... |
296-485 |
2.37e-18 |
|
thiamine ABC transporter, ATP-binding protein; This model describes the energy-transducing ATPase subunit ThiQ of the ThiBPQ thiamine (and thiamine pyrophosphate) ABC transporter in several Proteobacteria. This protein is found so far only in Proteobacteria, and is found in complete genomes only if the ThiB and ThiP subunits are also found. [Transport and binding proteins, Other]
Pssm-ID: 130344 [Multi-domain] Cd Length: 213 Bit Score: 84.53 E-value: 2.37e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 296 NFRIARGEIFGFLGSNGCGKSTTMKMLTGLLPASEGEAWLFGQpvDPKDIATRQR-VGYMSQAFSLYSELSVRQNLELHA 374
Cdd:TIGR01277 18 DLNVADGEIVAIMGPSGAGKSTLLNLIAGFIEPASGSIKVNDQ--SHTGLAPYQRpVSMLFQENNLFAHLTVRQNIGLGL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 375 RLFHIPDDEIAHRVAEMSERFMLTEVKDALPADLPLGIRQRLSLAVAVIHRPEMLILDEPTSGVDPVARDMFWQLMVDLA 454
Cdd:TIGR01277 96 HPGLKLNAEQQEKVVDAAQQVGIADYLDRLPEQLSGGQRQRVALARCLVRPNPILLLDEPFSALDPLLREEMLALVKQLC 175
|
170 180 190
....*....|....*....|....*....|..
gi 1820369315 455 RQDRVTIFISTHFMNEAER-CDRISLMHAGKV 485
Cdd:TIGR01277 176 SERQRTLLMVTHHLSDARAiASQIAVVSQGKI 207
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
295-490 |
2.37e-18 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 85.25 E-value: 2.37e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 295 VNFRIARGEIFGFLGSNGCGKSTTMKMLTGLLPASEGEAWLFGQPVDPKDIATR-----QRVGYMSQAFSLYSELSVRQN 369
Cdd:PRK11629 28 VSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPMSKLSSAAKaelrnQKLGFIYQFHHLLPDFTALEN 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 370 LELHARLFHIPDDEIAHRVAEMSERFMLTEVKDALPADLPLGIRQRLSLAVAVIHRPEMLILDEPTSGVDPVARDMFWQL 449
Cdd:PRK11629 108 VAMPLLIGKKKPAEINSRALEMLAAVGLEHRANHRPSELSGGERQRVAIARALVNNPRLVLADEPTGNLDARNADSIFQL 187
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1820369315 450 MVDLARQDRVTIFISTHFMNEAERCDRISLMHAGKVLASDT 490
Cdd:PRK11629 188 LGELNRLQGTAFLVVTHDLQLAKRMSRQLEMRDGRLTAELS 228
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
295-484 |
2.39e-18 |
|
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This subfamily is also known as MRP (multidrug resistance-associated protein). Some of the MRP members have five additional transmembrane segments in their N-terminus, but the function of these additional membrane-spanning domains is not clear. The MRP was found in the multidrug-resisting lung cancer cell in which p-glycoprotein was not overexpressed. MRP exports glutathione by drug stimulation, as well as, certain substrates in conjugated forms with anions, such as glutathione, glucuronate, and sulfate.
Pssm-ID: 213217 [Multi-domain] Cd Length: 204 Bit Score: 84.44 E-value: 2.39e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 295 VNFRIARGEIFGFLGSNGCGKSTTMKMLTGLLPASEGEAWLFGqpvdpkdiatrqRVGYMSQAFSLYSElSVRQNLelha 374
Cdd:cd03250 24 INLEVPKGELVAIVGPVGSGKSSLLSALLGELEKLSGSVSVPG------------SIAYVSQEPWIQNG-TIRENI---- 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 375 rLFHIPDDEiahrvaemsERFmlTEVKDA--LPADL---PLGI---------------RQRLSLAVAVIHRPEMLILDEP 434
Cdd:cd03250 87 -LFGKPFDE---------ERY--EKVIKAcaLEPDLeilPDGDlteigekginlsggqKQRISLARAVYSDADIYLLDDP 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1820369315 435 TSGVDP-VARDMFWQLMVDLARQDRvTIFISTHFMNEAERCDRISLMHAGK 484
Cdd:cd03250 155 LSAVDAhVGRHIFENCILGLLLNNK-TRILVTHQLQLLPHADQIVVLDNGR 204
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
16-237 |
2.74e-18 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 85.33 E-value: 2.74e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 16 ENVGQQYGATIALRDISLAIPARRMVGLIGPDGVGKSSLLSLIAGARAIEQGNVMVLGGDMRDVHHRRDVCPKIAWMPQG 95
Cdd:PRK10895 7 KNLAKAYKGRRVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEDISLLPLHARARRGIGYLPQE 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 96 lgKNLYHTLSVYENVDFFARLFGHDKAE-RELRINELLQSTGLAPFRDRPAGKLSGGMKQKLGLCCALIHDPQLLILDEP 174
Cdd:PRK10895 87 --ASIFRRLSVYDNLMAVLQIRDDLSAEqREDRANELMEEFHIEHLRDSMGQSLSGGERRRVEIARALAANPKFILLDEP 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1820369315 175 TTGVDPLSRAQFWELIDSIRQRQpeMSVLVATAYMEEA----ERfDWLVAMnaGEVLATGSAAELKA 237
Cdd:PRK10895 165 FAGVDPISVIDIKRIIEHLRDSG--LGVLITDHNVRETlavcER-AYIVSQ--GHLIAHGTPTEILQ 226
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
28-258 |
3.30e-18 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 85.94 E-value: 3.30e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 28 LRDISLAIPARRMVGLIGPDGVGKSSLLSLIAGARAIEQGNVMVLGGDM--RDVHHRRDvcpKIAWMPQGlGKNLYHTLS 105
Cdd:PRK13650 23 LNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIIDGDLLteENVWDIRH---KIGMVFQN-PDNQFVGAT 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 106 VYENVDFFARLFGHDKAERELRINELLQSTGLAPFRDRPAGKLSGGMKQKLGLCCALIHDPQLLILDEPTTGVDPLSRAQ 185
Cdd:PRK13650 99 VEDDVAFGLENKGIPHEEMKERVNEALELVGMQDFKEREPARLSGGQKQRVAIAGAVAMRPKIIILDEATSMLDPEGRLE 178
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1820369315 186 FWELIDSIRQrQPEMSVLVATAYMEEAERFDWLVAMNAGEVLATGSAAELKAQTG---SQTLEQAFIALLPEAQRQ 258
Cdd:PRK13650 179 LIKTIKGIRD-DYQMTVISITHDLDEVALSDRVLVMKNGQVESTSTPRELFSRGNdllQLGLDIPFTTSLVQSLRQ 253
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
31-190 |
3.54e-18 |
|
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: 83.70 E-value: 3.54e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 31 ISLAIPARRMVGLIGPDGVGKSSLLSLIAGARAIEQGNVMVLGgdmRDVHHRRDVCPK-IAWMpqGLGKNLYHTLSVYEN 109
Cdd:cd03231 19 LSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNG---GPLDFQRDSIARgLLYL--GHAPGIKTTLSVLEN 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 110 VDFFARLFGHDKAErelrinELLQSTGLAPFRDRPAGKLSGGMKQKLGLCCALIHDPQLLILDEPTTGVDPLSRAQFWEL 189
Cdd:cd03231 94 LRFWHADHSDEQVE------EALARVGLNGFEDRPVAQLSAGQQRRVALARLLLSGRPLWILDEPTTALDKAGVARFAEA 167
|
.
gi 1820369315 190 I 190
Cdd:cd03231 168 M 168
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
5-235 |
4.62e-18 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 87.20 E-value: 4.62e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 5 PQDTSPPIA--LLE--NVGQQYGATIALRDISLAIPARRMVGLIGPDGVGKSSLLSLIAGARAIEQGNVMVLGGDMRDVH 80
Cdd:PRK11607 8 PQAKTRKALtpLLEirNLTKSFDGQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVDLSHVP 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 81 -HRRdvcpKIAWMPQGLGknLYHTLSVYENVDFFARLFGHDKAERELRINELLQSTGLAPFRDRPAGKLSGGMKQKLGLC 159
Cdd:PRK11607 88 pYQR----PINMMFQSYA--LFPHMTVEQNIAFGLKQDKLPKAEIASRVNEMLGLVHMQEFAKRKPHQLSGGQRQRVALA 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1820369315 160 CALIHDPQLLILDEPTTGVDPLSRAQF-WELIDsIRQRQPEMSVLVaTAYMEEAERFDWLVA-MNAGEVLATGSAAEL 235
Cdd:PRK11607 162 RSLAKRPKLLLLDEPMGALDKKLRDRMqLEVVD-ILERVGVTCVMV-THDQEEAMTMAGRIAiMNRGKFVQIGEPEEI 237
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
277-466 |
6.46e-18 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 83.00 E-value: 6.46e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 277 IEARGLTMRFGNFVAVDHVNFRIARGEIFGFLGSNGCGKSTTMKMLTGLLPASEGEAWLFGQPVDPKDIATrqRVGYMSQ 356
Cdd:PRK13539 3 LEGEDLACVRGGRVLFSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDGGDIDDPDVAE--ACHYLGH 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 357 AFSLYSELSVRQNLELHARLFHIPDdeiaHRVAEMSERFMLTEVKDaLPA-DLPLGIRQRLSLA-VAVIHRPeMLILDEP 434
Cdd:PRK13539 81 RNAMKPALTVAENLEFWAAFLGGEE----LDIAAALEAVGLAPLAH-LPFgYLSAGQKRRVALArLLVSNRP-IWILDEP 154
|
170 180 190
....*....|....*....|....*....|..
gi 1820369315 435 TSGVDPVARDMFWQLMVDLARQDRvTIFISTH 466
Cdd:PRK13539 155 TAALDAAAVALFAELIRAHLAQGG-IVIAATH 185
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
291-500 |
6.70e-18 |
|
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; MsbA is an essential ABC transporter, closely related to eukaryotic MDR proteins. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213218 [Multi-domain] Cd Length: 234 Bit Score: 83.82 E-value: 6.70e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 291 AVDHVNFRIARGEIFGFLGSNGCGKSTTMKMLTGLLPASEGEAWLFGqpVDPKDIAT---RQRVGYMSQAFSLYSElSVR 367
Cdd:cd03251 17 VLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDG--HDVRDYTLaslRRQIGLVSQDVFLFND-TVA 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 368 QNLELHARlfHIPDDEI--AHRVAEMSERFM-LTEVKDALPAD----LPLGIRQRLSLAVAVIHRPEMLILDEPTSGVDP 440
Cdd:cd03251 94 ENIAYGRP--GATREEVeeAARAANAHEFIMeLPEGYDTVIGErgvkLSGGQRQRIAIARALLKDPPILILDEATSALDT 171
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 441 VArDMFWQLMVDLARQDRVTIFIStHFMNEAERCDRISLMHAGKVLASDTPQALVEQRGA 500
Cdd:cd03251 172 ES-ERLVQAALERLMKNRTTFVIA-HRLSTIENADRIVVLEDGKIVERGTHEELLAQGGV 229
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
15-248 |
6.85e-18 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 84.45 E-value: 6.85e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 15 LENVGQQYGATIALRDISLAIPARRMVGLIGPDGVGKSSLLSLIAGARAIEQGNVMvLGGDMRDVHHRRDVCPKIAWMPQ 94
Cdd:PRK10575 14 LRNVSFRVPGRTLLHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEIL-LDAQPLESWSSKAFARKVAYLPQ 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 95 GLGKNlyHTLSVYENV-----DFFARLFGHDKAERElRINELLQSTGLAPFRDRPAGKLSGGMKQKLGLCCALIHDPQLL 169
Cdd:PRK10575 93 QLPAA--EGMTVRELVaigryPWHGALGRFGAADRE-KVEEAISLVGLKPLAHRLVDSLSGGERQRAWIAMLVAQDSRCL 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 170 ILDEPTTGVDPLSRAQFWELIDSIRQrQPEMSVLVATAYMEEAERF-DWLVAMNAGEVLATGSAAELKAqtgSQTLEQAF 248
Cdd:PRK10575 170 LLDEPTSALDIAHQVDVLALVHRLSQ-ERGLTVIAVLHDINMAARYcDYLVALRGGEMIAQGTPAELMR---GETLEQIY 245
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
274-495 |
7.21e-18 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 84.65 E-value: 7.21e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 274 EIAIEARG--LTMRFGNFVAVDHVNFRIARGEIFGFLGSNGCGKSTTMKMLTGLLPASEGEAWLFGQPVD---PKDIAtr 348
Cdd:PRK10253 3 ESVARLRGeqLTLGYGKYTVAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIQhyaSKEVA-- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 349 QRVGYMSQAFSLYSELSVrQNLELHARLFHIP-------DDEIAhrVAEMSERFMLTEVKDALPADLPLGIRQRLSLAVA 421
Cdd:PRK10253 81 RRIGLLAQNATTPGDITV-QELVARGRYPHQPlftrwrkEDEEA--VTKAMQATGITHLADQSVDTLSGGQRQRAWIAMV 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1820369315 422 VIHRPEMLILDEPTSGVDPVARDMFWQLMVDLARQDRVTIFISTHFMNEAER-CDRISLMHAGKVLASDTPQALV 495
Cdd:PRK10253 158 LAQETAIMLLDEPTTWLDISHQIDLLELLSELNREKGYTLAAVLHDLNQACRyASHLIALREGKIVAQGAPKEIV 232
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
290-507 |
7.68e-18 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 84.21 E-value: 7.68e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 290 VAVDH----VNFRIARGEIFGFLGSNGCGKSTTMKMLTGLLPaSEGEAWLFGQPVDPKDIAT--RQRvGYMSQAFSLYSE 363
Cdd:PRK03695 6 VAVSTrlgpLSAEVRAGEILHLVGPNGAGKSTLLARMAGLLP-GSGSIQFAGQPLEAWSAAElaRHR-AYLSQQQTPPFA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 364 LSVRQNLELHaRLFHIPDDEIAHRVAEMSERFMLTevkDALP---ADLPLGIRQRLSLAVAV--IHR---PE--MLILDE 433
Cdd:PRK03695 84 MPVFQYLTLH-QPDKTRTEAVASALNEVAEALGLD---DKLGrsvNQLSGGEWQRVRLAAVVlqVWPdinPAgqLLLLDE 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1820369315 434 PTSGVDPVARDMFWQLMVDLARQDRvTIFISTHFMNE-AERCDRISLMHAGKVLASDTPQALVEQRGaasLEEAF 507
Cdd:PRK03695 160 PMNSLDVAQQAALDRLLSELCQQGI-AVVMSSHDLNHtLRHADRVWLLKQGKLLASGRRDEVLTPEN---LAQVF 230
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
295-497 |
9.34e-18 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 84.41 E-value: 9.34e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 295 VNFRIARGEIFGFLGSNGCGKSTTMKMLTGLLPASEGEAWLFGQPVDP----KDI-ATRQRVGYM-----SQAFslysEL 364
Cdd:PRK13649 26 VNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDDTLITStsknKDIkQIRKKVGLVfqfpeSQLF----EE 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 365 SVRQNLELHARLFHIPDDEiAHRVAEmsERFMLTEVKDAL----PADLPLGIRQRLSLAVAVIHRPEMLILDEPTSGVDP 440
Cdd:PRK13649 102 TVLKDVAFGPQNFGVSQEE-AEALAR--EKLALVGISESLfeknPFELSGGQMRRVAIAGILAMEPKILVLDEPTAGLDP 178
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1820369315 441 VARDMFWQLMVDLaRQDRVTIFISTHFMNE-AERCDRISLMHAGKVLASDTPQALVEQ 497
Cdd:PRK13649 179 KGRKELMTLFKKL-HQSGMTIVLVTHLMDDvANYADFVYVLEKGKLVLSGKPKDIFQD 235
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
16-248 |
1.17e-17 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 83.67 E-value: 1.17e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 16 ENVGQQYGATIALRDISLAIPARRMVGLIGPDGVGKSSLLSLIAGARAIEQGNVMVLGgdmRDVHH--------RRDVcp 87
Cdd:PRK13548 6 RNLSVRLGGRTLLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLNG---RPLADwspaelarRRAV-- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 88 kiawMPQglgknlYHTLS----VYENVDFFARLFGHDKAERELRINELLQSTGLAPFRDRPAGKLSGGMKQKLGLCCALI 163
Cdd:PRK13548 81 ----LPQ------HSSLSfpftVEEVVAMGRAPHGLSRAEDDALVAAALAQVDLAHLAGRDYPQLSGGEQQRVQLARVLA 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 164 ------HDPQLLILDEPTTGVDPlsrAQFWELIDSIRQRQPE--MSVLV-------ATAYmeeAERfdwLVAMNAGEVLA 228
Cdd:PRK13548 151 qlwepdGPPRWLLLDEPTSALDL---AHQHHVLRLARQLAHErgLAVIVvlhdlnlAARY---ADR---IVLLHQGRLVA 221
|
250 260
....*....|....*....|.
gi 1820369315 229 TGSAAE-LKAqtgsQTLEQAF 248
Cdd:PRK13548 222 DGTPAEvLTP----ETLRRVY 238
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
275-492 |
1.29e-17 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 85.52 E-value: 1.29e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 275 IAIEARGLTMRFGNFVAVDHVNFRIARGEIFGFLGSNGCGKSTTMKMLTGLLPASEGEAWLFGQPVDpKDIATRQRVGYM 354
Cdd:PRK10851 1 MSIEIANIKKSFGRTQVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFHGTDVS-RLHARDRKVGFV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 355 SQAFSLYSELSVRQN-------LELHARlfhiPD-DEIAHRVAEMSERFMLTEVKDALPADLPLGIRQRLSLAVAVIHRP 426
Cdd:PRK10851 80 FQHYALFRHMTVFDNiafgltvLPRRER----PNaAAIKAKVTQLLEMVQLAHLADRYPAQLSGGQKQRVALARALAVEP 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1820369315 427 EMLILDEPTSGVDPVARDMFWQLMVDLARQDRVTIFISTHFMNEA-ERCDRISLMHAGKVLASDTPQ 492
Cdd:PRK10851 156 QILLLDEPFGALDAQVRKELRRWLRQLHEELKFTSVFVTHDQEEAmEVADRVVVMSQGNIEQAGTPD 222
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
295-487 |
1.35e-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: 87.11 E-value: 1.35e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 295 VNFRIARGEIFGFLGSNGCGKSTTMKMLTGLLPASEGEAWLFGQPVDPKDIATRQR-VGYMSQAFSLYsELSVRQNLelh 373
Cdd:COG4618 351 VSFSLEPGEVLGVIGPSGSGKSTLARLLVGVWPPTAGSVRLDGADLSQWDREELGRhIGYLPQDVELF-DGTIAENI--- 426
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 374 ARlFHIPDDEIAHRVA------EMSERFML---TEVKDAlpaDLPL--GIRQRLSLAVAVIHRPEMLILDEPTSGVDPVA 442
Cdd:COG4618 427 AR-FGDADPEKVVAAAklagvhEMILRLPDgydTRIGEG---GARLsgGQRQRIGLARALYGDPRLVVLDEPNSNLDDEG 502
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1820369315 443 RDMFWQLMVDLaRQDRVTIFISTHFMNEAERCDRISLMHAGKVLA 487
Cdd:COG4618 503 EAALAAAIRAL-KARGATVVVITHRPSLLAAVDKLLVLRDGRVQA 546
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
24-235 |
1.81e-17 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 83.92 E-value: 1.81e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 24 ATIALRDISLAIPARRMVGLIGPDGVGKSSLLSLIAGARAIEQGNVMVlgGDMRDVHHRRDvcpkiawmpqglgKNLY-- 101
Cdd:PRK13634 19 ERRALYDVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVTI--GERVITAGKKN-------------KKLKpl 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 102 ------------HTL---SVYENVDFFARLFGHDKAERELRINELLQSTGLAP-FRDRPAGKLSGGMKQKLGLCCALIHD 165
Cdd:PRK13634 84 rkkvgivfqfpeHQLfeeTVEKDICFGPMNFGVSEEDAKQKAREMIELVGLPEeLLARSPFELSGGQMRRVAIAGVLAME 163
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1820369315 166 PQLLILDEPTTGVDPLSRAQFWELIDSIRQRQPEMSVLVaTAYMEEAERF-DWLVAMNAGEVLATGSAAEL 235
Cdd:PRK13634 164 PEVLVLDEPTAGLDPKGRKEMMEMFYKLHKEKGLTTVLV-THSMEDAARYaDQIVVMHKGTVFLQGTPREI 233
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
1-175 |
1.83e-17 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 86.66 E-value: 1.83e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 1 MKLTPQDTSPPIAL-LENVGQQYGATIALRDISLAIPARRMVGLIGPDGVGKSSLLSLIAGARAIEQGNVmVLGGDMrdv 79
Cdd:COG0488 303 IRFPPPERLGKKVLeLEGLSKSYGDKTLLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPDSGTV-KLGETV--- 378
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 80 hhrrdvcpKIAWMPQGLgKNLYHTLSVYENVdffaRLFGHDKAERELRinELLQSTGLAPFR-DRPAGKLSGGMKQKLGL 158
Cdd:COG0488 379 --------KIGYFDQHQ-EELDPDKTVLDEL----RDGAPGGTEQEVR--GYLGRFLFSGDDaFKPVGVLSGGEKARLAL 443
|
170
....*....|....*..
gi 1820369315 159 CCALIHDPQLLILDEPT 175
Cdd:COG0488 444 AKLLLSPPNVLLLDEPT 460
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
15-485 |
2.48e-17 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 85.94 E-value: 2.48e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 15 LENVGQQYGATIALRDISLAIPARRMVGLIGPDGVGKSSLLSLIAGARAIEQGNVMVLGGDMRDVHHRRDVCPKIAWMPQ 94
Cdd:PRK10982 1 MSNISKSFPGVKALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEIDFKSSKEALENGISMVHQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 95 GLgkNLYHTLSVYENVdFFAR-----LF-GHDKAERELR--INELlqSTGLAPfRDRPAgKLSGGMKQKLGLCCALIHDP 166
Cdd:PRK10982 81 EL--NLVLQRSVMDNM-WLGRyptkgMFvDQDKMYRDTKaiFDEL--DIDIDP-RAKVA-TLSVSQMQMIEIAKAFSYNA 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 167 QLLILDEPTTGVDPLSRAQFWELIDSIRQRQpeMSVLVATAYMEEAERF-DWLVAMNAGEVLATGSAAELkaqtgsqTLE 245
Cdd:PRK10982 154 KIVIMDEPTSSLTEKEVNHLFTIIRKLKERG--CGIVYISHKMEEIFQLcDEITILRDGQWIATQPLAGL-------TMD 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 246 QaFIALL---PEAQRqahktvvIPPRDSREEEIAIEARGLTMRfgNFVAVDHVNFRIARGEIFGFLGSNGCGKSTTMKML 322
Cdd:PRK10982 225 K-IIAMMvgrSLTQR-------FPDKENKPGEVILEVRNLTSL--RQPSIRDVSFDLHKGEILGIAGLVGAKRTDIVETL 294
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 323 TGLLPASEGEAWLFGQPVDPKD----------IATRQRvgymsQAFSLYSELSVRQNlELHARLfhipdDEIAHRVAEMS 392
Cdd:PRK10982 295 FGIREKSAGTITLHGKKINNHNaneainhgfaLVTEER-----RSTGIYAYLDIGFN-SLISNI-----RNYKNKVGLLD 363
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 393 ERFMLTE---VKDALPADLPL----------GIRQRLSLAVAVIHRPEMLILDEPTSGVDPVARDMFWQLMVDLARQDRV 459
Cdd:PRK10982 364 NSRMKSDtqwVIDSMRVKTPGhrtqigslsgGNQQKVIIGRWLLTQPEILMLDEPTRGIDVGAKFEIYQLIAELAKKDKG 443
|
490 500
....*....|....*....|....*.
gi 1820369315 460 TIFISTHFMNEAERCDRISLMHAGKV 485
Cdd:PRK10982 444 IIIISSEMPELLGITDRILVMSNGLV 469
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
261-491 |
2.59e-17 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 84.13 E-value: 2.59e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 261 KTVVIPPRDSREEEIaIEARGLTMRFGN-----FVAVDHVNFRIARGEIFGFLGSNGCGKSTTMKMLTGLLPASEGEAWL 335
Cdd:PRK13631 7 KKKLKVPNPLSDDII-LRVKNLYCVFDEkqeneLVALNNISYTFEKNKIYFIIGNSGSGKSTLVTHFNGLIKSKYGTIQV 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 336 FGQPVDPKDIATRQRVGYMSQAFSLYSEL------------------SVRQNLELHARLFHIPDDEIAHRVAEMSERFML 397
Cdd:PRK13631 86 GDIYIGDKKNNHELITNPYSKKIKNFKELrrrvsmvfqfpeyqlfkdTIEKDIMFGPVALGVKKSEAKKLAKFYLNKMGL 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 398 TE-VKDALPADLPLGIRQRLSLAVAVIHRPEMLILDEPTSGVDPVARDMFWQLMVDLARQDRvTIFISTHFM-NEAERCD 475
Cdd:PRK13631 166 DDsYLERSPFGLSGGQKRRVAIAGILAIQPEILIFDEPTAGLDPKGEHEMMQLILDAKANNK-TVFVITHTMeHVLEVAD 244
|
250
....*....|....*.
gi 1820369315 476 RISLMHAGKVLASDTP 491
Cdd:PRK13631 245 EVIVMDKGKILKTGTP 260
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
270-494 |
2.87e-17 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 82.89 E-value: 2.87e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 270 SREEEIAIEARGLTMRFGNFVAVDHVNFRIARGEIFGFLGSNGCGKSTTMKMLTGLLPASEGEAWLFGQPVDP----KDI 345
Cdd:PRK11831 1 EQSVANLVDMRGVSFTRGNRCIFDNISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEILFDGENIPAmsrsRLY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 346 ATRQRVGYMSQAFSLYSELSVRQN----LELHARLfhipDDEIAHRVAEMS-ERFMLTEVKDALPADLPLGIRQRLSLAV 420
Cdd:PRK11831 81 TVRKRMSMLFQSGALFTDMNVFDNvaypLREHTQL----PAPLLHSTVMMKlEAVGLRGAAKLMPSELSGGMARRAALAR 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1820369315 421 AVIHRPEMLILDEPTSGVDPVARDMFWQLMVDLARQDRVTIFISTHFMNEA-ERCDRISLMHAGKVLASDTPQAL 494
Cdd:PRK11831 157 AIALEPDLIMFDEPFVGQDPITMGVLVKLISELNSALGVTCVVVSHDVPEVlSIADHAYIVADKKIVAHGSAQAL 231
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
277-484 |
3.34e-17 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 85.79 E-value: 3.34e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 277 IEARGLTMRFG--NFvAVDHVNFRIARGEIFGFLGSNGCGKSTTMKMLTGLLPASEGEAWLFGQPVDPKDI-ATRQRVGY 353
Cdd:PRK10522 323 LELRNVTFAYQdnGF-SVGPINLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKPVTAEQPeDYRKLFSA 401
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 354 MSQAFSLYSELSVRQNLElharlfhiPDDEIahrVAEMSERFML---TEVKDALPADLPL--GIRQRLSLAVAVIHRPEM 428
Cdd:PRK10522 402 VFTDFHLFDQLLGPEGKP--------ANPAL---VEKWLERLKMahkLELEDGRISNLKLskGQKKRLALLLALAEERDI 470
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1820369315 429 LILDEPTSGVDPVARDMFWQLMVDLARQDRVTIFISTHFMNEAERCDRISLMHAGK 484
Cdd:PRK10522 471 LLLDEWAADQDPHFRREFYQVLLPLLQEMGKTIFAISHDDHYFIHADRLLEMRNGQ 526
|
|
| PvdE |
COG4615 |
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ... |
243-494 |
3.71e-17 |
|
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: 86.01 E-value: 3.71e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 243 TLEQAFIAL---------LPEAQRQAHKTVVIPPRDSREEeiaIEARGLTMRF------GNFvAVDHVNFRIARGEIFGF 307
Cdd:COG4615 288 TLSRANVALrkieelelaLAAAEPAAADAAAPPAPADFQT---LELRGVTYRYpgedgdEGF-TLGPIDLTIRRGELVFI 363
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 308 LGSNGCGKSTTMKMLTGLLPASEGEAWLFGQPVDPKDIAT-RQRvgyMSQAFS---LYSELSVRQNLELHARLfhipDD- 382
Cdd:COG4615 364 VGGNGSGKSTLAKLLTGLYRPESGEILLDGQPVTADNREAyRQL---FSAVFSdfhLFDRLLGLDGEADPARA----REl 436
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 383 ----EIAHRVAEMSERFMLTevkdalpaDLPLGIRQRLSLAVAVI-HRPeMLILDEPTSGVDPVARDMFW-QLMVDLARQ 456
Cdd:COG4615 437 lerlELDHKVSVEDGRFSTT--------DLSQGQRKRLALLVALLeDRP-ILVFDEWAADQDPEFRRVFYtELLPELKAR 507
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 1820369315 457 DRvTIFISTH----FmneaERCDRISLMHAGKVLASDTPQAL 494
Cdd:COG4615 508 GK-TVIAISHddryF----DLADRVLKMDYGKLVELTGPAAL 544
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
291-518 |
3.79e-17 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 82.73 E-value: 3.79e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 291 AVDHVNFRIARGEIFGFLGSNGCGKSTTMKMLTGLLPASEGEAWLFGqpVDPKDIA----TRQRVGYMSQ-AFSLYSELS 365
Cdd:PRK13644 17 ALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLVSG--IDTGDFSklqgIRKLVGIVFQnPETQFVGRT 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 366 VRQNLELHARLFHIPDDEIAHRVAEMSERFMLTEVKDALPADLPLGIRQRLSLAVAVIHRPEMLILDEPTSGVDPVARDM 445
Cdd:PRK13644 95 VEEDLAFGPENLCLPPIEIRKRVDRALAEIGLEKYRHRSPKTLSGGQGQCVALAGILTMEPECLIFDEVTSMLDPDSGIA 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 446 FWQLMVDLARQDRVTIFIsTHFMNEAERCDRISLMHAGKV--------LASD--------TPQALVEQRGAASLEEAFIA 509
Cdd:PRK13644 175 VLERIKKLHEKGKTIVYI-THNLEELHDADRIIVMDRGKIvlegepenVLSDvslqtlglTPPSLIELAENLKMHGVVIP 253
|
....*....
gi 1820369315 510 WLKEAQPSS 518
Cdd:PRK13644 254 WENTSSPSS 262
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
218-466 |
4.07e-17 |
|
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: 85.49 E-value: 4.07e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 218 LVAMNAGEVLATGSAAELKAQTGSQTLEQafIALLPEAQRQAHKTVVIPPRDSREEEIAIEARGLTMRF-GNFVAVDHVN 296
Cdd:TIGR02868 278 LLPLAAFEAFAALPAAAQQLTRVRAAAER--IVEVLDAAGPVAEGSAPAAGAVGLGKPTLELRDLSAGYpGAPPVLDGVS 355
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 297 FRIARGEIFGFLGSNGCGKSTTMKMLTGLLPASEGEAWLFGQPVDPKDI-ATRQRVGYMSQAFSLYSElSVRQNLELHAR 375
Cdd:TIGR02868 356 LDLPPGERVAILGPSGSGKSTLLATLAGLLDPLQGEVTLDGVPVSSLDQdEVRRRVSVCAQDAHLFDT-TVRENLRLARP 434
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 376 lfHIPDDEiahrVAEMSERFMLTEVKDALP-----------ADLPLGIRQRLSLAVAVIHRPEMLILDEPTSGVDPVARD 444
Cdd:TIGR02868 435 --DATDEE----LWAALERVGLADWLRALPdgldtvlgeggARLSGGERQRLALARALLADAPILLLDEPTEHLDAETAD 508
|
250 260
....*....|....*....|....
gi 1820369315 445 mfwQLMVDL--ARQDRVTIFISTH 466
Cdd:TIGR02868 509 ---ELLEDLlaALSGRTVVLITHH 529
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
28-247 |
4.13e-17 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 82.36 E-value: 4.13e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 28 LRDISLAIPARRMVGLIGPDGVGKSSLLSLIAGARAIEQGNVMVLGGDMRdvHHRRDVCP---KIAWMPQGLGKNLYHTl 104
Cdd:PRK13638 17 LKGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLRPQKGAVLWQGKPLD--YSKRGLLAlrqQVATVFQDPEQQIFYT- 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 105 SVYENVDFFARLFGHDKAERELRINELLQSTGLAPFRDRPAGKLSGGMKQKLGLCCALIHDPQLLILDEPTTGVDPLSRA 184
Cdd:PRK13638 94 DIDSDIAFSLRNLGVPEAEITRRVDEALTLVDAQHFRHQPIQCLSHGQKKRVAIAGALVLQARYLLLDEPTAGLDPAGRT 173
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1820369315 185 QFWELIDSIRQRQPEmsVLVATAYMEEA-ERFDWLVAMNAGEVLATGSAAELKAQTgsQTLEQA 247
Cdd:PRK13638 174 QMIAIIRRIVAQGNH--VIISSHDIDLIyEISDAVYVLRQGQILTHGAPGEVFACT--EAMEQA 233
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
271-484 |
4.39e-17 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 81.30 E-value: 4.39e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 271 REEEIAIEARGLTMRFGNFVAVDHVNFRIARGEIFGFLGSNGCGKSTTMKMLTGLLPASEGEAWLFGQpvdpkDIAT--- 347
Cdd:PRK10247 2 QENSPLLQLQNVGYLAGDAKILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFEGE-----DISTlkp 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 348 ---RQRVGYMSQAFSLYSElSVRQNLELHARLFHIPDDEiaHRVAEMSERFMLTE-VKDALPADLPLGIRQRLSLAVAVI 423
Cdd:PRK10247 77 eiyRQQVSYCAQTPTLFGD-TVYDNLIFPWQIRNQQPDP--AIFLDDLERFALPDtILTKNIAELSGGEKQRISLIRNLQ 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1820369315 424 HRPEMLILDEPTSGVDPVARDMFWQLMVDLARQDRVTIFISTHFMNEAERCDR-ISLM-HAGK 484
Cdd:PRK10247 154 FMPKVLLLDEITSALDESNKHNVNEIIHRYVREQNIAVLWVTHDKDEINHADKvITLQpHAGE 216
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
238-499 |
4.81e-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: 4.81e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 238 QTGSQTLEQAFiALLPEAQRQAHKTVVIPPRDSReeeiaIEARGLTMRFG--NFVAVDHVNFRIARGEIFGFLGSNGCGK 315
Cdd:TIGR02203 298 QRGLAAAESLF-TLLDSPPEKDTGTRAIERARGD-----VEFRNVTFRYPgrDRPALDSISLVIEPGETVALVGRSGSGK 371
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 316 STTMKMLTGLLPASEGEAWLFGQPVDPKDIAT-RQRVGYMSQAFSLYSElSVRQNLElHARLFHIPDDEIaHRVAEMSEr 394
Cdd:TIGR02203 372 STLVNLIPRFYEPDSGQILLDGHDLADYTLASlRRQVALVSQDVVLFND-TIANNIA-YGRTEQADRAEI-ERALAAAY- 447
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 395 fmLTEVKDALP-----------ADLPLGIRQRLSLAVAVIHRPEMLILDEPTSGVDPVARDMFwQLMVDLARQDRVTIFI 463
Cdd:TIGR02203 448 --AQDFVDKLPlgldtpigengVLLSGGQRQRLAIARALLKDAPILILDEATSALDNESERLV-QAALERLMQGRTTLVI 524
|
250 260 270
....*....|....*....|....*....|....*.
gi 1820369315 464 StHFMNEAERCDRISLMHAGKVLASDTPQALVEQRG 499
Cdd:TIGR02203 525 A-HRLSTIEKADRIVVMDDGRIVERGTHNELLARNG 559
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
282-512 |
5.26e-17 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 81.94 E-value: 5.26e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 282 LTMRFGNFVAVDHVNFRIARGEIFGFLGSNGCGKSTTMKMLTGLLPASEGEAWLFGQPV-------------DPKDIAT- 347
Cdd:PRK10619 11 LHKRYGEHEVLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNGQTInlvrdkdgqlkvaDKNQLRLl 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 348 RQRVGYMSQAFSLYSELSVRQN-LELHARLFHIPDDEIAHRVAEMSERFMLTE-VKDALPADLPLGIRQRLSLAVAVIHR 425
Cdd:PRK10619 91 RTRLTMVFQHFNLWSHMTVLENvMEAPIQVLGLSKQEARERAVKYLAKVGIDErAQGKYPVHLSGGQQQRVSIARALAME 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 426 PEMLILDEPTSGVDPVARDMFWQLMVDLARQDRvTIFISTHFMNEAERC-DRISLMHAGKVLASDTPQALVEQRGAASLE 504
Cdd:PRK10619 171 PEVLLFDEPTSALDPELVGEVLRIMQQLAEEGK-TMVVVTHEMGFARHVsSHVIFLHQGKIEEEGAPEQLFGNPQSPRLQ 249
|
....*...
gi 1820369315 505 EAFIAWLK 512
Cdd:PRK10619 250 QFLKGSLK 257
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
274-498 |
5.96e-17 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 81.98 E-value: 5.96e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 274 EIAIEARGLTMRFGNFVAVDHVNFRIARGEIFGFLGSNGCGKSTTMKMLTGLL---PASEGEAWLFGQPVD-----PKDI 345
Cdd:PRK09984 2 QTIIRVEKLAKTFNQHQALHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGLItgdKSAGSHIELLGRTVQregrlARDI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 346 -ATRQRVGYMSQAFSLYSELSVRQNLELHA--------RLFHIPDDEIAHRVAEMSERFMLTEVKDALPADLPLGIRQRL 416
Cdd:PRK09984 82 rKSRANTGYIFQQFNLVNRLSVLENVLIGAlgstpfwrTCFSWFTREQKQRALQALTRVGMVHFAHQRVSTLSGGQQQRV 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 417 SLAVAVIHRPEMLILDEPTSGVDPVARDMFWQLMVDLARQDRVTIFISTHFMNEAER-CDRISLMHAGKVLASDTPQALV 495
Cdd:PRK09984 162 AIARALMQQAKVILADEPIASLDPESARIVMDTLRDINQNDGITVVVTLHQVDYALRyCERIVALRQGHVFYDGSSQQFD 241
|
...
gi 1820369315 496 EQR 498
Cdd:PRK09984 242 NER 244
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
11-439 |
6.00e-17 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 85.25 E-value: 6.00e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 11 PIALLENVGQQYGATiALRDISLAIPAR-RMVGLIGPDGVGKSSLLSLIAGA---------------RAIEQ--GNVM-- 70
Cdd:PRK13409 72 PEELEEEPVHRYGVN-GFKLYGLPIPKEgKVTGILGPNGIGKTTAVKILSGElipnlgdyeeepswdEVLKRfrGTELqn 150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 71 ----VLGGDMRDVHhrrdvcpkiawmpqglgKNLYhtlsvyenVDFFARLFghDKAEREL--------RINELLQSTGLA 138
Cdd:PRK13409 151 yfkkLYNGEIKVVH-----------------KPQY--------VDLIPKVF--KGKVRELlkkvdergKLDEVVERLGLE 203
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 139 PFRDRPAGKLSGGMKQKLGLCCALIHDPQLLILDEPTTGVDplsraqfwelidsIRQRqpemsVLVATAYMEEAER---- 214
Cdd:PRK13409 204 NILDRDISELSGGELQRVAIAAALLRDADFYFFDEPTSYLD-------------IRQR-----LNVARLIRELAEGkyvl 265
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 215 --------FDWL---VAMNAGEVLATGSAAELK-AQTGSQTLEQAFialLPEA----QRQAHKTVVIPPRDSREEEIAIE 278
Cdd:PRK13409 266 vvehdlavLDYLadnVHIAYGEPGAYGVVSKPKgVRVGINEYLKGY---LPEEnmriRPEPIEFEERPPRDESERETLVE 342
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 279 ARGLTMRFGNF-VAVDHVNfrIARGEIFGFLGSNGCGKSTTMKMLTGLLPASEGEawlfgqpVDPKdiatrQRVGYMSQA 357
Cdd:PRK13409 343 YPDLTKKLGDFsLEVEGGE--IYEGEVIGIVGPNGIGKTTFAKLLAGVLKPDEGE-------VDPE-----LKISYKPQY 408
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 358 FSLYSELSVRQNLELHARLFHIP--DDEIAhrvaemsERFMLTEVKDALPADLPLGIRQRLSLAVAVIHRPEMLILDEPT 435
Cdd:PRK13409 409 IKPDYDGTVEDLLRSITDDLGSSyyKSEII-------KPLQLERLLDKNVKDLSGGELQRVAIAACLSRDADLYLLDEPS 481
|
....
gi 1820369315 436 SGVD 439
Cdd:PRK13409 482 AHLD 485
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
28-239 |
6.37e-17 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 82.06 E-value: 6.37e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 28 LRDISLAIPARRMVGLIGPDGVGKSSLLSLIAGARAIEQGnVMVLGGDMRDVHHRRDVCPKIAWMPQGlGKNLYHTLSVY 107
Cdd:PRK13642 23 LNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEG-KVKIDGELLTAENVWNLRRKIGMVFQN-PDNQFVGATVE 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 108 ENVDFFARLFGHDKAERELRINELLQSTGLAPFRDRPAGKLSGGMKQKLGLCCALIHDPQLLILDEPTTGVDPLSRAQFW 187
Cdd:PRK13642 101 DDVAFGMENQGIPREEMIKRVDEALLAVNMLDFKTREPARLSGGQKQRVAVAGIIALRPEIIILDESTSMLDPTGRQEIM 180
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1820369315 188 ELIDSIRQRQpEMSVLVATAYMEEAERFDWLVAMNAGEVLATGSAAELKAQT 239
Cdd:PRK13642 181 RVIHEIKEKY-QLTVLSITHDLDEAASSDRILVMKAGEIIKEAAPSELFATS 231
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
31-259 |
7.23e-17 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 84.90 E-value: 7.23e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 31 ISLAIPARRMVGLIGPDGVGKSSLLSLIAGARAIeQGNVMVLGGDMRDV---HHRRdvcpKIAWmpqgLGKN--LYHTlS 105
Cdd:PRK11174 369 LNFTLPAGQRIALVGPSGAGKTSLLNALLGFLPY-QGSLKINGIELRELdpeSWRK----HLSW----VGQNpqLPHG-T 438
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 106 VYENVdffarLFGHDKAERElRINELLQSTGLAPFRDRP-----------AGKLSGGMKQKLGLCCALIHDPQLLILDEP 174
Cdd:PRK11174 439 LRDNV-----LLGNPDASDE-QLQQALENAWVSEFLPLLpqgldtpigdqAAGLSVGQAQRLALARALLQPCQLLLLDEP 512
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 175 TTGVDPLSRAQFWELIDSIRQRQpemSVLVATAYMEEAERFDWLVAMNAGEVLATGSAAELKAQTGsqtleqAFIALLpe 254
Cdd:PRK11174 513 TASLDAHSEQLVMQALNAASRRQ---TTLMVTHQLEDLAQWDQIWVMQDGQIVQQGDYAELSQAGG------LFATLL-- 581
|
....*
gi 1820369315 255 AQRQA 259
Cdd:PRK11174 582 AHRQE 586
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
16-235 |
7.51e-17 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 81.43 E-value: 7.51e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 16 ENVGQQYGATIALRDISLAIPARRMVGLIGPDGVGKSSLLSliAGARAIE-------QGNVMVLG-----GDMRDVHHRR 83
Cdd:PRK14267 8 VNLRVYYGSNHVIKGVDLKIPQNGVFALMGPSGCGKSTLLR--TFNRLLElneearvEGEVRLFGrniysPDVDPIEVRR 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 84 DVCPKIAWmpqglgKNLYHTLSVYENVDFFARLFGHDKAEREL--RINELLQSTGL-APFRDR---PAGKLSGGMKQKLG 157
Cdd:PRK14267 86 EVGMVFQY------PNPFPHLTIYDNVAIGVKLNGLVKSKKELdeRVEWALKKAALwDEVKDRlndYPSNLSGGQRQRLV 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1820369315 158 LCCALIHDPQLLILDEPTTGVDPLSRAQFWELIDSIRQrqpEMSVLVATAYMEEAERF-DWLVAMNAGEVLATGSAAEL 235
Cdd:PRK14267 160 IARALAMKPKILLMDEPTANIDPVGTAKIEELLFELKK---EYTIVLVTHSPAQAARVsDYVAFLYLGKLIEVGPTRKV 235
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
7-235 |
7.55e-17 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 81.72 E-value: 7.55e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 7 DTSPPIALLENVGQQY--GATIALRDISLAIPARRMVGLIGPDGVGKSSLLSLIAGARAIEQGNVMVlggdmrdvhhrRD 84
Cdd:PRK13648 2 EDKNSIIVFKNVSFQYqsDASFTLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIFY-----------NN 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 85 VCPKiawmPQGLGKNLYHTLSVYENVD--F------FARLFG-------HDKAERelRINELLQSTGLAPFRDRPAGKLS 149
Cdd:PRK13648 71 QAIT----DDNFEKLRKHIGIVFQNPDnqFvgsivkYDVAFGlenhavpYDEMHR--RVSEALKQVDMLERADYEPNALS 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 150 GGMKQKLGLCCALIHDPQLLILDEPTTGVDPLSRAQFWELIDSIRQRQpEMSVLVATAYMEEAERFDWLVAMNAGEVLAT 229
Cdd:PRK13648 145 GGQKQRVAIAGVLALNPSVIILDEATSMLDPDARQNLLDLVRKVKSEH-NITIISITHDLSEAMEADHVIVMNKGTVYKE 223
|
....*.
gi 1820369315 230 GSAAEL 235
Cdd:PRK13648 224 GTPTEI 229
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
16-240 |
7.74e-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: 80.73 E-value: 7.74e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 16 ENVGQQY-GATIALRDISLAIPARRMVGLIGPDGVGKSSLLSLIAGARAIEQGNVMVLGGDMRDVhhrrdvcpKIAWMPQ 94
Cdd:cd03254 6 ENVNFSYdEKKPVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGIDIRDI--------SRKSLRS 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 95 GLGKNLYHTL----SVYENVDffarlFGHDKAERElRINELLQSTGLAPFRDR----------PAGK-LSGGMKQKLGLC 159
Cdd:cd03254 78 MIGVVLQDTFlfsgTIMENIR-----LGRPNATDE-EVIEAAKEAGAHDFIMKlpngydtvlgENGGnLSQGERQLLAIA 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 160 CALIHDPQLLILDEPTTGVDPLSRAQFWELIDSIRQRQpemSVLVATAYMEEAERFDWLVAMNAGEVLATGSAAELKAQT 239
Cdd:cd03254 152 RAMLRDPKILILDEATSNIDTETEKLIQEALEKLMKGR---TSIIIAHRLSTIKNADKILVLDDGKIIEEGTHDELLAKK 228
|
.
gi 1820369315 240 G 240
Cdd:cd03254 229 G 229
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
302-496 |
9.37e-17 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 81.37 E-value: 9.37e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 302 GEIFGFLGSNGCGKSTTMKMLTGLLPASEGEAWLFGQPVDP-KDIATRQRVGYMSQAFSLYSELSVRQNLEL-----HAR 375
Cdd:PRK10575 37 GKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPLESwSSKAFARKVAYLPQQLPAAEGMTVRELVAIgrypwHGA 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 376 L--FHIPDDEiahRVAEMSERFMLTEVKDALPADLPLGIRQRLSLAVAVIHRPEMLILDEPTSGVDPVARDMFWQLMVDL 453
Cdd:PRK10575 117 LgrFGAADRE---KVEEAISLVGLKPLAHRLVDSLSGGERQRAWIAMLVAQDSRCLLLDEPTSALDIAHQVDVLALVHRL 193
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1820369315 454 ARQDRVTIFISTHFMNEAER-CDRISLMHAGKVLASDTPQALVE 496
Cdd:PRK10575 194 SQERGLTVIAVLHDINMAARyCDYLVALRGGEMIAQGTPAELMR 237
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
277-491 |
1.01e-16 |
|
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: 79.76 E-value: 1.01e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 277 IEARGLTMRFGNFV--AVDHVNFRIARGEIFGFLGSNGCGKSTTMKMLTGLLPASEGEAwlfgqPVDPKDIAT------R 348
Cdd:cd03369 7 IEVENLSVRYAPDLppVLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKI-----EIDGIDISTipledlR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 349 QRVGYMSQAFSLYSElSVRQNLElhaRLFHIPDDEI--AHRVAEMSErfmltevkdalpaDLPLGIRQRLSLAVAVIHRP 426
Cdd:cd03369 82 SSLTIIPQDPTLFSG-TIRSNLD---PFDEYSDEEIygALRVSEGGL-------------NLSQGQRQLLCLARALLKRP 144
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1820369315 427 EMLILDEPTSGVDpVARDMFWQLMVDLARQDrVTIFISTHFMNEAERCDRISLMHAGKVLASDTP 491
Cdd:cd03369 145 RVLVLDEATASID-YATDALIQKTIREEFTN-STILTIAHRLRTIIDYDKILVMDAGEVKEYDHP 207
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
27-251 |
1.06e-16 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 81.36 E-value: 1.06e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 27 ALRDISLAIPARRMVGLIGPDGVGKSSLLSLIAGARAIEQGNVMVlgGDMRdVHHR------RDVCPKIAWMPQGLGKNL 100
Cdd:PRK13646 22 AIHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTV--DDIT-ITHKtkdkyiRPVRKRIGMVFQFPESQL 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 101 YHTlSVYENVDFFARLFGHDKAERELRINELLQSTG-------LAPFrdrpagKLSGGMKQKLGLCCALIHDPQLLILDE 173
Cdd:PRK13646 99 FED-TVEREIIFGPKNFKMNLDEVKNYAHRLLMDLGfsrdvmsQSPF------QMSGGQMRKIAIVSILAMNPDIIVLDE 171
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1820369315 174 PTTGVDPLSRAQFWELIDSIRQRQPEMSVLVATAYMEEAERFDWLVAMNAGEVLATGSAAELKAQTgsQTLEQAFIAL 251
Cdd:PRK13646 172 PTAGLDPQSKRQVMRLLKSLQTDENKTIILVSHDMNEVARYADEVIVMKEGSIVSQTSPKELFKDK--KKLADWHIGL 247
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
10-248 |
1.11e-16 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 83.35 E-value: 1.11e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 10 PPIALlENVGQQYGATIALRDISLAIPARRMVGLIGPDGVGKSSLLSLIAGARAIEQGNVMVLGgdmRDVHHR--RDVCP 87
Cdd:PRK09536 2 PMIDV-SDLSVEFGDTTVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAG---DDVEALsaRAASR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 88 KIAWMPQGlgKNLYHTLSVYENVDF-----FARLFGHDKAERELrINELLQSTGLAPFRDRPAGKLSGGMKQKLGLCCAL 162
Cdd:PRK09536 78 RVASVPQD--TSLSFEFDVRQVVEMgrtphRSRFDTWTETDRAA-VERAMERTGVAQFADRPVTSLSGGERQRVLLARAL 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 163 IHDPQLLILDEPTTGVDPLSRAQFWELIDsiRQRQPEMSVLVATAYMEEAERF-DWLVAMNAGEVLATGSAAELKAqtgS 241
Cdd:PRK09536 155 AQATPVLLLDEPTASLDINHQVRTLELVR--RLVDDGKTAVAAIHDLDLAARYcDELVLLADGRVRAAGPPADVLT---A 229
|
....*..
gi 1820369315 242 QTLEQAF 248
Cdd:PRK09536 230 DTLRAAF 236
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
11-439 |
1.28e-16 |
|
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: 84.45 E-value: 1.28e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 11 PIALLENVGQQYGATiALRDISLAIPAR-RMVGLIGPDGVGKSSLLSLIAGARAIEQGNV-------MVL----GGDMRD 78
Cdd:COG1245 72 PEELEEDPVHRYGEN-GFRLYGLPVPKKgKVTGILGPNGIGKSTALKILSGELKPNLGDYdeepswdEVLkrfrGTELQD 150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 79 vhHRRDVCP---KIAWMPQglgknlyhtlsvyeNVDFFARLFghdKAE-REL--------RINELLQSTGLAPFRDRPAG 146
Cdd:COG1245 151 --YFKKLANgeiKVAHKPQ--------------YVDLIPKVF---KGTvRELlekvdergKLDELAEKLGLENILDRDIS 211
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 147 KLSGGMKQKLGLCCALIHDPQLLILDEPTTGVDplsraqfwelidsIRQRqpemsVLVATAYMEEAER------------ 214
Cdd:COG1245 212 ELSGGELQRVAIAAALLRDADFYFFDEPSSYLD-------------IYQR-----LNVARLIRELAEEgkyvlvvehdla 273
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 215 -FDWL---VAMNAGEVLATGSAAELK-AQTG-SQTLEqafiALLPEA----QRQAHKTVVIPPRDSREEEIAIEARGLTM 284
Cdd:COG1245 274 iLDYLadyVHILYGEPGVYGVVSKPKsVRVGiNQYLD----GYLPEEnvriRDEPIEFEVHAPRREKEEETLVEYPDLTK 349
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 285 RFGNF-VAVDHVNFRiaRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGEawlfgqpVDPKdiatrQRVGYMSQAFSLYSE 363
Cdd:COG1245 350 SYGGFsLEVEGGEIR--EGEVLGIVGPNGIGKTTFAKILAGVLKPDEGE-------VDED-----LKISYKPQYISPDYD 415
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 364 LSVRQNLElharlFHIPDD--------EIAHRVAemSERFMLTEVKdalpaDLPLGIRQRLSLAVAVIHRPEMLILDEPT 435
Cdd:COG1245 416 GTVEEFLR-----SANTDDfgssyyktEIIKPLG--LEKLLDKNVK-----DLSGGELQRVAIAACLSRDADLYLLDEPS 483
|
....
gi 1820369315 436 SGVD 439
Cdd:COG1245 484 AHLD 487
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
28-212 |
1.39e-16 |
|
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: 79.82 E-value: 1.39e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 28 LRDISLAIPARRMVGLIGPDGVGKSSLLSLIAGARAIEQGNVMVLGGDMRDVHHRRDVCPKiawmpqglGKNLYHTLSVY 107
Cdd:TIGR01184 1 LKGVNLTIQQGEFISLIGHSGCGKSTLLNLISGLAQPTSGGVILEGKQITEPGPDRMVVFQ--------NYSLLPWLTVR 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 108 ENVDFFARLFGHD--KAERELRINELLQSTGLAPFRDRPAGKLSGGMKQKLGLCCALIHDPQLLILDEPTTGVDPLSRAQ 185
Cdd:TIGR01184 73 ENIALAVDRVLPDlsKSERRAIVEEHIALVGLTEAADKRPGQLSGGMKQRVAIARALSIRPKVLLLDEPFGALDALTRGN 152
|
170 180
....*....|....*....|....*..
gi 1820369315 186 FWELIDSIRQrQPEMSVLVATAYMEEA 212
Cdd:TIGR01184 153 LQEELMQIWE-EHRVTVLMVTHDVDEA 178
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
291-499 |
1.47e-16 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 84.11 E-value: 1.47e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 291 AVDHVNFRIARGEIFGFLGSNGCGKSTTMKMLTGLLPASEGEAWLFGQPV-DPKDIATRQRVGYMSQAFSLYSElSVRQN 369
Cdd:PRK11160 355 VLKGLSLQIKAGEKVALLGRTGCGKSTLLQLLTRAWDPQQGEILLNGQPIaDYSEAALRQAISVVSQRVHLFSA-TLRDN 433
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 370 LELHArlfHIPDDEIAHRVAEMSERFMLTEVKDALPADLPLGIRQ-------RLSLAVAVIHRPEMLILDEPTSGVDPVA 442
Cdd:PRK11160 434 LLLAA---PNASDEALIEVLQQVGLEKLLEDDKGLNAWLGEGGRQlsggeqrRLGIARALLHDAPLLLLDEPTEGLDAET 510
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1820369315 443 RDMFWQLMVDLArQDRVTIFIsTHFMNEAERCDRISLMHAGKVLASDTPQALVEQRG 499
Cdd:PRK11160 511 ERQILELLAEHA-QNKTVLMI-THRLTGLEQFDRICVMDNGQIIEQGTHQELLAQQG 565
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
291-439 |
1.52e-16 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 82.06 E-value: 1.52e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 291 AVDHVNFRIARGEIFGFLGSNGCGKSTTMKMLTGLLPASEGE-AWLfGQPV---DPKDI-ATRQRVGYMSQ--AFSLYSE 363
Cdd:PRK15079 36 AVDGVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGEvAWL-GKDLlgmKDDEWrAVRSDIQMIFQdpLASLNPR 114
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1820369315 364 LSVRQNLELHARLFH--IPDDEIAHRVAEMSERF-MLTEVKDALPADLPLGIRQRLSLAVAVIHRPEMLILDEPTSGVD 439
Cdd:PRK15079 115 MTIGEIIAEPLRTYHpkLSRQEVKDRVKAMMLKVgLLPNLINRYPHEFSGGQCQRIGIARALILEPKLIICDEPVSALD 193
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
277-485 |
1.91e-16 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 80.13 E-value: 1.91e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 277 IEARGLTMRFGN-----FVAVDHVNFRIARGEIFGFLGSNGCGKSTTMKMLTGLLPASEGEAWLFGQPVdpkdiaTR--- 348
Cdd:COG1101 2 LELKNLSKTFNPgtvneKRALDGLNLTIEEGDFVTVIGSNGAGKSTLLNAIAGSLPPDSGSILIDGKDV------TKlpe 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 349 -QRVGYMSQAF-------SlySELSVRQNLEL-----HARLFHIpddeiahRV-AEMSERFmltevKDALpADLPLGI-- 412
Cdd:COG1101 76 yKRAKYIGRVFqdpmmgtA--PSMTIEENLALayrrgKRRGLRR-------GLtKKRRELF-----RELL-ATLGLGLen 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 413 -------------RQRLSLAVAVIHRPEMLILDEPTSGVDPVARDMFWQLMVDLARQDRVTIFISTHFMNEAERC-DRIS 478
Cdd:COG1101 141 rldtkvgllsggqRQALSLLMATLTKPKLLLLDEHTAALDPKTAALVLELTEKIVEENNLTTLMVTHNMEQALDYgNRLI 220
|
....*..
gi 1820369315 479 LMHAGKV 485
Cdd:COG1101 221 MMHEGRI 227
|
|
| nickel_nikE |
TIGR02769 |
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a ... |
28-253 |
2.06e-16 |
|
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: 80.23 E-value: 2.06e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 28 LRDISLAIPARRMVGLIGPDGVGKSSLLSLIAGARAIEQGNVMVLGGDMRDVHH------RRDV------CPKiAWMPQG 95
Cdd:TIGR02769 27 LTNVSLSIEEGETVGLLGRSGCGKSTLARLLLGLEKPAQGTVSFRGQDLYQLDRkqrrafRRDVqlvfqdSPS-AVNPRM 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 96 -----LGKNLYHTLSVyenvdffarlfghDKAERELRINELLQSTGLAP--FRDRPAgKLSGGMKQKLGLCCALIHDPQL 168
Cdd:TIGR02769 106 tvrqiIGEPLRHLTSL-------------DESEQKARIAELLDMVGLRSedADKLPR-QLSGGQLQRINIARALAVKPKL 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 169 LILDEPTTGVDPLSRAQFWELIDSIRQRQpEMSVLVATAYMEEAERF-DWLVAMNAGEVLATGSAAEL--KAQTGSQTLE 245
Cdd:TIGR02769 172 IVLDEAVSNLDMVLQAVILELLRKLQQAF-GTAYLFITHDLRLVQSFcQRVAVMDKGQIVEECDVAQLlsFKHPAGRNLQ 250
|
....*...
gi 1820369315 246 QAFIALLP 253
Cdd:TIGR02769 251 SAVLPEHP 258
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
15-240 |
2.43e-16 |
|
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: 79.45 E-value: 2.43e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 15 LENVGQQYGA--TIALRDISLAIPARRMVGLIGPDGVGKSSLLSLIAGARAIEQGNVMVLGGDMRDVhhrrdvcpKIAWM 92
Cdd:cd03252 3 FEHVRFRYKPdgPVILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGHDLALA--------DPAWL 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 93 PQGLG----KNLYHTLSVYENVDFfarlfGHDKAERElRINELLQSTGLAPF-RDRPAG----------KLSGGMKQKLG 157
Cdd:cd03252 75 RRQVGvvlqENVLFNRSIRDNIAL-----ADPGMSME-RVIEAAKLAGAHDFiSELPEGydtivgeqgaGLSGGQRQRIA 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 158 LCCALIHDPQLLILDEPTTGVDPLSRAQfweLIDSIRQRQPEMSVLVATAYMEEAERFDWLVAMNAGEVLATGSAAELKA 237
Cdd:cd03252 149 IARALIHNPRILIFDEATSALDYESEHA---IMRNMHDICAGRTVIIIAHRLSTVKNADRIIVMEKGRIVEQGSHDELLA 225
|
...
gi 1820369315 238 QTG 240
Cdd:cd03252 226 ENG 228
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
25-247 |
2.44e-16 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 80.12 E-value: 2.44e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 25 TIALRDISLAIPARRMVGLIGPDGVGKSSLLSLIAGARAIEQGNVMVLGGDMR-DVHHRRDVCPKIAWMPQGLGKNLYHT 103
Cdd:PRK13639 15 TEALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIKGEPIKyDKKSLLEVRKTVGIVFQNPDDQLFAP 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 104 lSVYENVDFFARLFGHDKAERELRINELLQSTGLAPFRDRPAGKLSGGMKQKLGLCCALIHDPQLLILDEPTTGVDPLSR 183
Cdd:PRK13639 95 -TVEEDVAFGPLNLGLSKEEVEKRVKEALKAVGMEGFENKPPHHLSGGQKKRVAIAGILAMKPEIIVLDEPTSGLDPMGA 173
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1820369315 184 AQFWELIDSIRQRQpeMSVLVATAYMEEAERF-DWLVAMNAGEVLATGSAAELKAQtgSQTLEQA 247
Cdd:PRK13639 174 SQIMKLLYDLNKEG--ITIIISTHDVDLVPVYaDKVYVMSDGKIIKEGTPKEVFSD--IETIRKA 234
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
14-235 |
2.48e-16 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 80.44 E-value: 2.48e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 14 LLENVGQQYGATI-----ALRDISLAIPARRMVGLIGPDGVGKSSLLSLIAGARAIEQGNVMV----LGGDMRDVHHRRD 84
Cdd:PRK13645 8 ILDNVSYTYAKKTpfefkALNNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGLIISETGQTIVgdyaIPANLKKIKEVKR 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 85 VCPKIAWMPQGLGKNLYHTlSVYENVDFFARLFGHDKAERELRINELLQSTGLA-PFRDRPAGKLSGGMKQKLGLCCALI 163
Cdd:PRK13645 88 LRKEIGLVFQFPEYQLFQE-TIEKDIAFGPVNLGENKQEAYKKVPELLKLVQLPeDYVKRSPFELSGGQKRRVALAGIIA 166
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1820369315 164 HDPQLLILDEPTTGVDPLSRAQFWELIDSIRQRQPEMSVLVaTAYMEEAERF-DWLVAMNAGEVLATGSAAEL 235
Cdd:PRK13645 167 MDGNTLVLDEPTGGLDPKGEEDFINLFERLNKEYKKRIIMV-THNMDQVLRIaDEVIVMHEGKVISIGSPFEI 238
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
15-229 |
2.87e-16 |
|
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: 77.08 E-value: 2.87e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 15 LENVGQQYGATIALRDISLAIPARRMVGLIGPDGVGKSSLLSLIAGARAIEQGNVMVLGgdmRDVHhrrdvcpkiawmpq 94
Cdd:cd03216 3 LRGITKRFGGVKALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVDG---KEVS-------------- 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 95 glgknlyhtlsvyenvdffarlFGHDKAERELRINELLQstglapfrdrpagkLSGGMKQKLGLCCALIHDPQLLILDEP 174
Cdd:cd03216 66 ----------------------FASPRDARRAGIAMVYQ--------------LSVGERQMVEIARALARNARLLILDEP 109
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1820369315 175 TTGVDPLSRAQFWELIDSIRQRqpEMSVLVATAYMEEAERF-DWLVAMNAGEVLAT 229
Cdd:cd03216 110 TAALTPAEVERLFKVIRRLRAQ--GVAVIFISHRLDEVFEIaDRVTVLRDGRVVGT 163
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
28-227 |
2.99e-16 |
|
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: 77.98 E-value: 2.99e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 28 LRDISLAIPARRMVGLIGPDGVGKSSLLSLIAGARAIEQ--GNVMVLGGDMRDVHHRRdvcpKIAWMPQGLgkNLYHTLS 105
Cdd:cd03213 25 LKNVSGKAKPGELTAIMGPSGAGKSTLLNALAGRRTGLGvsGEVLINGRPLDKRSFRK----IIGYVPQDD--ILHPTLT 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 106 VYENVDFFARLFGhdkaerelrinellqstglapfrdrpagkLSGGMKQKLGLCCALIHDPQLLILDEPTTGVDPLSRAQ 185
Cdd:cd03213 99 VRETLMFAAKLRG-----------------------------LSGGERKRVSIALELVSNPSLLFLDEPTSGLDSSSALQ 149
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1820369315 186 FWELIDSIRQR---------QPEMSVLvataymeeaERFDWLVAMNAGEVL 227
Cdd:cd03213 150 VMSLLRRLADTgrtiicsihQPSSEIF---------ELFDKLLLLSQGRVI 191
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
15-230 |
3.29e-16 |
|
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: 77.35 E-value: 3.29e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 15 LENVGQQYG--ATIALRDISLAIPARRMVGLIGPDGVGKSSLLSLIAGARAIEQGNVMVLGGDmrdvhhrrdvcpkiawm 92
Cdd:cd03247 3 INNVSFSYPeqEQQVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDGVP----------------- 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 93 PQGLGKNLYHTLSVyenVDFFARLFGhdkaerelriNELLQSTGLapfrdrpagKLSGGMKQKLGLCCALIHDPQLLILD 172
Cdd:cd03247 66 VSDLEKALSSLISV---LNQRPYLFD----------TTLRNNLGR---------RFSGGERQRLALARILLQDAPIVLLD 123
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1820369315 173 EPTTGVDPLSRAQFWELIDSIRQrqpEMSVLVATAYMEEAERFDWLVAMNAGEVLATG 230
Cdd:cd03247 124 EPTVGLDPITERQLLSLIFEVLK---DKTLIWITHHLTGIEHMDKILFLENGKIIMQG 178
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
16-235 |
3.37e-16 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 81.62 E-value: 3.37e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 16 ENVGQQYGATIALRDISLAIPARRMVGLIGPDGVGKSSLLSLIAGARAIEQGNVMVLGGDM---RDVHHRRDVCPKIAWM 92
Cdd:PRK10070 32 EQILEKTGLSLGVKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIakiSDAELREVRRKKIAMV 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 93 PQGLGknLYHTLSVYENVDFFARLFGHDKAERELRINELLQSTGLAPFRDRPAGKLSGGMKQKLGLCCALIHDPQLLILD 172
Cdd:PRK10070 112 FQSFA--LMPHMTVLDNTAFGMELAGINAEERREKALDALRQVGLENYAHSYPDELSGGMRQRVGLARALAINPDILLMD 189
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1820369315 173 EPTTGVDPLSRAQFWELIDSIrQRQPEMSVLVATAYMEEAERF-DWLVAMNAGEVLATGSAAEL 235
Cdd:PRK10070 190 EAFSALDPLIRTEMQDELVKL-QAKHQRTIVFISHDLDEAMRIgDRIAIMQNGEVVQVGTPDEI 252
|
|
| BtuD |
COG4138 |
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ... |
28-258 |
4.29e-16 |
|
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism];
Pssm-ID: 443313 [Multi-domain] Cd Length: 248 Bit Score: 78.73 E-value: 4.29e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 28 LRDISLAIPARRMVGLIGPDGVGKSSLLSLIAGARAiEQGNVMVLGGDMRDV------HHRrdvcpkiAWMPQglgknly 101
Cdd:COG4138 12 LGPISAQVNAGELIHLIGPNGAGKSTLLARMAGLLP-GQGEILLNGRPLSDWsaaelaRHR-------AYLSQ------- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 102 HTLS-----VYENVDFFARLfGHDKAERELRINELLQSTGLAPFRDRPAGKLSGGMKQKLGLCCAL--IH-----DPQLL 169
Cdd:COG4138 77 QQSPpfampVFQYLALHQPA-GASSEAVEQLLAQLAEALGLEDKLSRPLTQLSGGEWQRVRLAAVLlqVWptinpEGQLL 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 170 ILDEPTTGVDPLSRAQFWELIDSIRQRQpeMSVLVATAYMEEAERF-D--WLvaMNAGEVLATGSAAE-LKAQTGSQTLE 245
Cdd:COG4138 156 LLDEPMNSLDVAQQAALDRLLRELCQQG--ITVVMSSHDLNHTLRHaDrvWL--LKQGKLVASGETAEvMTPENLSEVFG 231
|
250
....*....|...
gi 1820369315 246 QAFIALLPEAQRQ 258
Cdd:COG4138 232 VKFRRLEVEGHRW 244
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
287-439 |
4.60e-16 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 80.66 E-value: 4.60e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 287 GNFVAVDHVNFRIARGEIFGFLGSNGCGKSTTMKMLTGLLPASEGEAWLFGQPV---DPK--DIAtrqrvgyMS-QAFSL 360
Cdd:PRK11650 15 GKTQVIKGIDLDVADGEFIVLVGPSGCGKSTLLRMVAGLERITSGEIWIGGRVVnelEPAdrDIA-------MVfQNYAL 87
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1820369315 361 YSELSVRQNLELHARLFHIPDDEIAHRVAEMSERFMLTEVKDALPADLPLGIRQRLSLAVAVIHRPEMLILDEPTSGVD 439
Cdd:PRK11650 88 YPHMSVRENMAYGLKIRGMPKAEIEERVAEAARILELEPLLDRKPRELSGGQRQRVAMGRAIVREPAVFLFDEPLSNLD 166
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
289-491 |
5.18e-16 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 79.67 E-value: 5.18e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 289 FVAVDHVNFRIARGEIFGFLGSNGCGKSTTMKMLTGLLPASEGEAWL--FGQPVDPKDIAT----RQRVGYMSQ--AFSL 360
Cdd:PRK13645 24 FKALNNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGLIISETGQTIVgdYAIPANLKKIKEvkrlRKEIGLVFQfpEYQL 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 361 YSElSVRQNLELHARLFHIPDDEIAHRVAEMSERFMLTE--VKDAlPADLPLGIRQRLSLAVAVIHRPEMLILDEPTSGV 438
Cdd:PRK13645 104 FQE-TIEKDIAFGPVNLGENKQEAYKKVPELLKLVQLPEdyVKRS-PFELSGGQKRRVALAGIIAMDGNTLVLDEPTGGL 181
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1820369315 439 DPVARDMFWQLMVDLARQDRVTIFISTHFMNEAER-CDRISLMHAGKVLASDTP 491
Cdd:PRK13645 182 DPKGEEDFINLFERLNKEYKKRIIMVTHNMDQVLRiADEVIVMHEGKVISIGSP 235
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
289-497 |
5.39e-16 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 79.44 E-value: 5.39e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 289 FVAVDHVNFRIARGEIFGFLGSNGCGKSTTMKMLTGLLPASEGEAWLFGQPV----DPKDIAT-RQRVGYM-----SQAF 358
Cdd:PRK13646 20 HQAIHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVDDITIthktKDKYIRPvRKRIGMVfqfpeSQLF 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 359 slysELSVRQNLELHARLFHIPDDEIAHRVAEMSERFMLT-EVKDALPADLPLGIRQRLSLAVAVIHRPEMLILDEPTSG 437
Cdd:PRK13646 100 ----EDTVEREIIFGPKNFKMNLDEVKNYAHRLLMDLGFSrDVMSQSPFQMSGGQMRKIAIVSILAMNPDIIVLDEPTAG 175
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1820369315 438 VDPVARDMFWQLMVDLARQDRVTIFISTHFMNE-AERCDRISLMHAGKVLASDTPQALVEQ 497
Cdd:PRK13646 176 LDPQSKRQVMRLLKSLQTDENKTIILVSHDMNEvARYADEVIVMKEGSIVSQTSPKELFKD 236
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
277-496 |
5.90e-16 |
|
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in methanogenesis, methyl coenzyme M reductase, contains alpha, beta, and gamma chains. In older literature, the complex of alpha, beta, and gamma chains was termed component C, while this single chain protein was termed methyl coenzyme M reductase system component A2. [Energy metabolism, Methanogenesis]
Pssm-ID: 132313 [Multi-domain] Cd Length: 520 Bit Score: 81.77 E-value: 5.90e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 277 IEARGLTMRFGNFVAVDHVNFRIARGEIFGFLGSNGCGKSTTMKMLTGL--LPASEGE-----------AWL-------- 335
Cdd:TIGR03269 1 IEVKNLTKKFDGKEVLKNISFTIEEGEVLGILGRSGAGKSVLMHVLRGMdqYEPTSGRiiyhvalcekcGYVerpskvge 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 336 ---------------FGQPVDPKDIATRQRVGYMSQ-AFSLYSELSVRQNLELHARLFHIPDDEIAHRVAEMSERFMLTE 399
Cdd:TIGR03269 81 pcpvcggtlepeevdFWNLSDKLRRRIRKRIAIMLQrTFALYGDDTVLDNVLEALEEIGYEGKEAVGRAVDLIEMVQLSH 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 400 VKDALPADLPLGIRQRLSLAVAVIHRPEMLILDEPTSGVDPVARDMFWQLMVDLARQDRVTIFISTHFMNEAER-CDRIS 478
Cdd:TIGR03269 161 RITHIARDLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALEEAVKASGISMVLTSHWPEVIEDlSDKAI 240
|
250
....*....|....*...
gi 1820369315 479 LMHAGKVLASDTPQALVE 496
Cdd:TIGR03269 241 WLENGEIKEEGTPDEVVA 258
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
291-497 |
6.31e-16 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 79.39 E-value: 6.31e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 291 AVDHVNFRIARGEIFGFLGSNGCGKSTTMKMLTGLLPASEGEA----WLFGQPVDPKDIA-TRQRVGYMSQ--AFSLYSE 363
Cdd:PRK13643 21 ALFDIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVtvgdIVVSSTSKQKEIKpVRKKVGVVFQfpESQLFEE 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 364 lSVRQNLELHARLFHIPDDEIAHRVAEMSERFMLT-EVKDALPADLPLGIRQRLSLAVAVIHRPEMLILDEPTSGVDPVA 442
Cdd:PRK13643 101 -TVLKDVAFGPQNFGIPKEKAEKIAAEKLEMVGLAdEFWEKSPFELSGGQMRRVAIAGILAMEPEVLVLDEPTAGLDPKA 179
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1820369315 443 RDMFWQLMVDLaRQDRVTIFISTHFMNE-AERCDRISLMHAGKVLASDTPQALVEQ 497
Cdd:PRK13643 180 RIEMMQLFESI-HQSGQTVVLVTHLMDDvADYADYVYLLEKGHIISCGTPSDVFQE 234
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
15-195 |
6.74e-16 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 78.13 E-value: 6.74e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 15 LENVGQQYGATIALRDISLAIPARRMVGLIGPDGVGKSSLLSLIAGARAIEQGNVMVLGGDM---RDVHHRRdvcpkIAW 91
Cdd:COG4161 5 LKNINCFYGSHQALFDINLECPSGETLVLLGPSGAGKSSLLRVLNLLETPDSGQLNIAGHQFdfsQKPSEKA-----IRL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 92 MPQGLGK-----NLYHTLSVYEN-VDFFARLFGHDKAERELRINELLQSTGLAPFRDRPAGKLSGGMKQKLGLCCALIHD 165
Cdd:COG4161 80 LRQKVGMvfqqyNLWPHLTVMENlIEAPCKVLGLSKEQAREKAMKLLARLRLTDKADRFPLHLSGGQQQRVAIARALMME 159
|
170 180 190
....*....|....*....|....*....|
gi 1820369315 166 PQLLILDEPTTGVDPLSRAQFWELIDSIRQ 195
Cdd:COG4161 160 PQVLLFDEPTAALDPEITAQVVEIIRELSQ 189
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
276-471 |
8.39e-16 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 78.20 E-value: 8.39e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 276 AIEARGLTMRFGNFVAVDHVNFRIARGEIFGFLGSNGCGKSTTMKMLTGLLPASEGEAWLFGQPVDPKDiATRqrvGYMS 355
Cdd:PRK11248 1 MLQISHLYADYGGKPALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDGKPVEGPG-AER---GVVF 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 356 QAFSLYSELSVRQNLELHARLFHIPDDEIAHRVAEMSERFMLTEVKDALPADLPLGIRQRLSLAVAVIHRPEMLILDEPT 435
Cdd:PRK11248 77 QNEGLLPWRNVQDNVAFGLQLAGVEKMQRLEIAHQMLKKVGLEGAEKRYIWQLSGGQRQRVGIARALAANPQLLLLDEPF 156
|
170 180 190
....*....|....*....|....*....|....*.
gi 1820369315 436 SGVDPVARDMFWQLMVDLARQDRVTIFISTHFMNEA 471
Cdd:PRK11248 157 GALDAFTREQMQTLLLKLWQETGKQVLLITHDIEEA 192
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
15-226 |
9.17e-16 |
|
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: 76.10 E-value: 9.17e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 15 LENVGQQYGATIA--LRDISLAIPARRMVGLIGPDGVGKSSLLSLIAGARAIEQGNVMVLGGDMRDVhHRRDVCPKIAWM 92
Cdd:cd03246 3 VENVSFRYPGAEPpvLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDGADISQW-DPNELGDHVGYL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 93 PQGLgkNLYhTLSVYENVdffarlfghdkaerelrinellqstglapfrdrpagkLSGGMKQKLGLCCALIHDPQLLILD 172
Cdd:cd03246 82 PQDD--ELF-SGSIAENI-------------------------------------LSGGQRQRLGLARALYGNPRILVLD 121
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1820369315 173 EPTTGVDPLSRAQFWELIDSIRQRQpeMSVLVATAYMEEAERFDWLVAMNAGEV 226
Cdd:cd03246 122 EPNSHLDVEGERALNQAIAALKAAG--ATRIVIAHRPETLASADRILVLEDGRV 173
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
302-496 |
1.89e-15 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 80.48 E-value: 1.89e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 302 GEIFGFLGSNGCGKSTTMKMLTGLLPAS---EGEAWLFGQPVDPKDIatRQRVGYMSQAFSLYSELSVRQNLELHARLF- 377
Cdd:TIGR00955 51 GELLAVMGSSGAGKTTLMNALAFRSPKGvkgSGSVLLNGMPIDAKEM--RAISAYVQQDDLFIPTLTVREHLMFQAHLRm 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 378 --HIPDDEIAHRVAEMSERFMLTEVKDALPAD------LPLGIRQRLSLAVAVIHRPEMLILDEPTSGVDPVARDMFWQL 449
Cdd:TIGR00955 129 prRVTKKEKRERVDEVLQALGLRKCANTRIGVpgrvkgLSGGERKRLAFASELLTDPPLLFCDEPTSGLDSFMAYSVVQV 208
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1820369315 450 MVDLArQDRVTIFISTH------FmneaERCDRISLMHAGKVLASDTPQALVE 496
Cdd:TIGR00955 209 LKGLA-QKGKTIICTIHqpsselF----ELFDKIILMAEGRVAYLGSPDQAVP 256
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
7-235 |
1.90e-15 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 77.34 E-value: 1.90e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 7 DTSPPIALLENVGQQYGA--TIALRDISLAIPARRMVGLIGPDGVGKSSLLSLIAGARAIEQGNVMVLGGDMRDvHHRRD 84
Cdd:PRK13632 2 KNKSVMIKVENVSFSYPNseNNALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIDGITISK-ENLKE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 85 VCPKIAWMPQGlGKNLYHTLSVYENVDFFARLFGHDKAERELRINELLQSTGLAPFRDRPAGKLSGGMKQKLGLCCALIH 164
Cdd:PRK13632 81 IRKKIGIIFQN-PDNQFIGATVEDDIAFGLENKKVPPKKMKDIIDDLAKKVGMEDYLDKEPQNLSGGQKQRVAIASVLAL 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1820369315 165 DPQLLILDEPTTGVDPLSRAQFWELIDSIRQrQPEMSVLVATAYMEEAERFDWLVAMNAGEVLATGSAAEL 235
Cdd:PRK13632 160 NPEIIIFDESTSMLDPKGKREIKKIMVDLRK-TRKKTLISITHDMDEAILADKVIVFSEGKLIAQGKPKEI 229
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
28-262 |
1.94e-15 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 77.42 E-value: 1.94e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 28 LRDISLAIPARRMVGLIGPDGVGKSSLLSLIAGARAIEQGNVMVLGGDM------------RD-----------VHHRRD 84
Cdd:PRK10419 28 LNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWRGEPLaklnraqrkafrRDiqmvfqdsisaVNPRKT 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 85 VCPKIAwmpqglgKNLYHTLSVyenvdffarlfghDKAERELRINELLQSTGLAP-FRDRPAGKLSGGMKQKLGLCCALI 163
Cdd:PRK10419 108 VREIIR-------EPLRHLLSL-------------DKAERLARASEMLRAVDLDDsVLDKRPPQLSGGQLQRVCLARALA 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 164 HDPQLLILDEPTTGVDPLSRAQFWELIDSIRQrQPEMSVLVATAYMEEAERFDWLVA-MNAGEVLATGSAAELKAQT--G 240
Cdd:PRK10419 168 VEPKLLILDEAVSNLDLVLQAGVIRLLKKLQQ-QFGTACLFITHDLRLVERFCQRVMvMDNGQIVETQPVGDKLTFSspA 246
|
250 260
....*....|....*....|..
gi 1820369315 241 SQTLEQAFIALLPEAQRQAHKT 262
Cdd:PRK10419 247 GRVLQNAVLPAFPVRRRTTEKV 268
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
15-235 |
2.35e-15 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 77.48 E-value: 2.35e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 15 LENVGQQYGATI-----ALRDISLAIPARRMVGLIGPDGVGKSSLLSLIAGARAIEQGNVMVLGGDMRDVHHRRDVCP-- 87
Cdd:PRK13649 5 LQNVSYTYQAGTpfegrALFDVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDDTLITSTSKNKDIKQir 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 88 -KIAWMPQGLGKNLYHTlSVYENVDFFARLFGHDKAERELRINELLQSTGLAP-FRDRPAGKLSGGMKQKLGLCCALIHD 165
Cdd:PRK13649 85 kKVGLVFQFPESQLFEE-TVLKDVAFGPQNFGVSQEEAEALAREKLALVGISEsLFEKNPFELSGGQMRRVAIAGILAME 163
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1820369315 166 PQLLILDEPTTGVDPLSRAQFWELIDSIRQRQpeMSVLVATAYMEE-AERFDWLVAMNAGEVLATGSAAEL 235
Cdd:PRK13649 164 PKILVLDEPTAGLDPKGRKELMTLFKKLHQSG--MTIVLVTHLMDDvANYADFVYVLEKGKLVLSGKPKDI 232
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
273-495 |
2.48e-15 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 76.46 E-value: 2.48e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 273 EEIAIEARGLTMRFGNFVAVDHVNFRIARGEIFGFLGSNGCGKSTTMKMLTGLLPASEGEAWLfgqpvDPKDIATRQRVG 352
Cdd:PRK11614 2 EKVMLSFDKVSAHYGKIQALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVF-----DGKDITDWQTAK 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 353 YMSQAFSL-------YSELSVRQNLELHArlFHIPDDEIAHRVAEMSERF-MLTEVKDALPADLPLGIRQRLSLAVAVIH 424
Cdd:PRK11614 77 IMREAVAIvpegrrvFSRMTVEENLAMGG--FFAERDQFQERIKWVYELFpRLHERRIQRAGTMSGGEQQMLAIGRALMS 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1820369315 425 RPEMLILDEPTSGVDPVARDMFWQLMVDLaRQDRVTIFISTHFMNEAER-CDRISLMHAGKVLASDTPQALV 495
Cdd:PRK11614 155 QPRLLLLDEPSLGLAPIIIQQIFDTIEQL-REQGMTIFLVEQNANQALKlADRGYVLENGHVVLEDTGDALL 225
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
27-235 |
2.73e-15 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 77.15 E-value: 2.73e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 27 ALRDISLAIPARRMVGLIGPDGVGKSSLLSLIAGARAIEQGN---VMVLGGDM--RDVHHRRDvcpKIAWMPQGlGKNLY 101
Cdd:PRK13640 22 ALNDISFSIPRGSWTALIGHNGSGKSTISKLINGLLLPDDNPnskITVDGITLtaKTVWDIRE---KVGIVFQN-PDNQF 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 102 HTLSVYENVDFFARLFGHDKAERELRINELLQSTGLAPFRDRPAGKLSGGMKQKLGLCCALIHDPQLLILDEPTTGVDPL 181
Cdd:PRK13640 98 VGATVGDDVAFGLENRAVPRPEMIKIVRDVLADVGMLDYIDSEPANLSGGQKQRVAIAGILAVEPKIIILDESTSMLDPA 177
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1820369315 182 SRAQFWELIDSIrQRQPEMSVLVATAYMEEAERFDWLVAMNAGEVLATGSAAEL 235
Cdd:PRK13640 178 GKEQILKLIRKL-KKKNNLTVISITHDIDEANMADQVLVLDDGKLLAQGSPVEI 230
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
276-512 |
2.93e-15 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 76.85 E-value: 2.93e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 276 AIEARGLTMRFGN-FVAVDHVNFRIARGEIFGFLGSNGCGKSTTMKMLTGLLPASEGEAWLFGQPVDPkdiATRQR-VGY 353
Cdd:PRK15056 6 GIVVNDVTVTWRNgHTALRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKISILGQPTRQ---ALQKNlVAY 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 354 MSQ------AFSLYSELSVRQNLELHARLFHIPDDEIAHRVAEMSERFMLTEVKDALPADLPLGIRQRLSLAVAVIHRPE 427
Cdd:PRK15056 83 VPQseevdwSFPVLVEDVVMMGRYGHMGWLRRAKKRDRQIVTAALARVDMVEFRHRQIGELSGGQKKRVFLARAIAQQGQ 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 428 MLILDEPTSGVDPVARDMFWQLMVDLaRQDRVTIFISTHFMNE-AERCDrISLMHAGKVLASDTPQALVEqrgAASLEEA 506
Cdd:PRK15056 163 VILLDEPFTGVDVKTEARIISLLREL-RDEGKTMLVSTHNLGSvTEFCD-YTVMVKGTVLASGPTETTFT---AENLELA 237
|
....*.
gi 1820369315 507 FIAWLK 512
Cdd:PRK15056 238 FSGVLR 243
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
15-195 |
3.30e-15 |
|
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is a cytosolic protein required by fungal ribosomes for in vitro protein synthesis and for in vivo growth. EF-3 stimulates the binding of the EF-1: GTP: aa-tRNA ternary complex to the ribosomal A site by facilitated release of the deacylated tRNA from the E site. The reaction requires ATP hydrolysis. EF-3 contains two ATP nucleotide binding sequence (NBS) motifs. NBSI is sufficient for the intrinsic ATPase activity. NBSII is essential for the ribosome-stimulated functions.
Pssm-ID: 213188 [Multi-domain] Cd Length: 144 Bit Score: 73.64 E-value: 3.30e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 15 LENVGQQYGATIALRDISLAIPARRMVGLIGPDGVGKSSLLSLIAGARAIEQGNVmvlggdmrdvhhRRDVCPKIAWMPQ 94
Cdd:cd03221 3 LENLSKTYGGKLLLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIV------------TWGSTVKIGYFEQ 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 95 glgknlyhtlsvyenvdffarlfghdkaerelrinellqstglapfrdrpagkLSGGMKQKLGLCCALIHDPQLLILDEP 174
Cdd:cd03221 71 -----------------------------------------------------LSGGEKMRLALAKLLLENPNLLLLDEP 97
|
170 180
....*....|....*....|.
gi 1820369315 175 TTGVDPLSRAQfweLIDSIRQ 195
Cdd:cd03221 98 TNHLDLESIEA---LEEALKE 115
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
15-235 |
3.57e-15 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 77.96 E-value: 3.57e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 15 LENVGQQY-GATIALRDISLAIPARRMVGLIGPDGVGKSSLLSLIAGARAIEQGNVMVlggDMRDVHHR----RDvcpkI 89
Cdd:PRK11650 6 LQAVRKSYdGKTQVIKGIDLDVADGEFIVLVGPSGCGKSTLLRMVAGLERITSGEIWI---GGRVVNELepadRD----I 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 90 AWMPQglgkN--LYHTLSVYENVDFFARLFGHDKAERELRINELLQSTGLAPFRDRPAGKLSGGMKQKLGLCCALIHDPQ 167
Cdd:PRK11650 79 AMVFQ----NyaLYPHMSVRENMAYGLKIRGMPKAEIEERVAEAARILELEPLLDRKPRELSGGQRQRVAMGRAIVREPA 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1820369315 168 LLILDEPTTGVDPLSRAQFWELIDSIRQRQPEMSVLVATAYMEEAERFDWLVAMNAGEVLATGSAAEL 235
Cdd:PRK11650 155 VFLFDEPLSNLDAKLRVQMRLEIQRLHRRLKTTSLYVTHDQVEAMTLADRVVVMNGGVAEQIGTPVEV 222
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
277-484 |
3.64e-15 |
|
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is a cytosolic protein required by fungal ribosomes for in vitro protein synthesis and for in vivo growth. EF-3 stimulates the binding of the EF-1: GTP: aa-tRNA ternary complex to the ribosomal A site by facilitated release of the deacylated tRNA from the E site. The reaction requires ATP hydrolysis. EF-3 contains two ATP nucleotide binding sequence (NBS) motifs. NBSI is sufficient for the intrinsic ATPase activity. NBSII is essential for the ribosome-stimulated functions.
Pssm-ID: 213188 [Multi-domain] Cd Length: 144 Bit Score: 73.25 E-value: 3.64e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 277 IEARGLTMRFGNFVAVDHVNFRIARGEIFGFLGSNGCGKSTTMKMLTGLLPASEGEaWLFGQPVdpkdiatrqRVGYMSQ 356
Cdd:cd03221 1 IELENLSKTYGGKLLLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGI-VTWGSTV---------KIGYFEQ 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 357 afslyseLSvrqnlelharlfhipddeiahrvaemserfmltevkdalpadlpLGIRQRLSLAVAVIHRPEMLILDEPTS 436
Cdd:cd03221 71 -------LS--------------------------------------------GGEKMRLALAKLLLENPNLLLLDEPTN 99
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1820369315 437 GVDPVARDmfwQLMVDLARQDRVTIFIS--THFMNEAerCDRISLMHAGK 484
Cdd:cd03221 100 HLDLESIE---ALEEALKEYPGTVILVShdRYFLDQV--ATKIIELEDGK 144
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
4-240 |
3.81e-15 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 79.48 E-value: 3.81e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 4 TPQDTSPPIALlENVGQQY--GATIALRDISLAIPARRMVGLIGPDGVGKSSLLSLIAGARAIEQGNVMVLGGDMRDVHH 81
Cdd:PRK11160 331 TAAADQVSLTL-NNVSFTYpdQPQPVLKGLSLQIKAGEKVALLGRTGCGKSTLLQLLTRAWDPQQGEILLNGQPIADYSE 409
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 82 rrdvcpkiawmpqglgKNLYHTLSVY-ENVDFFA---R---LFGHDKAERElRINELLQSTGLAPFRDRPAG-------- 146
Cdd:PRK11160 410 ----------------AALRQAISVVsQRVHLFSatlRdnlLLAAPNASDE-ALIEVLQQVGLEKLLEDDKGlnawlgeg 472
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 147 --KLSGGMKQKLGLCCALIHDPQLLILDEPTTGVDPLSRAQFWELidsIRQRQPEMSVLVATAYMEEAERFDWLVAMNAG 224
Cdd:PRK11160 473 grQLSGGEQRRLGIARALLHDAPLLLLDEPTEGLDAETERQILEL---LAEHAQNKTVLMITHRLTGLEQFDRICVMDNG 549
|
250
....*....|....*.
gi 1820369315 225 EVLATGSAAELKAQTG 240
Cdd:PRK11160 550 QIIEQGTHQELLAQQG 565
|
|
| type_I_sec_PrtD |
TIGR01842 |
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in ... |
287-487 |
3.91e-15 |
|
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in some Gram-negative bacteria to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type I secretion apparatus. Targeted proteins are not cleaved at the N-terminus, but rather carry signals located toward the extreme C-terminus to direct type I secretion. [Protein fate, Protein and peptide secretion and trafficking]
Pssm-ID: 200134 [Multi-domain] Cd Length: 544 Bit Score: 79.31 E-value: 3.91e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 287 GNFVAVDHVNFRIARGEIFGFLGSNGCGKSTTMKMLTGLLPASEGEAWLFGQPVDPKDIAT-RQRVGYMSQAFSLYSElS 365
Cdd:TIGR01842 329 GKKPTLRGISFSLQAGEALAIIGPSGSGKSTLARLIVGIWPPTSGSVRLDGADLKQWDRETfGKHIGYLPQDVELFPG-T 407
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 366 VRQNLelhARLFHIPDDE---IAHRVA---EMSERFML---TEVKDAlPADLPLGIRQRLSLAVAVIHRPEMLILDEPTS 436
Cdd:TIGR01842 408 VAENI---ARFGENADPEkiiEAAKLAgvhELILRLPDgydTVIGPG-GATLSGGQRQRIALARALYGDPKLVVLDEPNS 483
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1820369315 437 GVDPVARDMFWQLMVDLARQDRVTIFIsTHFMNEAERCDRISLMHAGKVLA 487
Cdd:TIGR01842 484 NLDEEGEQALANAIKALKARGITVVVI-THRPSLLGCVDKILVLQDGRIAR 533
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
295-486 |
4.51e-15 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 76.24 E-value: 4.51e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 295 VNFRIARGEIFGFLGSNGCGKSTTMKMLTGLLP------ASEGEAWLFGQPVDPKD-IATRQRVGYMSQAFSLYSELSVR 367
Cdd:PRK14246 29 ITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLIEiydskiKVDGKVLYFGKDIFQIDaIKLRKEVGMVFQQPNPFPHLSIY 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 368 QNLELHARLFHIPDDEIAHRVAEMSERF--MLTEVKDAL--PAD-LPLGIRQRLSLAVAVIHRPEMLILDEPTSGVDPVA 442
Cdd:PRK14246 109 DNIAYPLKSHGIKEKREIKKIVEECLRKvgLWKEVYDRLnsPASqLSGGQQQRLTIARALALKPKVLLMDEPTSMIDIVN 188
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1820369315 443 RDMFWQLMVDLARQdrVTIFISTHFMNEAER-CDRISLMHAGKVL 486
Cdd:PRK14246 189 SQAIEKLITELKNE--IAIVIVSHNPQQVARvADYVAFLYNGELV 231
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
26-230 |
4.68e-15 |
|
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: 75.39 E-value: 4.68e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 26 IALRDISLAIPARRMVGLIGPDGVGKSSLLSLIAG---ARAIEQGNVMVLGGDMrdvhHRRDVCPKIAWMPQGlgKNLYH 102
Cdd:cd03234 21 RILNDVSLHVESGQVMAILGSSGSGKTTLLDAISGrveGGGTTSGQILFNGQPR----KPDQFQKCVAYVRQD--DILLP 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 103 TLSVYENVDFFARLFGH---DKAERELRI-NELLQSTGLAPFRDRPAGKLSGGMKQKLGLCCALIHDPQLLILDEPTTGV 178
Cdd:cd03234 95 GLTVRETLTYTAILRLPrksSDAIRKKRVeDVLLRDLALTRIGGNLVKGISGGERRRVSIAVQLLWDPKVLILDEPTSGL 174
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1820369315 179 DPLSRAQFWEL-----------IDSIRQRQPEMSVLvataymeeaerFDWLVAMNAGEVLATG 230
Cdd:cd03234 175 DSFTALNLVSTlsqlarrnrivILTIHQPRSDLFRL-----------FDRILLLSSGEIVYSG 226
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
28-332 |
4.70e-15 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 79.01 E-value: 4.70e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 28 LRDISLA-IP-ARrmVGLIGPDGVGKSSLLSLIAGARAIEQGNVMVLGGdmrdvhhrrdvcPKIAWMPQGlgKNLYHTLS 105
Cdd:PRK11819 23 LKDISLSfFPgAK--IGVLGLNGAGKSTLLRIMAGVDKEFEGEARPAPG------------IKVGYLPQE--PQLDPEKT 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 106 VYENV--------DFFARL------FGHDKA------ERELRINELLQSTGLA---------------PFRDRPAGKLSG 150
Cdd:PRK11819 87 VRENVeegvaevkAALDRFneiyaaYAEPDAdfdalaAEQGELQEIIDAADAWdldsqleiamdalrcPPWDAKVTKLSG 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 151 GMKQKLGLCCALIHDPQLLILDEPTTGVDPLSRA---QF-----------------------WEL-IDSIR--------- 194
Cdd:PRK11819 167 GERRRVALCRLLLEKPDMLLLDEPTNHLDAESVAwleQFlhdypgtvvavthdryfldnvagWILeLDRGRgipwegnys 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 195 ----QRQPEMsvlvATAYMEEAER-------FDWlVAMNAgevlatgsaaelKA-QTGSQTLEQAFIALLPEAQRQAHKT 262
Cdd:PRK11819 247 swleQKAKRL----AQEEKQEAARqkalkreLEW-VRQSP------------KArQAKSKARLARYEELLSEEYQKRNET 309
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1820369315 263 --VVIPPRDsREEEIAIEARGLTMRFGNFVAVDHVNFRIARGEIFGFLGSNGCGKSTTMKMLTGLLPASEGE 332
Cdd:PRK11819 310 neIFIPPGP-RLGDKVIEAENLSKSFGDRLLIDDLSFSLPPGGIVGIIGPNGAGKSTLFKMITGQEQPDSGT 380
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
32-214 |
4.76e-15 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 75.39 E-value: 4.76e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 32 SLAIPARRMVGLIGPDGVGKSSLLSLIAGARAIEQGNVMVLGGDmrdvhHRRDVCPK--IAWMPQglGKNLYHTLSVYEN 109
Cdd:PRK10771 19 DLTVERGERVAILGPSGAGKSTLLNLIAGFLTPASGSLTLNGQD-----HTTTPPSRrpVSMLFQ--ENNLFSHLTVAQN 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 110 V----DFFARLfghdKAERELRINELLQSTGLAPFRDRPAGKLSGGMKQKLGLCCALIHDPQLLILDEPTTGVDPLSRAQ 185
Cdd:PRK10771 92 IglglNPGLKL----NAAQREKLHAIARQMGIEDLLARLPGQLSGGQRQRVALARCLVREQPILLLDEPFSALDPALRQE 167
|
170 180 190
....*....|....*....|....*....|
gi 1820369315 186 FWELIDSI-RQRQpeMSVLVATAYMEEAER 214
Cdd:PRK10771 168 MLTLVSQVcQERQ--LTLLMVSHSLEDAAR 195
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
287-486 |
4.86e-15 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 77.46 E-value: 4.86e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 287 GNFVAVDHVNFRIARGEIFGFLGSNGCGKSTTMKMLTGLLPAS---EGEAWLFGQPVD--PKDIATRQRVGYMSQAF--- 358
Cdd:PRK09473 27 GDVTAVNDLNFSLRAGETLGIVGESGSGKSQTAFALMGLLAANgriGGSATFNGREILnlPEKELNKLRAEQISMIFqdp 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 359 --SLYSELSVRQNL----ELHARLFHipddeiaHRVAEMSERfMLTEVK--------DALPADLPLGIRQRLSLAVAVIH 424
Cdd:PRK09473 107 mtSLNPYMRVGEQLmevlMLHKGMSK-------AEAFEESVR-MLDAVKmpearkrmKMYPHEFSGGMRQRVMIAMALLC 178
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1820369315 425 RPEMLILDEPTSGVDPVARDMFWQLMVDLARQDRVTIFISTHFMN-EAERCDRISLMHAGKVL 486
Cdd:PRK09473 179 RPKLLIADEPTTALDVTVQAQIMTLLNELKREFNTAIIMITHDLGvVAGICDKVLVMYAGRTM 241
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
277-503 |
5.51e-15 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 75.89 E-value: 5.51e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 277 IEARGLTMRfGNFVAVDHVNFRIARGEIFGFLGSNGCGKSTTMKMLTGLLPA----SEGEAWLFGQPVDPKDIATRQRVG 352
Cdd:PRK10418 5 IELRNIALQ-AAQPLVHGVSLTLQRGRVLALVGGSGSGKSLTCAAALGILPAgvrqTAGRVLLDGKPVAPCALRGRKIAT 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 353 YMSQAFSLYSELsvrQNLELHARL------FHIPDDEIAHRVAEMSerfmLTEVKDAL---PADLPLGIRQRLSLAVAVI 423
Cdd:PRK10418 84 IMQNPRSAFNPL---HTMHTHAREtclalgKPADDATLTAALEAVG----LENAARVLklyPFEMSGGMLQRMMIALALL 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 424 HRPEMLILDEPTSGVDPVARDMFWQLMVDLARQDRVTIFISTHFMNEAERC-DRISLMHAGKvlasdtpqaLVEQRGAAS 502
Cdd:PRK10418 157 CEAPFIIADEPTTDLDVVAQARILDLLESIVQKRALGMLLVTHDMGVVARLaDDVAVMSHGR---------IVEQGDVET 227
|
.
gi 1820369315 503 L 503
Cdd:PRK10418 228 L 228
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
30-239 |
5.94e-15 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 75.96 E-value: 5.94e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 30 DISLAIPARRMVGLIGPDGVGKSSLLSLIAGARAIEQGNVMVLGGDMRDVHHRR--DVCPKIAWMPQGlgKNLYHTLSVY 107
Cdd:PRK11831 25 NISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEILFDGENIPAMSRSRlyTVRKRMSMLFQS--GALFTDMNVF 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 108 ENVDFFARlfghdkaERELRINELLQST--------GLAPFRDRPAGKLSGGMKQKLGLCCALIHDPQLLILDEPTTGVD 179
Cdd:PRK11831 103 DNVAYPLR-------EHTQLPAPLLHSTvmmkleavGLRGAAKLMPSELSGGMARRAALARAIALEPDLIMFDEPFVGQD 175
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 180 PLSRAQFWELIDSIRQRQPEMSVLVATAYMEEAERFDWLVAMNAGEVLATGSAAELKAQT 239
Cdd:PRK11831 176 PITMGVLVKLISELNSALGVTCVVVSHDVPEVLSIADHAYIVADKKIVAHGSAQALQANP 235
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
276-503 |
6.06e-15 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 75.56 E-value: 6.06e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 276 AIEARGLTMRFGNFVAVDHVNFRIARGEIFGFLGSNGCGKSTTMKMLTgLLPASEGEAWLFG-------QPVDPKDI--- 345
Cdd:PRK11264 3 AIEVKNLVKKFHGQTVLHGIDLEVKPGEVVAIIGPSGSGKTTLLRCIN-LLEQPEAGTIRVGditidtaRSLSQQKGlir 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 346 ATRQRVGYMSQAFSLYSELSVRQN-LELHARLFHIPDDEIAHRVAEMSERFMLTEVKDALPADLPLGIRQRLSLAVAVIH 424
Cdd:PRK11264 82 QLRQHVGFVFQNFNLFPHRTVLENiIEGPVIVKGEPKEEATARARELLAKVGLAGKETSYPRRLSGGQQQRVAIARALAM 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 425 RPEMLILDEPTSGVDPVARDMFWQLMVDLARQDRvTIFISTHFMNEA-ERCDRISLMHAGKVlasdtpqalVEQRGAASL 503
Cdd:PRK11264 162 RPEVILFDEPTSALDPELVGEVLNTIRQLAQEKR-TMVIVTHEMSFArDVADRAIFMDQGRI---------VEQGPAKAL 231
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
291-464 |
6.07e-15 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 76.93 E-value: 6.07e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 291 AVDHVNFRIARGEIFGFLGSNGCGKSTTMKMLTGLLPASEGEAWLFGQPVDPKDIAT----RQRVGYMSQafSLYSELSV 366
Cdd:PRK11308 30 ALDGVSFTLERGKTLAVVGESGCGKSTLARLLTMIETPTGGELYYQGQDLLKADPEAqkllRQKIQIVFQ--NPYGSLNP 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 367 RQN--------LELHARLfhiPDDEIAHRVAEMSERFML-TEVKDALPADLPLGIRQRLSLAVAVIHRPEMLILDEPTSG 437
Cdd:PRK11308 108 RKKvgqileepLLINTSL---SAAERREKALAMMAKVGLrPEHYDRYPHMFSGGQRQRIAIARALMLDPDVVVADEPVSA 184
|
170 180
....*....|....*....|....*...
gi 1820369315 438 VDPVARDMFWQLMVDLARQDRVT-IFIS 464
Cdd:PRK11308 185 LDVSVQAQVLNLMMDLQQELGLSyVFIS 212
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
278-488 |
7.88e-15 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 78.41 E-value: 7.88e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 278 EARGLTMRFGNFVAVDHVNFRIARGEIFGFLGSNGCGKSTTMKMLTGLLPASEGEAWLFGQPVDPKDI--ATRQRVGYMS 355
Cdd:PRK11288 6 SFDGIGKTFPGVKALDDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSILIDGQEMRFASTtaALAAGVAIIY 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 356 QAFSLYSELSVRQNL---ELHARLFHIPDDEIAHRVAEMSERFMLTEVKDALPADLPLGIRQRLSLAVAVIHRPEMLILD 432
Cdd:PRK11288 86 QELHLVPEMTVAENLylgQLPHKGGIVNRRLLNYEAREQLEHLGVDIDPDTPLKYLSIGQRQMVEIAKALARNARVIAFD 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1820369315 433 EPTSGVDPVARDMFWQLMVDLARQDRVTIFIStHFMNEAER-CDRISLMHAGKVLAS 488
Cdd:PRK11288 166 EPTSSLSAREIEQLFRVIRELRAEGRVILYVS-HRMEEIFAlCDAITVFKDGRYVAT 221
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
281-485 |
7.95e-15 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 75.49 E-value: 7.95e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 281 GLTMRFGNFVAVDHVNFRIARGEIFGFLGSNGCGKSTTMKMLTGLLPASEGEAWLFGQPV---DPKDIATRQRVGYM--S 355
Cdd:PRK10419 17 GLSGKHQHQTVLNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWRGEPLaklNRAQRKAFRRDIQMvfQ 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 356 QAFSLYS-ELSVRQNLELHAR-LFHIPDDEIAHRVAEMSERFMLT-EVKDALPADLPLGIRQRLSLAVAVIHRPEMLILD 432
Cdd:PRK10419 97 DSISAVNpRKTVREIIREPLRhLLSLDKAERLARASEMLRAVDLDdSVLDKRPPQLSGGQLQRVCLARALAVEPKLLILD 176
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1820369315 433 EPTSGVDPVARDMFWQLMVDLARQ-DRVTIFIsTHFMNEAER-CDRISLMHAGKV 485
Cdd:PRK10419 177 EAVSNLDLVLQAGVIRLLKKLQQQfGTACLFI-THDLRLVERfCQRVMVMDNGQI 230
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
16-240 |
8.93e-15 |
|
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: 78.22 E-value: 8.93e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 16 ENVGQQYGAT--IALRDISLAIPARRMVGLIGPDGVGKSSLLSLIAGARAIEQGNVMVLGGDMRDVHhRRDVCPKIAWMP 93
Cdd:TIGR02203 334 RNVTFRYPGRdrPALDSISLVIEPGETVALVGRSGSGKSTLVNLIPRFYEPDSGQILLDGHDLADYT-LASLRRQVALVS 412
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 94 QGLgkNLYHTlSVYENVDFFARlfghDKAERElRINELLQSTGLAPFRDR-PAG----------KLSGGMKQKLGLCCAL 162
Cdd:TIGR02203 413 QDV--VLFND-TIANNIAYGRT----EQADRA-EIERALAAAYAQDFVDKlPLGldtpigengvLLSGGQRQRLAIARAL 484
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1820369315 163 IHDPQLLILDEPTTGVDPLSRAQfweLIDSIRQRQPEMSVLVATAYMEEAERFDWLVAMNAGEVLATGSAAELKAQTG 240
Cdd:TIGR02203 485 LKDAPILILDEATSALDNESERL---VQAALERLMQGRTTLVIAHRLSTIEKADRIVVMDDGRIVERGTHNELLARNG 559
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
15-232 |
1.15e-14 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 75.05 E-value: 1.15e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 15 LENVGQQYGATIALRDISLAIPARRMVGLIGPDGVGKSSLL----SLIAGARAIEQ-----GNVMVLGGDM-RDVHHRRd 84
Cdd:PRK09984 7 VEKLAKTFNQHQALHAVDLNIHHGEMVALLGPSGSGKSTLLrhlsGLITGDKSAGShiellGRTVQREGRLaRDIRKSR- 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 85 vcPKIAWMPQGLgkNLYHTLSVYENVDFFA-----------RLFGHDKAERELRInelLQSTGLAPFRDRPAGKLSGGMK 153
Cdd:PRK09984 86 --ANTGYIFQQF--NLVNRLSVLENVLIGAlgstpfwrtcfSWFTREQKQRALQA---LTRVGMVHFAHQRVSTLSGGQQ 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 154 QKLGLCCALIHDPQLLILDEPTTGVDPLSRAQFWELIDSIRQRQpEMSVLVATAYMEEAERF-DWLVAMNAGEVLATGSA 232
Cdd:PRK09984 159 QRVAIARALMQQAKVILADEPIASLDPESARIVMDTLRDINQND-GITVVVTLHQVDYALRYcERIVALRQGHVFYDGSS 237
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
26-239 |
1.23e-14 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 74.74 E-value: 1.23e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 26 IALRDISLAIPARRMVGLIGPDGVGKSSLLSLIAGARAIEQGNVMVLGgdmRDV----HHRR---------D----VCPk 88
Cdd:COG1101 20 RALDGLNLTIEEGDFVTVIGSNGAGKSTLLNAIAGSLPPDSGSILIDG---KDVtklpEYKRakyigrvfqDpmmgTAP- 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 89 iawmpqglgknlyhTLSVYENVDFFAR-------LFGHDKAERElRINELLQSTGLApFRDR---PAGKLSGGMKQKLGL 158
Cdd:COG1101 96 --------------SMTIEENLALAYRrgkrrglRRGLTKKRRE-LFRELLATLGLG-LENRldtKVGLLSGGQRQALSL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 159 CCALIHDPQLLILDEPTTGVDPLSRAQFWELIDSIRQRQpEMSVLVATAYMEEAERF-DWLVAMNAGEVLATGSAAELKA 237
Cdd:COG1101 160 LMATLTKPKLLLLDEHTAALDPKTAALVLELTEKIVEEN-NLTTLMVTHNMEQALDYgNRLIMMHEGRIILDVSGEEKKK 238
|
..
gi 1820369315 238 QT 239
Cdd:COG1101 239 LT 240
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
28-235 |
1.28e-14 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 78.17 E-value: 1.28e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 28 LRDISLAIPARRMVGLIGPDGVGKSSLLSLIAGARA--IEQGNVMVLGGDMRDVHHRRDVCPKIawMPQGLgknLYHTLS 105
Cdd:TIGR00955 41 LKNVSGVAKPGELLAVMGSSGAGKTTLMNALAFRSPkgVKGSGSVLLNGMPIDAKEMRAISAYV--QQDDL---FIPTLT 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 106 VYENVDFFARLFGHD---KAERELRINELLQSTGLAPFRDRPAGK------LSGGMKQKLGLCCALIHDPQLLILDEPTT 176
Cdd:TIGR00955 116 VREHLMFQAHLRMPRrvtKKEKRERVDEVLQALGLRKCANTRIGVpgrvkgLSGGERKRLAFASELLTDPPLLFCDEPTS 195
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1820369315 177 GVDPLSRAQFWELIDSIRQRQPEMSVLVATAYMEEAERFDWLVAMNAGEVLATGSAAEL 235
Cdd:TIGR00955 196 GLDSFMAYSVVQVLKGLAQKGKTIICTIHQPSSELFELFDKIILMAEGRVAYLGSPDQA 254
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
295-500 |
1.41e-14 |
|
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC transporter that is expressed in the mitochondria. Although the specific function of ATM1 is unknown, its disruption results in the accumulation of excess mitochondrial iron, loss of mitochondrial cytochromes, oxidative damage to mitochondrial DNA, and decreased levels of cytosolic heme proteins. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213220 [Multi-domain] Cd Length: 236 Bit Score: 74.19 E-value: 1.41e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 295 VNFRIARGEIFGFLGSNGCGKSTTMKMLTGLLPASEGEAWLFGQPVDPKDIAT-RQRVGYMSQAFSLYSElSVRQNLElH 373
Cdd:cd03253 20 VSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDGQDIREVTLDSlRRAIGVVPQDTVLFND-TIGYNIR-Y 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 374 ARLfHIPDDEI--AHRVAEMSERFMltevkdALP-----------ADLPLGIRQRLSLAVAVIHRPEMLILDEPTSGVDP 440
Cdd:cd03253 98 GRP-DATDEEVieAAKAAQIHDKIM------RFPdgydtivgergLKLSGGEKQRVAIARAILKNPPILLLDEATSALDT 170
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 441 VARDMFWQLMVDLARqDRVTIFIsTHFMNEAERCDRISLMHAGKVLASDTPQALVEQRGA 500
Cdd:cd03253 171 HTEREIQAALRDVSK-GRTTIVI-AHRLSTIVNADKIIVLKDGRIVERGTHEELLAKGGL 228
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
277-503 |
1.90e-14 |
|
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: 77.03 E-value: 1.90e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 277 IEARGLTMRFGN----FVAVDHVNFRIARGEIFGFLGSNGCGKSTTMKMLTGLLPAS----EGEAWLFGQPVDPKDIATR 348
Cdd:COG4172 7 LSVEDLSVAFGQgggtVEAVKGVSFDIAAGETLALVGESGSGKSVTALSILRLLPDPaahpSGSILFDGQDLLGLSEREL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 349 QRV--GYMSQAF-----SLYSELSV-RQ---NLELHARLfhiPDDEIAHRVAEMSERFMLTEVK---DALPADLPLGIRQ 414
Cdd:COG4172 87 RRIrgNRIAMIFqepmtSLNPLHTIgKQiaeVLRLHRGL---SGAAARARALELLERVGIPDPErrlDAYPHQLSGGQRQ 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 415 RLSLAVAVIHRPEMLILDEPTSGVDPVARDMFWQLMVDLARQDRVTI-FIsTHFMNEAER-CDRISLMHAGKVlasdtpq 492
Cdd:COG4172 164 RVMIAMALANEPDLLIADEPTTALDVTVQAQILDLLKDLQRELGMALlLI-THDLGVVRRfADRVAVMRQGEI------- 235
|
250
....*....|.
gi 1820369315 493 alVEQRGAASL 503
Cdd:COG4172 236 --VEQGPTAEL 244
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
274-486 |
2.04e-14 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 74.44 E-value: 2.04e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 274 EIAIEARGLTMRF----GNF-----VAVDHVNFRIARGEIFGFLGSNGCGKSTTMKMLTGLLPASEGEAWLFGQPVDPKD 344
Cdd:PRK15112 2 ETLLEVRNLSKTFryrtGWFrrqtvEAVKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDHPLHFGD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 345 IATR-QRVGYMSQ--AFSLYSELSVRQNLELHARL-FHIPDDEIAHRV-AEMSERFMLTEVKDALPADLPLGIRQRLSLA 419
Cdd:PRK15112 82 YSYRsQRIRMIFQdpSTSLNPRQRISQILDFPLRLnTDLEPEQREKQIiETLRQVGLLPDHASYYPHMLAPGQKQRLGLA 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1820369315 420 VAVIHRPEMLILDEPTSGVDPVARDMFWQLMVDLARQDRVT-IFISTHFMNEAERCDRISLMHAGKVL 486
Cdd:PRK15112 162 RALILRPKVIIADEALASLDMSMRSQLINLMLELQEKQGISyIYVTQHLGMMKHISDQVLVMHQGEVV 229
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
9-236 |
2.15e-14 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 73.87 E-value: 2.15e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 9 SPPIALLENVGQQYGATIALRDISLAIPARRMVGLIGPDGVGKSSLLSLIAGARAIEQGNVMvlggdMRDVHHRRDVCPK 88
Cdd:PRK11300 2 SQPLLSVSGLMMRFGGLLAVNNVNLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTIL-----LRGQHIEGLPGHQ 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 89 IAWMpqGLGKN-----LYHTLSVYENV----------DFFARLF---GHDKAEREL--RINELLQSTGLAPFRDRPAGKL 148
Cdd:PRK11300 77 IARM--GVVRTfqhvrLFREMTVIENLlvaqhqqlktGLFSGLLktpAFRRAESEAldRAATWLERVGLLEHANRQAGNL 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 149 SGGMKQKLGLCCALIHDPQLLILDEPTTGVDPLSRAQFWELIDSIRqRQPEMSVLV----ATAYMEEAERfdwLVAMNAG 224
Cdd:PRK11300 155 AYGQQRRLEIARCMVTQPEILMLDEPAAGLNPKETKELDELIAELR-NEHNVTVLLiehdMKLVMGISDR---IYVVNQG 230
|
250
....*....|..
gi 1820369315 225 EVLATGSAAELK 236
Cdd:PRK11300 231 TPLANGTPEEIR 242
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
277-499 |
2.88e-14 |
|
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: 77.09 E-value: 2.88e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 277 IEARGLTMRFG-NFVAVDHVNFRIARGEIFGFLGSNGCGKSTTMKMLTGLLPASEGEAWLFGQPVDPKDIAT-RQRVGYM 354
Cdd:TIGR01193 474 IVINDVSYSYGyGSNILSDISLTIKMNSKTTIVGMSGSGKSTLAKLLVGFFQARSGEILLNGFSLKDIDRHTlRQFINYL 553
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 355 SQAFSLYSElSVRQNLELHARLfHIPDDEI--AHRVAEMS---ERFML---TEVKDAlPADLPLGIRQRLSLAVAVIHRP 426
Cdd:TIGR01193 554 PQEPYIFSG-SILENLLLGAKE-NVSQDEIwaACEIAEIKddiENMPLgyqTELSEE-GSSISGGQKQRIALARALLTDS 630
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1820369315 427 EMLILDEPTSGVDPVARDMFWQLMVDLarQDRVTIFIStHFMNEAERCDRISLMHAGKVLASDTPQALVEQRG 499
Cdd:TIGR01193 631 KVLILDESTSNLDTITEKKIVNNLLNL--QDKTIIFVA-HRLSVAKQSDKIIVLDHGKIIEQGSHDELLDRNG 700
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
276-473 |
3.73e-14 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 73.53 E-value: 3.73e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 276 AIEARGLTMRFGNFVAVDHVNFRIARGEIFGFLGSNGCGKSTTMKMLTGLLPAS-----EGEAWLFGQPVDPKDIAT--- 347
Cdd:PRK14258 7 AIKVNNLSFYYDTQKILEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLNRMNELEsevrvEGRVEFFNQNIYERRVNLnrl 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 348 RQRVGYMSQAFSLYSeLSVRQNLELHARLF----HIPDDEIAHRVAEMSErfMLTEVKDAL---PADLPLGIRQRLSLAV 420
Cdd:PRK14258 87 RRQVSMVHPKPNLFP-MSVYDNVAYGVKIVgwrpKLEIDDIVESALKDAD--LWDEIKHKIhksALDLSGGQQQRLCIAR 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1820369315 421 AVIHRPEMLILDEPTSGVDPVARDMFWQLMVDLARQDRVTIFISTHFMNEAER 473
Cdd:PRK14258 164 ALAVKPKVLLMDEPCFGLDPIASMKVESLIQSLRLRSELTMVIVSHNLHQVSR 216
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
293-500 |
4.38e-14 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 76.30 E-value: 4.38e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 293 DHVNFRIARGEIFGFLGSNGCGKSTTMKMLTGLLPASEGEAWLFGQPV---DPKDIAT--RQRVGYMSQAFSLYSELSVR 367
Cdd:PRK10535 25 KGISLDIYAGEMVAIVGASGSGKSTLMNILGCLDKPTSGTYRVAGQDVatlDADALAQlrREHFGFIFQRYHLLSHLTAA 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 368 QNLELHARLFHIPDDEIAHRVAEMSERFMLTEVKDALPADLPLGIRQRLSLAVAVIHRPEMLILDEPTSGVDPVARDMFW 447
Cdd:PRK10535 105 QNVEVPAVYAGLERKQRLLRAQELLQRLGLEDRVEYQPSQLSGGQQQRVSIARALMNGGQVILADEPTGALDSHSGEEVM 184
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1820369315 448 QLMVDLaRQDRVTIFISTHFMNEAERCDRISLMHAGKVLASDTPQALVEQRGA 500
Cdd:PRK10535 185 AILHQL-RDRGHTVIIVTHDPQVAAQAERVIEIRDGEIVRNPPAQEKVNVAGG 236
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
295-485 |
8.59e-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: 71.73 E-value: 8.59e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 295 VNFRIARGEIFGFLGSNGCGKSTTMKMLTGLLPASEGEAWLFGQPV-DPKDIATRQRVGYMSQAFSLYSElSVRQNLELH 373
Cdd:cd03248 33 VSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDGKPIsQYEHKYLHSKVSLVGQEPVLFAR-SLQDNIAYG 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 374 arLFHIPDDEI--------AHRVAEMSERFMLTEVKDAlPADLPLGIRQRLSLAVAVIHRPEMLILDEPTSGVDPVARDM 445
Cdd:cd03248 112 --LQSCSFECVkeaaqkahAHSFISELASGYDTEVGEK-GSQLSGGQKQRVAIARALIRNPQVLILDEATSALDAESEQQ 188
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1820369315 446 FWQLMVDLARqdRVTIFISTHFMNEAERCDRISLMHAGKV 485
Cdd:cd03248 189 VQQALYDWPE--RRTVLVIAHRLSTVERADQILVLDGGRI 226
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
296-500 |
1.07e-13 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 75.14 E-value: 1.07e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 296 NFRIARGEIFGFLGSNGCGKSTTMKMLTGLLPASEGEAWLFGQPVDPKD-IATRQRVGYMSQAFSLYSElSVRQNLELHa 374
Cdd:TIGR00958 501 TFTLHPGEVVALVGPSGSGKSTVAALLQNLYQPTGGQVLLDGVPLVQYDhHYLHRQVALVGQEPVLFSG-SVRENIAYG- 578
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 375 rLFHIPDDEI--------AHRVAEMSERFMLTEVKDAlPADLPLGIRQRLSLAVAVIHRPEMLILDEPTSGVDPVARDMF 446
Cdd:TIGR00958 579 -LTDTPDEEImaaakaanAHDFIMEFPNGYDTEVGEK-GSQLSGGQKQRIAIARALVRKPRVLILDEATSALDAECEQLL 656
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1820369315 447 WQLMvdlARQDRVTIFIsTHFMNEAERCDRISLMHAGKVLASDTPQALVEQRGA 500
Cdd:TIGR00958 657 QESR---SRASRTVLLI-AHRLSTVERADQILVLKKGSVVEMGTHKQLMEDQGC 706
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
276-501 |
1.33e-13 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 75.54 E-value: 1.33e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 276 AIEARGLTMRF-GNFVAVDH-VNFRIARGEIFGFLGSNGCGKSTTMKMLTGLLPASEGEAWlfgqpVDPKDIAT------ 347
Cdd:PLN03130 1237 SIKFEDVVLRYrPELPPVLHgLSFEISPSEKVGIVGRTGAGKSSMLNALFRIVELERGRIL-----IDGCDISKfglmdl 1311
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 348 RQRVGYMSQAFSLYSElSVRQNLElharlfhiPDDEiaHRVAEMSERFMLTEVKDA-------LPADL-------PLGIR 413
Cdd:PLN03130 1312 RKVLGIIPQAPVLFSG-TVRFNLD--------PFNE--HNDADLWESLERAHLKDVirrnslgLDAEVseagenfSVGQR 1380
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 414 QRLSLAVAVIHRPEMLILDEPTSGVDpVARDMFWQLMVdlaRQD--RVTIFISTHFMNEAERCDRISLMHAGKVLASDTP 491
Cdd:PLN03130 1381 QLLSLARALLRRSKILVLDEATAAVD-VRTDALIQKTI---REEfkSCTMLIIAHRLNTIIDCDRILVLDAGRVVEFDTP 1456
|
250
....*....|
gi 1820369315 492 QALVEQRGAA 501
Cdd:PLN03130 1457 ENLLSNEGSA 1466
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
11-214 |
1.92e-13 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 71.22 E-value: 1.92e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 11 PIALLENVGQQYGATIALRDISLAIPARRMVGLIGPDGVGKSSLLSLIAGARAIE-----QGNVMVLGGDM--RDVH--- 80
Cdd:PRK14258 6 PAIKVNNLSFYYDTQKILEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLNRMNELEsevrvEGRVEFFNQNIyeRRVNlnr 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 81 HRRDVC---PKIAWMPqglgknlyhtLSVYENVDFFARLFG-HDKAERELRINELLQSTGL----APFRDRPAGKLSGGM 152
Cdd:PRK14258 86 LRRQVSmvhPKPNLFP----------MSVYDNVAYGVKIVGwRPKLEIDDIVESALKDADLwdeiKHKIHKSALDLSGGQ 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1820369315 153 KQKLGLCCALIHDPQLLILDEPTTGVDPLSRAQFWELIDSIRQRQpEMSVLVATAYMEEAER 214
Cdd:PRK14258 156 QQRLCIARALAVKPKVLLMDEPCFGLDPIASMKVESLIQSLRLRS-ELTMVIVSHNLHQVSR 216
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
277-466 |
1.93e-13 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 70.22 E-value: 1.93e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 277 IEARGLTMRFGNFVAVDHVNFRIARGEIFGFLGSNGCGKSTTMKMLTGLLPASEGEAWLFGQPVDPKDIATRQRVGYMSQ 356
Cdd:PRK13538 2 LEARNLACERDERILFSGLSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVLWQGEPIRRQRDEYHQDLLYLGH 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 357 AFSLYSELSVRQNLELHARLFHIPDDEIAHRVAemsERFMLTEVKDALPADLPLGIRQRLSLAVAVIHRPEMLILDEPTS 436
Cdd:PRK13538 82 QPGIKTELTALENLRFYQRLHGPGDDEALWEAL---AQVGLAGFEDVPVRQLSAGQQRRVALARLWLTRAPLWILDEPFT 158
|
170 180 190
....*....|....*....|....*....|
gi 1820369315 437 GVDPVARDMFWQLMVDLARQDRVTIFiSTH 466
Cdd:PRK13538 159 AIDKQGVARLEALLAQHAEQGGMVIL-TTH 187
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
26-240 |
2.65e-13 |
|
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: 70.65 E-value: 2.65e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 26 IALRDISLAIPARRMVGLIGPDGVGKSSLLSLIAGARAIEQGNVMVLGGDMRD--VHHRRDvcpKIAWMPQGlgKNLYHT 103
Cdd:cd03249 17 PILKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEILLDGVDIRDlnLRWLRS---QIGLVSQE--PVLFDG 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 104 lSVYENVdffarLFGHDKAERELRINELLQS------TGLAPFRDRPAG----KLSGGMKQKLGLCCALIHDPQLLILDE 173
Cdd:cd03249 92 -TIAENI-----RYGKPDATDEEVEEAAKKAnihdfiMSLPDGYDTLVGergsQLSGGQKQRIAIARALLRNPKILLLDE 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1820369315 174 PTTGVDPLSRAQFWELIDSIRQrqpEMSVLVATAYMEEAERFDWLVAMNAGEVLATGSAAELKAQTG 240
Cdd:cd03249 166 ATSALDAESEKLVQEALDRAMK---GRTTIVIAHRLSTIRNADLIAVLQNGQVVEQGTHDELMAQKG 229
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
16-235 |
3.00e-13 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 70.79 E-value: 3.00e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 16 ENVGQQYGATIALRDISLAIPARRMVGLIGPDGVGKSSLLSLIAGARAIEQGNVMvLGGDMRDVHHRRDVCPKIAWMPQG 95
Cdd:PRK10253 11 EQLTLGYGKYTVAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVW-LDGEHIQHYASKEVARRIGLLAQN 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 96 lgKNLYHTLSVYENVdffAR-------LFGHDKAERELRINELLQSTGLAPFRDRPAGKLSGGMKQKLGLCCALIHDPQL 168
Cdd:PRK10253 90 --ATTPGDITVQELV---ARgryphqpLFTRWRKEDEEAVTKAMQATGITHLADQSVDTLSGGQRQRAWIAMVLAQETAI 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1820369315 169 LILDEPTTGVDPLSRAQFWELIDSIrQRQPEMSVLVATAYMEEAERF-DWLVAMNAGEVLATGSAAEL 235
Cdd:PRK10253 165 MLLDEPTTWLDISHQIDLLELLSEL-NREKGYTLAAVLHDLNQACRYaSHLIALREGKIVAQGAPKEI 231
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
291-473 |
4.46e-13 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 69.52 E-value: 4.46e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 291 AVDHVNFRIARGEIFGFLGSNGCGKSTTMKMLTGLLPASEGEAWLFGQPVD---PKDIA-TRQRVGYMSQAFSLYSELSV 366
Cdd:PRK10908 17 ALQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDITrlkNREVPfLRRQIGMIFQDHHLLMDRTV 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 367 RQNLELHARLFHIPDDEIAHRVAEMSERFMLTEVKDALPADLPLGIRQRLSLAVAVIHRPEMLILDEPTSGVDPVARDMF 446
Cdd:PRK10908 97 YDNVAIPLIIAGASGDDIRRRVSAALDKVGLLDKAKNFPIQLSGGEQQRVGIARAVVNKPAVLLADEPTGNLDDALSEGI 176
|
170 180
....*....|....*....|....*..
gi 1820369315 447 WQLMVDLARQDrVTIFISTHFMNEAER 473
Cdd:PRK10908 177 LRLFEEFNRVG-VTVLMATHDIGLISR 202
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
25-224 |
4.53e-13 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 69.84 E-value: 4.53e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 25 TIALRDISLAIPARRMVGLIGPDGVGKSSLLSLIAGARAIEQGNVMVLGGDMRDVHHRrdvcPKIAWMPQGLG--KNLYH 102
Cdd:PRK11629 22 TDVLHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPMSKLSSA----AKAELRNQKLGfiYQFHH 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 103 TL---SVYENVDFFARLFGHDKAERELRINELLQSTGLAPFRDRPAGKLSGGMKQKLGLCCALIHDPQLLILDEPTTGVD 179
Cdd:PRK11629 98 LLpdfTALENVAMPLLIGKKKPAEINSRALEMLAAVGLEHRANHRPSELSGGERQRVAIARALVNNPRLVLADEPTGNLD 177
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1820369315 180 PLSRAQFWELIDSIRQRQpEMSVLVATAYMEEAERFDWLVAMNAG 224
Cdd:PRK11629 178 ARNADSIFQLLGELNRLQ-GTAFLVVTHDLQLAKRMSRQLEMRDG 221
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
9-214 |
4.69e-13 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 70.19 E-value: 4.69e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 9 SPPIALLENVGQQYGATIALRDISLAIPARRMVGLIGPDGVGKSSLLsliagaRAIEQgnvmvlggdMRDVHHRRDVCPK 88
Cdd:PRK14239 2 TEPILQVSDLSVYYNKKKALNSVSLDFYPNEITALIGPSGSGKSTLL------RSINR---------MNDLNPEVTITGS 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 89 IAWMpqglGKNLYHT----------------------LSVYENVDFFARLFG-HDKAERELRINELLQSTGL-APFRDR- 143
Cdd:PRK14239 67 IVYN----GHNIYSPrtdtvdlrkeigmvfqqpnpfpMSIYENVVYGLRLKGiKDKQVLDEAVEKSLKGASIwDEVKDRl 142
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1820369315 144 --PAGKLSGGMKQKLGLCCALIHDPQLLILDEPTTGVDPLSRAQFWELIDSIRQrqpEMSVLVATAYMEEAER 214
Cdd:PRK14239 143 hdSALGLSGGQQQRVCIARVLATSPKIILLDEPTSALDPISAGKIEETLLGLKD---DYTMLLVTRSMQQASR 212
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
295-501 |
5.78e-13 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 73.47 E-value: 5.78e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 295 VNFRIARGEIFGFLGSNGCGKSTTMKMLTGLLPASEGEAWlfgqpVDPKDIAT------RQRVGYMSQAFSLYSElSVRQ 368
Cdd:PLN03232 1255 LSFFVSPSEKVGVVGRTGAGKSSMLNALFRIVELEKGRIM-----IDDCDVAKfgltdlRRVLSIIPQSPVLFSG-TVRF 1328
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 369 NLElharlfhiPDDEiaHRVAEMSERFMLTEVKDALP--------------ADLPLGIRQRLSLAVAVIHRPEMLILDEP 434
Cdd:PLN03232 1329 NID--------PFSE--HNDADLWEALERAHIKDVIDrnpfgldaevseggENFSVGQRQLLSLARALLRRSKILVLDEA 1398
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1820369315 435 TSGVDpVARDMFWQLMVdlaRQD--RVTIFISTHFMNEAERCDRISLMHAGKVLASDTPQALVEQRGAA 501
Cdd:PLN03232 1399 TASVD-VRTDSLIQRTI---REEfkSCTMLVIAHRLNTIIDCDKILVLSSGQVLEYDSPQELLSRDTSA 1463
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
276-494 |
6.26e-13 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 70.12 E-value: 6.26e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 276 AIEARGLTMRFGNFVAVDHVNFRIARGEIFGFLGSNGCGKSTTMKMLTGLLPASEG-----EAWLFGQPV-DPKDIAT-R 348
Cdd:PRK14271 21 AMAAVNLTLGFAGKTVLDQVSMGFPARAVTSLMGPTGSGKTTFLRTLNRMNDKVSGyrysgDVLLGGRSIfNYRDVLEfR 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 349 QRVGYMSQAFSLYSeLSVRQNLELHARLFH-IPDDEIAHRV-AEMSERFMLTEVKDAL---PADLPLGIRQRLSLAVAVI 423
Cdd:PRK14271 101 RRVGMLFQRPNPFP-MSIMDNVLAGVRAHKlVPRKEFRGVAqARLTEVGLWDAVKDRLsdsPFRLSGGQQQLLCLARTLA 179
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1820369315 424 HRPEMLILDEPTSGVDPVARDMFWQLMVDLArqDRVTIFISTHFMNEAER-CDRISLMHAGKVLASDTPQAL 494
Cdd:PRK14271 180 VNPEVLLLDEPTSALDPTTTEKIEEFIRSLA--DRLTVIIVTHNLAQAARiSDRAALFFDGRLVEEGPTEQL 249
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
14-204 |
6.90e-13 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 69.04 E-value: 6.90e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 14 LLENVGQQYGATIALRDISLAIPARRMVGLIGPDGVGKSSLLSLIAGARAIEQGNVMVLGGDMrdvhHRRDVCPKIAWMP 93
Cdd:PRK10584 12 LKKSVGQGEHELSILTGVELVVKRGETIALIGESGSGKSTLLAILAGLDDGSSGEVSLVGQPL----HQMDEEARAKLRA 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 94 QGLGK-----NLYHTLSVYENVDFFARLFGHDKAERELRINELLQSTGLAPFRDRPAGKLSGGMKQKLGLCCALIHDPQL 168
Cdd:PRK10584 88 KHVGFvfqsfMLIPTLNALENVELPALLRGESSRQSRNGAKALLEQLGLGKRLDHLPAQLSGGEQQRVALARAFNGRPDV 167
|
170 180 190
....*....|....*....|....*....|....*.
gi 1820369315 169 LILDEPTTGVDPLSRAQFWELIDSIRQRQPEMSVLV 204
Cdd:PRK10584 168 LFADEPTGNLDRQTGDKIADLLFSLNREHGTTLILV 203
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
27-235 |
9.14e-13 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 70.26 E-value: 9.14e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 27 ALRDISLAIPARRMVGLIGPDGVGKSSLLSLIAGARAIEQGNVMVlgGDMRDVHHRRDVCPKIAWMPQGLG--KNLYHTL 104
Cdd:PRK13631 41 ALNNISYTFEKNKIYFIIGNSGSGKSTLVTHFNGLIKSKYGTIQV--GDIYIGDKKNNHELITNPYSKKIKnfKELRRRV 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 105 S--------------VYENVDFFARLFGHDKAERELRINELLQSTGL-APFRDRPAGKLSGGMKQKLGLCCALIHDPQLL 169
Cdd:PRK13631 119 SmvfqfpeyqlfkdtIEKDIMFGPVALGVKKSEAKKLAKFYLNKMGLdDSYLERSPFGLSGGQKRRVAIAGILAIQPEIL 198
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1820369315 170 ILDEPTTGVDPLSRAQFWELI-DSIRQRQpemSVLVATAYMEEA-ERFDWLVAMNAGEVLATGSAAEL 235
Cdd:PRK13631 199 IFDEPTAGLDPKGEHEMMQLIlDAKANNK---TVFVITHTMEHVlEVADEVIVMDKGKILKTGTPYEI 263
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
13-196 |
1.37e-12 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 71.68 E-value: 1.37e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 13 ALLE--NVGQQY----GATIALRDISLAIPARRMVGLIGPDGVGKSSLLSLI-------AGARAIEQGNVMVLGGD---- 75
Cdd:PRK10535 3 ALLElkDIRRSYpsgeEQVEVLKGISLDIYAGEMVAIVGASGSGKSTLMNILgcldkptSGTYRVAGQDVATLDADalaq 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 76 MRDVHHrrdvcpkiawmpqGLGKNLYHTLS---VYENVDFFARLFGHDKAERELRINELLQSTGLAPFRDRPAGKLSGGM 152
Cdd:PRK10535 83 LRREHF-------------GFIFQRYHLLShltAAQNVEVPAVYAGLERKQRLLRAQELLQRLGLEDRVEYQPSQLSGGQ 149
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1820369315 153 KQKLGLCCALIHDPQLLILDEPTTGVDPLSRAQFWELIDSIRQR 196
Cdd:PRK10535 150 QQRVSIARALMNGGQVILADEPTGALDSHSGEEVMAILHQLRDR 193
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
22-240 |
1.50e-12 |
|
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The amino terminal domain (pfam03412) processes the N-terminal leader peptide from the bacteriocin while C-terminal domains resemble ABC transporter membrane protein and ATP-binding cassette domain. In general, bacteriocins are agents which are responsible for killing or inhibiting the closely related species or even different strains of the same species. Bacteriocins are usually encoded by bacterial plasmids. Bacteriocins are named after the species and hence in literature one encounters various names e.g., leucocin from Leuconostic geldium; pedicocin from Pedicoccus acidilactici; sakacin from Lactobacillus sake etc. [Protein fate, Protein and peptide secretion and trafficking, Protein fate, Protein modification and repair, Transport and binding proteins, Other]
Pssm-ID: 130261 [Multi-domain] Cd Length: 708 Bit Score: 71.31 E-value: 1.50e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 22 YGATIaLRDISLAIPARRMVGLIGPDGVGKSSLLSLIAGARAIEQGNVMVLGGDMRDV--HHRRDVcpkIAWMPQglgKN 99
Cdd:TIGR01193 485 YGSNI-LSDISLTIKMNSKTTIVGMSGSGKSTLAKLLVGFFQARSGEILLNGFSLKDIdrHTLRQF---INYLPQ---EP 557
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 100 LYHTLSVYENVdffarLFGhdkAERELRINELLQSTGLAPFRD--------------RPAGKLSGGMKQKLGLCCALIHD 165
Cdd:TIGR01193 558 YIFSGSILENL-----LLG---AKENVSQDEIWAACEIAEIKDdienmplgyqtelsEEGSSISGGQKQRIALARALLTD 629
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1820369315 166 PQLLILDEPTTGVDPLSRAQfweLIDSIRQRQPEMSVLVATAyMEEAERFDWLVAMNAGEVLATGSAAELKAQTG 240
Cdd:TIGR01193 630 SKVLILDESTSNLDTITEKK---IVNNLLNLQDKTIIFVAHR-LSVAKQSDKIIVLDHGKIIEQGSHDELLDRNG 700
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
20-196 |
1.59e-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: 67.84 E-value: 1.59e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 20 QQYGATI-ALRDISLAIPARRMVGLIGPDGVGKSSLLSLIAGARAIEQGNVMVL-GGDMRDVHH---------RRDVcpk 88
Cdd:COG4778 18 LQGGKRLpVLDGVSFSVAAGECVALTGPSGAGKSTLLKCIYGNYLPDSGSILVRhDGGWVDLAQaspreilalRRRT--- 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 89 IAWMPQGLgknlyHTL---SVYENVDFFARLFGHDKAERELRINELLQSTGLaPFR--DRPAGKLSGGMKQKLGLCCALI 163
Cdd:COG4778 95 IGYVSQFL-----RVIprvSALDVVAEPLLERGVDREEARARARELLARLNL-PERlwDLPPATFSGGEQQRVNIARGFI 168
|
170 180 190
....*....|....*....|....*....|...
gi 1820369315 164 HDPQLLILDEPTTGVDPLSRAQFWELIDSIRQR 196
Cdd:COG4778 169 ADPPLLLLDEPTASLDAANRAVVVELIEEAKAR 201
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
22-439 |
1.82e-12 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 71.13 E-value: 1.82e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 22 YGATIALRDISLAIPARRMVGLIGPDGVGKSSLLSLIAGARAIEQGNVMVlggdMRDV-----------HHRRDVCPKIA 90
Cdd:PRK11147 13 FSDAPLLDNAELHIEDNERVCLVGRNGAGKSTLMKILNGEVLLDDGRIIY----EQDLivarlqqdpprNVEGTVYDFVA 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 91 WMPQGLGKNL--YHTLSvyenvdffaRLFGHDKAEREL--------------------RINELLQSTGLAPfrDRPAGKL 148
Cdd:PRK11147 89 EGIEEQAEYLkrYHDIS---------HLVETDPSEKNLnelaklqeqldhhnlwqlenRINEVLAQLGLDP--DAALSSL 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 149 SGGMKQKLGLCCALIHDPQLLILDEPTTGVDplsraqfwelIDSI--------------------RQRQPEMS------- 201
Cdd:PRK11147 158 SGGWLRKAALGRALVSNPDVLLLDEPTNHLD----------IETIewlegflktfqgsiifishdRSFIRNMAtrivdld 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 202 --VLVA-----TAYM---EEAER--------FDWLVAM---------------NAGEVLAtgsaaeLKA--QTGSQTLEq 246
Cdd:PRK11147 228 rgKLVSypgnyDQYLlekEEALRveelqnaeFDRKLAQeevwirqgikarrtrNEGRVRA------LKAlrRERSERRE- 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 247 afiaLLPEAQRQAHKTvvipprdSREEEIAIEARGLTMRFGNFVAVDHVNFRIARGEIFGFLGSNGCGKSTTMKMLTGLL 326
Cdd:PRK11147 301 ----VMGTAKMQVEEA-------SRSGKIVFEMENVNYQIDGKQLVKDFSAQVQRGDKIALIGPNGCGKTTLLKLMLGQL 369
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 327 PASEGEAwlfgqpvdpkDIATRQRVGYMSQ-AFSLYSELSVRQNLE------------------LHARLFHiPddeiahr 387
Cdd:PRK11147 370 QADSGRI----------HCGTKLEVAYFDQhRAELDPEKTVMDNLAegkqevmvngrprhvlgyLQDFLFH-P------- 431
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|..
gi 1820369315 388 vaemsERFMlTEVKdALPAdlplGIRQRLSLAVAVIHRPEMLILDEPTSGVD 439
Cdd:PRK11147 432 -----KRAM-TPVK-ALSG----GERNRLLLARLFLKPSNLLILDEPTNDLD 472
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
24-226 |
1.90e-12 |
|
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: 67.88 E-value: 1.90e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 24 ATIALRDISLAIPARRMVGLIGPDGVGKSSLLSLIAGARAIEQGNVMVLGGDMRDVHHR--RDVCPKIAWMPQGLGKNLY 101
Cdd:cd03248 26 DTLVLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDGKPISQYEHKylHSKVSLVGQEPVLFARSLQ 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 102 HTLSV-YENVDFFARLFGHDKAERELRINELLQstGLAPFRDRPAGKLSGGMKQKLGLCCALIHDPQLLILDEPTTGVDP 180
Cdd:cd03248 106 DNIAYgLQSCSFECVKEAAQKAHAHSFISELAS--GYDTEVGEKGSQLSGGQKQRVAIARALIRNPQVLILDEATSALDA 183
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1820369315 181 LSRAQFWELIDSIRQRQpemSVLVATAYMEEAERFDWLVAMNAGEV 226
Cdd:cd03248 184 ESEQQVQQALYDWPERR---TVLVIAHRLSTVERADQILVLDGGRI 226
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
279-492 |
2.64e-12 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 68.03 E-value: 2.64e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 279 ARGLTMRFGNFVAVDHVNFRIARGEIFGFLGSNGCGKSTTMKMLTGLLPASEGEAWLFGQPVDPKDIATrqrvgyMSQA- 357
Cdd:PRK11701 9 VRGLTKLYGPRKGCRDVSFDLYPGEVLGIVGESGSGKTTLLNALSARLAPDAGEVHYRMRDGQLRDLYA------LSEAe 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 358 --FSLYSELS-VRQNlelharlfhiPDDEIAHRV---AEMSERFM-----------------LTEVK------DALPADL 408
Cdd:PRK11701 83 rrRLLRTEWGfVHQH----------PRDGLRMQVsagGNIGERLMavgarhygdiratagdwLERVEidaariDDLPTTF 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 409 PLGIRQRLSLAVAVIHRPEMLILDEPTSGVDPVARDMFWQLMVDLARQDRVTIFISTHFMNEAeR--CDRISLMHAGKVL 486
Cdd:PRK11701 153 SGGMQQRLQIARNLVTHPRLVFMDEPTGGLDVSVQARLLDLLRGLVRELGLAVVIVTHDLAVA-RllAHRLLVMKQGRVV 231
|
250
....*....|...
gi 1820369315 487 AS-------DTPQ 492
Cdd:PRK11701 232 ESgltdqvlDDPQ 244
|
|
| CP_lyasePhnK |
TIGR02323 |
phosphonate C-P lyase system protein PhnK; Members of this family are the PhnK protein of C-P ... |
10-230 |
2.94e-12 |
|
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: 67.55 E-value: 2.94e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 10 PPIALLENVGQQYGATIALRDISLAIPARRMVGLIGPDGVGKSSLLSLIAGARAIEQGNVmvlGGDMRDVHHR------- 82
Cdd:TIGR02323 1 KPLLQVSGLSKSYGGGKGCRDVSFDLYPGEVLGIVGESGSGKSTLLGCLAGRLAPDHGTA---TYIMRSGAELelyqlse 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 83 --RDVCPKIAW--MPQGLGKNLYHTLSVYENV-----DFFARLFGHDKAERElrinELLQSTGLAPFR--DRPAgKLSGG 151
Cdd:TIGR02323 78 aeRRRLMRTEWgfVHQNPRDGLRMRVSAGANIgerlmAIGARHYGNIRATAQ----DWLEEVEIDPTRidDLPR-AFSGG 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 152 MKQKLGLCCALIHDPQLLILDEPTTGVDPLSRAQFWELIDSIrQRQPEMSVLVATAYMEEAERF-DWLVAMNAGEVLATG 230
Cdd:TIGR02323 153 MQQRLQIARNLVTRPRLVFMDEPTGGLDVSVQARLLDLLRGL-VRDLGLAVIIVTHDLGVARLLaQRLLVMQQGRVVESG 231
|
|
| ABC2_membrane |
pfam01061 |
ABC-2 type transporter; |
727-877 |
3.31e-12 |
|
ABC-2 type transporter;
Pssm-ID: 426023 [Multi-domain] Cd Length: 204 Bit Score: 66.53 E-value: 3.31e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 727 LLLMMIPAMLSALSVVREKELGSIINLYVTPT-TRSEFLLGKQLPYIVLGMFNFFLLCALSVFVFGVA-HKGSFLTLTLA 804
Cdd:pfam01061 53 SILFNAFSALSGISPVFEKERGVLYRELASPLySPSAYVLAKILSELPLSLLQSLIFLLIVYFMVGLPpSAGRFFLFLLV 132
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1820369315 805 ALLYVTIATGLGLLISTFMKSQIAAIFGTAIITLiPATQFSGMIDPVASLEGPGRWIGQIYPTSHFLTIARGT 877
Cdd:pfam01061 133 LLLTALAASSLGLFISALAPSFEDASQLGPLVLL-PLLLLSGFFIPIDSMPVWWQWIYYLNPLTYAIEALRAN 204
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
28-238 |
3.35e-12 |
|
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular trafficking, secretion, and vesicular transport];
Pssm-ID: 443660 [Multi-domain] Cd Length: 563 Bit Score: 70.16 E-value: 3.35e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 28 LRDISLAIPARRMVGLIGPDGVGKSSLLSLIAGARAIEQGNVMVlggDMRDVHH--RRDVCPKIAWMPQGLGknlyhtL- 104
Cdd:COG4618 348 LRGVSFSLEPGEVLGVIGPSGSGKSTLARLLVGVWPPTAGSVRL---DGADLSQwdREELGRHIGYLPQDVE------Lf 418
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 105 --SVYENVdffARLFGHD-----KAERELRINELLQS------TGLApfrdrPAGK-LSGGMKQKLGLCCALIHDPQLLI 170
Cdd:COG4618 419 dgTIAENI---ARFGDADpekvvAAAKLAGVHEMILRlpdgydTRIG-----EGGArLSGGQRQRIGLARALYGDPRLVV 490
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1820369315 171 LDEPTTGVDPLSRAQFWELIDSIRQRQpeMSVLVAT---AYMEEAerfDWLVAMNAGEVLATGSAAELKAQ 238
Cdd:COG4618 491 LDEPNSNLDDEGEAALAAAIRALKARG--ATVVVIThrpSLLAAV---DKLLVLRDGRVQAFGPRDEVLAR 556
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
15-237 |
3.39e-12 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 67.47 E-value: 3.39e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 15 LENVGQQYGATIALRDISLAIPARRMVGLIGPDGVGKSSLLSLIAGARAIEQGNVMV----------LGGDMRDVHHRRD 84
Cdd:PRK11264 6 VKNLVKKFHGQTVLHGIDLEVKPGEVVAIIGPSGSGKTTLLRCINLLEQPEAGTIRVgditidtarsLSQQKGLIRQLRQ 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 85 vcpKIAWMPQGLgkNLYHTLSVYENV-DFFARLFGHDKAERELRINELLQSTGLAPFRDRPAGKLSGGMKQKLGLCCALI 163
Cdd:PRK11264 86 ---HVGFVFQNF--NLFPHRTVLENIiEGPVIVKGEPKEEATARARELLAKVGLAGKETSYPRRLSGGQQQRVAIARALA 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1820369315 164 HDPQLLILDEPTTGVDPlsrAQFWELIDSIRQRQPEMSVLV-ATAYMEEA-ERFDWLVAMNAGEVLATGSAAELKA 237
Cdd:PRK11264 161 MRPEVILFDEPTSALDP---ELVGEVLNTIRQLAQEKRTMViVTHEMSFArDVADRAIFMDQGRIVEQGPAKALFA 233
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
29-191 |
3.81e-12 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 66.37 E-value: 3.81e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 29 RDISLAIPARRMVGLIGPDGVGKSSLLSLIAGARAIEQGNVMVLGGDM---RDVHHRrdvcpKIAWmpqgLG-----KNL 100
Cdd:PRK13538 18 SGLSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVLWQGEPIrrqRDEYHQ-----DLLY----LGhqpgiKTE 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 101 yhtLSVYENVDFFARLfgHDKAERElRINELLQSTGLAPFRDRPAGKLSGGMKQKLGLCCALIHDPQLLILDEPTTGVDP 180
Cdd:PRK13538 89 ---LTALENLRFYQRL--HGPGDDE-ALWEALAQVGLAGFEDVPVRQLSAGQQRRVALARLWLTRAPLWILDEPFTAIDK 162
|
170
....*....|.
gi 1820369315 181 LSRAQFWELID 191
Cdd:PRK13538 163 QGVARLEALLA 173
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
15-240 |
4.23e-12 |
|
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: 66.87 E-value: 4.23e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 15 LENVGQQYGAT-IALRDISLAIPARRMVGLIGPDGVGKSSLLSLIAGARAIEQGNVMVLGGDMRDVHH---RRdvcpKIA 90
Cdd:cd03253 3 FENVTFAYDPGrPVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDGQDIREVTLdslRR----AIG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 91 WMPQGLgkNLYHTlSVYENVDFfARLFGHD----KAERELRINELLQSTglaPFR-DRPAG----KLSGGMKQKLGLCCA 161
Cdd:cd03253 79 VVPQDT--VLFND-TIGYNIRY-GRPDATDeeviEAAKAAQIHDKIMRF---PDGyDTIVGerglKLSGGEKQRVAIARA 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1820369315 162 LIHDPQLLILDEPTTGVDPLSRAQFWELIDSIRQRQpemSVLVATAYMEEAERFDWLVAMNAGEVLATGSAAELKAQTG 240
Cdd:cd03253 152 ILKNPPILLLDEATSALDTHTEREIQAALRDVSKGR---TTIVIAHRLSTIVNADKIIVLKDGRIVERGTHEELLAKGG 227
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
291-498 |
4.84e-12 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 69.26 E-value: 4.84e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 291 AVDHVNFRIARGEIFGFLGSNGCGKSTTMKMLTGLLPASEGEAWLFGQPVD---PKDiATRQRVGYMSQAFSLYSELSVR 367
Cdd:PRK10762 19 ALSGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSILYLGKEVTfngPKS-SQEAGIGIIHQELNLIPQLTIA 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 368 QNL----ELHARLFHIPDDEIAHRVAEMSERFMLTEVKDALPADLPLGIRQRLSLAVAVIHRPEMLILDEPTSGVDPVAR 443
Cdd:PRK10762 98 ENIflgrEFVNRFGRIDWKKMYAEADKLLARLNLRFSSDKLVGELSIGEQQMVEIAKVLSFESKVIIMDEPTDALTDTET 177
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1820369315 444 DMFWQLMVDLARQDRVTIFIStHFMNEA-ERCDRISLMHAGKVLASDTPQALVEQR 498
Cdd:PRK10762 178 ESLFRVIRELKSQGRGIVYIS-HRLKEIfEICDDVTVFRDGQFIAEREVADLTEDS 232
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
20-246 |
5.33e-12 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 66.92 E-value: 5.33e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 20 QQYGATIALRDISLAIPARRMVGLIGPDGVGKSSLLSLIAGARAIEQGNVMVLGGDMR------------DVHHRRDVCP 87
Cdd:PRK10619 13 KRYGEHEVLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNGQTINlvrdkdgqlkvaDKNQLRLLRT 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 88 KIAWMPQGLgkNLYHTLSVYENV-DFFARLFGHDKAERELRINELLQSTGLApfrDRPAGK----LSGGMKQKLGLCCAL 162
Cdd:PRK10619 93 RLTMVFQHF--NLWSHMTVLENVmEAPIQVLGLSKQEARERAVKYLAKVGID---ERAQGKypvhLSGGQQQRVSIARAL 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 163 IHDPQLLILDEPTTGVDPLSRAQFWELIDSIRQRQPEMsvLVATAYMEEAERF-DWLVAMNAGEVLATGSAAELKAQTGS 241
Cdd:PRK10619 168 AMEPEVLLFDEPTSALDPELVGEVLRIMQQLAEEGKTM--VVVTHEMGFARHVsSHVIFLHQGKIEEEGAPEQLFGNPQS 245
|
....*
gi 1820369315 242 QTLEQ 246
Cdd:PRK10619 246 PRLQQ 250
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
7-214 |
5.66e-12 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 67.43 E-value: 5.66e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 7 DTSPPIALLENVGQQYGATIALRDISLAIPARRMVGLIGPDGVGKSSLLSL-------IAGARAieQGNVMvLGGdmRDV 79
Cdd:PRK14271 16 DAAAPAMAAVNLTLGFAGKTVLDQVSMGFPARAVTSLMGPTGSGKTTFLRTlnrmndkVSGYRY--SGDVL-LGG--RSI 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 80 HHRRDVCPKIAWMPQGLGKNLYHTLSVYENVdfFARLFGHDKAER-ELR--INELLQSTGL-APFRDRPAG---KLSGGM 152
Cdd:PRK14271 91 FNYRDVLEFRRRVGMLFQRPNPFPMSIMDNV--LAGVRAHKLVPRkEFRgvAQARLTEVGLwDAVKDRLSDspfRLSGGQ 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1820369315 153 KQKLGLCCALIHDPQLLILDEPTTGVDPLSRAQFWELIDSIRQRqpeMSVLVATAYMEEAER 214
Cdd:PRK14271 169 QQLLCLARTLAVNPEVLLLDEPTSALDPTTTEKIEEFIRSLADR---LTVIIVTHNLAQAAR 227
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
27-237 |
7.04e-12 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 66.74 E-value: 7.04e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 27 ALRDISLAIPARRMVGLIGPDGVGKSSLLSLIAGARAIEQGNVMVLGGDMR--DVHHRRDvcpKIAWMPQGLGKNLYHTL 104
Cdd:PRK15112 28 AVKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDHPLHfgDYSYRSQ---RIRMIFQDPSTSLNPRQ 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 105 SVYENVDFFARL-FGHDKAERELRINELLQSTGLAPfrDRPA---GKLSGGMKQKLGLCCALIHDPQLLILDEPTTGVDP 180
Cdd:PRK15112 105 RISQILDFPLRLnTDLEPEQREKQIIETLRQVGLLP--DHASyypHMLAPGQKQRLGLARALILRPKVIIADEALASLDM 182
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1820369315 181 LSRAQFWELIDSIRQRQpEMSVLVATAYMEEAERF-DWLVAMNAGEVLATGSAAELKA 237
Cdd:PRK15112 183 SMRSQLINLMLELQEKQ-GISYIYVTQHLGMMKHIsDQVLVMHQGEVVERGSTADVLA 239
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
27-225 |
8.29e-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: 65.18 E-value: 8.29e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 27 ALRDISLAIPARRMVGLIGPDGVGKSSLLSLIAGARAIEQGNVMVLGgdmrdvhhRRDVCPKIAWMPQGlgknlyhtlSV 106
Cdd:cd03250 20 TLKDINLEVPKGELVAIVGPVGSGKSSLLSALLGELEKLSGSVSVPG--------SIAYVSQEPWIQNG---------TI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 107 YENVdffarLFGHDkaERELRINELLQSTGLAP-FRDRPAG----------KLSGGMKQKLGLCCALIHDPQLLILDEPT 175
Cdd:cd03250 83 RENI-----LFGKP--FDEERYEKVIKACALEPdLEILPDGdlteigekgiNLSGGQKQRISLARAVYSDADIYLLDDPL 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1820369315 176 TGVDPLSRAQFWEliDSIRqrqPEMS----VLVATAYMEEAERFDWLVAMNAGE 225
Cdd:cd03250 156 SAVDAHVGRHIFE--NCIL---GLLLnnktRILVTHQLQLLPHADQIVVLDNGR 204
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
273-486 |
9.04e-12 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 66.34 E-value: 9.04e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 273 EEIaIEARGLTMRFGNFVAVDHVNFRIARGEIFGFLGSNGCGKSTTMKMLT---GLLP-------ASEGEAWLFGQPVDP 342
Cdd:PRK14239 3 EPI-LQVSDLSVYYNKKKALNSVSLDFYPNEITALIGPSGSGKSTLLRSINrmnDLNPevtitgsIVYNGHNIYSPRTDT 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 343 KDIatRQRVGYMSQAFSLYSeLSVRQNLELHARLFHIPDDEIAHRVAEMSER--FMLTEVKDALPAD---LPLGIRQRLS 417
Cdd:PRK14239 82 VDL--RKEIGMVFQQPNPFP-MSIYENVVYGLRLKGIKDKQVLDEAVEKSLKgaSIWDEVKDRLHDSalgLSGGQQQRVC 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 418 LAVAVIHRPEMLILDEPTSGVDPVARDMFWQLMVDLarQDRVTIFISTHFMNEAER-CDRISLMHAGKVL 486
Cdd:PRK14239 159 IARVLATSPKIILLDEPTSALDPISAGKIEETLLGL--KDDYTMLLVTRSMQQASRiSDRTGFFLDGDLI 226
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
308-483 |
9.24e-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: 9.24e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 308 LGSNGCGKSTTMKMLTGLLPAS--EGEAWLFGQPvdpKDIATRQRVGYMSQAFSLYSELSVRQNLELHARLfhipddeia 385
Cdd:cd03232 39 MGESGAGKTTLLDVLAGRKTAGviTGEILINGRP---LDKNFQRSTGYVEQQDVHSPNLTVREALRFSALL--------- 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 386 hrvaemseRfmltevkdalpaDLPLGIRQRLSLAVAVIHRPEMLILDEPTSGVDPVARDMFWQLMVDLARQDRvTIFIST 465
Cdd:cd03232 107 --------R------------GLSVEQRKRLTIGVELAAKPSILFLDEPTSGLDSQAAYNIVRFLKKLADSGQ-AILCTI 165
|
170 180
....*....|....*....|
gi 1820369315 466 HFMNEA--ERCDRISLMHAG 483
Cdd:cd03232 166 HQPSASifEKFDRLLLLKRG 185
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
23-196 |
9.44e-12 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 68.58 E-value: 9.44e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 23 GATIALRDISLAIPARRMVGLIGPDGVGKSS----LLSLIAgaraiEQGNVMVlggDMRDVHH--RRDVCP---KIAWMP 93
Cdd:PRK15134 297 DHNVVVKNISFTLRPGETLGLVGESGSGKSTtglaLLRLIN-----SQGEIWF---DGQPLHNlnRRQLLPvrhRIQVVF 368
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 94 QGLGKNLYHTLSVYENVDFFARLfgHDK----AERELRINELLQSTGLAP-FRDRPAGKLSGGMKQKLGLCCALIHDPQL 168
Cdd:PRK15134 369 QDPNSSLNPRLNVLQIIEEGLRV--HQPtlsaAQREQQVIAVMEEVGLDPeTRHRYPAEFSGGQRQRIAIARALILKPSL 446
|
170 180
....*....|....*....|....*...
gi 1820369315 169 LILDEPTTGVDPLSRAQFWELIDSIRQR 196
Cdd:PRK15134 447 IILDEPTSSLDKTVQAQILALLKSLQQK 474
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
276-522 |
9.76e-12 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 68.83 E-value: 9.76e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 276 AIEARGLTMRFGNFV-AVDHVNFRIARGEIFGFLGSNGCGKSTTMKMLTGLLPASEGEAwlfgqPVDPKDIAT------R 348
Cdd:PRK13657 334 AVEFDDVSFSYDNSRqGVEDVSFEAKPGQTVAIVGPTGAGKSTLINLLQRVFDPQSGRI-----LIDGTDIRTvtraslR 408
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 349 QRVGYMSQAFSLYSElSVRQNLELHArlfhiPD--DEIAHRVAEMSE--RFMLTEVK--DALPAD----LPLGIRQRLSL 418
Cdd:PRK13657 409 RNIAVVFQDAGLFNR-SIEDNIRVGR-----PDatDEEMRAAAERAQahDFIERKPDgyDTVVGErgrqLSGGERQRLAI 482
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 419 AVAVIHRPEMLILDEPTSGVDpVARDMFWQLMVDLARQDRVTiFISTHFMNEAERCDRISLMHAGKVLASDTPQALVEQR 498
Cdd:PRK13657 483 ARALLKDPPILILDEATSALD-VETEAKVKAALDELMKGRTT-FIIAHRLSTVRNADRILVFDNGRVVESGSFDELVARG 560
|
250 260
....*....|....*....|....*.
gi 1820369315 499 G--AASLEEAFIAwLKEAQPSSPVPE 522
Cdd:PRK13657 561 GrfAALLRAQGML-QEDERRKQPAAE 585
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
277-486 |
1.29e-11 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 66.65 E-value: 1.29e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 277 IEARGLTMRFGN-----FVAVDHVNFRIARGEIFGFLGSNGCGKSTTMKMLTGLLPASEGEA-WLFGQPVDPKDIAT--- 347
Cdd:PRK13651 3 IKVKNIVKIFNKklpteLKALDNVSVEINQGEFIAIIGQTGSGKTTFIEHLNALLLPDTGTIeWIFKDEKNKKKTKEkek 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 348 ---------------------RQRVGYMSQaFSLYS--ELSVRQNLELHARLFHIPDDEIAHRVAEMSERFMLTEvkDAL 404
Cdd:PRK13651 83 vleklviqktrfkkikkikeiRRRVGVVFQ-FAEYQlfEQTIEKDIIFGPVSMGVSKEEAKKRAAKYIELVGLDE--SYL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 405 ---PADLPLGIRQRLSLAVAVIHRPEMLILDEPTSGVDPVARDMFWQLMVDLARQDRvTIFISTHFMNEA-ERCDRISLM 480
Cdd:PRK13651 160 qrsPFELSGGQKRRVALAGILAMEPDFLVFDEPTAGLDPQGVKEILEIFDNLNKQGK-TIILVTHDLDNVlEWTKRTIFF 238
|
....*.
gi 1820369315 481 HAGKVL 486
Cdd:PRK13651 239 KDGKII 244
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
11-238 |
1.43e-11 |
|
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: 67.91 E-value: 1.43e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 11 PIALLENVGQQY-----GATIALRDISLAIPARRMVGLIGPDGVGKSSLLSLIAGARAIEQGNVMVLGG----DMRD--V 79
Cdd:TIGR03269 278 PIIKVRNVSKRYisvdrGVVKAVDNVSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGEVNVRVGdewvDMTKpgP 357
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 80 HHRRDVCPKIAWMPQGLGknLYHTLSVYENV---------DFFARL----------FGHDKAERELrinellqstglapf 140
Cdd:TIGR03269 358 DGRGRAKRYIGILHQEYD--LYPHRTVLDNLteaiglelpDELARMkavitlkmvgFDEEKAEEIL-------------- 421
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 141 rDRPAGKLSGGMKQKLGLCCALIHDPQLLILDEPTTGVDPLSRAQFWELIDSIRQRQPEMSVLVATAYMEEAERFDWLVA 220
Cdd:TIGR03269 422 -DKYPDELSEGERHRVALAQVLIKEPRIVILDEPTGTMDPITKVDVTHSILKAREEMEQTFIIVSHDMDFVLDVCDRAAL 500
|
250
....*....|....*...
gi 1820369315 221 MNAGEVLATGSAAELKAQ 238
Cdd:TIGR03269 501 MRDGKIVKIGDPEEIVEE 518
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
257-466 |
1.96e-11 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 64.59 E-value: 1.96e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 257 RQAHKTVVIPPRDSREEEIAIEARGLTMRFGNFVAVDHVNFRIARGEIFGFLGSNGCGKSTTMKMLTGLLPASEGEAWlf 336
Cdd:COG2401 11 MRVTKVYSSVLDLSERVAIVLEAFGVELRVVERYVLRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGALKGTPVAGC-- 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 337 gqpVDPKDIatrqrvgymsqafSLYSELSVRQNLelhARLFHIPDD-EIAHRVAEMSERFMLtevkdALPADLPLGIRQR 415
Cdd:COG2401 89 ---VDVPDN-------------QFGREASLIDAI---GRKGDFKDAvELLNAVGLSDAVLWL-----RRFKELSTGQKFR 144
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1820369315 416 LSLAVAVIHRPEMLILDEPTSGVDP-----VARDmfwqlMVDLARQDRVTIFISTH 466
Cdd:COG2401 145 FRLALLLAERPKLLVIDEFCSHLDRqtakrVARN-----LQKLARRAGITLVVATH 195
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
28-240 |
2.24e-11 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 67.44 E-value: 2.24e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 28 LRDISLAIPARRMVGLIGPDGVGKSSLLSLIAGARAIEQGNVMVLGGDMRDVHHR--RDVCPKIAWMPQGLGKnlyhtlS 105
Cdd:PRK10790 357 LQNINLSVPSRGFVALVGHTGSGKSTLASLLMGYYPLTEGEIRLDGRPLSSLSHSvlRQGVAMVQQDPVVLAD------T 430
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 106 VYENVDffarlFGHDKAERelRINELLQSTGLAPF-RDRPAG----------KLSGGMKQKLGLCCALIHDPQLLILDEP 174
Cdd:PRK10790 431 FLANVT-----LGRDISEE--QVWQALETVQLAELaRSLPDGlytplgeqgnNLSVGQKQLLALARVLVQTPQILILDEA 503
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 175 TTGVDPLSRAQFWELIDSIRQRqpemSVLVATAY----MEEAerfDWLVAMNAGEVLATGSAAELKAQTG 240
Cdd:PRK10790 504 TANIDSGTEQAIQQALAAVREH----TTLVVIAHrlstIVEA---DTILVLHRGQAVEQGTHQQLLAAQG 566
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
118-254 |
3.14e-11 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 65.53 E-value: 3.14e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 118 GHDKAERELRINELLQSTGLAPFRDR----PAgKLSGGMKQKLGLCCALIHDPQLLILDEPTTGVDPLSRAQFWELIDSI 193
Cdd:PRK11022 121 GGNKKTRRQRAIDLLNQVGIPDPASRldvyPH-QLSGGMSQRVMIAMAIACRPKLLIADEPTTALDVTIQAQIIELLLEL 199
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1820369315 194 RQRQPEMSVLVATAYMEEAERFDWLVAMNAGEVLATGSAAEL-KAQTGSQTleQAFIALLPE 254
Cdd:PRK11022 200 QQKENMALVLITHDLALVAEAAHKIIVMYAGQVVETGKAHDIfRAPRHPYT--QALLRALPE 259
|
|
| nickel_nikD |
TIGR02770 |
nickel import ATP-binding protein NikD; This family represents the NikD subunit of a ... |
30-235 |
3.86e-11 |
|
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: 63.93 E-value: 3.86e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 30 DISLAIPARRMVGLIGPDGVGKS----SLLSLIAGARAIEQGNVMVLGGDMRDVHHR-RDVC-----PKIAWMP-QGLGK 98
Cdd:TIGR02770 4 DLNLSLKRGEVLALVGESGSGKSltclAILGLLPPGLTQTSGEILLDGRPLLPLSIRgRHIAtimqnPRTAFNPlFTMGN 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 99 NLYHTLsvyenvdffaRLFGHDKAERELRINELLQSTGLA---------PFrdrpagKLSGGMKQKLGLCCALIHDPQLL 169
Cdd:TIGR02770 84 HAIETL----------RSLGKLSKQARALILEALEAVGLPdpeevlkkyPF------QLSGGMLQRVMIALALLLEPPFL 147
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1820369315 170 ILDEPTTGVDPLSRAQFWELIDSIRQRQpEMSVLVATAYMEE-AERFDWLVAMNAGEVLATGSAAEL 235
Cdd:TIGR02770 148 IADEPTTDLDVVNQARVLKLLRELRQLF-GTGILLITHDLGVvARIADEVAVMDDGRIVERGTVKEI 213
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
282-488 |
6.19e-11 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 64.76 E-value: 6.19e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 282 LTMRFGN----FVAVDHVNFRIARGEIFGFLGSNGCGKSTTMKMLTGLL--PAS-EGEAWLFGQpVDPKDIATRQR---- 350
Cdd:PRK11022 9 LSVHFGDesapFRAVDRISYSVKQGEVVGIVGESGSGKSVSSLAIMGLIdyPGRvMAEKLEFNG-QDLQRISEKERrnlv 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 351 ---VGYMSQ------------AFSLYSELSVRQNLELHAR---------LFHIPDDeiAHRVaemserfmltevkDALPA 406
Cdd:PRK11022 88 gaeVAMIFQdpmtslnpcytvGFQIMEAIKVHQGGNKKTRrqraidllnQVGIPDP--ASRL-------------DVYPH 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 407 DLPLGIRQRLSLAVAVIHRPEMLILDEPTSGVDPVARDMFWQLMVDLARQDRVTIFISTHFMN-EAERCDRISLMHAGKV 485
Cdd:PRK11022 153 QLSGGMSQRVMIAMAIACRPKLLIADEPTTALDVTIQAQIIELLLELQQKENMALVLITHDLAlVAEAAHKIIVMYAGQV 232
|
...
gi 1820369315 486 LAS 488
Cdd:PRK11022 233 VET 235
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
22-182 |
8.02e-11 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 62.27 E-value: 8.02e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 22 YGATIALRDISLAIPARRMVGLIGPDGVGKSSLLSLIAGARAIEQGNVMVLGGDMRdvhhrRDVCP---KIAWMPQGLGK 98
Cdd:PRK13540 11 YHDQPLLQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEILFERQSIK-----KDLCTyqkQLCFVGHRSGI 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 99 NLYHTLSvyENVdffarLFGHDKAERELRINELLQSTGLAPFRDRPAGKLSGGMKQKLGLCCALIHDPQLLILDEPTTGV 178
Cdd:PRK13540 86 NPYLTLR--ENC-----LYDIHFSPGAVGITELCRLFSLEHLIDYPCGLLSSGQKRQVALLRLWMSKAKLWLLDEPLVAL 158
|
....
gi 1820369315 179 DPLS 182
Cdd:PRK13540 159 DELS 162
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
23-569 |
1.05e-10 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 65.58 E-value: 1.05e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 23 GATIALRDISLAIPARRMVGLIGPDGVGKSSLLSLIAGARAIEQGNVMVLGGdmrdvhhrrdvcPKIAWMPQGL------ 96
Cdd:PRK10636 12 GVRVLLDNATATINPGQKVGLVGKNGCGKSTLLALLKNEISADGGSYTFPGN------------WQLAWVNQETpalpqp 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 97 -------GKNLYHTLS-----VYENVDFFARLFGHDKAER------ELRINELLQSTGLA-PFRDRPAGKLSGGMKQKLG 157
Cdd:PRK10636 80 aleyvidGDREYRQLEaqlhdANERNDGHAIATIHGKLDAidawtiRSRAASLLHGLGFSnEQLERPVSDFSGGWRMRLN 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 158 LCCALIHDPQLLILDEPTTGVDplSRAQFW----------ELIDSIRQRQPEMSVLVATAYMEEAERFDWLVAMNAGEV- 226
Cdd:PRK10636 160 LAQALICRSDLLLLDEPTNHLD--LDAVIWlekwlksyqgTLILISHDRDFLDPIVDKIIHIEQQSLFEYTGNYSSFEVq 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 227 ----LATGSA---------AEL-------KAQTGSQTLEQAFIALLPEAQRQAHKTVVIPPRDSREEEIAIEARGLTMR- 285
Cdd:PRK10636 238 ratrLAQQQAmyesqqervAHLqsyidrfRAKATKAKQAQSRIKMLERMELIAPAHVDNPFHFSFRAPESLPNPLLKMEk 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 286 ----FGNFVAVDHVNFRIARGEIFGFLGSNGCGKSTTMKMLTGLLPASEGEAWLfgqpvdPKDIatrqRVGYMSQ---AF 358
Cdd:PRK10636 318 vsagYGDRIILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELAPVSGEIGL------AKGI----KLGYFAQhqlEF 387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 359 sLYSELSVRQNL------ELHARL------FHIPDDeiahRVAEMSERFMLTEvkdalpadlplgiRQRLSLAVAVIHRP 426
Cdd:PRK10636 388 -LRADESPLQHLarlapqELEQKLrdylggFGFQGD----KVTEETRRFSGGE-------------KARLVLALIVWQRP 449
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 427 EMLILDEPTSGVDPVARDMFWQLMVD------LARQDRVTIFISThfmneaercDRISLMHAGKVLASDtpqalveqrga 500
Cdd:PRK10636 450 NLLLLDEPTNHLDLDMRQALTEALIDfegalvVVSHDRHLLRSTT---------DDLYLVHDGKVEPFD----------- 509
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1820369315 501 ASLEEaFIAWLKEAQPSSPVPEDPTSAVASHSEHTAPRQafslrrlfsySRREAlELRR--DPVRSTLALL 569
Cdd:PRK10636 510 GDLED-YQQWLSDVQKQENQTDEAPKENNANSAQARKDQ----------KRREA-ELRTqtQPLRKEIARL 568
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
25-240 |
1.08e-10 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 65.43 E-value: 1.08e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 25 TIALRDISLAIPARRMVGLIGPDGVGKSSLLSLIAGARAIEQGNVMVLGGDMRDvHHRRDVCPKIAWMPQGLgkNLYH-T 103
Cdd:PRK11176 356 VPALRNINFKIPAGKTVALVGRSGSGKSTIANLLTRFYDIDEGEILLDGHDLRD-YTLASLRNQVALVSQNV--HLFNdT 432
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 104 LS---VYENVDFFARlfghDKAERELR-------INELLQstGLapfrDRPAGK----LSGGMKQKLGLCCALIHDPQLL 169
Cdd:PRK11176 433 IAnniAYARTEQYSR----EQIEEAARmayamdfINKMDN--GL----DTVIGEngvlLSGGQRQRIAIARALLRDSPIL 502
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1820369315 170 ILDEPTTGVDPLSRAQFWELIDSIrqrQPEMSVLVATAYMEEAERFDWLVAMNAGEVLATGSAAELKAQTG 240
Cdd:PRK11176 503 ILDEATSALDTESERAIQAALDEL---QKNRTSLVIAHRLSTIEKADEILVVEDGEIVERGTHAELLAQNG 570
|
|
| ABC2_membrane_2 |
pfam12679 |
ABC-2 family transporter protein; This family is related to the ABC-2 membrane transporter ... |
727-875 |
1.24e-10 |
|
ABC-2 family transporter protein; This family is related to the ABC-2 membrane transporter family.
Pssm-ID: 403774 [Multi-domain] Cd Length: 281 Bit Score: 63.18 E-value: 1.24e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 727 LLLMMIPAMLSALSVVREKELGSIINLYVTPTTRSEFLLGKQLPYIVLGMFNffLLCALSVFVFGVAHKGSFLTLTLAAL 806
Cdd:pfam12679 76 FLIPVIAALLGADAIAGERERGTIELLLSLPVSRSEILLGKFIGRLAIGLIL--AVALLAGVLLALAITLALGDPLDLGD 153
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 807 LYVTIA-----------TGLGLLISTFMKSQIAAIFGTAIITLIPATQFSGMIDPVASLEGPGRWIGQIYPTSHFLTIAR 875
Cdd:pfam12679 154 LLLLVAasvllalalvfLSIGLLLSSVARSTRTAAAIALGLFFVLAILWPIVLYGLAELLAGPAPPQELLDFLLFLNPTS 233
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
254-500 |
1.64e-10 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 64.87 E-value: 1.64e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 254 EAQRQAHKTVvipprdSREEEIAIEARGLTMRF--GNfVAVDHVNFRIARGEIFGFLGSNGCGKSTTMKMLTGLLPaSEG 331
Cdd:PRK11174 333 AHPQQGEKEL------ASNDPVTIEAEDLEILSpdGK-TLAGPLNFTLPAGQRIALVGPSGAGKTSLLNALLGFLP-YQG 404
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 332 EAWLFGQPVDPKDIAT-RQRVGYMSQAFSLYsELSVRQNLELHArlFHIPDDEIAH-----RVAEMSERFML---TEVKD 402
Cdd:PRK11174 405 SLKINGIELRELDPESwRKHLSWVGQNPQLP-HGTLRDNVLLGN--PDASDEQLQQalenaWVSEFLPLLPQgldTPIGD 481
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 403 AlPADLPLGIRQRLSLAVAVIHRPEMLILDEPTSGVDPVARDmfwQLMVDL--ARQDRVTIFIsTHFMNEAERCDRISLM 480
Cdd:PRK11174 482 Q-AAGLSVGQAQRLALARALLQPCQLLLLDEPTASLDAHSEQ---LVMQALnaASRRQTTLMV-THQLEDLAQWDQIWVM 556
|
250 260
....*....|....*....|
gi 1820369315 481 HAGKVLASDTPQALVEQRGA 500
Cdd:PRK11174 557 QDGQIVQQGDYAELSQAGGL 576
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
306-439 |
1.75e-10 |
|
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: 64.57 E-value: 1.75e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 306 GFLGSNGCGKSTTMKMLTGLLPASEGEAWLfgQPvdpkDIatrqRVGYMSQAFSLYSELSVRQNLE--------LHARLF 377
Cdd:TIGR03719 35 GVLGLNGAGKSTLLRIMAGVDKDFNGEARP--QP----GI----KVGYLPQEPQLDPTKTVRENVEegvaeikdALDRFN 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 378 HI------PDDEIAHRVAEMSErfmLTEVKDAL-------------------PADLPL-----GIRQRLSLAVAVIHRPE 427
Cdd:TIGR03719 105 EIsakyaePDADFDKLAAEQAE---LQEIIDAAdawdldsqleiamdalrcpPWDADVtklsgGERRRVALCRLLLSKPD 181
|
170
....*....|..
gi 1820369315 428 MLILDEPTSGVD 439
Cdd:TIGR03719 182 MLLLDEPTNHLD 193
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
31-248 |
1.93e-10 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 62.26 E-value: 1.93e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 31 ISLAIPARRMVGLIGPDGVGKSSLLSLIAGARAIEqGNVMVLGGDMRD------VHHRRDVC----PKIAwMPqglgknL 100
Cdd:PRK03695 15 LSAEVRAGEILHLVGPNGAGKSTLLARMAGLLPGS-GSIQFAGQPLEAwsaaelARHRAYLSqqqtPPFA-MP------V 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 101 YHTLSvyenvdffarLFGHDKA---ERELRINELLQSTGLAPFRDRPAGKLSGGMKQKLGLCCAL--IH-----DPQLLI 170
Cdd:PRK03695 87 FQYLT----------LHQPDKTrteAVASALNEVAEALGLDDKLGRSVNQLSGGEWQRVRLAAVVlqVWpdinpAGQLLL 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 171 LDEPTTGVDPLSRAQFWELIDSIRQRQpeMSVLVAT----AYMEEAERFdWLvaMNAGEVLATGSAAE-LKAQTGSQTLE 245
Cdd:PRK03695 157 LDEPMNSLDVAQQAALDRLLSELCQQG--IAVVMSShdlnHTLRHADRV-WL--LKQGKLLASGRRDEvLTPENLAQVFG 231
|
...
gi 1820369315 246 QAF 248
Cdd:PRK03695 232 VNF 234
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
28-241 |
1.97e-10 |
|
multi drug resistance-associated protein (MRP); This model describes multi drug resistance-associated protein (MRP) in eukaryotes. The multidrug resistance-associated protein is an integral membrane protein that causes multidrug resistance when overexpressed in mammalian cells. It belongs to ABC transporter superfamily. The protein topology and function was experimentally demonstrated by epitope tagging and immunofluorescence. Insertion of tags in the critical regions associated with drug efflux, abrogated its function. The C-terminal domain seem to highly conserved. [Transport and binding proteins, Other]
Pssm-ID: 188098 [Multi-domain] Cd Length: 1522 Bit Score: 64.97 E-value: 1.97e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 28 LRDISLAIPARRMVGLIGPDGVGKSSLLSLIAGARAIEQGNVMVLGgdmrdvhhrrdvcpKIAWMPQglgKNLYHTLSVY 107
Cdd:TIGR00957 654 LNGITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVHMKG--------------SVAYVPQ---QAWIQNDSLR 716
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 108 ENVdffarLFGHdkAERELRINELLQSTGLAP-FRDRPAG----------KLSGGMKQKLGLCCALIHDPQLLILDEPTT 176
Cdd:TIGR00957 717 ENI-----LFGK--ALNEKYYQQVLEACALLPdLEILPSGdrteigekgvNLSGGQKQRVSLARAVYSNADIYLFDDPLS 789
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1820369315 177 GVDP-LSRAQFWELIDSIRQRQPEMSVLVaTAYMEEAERFDWLVAMNAGEVLATGSAAELKAQTGS 241
Cdd:TIGR00957 790 AVDAhVGKHIFEHVIGPEGVLKNKTRILV-THGISYLPQVDVIIVMSGGKISEMGSYQELLQRDGA 854
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
254-464 |
2.22e-10 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 64.44 E-value: 2.22e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 254 EAQRQAHKTVVIPPRDSREEEIAIEARGLTMRFGNF-VAVDHVNFRIARGEifGFL--GSNGCGKSTTMKMLTGLLPASE 330
Cdd:COG4178 340 EALEAADALPEAASRIETSEDGALALEDLTLRTPDGrPLLEDLSLSLKPGE--RLLitGPSGSGKSTLLRAIAGLWPYGS 417
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 331 GEAwlfGQPVDPKDIATRQRVgYMSQAfslyselSVRQNLELHARLFHIPDDEIA---HRV--AEMSERFmltEVKDALP 405
Cdd:COG4178 418 GRI---ARPAGARVLFLPQRP-YLPLG-------TLREALLYPATAEAFSDAELRealEAVglGHLAERL---DEEADWD 483
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1820369315 406 ADLPLGIRQRLSLAVAVIHRPEMLILDEPTSGVDPVARDMFWQLMVDLARQdrvTIFIS 464
Cdd:COG4178 484 QVLSLGEQQRLAFARLLLHKPDWLFLDEATSALDEENEAALYQLLREELPG---TTVIS 539
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
292-442 |
2.36e-10 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 61.12 E-value: 2.36e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 292 VDHVNFRIARGEIFGFLGSNGCGKSTTMKMLTGLLPASEGEAWLFGQPVDpKDIATRQR----VGYMSqafSLYSELSVR 367
Cdd:PRK13540 17 LQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEILFERQSIK-KDLCTYQKqlcfVGHRS---GINPYLTLR 92
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1820369315 368 QNLelharLFHIPDDEIAHRVAEMSERFMLTEVKDALPADLPLGIRQRLSLAVAVIHRPEMLILDEPTSGVDPVA 442
Cdd:PRK13540 93 ENC-----LYDIHFSPGAVGITELCRLFSLEHLIDYPCGLLSSGQKRQVALLRLWMSKAKLWLLDEPLVALDELS 162
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
277-499 |
2.88e-10 |
|
multi drug resistance-associated protein (MRP); This model describes multi drug resistance-associated protein (MRP) in eukaryotes. The multidrug resistance-associated protein is an integral membrane protein that causes multidrug resistance when overexpressed in mammalian cells. It belongs to ABC transporter superfamily. The protein topology and function was experimentally demonstrated by epitope tagging and immunofluorescence. Insertion of tags in the critical regions associated with drug efflux, abrogated its function. The C-terminal domain seem to highly conserved. [Transport and binding proteins, Other]
Pssm-ID: 188098 [Multi-domain] Cd Length: 1522 Bit Score: 64.58 E-value: 2.88e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 277 IEARGLTMRF--GNFVAVDHVNFRIARGEIFGFLGSNGCGKSTTMKMLTGLLPASEGEAWLFGQ---------------- 338
Cdd:TIGR00957 1285 VEFRNYCLRYreDLDLVLRHINVTIHGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGLniakiglhdlrfkiti 1364
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 339 -PVDPKDIATRQRVGYmsQAFSLYSELSVRQNLEL-HARLF--HIPDdEIAHRVAEMSErfmltevkdalpaDLPLGIRQ 414
Cdd:TIGR00957 1365 iPQDPVLFSGSLRMNL--DPFSQYSDEEVWWALELaHLKTFvsALPD-KLDHECAEGGE-------------NLSVGQRQ 1428
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 415 RLSLAVAVIHRPEMLILDEPTSGVDpVARDMFWQLMVDLARQDrVTIFISTHFMNEAERCDRISLMHAGKVLASDTPQAL 494
Cdd:TIGR00957 1429 LVCLARALLRKTKILVLDEATAAVD-LETDNLIQSTIRTQFED-CTVLTIAHRLNTIMDYTRVIVLDKGEVAEFGAPSNL 1506
|
....*
gi 1820369315 495 VEQRG 499
Cdd:TIGR00957 1507 LQQRG 1511
|
|
| PRK15093 |
PRK15093 |
peptide ABC transporter ATP-binding protein SapD; |
277-495 |
3.07e-10 |
|
peptide ABC transporter ATP-binding protein SapD;
Pssm-ID: 185049 [Multi-domain] Cd Length: 330 Bit Score: 62.51 E-value: 3.07e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 277 IEARGLTMRF----GNFVAVDHVNFRIARGEIFGFLGSNGCGKSTTMKMLTG-------------------LLPASEGE- 332
Cdd:PRK15093 4 LDIRNLTIEFktsdGWVKAVDRVSMTLTEGEIRGLVGESGSGKSLIAKAICGvtkdnwrvtadrmrfddidLLRLSPREr 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 333 --------AWLFGQP---VDPKDIATRQRVgymsQAFSLYSeLSVRQNLELHARLfhipddeiaHRVAEMSERFMLTEVK 401
Cdd:PRK15093 84 rklvghnvSMIFQEPqscLDPSERVGRQLM----QNIPGWT-YKGRWWQRFGWRK---------RRAIELLHRVGIKDHK 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 402 DAL---PADLPLGIRQRLSLAVAVIHRPEMLILDEPTSGVDPVARDMFWQLMVDLARQDRVTIFISTHFMNEAER-CDRI 477
Cdd:PRK15093 150 DAMrsfPYELTEGECQKVMIAIALANQPRLLIADEPTNAMEPTTQAQIFRLLTRLNQNNNTTILLISHDLQMLSQwADKI 229
|
250
....*....|....*...
gi 1820369315 478 SLMHAGKVLASDTPQALV 495
Cdd:PRK15093 230 NVLYCGQTVETAPSKELV 247
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
8-230 |
3.11e-10 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 61.87 E-value: 3.11e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 8 TSPPIALLENVGQQYGATIALRDISLAIPARRMVGLIGPDGVGKSSLLSLIAGARAIEQGNVM--VLGGDMRDVHH---- 81
Cdd:PRK11701 2 MDQPLLSVRGLTKLYGPRKGCRDVSFDLYPGEVLGIVGESGSGKTTLLNALSARLAPDAGEVHyrMRDGQLRDLYAlsea 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 82 RRDVCPKIAW--MPQGLGKNLYHTLSVYENV-----DFFARLFGHDKAERElrinELLQSTGLAPFR--DRPAgKLSGGM 152
Cdd:PRK11701 82 ERRRLLRTEWgfVHQHPRDGLRMQVSAGGNIgerlmAVGARHYGDIRATAG----DWLERVEIDAARidDLPT-TFSGGM 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 153 KQKLGLCCALIHDPQLLILDEPTTGVDPLSRAQfweLIDSIRQ--RQPEMSVLVATAYMEEAeRF--DWLVAMNAGEVLA 228
Cdd:PRK11701 157 QQRLQIARNLVTHPRLVFMDEPTGGLDVSVQAR---LLDLLRGlvRELGLAVVIVTHDLAVA-RLlaHRLLVMKQGRVVE 232
|
..
gi 1820369315 229 TG 230
Cdd:PRK11701 233 SG 234
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
8-190 |
3.49e-10 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 60.88 E-value: 3.49e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 8 TSPPIALLENVGQQYGATIALRDISLAIPARRMVGLIGPDGVGKSSLLSLIAGARAIEQGNVMVLGGDMRDV---HHRRD 84
Cdd:PRK10247 3 ENSPLLQLQNVGYLAGDAKILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFEGEDISTLkpeIYRQQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 85 V--CpkiAWMPQGLGKnlyhtlSVYENVdFFARLFGHDKAERElRINELLQSTGLA-PFRDRPAGKLSGGMKQKLGLCCA 161
Cdd:PRK10247 83 VsyC---AQTPTLFGD------TVYDNL-IFPWQIRNQQPDPA-IFLDDLERFALPdTILTKNIAELSGGEKQRISLIRN 151
|
170 180
....*....|....*....|....*....
gi 1820369315 162 LIHDPQLLILDEPTTGVDPLSRAQFWELI 190
Cdd:PRK10247 152 LQFMPKVLLLDEITSALDESNKHNVNEII 180
|
|
| NosY |
COG1277 |
ABC-type transport system involved in multi-copper enzyme maturation, permease component ... |
724-839 |
3.58e-10 |
|
ABC-type transport system involved in multi-copper enzyme maturation, permease component [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440888 [Multi-domain] Cd Length: 201 Bit Score: 60.60 E-value: 3.58e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 724 VIPLLLMMIPAMLSALSVVREKELGSIINLYVTPTTRSEFLLGKqlpyiVLGMFNFFLLCALSVFVF----GVAHKGSFL 799
Cdd:COG1277 56 LLSLLLPLLAPALGMDAISGERESGTLELLLTLPISRWEIVLGK-----FLGALLVLLLALLITFLLalllGLLLFGSPP 130
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 1820369315 800 TLTLAALL-------YVTIATGLGLLISTFMKSQIAAIFGTAIITLI 839
Cdd:COG1277 131 PDLGAILGfylglllLGLAFLAIGLFISALTRNQIVAAILAIALWLL 177
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
280-498 |
5.02e-10 |
|
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis fibrosis transmembrane conductor regulator (CFTR) in eukaryotes. The principal role of this protein is chloride ion conductance. The protein is predicted to consist of 12 transmembrane domains. Mutations or lesions in the genetic loci have been linked to the aetiology of asthma, bronchiectasis, chronic obstructive pulmonary disease etc. Disease-causing mutations have been studied by 36Cl efflux assays in vitro cell cultures and electrophysiology, all of which point to the impairment of chloride channel stability and not the biosynthetic processing per se. [Transport and binding proteins, Anions]
Pssm-ID: 273530 [Multi-domain] Cd Length: 1490 Bit Score: 63.78 E-value: 5.02e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 280 RGLTMRF---GNFVAVDhVNFRIARGEIFGFLGSNGCGKSTTMKMLTGLLpASEGEAWLFGQPVDPKDIAT-RQRVGYMS 355
Cdd:TIGR01271 1221 QGLTAKYteaGRAVLQD-LSFSVEGGQRVGLLGRTGSGKSTLLSALLRLL-STEGEIQIDGVSWNSVTLQTwRKAFGVIP 1298
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 356 QAFSLYSElSVRQNLELHARLfhiPDDEIAHRVAEMSERFMLTEVKDALpaDLPL---------GIRQRLSLAVAVIHRP 426
Cdd:TIGR01271 1299 QKVFIFSG-TFRKNLDPYEQW---SDEEIWKVAEEVGLKSVIEQFPDKL--DFVLvdggyvlsnGHKQLMCLARSILSKA 1372
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1820369315 427 EMLILDEPTSGVDPVArdmfWQLMVDLARQ--DRVTIFISTHFMNEAERCDRISLMHAGKVLASDTPQALVEQR 498
Cdd:TIGR01271 1373 KILLLDEPSAHLDPVT----LQIIRKTLKQsfSNCTVILSEHRVEALLECQQFLVIEGSSVKQYDSIQKLLNET 1442
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
295-464 |
5.32e-10 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 63.51 E-value: 5.32e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 295 VNFRIARGEIFGFLGSNGCGKSTTMKMLTGLLPASEGEAwLFGQPVDPKDIAT---RQRVGYMSQAFSLYSElSVRQNLE 371
Cdd:PTZ00265 404 LNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDI-IINDSHNLKDINLkwwRSKIGVVSQDPLLFSN-SIKNNIK 481
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 372 LhaRLFHIPD------------------------------------------DEIAH-----------RVAEMSERFMLT 398
Cdd:PTZ00265 482 Y--SLYSLKDlealsnyynedgndsqenknkrnscrakcagdlndmsnttdsNELIEmrknyqtikdsEVVDVSKKVLIH 559
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1820369315 399 EVKDALP-----------ADLPLGIRQRLSLAVAVIHRPEMLILDEPTSGVDPVARDMFWQLMVDL-ARQDRVTIFIS 464
Cdd:PTZ00265 560 DFVSALPdkyetlvgsnaSKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQKTINNLkGNENRITIIIA 637
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
299-466 |
6.98e-10 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 62.97 E-value: 6.98e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 299 IARGEIFGFLGSNGCGKSTTMKMLTGLLPASEGEAWLF---GQPVDPkdiaTRQRVGYMSQAFSLYSELSVRQNLeLHAR 375
Cdd:PLN03211 91 ASPGEILAVLGPSGSGKSTLLNALAGRIQGNNFTGTILannRKPTKQ----ILKRTGFVTQDDILYPHLTVRETL-VFCS 165
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 376 LFHIPDD---EIAHRVAE--MSErFMLTEVKDALPAD-----LPLGIRQRLSLAVAVIHRPEMLILDEPTSGVDPVARDM 445
Cdd:PLN03211 166 LLRLPKSltkQEKILVAEsvISE-LGLTKCENTIIGNsfirgISGGERKRVSIAHEMLINPSLLILDEPTSGLDATAAYR 244
|
170 180
....*....|....*....|.
gi 1820369315 446 FWQLMVDLARQDRvTIFISTH 466
Cdd:PLN03211 245 LVLTLGSLAQKGK-TIVTSMH 264
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
290-491 |
7.08e-10 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 61.00 E-value: 7.08e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 290 VAVDHVNFRIARGEIFGFLGSNGCGKSTTMKMLTGLLPAS--------EGEAWLFGQP---VDPKDIATRQRVgyMSQAF 358
Cdd:PRK13547 15 AILRDLSLRIEPGRVTALLGRNGAGKSTLLKALAGDLTGGgaprgarvTGDVTLNGEPlaaIDAPRLARLRAV--LPQAA 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 359 SLYSELSVRQNLEL----HARlfhiPDDEIAHRVAEMSERFMLTEVKDALPA----DLPLGIRQRLSLA--VAVIH---- 424
Cdd:PRK13547 93 QPAFAFSAREIVLLgrypHAR----RAGALTHRDGEIAWQALALAGATALVGrdvtTLSGGELARVQFArvLAQLWpphd 168
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1820369315 425 ---RPEMLILDEPTSGVDPVARDMFWQLMVDLARQDRVTIFISTHFMNEAER-CDRISLMHAGKVLASDTP 491
Cdd:PRK13547 169 aaqPPRYLLLDEPTAALDLAHQHRLLDTVRRLARDWNLGVLAIVHDPNLAARhADRIAMLADGAIVAHGAP 239
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
291-488 |
8.61e-10 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 62.05 E-value: 8.61e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 291 AVDHVNFRIARGEIFGFLGSNGCGKSTTMKMLTGLLPASEGEAWLFGQPVDPKDI--ATRQRVGYMSQAFSLYSELSVRQ 368
Cdd:PRK10982 13 ALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEIDFKSSkeALENGISMVHQELNLVLQRSVMD 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 369 NLEL-----------HARLFhipDDEIahrvAEMSERFMLTEVKDALpADLPLGIRQRLSLAVAVIHRPEMLILDEPTSG 437
Cdd:PRK10982 93 NMWLgryptkgmfvdQDKMY---RDTK----AIFDELDIDIDPRAKV-ATLSVSQMQMIEIAKAFSYNAKIVIMDEPTSS 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1820369315 438 VDPVARDMFWQLMVDLARQDRVTIFIStHFMNEA-ERCDRISLMHAGKVLAS 488
Cdd:PRK10982 165 LTEKEVNHLFTIIRKLKERGCGIVYIS-HKMEEIfQLCDEITILRDGQWIAT 215
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
290-454 |
9.77e-10 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 62.82 E-value: 9.77e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 290 VAVDHVNFRIARGEIFGFLGSNGCGKSTTMKML-----TGLLpaSEGEAWLFGQPVDpkdiATRQR-VGYMSQAFSLYSE 363
Cdd:TIGR00956 777 VILNNVDGWVKPGTLTALMGASGAGKTTLLNVLaervtTGVI--TGGDRLVNGRPLD----SSFQRsIGYVQQQDLHLPT 850
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 364 LSVRQNLELHARLF---HIPDDEIAHRVAEMSERFMLTEVKDALPADLPLGI----RQRLSLAVAVIHRPEMLI-LDEPT 435
Cdd:TIGR00956 851 STVRESLRFSAYLRqpkSVSKSEKMEYVEEVIKLLEMESYADAVVGVPGEGLnveqRKRLTIGVELVAKPKLLLfLDEPT 930
|
170
....*....|....*....
gi 1820369315 436 SGVDPVARDMFWQLMVDLA 454
Cdd:TIGR00956 931 SGLDSQTAWSICKLMRKLA 949
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
27-231 |
1.27e-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: 59.43 E-value: 1.27e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 27 ALRDISLAIPARRMVGLIGPDGVGKSSLLSliAGARAIE--QGNVMVLGGDMRDVHHRR-----DVCPKIAWMPQGlgkn 99
Cdd:cd03244 19 VLKNISFSIKPGEKVGIVGRTGSGKSSLLL--ALFRLVElsSGSILIDGVDISKIGLHDlrsriSIIPQDPVLFSG---- 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 100 lyhtlSVYENVDFFARlfgHDKAErelrINELLQSTGLAPFRDRPAGKL-----------SGGMKQKLGLCCALIHDPQL 168
Cdd:cd03244 93 -----TIRSNLDPFGE---YSDEE----LWQALERVGLKEFVESLPGGLdtvveeggenlSVGQRQLLCLARALLRKSKI 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1820369315 169 LILDEPTTGVDPLSRAQfweLIDSIRQRQPEMSVLVAtaymeeAER------FDWLVAMNAGEVLATGS 231
Cdd:cd03244 161 LVLDEATASVDPETDAL---IQKTIREAFKDCTVLTI------AHRldtiidSDRILVLDKGRVVEFDS 220
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
277-498 |
1.36e-09 |
|
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator (CFTR), the product of the gene mutated in patients with cystic fibrosis, has adapted the ABC transporter structural motif to form a tightly regulated anion channel at the apical surface of many epithelia. Use of the term assembly of a functional ion channel implies the coming together of subunits or at least smaller not-yet functional components of the active whole. In fact, on the basis of current knowledge only the CFTR polypeptide itself is required to form an ATP- and protein kinase A-dependent low-conductance chloride channel of the type present in the apical membrane of many epithelial cells. CFTR displays the typical organization (IM-ABC)2 and carries a characteristic hydrophilic R-domain that separates IM1-ABC1 from IM2-ABC2.
Pssm-ID: 213256 [Multi-domain] Cd Length: 275 Bit Score: 60.25 E-value: 1.36e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 277 IEARGLTMRF---GNFVaVDHVNFRIARGEIFGFLGSNGCGKSTTMKMLTGLLpASEGEAWLFGQPVDPKDIAT-RQRVG 352
Cdd:cd03289 3 MTVKDLTAKYtegGNAV-LENISFSISPGQRVGLLGRTGSGKSTLLSAFLRLL-NTEGDIQIDGVSWNSVPLQKwRKAFG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 353 YMSQAFSLYSElSVRQNLELHARLfhipDDEIAHRVAEmseRFMLTEVKDALPADLPL-----------GIRQRLSLAVA 421
Cdd:cd03289 81 VIPQKVFIFSG-TFRKNLDPYGKW----SDEEIWKVAE---EVGLKSVIEQFPGQLDFvlvdggcvlshGHKQLMCLARS 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1820369315 422 VIHRPEMLILDEPTSGVDPVArdmfWQLMVDLARQ--DRVTIFISTHFMNEAERCDRISLMHAGKVLASDTPQALVEQR 498
Cdd:cd03289 153 VLSKAKILLLDEPSAHLDPIT----YQVIRKTLKQafADCTVILSEHRIEAMLECQRFLVIEENKVRQYDSIQKLLNEK 227
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
291-499 |
1.38e-09 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 61.65 E-value: 1.38e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 291 AVDHVNFRIARGEIFGFLGSNGCGKSTTMKMLTGLLPASEGEAWLFGQPV-DPKDIATRQRVGYMSQAFSLYSElSVRQN 369
Cdd:PRK10789 330 ALENVNFTLKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGDIRFHDIPLtKLQLDSWRSRLAVVSQTPFLFSD-TVANN 408
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 370 LELH------------ARLFHIPDDEIahRV-----AEMSER-FMLTEvkdalpadlplGIRQRLSLAVAVIHRPEMLIL 431
Cdd:PRK10789 409 IALGrpdatqqeiehvARLASVHDDIL--RLpqgydTEVGERgVMLSG-----------GQKQRISIARALLLNAEILIL 475
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 432 DEPTSGVDPVARdmfWQLMVDLA--RQDRvTIFISTHFMNEAERCDRISLMHAGKVLASDTPQALVEQRG 499
Cdd:PRK10789 476 DDALSAVDGRTE---HQILHNLRqwGEGR-TVIISAHRLSALTEASEILVMQHGHIAQRGNHDQLAQQSG 541
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
277-497 |
1.65e-09 |
|
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: 58.31 E-value: 1.65e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 277 IEARGLTMRFGNFVAVDHVNFRIARGEIFGFLGSNGCGKSTTMKMLTGLlPASE---GEAWLFGQPVDPKDIATRQRVG- 352
Cdd:cd03217 1 LEIKDLHVSVGGKEILKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMGH-PKYEvteGEILFKGEDITDLPPEERARLGi 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 353 YMSqafslyselsvrqnlelharlFHIPDdeiahRVAEMSERFMLTEVKDALPAdlplGIRQRLSLAVAVIHRPEMLILD 432
Cdd:cd03217 80 FLA---------------------FQYPP-----EIPGVKNADFLRYVNEGFSG----GEKKRNEILQLLLLEPDLAILD 129
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1820369315 433 EPTSGVDPVARDMFWQLMVDLARQDRvTIFISTHFMNEAE--RCDRISLMHAGKVLASDtPQALVEQ 497
Cdd:cd03217 130 EPDSGLDIDALRLVAEVINKLREEGK-SVLIITHYQRLLDyiKPDRVHVLYDGRIVKSG-DKELALE 194
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
306-435 |
1.79e-09 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 61.29 E-value: 1.79e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 306 GFLGSNGCGKSTTMKMLTGLLPASEGEAWLfgqpvdpkdiATRQRVGYMSQAFSLYSELSVRQNLE--------LHARLF 377
Cdd:PRK11819 37 GVLGLNGAGKSTLLRIMAGVDKEFEGEARP----------APGIKVGYLPQEPQLDPEKTVRENVEegvaevkaALDRFN 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 378 HI------PDDEIAHRVAEMS------------------ERFMltevkDAL---PADLPL-----GIRQRLSLAVAVIHR 425
Cdd:PRK11819 107 EIyaayaePDADFDALAAEQGelqeiidaadawdldsqlEIAM-----DALrcpPWDAKVtklsgGERRRVALCRLLLEK 181
|
170
....*....|
gi 1820369315 426 PEMLILDEPT 435
Cdd:PRK11819 182 PDMLLLDEPT 191
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
282-439 |
1.81e-09 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 59.36 E-value: 1.81e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 282 LTMRFGNFVAVDHVNFRIARGEIFGFLGSNGCGKSTTMKMLTGLLPASEGeawlfgqpvdpkdIATRQ---RVGYMSQAF 358
Cdd:PRK09544 10 VSVSFGQRRVLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEG-------------VIKRNgklRIGYVPQKL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 359 SLYSELSVrqnlelharlfhipddeiahrvaeMSERFML----TEVKDALPA----------DLPL-----GIRQRLSLA 419
Cdd:PRK09544 77 YLDTTLPL------------------------TVNRFLRlrpgTKKEDILPAlkrvqaghliDAPMqklsgGETQRVLLA 132
|
170 180
....*....|....*....|
gi 1820369315 420 VAVIHRPEMLILDEPTSGVD 439
Cdd:PRK09544 133 RALLNRPQLLVLDEPTQGVD 152
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
27-185 |
2.09e-09 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 60.13 E-value: 2.09e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 27 ALRDISLAIPARRMVGLIGPDGVGKSSL----LSLI---AGARAIEQGNVMVLGG-DMRDVhhRRDVcpkiawmpQGLGK 98
Cdd:COG4608 33 AVDGVSFDIRRGETLGLVGESGCGKSTLgrllLRLEeptSGEILFDGQDITGLSGrELRPL--RRRM--------QMVFQ 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 99 NLYHTL----SVYENVDFFARLFG-HDKAERELRINELLQSTGLAP-FRDRPAGKLSGGMKQKLGLCCALIHDPQLLILD 172
Cdd:COG4608 103 DPYASLnprmTVGDIIAEPLRIHGlASKAERRERVAELLELVGLRPeHADRYPHEFSGGQRQRIGIARALALNPKLIVCD 182
|
170
....*....|....
gi 1820369315 173 EPTTGVDpLS-RAQ 185
Cdd:COG4608 183 EPVSALD-VSiQAQ 195
|
|
| PRK13546 |
PRK13546 |
teichoic acids export ABC transporter ATP-binding subunit TagH; |
289-485 |
2.48e-09 |
|
teichoic acids export ABC transporter ATP-binding subunit TagH;
Pssm-ID: 184131 [Multi-domain] Cd Length: 264 Bit Score: 59.06 E-value: 2.48e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 289 FVAVDHVNFRIARGEIFGFLGSNGCGKSTTMKMLTGLLPASEGEAWLFGQpvdpkdiatrqrVGYMSQAFSLYSELSVRQ 368
Cdd:PRK13546 37 FFALDDISLKAYEGDVIGLVGINGSGKSTLSNIIGGSLSPTVGKVDRNGE------------VSVIAISAGLSGQLTGIE 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 369 NLELHARLFHIPDDEIAH---RVAEMSE--RFMLTEVKdalpaDLPLGIRQRLSLAVAVIHRPEMLILDEPTSGVDPVAR 443
Cdd:PRK13546 105 NIEFKMLCMGFKRKEIKAmtpKIIEFSElgEFIYQPVK-----KYSSGMRAKLGFSINITVNPDILVIDEALSVGDQTFA 179
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1820369315 444 DMFWQLMVDLARQDRVTIFISTHFMNEAERCDRISLMHAGKV 485
Cdd:PRK13546 180 QKCLDKIYEFKEQNKTIFFVSHNLGQVRQFCTKIAWIEGGKL 221
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
291-500 |
2.55e-09 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 60.80 E-value: 2.55e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 291 AVDHVNFRIARGEIFGFLGSNGCGKSTTMKMLTGLLPASEGEAWLFGqpVDPKDI---ATRQRVGYMSQAFSLYSElSVR 367
Cdd:PRK11176 358 ALRNINFKIPAGKTVALVGRSGSGKSTIANLLTRFYDIDEGEILLDG--HDLRDYtlaSLRNQVALVSQNVHLFND-TIA 434
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 368 QNLElHARLFHIPDDEI--AHRVAEMSErfMLTEVKDALP-------ADLPLGIRQRLSLAVAVIHRPEMLILDEPTSGV 438
Cdd:PRK11176 435 NNIA-YARTEQYSREQIeeAARMAYAMD--FINKMDNGLDtvigengVLLSGGQRQRIAIARALLRDSPILILDEATSAL 511
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1820369315 439 DpVARDMFWQLMVDLARQDRVTIFIStHFMNEAERCDRISLMHAGKVLASDTPQALVEQRGA 500
Cdd:PRK11176 512 D-TESERAIQAALDELQKNRTSLVIA-HRLSTIEKADEILVVEDGEIVERGTHAELLAQNGV 571
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
28-203 |
3.07e-09 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 60.59 E-value: 3.07e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 28 LRDISLAIPARRMVGLIGPDGVGKSSLLSLIAGARAIEQGNVMVLGGDmrdvhhrrdvcpKIAWMPQ----GLGkNLYHT 103
Cdd:COG4178 379 LEDLSLSLKPGERLLITGPSGSGKSTLLRAIAGLWPYGSGRIARPAGA------------RVLFLPQrpylPLG-TLREA 445
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 104 LSvYENvdffarlfGHDKAERElRINELLQSTGLAPFRDRP------AGKLSGGMKQKLGLCCALIHDPQLLILDEPTTG 177
Cdd:COG4178 446 LL-YPA--------TAEAFSDA-ELREALEAVGLGHLAERLdeeadwDQVLSLGEQQRLAFARLLLHKPDWLFLDEATSA 515
|
170 180
....*....|....*....|....*.
gi 1820369315 178 VDPLSRAQFWELidsIRQRQPEMSVL 203
Cdd:COG4178 516 LDEENEAALYQL---LREELPGTTVI 538
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
299-466 |
3.11e-09 |
|
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: 58.57 E-value: 3.11e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 299 IARGEIFGFLGSNGCGKSTTMKMLTGLLPASEGEAwlfgqpvdpkdIATRQRVGYMSQAFSLYSELSVRqnlelhARLFH 378
Cdd:cd03237 22 ISESEVIGILGPNGIGKTTFIKMLAGVLKPDEGDI-----------EIELDTVSYKPQYIKADYEGTVR------DLLSS 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 379 IPDDEIAHR--VAEMSERFMLTEVKDALPADLPLGIRQRLSLAVAVIHRPEMLILDEPTSGVDPVARDMFWQLMVDLARQ 456
Cdd:cd03237 85 ITKDFYTHPyfKTEIAKPLQIEQILDREVPELSGGELQRVAIAACLSKDADIYLLDEPSAYLDVEQRLMASKVIRRFAEN 164
|
170
....*....|
gi 1820369315 457 DRVTIFISTH 466
Cdd:cd03237 165 NEKTAFVVEH 174
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
292-521 |
3.91e-09 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 60.10 E-value: 3.91e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 292 VDHVNFRIARGEIFGFLGSNGCGKSTTMKMLTGLLPAS-----EGEAWLFGQPVDPKDIATRQRV--GYMSQAFS----- 359
Cdd:PRK15134 25 VNDVSLQIEAGETLALVGESGSGKSVTALSILRLLPSPpvvypSGDIRFHGESLLHASEQTLRGVrgNKIAMIFQepmvs 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 360 ----------LYSELSVRQNLELHArlfhiPDDEIAHRVAEMSERFMLTEVKDaLPADLPLGIRQRLSLAVAVIHRPEML 429
Cdd:PRK15134 105 lnplhtlekqLYEVLSLHRGMRREA-----ARGEILNCLDRVGIRQAAKRLTD-YPHQLSGGERQRVMIAMALLTRPELL 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 430 ILDEPTSGVDPVARDMFWQLMVDLARQDRVTIFISTHFMNEAER-CDRISLMHAGKVLASDTPQALVeqrgaASLEEAFI 508
Cdd:PRK15134 179 IADEPTTALDVSVQAQILQLLRELQQELNMGLLFITHNLSIVRKlADRVAVMQNGRCVEQNRAATLF-----SAPTHPYT 253
|
250
....*....|....
gi 1820369315 509 AWLKEAQPS-SPVP 521
Cdd:PRK15134 254 QKLLNSEPSgDPVP 267
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
28-240 |
4.21e-09 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 60.51 E-value: 4.21e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 28 LRDISLAIPARRMVGLIGPDGVGKSSLLSLIAGARAIEQGNVMVLGGDMRDVHHRRdVCPKIAWMPQglgKNLYHTLSVY 107
Cdd:TIGR00958 497 LKGLTFTLHPGEVVALVGPSGSGKSTVAALLQNLYQPTGGQVLLDGVPLVQYDHHY-LHRQVALVGQ---EPVLFSGSVR 572
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 108 ENVdffarLFGHDKAERELRINELLQS------TGLAPFRDRPAGK----LSGGMKQKLGLCCALIHDPQLLILDEPTTG 177
Cdd:TIGR00958 573 ENI-----AYGLTDTPDEEIMAAAKAAnahdfiMEFPNGYDTEVGEkgsqLSGGQKQRIAIARALVRKPRVLILDEATSA 647
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1820369315 178 VDPLSRAQFWELidsiRQRQpEMSVLVATAYMEEAERFDWLVAMNAGEVLATGSAAELKAQTG 240
Cdd:TIGR00958 648 LDAECEQLLQES----RSRA-SRTVLLIAHRLSTVERADQILVLKKGSVVEMGTHKQLMEDQG 705
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
286-483 |
4.29e-09 |
|
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis fibrosis transmembrane conductor regulator (CFTR) in eukaryotes. The principal role of this protein is chloride ion conductance. The protein is predicted to consist of 12 transmembrane domains. Mutations or lesions in the genetic loci have been linked to the aetiology of asthma, bronchiectasis, chronic obstructive pulmonary disease etc. Disease-causing mutations have been studied by 36Cl efflux assays in vitro cell cultures and electrophysiology, all of which point to the impairment of chloride channel stability and not the biosynthetic processing per se. [Transport and binding proteins, Anions]
Pssm-ID: 273530 [Multi-domain] Cd Length: 1490 Bit Score: 60.69 E-value: 4.29e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 286 FGNFV-----AVDHVNFRIARGEIFGFLGSNGCGKSTTMKMLTGLLPASEGEawlfgqpvdpkdIATRQRVGYMSQaFSL 360
Cdd:TIGR01271 431 FSNFSlyvtpVLKNISFKLEKGQLLAVAGSTGSGKSSLLMMIMGELEPSEGK------------IKHSGRISFSPQ-TSW 497
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 361 YSELSVRQNLelharLFHIPDDEIAHR----VAEMSERFMLTEVKDALP-----ADLPLGIRQRLSLAVAVIHRPEMLIL 431
Cdd:TIGR01271 498 IMPGTIKDNI-----IFGLSYDEYRYTsvikACQLEEDIALFPEKDKTVlgeggITLSGGQRARISLARAVYKDADLYLL 572
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1820369315 432 DEPTSGVDPVA-RDMFWQLMVDL-ARQDRVTIfisTHFMNEAERCDRISLMHAG 483
Cdd:TIGR01271 573 DSPFTHLDVVTeKEIFESCLCKLmSNKTRILV---TSKLEHLKKADKILLLHEG 623
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
15-179 |
4.39e-09 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 57.58 E-value: 4.39e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 15 LENVGQQY-GATIALRDISLAIPARRMVGLIGPDGVGKSSLLSLIAGARAIEQGNVMVLGGDMRDVHHRrdvcpKIAWMP 93
Cdd:PRK10908 4 FEHVSKAYlGGRQALQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDITRLKNR-----EVPFLR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 94 QGLGKNL--YHTL---SVYENVDFFARLFGHDKAERELRINELLQSTGLAPFRDRPAGKLSGGMKQKLGLCCALIHDPQL 168
Cdd:PRK10908 79 RQIGMIFqdHHLLmdrTVYDNVAIPLIIAGASGDDIRRRVSAALDKVGLLDKAKNFPIQLSGGEQQRVGIARAVVNKPAV 158
|
170
....*....|.
gi 1820369315 169 LILDEPTTGVD 179
Cdd:PRK10908 159 LLADEPTGNLD 169
|
|
| tagH |
PRK13545 |
teichoic acids export protein ATP-binding subunit; Provisional |
27-173 |
4.64e-09 |
|
teichoic acids export protein ATP-binding subunit; Provisional
Pssm-ID: 184130 [Multi-domain] Cd Length: 549 Bit Score: 59.90 E-value: 4.64e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 27 ALRDISLAIPARRMVGLIGPDGVGKSSLLSLIAGARAIEQGNVMVLGGdmrdvhhrrdvCPKIAwmpqgLGKNLYHTLSV 106
Cdd:PRK13545 39 ALNNISFEVPEGEIVGIIGLNGSGKSTLSNLIAGVTMPNKGTVDIKGS-----------AALIA-----ISSGLNGQLTG 102
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1820369315 107 YENVDFFARLFGHDKAERELRINELLQSTGLAPFRDRPAGKLSGGMKQKLGLCCALIHDPQLLILDE 173
Cdd:PRK13545 103 IENIELKGLMMGLTKEKIKEIIPEIIEFADIGKFIYQPVKTYSSGMKSRLGFAISVHINPDILVIDE 169
|
|
| tagH |
PRK13545 |
teichoic acids export protein ATP-binding subunit; Provisional |
291-485 |
4.80e-09 |
|
teichoic acids export protein ATP-binding subunit; Provisional
Pssm-ID: 184130 [Multi-domain] Cd Length: 549 Bit Score: 59.90 E-value: 4.80e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 291 AVDHVNFRIARGEIFGFLGSNGCGKSTTMKMLTGLLPASEGEawlfgqpVDPKDIATRQRVGYmsqafSLYSELSVRQNL 370
Cdd:PRK13545 39 ALNNISFEVPEGEIVGIIGLNGSGKSTLSNLIAGVTMPNKGT-------VDIKGSAALIAISS-----GLNGQLTGIENI 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 371 ELHARLFHIPDD---EIAHRVAEMSE--RFMLTEVKdalpaDLPLGIRQRLSLAVAVIHRPEMLILDEPTSGVDPVARDM 445
Cdd:PRK13545 107 ELKGLMMGLTKEkikEIIPEIIEFADigKFIYQPVK-----TYSSGMKSRLGFAISVHINPDILVIDEALSVGDQTFTKK 181
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1820369315 446 FWQLMVDLARQDRvTIFISTHFMNEAER-CDRISLMHAGKV 485
Cdd:PRK13545 182 CLDKMNEFKEQGK-TIFFISHSLSQVKSfCTKALWLHYGQV 221
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
17-234 |
4.91e-09 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 59.12 E-value: 4.91e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 17 NVGQQYGATiALrDISLAIPARRMVGLIGPDGVGKSSLLSLIAGARAIEQGNVmVLGGD-MRDVHHRRDVCP---KIAWM 92
Cdd:PRK11144 5 NFKQQLGDL-CL-TVNLTLPAQGITAIFGRSGAGKTSLINAISGLTRPQKGRI-VLNGRvLFDAEKGICLPPekrRIGYV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 93 PQGlgknlyhtlsvyenvdffARLFGHDKAERELR-------------INELLqstGLAPFRDRPAGKLSGGMKQKLGLC 159
Cdd:PRK11144 82 FQD------------------ARLFPHYKVRGNLRygmaksmvaqfdkIVALL---GIEPLLDRYPGSLSGGEKQRVAIG 140
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1820369315 160 CALIHDPQLLILDEPTTGVDpLSRAQfwELIDSIRQ--RQPEMSVLVATAYMEEAERF-DWLVAMNAGEVLATGSAAE 234
Cdd:PRK11144 141 RALLTAPELLLMDEPLASLD-LPRKR--ELLPYLERlaREINIPILYVSHSLDEILRLaDRVVVLEQGKVKAFGPLEE 215
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
31-259 |
4.93e-09 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 59.92 E-value: 4.93e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 31 ISLAIPARRMVGLIGPDGVGKSSLLSLIAGARAIEQGNVMvLGGDMRDVHHRRD-------VCPK-------IAwmpqgl 96
Cdd:PRK11288 272 ISFSVRAGEIVGLFGLVGAGRSELMKLLYGATRRTAGQVY-LDGKPIDIRSPRDairagimLCPEdrkaegiIP------ 344
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 97 gknlyhTLSVYENVDFFAR-------LFGHDKAEREL---RINELLQSTglaPFRDRPAGKLSGGMKQKLGLCCALIHDP 166
Cdd:PRK11288 345 ------VHSVADNINISARrhhlragCLINNRWEAENadrFIRSLNIKT---PSREQLIMNLSGGNQQKAILGRWLSEDM 415
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 167 QLLILDEPTTGVDPLSRAQFWELIDSIRQRQpeMSVLVATAYMEE----AERfdwLVAMNAGEVlatgsAAEL-KAQTGS 241
Cdd:PRK11288 416 KVILLDEPTRGIDVGAKHEIYNVIYELAAQG--VAVLFVSSDLPEvlgvADR---IVVMREGRI-----AGELaREQATE 485
|
250
....*....|....*...
gi 1820369315 242 QTLEQAfiALLPEAQRQA 259
Cdd:PRK11288 486 RQALSL--ALPRTSAAVA 501
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
25-235 |
5.04e-09 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 58.69 E-value: 5.04e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 25 TIALRDISLAIPARRMVGLIGPDGVGKSSLLSLIAGARAIEQGNVMVLG---------GDMRDVhhRRDVCPKIAWMPQG 95
Cdd:PRK13641 20 KKGLDNISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITIAGyhitpetgnKNLKKL--RKKVSLVFQFPEAQ 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 96 LGKNlyhtlSVYENVDFFARLFGHDKAERELRINELLQSTGL-------APFrdrpagKLSGGMKQKLGLCCALIHDPQL 168
Cdd:PRK13641 98 LFEN-----TVLKDVEFGPKNFGFSEDEAKEKALKWLKKVGLsedliskSPF------ELSGGQMRRVAIAGVMAYEPEI 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1820369315 169 LILDEPTTGVDPLSRAQFWELIDSIrQRQPEMSVLVATAYMEEAERFDWLVAMNAGEVLATGSAAEL 235
Cdd:PRK13641 167 LCLDEPAAGLDPEGRKEMMQLFKDY-QKAGHTVILVTHNMDDVAEYADDVLVLEHGKLIKHASPKEI 232
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
2-196 |
5.17e-09 |
|
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: 59.70 E-value: 5.17e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 2 KLTPQDTSPPIALLENV-----------GQQYGATIALRDISLAIPARRMVGLIGPDGVGKSSLlsliagARAI-----E 65
Cdd:COG4172 265 PRPVPPDAPPLLEARDLkvwfpikrglfRRTVGHVKAVDGVSLTLRRGETLGLVGESGSGKSTL------GLALlrlipS 338
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 66 QGNVMVLG--------GDMRdvHHRRDVcpkiawmpQGLGKNLYHTLS--------VYENVDFFARlfGHDKAERELRIN 129
Cdd:COG4172 339 EGEIRFDGqdldglsrRALR--PLRRRM--------QVVFQDPFGSLSprmtvgqiIAEGLRVHGP--GLSAAERRARVA 406
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1820369315 130 ELLQSTGLAP-FRDRPAGKLSGGMKQKLGLCCALIHDPQLLILDEPTTGVDPLSRAQFWELIDSIRQR 196
Cdd:COG4172 407 EALEEVGLDPaARHRYPHEFSGGQRQRIAIARALILEPKLLVLDEPTSALDVSVQAQILDLLRDLQRE 474
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
165-500 |
6.31e-09 |
|
multi drug resistance-associated protein (MRP); This model describes multi drug resistance-associated protein (MRP) in eukaryotes. The multidrug resistance-associated protein is an integral membrane protein that causes multidrug resistance when overexpressed in mammalian cells. It belongs to ABC transporter superfamily. The protein topology and function was experimentally demonstrated by epitope tagging and immunofluorescence. Insertion of tags in the critical regions associated with drug efflux, abrogated its function. The C-terminal domain seem to highly conserved. [Transport and binding proteins, Other]
Pssm-ID: 188098 [Multi-domain] Cd Length: 1522 Bit Score: 59.96 E-value: 6.31e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 165 DPQLLILDEPTTGVDPLsRAQFWEL-----IDSIRQRqpEMSVLVATAYMEEAERFDW-----LVAMNAGEVLATGSAAE 234
Cdd:TIGR00957 493 DNRIKLMNEILNGIKVL-KLYAWELafldkVEGIRQE--ELKVLKKSAYLHAVGTFTWvctpfLVALITFAVYVTVDENN 569
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 235 -LKAQTGSQTLEQAFIALLP--------EAQRQAH---KTVVIPPRDSREEEIAIEAR--------GLTMRFGNFV---- 290
Cdd:TIGR00957 570 iLDAEKAFVSLALFNILRFPlnilpmviSSIVQASvslKRLRIFLSHEELEPDSIERRtikpgegnSITVHNATFTward 649
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 291 ---AVDHVNFRIARGEIFGFLGSNGCGKSTTMKMLTGLLPASEGEawlfgqpvdpkdIATRQRVGYMSQAFSLYSElSVR 367
Cdd:TIGR00957 650 lppTLNGITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEGH------------VHMKGSVAYVPQQAWIQND-SLR 716
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 368 QNLelharLFHIPDDEIAHR-----VAEMSERFML-----TEVKDAlPADLPLGIRQRLSLAVAVIHRPEMLILDEPTSG 437
Cdd:TIGR00957 717 ENI-----LFGKALNEKYYQqvleaCALLPDLEILpsgdrTEIGEK-GVNLSGGQKQRVSLARAVYSNADIYLFDDPLSA 790
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1820369315 438 VDP-VARDMFWQL---MVDLARQDRVTIfisTHFMNEAERCDRISLMHAGKVLASDTPQALVEQRGA 500
Cdd:TIGR00957 791 VDAhVGKHIFEHVigpEGVLKNKTRILV---THGISYLPQVDVIIVMSGGKISEMGSYQELLQRDGA 854
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
234-499 |
9.99e-09 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 58.96 E-value: 9.99e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 234 ELKAQtgSQTLEQAFIA-----LLPEAQRQAHKTVVIPPRDSReeeIAIEARGLTMRFGNFVaVDHVNFRI-ARGEIfGF 307
Cdd:PRK10790 300 ELTTQ--QSMLQQAVVAgervfELMDGPRQQYGNDDRPLQSGR---IDIDNVSFAYRDDNLV-LQNINLSVpSRGFV-AL 372
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 308 LGSNGCGKSTTMKMLTGLLPASEGEAWLFGQPVDPKDIAT-RQRVGYMSQAFSLYSElSVRQNLELhARlfhipdDEIAH 386
Cdd:PRK10790 373 VGHTGSGKSTLASLLMGYYPLTEGEIRLDGRPLSSLSHSVlRQGVAMVQQDPVVLAD-TFLANVTL-GR------DISEE 444
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 387 RVAEMSERFMLTEVKDALPA-----------DLPLGIRQRLSLAVAVIHRPEMLILDEPTSGVDPVARDMFWQLMVdlAR 455
Cdd:PRK10790 445 QVWQALETVQLAELARSLPDglytplgeqgnNLSVGQKQLLALARVLVQTPQILILDEATANIDSGTEQAIQQALA--AV 522
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 1820369315 456 QDRVTIFISTHFMNEAERCDRISLMHAGKVLASDTPQALVEQRG 499
Cdd:PRK10790 523 REHTTLVVIAHRLSTIVEADTILVLHRGQAVEQGTHQQLLAAQG 566
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
16-240 |
1.36e-08 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 58.43 E-value: 1.36e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 16 ENVGQQY-GATIALRDISLAIPARRMVGLIGPDGVGKSSLLSLIAGARAIEQGNVMVLGGDMRDVHhRRDVCPKIAWMPQ 94
Cdd:PRK13657 338 DDVSFSYdNSRQGVEDVSFEAKPGQTVAIVGPTGAGKSTLINLLQRVFDPQSGRILIDGTDIRTVT-RASLRRNIAVVFQ 416
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 95 GLGknLYHTlSVYENVdffaRLFGHDKAERELRinELLQSTGLAPFRDRPAGK-----------LSGGMKQKLGLCCALI 163
Cdd:PRK13657 417 DAG--LFNR-SIEDNI----RVGRPDATDEEMR--AAAERAQAHDFIERKPDGydtvvgergrqLSGGERQRLAIARALL 487
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1820369315 164 HDPQLLILDEPTTGVDPLSRAQFWELIDSIRQRQPEMSVLVATAYMEEAERfdwLVAMNAGEVLATGSAAELKAQTG 240
Cdd:PRK13657 488 KDPPILILDEATSALDVETEAKVKAALDELMKGRTTFIIAHRLSTVRNADR---ILVFDNGRVVESGSFDELVARGG 561
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
277-439 |
1.52e-08 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 58.36 E-value: 1.52e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 277 IEARGLTMRFGNFVAVDHVNFRIARGEIFGFLGSNGCGKSTTMKMLTGLLPASEGEAWLfgqpvDPKdiatrQRVGYMSQ 356
Cdd:PRK15064 2 LSTANITMQFGAKPLFENISVKFGGGNRYGLIGANGCGKSTFMKILGGDLEPSAGNVSL-----DPN-----ERLGKLRQ 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 357 ---AFSLYSELSV--RQNLELHA------RLFHIPD--DEIAHRVAEMSERF--MLTEVKDALPADLPLGI--------- 412
Cdd:PRK15064 72 dqfAFEEFTVLDTviMGHTELWEvkqerdRIYALPEmsEEDGMKVADLEVKFaeMDGYTAEARAGELLLGVgipeeqhyg 151
|
170 180 190
....*....|....*....|....*....|....*.
gi 1820369315 413 ---------RQRLSLAVAVIHRPEMLILDEPTSGVD 439
Cdd:PRK15064 152 lmsevapgwKLRVLLAQALFSNPDILLLDEPTNNLD 187
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
28-236 |
1.54e-08 |
|
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: 55.61 E-value: 1.54e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 28 LRDISLAIPARRMVGLIGPDGVGKSSLLSLIAG--ARAIEQGNVMVLGGDMRDvhhrrdvcpkiawmpqglgknlyhtLS 105
Cdd:cd03217 16 LKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMGhpKYEVTEGEILFKGEDITD-------------------------LP 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 106 VYENvdffARL-----FGHDKAERELRINELLqstglapfRDRPAGkLSGGMKQKLGLCCALIHDPQLLILDEPTTGVDp 180
Cdd:cd03217 71 PEER----ARLgiflaFQYPPEIPGVKNADFL--------RYVNEG-FSGGEKKRNEILQLLLLEPDLAILDEPDSGLD- 136
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1820369315 181 lsraqfwelIDSIRQ--------RQPEMSVLVATAYMEEAE--RFDWLVAMNAGEVLATGSAAELK 236
Cdd:cd03217 137 ---------IDALRLvaevinklREEGKSVLIITHYQRLLDyiKPDRVHVLYDGRIVKSGDKELAL 193
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
25-238 |
1.57e-08 |
|
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis fibrosis transmembrane conductor regulator (CFTR) in eukaryotes. The principal role of this protein is chloride ion conductance. The protein is predicted to consist of 12 transmembrane domains. Mutations or lesions in the genetic loci have been linked to the aetiology of asthma, bronchiectasis, chronic obstructive pulmonary disease etc. Disease-causing mutations have been studied by 36Cl efflux assays in vitro cell cultures and electrophysiology, all of which point to the impairment of chloride channel stability and not the biosynthetic processing per se. [Transport and binding proteins, Anions]
Pssm-ID: 273530 [Multi-domain] Cd Length: 1490 Bit Score: 58.77 E-value: 1.57e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 25 TIALRDISLAIPARRMVGLIGPDGVGKSSLLSLIAGARAIEQGNVMVLGgdmrdvhhRRDVCPKIAW-MPQGLGKNLYHT 103
Cdd:TIGR01271 439 TPVLKNISFKLEKGQLLAVAGSTGSGKSSLLMMIMGELEPSEGKIKHSG--------RISFSPQTSWiMPGTIKDNIIFG 510
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 104 LSvyenvdffarlfgHDKAERELRIN--ELLQSTGLAPFRDR-PAGK----LSGGMKQKLGLCCALIHDPQLLILDEPTT 176
Cdd:TIGR01271 511 LS-------------YDEYRYTSVIKacQLEEDIALFPEKDKtVLGEggitLSGGQRARISLARAVYKDADLYLLDSPFT 577
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1820369315 177 GVDPLSRAQFWEliDSIRQRQPEMSVLVATAYMEEAERFDWLVAMNAGEVLATGSAAELKAQ 238
Cdd:TIGR01271 578 HLDVVTEKEIFE--SCLCKLMSNKTRILVTSKLEHLKKADKILLLHEGVCYFYGTFSELQAK 637
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
16-179 |
1.72e-08 |
|
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: 58.29 E-value: 1.72e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 16 ENVGQQYGA--TIaLRDISLAIPARRMVGLIGPDGVGKSSLLSLIAGARAIEQGNVMVLGGDMRDVHH---RRDvcpkIA 90
Cdd:COG5265 361 ENVSFGYDPerPI-LKGVSFEVPAGKTVAIVGPSGAGKSTLARLLFRFYDVTSGRILIDGQDIRDVTQaslRAA----IG 435
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 91 WMPQglgknlyHTL----SVYENVdffarLFGHDKAERElRINELLQSTGLAPFRDR-PAG----------KLSGGMKQK 155
Cdd:COG5265 436 IVPQ-------DTVlfndTIAYNI-----AYGRPDASEE-EVEAAARAAQIHDFIESlPDGydtrvgerglKLSGGEKQR 502
|
170 180
....*....|....*....|....
gi 1820369315 156 LGLCCALIHDPQLLILDEPTTGVD 179
Cdd:COG5265 503 VAIARTLLKNPPILIFDEATSALD 526
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
288-483 |
1.75e-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: 55.80 E-value: 1.75e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 288 NFVAVDHVNFRIARGEIFGFLGSNGCGKSTTMKMLTGLLPASEGEA-WLFGQPVDPKDIATRQR----VGYMSQAFSLYS 362
Cdd:cd03290 13 GLATLSNINIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVhWSNKNESEPSFEATRSRnrysVAYAAQKPWLLN 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 363 ElSVRQNLelharLFHIPDDEiaHRVAEMSERFMLTEVKDALP-----------ADLPLGIRQRLSLAVAVIHRPEMLIL 431
Cdd:cd03290 93 A-TVEENI-----TFGSPFNK--QRYKAVTDACSLQPDIDLLPfgdqteigergINLSGGQRQRICVARALYQNTNIVFL 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1820369315 432 DEPTSGVDPVARDMFWQL-MVDLARQDRVTIFISTHFMNEAERCDRISLMHAG 483
Cdd:cd03290 165 DDPFSALDIHLSDHLMQEgILKFLQDDKRTLVLVTHKLQYLPHADWIIAMKDG 217
|
|
| PRK13546 |
PRK13546 |
teichoic acids export ABC transporter ATP-binding subunit TagH; |
27-173 |
2.41e-08 |
|
teichoic acids export ABC transporter ATP-binding subunit TagH;
Pssm-ID: 184131 [Multi-domain] Cd Length: 264 Bit Score: 55.98 E-value: 2.41e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 27 ALRDISLAIPARRMVGLIGPDGVGKSSLLSLIAGARAIEQGNVMVLGgdmrdvhhrrDVcpKIAWMPQGLGKNLyhtlSV 106
Cdd:PRK13546 39 ALDDISLKAYEGDVIGLVGINGSGKSTLSNIIGGSLSPTVGKVDRNG----------EV--SVIAISAGLSGQL----TG 102
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1820369315 107 YENVDFFARLFGHDKAERELRINELLQSTGLAPFRDRPAGKLSGGMKQKLGLCCALIHDPQLLILDE 173
Cdd:PRK13546 103 IENIEFKMLCMGFKRKEIKAMTPKIIEFSELGEFIYQPVKKYSSGMRAKLGFSINITVNPDILVIDE 169
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
27-200 |
2.86e-08 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 56.64 E-value: 2.86e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 27 ALRDISLAIPARRMVGLIGPDGVGKSSLLSLIAGARAIEQGNVMVLGGDMRDVHH--RRDVCPKIAWMPQGLGKNLYHTL 104
Cdd:PRK15079 36 AVDGVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGEVAWLGKDLLGMKDdeWRAVRSDIQMIFQDPLASLNPRM 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 105 SVYENV-----DFFARLfghDKAERELRINELLQSTGLAP-FRDRPAGKLSGGMKQKLGLCCALIHDPQLLILDEPTTGV 178
Cdd:PRK15079 116 TIGEIIaeplrTYHPKL---SRQEVKDRVKAMMLKVGLLPnLINRYPHEFSGGQCQRIGIARALILEPKLIICDEPVSAL 192
|
170 180
....*....|....*....|..
gi 1820369315 179 DPLSRAQfweLIDSIRQRQPEM 200
Cdd:PRK15079 193 DVSIQAQ---VVNLLQQLQREM 211
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
266-485 |
6.51e-08 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 56.34 E-value: 6.51e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 266 PPRDSREEEIAIEARGLTMR---FGNFVAVDHVNFRIARGEIFGFLGSNGCGKsTTMKMltGLLPAS-----EGEAWLFG 337
Cdd:NF040905 247 PERTPKIGEVVFEVKNWTVYhplHPERKVVDDVSLNVRRGEIVGIAGLMGAGR-TELAM--SVFGRSygrniSGTVFKDG 323
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 338 QPVDPKDI--ATRQRVGYMSQ---AFSLYSELSVRQNLELhARL-----FHIPDDEIAHRVAEMSERFMltEVK----DA 403
Cdd:NF040905 324 KEVDVSTVsdAIDAGLAYVTEdrkGYGLNLIDDIKRNITL-ANLgkvsrRGVIDENEEIKVAEEYRKKM--NIKtpsvFQ 400
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 404 LPADLPLGIRQRLSLAVAVIHRPEMLILDEPTSGVDPVARDMFWQLMVDLARQDRVTIFISTHfMNEA-ERCDRISLMHA 482
Cdd:NF040905 401 KVGNLSGGNQQKVVLSKWLFTDPDVLILDEPTRGIDVGAKYEIYTIINELAAEGKGVIVISSE-LPELlGMCDRIYVMNE 479
|
...
gi 1820369315 483 GKV 485
Cdd:NF040905 480 GRI 482
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
28-238 |
8.05e-08 |
|
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The CFTR subfamily domain 1. The cystic fibrosis transmembrane regulator (CFTR), the product of the gene mutated in patients with cystic fibrosis, has adapted the ABC transporter structural motif to form a tightly regulated anion channel at the apical surface of many epithelia. Use of the term assembly of a functional ion channel implies the coming together of subunits, or at least smaller not-yet functional components of the active whole. In fact, on the basis of current knowledge only the CFTR polypeptide itself is required to form an ATP- and protein kinase A-dependent low-conductance chloride channel of the type present in the apical membrane of many epithelial cells. CFTR displays the typical organization (IM-ABC)2 and carries a characteristic hydrophilic R-domain that separates IM1-ABC1 from IM2-ABC2.
Pssm-ID: 213258 [Multi-domain] Cd Length: 282 Bit Score: 54.86 E-value: 8.05e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 28 LRDISLAIPARRMVGLIGPDGVGKSSLLSLIAGARAIEQGNVMVLGgdmrdvhhRRDVCPKIAW-MPQGLGKNLYHTLSV 106
Cdd:cd03291 53 LKNINLKIEKGEMLAITGSTGSGKTSLLMLILGELEPSEGKIKHSG--------RISFSSQFSWiMPGTIKENIIFGVSY 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 107 ----YENVDFFARLfGHDKAERELRINELLQSTGLApfrdrpagkLSGGMKQKLGLCCALIHDPQLLILDEPTTGVDPLS 182
Cdd:cd03291 125 deyrYKSVVKACQL-EEDITKFPEKDNTVLGEGGIT---------LSGGQRARISLARAVYKDADLYLLDSPFGYLDVFT 194
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1820369315 183 RAQFWEliDSIRQRQPEMSVLVATAYMEEAERFDWLVAMNAGEVLATGSAAELKAQ 238
Cdd:cd03291 195 EKEIFE--SCVCKLMANKTRILVTSKMEHLKKADKILILHEGSSYFYGTFSELQSL 248
|
|
| ABC_UvrA_II |
cd03271 |
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair ... |
28-231 |
9.31e-08 |
|
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: 54.16 E-value: 9.31e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 28 LRDISLAIPARRMVGLIGPDGVGKSSL--------LSLIAGARAIEQGNVMVLGG------------------------- 74
Cdd:cd03271 11 LKNIDVDIPLGVLTCVTGVSGSGKSSLindtlypaLARRLHLKKEQPGNHDRIEGlehidkvividqspigrtprsnpat 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 75 ------DMRDVHHrrDVCPKIAWMPQGL-----GKNLYHTL--SVYENVDFFArlfGHDKAERELRineLLQSTGLAPFR 141
Cdd:cd03271 91 ytgvfdEIRELFC--EVCKGKRYNRETLevrykGKSIADVLdmTVEEALEFFE---NIPKIARKLQ---TLCDVGLGYIK 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 142 -DRPAGKLSGGMKQKLGLCCALIH---DPQLLILDEPTTGVDPLSRAQFWELIDSIRQRQPemSVLVATAYMEEAERFDW 217
Cdd:cd03271 163 lGQPATTLSGGEAQRIKLAKELSKrstGKTLYILDEPTTGLHFHDVKKLLEVLQRLVDKGN--TVVVIEHNLDVIKCADW 240
|
250 260
....*....|....*....|
gi 1820369315 218 LVAM------NAGEVLATGS 231
Cdd:cd03271 241 IIDLgpeggdGGGQVVASGT 260
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
295-440 |
9.56e-08 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 53.70 E-value: 9.56e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 295 VNFRIARGEIFGFLGSNGCGKSTTMKMLTGLLPASEGEAWLFGQPVDPKDiatRQR-VGYMSQAFSLYSELSVRQNLE-- 371
Cdd:PRK13543 30 LDFHVDAGEALLVQGDNGAGKTTLLRVLAGLLHVESGQIQIDGKTATRGD---RSRfMAYLGHLPGLKADLSTLENLHfl 106
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1820369315 372 --LHARlfhipddeiahRVAEMSERFM----LTEVKDALPADLPLGIRQRLSLAVAVIHRPEMLILDEPTSGVDP 440
Cdd:PRK13543 107 cgLHGR-----------RAKQMPGSALaivgLAGYEDTLVRQLSAGQKKRLALARLWLSPAPLWLLDEPYANLDL 170
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
295-498 |
1.11e-07 |
|
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: 54.48 E-value: 1.11e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 295 VNFRIARGEIFGFLGSNGCGKSTTMKMLTGLLPASEGEawlfgqpvdpkdIATRQRVGYMSQaFSLYSELSVRQNLelha 374
Cdd:cd03291 56 INLKIEKGEMLAITGSTGSGKTSLLMLILGELEPSEGK------------IKHSGRISFSSQ-FSWIMPGTIKENI---- 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 375 rLFHIPDDEIAHR----VAEMSERFMLTEVKDALP-----ADLPLGIRQRLSLAVAVIHRPEMLILDEPTSGVDPVA-RD 444
Cdd:cd03291 119 -IFGVSYDEYRYKsvvkACQLEEDITKFPEKDNTVlgeggITLSGGQRARISLARAVYKDADLYLLDSPFGYLDVFTeKE 197
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1820369315 445 MFWQLMVDL-ARQDRVTIfisTHFMNEAERCDRISLMHAGKVLASDTPQALVEQR 498
Cdd:cd03291 198 IFESCVCKLmANKTRILV---TSKMEHLKKADKILILHEGSSYFYGTFSELQSLR 249
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
294-505 |
1.14e-07 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 55.90 E-value: 1.14e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 294 HVNFRIARGEIFGFLGSNGCGKSTTMKMLTGLLPasegeawlfgqPVDPKDIATRQRVGYMSQAFSLYSElSVRQNLelh 373
Cdd:PLN03130 635 NINLDVPVGSLVAIVGSTGEGKTSLISAMLGELP-----------PRSDASVVIRGTVAYVPQVSWIFNA-TVRDNI--- 699
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 374 arLFHIPDD----EIAHRVAEMSERFML------TEVKDAlPADLPLGIRQRLSLAVAVIHRPEMLILDEPTSGVDP-VA 442
Cdd:PLN03130 700 --LFGSPFDperyERAIDVTALQHDLDLlpggdlTEIGER-GVNISGGQKQRVSMARAVYSNSDVYIFDDPLSALDAhVG 776
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1820369315 443 RDMFWQLMVD-LARQDRVTIFISTHFMNeaeRCDRISLMHAGKV--------LASDTP--QALVEQrgAASLEE 505
Cdd:PLN03130 777 RQVFDKCIKDeLRGKTRVLVTNQLHFLS---QVDRIILVHEGMIkeegtyeeLSNNGPlfQKLMEN--AGKMEE 845
|
|
| ABCC_SUR2 |
cd03288 |
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The ... |
274-498 |
1.36e-07 |
|
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The sulfonylurea receptor SUR is an ATP binding cassette (ABC) protein of the ABCC/MRP family. Unlike other ABC proteins, it has no intrinsic transport function, neither active nor passive, but associates with the potassium channel proteins Kir6.1 or Kir6.2 to form the ATP-sensitive potassium (K(ATP)) channel. Within the channel complex, SUR serves as a regulatory subunit that fine-tunes the gating of Kir6.x in response to alterations in cellular metabolism. It constitutes a major pharmaceutical target as it binds numerous drugs, K(ATP) channel openers and blockers, capable of up- or down-regulating channel activity.
Pssm-ID: 213255 [Multi-domain] Cd Length: 257 Bit Score: 53.76 E-value: 1.36e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 274 EIAIEarGLTMRFGNFV--AVDHVNFRIARGEIFGFLGSNGCGKSTTMKMLTGLLPASEGEAWLFGQPVDPKDIAT-RQR 350
Cdd:cd03288 19 EIKIH--DLCVRYENNLkpVLKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVIDGIDISKLPLHTlRSR 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 351 VGYMSQAFSLYSElSVRQNLELHARlfhIPDDeiahRVAEMSERFMLTEVKDALPADL-----------PLGIRQRLSLA 419
Cdd:cd03288 97 LSIILQDPILFSG-SIRFNLDPECK---CTDD----RLWEALEIAQLKNMVKSLPGGLdavvteggenfSVGQRQLFCLA 168
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1820369315 420 VAVIHRPEMLILDEPTSGVDpVARDMFWQLMVDLARQDRVTIFIStHFMNEAERCDRISLMHAGKVLASDTPQALVEQR 498
Cdd:cd03288 169 RAFVRKSSILIMDEATASID-MATENILQKVVMTAFADRTVVTIA-HRVSTILDADLVLVLSRGILVECDTPENLLAQE 245
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
7-183 |
3.67e-07 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 53.87 E-value: 3.67e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 7 DTSPPIaLLENVGQQYGATIALRDISLAIPARRMVGLIGPDGVGKSSLLSLIAGARAieQG--NVMVLGGdmrdvhHRR- 83
Cdd:PRK10938 256 ANEPRI-VLNNGVVSYNDRPILHNLSWQVNPGEHWQIVGPNGAGKSTLLSLITGDHP--QGysNDLTLFG------RRRg 326
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 84 ------DVCPKIAWMPQGLGKNlYHTLSVYENV---DFF----------ARLfgHDKAERELRINELLQSTGLAPFRDrp 144
Cdd:PRK10938 327 sgetiwDIKKHIGYVSSSLHLD-YRVSTSVRNVilsGFFdsigiyqavsDRQ--QKLAQQWLDILGIDKRTADAPFHS-- 401
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1820369315 145 agkLSGGmKQKLGLCC-ALIHDPQLLILDEPTTGVDPLSR 183
Cdd:PRK10938 402 ---LSWG-QQRLALIVrALVKHPTLLILDEPLQGLDPLNR 437
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
148-251 |
5.35e-07 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 52.01 E-value: 5.35e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 148 LSGGMKQKLGLCCALIHDPQLLILDEPTTGVDPLSRAQFWELIDSIRQRQpEMSVLVATAYMEEAERF-DWLVAMNAGEV 226
Cdd:PRK10418 141 MSGGMLQRMMIALALLCEAPFIIADEPTTDLDVVAQARILDLLESIVQKR-ALGMLLVTHDMGVVARLaDDVAVMSHGRI 219
|
90 100
....*....|....*....|....*...
gi 1820369315 227 LATGSAAELKAQTGS---QTLEQAFIAL 251
Cdd:PRK10418 220 VEQGDVETLFNAPKHavtRSLVSAHLAL 247
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
27-180 |
6.95e-07 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 52.01 E-value: 6.95e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 27 ALRDISLAIPARRMVGLIGPDGVGKSSLLSLIAGARAIEQGNVMVLGGD-----------------------MRDVHHRR 83
Cdd:PRK13651 22 ALDNVSVEINQGEFIAIIGQTGSGKTTFIEHLNALLLPDTGTIEWIFKDeknkkktkekekvleklviqktrFKKIKKIK 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 84 DVCPKIAWMPQGLGKNLYHTlSVYENVDFFARLFGHDKAERELRINELLQSTGL-APFRDRPAGKLSGGMKQKLGLCCAL 162
Cdd:PRK13651 102 EIRRRVGVVFQFAEYQLFEQ-TIEKDIIFGPVSMGVSKEEAKKRAAKYIELVGLdESYLQRSPFELSGGQKRRVALAGIL 180
|
170
....*....|....*...
gi 1820369315 163 IHDPQLLILDEPTTGVDP 180
Cdd:PRK13651 181 AMEPDFLVFDEPTAGLDP 198
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
17-356 |
7.39e-07 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 52.97 E-value: 7.39e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 17 NVGQQYGATIALRDISLAIPARRMVGLIGPDGVGKSSLLSLIAGARAIEQGNVMVlggdmrDVHHRrdvcpkiawmpqgL 96
Cdd:PRK15064 6 NITMQFGAKPLFENISVKFGGGNRYGLIGANGCGKSTFMKILGGDLEPSAGNVSL------DPNER-------------L 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 97 GKnL------YHTLSVYENVdffarLFGHD-----KAER--------------------------------ELRINELLQ 133
Cdd:PRK15064 67 GK-LrqdqfaFEEFTVLDTV-----IMGHTelwevKQERdriyalpemseedgmkvadlevkfaemdgytaEARAGELLL 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 134 STGLA-PFRDRPAGKLSGGMKQKLGLCCALIHDPQLLILDEPTTGVDplsraqfwelIDSIR-------QRQPEM----- 200
Cdd:PRK15064 141 GVGIPeEQHYGLMSEVAPGWKLRVLLAQALFSNPDILLLDEPTNNLD----------INTIRwledvlnERNSTMiiish 210
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 201 ------SVLVATA----------------YMEEA----ERfdwLVAMNAGevlATGSAAELkaqtgsQTLEQAFIALLPE 254
Cdd:PRK15064 211 drhflnSVCTHMAdldygelrvypgnydeYMTAAtqarER---LLADNAK---KKAQIAEL------QSFVSRFSANASK 278
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 255 A------QRQAHKtvvIPPRD----SR-------EEE-----IAIEARGLTMRFGNFVAVDHVNFRIARGEIFGFLGSNG 312
Cdd:PRK15064 279 AkqatsrAKQIDK---IKLEEvkpsSRqnpfirfEQDkklhrNALEVENLTKGFDNGPLFKNLNLLLEAGERLAIIGENG 355
|
410 420 430 440
....*....|....*....|....*....|....*....|....*
gi 1820369315 313 CGKSTTMKMLTGLLPASEGEA-WlfgqpvdpkdiATRQRVGYMSQ 356
Cdd:PRK15064 356 VGKTTLLRTLVGELEPDSGTVkW-----------SENANIGYYAQ 389
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
296-544 |
7.50e-07 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 52.71 E-value: 7.50e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 296 NFRIARGEIFGFLGSNGCGKSTTMKMLTGLLPASEGEAwlfgqpvdpkdIATRQRVGYMS--QAFSLYSELSVRQNLELH 373
Cdd:PRK10938 23 SLTLNAGDSWAFVGANGSGKSALARALAGELPLLSGER-----------QSQFSHITRLSfeQLQKLVSDEWQRNNTDML 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 374 ArlfhiPD-DEIAHRVAEMserfMLTEVKD-ALPADLP--LGIRQRLS---------------LAVAVIHRPEMLILDEP 434
Cdd:PRK10938 92 S-----PGeDDTGRTTAEI----IQDEVKDpARCEQLAqqFGITALLDrrfkylstgetrktlLCQALMSEPDLLILDEP 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 435 TSGVDPVARDMFWQLMVDLARQDRVTIFISTHFmneaercDRIS--LMHAGkVLASDTpqaLVEQ-RGAASLEEAFIAWL 511
Cdd:PRK10938 163 FDGLDVASRQQLAELLASLHQSGITLVLVLNRF-------DEIPdfVQFAG-VLADCT---LAETgEREEILQQALVAQL 231
|
250 260 270
....*....|....*....|....*....|....
gi 1820369315 512 KEAQPSSPVPEdPTSAVASHSEHTAPRQA-FSLR 544
Cdd:PRK10938 232 AHSEQLEGVQL-PEPDEPSARHALPANEPrIVLN 264
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
304-518 |
8.53e-07 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 52.18 E-value: 8.53e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 304 IFGFLGSngcGKSTTMKMLTGLLPASEGEAWLFGQP-VDP-KDI---ATRQRVGYMSQAFSLYSELSVRQNLELHARlfh 378
Cdd:PRK11144 29 IFGRSGA---GKTSLINAISGLTRPQKGRIVLNGRVlFDAeKGIclpPEKRRIGYVFQDARLFPHYKVRGNLRYGMA--- 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 379 ipddeiahrvAEMSERFM-------LTEVKDALPADLPLGIRQRLSLAVAVIHRPEMLILDEPTSGVD-PVARdmfwQLM 450
Cdd:PRK11144 103 ----------KSMVAQFDkivallgIEPLLDRYPGSLSGGEKQRVAIGRALLTAPELLLMDEPLASLDlPRKR----ELL 168
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1820369315 451 V---DLARQDRVTIFISTHFMNEAER-CDRISLMHAGKVLASDtpqalveqrgaaSLEE-----AFIAWLKEAQPSS 518
Cdd:PRK11144 169 PyleRLAREINIPILYVSHSLDEILRlADRVVVLEQGKVKAFG------------PLEEvwassAMRPWLPKEEQSS 233
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
292-464 |
1.05e-06 |
|
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding cassette transporter (Pat) is involved in the import of very long-chain fatty acids (VLCFA) into the peroxisome. The peroxisomal membrane forms a permeability barrier for a wide variety of metabolites required for and formed during fatty acid beta-oxidation. To communicate with the cytoplasm and mitochondria, peroxisomes need dedicated proteins to transport such hydrophilic molecules across their membranes. X-linked adrenoleukodystrophy (X-ALD) is caused by mutations in the ALD gene, which encodes ALDP (adrenoleukodystrophy protein ), a peroxisomal integral membrane protein that is a member of the ATP-binding cassette (ABC) transporter protein family. The disease is characterized by a striking and unpredictable variation in phenotypic expression. Phenotypes include the rapidly progressive childhood cerebral form (CCALD), the milder adult form, adrenomyeloneuropathy (AMN), and variants without neurologic involvement (i.e. asymptomatic).
Pssm-ID: 213190 [Multi-domain] Cd Length: 166 Bit Score: 49.46 E-value: 1.05e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 292 VDHVNFRIARGEIFGFLGSNGCGKSTTMKMLTGLLPASEGEAwlfgqpvdpkDIATRQRVGYMSQAfSLYSELSVRQNLe 371
Cdd:cd03223 17 LKDLSFEIKPGDRLLITGPSGTGKSSLFRALAGLWPWGSGRI----------GMPEGEDLLFLPQR-PYLPLGTLREQL- 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 372 lharlfhipddeiahrvaemserfmltevkdALPAD--LPLGIRQRLSLAVAVIHRPEMLILDEPTSGVDPVARDMFWQL 449
Cdd:cd03223 85 -------------------------------IYPWDdvLSGGEQQRLAFARLLLHKPKFVFLDEATSALDEESEDRLYQL 133
|
170
....*....|....*
gi 1820369315 450 MvdlarQDRVTIFIS 464
Cdd:cd03223 134 L-----KELGITVIS 143
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
22-224 |
1.14e-06 |
|
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The sulfonylurea receptor SUR is an ATP transporter of the ABCC/MRP family with tandem ATPase binding domains. Unlike other ABC proteins, it has no intrinsic transport function, neither active nor passive, but associates with the potassium channel proteins Kir6.1 or Kir6.2 to form the ATP-sensitive potassium (K(ATP)) channel. Within the channel complex, SUR serves as a regulatory subunit that fine-tunes the gating of Kir6.x in response to alterations in cellular metabolism. It constitutes a major pharmaceutical target as it binds numerous drugs, K(ATP) channel openers and blockers, capable of up- or down-regulating channel activity.
Pssm-ID: 213257 [Multi-domain] Cd Length: 218 Bit Score: 50.41 E-value: 1.14e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 22 YGATIA-LRDISLAIPARRMVGLIGPDGVGKSSLLSLIAGARAIEQGNVM-------VLGGDMRDVHHRRDVcpkiAWMP 93
Cdd:cd03290 10 WGSGLAtLSNINIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHwsnknesEPSFEATRSRNRYSV----AYAA 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 94 QglgKNLYHTLSVYENVDfFARLFGHDKAERELRINELLQSTGLAPFRDRP-----AGKLSGGMKQKLGLCCALIHDPQL 168
Cdd:cd03290 86 Q---KPWLLNATVEENIT-FGSPFNKQRYKAVTDACSLQPDIDLLPFGDQTeigerGINLSGGQRQRICVARALYQNTNI 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1820369315 169 LILDEPTTGVD-PLSRAQFWELIDSIRQRQPEMSVLVaTAYMEEAERFDWLVAMNAG 224
Cdd:cd03290 162 VFLDDPFSALDiHLSDHLMQEGILKFLQDDKRTLVLV-THKLQYLPHADWIIAMKDG 217
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
104-240 |
1.14e-06 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 52.72 E-value: 1.14e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 104 LSVYENVDFfarlfGHDKAERE--------LRINELLQS------TGLAPFrdrpaGK-LSGGMKQKLGLCCALIHDPQL 168
Cdd:PTZ00265 1310 MSIYENIKF-----GKEDATREdvkrackfAAIDEFIESlpnkydTNVGPY-----GKsLSGGQKQRIAIARALLREPKI 1379
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1820369315 169 LILDEPTTGVDPLSRAQFWELIDSIRQRQPEMSVLVATAyMEEAERFDWLVAMNAGE-----VLATGSAAE-LKAQTG 240
Cdd:PTZ00265 1380 LLLDEATSSLDSNSEKLIEKTIVDIKDKADKTIITIAHR-IASIKRSDKIVVFNNPDrtgsfVQAHGTHEElLSVQDG 1456
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
16-179 |
1.55e-06 |
|
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: 51.86 E-value: 1.55e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 16 ENVGQQYGATIALRDISLAIPARRMVGLIGPDGVGKSSLLSLIAGARAIEQGNVMVlgGDMrdvhhrrdvcPKIAWMPQG 95
Cdd:TIGR03719 326 ENLTKAFGDKLLIDDLSFKLPPGGIVGVIGPNGAGKSTLFRMITGQEQPDSGTIEI--GET----------VKLAYVDQS 393
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 96 LgKNLYHTLSVYENVDffarlFGHDkaerELRIN--ELLQSTGLAPF------RDRPAGKLSGGMKQKLGLCCALIHDPQ 167
Cdd:TIGR03719 394 R-DALDPNKTVWEEIS-----GGLD----IIKLGkrEIPSRAYVGRFnfkgsdQQKKVGQLSGGERNRVHLAKTLKSGGN 463
|
170
....*....|..
gi 1820369315 168 LLILDEPTTGVD 179
Cdd:TIGR03719 464 VLLLDEPTNDLD 475
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
28-179 |
2.04e-06 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 51.90 E-value: 2.04e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 28 LRDISLAIPARRMVGLIGPDGVGKSSLLSLIAGARAIEQGNVMVLGGDMRDVhhrrdvcPKIAWMpqglgknlyHTLSVY 107
Cdd:PLN03232 633 LSDINLEIPVGSLVAIVGGTGEGKTSLISAMLGELSHAETSSVVIRGSVAYV-------PQVSWI---------FNATVR 696
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1820369315 108 ENVdFFARLFGHDKAERELRINELLQSTGLAPFRDRP-----AGKLSGGMKQKLGLCCALIHDPQLLILDEPTTGVD 179
Cdd:PLN03232 697 ENI-LFGSDFESERYWRAIDVTALQHDLDLLPGRDLTeigerGVNISGGQKQRVSMARAVYSNSDIYIFDDPLSALD 772
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
41-179 |
2.24e-06 |
|
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: 50.10 E-value: 2.24e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 41 VGLIGPDGVGKSSLLSLIAGARAIEQGNVMVLGgdmrdvhhrrdvcPKIAWMPQglgknlYHTLSVYENVDFFARLFGHD 120
Cdd:cd03237 28 IGILGPNGIGKTTFIKMLAGVLKPDEGDIEIEL-------------DTVSYKPQ------YIKADYEGTVRDLLSSITKD 88
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 1820369315 121 KAERELRINELLQSTGLAPFRDRPAGKLSGGMKQKLGLCCALIHDPQLLILDEPTTGVD 179
Cdd:cd03237 89 FYTHPYFKTEIAKPLQIEQILDREVPELSGGELQRVAIAACLSKDADIYLLDEPSAYLD 147
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
28-190 |
2.54e-06 |
|
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding cassette transporter (Pat) is involved in the import of very long-chain fatty acids (VLCFA) into the peroxisome. The peroxisomal membrane forms a permeability barrier for a wide variety of metabolites required for and formed during fatty acid beta-oxidation. To communicate with the cytoplasm and mitochondria, peroxisomes need dedicated proteins to transport such hydrophilic molecules across their membranes. X-linked adrenoleukodystrophy (X-ALD) is caused by mutations in the ALD gene, which encodes ALDP (adrenoleukodystrophy protein ), a peroxisomal integral membrane protein that is a member of the ATP-binding cassette (ABC) transporter protein family. The disease is characterized by a striking and unpredictable variation in phenotypic expression. Phenotypes include the rapidly progressive childhood cerebral form (CCALD), the milder adult form, adrenomyeloneuropathy (AMN), and variants without neurologic involvement (i.e. asymptomatic).
Pssm-ID: 213190 [Multi-domain] Cd Length: 166 Bit Score: 48.30 E-value: 2.54e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 28 LRDISLAIPARRMVGLIGPDGVGKSSLLSLIAGARAIEQGNVmvlggdmrDVHHRRDV--CPKIAWMPQGlgknlyhTLs 105
Cdd:cd03223 17 LKDLSFEIKPGDRLLITGPSGTGKSSLFRALAGLWPWGSGRI--------GMPEGEDLlfLPQRPYLPLG-------TL- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 106 vyenvdffarlfghdkaeRELRInellqstglAPFRDRpagkLSGGMKQKLGLCCALIHDPQLLILDEPTTGVDPLSRAQ 185
Cdd:cd03223 81 ------------------REQLI---------YPWDDV----LSGGEQQRLAFARLLLHKPKFVFLDEATSALDEESEDR 129
|
....*
gi 1820369315 186 FWELI 190
Cdd:cd03223 130 LYQLL 134
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
28-226 |
3.12e-06 |
|
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: 48.80 E-value: 3.12e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 28 LRDISLAIPARRMVGLIGPDGVGKSSLLSLIAGARAieqGNVMVLG--------GDMRDVHHRRDvcpkIAWMPQGlgKN 99
Cdd:cd03233 23 LKDFSGVVKPGEMVLVLGRPGSGCSTLLKALANRTE---GNVSVEGdihyngipYKEFAEKYPGE----IIYVSEE--DV 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 100 LYHTLSVYENVDFFARLFGHDKaereLRinellqstglapfrdrpagKLSGGMKQKLGLCCALIHDPQLLILDEPTTGVD 179
Cdd:cd03233 94 HFPTLTVRETLDFALRCKGNEF----VR-------------------GISGGERKRVSIAEALVSRASVLCWDNSTRGLD 150
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1820369315 180 PLSRAQFwelIDSIRQ--RQPEMSVLVAT--AYMEEAERFDWLVAMNAGEV 226
Cdd:cd03233 151 SSTALEI---LKCIRTmaDVLKTTTFVSLyqASDEIYDLFDKVLVLYEGRQ 198
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
4-191 |
3.27e-06 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 50.94 E-value: 3.27e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 4 TPQDTSPPIALLENVGQQYGATIALRDISL-AIPARRmVGLIGPDGVGKSSLLSLIAGARAIEQGNVMVLGGdmrdvhhr 82
Cdd:PRK10636 304 APESLPNPLLKMEKVSAGYGDRIILDSIKLnLVPGSR-IGLLGRNGAGKSTLIKLLAGELAPVSGEIGLAKG-------- 374
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 83 rdvcPKIAWMPQglgknlyHTLSvYENVD-----FFARLfghdkAERELRiNELLQSTGLAPFR-DR---PAGKLSGGMK 153
Cdd:PRK10636 375 ----IKLGYFAQ-------HQLE-FLRADesplqHLARL-----APQELE-QKLRDYLGGFGFQgDKvteETRRFSGGEK 436
|
170 180 190
....*....|....*....|....*....|....*....
gi 1820369315 154 QKLGLCCALIHDPQLLILDEPTTGVDPLSRAQFWE-LID 191
Cdd:PRK10636 437 ARLVLALIVWQRPNLLLLDEPTNHLDLDMRQALTEaLID 475
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
282-439 |
4.80e-06 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 50.55 E-value: 4.80e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 282 LTMRFGNFVAVDHVNFRIARGEIFGFLGSNGCGKSTTMKMLTGLLPASEGE---------AWLfGQPVDPKDIATRQRVG 352
Cdd:PRK10636 7 LQIRRGVRVLLDNATATINPGQKVGLVGKNGCGKSTLLALLKNEISADGGSytfpgnwqlAWV-NQETPALPQPALEYVI 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 353 YMSQAF-SLYSELSV--RQN-----LELHARLFHIPDDEIAHRVAEMSERFMLTEVKDALP-ADLPLGIRQRLSLAVAVI 423
Cdd:PRK10636 86 DGDREYrQLEAQLHDanERNdghaiATIHGKLDAIDAWTIRSRAASLLHGLGFSNEQLERPvSDFSGGWRMRLNLAQALI 165
|
170
....*....|....*.
gi 1820369315 424 HRPEMLILDEPTSGVD 439
Cdd:PRK10636 166 CRSDLLLLDEPTNHLD 181
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
302-442 |
5.39e-06 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 50.61 E-value: 5.39e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 302 GEIFGFLGSNGCGKSTTMKMLTGLLPAS--EGEAWLFGQPvdpKDIATRQRV-GYMSQAFSLYSELSVRQNLELHARL-- 376
Cdd:PLN03140 906 GVLTALMGVSGAGKTTLMDVLAGRKTGGyiEGDIRISGFP---KKQETFARIsGYCEQNDIHSPQVTVRESLIYSAFLrl 982
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1820369315 377 -FHIPDDEIAHRVAEMSERFMLTEVKDA---LPADLPLGI--RQRLSLAVAVIHRPEMLILDEPTSGVDPVA 442
Cdd:PLN03140 983 pKEVSKEEKMMFVDEVMELVELDNLKDAivgLPGVTGLSTeqRKRLTIAVELVANPSIIFMDEPTSGLDARA 1054
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
27-185 |
7.37e-06 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 49.19 E-value: 7.37e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 27 ALRDISLAIPARRMVGLIGPDGVGKSSL---LSLI----AGARAIEQGNVmvLGGDMRDVHHRRDvcpKIawmpQGLGKN 99
Cdd:PRK11308 30 ALDGVSFTLERGKTLAVVGESGCGKSTLarlLTMIetptGGELYYQGQDL--LKADPEAQKLLRQ---KI----QIVFQN 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 100 LYHTLS--------VYENVDFFARLfghDKAERELRINELLQSTGLAP-FRDRPAGKLSGGMKQKLGLCCALIHDPQLLI 170
Cdd:PRK11308 101 PYGSLNprkkvgqiLEEPLLINTSL---SAAERREKALAMMAKVGLRPeHYDRYPHMFSGGQRQRIAIARALMLDPDVVV 177
|
170
....*....|....*
gi 1820369315 171 LDEPTTGVDPLSRAQ 185
Cdd:PRK11308 178 ADEPVSALDVSVQAQ 192
|
|
| PRK13541 |
PRK13541 |
cytochrome c biogenesis protein CcmA; Provisional |
28-190 |
8.45e-06 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184128 [Multi-domain] Cd Length: 195 Bit Score: 47.56 E-value: 8.45e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 28 LRDISLAIPARRMVGLIGPDGVGKSSLLSLIAGARAIEQGNVMVLGGDMRDVHHrrdvcPKIAWMPQGLGKNLyhTLSVY 107
Cdd:PRK13541 16 LFDLSITFLPSAITYIKGANGCGKSSLLRMIAGIMQPSSGNIYYKNCNINNIAK-----PYCTYIGHNLGLKL--EMTVF 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 108 ENVDFFARLFghDKAErelRINELLQSTGLAPFRDRPAGKLSGGMKQKLGLCCALIHDPQLLILDEPTTGVDPLSRAQFW 187
Cdd:PRK13541 89 ENLKFWSEIY--NSAE---TLYAAIHYFKLHDLLDEKCYSLSSGMQKIVAIARLIACQSDLWLLDEVETNLSKENRDLLN 163
|
...
gi 1820369315 188 ELI 190
Cdd:PRK13541 164 NLI 166
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
149-195 |
9.78e-06 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 48.57 E-value: 9.78e-06
10 20 30 40
....*....|....*....|....*....|....*....|....*..
gi 1820369315 149 SGGMKQKLGLCCALIHDPQLLILDEPTTGVDPLSRAQFWELIDSIRQ 195
Cdd:PRK09473 163 SGGMRQRVMIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKR 209
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
29-205 |
9.99e-06 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 49.64 E-value: 9.99e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 29 RDISLAIPARRMVGLIGPDGVGKSSLLSLIAGARAIEQGNVMVlggdmRDVHHRRDVcpKIAWMPQGLG----------- 97
Cdd:PTZ00265 402 KDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIII-----NDSHNLKDI--NLKWWRSKIGvvsqdpllfsn 474
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 98 --KN-----LY-----HTLSVYENVDFFARLFGHDK-----AERELRINELLQ---STGLAPFRDR-------------- 143
Cdd:PTZ00265 475 siKNnikysLYslkdlEALSNYYNEDGNDSQENKNKrnscrAKCAGDLNDMSNttdSNELIEMRKNyqtikdsevvdvsk 554
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 144 ---------------------PAGKLSGGMKQKLGLCCALIHDPQLLILDEPTTGVDPLSRAQFWELIDSIRQRQPEMSV 202
Cdd:PTZ00265 555 kvlihdfvsalpdkyetlvgsNASKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQKTINNLKGNENRITI 634
|
...
gi 1820369315 203 LVA 205
Cdd:PTZ00265 635 IIA 637
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
28-235 |
1.20e-05 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 47.90 E-value: 1.20e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 28 LRDISLAIPARRMVGLIGPDGVGKSSLLSLIAG--ARAIEQGNVMVLGG-----------DMRDVHHRRDVCPKIAWMPQ 94
Cdd:PRK13547 17 LRDLSLRIEPGRVTALLGRNGAGKSTLLKALAGdlTGGGAPRGARVTGDvtlngeplaaiDAPRLARLRAVLPQAAQPAF 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 95 GLGKNLYHTLSVYENVDFFARLFGHDkaeRELrINELLQSTGLAPFRDRPAGKLSGGMKQKLGLCCAL---------IHD 165
Cdd:PRK13547 97 AFSAREIVLLGRYPHARRAGALTHRD---GEI-AWQALALAGATALVGRDVTTLSGGELARVQFARVLaqlwpphdaAQP 172
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1820369315 166 PQLLILDEPTTGVDplsRAQFWELIDSIRQ--RQPEMSVLVATAYMEEAERFDWLVAMNA-GEVLATGSAAEL 235
Cdd:PRK13547 173 PRYLLLDEPTAALD---LAHQHRLLDTVRRlaRDWNLGVLAIVHDPNLAARHADRIAMLAdGAIVAHGAPADV 242
|
|
| PRK13541 |
PRK13541 |
cytochrome c biogenesis protein CcmA; Provisional |
309-451 |
1.24e-05 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184128 [Multi-domain] Cd Length: 195 Bit Score: 47.17 E-value: 1.24e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 309 GSNGCGKSTTMKMLTGLLPASEGEawLFGQPVDPKDIAtRQRVGYMSQAFSLYSELSVRQNLELHARLFhipddEIAHRV 388
Cdd:PRK13541 33 GANGCGKSSLLRMIAGIMQPSSGN--IYYKNCNINNIA-KPYCTYIGHNLGLKLEMTVFENLKFWSEIY-----NSAETL 104
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1820369315 389 AEMSERFMLTEVKDALPADLPLGIRQRLSLAVAVIHRPEMLILDEPTSGVDPVARDMFWQLMV 451
Cdd:PRK13541 105 YAAIHYFKLHDLLDEKCYSLSSGMQKIVAIARLIACQSDLWLLDEVETNLSKENRDLLNNLIV 167
|
|
| 3a01203 |
TIGR00954 |
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ... |
290-466 |
1.26e-05 |
|
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: 48.98 E-value: 1.26e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 290 VAVDHVNFRIARGEIFGFLGSNGCGKSTTMKMLTGLLPASEG------EAWLFGQPVDP-KDIAT-RQRVGYMSQAFSL- 360
Cdd:TIGR00954 466 VLIESLSFEVPSGNNLLICGPNGCGKSSLFRILGELWPVYGGrltkpaKGKLFYVPQRPyMTLGTlRDQIIYPDSSEDMk 545
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 361 ---YSELSVRQNLELhARLFHIPDDEIAhrvaemserfmLTEVKDALPAdLPLGIRQRLSLAVAVIHRPEMLILDEPTSG 437
Cdd:TIGR00954 546 rrgLSDKDLEQILDN-VQLTHILEREGG-----------WSAVQDWMDV-LSGGEKQRIAMARLFYHKPQFAILDECTSA 612
|
170 180
....*....|....*....|....*....
gi 1820369315 438 VDPvarDMfWQLMVDLARQDRVTIFISTH 466
Cdd:TIGR00954 613 VSV---DV-EGYMYRLCREFGITLFSVSH 637
|
|
| SapD |
COG4170 |
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms]; |
148-267 |
1.42e-05 |
|
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms];
Pssm-ID: 443330 [Multi-domain] Cd Length: 331 Bit Score: 47.98 E-value: 1.42e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 148 LSGGMKQKLGLCCALIHDPQLLILDEPTTGVDPLSRAQFWELIDSIRQRQpEMSVLVATAYMEE-AERFDWLVAMNAGEV 226
Cdd:COG4170 159 LTEGECQKVMIAMAIANQPRLLIADEPTNAMESTTQAQIFRLLARLNQLQ-GTSILLISHDLESiSQWADTITVLYCGQT 237
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 1820369315 227 LATGSAAELKAQ-----TgsqtleQAFIALLPEAQRQ-AHKTV------VIPP 267
Cdd:COG4170 238 VESGPTEQILKSphhpyT------KALLRSMPDFRQPlPHKSRlntlpgSIPP 284
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
27-240 |
1.90e-05 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 48.17 E-value: 1.90e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 27 ALRDISLAIPARRMVGLIGPDGVGKSSLLSLIAGARAIEQGNVMVLGGDMRDVhhRRDvcpkiAWMPQglgknlyhtLSV 106
Cdd:PRK10789 330 ALENVNFTLKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGDIRFHDIPLTKL--QLD-----SWRSR---------LAV 393
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 107 YENVDFfarLF----------GHDKAERElrinELLQSTGLAPFRDR----PAG----------KLSGGMKQKLGLCCAL 162
Cdd:PRK10789 394 VSQTPF---LFsdtvannialGRPDATQQ----EIEHVARLASVHDDilrlPQGydtevgergvMLSGGQKQRISIARAL 466
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1820369315 163 IHDPQLLILDEPTTGVDPLSRAQfweLIDSIRQRQPEMSVLVATAYMEEAERFDWLVAMNAGEVLATGSAAELKAQTG 240
Cdd:PRK10789 467 LLNAEILILDDALSAVDGRTEHQ---ILHNLRQWGEGRTVIISAHRLSALTEASEILVMQHGHIAQRGNHDQLAQQSG 541
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
27-230 |
1.99e-05 |
|
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: 46.16 E-value: 1.99e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 27 ALRDISLAIPARRMVGLIGPDGVGKSSLLSLIAGARaieqgnvmvlggdmrdvhhrrdvcpkiawmpqglGKNLYHTlsv 106
Cdd:cd03238 10 NLQNLDVSIPLNVLVVVTGVSGSGKSTLVNEGLYAS----------------------------------GKARLIS--- 52
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 107 yenvdfFARLFGHDKAereLRINEL--LQSTGLAPFR-DRPAGKLSGGMKQKLGLCCALIHDPQ--LLILDEPTTGVDPL 181
Cdd:cd03238 53 ------FLPKFSRNKL---IFIDQLqfLIDVGLGYLTlGQKLSTLSGGELQRVKLASELFSEPPgtLFILDEPSTGLHQQ 123
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1820369315 182 SRAQFWELIDSIRQRQpeMSVLVATAYMEEAERFDWLVAM------NAGEVLATG 230
Cdd:cd03238 124 DINQLLEVIKGLIDLG--NTVILIEHNLDVLSSADWIIDFgpgsgkSGGKVVFSG 176
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
33-204 |
2.32e-05 |
|
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: 46.98 E-value: 2.32e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 33 LAIPARRMV-GLIGPDGVGKSSLLSLIAGA---------------------RAIEQGNVM--VLGGDMRDVHHRR--DVC 86
Cdd:cd03236 20 LPVPREGQVlGLVGPNGIGKSTALKILAGKlkpnlgkfddppdwdeildefRGSELQNYFtkLLEGDVKVIVKPQyvDLI 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 87 PKiawmpQGLGKnlyhTLSVYENVDffarlfghdkaERElRINELLQSTGLAPFRDRPAGKLSGGMKQKLGLCCALIHDP 166
Cdd:cd03236 100 PK-----AVKGK----VGELLKKKD-----------ERG-KLDELVDQLELRHVLDRNIDQLSGGELQRVAIAAALARDA 158
|
170 180 190
....*....|....*....|....*....|....*...
gi 1820369315 167 QLLILDEPTTGVDPLSRAQFWELIDSIrqRQPEMSVLV 204
Cdd:cd03236 159 DFYFFDEPSSYLDIKQRLNAARLIREL--AEDDNYVLV 194
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
45-180 |
3.87e-05 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 46.00 E-value: 3.87e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 45 GPDGVGKSSLLSLIAGARAIEQGNVMVlggdmrDVHH--RRDVCPKIAWMPQGLGknLYHTLSVYENVDFFARLfgHDKA 122
Cdd:PRK13543 44 GDNGAGKTTLLRVLAGLLHVESGQIQI------DGKTatRGDRSRFMAYLGHLPG--LKADLSTLENLHFLCGL--HGRR 113
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 1820369315 123 ERELRINELlQSTGLAPFRDRPAGKLSGGMKQKLGLCCALIHDPQLLILDEPTTGVDP 180
Cdd:PRK13543 114 AKQMPGSAL-AIVGLAGYEDTLVRQLSAGQKKRLALARLWLSPAPLWLLDEPYANLDL 170
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
138-179 |
4.45e-05 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 47.09 E-value: 4.45e-05
10 20 30 40
....*....|....*....|....*....|....*....|..
gi 1820369315 138 APFRDRPAGKLSGGMKQKLGLCCALIHDPQLLILDEPTTGVD 179
Cdd:NF040905 395 TPSVFQKVGNLSGGNQQKVVLSKWLFTDPDVLILDEPTRGID 436
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
147-221 |
5.35e-05 |
|
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: 44.66 E-value: 5.35e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1820369315 147 KLSGGMKQKLGLCCALIH----DPQLLILDEPTTGVDPLSRAQFWELIdsIRQRQPEMSVLVATAYMEEAERFDWLVAM 221
Cdd:cd03227 77 QLSGGEKELSALALILALaslkPRPLYILDEIDRGLDPRDGQALAEAI--LEHLVKGAQVIVITHLPELAELADKLIHI 153
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
84-235 |
7.75e-05 |
|
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: 46.54 E-value: 7.75e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 84 DVCPKIAWMPQGL-----GKNLYHTL--SVYENVDFFArlfGHDKAERELrinELLQSTGLAPFR-DRPAGKLSGGMKQK 155
Cdd:TIGR00630 764 EVCKGKRYNRETLevkykGKNIADVLdmTVEEAYEFFE---AVPSISRKL---QTLCDVGLGYIRlGQPATTLSGGEAQR 837
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 156 LGLCCALIHD---PQLLILDEPTTGvdpLSRAQFWELIDSIrQRQPEM--SVLVATAYMEEAERFDWLV------AMNAG 224
Cdd:TIGR00630 838 IKLAKELSKRstgRTLYILDEPTTG---LHFDDIKKLLEVL-QRLVDKgnTVVVIEHNLDVIKTADYIIdlgpegGDGGG 913
|
170
....*....|.
gi 1820369315 225 EVLATGSAAEL 235
Cdd:TIGR00630 914 TVVASGTPEEV 924
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
28-179 |
7.99e-05 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 46.65 E-value: 7.99e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 28 LRDISLAIPARRMVGLIGPDGVGKSSLLSLIAGARAIEQGNVMVLGGDMRDVhhrrdvcPKIAWMpqglgknlyHTLSVY 107
Cdd:PLN03130 633 LSNINLDVPVGSLVAIVGSTGEGKTSLISAMLGELPPRSDASVVIRGTVAYV-------PQVSWI---------FNATVR 696
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1820369315 108 ENVdFFARLFGHDKAERELRINELLQSTGLAPFRDRP-----AGKLSGGMKQKLGLCCALIHDPQLLILDEPTTGVD 179
Cdd:PLN03130 697 DNI-LFGSPFDPERYERAIDVTALQHDLDLLPGGDLTeigerGVNISGGQKQRVSMARAVYSNSDVYIFDDPLSALD 772
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
28-237 |
1.04e-04 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 46.26 E-value: 1.04e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 28 LRDISLAIPARRMVGLIGPDGVGKSSLLSLIAGAraIEQGNVMVLGGDMRDVHHRRDVcpkiawMPQGLGKNLY------ 101
Cdd:TIGR00956 77 LKPMDGLIKPGELTVVLGRPGSGCSTLLKTIASN--TDGFHIGVEGVITYDGITPEEI------KKHYRGDVVYnaetdv 148
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 102 H--TLSVYENVDFFARL-------FGHDKAERELRINELLQST-GLAPFRDRPAGK-----LSGGMKQKLGLCCALIHDP 166
Cdd:TIGR00956 149 HfpHLTVGETLDFAARCktpqnrpDGVSREEYAKHIADVYMATyGLSHTRNTKVGNdfvrgVSGGERKRVSIAEASLGGA 228
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1820369315 167 QLLILDEPTTGVDPLSRAQFwelidsIRQRQPEMSVLVATAYM------EEA-ERFDWLVAMNAGEVLATGSAAELKA 237
Cdd:TIGR00956 229 KIQCWDNATRGLDSATALEF------IRALKTSANILDTTPLVaiyqcsQDAyELFDKVIVLYEGYQIYFGPADKAKQ 300
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
358-477 |
1.17e-04 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 46.18 E-value: 1.17e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 358 FSLYSELSVRQNLELHARLFHIPDDEIAHRVAEMSERFMLTEVKDALP-----------ADLPLGIRQRLSLAVAVIHRP 426
Cdd:PTZ00265 1298 FSIVSQEPMLFNMSIYENIKFGKEDATREDVKRACKFAAIDEFIESLPnkydtnvgpygKSLSGGQKQRIAIARALLREP 1377
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 1820369315 427 EMLILDEPTSGVDPVARDMFWQLMVDLARQDRVTIFISTHFMNEAERCDRI 477
Cdd:PTZ00265 1378 KILLLDEATSSLDSNSEKLIEKTIVDIKDKADKTIITIAHRIASIKRSDKI 1428
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
295-485 |
1.49e-04 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 45.74 E-value: 1.49e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 295 VNFRIARGEIFGFLGSNGCGKSTTMKMLTGLLPasegeawlfgqPVDPKDIATRQRVGYMSQAFSLYSElSVRQNL---- 370
Cdd:PLN03232 636 INLEIPVGSLVAIVGGTGEGKTSLISAMLGELS-----------HAETSSVVIRGSVAYVPQVSWIFNA-TVRENIlfgs 703
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 371 ----ELHAR------LFHIPDDEIAHRVAEMSERfmltevkdalPADLPLGIRQRLSLAVAVIHRPEMLILDEPTSGVDP 440
Cdd:PLN03232 704 dfesERYWRaidvtaLQHDLDLLPGRDLTEIGER----------GVNISGGQKQRVSMARAVYSNSDIYIFDDPLSALDA 773
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1820369315 441 -VARDMFWQLMVD-LARQDRVTIFISTHFMNEAercDRISLMHAGKV 485
Cdd:PLN03232 774 hVAHQVFDSCMKDeLKGKTRVLVTNQLHFLPLM---DRIILVSEGMI 817
|
|
| PRK15093 |
PRK15093 |
peptide ABC transporter ATP-binding protein SapD; |
124-262 |
1.72e-04 |
|
peptide ABC transporter ATP-binding protein SapD;
Pssm-ID: 185049 [Multi-domain] Cd Length: 330 Bit Score: 44.79 E-value: 1.72e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 124 RELRINELLQSTGLAPFRDRPAG---KLSGGMKQKLGLCCALIHDPQLLILDEPTTGVDPLSRAQFWELIDSIRQRQPEM 200
Cdd:PRK15093 132 RKRRAIELLHRVGIKDHKDAMRSfpyELTEGECQKVMIAIALANQPRLLIADEPTNAMEPTTQAQIFRLLTRLNQNNNTT 211
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1820369315 201 SVLVATAYMEEAERFDWLVAMNAGEVLATGSAAELKAqTGSQTLEQAFIALLPEAQRQ-AHKT 262
Cdd:PRK15093 212 ILLISHDLQMLSQWADKINVLYCGQTVETAPSKELVT-TPHHPYTQALIRAIPDFGSAmPHKS 273
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
302-461 |
1.88e-04 |
|
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: 44.28 E-value: 1.88e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 302 GEIFGFLGSNGCGKSTTMKMLTGLLPASEGEawlFGQPVDPKDIATRQRVGYMSQAFSLYSELSVR-----QNLELHARL 376
Cdd:cd03236 26 GQVLGLVGPNGIGKSTALKILAGKLKPNLGK---FDDPPDWDEILDEFRGSELQNYFTKLLEGDVKvivkpQYVDLIPKA 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 377 FHIPDDEIAHRVAE------MSERFMLTEVKDALPADLPLGIRQRLSLAVAVIHRPEMLILDEPTSGVDPVARDMFWQLM 450
Cdd:cd03236 103 VKGKVGELLKKKDErgkldeLVDQLELRHVLDRNIDQLSGGELQRVAIAAALARDADFYFFDEPSSYLDIKQRLNAARLI 182
|
170
....*....|.
gi 1820369315 451 VDLARQDRVTI 461
Cdd:cd03236 183 RELAEDDNYVL 193
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
40-179 |
3.22e-04 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 44.49 E-value: 3.22e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 40 MVGLIGPDGVGKSSLLSLIAGARaieQGNVM---VLGGDMRDVhhrRDVCPKIAWMPQGlgKNLYHTLSVYENVDFFARL 116
Cdd:PLN03211 96 ILAVLGPSGSGKSTLLNALAGRI---QGNNFtgtILANNRKPT---KQILKRTGFVTQD--DILYPHLTVRETLVFCSLL 167
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1820369315 117 F---GHDKAERELRINELLQSTGLAPFRDRPAGK-----LSGGMKQKLGLCCALIHDPQLLILDEPTTGVD 179
Cdd:PLN03211 168 RlpkSLTKQEKILVAESVISELGLTKCENTIIGNsfirgISGGERKRVSIAHEMLINPSLLILDEPTSGLD 238
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
368-542 |
3.40e-04 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 44.82 E-value: 3.40e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 368 QNLELHARLFHIPDdeIAHRVAEMSERFMLTEVK-------------DALPADLPL-----GIRQRLSLA---VAVIHRP 426
Cdd:PRK00635 754 QVLEVRYKGKNIAD--ILEMTAYEAEKFFLDEPSihekihalcslglDYLPLGRPLsslsgGEIQRLKLAyelLAPSKKP 831
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 427 EMLILDEPTSGVDPVARDMFWQLMVDLARQDRvTIFISTHFMNEAERCDRISLM------HAGKVLASDTPQALVEQR-- 498
Cdd:PRK00635 832 TLYVLDEPTTGLHTHDIKALIYVLQSLTHQGH-TVVIIEHNMHVVKVADYVLELgpeggnLGGYLLASCSPEELIHLHtp 910
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1820369315 499 GAASLEEAF-----IAWLKEAQPSSPVPEDPTSAVASHS--EH---TAPRQAFS 542
Cdd:PRK00635 911 TAKALRPYLsspqeLPYLPDPSPKPPVPADITIKNAYQHnlKHidlSLPRNALT 964
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
16-71 |
3.67e-04 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 44.34 E-value: 3.67e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 1820369315 16 ENVGQQYGATIALRDISLAIPARRMVGLIGPDGVGKSSLLSLIAGARAIEQGNVMV 71
Cdd:PRK11819 328 ENLSKSFGDRLLIDDLSFSLPPGGIVGIIGPNGAGKSTLFKMITGQEQPDSGTIKI 383
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
15-179 |
6.73e-04 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 43.34 E-value: 6.73e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 15 LENVGQQYGATIALRDISLAIPARRMVGLIGPDGVGKSSLLSLIAGARAIEQGNVmvlggdmrdvhhrrdvcpK------ 88
Cdd:PRK15064 322 VENLTKGFDNGPLFKNLNLLLEAGERLAIIGENGVGKTTLLRTLVGELEPDSGTV------------------Kwsenan 383
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 89 IAWMPQGLGKNLYHTLSVYENVDFFaRLFGHDkaERELR--INELLQSTGLAPfrdRPAGKLSGGMKQKLGLCCALIHDP 166
Cdd:PRK15064 384 IGYYAQDHAYDFENDLTLFDWMSQW-RQEGDD--EQAVRgtLGRLLFSQDDIK---KSVKVLSGGEKGRMLFGKLMMQKP 457
|
170
....*....|...
gi 1820369315 167 QLLILDEPTTGVD 179
Cdd:PRK15064 458 NVLVMDEPTNHMD 470
|
|
| PRK15369 |
PRK15369 |
two component system response regulator; |
158-244 |
1.07e-03 |
|
two component system response regulator;
Pssm-ID: 185267 [Multi-domain] Cd Length: 211 Bit Score: 41.22 E-value: 1.07e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 158 LCCALihDPQLLILDEPTTGVDPLsraqfwELIDSIRQRQPEMSVLVATAYMEEaerfdwlvaMNAGEVLATGSAAELKA 237
Cdd:PRK15369 44 ACRQL--EPDIVILDLGLPGMNGL------DVIPQLHQRWPAMNILVLTARQEE---------HMASRTLAAGALGYVLK 106
|
....*..
gi 1820369315 238 QTGSQTL 244
Cdd:PRK15369 107 KSPQQIL 113
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
4-179 |
1.08e-03 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 42.92 E-value: 1.08e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 4 TPQDT-SPPIALLENVGQQY-GATIALRDISLAIPARRMVGLIGPDGVGKSSLLSLIAGARAIEQGNVMvlggdmrdvhh 81
Cdd:PLN03073 499 TPDDRpGPPIISFSDASFGYpGGPLLFKNLNFGIDLDSRIAMVGPNGIGKSTILKLISGELQPSSGTVF----------- 567
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 82 rRDVCPKIAWMPQGL--GKNLYHTLSVYenvdfFARLFGhDKAERELRINelLQSTGLA-PFRDRPAGKLSGGMKQKLGL 158
Cdd:PLN03073 568 -RSAKVRMAVFSQHHvdGLDLSSNPLLY-----MMRCFP-GVPEQKLRAH--LGSFGVTgNLALQPMYTLSGGQKSRVAF 638
|
170 180
....*....|....*....|.
gi 1820369315 159 CCALIHDPQLLILDEPTTGVD 179
Cdd:PLN03073 639 AKITFKKPHILLLDEPSNHLD 659
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
28-178 |
1.16e-03 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 42.89 E-value: 1.16e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 28 LRDISLAIPARRMVGLIGPDGVGKSSLL--SLI-AGARAIEQG---NVMVLGGDM-RDVHHRRDV--------------- 85
Cdd:PRK00635 611 LKDLTISLPLGRLTVVTGVSGSGKSSLIndTLVpAVEEFIEQGfcsNLSIQWGAIsRLVHITRDLpgrsqrsipltyika 690
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 86 ----------------------------------------------------CPKIA---WMPQGL-----GKNLYHTL- 104
Cdd:PRK00635 691 fddlrelfaeqprskrlgltkshfsfntplgacaecqglgsitttdnrtsipCPSCLgkrFLPQVLevrykGKNIADILe 770
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 105 -SVYENVDFFarlFGHDKAERELrinELLQSTGLA--PFrDRPAGKLSGGMKQKLGLCCALIH---DPQLLILDEPTTGV 178
Cdd:PRK00635 771 mTAYEAEKFF---LDEPSIHEKI---HALCSLGLDylPL-GRPLSSLSGGEIQRLKLAYELLApskKPTLYVLDEPTTGL 843
|
|
| ABC2_membrane_4 |
pfam12730 |
ABC-2 family transporter protein; This family is related to the ABC-2 membrane transporter ... |
727-839 |
1.18e-03 |
|
ABC-2 family transporter protein; This family is related to the ABC-2 membrane transporter family pfam01061.
Pssm-ID: 403819 Cd Length: 179 Bit Score: 40.65 E-value: 1.18e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 727 LLLMMIPAMLSALSVVREKELGSIINLYVTPTTRSEFLLGKqlpYIVLGMFNFF--LLCALSVFVFGV-AHKGSFLTLTL 803
Cdd:pfam12730 58 LLLPIILGIIASYLFFREYDNDTLKNLLTIPVSRRKLLFAK---LIVLLLLSVLfmLVTFLITVLFGLlSGFVGFSWGLI 134
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 1820369315 804 AALLYVTIATGLG--------LLISTFMKSQIAAIfgtaIITLI 839
Cdd:pfam12730 135 LYLLKKCLEIGLLvffavlpiIALALLFKGYVLPV----ILTLV 174
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
282-360 |
1.50e-03 |
|
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: 40.63 E-value: 1.50e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 282 LTMRFGNFvavdHVNFR---IARGEIFGFLGSNGCGKSTTMKMLTGLLpasegeawlfgQPVDPKDIATRQRVGYMSQAF 358
Cdd:cd03222 6 CVKRYGVF----FLLVElgvVKEGEVIGIVGPNGTGKTTAVKILAGQL-----------IPNGDNDEWDGITPVYKPQYI 70
|
..
gi 1820369315 359 SL 360
Cdd:cd03222 71 DL 72
|
|
| ABC_Rad50 |
cd03240 |
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ... |
294-440 |
2.39e-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: 40.28 E-value: 2.39e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 294 HVNFRIA-RGEIFGFLGSNGCGKSTTM---KM-LTGLLPASegeawLFGQPVDPKDIATRQRVGYMSQAFSLYS--ELSV 366
Cdd:cd03240 13 HERSEIEfFSPLTLIVGQNGAGKTTIIealKYaLTGELPPN-----SKGGAHDPKLIREGEVRAQVKLAFENANgkKYTI 87
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1820369315 367 RQNLELHARLFHIPDDEIAHRVAEMSERfmLTEVKDALpadlpLGIRQRLSLAVAVIHRPEMLILDEPTSGVDP 440
Cdd:cd03240 88 TRSLAILENVIFCHQGESNWPLLDMRGR--CSGGEKVL-----ASLIIRLALAETFGSNCGILALDEPTTNLDE 154
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
270-486 |
2.80e-03 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 40.40 E-value: 2.80e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 270 SREEEIAIEARGLTMRFGNFVAVDHVNFRIARGEIFGFLGSNGCGKSTTMKMLTGlLPA---SEGEAWLFGQPVDPKDIA 346
Cdd:CHL00131 1 MNKNKPILEIKNLHASVNENEILKGLNLSINKGEIHAIMGPNGSGKSTLSKVIAG-HPAykiLEGDILFKGESILDLEPE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 347 TRQRVGyMSQAFSLYSELSVRQN-----LELHARLFHIPDDEIAH-----------RVAEMSERFMLTEVKDALPAdlpl 410
Cdd:CHL00131 80 ERAHLG-IFLAFQYPIEIPGVSNadflrLAYNSKRKFQGLPELDPlefleiineklKLVGMDPSFLSRNVNEGFSG---- 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1820369315 411 GIRQRLSLAVAVIHRPEMLILDEPTSGVDPVARDMFWQLMVDLARQDRVTIFIsTHFMNEAE--RCDRISLMHAGKVL 486
Cdd:CHL00131 155 GEKKRNEILQMALLDSELAILDETDSGLDIDALKIIAEGINKLMTSENSIILI-THYQRLLDyiKPDYVHVMQNGKII 231
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
97-317 |
4.17e-03 |
|
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of proteins of which all members for which functions are known except the UvrA proteins are involved in the transport of material through membranes. UvrA orthologs are involved in the recognition of DNA damage as a step in nucleotide excision repair. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 273184 [Multi-domain] Cd Length: 925 Bit Score: 41.15 E-value: 4.17e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 97 GKNL--YHTLSVYENVDFFARLFGHDK----AERELR--INEL--LQSTGLAPFR-DRPAGKLSGGMKQKLGLC----CA 161
Cdd:TIGR00630 427 GKSIadVSELSIREAHEFFNQLTLTPEekkiAEEVLKeiRERLgfLIDVGLDYLSlSRAAGTLSGGEAQRIRLAtqigSG 506
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 162 LIHdpQLLILDEPTTGVDPLSRAQfweLIDSIRQRQPEMSVLVATAYMEEAERF-DWLVAM------NAGEVLATGSAAE 234
Cdd:TIGR00630 507 LTG--VLYVLDEPSIGLHQRDNRR---LINTLKRLRDLGNTLIVVEHDEDTIRAaDYVIDIgpgageHGGEVVASGTPEE 581
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 235 LKAQTGSQT---LEQAFIALLPEAQRQAHKTvVIPPRDSREEEIaieaRGLTMRF--GNFVAVDhvnfriargeifgflG 309
Cdd:TIGR00630 582 ILANPDSLTgqyLSGRKKIEVPAERRPGNGK-FLTLKGARENNL----KNITVSIplGLFTCIT---------------G 641
|
....*...
gi 1820369315 310 SNGCGKST 317
Cdd:TIGR00630 642 VSGSGKST 649
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
301-466 |
5.77e-03 |
|
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: 38.51 E-value: 5.77e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 301 RGEIFGFLGSNGCGKSTTMKMLTGLLPASEGEAwlfgqpvdpkdiatrqrvgymsqafslyselsvrqnLELHARLFHIP 380
Cdd:smart00382 1 PGEVILIVGPPGSGKTTLARALARELGPPGGGV------------------------------------IYIDGEDILEE 44
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820369315 381 DDEIAHRVAEMSERFMLTEVKdalpadlplgiRQRLSLAVAVIHRPEMLILDEPTSGVDPVARDM-----FWQLMVDLAR 455
Cdd:smart00382 45 VLDQLLLIIVGGKKASGSGEL-----------RLRLALALARKLKPDVLILDEITSLLDAEQEALlllleELRLLLLLKS 113
|
170
....*....|.
gi 1820369315 456 QDRVTIFISTH 466
Cdd:smart00382 114 EKNLTVILTTN 124
|
|
| |
