|
Name |
Accession |
Description |
Interval |
E-value |
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
8-915 |
0e+00 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 1887.14 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 8 VASLRGVSLRYGETRAVDDVSLEIPANRMVGLIGPDGVGKSSLLALLAGARKMQDGEIRVLDGDMRDRRHRRAVCPRIAY 87
Cdd:NF033858 1 VARLEGVSHRYGKTVALDDVSLDIPAGCMVGLIGPDGVGKSSLLSLIAGARKIQQGRVEVLGGDMADARHRRAVCPRIAY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 88 MPQGLGKNLYPTLSVFENVDFFGRLFGHDKAERERRIADLLQSTGLAPFAERPAGKLSGGMKQKLGLCCALIHDPDLLIL 167
Cdd:NF033858 81 MPQGLGKNLYPTLSVFENLDFFGRLFGQDAAERRRRIDELLRATGLAPFADRPAGKLSGGMKQKLGLCCALIHDPDLLIL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 168 DEPTTGVDPLSRNQFWELIGRIRAGREGMSVLVATAYMEEAERFDWLVAMDDGKVLATGTPQELRERTGTQSLESAFIAL 247
Cdd:NF033858 161 DEPTTGVDPLSRRQFWELIDRIRAERPGMSVLVATAYMEEAERFDWLVAMDAGRVLATGTPAELLARTGADTLEAAFIAL 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 248 LPESKRAGHHRLVIPPRPQSEGAPrIAIEAEGLTCRFGDFVAVDHVSFRIERGEIFGFLGSNGCGKSTTMKMLTGLLPAS 327
Cdd:NF033858 241 LPEEKRRGHQPVVIPPRPADDDDE-PAIEARGLTMRFGDFTAVDHVSFRIRRGEIFGFLGSNGCGKSTTMKMLTGLLPAS 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 328 EGTCALFGQPVDASDMATRRRVGYMSQAFSLYAELSVRQNLVLHARLFHLPADGIPARVGEMLRRFDLEKVADELPNDLP 407
Cdd:NF033858 320 EGEAWLFGQPVDAGDIATRRRVGYMSQAFSLYGELTVRQNLELHARLFHLPAAEIAARVAEMLERFDLADVADALPDSLP 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 408 LGIRQRLSLAVAVIHKPEILILDEPTSGVDPVARDGFWELMVELSRRDGVTIFISTHFMNEAQRCDRISLMHAGKVLASD 487
Cdd:NF033858 400 LGIRQRLSLAVAVIHKPELLILDEPTSGVDPVARDMFWRLLIELSREDGVTIFISTHFMNEAERCDRISLMHAGRVLASD 479
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 488 TPDELVRQRGLPTLEATFIAYLEEAAGAAAPAQPAEAPAVAEQPGDGQeRQAQRERFSPLRLFSYARREAMELRRDPIRL 567
Cdd:NF033858 480 TPAALVAARGAATLEEAFIAYLEEAAGAAAAPAAAAAPAAAAAAPAAP-APAPRRRFSLRRLLAYARREALELLRDPIRL 558
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 568 TLALLGTALLMFIIGYGINMDVEDLSWAVLDRDQTTTSQAYALNIAGSRYFVEHAPITDPDDLDRRLRSGELSLAVEIPP 647
Cdd:NF033858 559 TFALLGSVILMFVMGYGISLDVENLTFAVLDRDQTPESRAYLLNFAGSRYFIEQPPIADYAELDRRMRSGELSLAIEIPP 638
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 648 NFGRDLKRGSDPAIGVWIDGAMPTRANTVLGYVQGLHTSYLADLSRQAGGAEASAAASTEVRYRYNPDVESLKAMVPAVI 727
Cdd:NF033858 639 GFGRDLLRGRPPEVGAWIDGAMPFRAETIRGYVQGMHQQWLADLARERGGAAAASPATIETRYRYNPDFKSLPAMVPAVI 718
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 728 PLLLIMIPAMLTALGVVREKELGSITNLYVTPVTRLEFLVGKQLPYVAMGMINFLLMLVLAIVVFRVPLKGSFLALTIGA 807
Cdd:NF033858 719 PLLLMLIPAMLTALSVVREKELGSITNLYVTPVTRLEFLLGKQLPYVALAMLNFLLLVLLAVFVFGVPLKGSFLALALGA 798
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 808 FLYVVTSTGLGLFLSTFMRSQIAAVFGVAIATMIPAIQFSGLIHPVSSLEGAAAWIGKLYPTSHFLVVSRGAFSKSLGLS 887
Cdd:NF033858 799 LLYVTATTGLGLLISTFTRSQIAAIFGTAILTLIPAVQFSGLLDPVSSLEGAGRLIGRIFPATYFLTISRGTFTKGLGFA 878
|
890 900
....*....|....*....|....*...
gi 15600424 888 DLWAYYLPLAASIVVLTLLSVACLKKQE 915
Cdd:NF033858 879 DLWPSFLALAAFIPVLLGLSVLLLKKQE 906
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
275-506 |
3.82e-100 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 312.38 E-value: 3.82e-100
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 275 IEAEGLTCRFGDFVAVDHVSFRIERGEIFGFLGSNGCGKSTTMKMLTGLLPASEGTCALFGQPVDASDMATRRRVGYMSQ 354
Cdd:COG1131 1 IEVRGLTKRYGDKTALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRVLGEDVARDPAEVRRRIGYVPQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 355 AFSLYAELSVRQNLVLHARLFHLPADGIPARVGEMLRRFDLEKVADELPNDLPLGIRQRLSLAVAVIHKPEILILDEPTS 434
Cdd:COG1131 81 EPALYPDLTVRENLRFFARLYGLPRKEARERIDELLELFGLTDAADRKVGTLSGGMKQRLGLALALLHDPELLILDEPTS 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15600424 435 GVDPVARDGFWELMVELsRRDGVTIFISTHFMNEAQR-CDRISLMHAGKVLASDTPDELVRQrglpTLEATFI 506
Cdd:COG1131 161 GLDPEARRELWELLREL-AAEGKTVLLSTHYLEEAERlCDRVAIIDKGRIVADGTPDELKAR----LLEDVFL 228
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
10-253 |
8.68e-96 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 300.83 E-value: 8.68e-96
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 10 SLRGVSLRYGETRAVDDVSLEIPANRMVGLIGPDGVGKSSLLALLAGARKMQDGEIRVLDGDMRdrRHRRAVCPRIAYMP 89
Cdd:COG1131 2 EVRGLTKRYGDKTALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRVLGEDVA--RDPAEVRRRIGYVP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 90 QGLgkNLYPTLSVFENVDFFGRLFGHDKAERERRIADLLQSTGLAPFAERPAGKLSGGMKQKLGLCCALIHDPDLLILDE 169
Cdd:COG1131 80 QEP--ALYPDLTVRENLRFFARLYGLPRKEARERIDELLELFGLTDAADRKVGTLSGGMKQRLGLALALLHDPELLILDE 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 170 PTTGVDPLSRNQFWELIGRIRAgrEGMSVLVATAYMEEAERF-DWLVAMDDGKVLATGTPQELRERTgtqsLESAFIALL 248
Cdd:COG1131 158 PTSGLDPEARRELWELLRELAA--EGKTVLLSTHYLEEAERLcDRVAIIDKGRIVADGTPDELKARL----LEDVFLELT 231
|
....*
gi 15600424 249 PESKR 253
Cdd:COG1131 232 GEEAR 236
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
8-492 |
1.10e-93 |
|
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: 305.29 E-value: 1.10e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 8 VASLRGVSLRY--GETRAVDDVSLEIPANRMVGLIGPDGVGKSSLLALLAG---ARKMQDGEIRVLDGDMRDRRHRRAvC 82
Cdd:COG1123 4 LLEVRDLSVRYpgGDVPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGllpHGGRISGEVLLDGRDLLELSEALR-G 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 83 PRIAYMPQGLGKNLYPtLSVFENVDFFGRLFGHDKAERERRIADLLQSTGLAPFAERPAGKLSGGMKQKLGLCCALIHDP 162
Cdd:COG1123 83 RRIGMVFQDPMTQLNP-VTVGDQIAEALENLGLSRAEARARVLELLEAVGLERRLDRYPHQLSGGQRQRVAIAMALALDP 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 163 DLLILDEPTTGVDPLSRNQFWELIGRIRAgREGMSVLVATAYMEE-AERFDWLVAMDDGKVLATGTPQELRERtgTQSLE 241
Cdd:COG1123 162 DLLIADEPTTALDVTTQAEILDLLRELQR-ERGTTVLLITHDLGVvAEIADRVVVMDDGRIVEDGPPEEILAA--PQALA 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 242 SAfiallpesKRAGHHRLVIPPRPQsegAPRIAIEAEGLTCRF-----GDFVAVDHVSFRIERGEIFGFLGSNGCGKSTT 316
Cdd:COG1123 239 AV--------PRLGAARGRAAPAAA---AAEPLLEVRNLSKRYpvrgkGGVRAVDDVSLTLRRGETLGLVGESGSGKSTL 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 317 MKMLTGLLPASEGTCALFGQPVDASDMAT----RRRVGYMSQ--AFSLYAELSVRQNLVLHARLFH-LPADGIPARVGEM 389
Cdd:COG1123 308 ARLLLGLLRPTSGSILFDGKDLTKLSRRSlrelRRRVQMVFQdpYSSLNPRMTVGDIIAEPLRLHGlLSRAERRERVAEL 387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 390 LRRFDL-EKVADELPNDLPLGIRQRLSLAVAVIHKPEILILDEPTSGVDPVARDGFWELMVELSRRDGVT-IFIsTHFMN 467
Cdd:COG1123 388 LERVGLpPDLADRYPHELSGGQRQRVAIARALALEPKLLILDEPTSALDVSVQAQILNLLRDLQRELGLTyLFI-SHDLA 466
|
490 500
....*....|....*....|....*.
gi 15600424 468 EAQR-CDRISLMHAGKVLASDTPDEL 492
Cdd:COG1123 467 VVRYiADRVAVMYDGRIVEDGPTEEV 492
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
275-506 |
7.15e-73 |
|
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: 239.76 E-value: 7.15e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 275 IEAEGLTCRFGDFVAVDHVSFRIERGEIFGFLGSNGCGKSTTMKMLTGLLPASEGTCALFGQPVDASDMATRRRVGYMSQ 354
Cdd:COG4555 2 IEVENLSKKYGKVPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIDGEDVRKEPREARRQIGVLPD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 355 AFSLYAELSVRQNLVLHARLFHLPADGIPARVGEMLRRFDLEKVADELPNDLPLGIRQRLSLAVAVIHKPEILILDEPTS 434
Cdd:COG4555 82 ERGLYDRLTVRENIRYFAELYGLFDEELKKRIEELIELLGLEEFLDRRVGELSTGMKKKVALARALVHDPKVLLLDEPTN 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15600424 435 GVDPVARDGFWELMVELsRRDGVTIFISTHFMNEAQR-CDRISLMHAGKVLASDTPDELVRQRGLPTLEATFI 506
Cdd:COG4555 162 GLDVMARRLLREILRAL-KKEGKTVLFSSHIMQEVEAlCDRVVILHKGKVVAQGSLDELREEIGEENLEDAFV 233
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
275-483 |
3.68e-72 |
|
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: 234.98 E-value: 3.68e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 275 IEAEGLTCRFGDFVAVDHVSFRIERGEIFGFLGSNGCGKSTTMKMLTGLLPASEGTCALFGQPVDASDMATRRRVGYMSQ 354
Cdd:cd03230 1 IEVRNLSKRYGKKTALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVLGKDIKKEPEEVKRRIGYLPE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 355 AFSLYAELSVRQNLvlharlfhlpadgiparvgemlrrfdlekvadelpnDLPLGIRQRLSLAVAVIHKPEILILDEPTS 434
Cdd:cd03230 81 EPSLYENLTVRENL------------------------------------KLSGGMKQRLALAQALLHDPELLILDEPTS 124
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 15600424 435 GVDPVARDGFWELMVELsRRDGVTIFISTHFMNEAQR-CDRISLMHAGKV 483
Cdd:cd03230 125 GLDPESRREFWELLREL-KKEGKTILLSSHILEEAERlCDRVAILNNGRI 173
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
275-492 |
9.86e-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: 235.73 E-value: 9.86e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 275 IEAEGLTCRFGDFVAVDHVSFRIERGEIFGFLGSNGCGKSTTMKMLTGLLPASEGTCALFGQPVDASDMATRRRVGYMSQ 354
Cdd:cd03265 1 IEVENLVKKYGDFEAVRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATVAGHDVVREPREVRRRIGIVFQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 355 AFSLYAELSVRQNLVLHARLFHLPADGIPARVGEMLRRFDLEKVADELPNDLPLGIRQRLSLAVAVIHKPEILILDEPTS 434
Cdd:cd03265 81 DLSVDDELTGWENLYIHARLYGVPGAERRERIDELLDFVGLLEAADRLVKTYSGGMRRRLEIARSLVHRPEVLFLDEPTI 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 15600424 435 GVDPVARDGFWELMVELSRRDGVTIFISTHFMNEA-QRCDRISLMHAGKVLASDTPDEL 492
Cdd:cd03265 161 GLDPQTRAHVWEYIEKLKEEFGMTILLTTHYMEEAeQLCDRVAIIDHGRIIAEGTPEEL 219
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
274-502 |
2.59e-70 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 235.00 E-value: 2.59e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 274 AIEAEGLTCRFGDFVAVDHVSFRIERGEIFGFLGSNGCGKSTTMKMLTGLLPASEGTCALFGQPVDASDmatRRRVGYMS 353
Cdd:COG4152 1 MLELKGLTKRFGDKTAVDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDSGEVLWDGEPLDPED---RRRIGYLP 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 354 QAFSLYAELSVRQNLVLHARLFHLPADGIPARVGEMLRRFDLEKVADELPNDLPLGIRQRLSLAVAVIHKPEILILDEPT 433
Cdd:COG4152 78 EERGLYPKMKVGEQLVYLARLKGLSKAEAKRRADEWLERLGLGDRANKKVEELSKGNQQKVQLIAALLHDPELLILDEPF 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 434 SGVDPVARDGFWELMVELsRRDGVTIFISTHFMNEAQR-CDRISLMHAGKVLASDTPDELVRQRGLPTLE 502
Cdd:COG4152 158 SGLDPVNVELLKDVIREL-AAKGTTVIFSSHQMELVEElCDRIVIINKGRKVLSGSVDEIRRQFGRNTLR 226
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
11-252 |
1.59e-67 |
|
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: 225.12 E-value: 1.59e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 11 LRGVSLRYGETRAVDDVSLEIPANRMVGLIGPDGVGKSSLLALLAGARKMQDGEIRVLDGDMR--DRRHRRavcpRIAYM 88
Cdd:COG4555 4 VENLSKKYGKVPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIDGEDVRkePREARR----QIGVL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 89 PQGLGknLYPTLSVFENVDFFGRLFGHDKAERERRIADLLQSTGLAPFAERPAGKLSGGMKQKLGLCCALIHDPDLLILD 168
Cdd:COG4555 80 PDERG--LYDRLTVRENIRYFAELYGLFDEELKKRIEELIELLGLEEFLDRRVGELSTGMKKKVALARALVHDPKVLLLD 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 169 EPTTGVDPLSRNQFWELIGRIRAgrEGMSVLVATAYMEEAER-FDWLVAMDDGKVLATGTPQELRERTGTQSLESAFIAL 247
Cdd:COG4555 158 EPTNGLDVMARRLLREILRALKK--EGKTVLFSSHIMQEVEAlCDRVVILHKGKVVAQGSLDELREEIGEENLEDAFVAL 235
|
....*
gi 15600424 248 LPESK 252
Cdd:COG4555 236 IGSEE 240
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
275-492 |
4.83e-66 |
|
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: 220.45 E-value: 4.83e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 275 IEAEGLTCRFGD--FVAVDHVSFRIERGEIFGFLGSNGCGKSTTMKMLTGLLPASEGTCALFGQPVDASDMATRRRVGYM 352
Cdd:cd03263 1 LQIRNLTKTYKKgtKPAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYINGYSIRTDRKAARQSLGYC 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 353 SQAFSLYAELSVRQNLVLHARLFHLPADGIPARVGEMLRRFDLEKVADELPNDLPLGIRQRLSLAVAVIHKPEILILDEP 432
Cdd:cd03263 81 PQFDALFDELTVREHLRFYARLKGLPKSEIKEEVELLLRVLGLTDKANKRARTLSGGMKRKLSLAIALIGGPSVLLLDEP 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15600424 433 TSGVDPVARDGFWELMVELsrRDGVTIFISTHFMNEAQR-CDRISLMHAGKVLASDTPDEL 492
Cdd:cd03263 161 TSGLDPASRRAIWDLILEV--RKGRSIILTTHSMDEAEAlCDRIAIMSDGKLRCIGSPQEL 219
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
10-222 |
4.28e-62 |
|
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: 207.64 E-value: 4.28e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 10 SLRGVSLRYGETRAVDDVSLEIPANRMVGLIGPDGVGKSSLLALLAGARKMQDGEIRVLDGDMRdrRHRRAVCPRIAYMP 89
Cdd:cd03230 2 EVRNLSKRYGKKTALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVLGKDIK--KEPEEVKRRIGYLP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 90 QGLGknLYPTLSVFENVdffgrlfghdkaererriadllqstglapfaerpagKLSGGMKQKLGLCCALIHDPDLLILDE 169
Cdd:cd03230 80 EEPS--LYENLTVRENL------------------------------------KLSGGMKQRLALAQALLHDPELLILDE 121
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 15600424 170 PTTGVDPLSRNQFWELIGRIRagREGMSVLVATAYMEEAER-FDWLVAMDDGKV 222
Cdd:cd03230 122 PTSGLDPESRREFWELLRELK--KEGKTILLSSHILEEAERlCDRVAILNNGRI 173
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
10-232 |
2.58e-58 |
|
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: 198.88 E-value: 2.58e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 10 SLRGVSLRYGETR--AVDDVSLEIPANRMVGLIGPDGVGKSSLLALLAGARKMQDGEIRVLDGDMRdrRHRRAVCPRIAY 87
Cdd:cd03263 2 QIRNLTKTYKKGTkpAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYINGYSIR--TDRKAARQSLGY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 88 MPQGlgKNLYPTLSVFENVDFFGRLFGHDKAERERRIADLLQSTGLAPFAERPAGKLSGGMKQKLGLCCALIHDPDLLIL 167
Cdd:cd03263 80 CPQF--DALFDELTVREHLRFYARLKGLPKSEIKEEVELLLRVLGLTDKANKRARTLSGGMKRKLSLAIALIGGPSVLLL 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15600424 168 DEPTTGVDPLSRNQFWELIGRIRAGRegmSVLVATAYMEEAERF-DWLVAMDDGKVLATGTPQELR 232
Cdd:cd03263 158 DEPTSGLDPASRRAIWDLILEVRKGR---SIILTTHSMDEAEALcDRIAIMSDGKLRCIGSPQELK 220
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
275-485 |
3.85e-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: 198.27 E-value: 3.85e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 275 IEAEGLTCRFGDFVAVDHVSFRIERGEIFGFLGSNGCGKSTTMKMLTGLLPASEGTCALFGQPVDAsdmATRRRVGYMSQ 354
Cdd:cd03269 1 LEVENVTKRFGRVTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDGKPLDI---AARNRIGYLPE 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 355 AFSLYAELSVRQNLVLHARLFHLPADGIPARVGEMLRRFDLEKVADELPNDLPLGIRQRLSLAVAVIHKPEILILDEPTS 434
Cdd:cd03269 78 ERGLYPKMKVIDQLVYLAQLKGLKKEEARRRIDEWLERLELSEYANKRVEELSKGNQQKVQFIAAVIHDPELLILDEPFS 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 15600424 435 GVDPVARDGFWELMVELsRRDGVTIFISTHFMNEAQR-CDRISLMHAGKVLA 485
Cdd:cd03269 158 GLDPVNVELLKDVIREL-ARAGKTVILSTHQMELVEElCDRVLLLNKGRAVL 208
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
10-483 |
7.15e-56 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 201.40 E-value: 7.15e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 10 SLRGVSLRYGETRAVDDVSLEIPANRMVGLIGPDGVGKSSLLALLAGARKMQDGEIRvLDGDMRDRRHrravcPR----- 84
Cdd:COG1129 6 EMRGISKSFGGVKALDGVSLELRPGEVHALLGENGAGKSTLMKILSGVYQPDSGEIL-LDGEPVRFRS-----PRdaqaa 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 85 -IAYMPQGLgkNLYPTLSVFENVdFFGRLFGH----DKAERERRIADLLQSTGLAPFAERPAGKLSGGMKQKLGLCCALI 159
Cdd:COG1129 80 gIAIIHQEL--NLVPNLSVAENI-FLGREPRRggliDWRAMRRRARELLARLGLDIDPDTPVGDLSVAQQQLVEIARALS 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 160 HDPDLLILDEPTTgvdPLSRN---QFWELIGRIRAgrEGMSVLVATAYMEEAERF-DWLVAMDDGKVLATGTPQELRER- 234
Cdd:COG1129 157 RDARVLILDEPTA---SLTEReveRLFRIIRRLKA--QGVAIIYISHRLDEVFEIaDRVTVLRDGRLVGTGPVAELTEDe 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 235 -----TGtQSLESAFiallpeskraghhrlviPPRPQSEGAPriAIEAEGLTCRfgdfVAVDHVSFRIERGEIFGFLGSN 309
Cdd:COG1129 232 lvrlmVG-RELEDLF-----------------PKRAAAPGEV--VLEVEGLSVG----GVVRDVSFSVRAGEILGIAGLV 287
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 310 GCGKSTTMKMLTGLLPASEGTCALFGQPVDASD--MATRRRVGYMS---QAFSLYAELSVRQNLVL-----HARLFHLPA 379
Cdd:COG1129 288 GAGRTELARALFGADPADSGEIRLDGKPVRIRSprDAIRAGIAYVPedrKGEGLVLDLSIRENITLasldrLSRGGLLDR 367
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 380 DGIPARVGEMLRRFDLeKVADElpnDLPL-----GIRQRLSLAVAVIHKPEILILDEPTSGVDPVARDGFWELMVELSRR 454
Cdd:COG1129 368 RRERALAEEYIKRLRI-KTPSP---EQPVgnlsgGNQQKVVLAKWLATDPKVLILDEPTRGIDVGAKAEIYRLIRELAAE 443
|
490 500 510
....*....|....*....|....*....|
gi 15600424 455 DGVTIFISTHfMNEAQR-CDRISLMHAGKV 483
Cdd:COG1129 444 GKAVIVISSE-LPELLGlSDRILVMREGRI 472
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
270-492 |
1.28e-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: 192.12 E-value: 1.28e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 270 APRIAIEAEGLTCRFGDFVAVDHVSFRIERGEIFGFLGSNGCGKSTTMKMLTGLLPASEGTCALFGQPVDASD----MAT 345
Cdd:COG1127 1 MSEPMIEVRNLTKSFGDRVVLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEILVDGQDITGLSekelYEL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 346 RRRVGYMSQAFSLYAELSVRQNLVLHAR-LFHLPADGIPARVGEMLRRFDLEKVADELPNDLPLGIRQRLSLAVAVIHKP 424
Cdd:COG1127 81 RRRIGMLFQGGALFDSLTVFENVAFPLReHTDLSEAEIRELVLEKLELVGLPGAADKMPSELSGGMRKRVALARALALDP 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15600424 425 EILILDEPTSGVDPVARDGFWELMVELSRRDGVTIFISTHFMNEAQR-CDRISLMHAGKVLASDTPDEL 492
Cdd:COG1127 161 EILLYDEPTAGLDPITSAVIDELIRELRDELGLTSVVVTHDLDSAFAiADRVAVLADGKIIAEGTPEEL 229
|
|
| drrA |
TIGR01188 |
daunorubicin resistance ABC transporter ATP-binding subunit; This model describes daunorubicin ... |
17-248 |
4.65e-55 |
|
daunorubicin resistance ABC transporter ATP-binding subunit; This model describes daunorubicin resistance ABC transporter, ATP binding subunit in bacteria and archaea. This model is restricted in its scope to preferentially recognize the ATP binding subunit associated with effux of the drug, daunorubicin. This transport system belong to the larger ATP-Binding Cassette (ABC) transporter superfamily. The characteristic feature of these transporter is the obligatory coupling of ATP hydrolysis to substrate translocation. The minimal configuration of bacterial ABC transport system: an ATPase or ATP binding subunit; An integral membrane protein; a hydrophilic polypetpide, which likely functions as substrate binding protein. In eukaryotes proteins of similar function include p-gyco proteins, multidrug resistance protein etc. [Transport and binding proteins, Other]
Pssm-ID: 130256 [Multi-domain] Cd Length: 302 Bit Score: 192.99 E-value: 4.65e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 17 RYGETRAVDDVSLEIPANRMVGLIGPDGVGKSSLLALLAGARKMQDGEIRVLDGDMRdrRHRRAVCPRIAYMPQGlgKNL 96
Cdd:TIGR01188 2 VYGDFKAVDGVNFKVREGEVFGFLGPNGAGKTTTIRMLTTLLRPTSGTARVAGYDVV--REPRKVRRSIGIVPQY--ASV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 97 YPTLSVFENVDFFGRLFGHDKAERERRIADLLQSTGLAPFAERPAGKLSGGMKQKLGLCCALIHDPDLLILDEPTTGVDP 176
Cdd:TIGR01188 78 DEDLTGRENLEMMGRLYGLPKDEAEERAEELLELFELGEAADRPVGTYSGGMRRRLDIAASLIHQPDVLFLDEPTTGLDP 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15600424 177 LSRNQFWELIGRIRagREGMSVLVATAYMEEAERF-DWLVAMDDGKVLATGTPQELRERTGTQSLESAFIALL 248
Cdd:TIGR01188 158 RTRRAIWDYIRALK--EEGVTILLTTHYMEEADKLcDRIAIIDHGRIIAEGTPEELKRRLGKDTLESRPRDIQ 228
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
275-496 |
4.04e-54 |
|
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: 187.54 E-value: 4.04e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 275 IEAEGLTCRF-GDFVAVDHVSFRIERGEIFGFLGSNGCGKSTTMKMLTGLLPASEGTCALFGQPVDASDMAT-RRRVGYM 352
Cdd:COG1122 1 IELENLSFSYpGGTPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVDGKDITKKNLRElRRKVGLV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 353 -----SQAFslyaELSVRQNLVLHARLFHLPADGIPARVGEMLRRFDLEKVADELPNDLPLGIRQRLSLAVAVIHKPEIL 427
Cdd:COG1122 81 fqnpdDQLF----APTVEEDVAFGPENLGLPREEIRERVEEALELVGLEHLADRPPHELSGGQKQRVAIAGVLAMEPEVL 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 428 ILDEPTSGVDPVARDGFWELMVELsRRDGVTIFISTHFMNEAQR-CDRISLMHAGKVLASDTPDELVRQR 496
Cdd:COG1122 157 VLDEPTAGLDPRGRRELLELLKRL-NKEGKTVIIVTHDLDLVAElADRVIVLDDGRIVADGTPREVFSDY 225
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
10-241 |
6.33e-54 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 189.55 E-value: 6.33e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 10 SLRGVSLRYGETRAVDDVSLEIPANRMVGLIGPDGVGKSSLLALLAGARKMQDGEIRVlDGDMRDRRHRRavcpRIAYMP 89
Cdd:COG4152 3 ELKGLTKRFGDKTAVDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDSGEVLW-DGEPLDPEDRR----RIGYLP 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 90 QGLGknLYPTLSVFENVDFFGRLFGHDKAERERRIADLLQSTGLAPFAERPAGKLSGGMKQKLGLCCALIHDPDLLILDE 169
Cdd:COG4152 78 EERG--LYPKMKVGEQLVYLARLKGLSKAEAKRRADEWLERLGLGDRANKKVEELSKGNQQKVQLIAALLHDPELLILDE 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15600424 170 PTTGVDPLSRNQFWELIGRIRAgrEGMSVLVATAYMEEAERF-DWLVAMDDGKVLATGTPQELRERTGTQSLE 241
Cdd:COG4152 156 PFSGLDPVNVELLKDVIRELAA--KGTTVIFSSHQMELVEELcDRIVIINKGRKVLSGSVDEIRRQFGRNTLR 226
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
17-232 |
1.58e-53 |
|
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: 185.65 E-value: 1.58e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 17 RYGETRAVDDVSLEIPANRMVGLIGPDGVGKSSLLALLAGARKMQDGEIRVLDGDMRdrRHRRAVCPRIAYMPQGLgkNL 96
Cdd:cd03265 9 KYGDFEAVRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATVAGHDVV--REPREVRRRIGIVFQDL--SV 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 97 YPTLSVFENVDFFGRLFGHDKAERERRIADLLQSTGLAPFAERPAGKLSGGMKQKLGLCCALIHDPDLLILDEPTTGVDP 176
Cdd:cd03265 85 DDELTGWENLYIHARLYGVPGAERRERIDELLDFVGLLEAADRLVKTYSGGMRRRLEIARSLVHRPEVLFLDEPTIGLDP 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 15600424 177 LSRNQFWELIGRIRAgREGMSVLVATAYMEEAERF-DWLVAMDDGKVLATGTPQELR 232
Cdd:cd03265 165 QTRAHVWEYIEKLKE-EFGMTILLTTHYMEEAEQLcDRVAIIDHGRIIAEGTPEELK 220
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
10-231 |
2.49e-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: 185.61 E-value: 2.49e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 10 SLRGVSLRY-GETRAVDDVSLEIPANRMVGLIGPDGVGKSSLLALLAGARKMQDGEIRVlDGDMRDRRHRRAVCPRIAYM 88
Cdd:COG1122 2 ELENLSFSYpGGTPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLV-DGKDITKKNLRELRRKVGLV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 89 PQglgknlYP-----TLSVFENVDFFGRLFGHDKAERERRIADLLQSTGLAPFAERPAGKLSGGMKQKLGLCCALIHDPD 163
Cdd:COG1122 81 FQ------NPddqlfAPTVEEDVAFGPENLGLPREEIRERVEEALELVGLEHLADRPPHELSGGQKQRVAIAGVLAMEPE 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15600424 164 LLILDEPTTGVDPLSRNQFWELIGRIRagREGMSVLVATAYMEEAER-FDWLVAMDDGKVLATGTPQEL 231
Cdd:COG1122 155 VLVLDEPTAGLDPRGRRELLELLKRLN--KEGKTVIIVTHDLDLVAElADRVIVLDDGRIVADGTPREV 221
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
265-502 |
3.56e-53 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 188.89 E-value: 3.56e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 265 PQSEGAPRIAIEAEGLTCRFGDFVAVDHVSFRIERGEIFGFLGSNGCGKSTTMKMLTGLLPASEGTCALFGQPVDASDMA 344
Cdd:PRK13536 32 SIPGSMSTVAIDLAGVSKSYGDKAVVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKITVLGVPVPARARL 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 345 TRRRVGYMSQAFSLYAELSVRQNLVLHARLFHLPADGIPARVGEMLRRFDLEKVADELPNDLPLGIRQRLSLAVAVIHKP 424
Cdd:PRK13536 112 ARARIGVVPQFDNLDLEFTVRENLLVFGRYFGMSTREIEAVIPSLLEFARLESKADARVSDLSGGMKRRLTLARALINDP 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 425 EILILDEPTSGVDPVARDGFWELMVELSRRdGVTIFISTHFMNEAQR-CDRISLMHAGKVLASDTPDELVRQR-GLPTLE 502
Cdd:PRK13536 192 QLLILDEPTTGLDPHARHLIWERLRSLLAR-GKTILLTTHFMEEAERlCDRLCVLEAGRKIAEGRPHALIDEHiGCQVIE 270
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
271-491 |
1.21e-52 |
|
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid transport and metabolism];
Pssm-ID: 440180 [Multi-domain] Cd Length: 257 Bit Score: 184.47 E-value: 1.21e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 271 PRIAIEAEGLTCRFGDFVAVDHVSFRIERGEIFGFLGSNGCGKSTTMKMLTGLLPASEGTCALFGQPVdaSDMATRRRVG 350
Cdd:COG0411 1 SDPLLEVRGLTKRFGGLVAVDDVSLEVERGEIVGLIGPNGAGKTTLFNLITGFYRPTSGRILFDGRDI--TGLPPHRIAR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 351 Y-MSQAF---SLYAELSVRQNLVL--HAR--------LFHLPA-----DGIPARVGEMLRRFDLEKVADELPNDLPLGIR 411
Cdd:COG0411 79 LgIARTFqnpRLFPELTVLENVLVaaHARlgrgllaaLLRLPRarreeREARERAEELLERVGLADRADEPAGNLSYGQQ 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 412 QRLSLAVAVIHKPEILILDEPTSGVDPVARDGFWELMVELSRRDGVTIFISTHFMNEAQR-CDRISLMHAGKVLASDTPD 490
Cdd:COG0411 159 RRLEIARALATEPKLLLLDEPAAGLNPEETEELAELIRRLRDERGITILLIEHDMDLVMGlADRIVVLDFGRVIAEGTPA 238
|
.
gi 15600424 491 E 491
Cdd:COG0411 239 E 239
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
10-226 |
5.80e-52 |
|
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: 180.85 E-value: 5.80e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 10 SLRGVSLRYGETRAVDDVSLEIPaNRMVGLIGPDGVGKSSLLALLAGARKMQDGEIRVLDGDmrDRRHRRAVCPRIAYMP 89
Cdd:cd03264 2 QLENLTKRYGKKRALDGVSLTLG-PGMYGLLGPNGAGKTTLMRILATLTPPSSGTIRIDGQD--VLKQPQKLRRRIGYLP 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 90 QGLGknLYPTLSVFENVDFFGRLFGHDKAERERRIADLLQSTGLAPFAERPAGKLSGGMKQKLGLCCALIHDPDLLILDE 169
Cdd:cd03264 79 QEFG--VYPNFTVREFLDYIAWLKGIPSKEVKARVDEVLELVNLGDRAKKKIGSLSGGMRRRVGIAQALVGDPSILIVDE 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 15600424 170 PTTGVDPLSRNQFWELIGRIRAGRegmSVLVATAYMEEAERF-DWLVAMDDGKVLATG 226
Cdd:cd03264 157 PTAGLDPEERIRFRNLLSELGEDR---IVILSTHIVEDVESLcNQVAVLNKGKLVFEG 211
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
275-486 |
6.51e-52 |
|
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a bacterial ABC-type Na+ transport system called NatAB, which catalyzes ATP-dependent electrogenic Na+ extrusion without mechanically coupled proton or K+ uptake. NatB possess six putative membrane spanning regions at its C-terminus. In B. subtilis, NatAB is inducible by agents such as ethanol and protonophores, which lower the proton-motive force across the membrane. The closest sequence similarity to NatA is exhibited by DrrA of the two-component daunorubicin- and doxorubicin-efflux system. Hence, the functional NatAB is presumably assembled with two copies of a single ATP-binding protein and a single integral membrane protein.
Pssm-ID: 213233 [Multi-domain] Cd Length: 218 Bit Score: 181.03 E-value: 6.51e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 275 IEAEGLTCRFGD----FVAVDHVSFRIERGEIFGFLGSNGCGKSTTMKMLTGLLPASEGTCALFGQPVDASDMATRRRVG 350
Cdd:cd03266 2 ITADALTKRFRDvkktVQAVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDGFDVVKEPAEARRRLG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 351 YMSQAFSLYAELSVRQNLVLHARLFHLPADGIPARVGEMLRRFDLEKVADELPNDLPLGIRQRLSLAVAVIHKPEILILD 430
Cdd:cd03266 82 FVSDSTGLYDRLTARENLEYFAGLYGLKGDELTARLEELADRLGMEELLDRRVGGFSTGMRQKVAIARALVHDPPVLLLD 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 15600424 431 EPTSGVDPVARDGFWELMVELsRRDGVTIFISTHFMNEAQR-CDRISLMHAGKVLAS 486
Cdd:cd03266 162 EPTTGLDVMATRALREFIRQL-RALGKCILFSTHIMQEVERlCDRVVVLHRGRVVYE 217
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
275-486 |
9.29e-52 |
|
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily represents ABC transporters involved in peptide antibiotic resistance. Bacitracin is a dodecapeptide antibiotic produced by B. licheniformis and B. subtilis. The synthesis of bacitracin is non-ribosomally catalyzed by a multi-enzyme complex BcrABC. Bacitracin has potent antibiotic activity against gram-positive bacteria. The inhibition of peptidoglycan biosynthesis is the best characterized bacterial effect of bacitracin. The bacitracin resistance of B. licheniformis is mediated by the ABC transporter Bcr which is composed of two identical BcrA ATP-binding subunits and one each of the integral membrane proteins, BcrB and BcrC. B. subtilis cells carrying bcr genes on high-copy number plasmids develop collateral detergent sensitivity, a similar phenomenon in human cells with overexpressed multi-drug resistance P-glycoprotein.
Pssm-ID: 213235 [Multi-domain] Cd Length: 208 Bit Score: 180.11 E-value: 9.29e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 275 IEAEGLTCRFGDFVAVDHVSFRIERGEIFGFLGSNGCGKSTTMKMLTGLLPASEGTCALFGQPVDaSDMATRRRVGYMSQ 354
Cdd:cd03268 1 LKTNDLTKTYGKKRVLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEITFDGKSYQ-KNIEALRRIGALIE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 355 AFSLYAELSVRQNLVLHARLFhlpadGIP-ARVGEMLRRFDLEKVADELPNDLPLGIRQRLSLAVAVIHKPEILILDEPT 433
Cdd:cd03268 80 APGFYPNLTARENLRLLARLL-----GIRkKRIDEVLDVVGLKDSAKKKVKGFSLGMKQRLGIALALLGNPDLLILDEPT 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 15600424 434 SGVDPVARDGFWELMVELsRRDGVTIFISTHFMNEAQR-CDRISLMHAGKVLAS 486
Cdd:cd03268 155 NGLDPDGIKELRELILSL-RDQGITVLISSHLLSEIQKvADRIGIINKGKLIEE 207
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
274-493 |
1.55e-50 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 180.39 E-value: 1.55e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 274 AIEAEGLTCRFGDFVAVDHVSFRIERGEIFGFLGSNGCGKSTTMKMLTGLLPASEGTCALFGQPVDASDMATRRRVGYMS 353
Cdd:PRK13537 7 PIDFRNVEKRYGDKLVVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCGEPVPSRARHARQRVGVVP 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 354 QAFSLYAELSVRQNLVLHARLFHLPADGIPARVGEMLRRFDLEKVADELPNDLPLGIRQRLSLAVAVIHKPEILILDEPT 433
Cdd:PRK13537 87 QFDNLDPDFTVRENLLVFGRYFGLSAAAARALVPPLLEFAKLENKADAKVGELSGGMKRRLTLARALVNDPDVLVLDEPT 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15600424 434 SGVDPVARDGFWELMVELSRRdGVTIFISTHFMNEAQR-CDRISLMHAGKVLASDTPDELV 493
Cdd:PRK13537 167 TGLDPQARHLMWERLRSLLAR-GKTILLTTHFMEEAERlCDRLCVIEEGRKIAEGAPHALI 226
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
275-486 |
7.75e-50 |
|
ABC-type multidrug transport system, ATPase component; The biological function of this family is not well characterized, but display ABC domains similar to members of ABCA subfamily. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213231 [Multi-domain] Cd Length: 211 Bit Score: 175.07 E-value: 7.75e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 275 IEAEGLTCRFGDFVAVDHVSFRIERGeIFGFLGSNGCGKSTTMKMLTGLLPASEGTCALFGQPVDASDMATRRRVGYMSQ 354
Cdd:cd03264 1 LQLENLTKRYGKKRALDGVSLTLGPG-MYGLLGPNGAGKTTLMRILATLTPPSSGTIRIDGQDVLKQPQKLRRRIGYLPQ 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 355 AFSLYAELSVRQNLVLHARLFHLPADGIPARVGEMLRRFDLEKVADELPNDLPLGIRQRLSLAVAVIHKPEILILDEPTS 434
Cdd:cd03264 80 EFGVYPNFTVREFLDYIAWLKGIPSKEVKARVDEVLELVNLGDRAKKKIGSLSGGMRRRVGIAQALVGDPSILIVDEPTA 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 15600424 435 GVDPVARDGFWELMVELSrrDGVTIFISTHFMNE-AQRCDRISLMHAGKVLAS 486
Cdd:cd03264 160 GLDPEERIRFRNLLSELG--EDRIVILSTHIVEDvESLCNQVAVLNKGKLVFE 210
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
10-483 |
1.71e-49 |
|
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: 183.73 E-value: 1.71e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 10 SLRGVSLRYG----ETRAVDDVSLEIPANRMVGLIGPDGVGKS----SLLALLAGARKMQDGEIRvLDG-DMR--DRRHR 78
Cdd:COG4172 8 SVEDLSVAFGqgggTVEAVKGVSFDIAAGETLALVGESGSGKSvtalSILRLLPDPAAHPSGSIL-FDGqDLLglSEREL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 79 RAVC-PRIAYMPQ----------GLGKNLYPTLSVFEnvdffgrlfGHDKAERERRIADLLQSTGLaPFAERPAGK---- 143
Cdd:COG4172 87 RRIRgNRIAMIFQepmtslnplhTIGKQIAEVLRLHR---------GLSGAAARARALELLERVGI-PDPERRLDAyphq 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 144 LSGGMKQKLGLCCALIHDPDLLILDEPTTGVDPLSRNQFWELIGRIRAgREGMSVLVATAYMEEAERF-DWLVAMDDGKV 222
Cdd:COG4172 157 LSGGQRQRVMIAMALANEPDLLIADEPTTALDVTVQAQILDLLKDLQR-ELGMALLLITHDLGVVRRFaDRVAVMRQGEI 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 223 LATGTPQELRERTG---TQSLesafIALLPEskraghhrlvIPPRPQSEGAPRIaIEAEGLTCRF-----------GDFV 288
Cdd:COG4172 236 VEQGPTAELFAAPQhpyTRKL----LAAEPR----------GDPRPVPPDAPPL-LEARDLKVWFpikrglfrrtvGHVK 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 289 AVDHVSFRIERGEIFGFLGSNGCGKSTTMKMLTGLLPaSEGTCALFGQPVDA---SDM-ATRRRVgymsQA-F-----SL 358
Cdd:COG4172 301 AVDGVSLTLRRGETLGLVGESGSGKSTLGLALLRLIP-SEGEIRFDGQDLDGlsrRALrPLRRRM----QVvFqdpfgSL 375
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 359 YAELSVRQ----NLVLHARlfHLPADGIPARVGEMLRRFDL-EKVADELPNDLPLGIRQRLSLAVAVIHKPEILILDEPT 433
Cdd:COG4172 376 SPRMTVGQiiaeGLRVHGP--GLSAAERRARVAEALEEVGLdPAARHRYPHEFSGGQRQRIAIARALILEPKLLVLDEPT 453
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*..
gi 15600424 434 SGVDPVARDGFWELMVELSRRDGVT-IFIStH------FMneaqrCDRISLMHAGKV 483
Cdd:COG4172 454 SALDVSVQAQILDLLRDLQREHGLAyLFIS-HdlavvrAL-----AHRVMVMKDGKV 504
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
274-492 |
2.59e-49 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 178.37 E-value: 2.59e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 274 AIEAEGLTCRFGDFVAVDHVSFRIERGEIFGFLGSNGCGKSTTMKMLTGLLPASEGTCALFGQPVdaSDMAT-RRRVGYM 352
Cdd:COG3842 5 ALELENVSKRYGDVTALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRILLDGRDV--TGLPPeKRNVGMV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 353 SQAFSLYAELSVRQNLVLHARLFHLPADGIPARVGEMLRRFDLEKVADELPNDLPLGIRQRLSLAVAVIHKPEILILDEP 432
Cdd:COG3842 83 FQDYALFPHLTVAENVAFGLRMRGVPKAEIRARVAELLELVGLEGLADRYPHQLSGGQQQRVALARALAPEPRVLLLDEP 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15600424 433 TSGVDPVARDGFWELMVELSRRDGVTIFISTHFMNEAQR-CDRISLMHAGKVLASDTPDEL 492
Cdd:COG3842 163 LSALDAKLREEMREELRRLQRELGITFIYVTHDQEEALAlADRIAVMNDGRIEQVGTPEEI 223
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
10-231 |
3.85e-49 |
|
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: 174.46 E-value: 3.85e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 10 SLRGVSLRYGETRAVDDVSLEIPANRMVGLIGPDGVGKSSLLALLAGARKMQDGEIRVLDGDMRDRRhRRAVCPRIAYMP 89
Cdd:COG1120 3 EAENLSVGYGGRPVLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDGRDLASLS-RRELARRIAYVP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 90 QGLgkNLYPTLSVFENVdFFGR-----LFGHDKAERERRIADLLQSTGLAPFAERPAGKLSGGMKQKLGLCCALIHDPDL 164
Cdd:COG1120 82 QEP--PAPFGLTVRELV-ALGRyphlgLFGRPSAEDREAVEEALERTGLEHLADRPVDELSGGERQRVLIARALAQEPPL 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 165 LILDEPTTGVDPlsRNQFwELIGRIR--AGREGMSVLVATAYMEEAERF-DWLVAMDDGKVLATGTPQEL 231
Cdd:COG1120 159 LLLDEPTSHLDL--AHQL-EVLELLRrlARERGRTVVMVLHDLNLAARYaDRLVLLKDGRIVAQGPPEEV 225
|
|
| YadH |
COG0842 |
ABC-type multidrug transport system, permease component [Defense mechanisms]; |
722-916 |
7.27e-49 |
|
ABC-type multidrug transport system, permease component [Defense mechanisms];
Pssm-ID: 440604 [Multi-domain] Cd Length: 200 Bit Score: 171.92 E-value: 7.27e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 722 MVPAVIPLLLIMIPAMLTALGVVREKELGSITNLYVTPVTRLEFLVGKQLPYVAMGMINFLLMLVLAIVVFRVPLKG-SF 800
Cdd:COG0842 5 LVPGLLAMSLLFTALMLTALSIAREREQGTLERLLVTPVSRLEILLGKVLAYLLRGLLQALLVLLVALLFFGVPLRGlSL 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 801 LALTIGAFLYVVTSTGLGLFLSTFMRSQIAAVfGVAIATMIPAIQFSGLIHPVSSLEGAAAWIGKLYPTSHFLVVSRGAF 880
Cdd:COG0842 85 LLLLLVLLLFALAFSGLGLLISTLARSQEQAS-AISNLVILPLTFLSGAFFPIESLPGWLQAIAYLNPLTYFVEALRALF 163
|
170 180 190
....*....|....*....|....*....|....*.
gi 15600424 881 SKSLGLSDLWAYYLPLAASIVVLTLLSVACLKKQED 916
Cdd:COG0842 164 LGGAGLADVWPSLLVLLAFAVVLLALALRLFRRRLR 199
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
11-483 |
8.33e-49 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 181.42 E-value: 8.33e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 11 LRGVSLRYGETRAVDDVSLEIPANRMVGLIGPDGVGKSSLLALLAGARKMQDGEIrVLDGDMRdrrhrravcprIAYMPQ 90
Cdd:COG0488 1 LENLSKSFGGRPLLDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEV-SIPKGLR-----------IGYLPQ 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 91 GLgkNLYPTLSVFENV-DFFGRL---------------FGHDKAER----------------ERRIADLLQSTGLAPF-A 137
Cdd:COG0488 69 EP--PLDDDLTVLDTVlDGDAELraleaeleeleaklaEPDEDLERlaelqeefealggweaEARAEEILSGLGFPEEdL 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 138 ERPAGKLSGGMKQKLGLCCALIHDPDLLILDEPTTGVDPLSRNqfWeLIGRIRaGREGmSVLVAT--------------- 202
Cdd:COG0488 147 DRPVSELSGGWRRRVALARALLSEPDLLLLDEPTNHLDLESIE--W-LEEFLK-NYPG-TVLVVShdryfldrvatrile 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 203 --------------AYMEE-AERFDWLVAMDD--GKVLAtgtpQEL--------RERTGTQ--SLESAFIALLPESK--R 253
Cdd:COG0488 222 ldrgkltlypgnysAYLEQrAERLEQEAAAYAkqQKKIA----KEEefirrfraKARKAKQaqSRIKALEKLEREEPprR 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 254 AGHHRLVIPPRPQSegaPRIAIEAEGLTCRFGDFVAVDHVSFRIERGEIFGFLGSNGCGKSTTMKMLTGLLPASEGTCAL 333
Cdd:COG0488 298 DKTVEIRFPPPERL---GKKVLELEGLSKSYGDKTLLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPDSGTVKL 374
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 334 fGQPVdasdmatrrRVGYMSQAF-SLYAELSVRQNLVLHARlfhlpaDGIPARVGEMLRRF-----DLEKVAdelpNDLP 407
Cdd:COG0488 375 -GETV---------KIGYFDQHQeELDPDKTVLDELRDGAP------GGTEQEVRGYLGRFlfsgdDAFKPV----GVLS 434
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15600424 408 LGIRQRLSLAVAVIHKPEILILDEPTSGVDPVARdgfwELMVE-LSRRDGVTIFIS--THFMNEAqrCDRISLMHAGKV 483
Cdd:COG0488 435 GGEKARLALAKLLLSPPNVLLLDEPTNHLDIETL----EALEEaLDDFPGTVLLVShdRYFLDRV--ATRILEFEDGGV 507
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
275-494 |
5.32e-48 |
|
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: 170.70 E-value: 5.32e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 275 IEAEGLTCRFGDFVAVDHVSFRIERGEIFGFLGSNGCGKSTTMKMLTGLLPASEGTCALFGQPVDASDMATRRRVGyMSQ 354
Cdd:cd03219 1 LEVRGLTKRFGGLVALDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFDGEDITGLPPHEIARLG-IGR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 355 AF---SLYAELSVRQNLVL--HARLFHLPADG--------IPARVGEMLRRFDLEKVADELPNDLPLGIRQRLSLAVAVI 421
Cdd:cd03219 80 TFqipRLFPELTVLENVMVaaQARTGSGLLLArarreereARERAEELLERVGLADLADRPAGELSYGQQRRLEIARALA 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15600424 422 HKPEILILDEPTSGVDPVARDGFWELMVELsRRDGVTIFISTHFMNEAQR-CDRISLMHAGKVLASDTPDELVR 494
Cdd:cd03219 160 TDPKLLLLDEPAAGLNPEETEELAELIREL-RERGITVLLVEHDMDVVMSlADRVTVLDQGRVIAEGTPDEVRN 232
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
275-494 |
5.44e-48 |
|
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: 170.76 E-value: 5.44e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 275 IEAEGLTCRFGDFVAVDHVSFRIERGEIFGFLGSNGCGKSTTMKMLTGLLPASEGTCALFGQPVD----ASDMATRRRVG 350
Cdd:cd03261 1 IELRGLTKSFGGRTVLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGEDISglseAELYRLRRRMG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 351 YMSQAFSLYAELSVRQNLVLHARLFH-LPADGIPARVGEMLRRFDLEKVADELPNDLPLGIRQRLSLAVAVIHKPEILIL 429
Cdd:cd03261 81 MLFQSGALFDSLTVFENVAFPLREHTrLSEEEIREIVLEKLEAVGLRGAEDLYPAELSGGMKKRVALARALALDPELLLY 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15600424 430 DEPTSGVDPVARDGFWELMVELSRRDGVTIFISTHFMNEAQR-CDRISLMHAGKVLASDTPDELVR 494
Cdd:cd03261 161 DEPTAGLDPIASGVIDDLIRSLKKELGLTSIMVTHDLDTAFAiADRIAVLYDGKIVAEGTPEELRA 226
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
10-221 |
7.94e-48 |
|
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: 169.18 E-value: 7.94e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 10 SLRGVSLRY--GETRAVDDVSLEIPANRMVGLIGPDGVGKSSLLALLAGARKMQDGEIRVLDGDMRDRRhRRAVCPRIAY 87
Cdd:cd03225 1 ELKNLSFSYpdGARPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDLTKLS-LKELRRKVGL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 88 MPQglgknlYP-----TLSVFENVDFFGRLFGHDKAERERRIADLLQSTGLAPFAERPAGKLSGGMKQKLGLCCALIHDP 162
Cdd:cd03225 80 VFQ------NPddqffGPTVEEEVAFGLENLGLPEEEIEERVEEALELVGLEGLRDRSPFTLSGGQKQRVAIAGVLAMDP 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 163 DLLILDEPTTGVDPLSRNQFWELIGRIRagREGMSVLVATAYMEEAERF-DWLVAMDDGK 221
Cdd:cd03225 154 DILLLDEPTAGLDPAGRRELLELLKKLK--AEGKTIIIVTHDLDLLLELaDRVIVLEDGK 211
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
275-485 |
9.15e-48 |
|
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: 169.24 E-value: 9.15e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 275 IEAEGLTCRFGDFVAVDHVSFRIERGEIFGFLGSNGCGKSTTMKMLTGLLPASEGTCALFGQPVdASDMATRRRVGYMSQ 354
Cdd:cd03259 1 LELKGLSKTYGSVRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDGRDV-TGVPPERRNIGMVFQ 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 355 AFSLYAELSVRQNLVLHARLFHLPADGIPARVGEMLRRFDLEKVADELPNDLPLGIRQRLSLAVAVIHKPEILILDEPTS 434
Cdd:cd03259 80 DYALFPHLTVAENIAFGLKLRGVPKAEIRARVRELLELVGLEGLLNRYPHELSGGQQQRVALARALAREPSLLLLDEPLS 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 15600424 435 GVDPVARDGFWELMVELSRRDGVTIFISTHFMNEAQR-CDRISLMHAGKVLA 485
Cdd:cd03259 160 ALDAKLREELREELKELQRELGITTIYVTHDQEEALAlADRIAVMNEGRIVQ 211
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
274-505 |
1.02e-47 |
|
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: 170.61 E-value: 1.02e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 274 AIEAEGLTCRFGDFVAVDHVSFRIERGEIFGFLGSNGCGKSTTMKMLTGLLPASEGTCALFGQPVdaSDMATR---RRVG 350
Cdd:COG1120 1 MLEAENLSVGYGGRPVLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDGRDL--ASLSRRelaRRIA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 351 YMSQAFSLYAELSVRQnLVLHARLFHLPADGIP-----ARVGEMLRRFDLEKVADELPNDLPLGIRQRLSLAVAVIHKPE 425
Cdd:COG1120 79 YVPQEPPAPFGLTVRE-LVALGRYPHLGLFGRPsaedrEAVEEALERTGLEHLADRPVDELSGGERQRVLIARALAQEPP 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 426 ILILDEPTSGVDPVARDGFWELMVELSRRDGVTIFISTHFMNEAQR-CDRISLMHAGKVLASDTPDELVRQrglPTLEAT 504
Cdd:COG1120 158 LLLLDEPTSHLDLAHQLEVLELLRRLARERGRTVVMVLHDLNLAARyADRLVLLKDGRIVAQGPPEEVLTP---ELLEEV 234
|
.
gi 15600424 505 F 505
Cdd:COG1120 235 Y 235
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
10-230 |
2.03e-47 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 169.50 E-value: 2.03e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 10 SLRGVSLRYGETRAVDDVSLEIPANRMVGLIGPDGVGKSSLLALLAGARKMQDGEIRVLDGDMRDRRHRravcprIAYMP 89
Cdd:COG1121 8 ELENLTVSYGGRPVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLFGKPPRRARRR------IGYVP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 90 QGLGKNLYPTLSVFENV----DFFGRLFGHDKAERERRIADLLQSTGLAPFAERPAGKLSGGMKQKLGLCCALIHDPDLL 165
Cdd:COG1121 82 QRAEVDWDFPITVRDVVlmgrYGRRGLFRRPSRADREAVDEALERVGLEDLADRPIGELSGGQQQRVLLARALAQDPDLL 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15600424 166 ILDEPTTGVDPLSRNQFWELIGRIRagREGMSVLVATAYMEEAER-FDWLVAMDDGkVLATGTPQE 230
Cdd:COG1121 162 LLDEPFAGVDAATEEALYELLRELR--REGKTILVVTHDLGAVREyFDRVLLLNRG-LVAHGPPEE 224
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
275-483 |
4.06e-47 |
|
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: 167.67 E-value: 4.06e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 275 IEAEGLTCRFGD----FVAVDHVSFRIERGEIFGFLGSNGCGKSTTMKMLTGLLPASEGTCALFGQPVDASDMAT----- 345
Cdd:cd03255 1 IELKNLSKTYGGggekVQALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRVDGTDISKLSEKElaafr 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 346 RRRVGYMSQAFSLYAELSVRQNLVLHARLFHLPADGIPARVGEMLRRFDLEKVADELPNDLPLGIRQRLSLAVAVIHKPE 425
Cdd:cd03255 81 RRHIGFVFQSFNLLPDLTALENVELPLLLAGVPKKERRERAEELLERVGLGDRLNHYPSELSGGQQQRVAIARALANDPK 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 15600424 426 ILILDEPTSGVDPVARDGFWELMVELSRRDGVTIFISTHFMNEAQRCDRISLMHAGKV 483
Cdd:cd03255 161 IILADEPTGNLDSETGKEVMELLRELNKEAGTTIVVVTHDPELAEYADRIIELRDGKI 218
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
276-482 |
5.39e-47 |
|
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: 166.87 E-value: 5.39e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 276 EAEGLTCRFGDF--VAVDHVSFRIERGEIFGFLGSNGCGKSTTMKMLTGLLPASEGTCALFGQPVDASDMAT-RRRVGYM 352
Cdd:cd03225 1 ELKNLSFSYPDGarPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDLTKLSLKElRRKVGLV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 353 -----SQAFslyaELSVRQNLVLHARLFHLPADGIPARVGEMLRRFDLEKVADELPNDLPLGIRQRLSLAVAVIHKPEIL 427
Cdd:cd03225 81 fqnpdDQFF----GPTVEEEVAFGLENLGLPEEEIEERVEEALELVGLEGLRDRSPFTLSGGQKQRVAIAGVLAMDPDIL 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 15600424 428 ILDEPTSGVDPVARDGFWELMVELsRRDGVTIFISTHFMNEAQR-CDRISLMHAGK 482
Cdd:cd03225 157 LLDEPTAGLDPAGRRELLELLKKL-KAEGKTIIIVTHDLDLLLElADRVIVLEDGK 211
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
10-226 |
1.33e-46 |
|
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: 165.92 E-value: 1.33e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 10 SLRGVSLRYGETRAVDDVSLEIPANRMVGLIGPDGVGKSSLLALLAGARKMQDGEIRVlDGDMRDRRHRRavcpRIAYMP 89
Cdd:cd03269 2 EVENVTKRFGRVTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLF-DGKPLDIAARN----RIGYLP 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 90 QGLGknLYPTLSVFENVDFFGRLFGHDKAERERRIADLLQSTGLAPFAERPAGKLSGGMKQKLGLCCALIHDPDLLILDE 169
Cdd:cd03269 77 EERG--LYPKMKVIDQLVYLAQLKGLKKEEARRRIDEWLERLELSEYANKRVEELSKGNQQKVQFIAAVIHDPELLILDE 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 15600424 170 PTTGVDPLSRNQFWELIGRIRagREGMSVLVATAYMEEAERF-DWLVAMDDGKVLATG 226
Cdd:cd03269 155 PFSGLDPVNVELLKDVIRELA--RAGKTVILSTHQMELVEELcDRVLLLNKGRAVLYG 210
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
275-477 |
3.42e-46 |
|
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: 164.57 E-value: 3.42e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 275 IEAEGLTCRFGDFVAVDHVSFRIERGEIFGFLGSNGCGKSTTMKMLTGLLPASEGTCALFGQPVDASDMATRRRVGYMSQ 354
Cdd:COG4133 3 LEAENLSCRRGERLLFSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWNGEPIRDAREDYRRRLAYLGH 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 355 AFSLYAELSVRQNLVLHARLFHLPADGipARVGEMLRRFDLEKVADELPNDLPLGIRQRLSLAVAVIHKPEILILDEPTS 434
Cdd:COG4133 83 ADGLKPELTVRENLRFWAALYGLRADR--EAIDEALEAVGLAGLADLPVRQLSAGQKRRVALARLLLSPAPLWLLDEPFT 160
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 15600424 435 GVDPVARDGFWELMVELsRRDGVTIFISTHFMNEAQRCDRISL 477
Cdd:COG4133 161 ALDAAGVALLAELIAAH-LARGGAVLLTTHQPLELAAARVLDL 202
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
270-481 |
1.64e-45 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 164.49 E-value: 1.64e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 270 APRIAIEAEGLTCRF----GDFVAVDHVSFRIERGEIFGFLGSNGCGKSTTMKMLTGLLPASEGTCALFGQPVDAsdmaT 345
Cdd:COG1116 3 AAAPALELRGVSKRFptggGGVTALDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPTSGEVLVDGKPVTG----P 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 346 RRRVGYMSQAFSLYAELSVRQNLVLHARLFHLPADGIPARVGEMLRRFDLEKVADELPNDLPLGIRQRLSLAVAVIHKPE 425
Cdd:COG1116 79 GPDRGVVFQEPALLPWLTVLDNVALGLELRGVPKAERRERARELLELVGLAGFEDAYPHQLSGGMRQRVAIARALANDPE 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 15600424 426 ILILDEPTSGVDPVARDGFWELMVELSRRDGVTIFISTHFMNEAQR-CDRISLMHAG 481
Cdd:COG1116 159 VLLMDEPFGALDALTRERLQDELLRLWQETGKTVLFVTHDVDEAVFlADRVVVLSAR 215
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
11-495 |
5.69e-45 |
|
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in methanogenesis, methyl coenzyme M reductase, contains alpha, beta, and gamma chains. In older literature, the complex of alpha, beta, and gamma chains was termed component C, while this single chain protein was termed methyl coenzyme M reductase system component A2. [Energy metabolism, Methanogenesis]
Pssm-ID: 132313 [Multi-domain] Cd Length: 520 Bit Score: 170.37 E-value: 5.69e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 11 LRGVSLRYGETRAVDDVSLEIPANRMVGLIGPDGVGKSSLLALLAGARKMQDGEIRVL---------------------- 68
Cdd:TIGR03269 3 VKNLTKKFDGKEVLKNISFTIEEGEVLGILGRSGAGKSVLMHVLRGMDQYEPTSGRIIyhvalcekcgyverpskvgepc 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 69 ---DGDMR---------DRRHRRAVCPRIAYMPQGLGKnLYPTLSVFENVDFFGRLFGHDKAERERRIADLLQSTGLAPF 136
Cdd:TIGR03269 83 pvcGGTLEpeevdfwnlSDKLRRRIRKRIAIMLQRTFA-LYGDDTVLDNVLEALEEIGYEGKEAVGRAVDLIEMVQLSHR 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 137 AERPAGKLSGGMKQKLGLCCALIHDPDLLILDEPTTGVDPLSRNQFWELIgRIRAGREGMSVLVATAYMEEAERF-DWLV 215
Cdd:TIGR03269 162 ITHIARDLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNAL-EEAVKASGISMVLTSHWPEVIEDLsDKAI 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 216 AMDDGKVLATGTPQELRERtgtqslesaFIALLPESKRAghhrlvippRPQSEGAPriAIEAEGLTCRF-----GDFVAV 290
Cdd:TIGR03269 241 WLENGEIKEEGTPDEVVAV---------FMEGVSEVEKE---------CEVEVGEP--IIKVRNVSKRYisvdrGVVKAV 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 291 DHVSFRIERGEIFGFLGSNGCGKSTTMKMLTGLLPASEG-TCALFGQpvDASDMATR---------RRVGYMSQAFSLYA 360
Cdd:TIGR03269 301 DNVSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGeVNVRVGD--EWVDMTKPgpdgrgrakRYIGILHQEYDLYP 378
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 361 ELSVRQNLVlHARLFHLPADGIPARVGEMLRR--FDLEK---VADELPNDLPLGIRQRLSLAVAVIHKPEILILDEPTSG 435
Cdd:TIGR03269 379 HRTVLDNLT-EAIGLELPDELARMKAVITLKMvgFDEEKaeeILDKYPDELSEGERHRVALAQVLIKEPRIVILDEPTGT 457
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15600424 436 VDPVARDGFWELMVELSRRDGVTIFISTH---FMNEAqrCDRISLMHAGKVLASDTPDELVRQ 495
Cdd:TIGR03269 458 MDPITKVDVTHSILKAREEMEQTFIIVSHdmdFVLDV--CDRAALMRDGKIVKIGDPEEIVEE 518
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
275-494 |
7.62e-45 |
|
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: 162.08 E-value: 7.62e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 275 IEAEGLTCRFGD-FVAVDHVSFRIERGEIFGFLGSNGCGKSTTMKMLTGLLPASEGTCALFGQPVDASD-MATRRRVGYM 352
Cdd:cd03295 1 IEFENVTKRYGGgKKAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGEDIREQDpVELRRKIGYV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 353 SQAFSLYAELSVRQNLVLHARLFHLPADGIPARVGEMLRRFDLE--KVADELPNDLPLGIRQRLSLAVAVIHKPEILILD 430
Cdd:cd03295 81 IQQIGLFPHMTVEENIALVPKLLKWPKEKIRERADELLALVGLDpaEFADRYPHELSGGQQQRVGVARALAADPPLLLMD 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15600424 431 EPTSGVDPVARDGFWELMVELSRRDGVTIFISTHFMNEAQR-CDRISLMHAGKVLASDTPDELVR 494
Cdd:cd03295 161 EPFGALDPITRDQLQEEFKRLQQELGKTIVFVTHDIDEAFRlADRIAIMKNGEIVQVGTPDEILR 225
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
274-485 |
8.14e-45 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 161.36 E-value: 8.14e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 274 AIEAEGLTCRFGD----FVAVDHVSFRIERGEIFGFLGSNGCGKSTTMKMLTGLLPASEGTCALFGQPV---DASDMAT- 345
Cdd:COG1136 4 LLELRNLTKSYGTgegeVTALRGVSLSIEAGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVLIDGQDIsslSERELARl 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 346 -RRRVGYMSQAFSLYAELSVRQNLVLHARLFHLPADGIPARVGEMLRRFDLEKVADELPNDLPLGIRQRLSLAVAVIHKP 424
Cdd:COG1136 84 rRRHIGFVFQFFNLLPELTALENVALPLLLAGVSRKERRERARELLERVGLGDRLDHRPSQLSGGQQQRVAIARALVNRP 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15600424 425 EILILDEPTSGVDPVARDGFWELMVELSRRDGVTIFISTHFMNEAQRCDRISLMHAGKVLA 485
Cdd:COG1136 164 KLILADEPTGNLDSKTGEEVLELLRELNRELGTTIVMVTHDPELAARADRVIRLRDGRIVS 224
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
274-505 |
1.11e-44 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 161.41 E-value: 1.11e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 274 AIEAEGLTCRFGDFVAVDHVSFRIERGEIFGFLGSNGCGKSTTMKMLTGLLPASEGTCALFGQPVDASdmatRRRVGYMS 353
Cdd:COG1121 6 AIELENLTVSYGGRPVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLFGKPPRRA----RRRIGYVP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 354 QAFSLYAE--LSVRQnLVLHARLFHLPADGIP-----ARVGEMLRRFDLEKVADELPNDLPLGIRQRLSLAVAVIHKPEI 426
Cdd:COG1121 82 QRAEVDWDfpITVRD-VVLMGRYGRRGLFRRPsradrEAVDEALERVGLEDLADRPIGELSGGQQQRVLLARALAQDPDL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 427 LILDEPTSGVDPVARDGFWELMVELsRRDGVTIFISTHFMNEAQR-CDRISLMhAGKVLASDTPDELVRQrglPTLEATF 505
Cdd:COG1121 161 LLLDEPFAGVDAATEEALYELLREL-RREGKTILVVTHDLGAVREyFDRVLLL-NRGLVAHGPPEEVLTP---ENLSRAY 235
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
10-202 |
4.11e-44 |
|
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: 158.41 E-value: 4.11e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 10 SLRGVSLRYGETRAVDDVSLEIPANRMVGLIGPDGVGKSSLLALLAGARKMQDGEIRVLDGDMRDRRhrRAVCPRIAYMP 89
Cdd:COG4133 4 EAENLSCRRGERLLFSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWNGEPIRDAR--EDYRRRLAYLG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 90 QGLGknLYPTLSVFENVDFFGRLFGHDKAERerRIADLLQSTGLAPFAERPAGKLSGGMKQKLGLCCALIHDPDLLILDE 169
Cdd:COG4133 82 HADG--LKPELTVRENLRFWAALYGLRADRE--AIDEALEAVGLAGLADLPVRQLSAGQKRRVALARLLLSPAPLWLLDE 157
|
170 180 190
....*....|....*....|....*....|...
gi 15600424 170 PTTGVDPLSRNQFWELIgRIRAGREGMsVLVAT 202
Cdd:COG4133 158 PFTALDAAGVALLAELI-AAHLARGGA-VLLTT 188
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
10-234 |
4.30e-44 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 161.90 E-value: 4.30e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 10 SLRGVSLRYGETRAVDDVSLEIPANRMVGLIGPDGVGKSSLLALLAGARKMQDGEIRVLDGDMRDR-RHRRAvcpRIAYM 88
Cdd:PRK13537 9 DFRNVEKRYGDKLVVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCGEPVPSRaRHARQ---RVGVV 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 89 PQGlgKNLYPTLSVFENVDFFGRLFGHDKAERERRIADLLQSTGLAPFAERPAGKLSGGMKQKLGLCCALIHDPDLLILD 168
Cdd:PRK13537 86 PQF--DNLDPDFTVRENLLVFGRYFGLSAAAARALVPPLLEFAKLENKADAKVGELSGGMKRRLTLARALVNDPDVLVLD 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15600424 169 EPTTGVDPLSRNQFWELIGRIRAgrEGMSVLVATAYMEEAERF-DWLVAMDDGKVLATGTPQELRER 234
Cdd:PRK13537 164 EPTTGLDPQARHLMWERLRSLLA--RGKTILLTTHFMEEAERLcDRLCVIEEGRKIAEGAPHALIES 228
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
275-485 |
9.80e-44 |
|
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: 158.02 E-value: 9.80e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 275 IEAEGLTCRFGD----FVAVDHVSFRIERGEIFGFLGSNGCGKSTTMKMLTGLLPASEGTCALFGQPVDAsdmaTRRRVG 350
Cdd:cd03293 1 LEVRNVSKTYGGgggaVTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVDGEPVTG----PGPDRG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 351 YMSQAFSLYAELSVRQNLVLHARLFHLPADGIPARVGEMLRRFDLEKVADELPNDLPLGIRQRLSLAVAVIHKPEILILD 430
Cdd:cd03293 77 YVFQQDALLPWLTVLDNVALGLELQGVPKAEARERAEELLELVGLSGFENAYPHQLSGGMRQRVALARALAVDPDVLLLD 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 15600424 431 EPTSGVDPVARDGFWELMVELSRRDGVTIFISTHFMNEAQR-CDRISLMHA--GKVLA 485
Cdd:cd03293 157 EPFSALDALTREQLQEELLDIWRETGKTVLLVTHDIDEAVFlADRVVVLSArpGRIVA 214
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
10-233 |
2.74e-43 |
|
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: 157.45 E-value: 2.74e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 10 SLRGVSLRYGETRAVDDVSLEIPANRMVGLIGPDGVGKSSLLALLAGARKMQDGEIRVLDGDMR--DRRHRRAVCPRIAY 87
Cdd:COG1127 7 EVRNLTKSFGDRVVLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEILVDGQDITglSEKELYELRRRIGM 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 88 MPQGLGknLYPTLSVFENVDFFGRLFGH-DKAERERRIADLLQSTGLAPFAERPAGKLSGGMKQKLGLCCALIHDPDLLI 166
Cdd:COG1127 87 LFQGGA--LFDSLTVFENVAFPLREHTDlSEAEIRELVLEKLELVGLPGAADKMPSELSGGMRKRVALARALALDPEILL 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15600424 167 LDEPTTGVDPLSRNQFWELIGRIRAgREGMSVLVATAYMEEAERF-DWLVAMDDGKVLATGTPQELRE 233
Cdd:COG1127 165 YDEPTAGLDPITSAVIDELIRELRD-ELGLTSVVVTHDLDSAFAIaDRVAVLADGKIIAEGTPEELLA 231
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
274-494 |
3.65e-43 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 164.81 E-value: 3.65e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 274 AIEAEGLTCRFGDFVAVDHVSFRIERGEIFGFLGSNGCGKSTTMKMLTGLLPASEGTCALFGQPVDASD--MATRRRVGY 351
Cdd:COG3845 5 ALELRGITKRFGGVVANDDVSLTVRPGEIHALLGENGAGKSTLMKILYGLYQPDSGEILIDGKPVRIRSprDAIALGIGM 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 352 MSQAFSLYAELSVRQNLVL---HARLFHLPADGIPARVGEMLRRFDLEKVADELPNDLPLGIRQRLSLAVAVIHKPEILI 428
Cdd:COG3845 85 VHQHFMLVPNLTVAENIVLglePTKGGRLDRKAARARIRELSERYGLDVDPDAKVEDLSVGEQQRVEILKALYRGARILI 164
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15600424 429 LDEPTSGVDPVARDGFWELMVELsRRDGVTIFISTHFMNEAQR-CDRISLMHAGKV-----LASDTPDELVR 494
Cdd:COG3845 165 LDEPTAVLTPQEADELFEILRRL-AAEGKSIIFITHKLREVMAiADRVTVLRRGKVvgtvdTAETSEEELAE 235
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
10-232 |
5.17e-43 |
|
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: 157.12 E-value: 5.17e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 10 SLRGVSLRYGETRAVDDVSLEIPANRMVGLIGPDGVGKSSLLALLAGARKMQDGEIRVLDGDMRDRR-HRRAvcpRiaym 88
Cdd:COG0411 6 EVRGLTKRFGGLVAVDDVSLEVERGEIVGLIGPNGAGKTTLFNLITGFYRPTSGRILFDGRDITGLPpHRIA---R---- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 89 pQGLGK-----NLYPTLSVFENV-------------DFFGRLFGHDKAERE--RRIADLLQSTGLAPFAERPAGKLSGGM 148
Cdd:COG0411 79 -LGIARtfqnpRLFPELTVLENVlvaaharlgrgllAALLRLPRARREEREarERAEELLERVGLADRADEPAGNLSYGQ 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 149 KQKLGLCCALIHDPDLLILDEPTTGVDPLSRNQFWELIGRIRAGReGMSVL--------VatayMEEAerfDWLVAMDDG 220
Cdd:COG0411 158 QRRLEIARALATEPKLLLLDEPAAGLNPEETEELAELIRRLRDER-GITILliehdmdlV----MGLA---DRIVVLDFG 229
|
250
....*....|..
gi 15600424 221 KVLATGTPQELR 232
Cdd:COG0411 230 RVIAEGTPAEVR 241
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
275-482 |
1.72e-42 |
|
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: 152.73 E-value: 1.72e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 275 IEAEGLTCRFGDFVAVDHVSFRIERGEIFGFLGSNGCGKSTTMKMLTGLLPASEGTCALFGQPVDASDMAT---RRRVGY 351
Cdd:cd03229 1 LELKNVSKRYGQKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGEDLTDLEDELpplRRRIGM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 352 MSQAFSLYAELSVRQNLVlharlfhlpadgiparvgemlrrfdlekvadelpndLPL--GIRQRLSLAVAVIHKPEILIL 429
Cdd:cd03229 81 VFQDFALFPHLTVLENIA------------------------------------LGLsgGQQQRVALARALAMDPDVLLL 124
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 15600424 430 DEPTSGVDPVARDGFWELMVELSRRDGVTIFISTHFMNEAQR-CDRISLMHAGK 482
Cdd:cd03229 125 DEPTSALDPITRREVRALLKSLQAQLGITVVLVTHDLDEAARlADRVVVLRDGK 178
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
272-495 |
1.95e-42 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 157.56 E-value: 1.95e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 272 RIAIEAEGLTCRFGDFV--------AVDHVSFRIERGEIFGFLGSNGCGKSTTMKMLTGLLPASEGTCALFG-QPVdasd 342
Cdd:COG4586 12 RVYEKEPGLKGALKGLFrreyreveAVDDISFTIEPGEIVGFIGPNGAGKSTTIKMLTGILVPTSGEVRVLGyVPF---- 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 343 matRRRVGY-------MSQAFSLYAELSVRQNLVLHARLFHLPADGIPARVGEMLRRFDLEKVADELPNDLPLGIRQRLS 415
Cdd:COG4586 88 ---KRRKEFarrigvvFGQRSQLWWDLPAIDSFRLLKAIYRIPDAEYKKRLDELVELLDLGELLDTPVRQLSLGQRMRCE 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 416 LAVAVIHKPEILILDEPTSGVDPVARDGFWELMVELSRRDGVTIFISTHFMNEAQR-CDRISLMHAGKVLASDTPDELVR 494
Cdd:COG4586 165 LAAALLHRPKILFLDEPTIGLDVVSKEAIREFLKEYNRERGTTILLTSHDMDDIEAlCDRVIVIDHGRIIYDGSLEELKE 244
|
.
gi 15600424 495 Q 495
Cdd:COG4586 245 R 245
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
11-226 |
2.09e-42 |
|
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: 153.83 E-value: 2.09e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 11 LRGVSLRYGETRAVDDVSLEIPANRMVGLIGPDGVGKSSLLALLAGARKMQDGEIRVLDGDMRDRR-HRRavcpRIAYMP 89
Cdd:cd03259 3 LKGLSKTYGSVRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDGRDVTGVPpERR----NIGMVF 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 90 QGLgkNLYPTLSVFENVDFFGRLFGHDKAERERRIADLLQSTGLAPFAERPAGKLSGGMKQKLGLCCALIHDPDLLILDE 169
Cdd:cd03259 79 QDY--ALFPHLTVAENIAFGLKLRGVPKAEIRARVRELLELVGLEGLLNRYPHELSGGQQQRVALARALAREPSLLLLDE 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 15600424 170 PTTGVDPLSRNQFWELIGRIRAgREGMSVLVATAYMEEAERF-DWLVAMDDGKVLATG 226
Cdd:cd03259 157 PLSALDAKLREELREELKELQR-ELGITTIYVTHDQEEALALaDRIAVMNEGRIVQVG 213
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
10-226 |
2.61e-42 |
|
ATP-binding cassette domain of the metal-type transporters; This family includes transporters involved in the uptake of various metallic cations such as iron, manganese, and zinc. The ATPases of this group of transporters are very similar to members of iron-siderophore uptake family suggesting that they share a common ancestor. The best characterized metal-type ABC transporters are the YfeABCD system of Y. pestis, the SitABCD system of Salmonella enterica serovar Typhimurium, and the SitABCD transporter of Shigella flexneri. Moreover other uncharacterized homologs of these metal-type transporters are mainly found in pathogens like Haemophilus or enteroinvasive E. coli isolates.
Pssm-ID: 213202 [Multi-domain] Cd Length: 213 Bit Score: 153.46 E-value: 2.61e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 10 SLRGVSLRYGETRAVDDVSLEIPANRMVGLIGPDGVGKSSLLALLAGARKMQDGEIRVLDGDMRDRRHRravcprIAYMP 89
Cdd:cd03235 1 EVEDLTVSYGGHPVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFGKPLEKERKR------IGYVP 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 90 QGLGKNLYPTLSVFENV----DFFGRLFGHDKAERERRIADLLQSTGLAPFAERPAGKLSGGMKQKLGLCCALIHDPDLL 165
Cdd:cd03235 75 QRRSIDRDFPISVRDVVlmglYGHKGLFRRLSKADKAKVDEALERVGLSELADRQIGELSGGQQQRVLLARALVQDPDLL 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15600424 166 ILDEPTTGVDPLSRNQFWELIGRIRagREGMSVLVATAYMEEAER-FDWlVAMDDGKVLATG 226
Cdd:cd03235 155 LLDEPFAGVDPKTQEDIYELLRELR--REGMTILVVTHDLGLVLEyFDR-VLLLNRTVVASG 213
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
1-208 |
2.92e-42 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 155.25 E-value: 2.92e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 1 MTAGGSGVaSLRGVSLRY----GETRAVDDVSLEIPANRMVGLIGPDGVGKSSLLALLAGARKMQDGEIRVldgdmrDRR 76
Cdd:COG1116 1 MSAAAPAL-ELRGVSKRFptggGGVTALDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPTSGEVLV------DGK 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 77 HRRAVCPRIAYMPQGLgkNLYPTLSVFENVDFFGRLFGHDKAERERRIADLLQSTGLAPFAERPAGKLSGGMKQKLGLCC 156
Cdd:COG1116 74 PVTGPGPDRGVVFQEP--ALLPWLTVLDNVALGLELRGVPKAERRERARELLELVGLAGFEDAYPHQLSGGMRQRVAIAR 151
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 15600424 157 ALIHDPDLLILDEPTTGVDPLSRNQFWELIGRIRAgREGMSVLVATAYMEEA 208
Cdd:COG1116 152 ALANDPEVLLMDEPFGALDALTRERLQDELLRLWQ-ETGKTVLFVTHDVDEA 202
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
274-495 |
4.35e-42 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 157.54 E-value: 4.35e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 274 AIEAEGLTCRFGDFVAVDHVSFRIERGEIFGFLGSNGCGKSTTMKMLTGLLPASEGTCALFGQPVdaSDMATRRR-VGYM 352
Cdd:COG3839 3 SLELENVSKSYGGVEALKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAGLEDPTSGEILIGGRDV--TDLPPKDRnIAMV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 353 SQAFSLYAELSVRQNLVLHARLFHLPADGIPARVGEMLRRFDLEKVADELPNDLPLGIRQRLSLAVAVIHKPEILILDEP 432
Cdd:COG3839 81 FQSYALYPHMTVYENIAFPLKLRKVPKAEIDRRVREAAELLGLEDLLDRKPKQLSGGQRQRVALGRALVREPKVFLLDEP 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15600424 433 TSGVDPVARdgfWELMVELS---RRDGVTIFISTHFMNEAQR-CDRISLMHAGKVLASDTPDELVRQ 495
Cdd:COG3839 161 LSNLDAKLR---VEMRAEIKrlhRRLGTTTIYVTHDQVEAMTlADRIAVMNDGRIQQVGTPEELYDR 224
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
10-496 |
4.41e-42 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 161.35 E-value: 4.41e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 10 SLRGVSLRYGETRAVDDVSLEIPANRMVGLIGPDGVGKSSLLALLAGARKMQDGEIRVlDGdmRDRRHRRavcPRIAyMP 89
Cdd:COG3845 7 ELRGITKRFGGVVANDDVSLTVRPGEIHALLGENGAGKSTLMKILYGLYQPDSGEILI-DG--KPVRIRS---PRDA-IA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 90 QGLGK-----NLYPTLSVFENV------DFFGRLfghDKAERERRIADLLQSTGLA--PfaERPAGKLSGGMKQKLGLCC 156
Cdd:COG3845 80 LGIGMvhqhfMLVPNLTVAENIvlglepTKGGRL---DRKAARARIRELSERYGLDvdP--DAKVEDLSVGEQQRVEILK 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 157 ALIHDPDLLILDEPTTGVDPLSRNQFWELIGRIRAgrEGMSVLVATAYMEEAERF-DWLVAMDDGKVLATGTPQElrerT 235
Cdd:COG3845 155 ALYRGARILILDEPTAVLTPQEADELFEILRRLAA--EGKSIIFITHKLREVMAIaDRVTVLRRGKVVGTVDTAE----T 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 236 GTQSLESAFIallpeskraGHH-RLVIPPRPQSEGAPRiaIEAEGLTCRFGD-FVAVDHVSFRIERGEIFGFLGSNGCGK 313
Cdd:COG3845 229 SEEELAELMV---------GREvLLRVEKAPAEPGEVV--LEVENLSVRDDRgVPALKDVSLEVRAGEILGIAGVAGNGQ 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 314 STTMKMLTGLLPASEGTCALFGQPVDASDMATRRR--VGYMS---QAFSLYAELSVRQNLVLH-------ARLFHLPADG 381
Cdd:COG3845 298 SELAEALAGLRPPASGSIRLDGEDITGLSPRERRRlgVAYIPedrLGRGLVPDMSVAENLILGryrrppfSRGGFLDRKA 377
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 382 IPARVGEMLRRFDLeKVADElpnDLPlgIR-------QRLSLAVAVIHKPEILILDEPTSGVDPVARDGFWELMVELsRR 454
Cdd:COG3845 378 IRAFAEELIEEFDV-RTPGP---DTP--ARslsggnqQKVILARELSRDPKLLIAAQPTRGLDVGAIEFIHQRLLEL-RD 450
|
490 500 510 520
....*....|....*....|....*....|....*....|....
gi 15600424 455 DGVTI-FISTHfMNEAQR-CDRISLMHAGKVLASDTPDELVRQR 496
Cdd:COG3845 451 AGAAVlLISED-LDEILAlSDRIAVMYEGRIVGEVPAAEATREE 493
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
10-232 |
5.44e-42 |
|
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: 153.36 E-value: 5.44e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 10 SLRGVSLRYGETRAVDDVSLEIPANRMVGLIGPDGVGKSSLLALLAGARKMQDGEIRVLDGDMRDRR-HRRAVcpriaym 88
Cdd:cd03219 2 EVRGLTKRFGGLVALDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFDGEDITGLPpHEIAR------- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 89 pQGLGK-----NLYPTLSVFENV----------DFFGRLFGHDKAERERRIADLLQSTGLAPFAERPAGKLSGGMKQKLG 153
Cdd:cd03219 75 -LGIGRtfqipRLFPELTVLENVmvaaqartgsGLLLARARREEREARERAEELLERVGLADLADRPAGELSYGQQRRLE 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 154 LCCALIHDPDLLILDEPTTGVDPLSRNQFWELIGRIRagREGMSVLVA----TAYMEEAERfdwLVAMDDGKVLATGTPQ 229
Cdd:cd03219 154 IARALATDPKLLLLDEPAAGLNPEETEELAELIRELR--ERGITVLLVehdmDVVMSLADR---VTVLDQGRVIAEGTPD 228
|
...
gi 15600424 230 ELR 232
Cdd:cd03219 229 EVR 231
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
275-493 |
8.21e-42 |
|
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: 152.70 E-value: 8.21e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 275 IEAEGLTCRFGDFVAVDHVSFRIERGEIFGFLGSNGCGKSTTMKMLTGLLPASEGTCALFGQPVDASDMATRRR--VGYM 352
Cdd:cd03218 1 LRAENLSKRYGKRKVVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDGQDITKLPMHKRARlgIGYL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 353 SQAFSLYAELSVRQNLVLHARLFHLPADGIPARVGEMLRRFDLEKVADELPNDLPLGIRQRLSLAVAVIHKPEILILDEP 432
Cdd:cd03218 81 PQEASIFRKLTVEENILAVLEIRGLSKKEREEKLEELLEEFHITHLRKSKASSLSGGERRRVEIARALATNPKFLLLDEP 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15600424 433 TSGVDPVARDGFWELMVELSRRdGVTIFISTHFMNEA-QRCDRISLMHAGKVLASDTPDELV 493
Cdd:cd03218 161 FAGVDPIAVQDIQKIIKILKDR-GIGVLITDHNVRETlSITDRAYIIYEGKVLAEGTPEEIA 221
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
10-234 |
2.40e-41 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 155.64 E-value: 2.40e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 10 SLRGVSLRYGETRAVDDVSLEIPANRMVGLIGPDGVGKSSLLALLAGARKMQDGEIRvLDG-DMRDRR-HRRavcpRIAY 87
Cdd:COG3842 7 ELENVSKRYGDVTALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRIL-LDGrDVTGLPpEKR----NVGM 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 88 MPQGLGknLYPTLSVFENVDFFGRLFGHDKAERERRIADLLQSTGLAPFAERPAGKLSGGMKQKLGLCCALIHDPDLLIL 167
Cdd:COG3842 82 VFQDYA--LFPHLTVAENVAFGLRMRGVPKAEIRARVAELLELVGLEGLADRYPHQLSGGQQQRVALARALAPEPRVLLL 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15600424 168 DEPTTGVDPLSRNQFWELIGRIRAgREGMSVLVATAYMEEAERF-DWLVAMDDGKVLATGTPQELRER 234
Cdd:COG3842 160 DEPLSALDAKLREEMREELRRLQR-ELGITFIYVTHDQEEALALaDRIAVMNDGRIEQVGTPEEIYER 226
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
10-222 |
2.47e-41 |
|
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: 151.10 E-value: 2.47e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 10 SLRGVSLRYG----ETRAVDDVSLEIPANRMVGLIGPDGVGKSSLLALLAGARKMQDGEIRVLDGDM-----RDRRH-RR 79
Cdd:cd03255 2 ELKNLSKTYGgggeKVQALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRVDGTDIsklseKELAAfRR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 80 AvcpRIAYMPQGLgkNLYPTLSVFENVDFFGRLFGHDKAERERRIADLLQSTGLAPFAERPAGKLSGGMKQKLGLCCALI 159
Cdd:cd03255 82 R---HIGFVFQSF--NLLPDLTALENVELPLLLAGVPKKERRERAEELLERVGLGDRLNHYPSELSGGQQQRVAIARALA 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15600424 160 HDPDLLILDEPTTGVDPLSRNQFWELIGRIrAGREGMSVLVATAYMEEAERFDWLVAMDDGKV 222
Cdd:cd03255 157 NDPKIILADEPTGNLDSETGKEVMELLREL-NKEAGTTIVVVTHDPELAEYADRIIELRDGKI 218
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
11-241 |
2.68e-41 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 154.99 E-value: 2.68e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 11 LRGVSLRYGETRAVDDVSLEIPANRMVGLIGPDGVGKSSLLALLAGARKMQDGEIRVLDGDMRDRRhrRAVCPRIAYMPQ 90
Cdd:PRK13536 44 LAGVSKSYGDKAVVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKITVLGVPVPARA--RLARARIGVVPQ 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 91 GlgKNLYPTLSVFENVDFFGRLFGHDKAERERRIADLLQSTGLAPFAERPAGKLSGGMKQKLGLCCALIHDPDLLILDEP 170
Cdd:PRK13536 122 F--DNLDLEFTVRENLLVFGRYFGMSTREIEAVIPSLLEFARLESKADARVSDLSGGMKRRLTLARALINDPQLLILDEP 199
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15600424 171 TTGVDPLSRNQFWEligRIRA-GREGMSVLVATAYMEEAERF-DWLVAMDDGKVLATGTPQEL-RERTGTQSLE 241
Cdd:PRK13536 200 TTGLDPHARHLIWE---RLRSlLARGKTILLTTHFMEEAERLcDRLCVLEAGRKIAEGRPHALiDEHIGCQVIE 270
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
23-226 |
2.98e-41 |
|
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: 150.98 E-value: 2.98e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 23 AVDDVSLEIPANRMVGLIGPDGVGKSSLLALLAGARKMQDGEIRVlDGdMRDRRHRRAVCPRIAYMPQGLGknLYPTLSV 102
Cdd:cd03266 20 AVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATV-DG-FDVVKEPAEARRRLGFVSDSTG--LYDRLTA 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 103 FENVDFFGRLFGHDKAERERRIADLLQSTGLAPFAERPAGKLSGGMKQKLGLCCALIHDPDLLILDEPTTGVDPLSRNQF 182
Cdd:cd03266 96 RENLEYFAGLYGLKGDELTARLEELADRLGMEELLDRRVGGFSTGMRQKVAIARALVHDPPVLLLDEPTTGLDVMATRAL 175
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 15600424 183 WELIGRIRAgrEGMSVLVATAYMEEAERF-DWLVAMDDGKVLATG 226
Cdd:cd03266 176 REFIRQLRA--LGKCILFSTHIMQEVERLcDRVVVLHRGRVVYEG 218
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
275-492 |
3.66e-41 |
|
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: 150.79 E-value: 3.66e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 275 IEAEGLTCRFGDFVAVDHVSFRIERGEIFGFLGSNGCGKSTTMKMLTGLLPA-----SEGTCALFGQPVDASDM---ATR 346
Cdd:cd03260 1 IELRDLNVYYGDKHALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRLNDLipgapDEGEVLLDGKDIYDLDVdvlELR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 347 RRVGYMSQAFSLYAeLSVRQNLVLHARLfH--LPADGIPARVGEMLRRFDL-EKVADEL-PNDLPLGIRQRLSLAVAVIH 422
Cdd:cd03260 81 RRVGMVFQKPNPFP-GSIYDNVAYGLRL-HgiKLKEELDERVEEALRKAALwDEVKDRLhALGLSGGQQQRLCLARALAN 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15600424 423 KPEILILDEPTSGVDPVARDGFWELMVELSRRdgVTIFISTHFMNEAQRC-DRISLMHAGKVLASDTPDEL 492
Cdd:cd03260 159 EPEVLLLDEPTSALDPISTAKIEELIAELKKE--YTIVIVTHNMQQAARVaDRTAFLLNGRLVEFGPTEQI 227
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
275-495 |
4.49e-41 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 154.53 E-value: 4.49e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 275 IEAEGLTCRFGDFVAVDHVSFRIERGEIFGFLGSNGCGKSTTMKMLTGLLPASEGTCALFGQPVDaSDMATR-RRVGYMS 353
Cdd:COG1118 3 IEVRNISKRFGSFTLLDDVSLEIASGELVALLGPSGSGKTTLLRIIAGLETPDSGRIVLNGRDLF-TNLPPReRRVGFVF 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 354 QAFSLYAELSVRQNLVLHARLFHLPADGIPARVGEMLRRFDLEKVADELPNDLPLGIRQRLSLAVAVIHKPEILILDEPT 433
Cdd:COG1118 82 QHYALFPHMTVAENIAFGLRVRPPSKAEIRARVEELLELVQLEGLADRYPSQLSGGQRQRVALARALAVEPEVLLLDEPF 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15600424 434 SGVDPVARDGFWELMVELSRRDGVTIFISTHFMNEAQR-CDRISLMHAGKVLASDTPDELVRQ 495
Cdd:COG1118 162 GALDAKVRKELRRWLRRLHDELGGTTVFVTHDQEEALElADRVVVMNQGRIEQVGTPDEVYDR 224
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
276-487 |
7.37e-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: 149.61 E-value: 7.37e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 276 EAEGLTCRFGDFVAVDHVSFRIERGEIFGFLGSNGCGKSTTMKMLTGLLPASEGTCALFGQPVdasdMATRRRVGYMSQA 355
Cdd:cd03235 1 EVEDLTVSYGGHPVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFGKPL----EKERKRIGYVPQR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 356 FSL--YAELSVRQnLVLHARLFHLPADGIP-----ARVGEMLRRFDLEKVADELPNDLPLGIRQRLSLAVAVIHKPEILI 428
Cdd:cd03235 77 RSIdrDFPISVRD-VVLMGLYGHKGLFRRLskadkAKVDEALERVGLSELADRQIGELSGGQQQRVLLARALVQDPDLLL 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 429 LDEPTSGVDPVARDGFWELMVELsRRDGVTIFISTHFMNEAQR-CDRISLMhAGKVLASD 487
Cdd:cd03235 156 LDEPFAGVDPKTQEDIYELLREL-RREGMTILVVTHDLGLVLEyFDRVLLL-NRTVVASG 213
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
274-494 |
8.69e-41 |
|
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: 150.34 E-value: 8.69e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 274 AIEAEGLTCRFG----DFVAVDHVSFRIERGEIFGFLGSNGCGKSTTMKMLTGLLPASEGTCALFGQPV-DASDMATRRR 348
Cdd:COG1124 1 MLEVRNLSVSYGqggrRVPVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVTFDGRPVtRRRRKAFRRR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 349 VGYMSQ--AFSLYAELSVRQNLVLHARLFHLPAdgIPARVGEMLRRFDL-EKVADELPNDLPLGIRQRLSLAVAVIHKPE 425
Cdd:COG1124 81 VQMVFQdpYASLHPRHTVDRILAEPLRIHGLPD--REERIAELLEQVGLpPSFLDRYPHQLSGGQRQRVAIARALILEPE 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 426 ILILDEPTSGVDPVARDGFWELMVELSRRDGVTIFISTHFMNEAQR-CDRISLMHAGKVLASDTPDELVR 494
Cdd:COG1124 159 LLLLDEPTSALDVSVQAEILNLLKDLREERGLTYLFVSHDLAVVAHlCDRVAVMQNGRIVEELTVADLLA 228
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
275-495 |
2.45e-40 |
|
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: 148.54 E-value: 2.45e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 275 IEAEGLTCRFGDFVAVDHVSFRIERGEIFGFLGSNGCGKSTTMKMLTGLLPASEGTCALFGQPVDASDmATRRRVGYMSQ 354
Cdd:cd03300 1 IELENVSKFYGGFVALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGKDITNLP-PHKRPVNTVFQ 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 355 AFSLYAELSVRQNLVLHARLFHLPADGIPARVGEMLRRFDLEKVADELPNDLPLGIRQRLSLAVAVIHKPEILILDEPTS 434
Cdd:cd03300 80 NYALFPHLTVFENIAFGLRLKKLPKAEIKERVAEALDLVQLEGYANRKPSQLSGGQQQRVAIARALVNEPKVLLLDEPLG 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15600424 435 GVDPVARDGFWELMVELSRRDGVTIFISTHFMNEA-QRCDRISLMHAGKVLASDTPDELVRQ 495
Cdd:cd03300 160 ALDLKLRKDMQLELKRLQKELGITFVFVTHDQEEAlTMSDRIAVMNKGKIQQIGTPEEIYEE 221
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
274-495 |
4.14e-40 |
|
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: 155.83 E-value: 4.14e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 274 AIEAEGLTCRF--GDFVAVDHVSFRIERGEIFGFLGSNGCGKSTTMKMLTGLLPAS---EGTCALFGQPVDASDMATR-R 347
Cdd:COG1123 4 LLEVRDLSVRYpgGDVPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGLLPHGgriSGEVLLDGRDLLELSEALRgR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 348 RVGYMSQ-AFSLYAELSVRQNLVLHARLFHLPADGIPARVGEMLRRFDLEKVADELPNDLPLGIRQRLSLAVAVIHKPEI 426
Cdd:COG1123 84 RIGMVFQdPMTQLNPVTVGDQIAEALENLGLSRAEARARVLELLEAVGLERRLDRYPHQLSGGQRQRVAIAMALALDPDL 163
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 427 LILDEPTSGVDPVARDGFWELMVELSRRDGVTIFISTHFMNE-AQRCDRISLMHAGKVLASDTPDELVRQ 495
Cdd:COG1123 164 LIADEPTTALDVTTQAEILDLLRELQRERGTTVLLITHDLGVvAEIADRVVVMDDGRIVEDGPPEEILAA 233
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
275-483 |
5.97e-40 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 147.12 E-value: 5.97e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 275 IEAEGLTCRF-GDFVAVDHVSFRIERGEiFGFL-GSNGCGKSTTMKMLTGLLPASEGTCALFGQPV---DASDMA-TRRR 348
Cdd:COG2884 2 IRFENVSKRYpGGREALSDVSLEIEKGE-FVFLtGPSGAGKSTLLKLLYGEERPTSGQVLVNGQDLsrlKRREIPyLRRR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 349 VGYMSQAFSLYAELSVRQNLVLHARLFHLPADGIPARVGEMLRRFDLEKVADELPNDLPLGIRQRLSLAVAVIHKPEILI 428
Cdd:COG2884 81 IGVVFQDFRLLPDRTVYENVALPLRVTGKSRKEIRRRVREVLDLVGLSDKAKALPHELSGGEQQRVAIARALVNRPELLL 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 15600424 429 LDEPTSGVDPVARDGFWELMVELSRRdGVTIFISTH---FMNEAQRcdRISLMHAGKV 483
Cdd:COG2884 161 ADEPTGNLDPETSWEIMELLEEINRR-GTTVLIATHdleLVDRMPK--RVLELEDGRL 215
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
10-232 |
1.05e-39 |
|
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: 146.88 E-value: 1.05e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 10 SLRGVSLRYGETRAVDDVSLEIPANRMVGLIGPDGVGKSSLLALLAGARKMQDGEIRVLDGDMRD------RRHRRavcp 83
Cdd:cd03261 2 ELRGLTKSFGGRTVLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGEDISGlseaelYRLRR---- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 84 RIAYMPQGLGknLYPTLSVFENVDFFGRLFGHDKAERERRIADL-LQSTGLAPFAERPAGKLSGGMKQKLGLCCALIHDP 162
Cdd:cd03261 78 RMGMLFQSGA--LFDSLTVFENVAFPLREHTRLSEEEIREIVLEkLEAVGLRGAEDLYPAELSGGMKKRVALARALALDP 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15600424 163 DLLILDEPTTGVDPLSRNQFWELIGRIRAgREGMSVLVATAYMEEAERF-DWLVAMDDGKVLATGTPQELR 232
Cdd:cd03261 156 ELLLYDEPTAGLDPIASGVIDDLIRSLKK-ELGLTSIMVTHDLDTAFAIaDRIAVLYDGKIVAEGTPEELR 225
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
10-208 |
1.12e-39 |
|
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ATP-binding subunits of the bacterial ABC-type nitrate and sulfonate transport systems, respectively. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213260 [Multi-domain] Cd Length: 220 Bit Score: 146.46 E-value: 1.12e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 10 SLRGVSLRYG----ETRAVDDVSLEIPANRMVGLIGPDGVGKSSLLALLAGARKMQDGEIRVlDGDMRDRRHrravcPRI 85
Cdd:cd03293 2 EVRNVSKTYGggggAVTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLV-DGEPVTGPG-----PDR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 86 AYMPQGlgKNLYPTLSVFENVDFFGRLFGHDKAERERRIADLLQSTGLAPFAERPAGKLSGGMKQKLGLCCALIHDPDLL 165
Cdd:cd03293 76 GYVFQQ--DALLPWLTVLDNVALGLELQGVPKAEARERAEELLELVGLSGFENAYPHQLSGGMRQRVALARALAVDPDVL 153
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 15600424 166 ILDEPTTGVDPLSRNQFWELIGRIRAgREGMSVLVATAYMEEA 208
Cdd:cd03293 154 LLDEPFSALDALTREQLQEELLDIWR-ETGKTVLLVTHDIDEA 195
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
275-492 |
2.25e-39 |
|
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: 145.80 E-value: 2.25e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 275 IEAEGLTCRFGD----FVAVDHVSFRIERGEIFGFLGSNGCGKSTTMKMLTGLLPASEGTCALFGQPVD----ASDMATR 346
Cdd:cd03258 2 IELKNVSKVFGDtggkVTALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGSVLVDGTDLTllsgKELRKAR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 347 RRVGYMSQAFSLYAELSVRQNLVLHARLFHLPADGIPARVGEMLRRFDLEKVADELPNDLPLGIRQRLSLAVAVIHKPEI 426
Cdd:cd03258 82 RRIGMIFQHFNLLSSRTVFENVALPLEIAGVPKAEIEERVLELLELVGLEDKADAYPAQLSGGQKQRVGIARALANNPKV 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15600424 427 LILDEPTSGVDPVARDGFWELMVELSRRDGVTIFISTHFMNEAQR-CDRISLMHAGKVLASDTPDEL 492
Cdd:cd03258 162 LLCDEATSALDPETTQSILALLRDINRELGLTIVLITHEMEVVKRiCDRVAVMEKGEVVEEGTVEEV 228
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
274-492 |
2.46e-39 |
|
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: 145.94 E-value: 2.46e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 274 AIEAEGLTCRFGDFVAVDHVSFRIERGEIFGFLGSNGCGKSTTMKMLTGLLPASEGTCALFGQpvDASDMATRRR-VGYM 352
Cdd:cd03296 2 SIEVRNVSKRFGDFVALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGGE--DATDVPVQERnVGFV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 353 SQAFSLYAELSVRQN----LVLHARLFHLPADGIPARVGEMLRRFDLEKVADELPNDLPLGIRQRLSLAVAVIHKPEILI 428
Cdd:cd03296 80 FQHYALFRHMTVFDNvafgLRVKPRSERPPEAEIRAKVHELLKLVQLDWLADRYPAQLSGGQRQRVALARALAVEPKVLL 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15600424 429 LDEPTSGVDPVARDGFWELMVELSRRDGVTIFISTHFMNEA-QRCDRISLMHAGKVLASDTPDEL 492
Cdd:cd03296 160 LDEPFGALDAKVRKELRRWLRRLHDELHVTTVFVTHDQEEAlEVADRVVVMNKGRIEQVGTPDEV 224
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
271-494 |
2.73e-39 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 152.87 E-value: 2.73e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 271 PRIAIEAEGLTCRFGDFVAVDHVSFRIERGEIFGFLGSNGCGKSTTMKMLTGLLPASEGTCALFGQPVDASD--MATRRR 348
Cdd:COG1129 1 AEPLLEMRGISKSFGGVKALDGVSLELRPGEVHALLGENGAGKSTLMKILSGVYQPDSGEILLDGEPVRFRSprDAQAAG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 349 VGYMSQAFSLYAELSVRQNLVLHarlfHLPADG-------IPARVGEMLRRFDLEKVADELPNDLPLGIRQRLSLAVAVI 421
Cdd:COG1129 81 IAIIHQELNLVPNLSVAENIFLG----REPRRGglidwraMRRRARELLARLGLDIDPDTPVGDLSVAQQQLVEIARALS 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 422 HKPEILILDEPTSGVDPVARDGFWELMVELsRRDGVTI-FIStHFMNEAQR-CDRISLMHAGKVLASD-----TPDELVR 494
Cdd:COG1129 157 RDARVLILDEPTASLTEREVERLFRIIRRL-KAQGVAIiYIS-HRLDEVFEiADRVTVLRDGRLVGTGpvaelTEDELVR 234
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
10-224 |
4.47e-39 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 144.80 E-value: 4.47e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 10 SLRGVSLRYG----ETRAVDDVSLEIPANRMVGLIGPDGVGKSSLLALLAGARKMQDGEIRVLD---GDMRDR---RHRR 79
Cdd:COG1136 6 ELRNLTKSYGtgegEVTALRGVSLSIEAGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVLIDGqdiSSLSERelaRLRR 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 80 AvcpRIAYMPQGLgkNLYPTLSVFENVDFFGRLFGHDKAERERRIADLLQSTGLAPFAERPAGKLSGGMKQKLGLCCALI 159
Cdd:COG1136 86 R---HIGFVFQFF--NLLPELTALENVALPLLLAGVSRKERRERARELLERVGLGDRLDHRPSQLSGGQQQRVAIARALV 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15600424 160 HDPDLLILDEPTTGVDPLSRNQFWELIGRIRAgREGMSVLVATAYMEEAERFDWLVAMDDGKVLA 224
Cdd:COG1136 161 NRPKLILADEPTGNLDSKTGEEVLELLRELNR-ELGTTIVMVTHDPELAARADRVIRLRDGRIVS 224
|
|
| proV |
TIGR01186 |
glycine betaine/L-proline transport ATP binding subunit; This model describes the glycine ... |
285-494 |
6.97e-39 |
|
glycine betaine/L-proline transport ATP binding subunit; This model describes the glycine betaine/L-proline ATP binding subunit in bacteria and its equivalents in archaea. This transport system belong to the larger ATP-Binding Cassette (ABC) transporter superfamily. The characteristic feature of these transporter is the obligatory coupling of ATP hydrolysis to substrate translocation. The minimal configuration of bacterial ABC transport system: an ATPase or ATP binding subunit; An integral membrane protein; a hydrophilic polypetpide, which likely functions as substrate binding protein. Functionally, this transport system is involved in osmoregulation. Under conditions of stress, the organism recruits these transport system to accumulate glycine betaine and other solutes which offer osmo-protection. It has been demonstrated that glycine betaine uptake is accompanied by symport with sodium ions. The locus has been named variously as proU or opuA. A gene library from L.lactis functionally complements an E.coli proU mutant. The comlementing locus is similar to a opuA locus in B.sutlis. This clarifies the differences in nomenclature. [Transport and binding proteins, Amino acids, peptides and amines]
Pssm-ID: 130254 [Multi-domain] Cd Length: 363 Bit Score: 148.46 E-value: 6.97e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 285 GDFVAVDHVSFRIERGEIFGFLGSNGCGKSTTMKMLTGLLPASEGTCALFGQPVDASDMA-----TRRRVGYMSQAFSLY 359
Cdd:TIGR01186 4 GGKKGVNDADLAIAKGEIFVIMGLSGSGKSTTVRMLNRLIEPTAGQIFIDGENIMKQSPVelrevRRKKIGMVFQQFALF 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 360 AELSVRQNLVLHARLFHLPADGIPARVGEMLRRFDLEKVADELPNDLPLGIRQRLSLAVAVIHKPEILILDEPTSGVDPV 439
Cdd:TIGR01186 84 PHMTILQNTSLGPELLGWPEQERKEKALELLKLVGLEEYEHRYPDELSGGMQQRVGLARALAAEPDILLMDEAFSALDPL 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 15600424 440 ARDGFWELMVELSRRDGVTIFISTHFMNEAQRC-DRISLMHAGKVLASDTPDELVR 494
Cdd:TIGR01186 164 IRDSMQDELKKLQATLQKTIVFITHDLDEAIRIgDRIVIMKAGEIVQVGTPDEILR 219
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
283-487 |
7.97e-39 |
|
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: 144.40 E-value: 7.97e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 283 RFGDFVAVDHVSFRIERGEIFGFLGSNGCGKSTTMKMLTGLLPASEGTCALFGQ-PVDASDmATRRRVGY-MSQAFSLYA 360
Cdd:cd03267 30 KYREVEALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRVAGLvPWKRRK-KFLRRIGVvFGQKTQLWW 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 361 ELSVRQNLVLHARLFHLPADGIPARVGEMLRRFDLEKVADELPNDLPLGIRQRLSLAVAVIHKPEILILDEPTSGVDPVA 440
Cdd:cd03267 109 DLPVIDSFYLLAAIYDLPPARFKKRLDELSELLDLEELLDTPVRQLSLGQRMRAEIAAALLHEPEILFLDEPTIGLDVVA 188
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 15600424 441 RDGFWELMVELSRRDGVTIFISTHFMNE-AQRCDRISLMHAGKVLASD 487
Cdd:cd03267 189 QENIRNFLKEYNRERGTTVLLTSHYMKDiEALARRVLVIDKGRLLYDG 236
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
11-222 |
1.37e-38 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 143.27 E-value: 1.37e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 11 LRGVSLRYGETR-AVDDVSLEIPANRMVGLIGPDGVGKSSLLALLAGARKMQDGEIRVLDGDMRDRRHRRavcprIAYMP 89
Cdd:COG2884 4 FENVSKRYPGGReALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLVNGQDLSRLKRRE-----IPYLR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 90 QGLG------KnLYPTLSVFENVDFFGRLFGHDKAERERRIADLLQSTGLAPFAERPAGKLSGGMKQKLGLCCALIHDPD 163
Cdd:COG2884 79 RRIGvvfqdfR-LLPDRTVYENVALPLRVTGKSRKEIRRRVREVLDLVGLSDKAKALPHELSGGEQQRVAIARALVNRPE 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 164 LLILDEPTTGVDPLSRNQFWELIGRIRagREGMSVLVATAYMEEAERFDW-LVAMDDGKV 222
Cdd:COG2884 158 LLLADEPTGNLDPETSWEIMELLEEIN--RRGTTVLIATHDLELVDRMPKrVLELEDGRL 215
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
276-486 |
1.44e-38 |
|
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: 141.80 E-value: 1.44e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 276 EAEGLTCRFGDFVAVDHVSFRIERGEIFGFLGSNGCGKSTTMKMLTGLLPASEGTCALFGQPVDASDMATR-RRVGYMSQ 354
Cdd:cd03214 1 EVENLSVGYGGRTVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDGKDLASLSPKELaRKIAYVPQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 355 AfslyaelsvrqnlvlharlfhlpadgiparvgemLRRFDLEKVADELPNDLPLGIRQRLSLAVAVIHKPEILILDEPTS 434
Cdd:cd03214 81 A----------------------------------LELLGLAHLADRPFNELSGGERQRVLLARALAQEPPILLLDEPTS 126
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 15600424 435 GVDPVARDGFWELMVELSRRDGVTIFISTHFMNEAQR-CDRISLMHAGKVLAS 486
Cdd:cd03214 127 HLDIAHQIELLELLRRLARERGKTVVMVLHDLNLAARyADRVILLKDGRIVAQ 179
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
10-226 |
1.46e-38 |
|
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: 142.74 E-value: 1.46e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 10 SLRGVSLRYGETRAVDDVSLEIPANRMVGLIGPDGVGKSSLLALLAGARKMQDGEIRVLDGDMRDRRHRRAvcpRIAYMP 89
Cdd:cd03268 2 KTNDLTKTYGKKRVLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEITFDGKSYQKNIEALR---RIGALI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 90 QGLGknLYPTLSVFENVDFFGRLFGhdkaERERRIADLLQSTGLAPFAERPAGKLSGGMKQKLGLCCALIHDPDLLILDE 169
Cdd:cd03268 79 EAPG--FYPNLTARENLRLLARLLG----IRKKRIDEVLDVVGLKDSAKKKVKGFSLGMKQRLGIALALLGNPDLLILDE 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 15600424 170 PTTGVDPLSRNQFWELIGRIRAgrEGMSVLVATAYMEEAERF-DWLVAMDDGKVLATG 226
Cdd:cd03268 153 PTNGLDPDGIKELRELILSLRD--QGITVLISSHLLSEIQKVaDRIGIINKGKLIEEG 208
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
10-226 |
1.89e-38 |
|
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: 141.42 E-value: 1.89e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 10 SLRGVSLRYGETRAVDDVSLEIPANRMVGLIGPDGVGKSSLLALLAGARKMQDGEIRvLDGDMRDRRHRRAVCPRIAYMP 89
Cdd:cd03214 1 EVENLSVGYGGRTVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEIL-LDGKDLASLSPKELARKIAYVP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 90 QglgknlyptlsvfenvdffgrlfghdkaererriadLLQSTGLAPFAERPAGKLSGGMKQKLGLCCALIHDPDLLILDE 169
Cdd:cd03214 80 Q------------------------------------ALELLGLAHLADRPFNELSGGERQRVLLARALAQEPPILLLDE 123
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 170 PTTGVDPlsRNQFwELIGRIR--AGREGMSVLVATAYMEEAERF-DWLVAMDDGKVLATG 226
Cdd:cd03214 124 PTSHLDI--AHQI-ELLELLRrlARERGKTVVMVLHDLNLAARYaDRVILLKDGRIVAQG 180
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
276-482 |
2.85e-38 |
|
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: 140.07 E-value: 2.85e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 276 EAEGLTCRFGDFVAVDHVSFRIERGEIFGFLGSNGCGKSTTMKMLTGLLPASEGTCALFGQPVDASDMAT-RRRVGYMSQ 354
Cdd:cd00267 1 EIENLSFRYGGRTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGKDIAKLPLEElRRRIGYVPQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 355 afslyaeLSVrqnlvlharlfhlpadgiparvGEmlrrfdlekvadelpndlplgiRQRLSLAVAVIHKPEILILDEPTS 434
Cdd:cd00267 81 -------LSG----------------------GQ----------------------RQRVALARALLLNPDLLLLDEPTS 109
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 15600424 435 GVDPVARDGFWELMVELSRRdGVTIFISTHFMNEAQR-CDRISLMHAGK 482
Cdd:cd00267 110 GLDPASRERLLELLRELAEE-GRTVIIVTHDPELAELaADRVIVLKDGK 157
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
275-483 |
2.87e-38 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 141.88 E-value: 2.87e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 275 IEAEGLTCRFGDFVAVDHVSFRIERGEIFGFLGSNGCGKSTTMKMLTGLLPASEGTCALFGQPVDASDMAT-RRRVGYMS 353
Cdd:COG4619 1 LELEGLSFRVGGKPILSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIYLDGKPLSAMPPPEwRRQVAYVP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 354 QAFSLYAElSVRQNLVLHARLFHLPADgiPARVGEMLRRFDL-EKVADELPNDLPLGIRQRLSLAVAVIHKPEILILDEP 432
Cdd:COG4619 81 QEPALWGG-TVRDNLPFPFQLRERKFD--RERALELLERLGLpPDILDKPVERLSGGERQRLALIRALLLQPDVLLLDEP 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 15600424 433 TSGVDPVARDGFWELMVELSRRDGVTIFISTHFMNEAQR-CDRISLMHAGKV 483
Cdd:COG4619 158 TSALDPENTRRVEELLREYLAEEGRAVLWVSHDPEQIERvADRVLTLEAGRL 209
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
10-233 |
4.87e-38 |
|
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of the LIV-I bacterial ABC-type two-component transport system that imports neutral, branched-chain amino acids. The E. coli branched-chain amino acid transporter comprises a heterodimer of ABC transporters (LivF and LivG), a heterodimer of six-helix TM domains (LivM and LivH), and one of two alternative soluble periplasmic substrate binding proteins (LivK or LivJ). ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules.
Pssm-ID: 213191 [Multi-domain] Cd Length: 222 Bit Score: 141.80 E-value: 4.87e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 10 SLRGVSLRYGETRAVDDVSLEIPANRMVGLIGPDGVGKSSLLALLAGARKMQDGEIRVLDGDMRDRR-HRRAvcpR--IA 86
Cdd:cd03224 2 EVENLNAGYGKSQILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDGRDITGLPpHERA---RagIG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 87 YMPQglGKNLYPTLSVFENVdffgRL--FGHDKAERERRIADLLQS-TGLAPFAERPAGKLSGGMKQKLGLCCALIHDPD 163
Cdd:cd03224 79 YVPE--GRRIFPELTVEENL----LLgaYARRRAKRKARLERVYELfPRLKERRKQLAGTLSGGEQQMLAIARALMSRPK 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15600424 164 LLILDEPTTGVDPLSRNQFWELIGRIRagREGMSVLV----ATAYMEEAERFdwlVAMDDGKVLATGTPQELRE 233
Cdd:cd03224 153 LLLLDEPSEGLAPKIVEEIFEAIRELR--DEGVTILLveqnARFALEIADRA---YVLERGRVVLEGTAAELLA 221
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
10-233 |
6.57e-38 |
|
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: 141.66 E-value: 6.57e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 10 SLRGVSLRYGETRAVDDVSLEIPANRMVGLIGPDGVGKSSLLALLAGARKMQDGEIRVLDGDMRDRR-HRRAvcpR--IA 86
Cdd:COG0410 5 EVENLHAGYGGIHVLHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRSGSIRFDGEDITGLPpHRIA---RlgIG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 87 YMPQGlgKNLYPTLSVFENVDFfGRLFGHDKAERERRIADLLQst-gLAPFAERPAGKLSGGMKQKLGLCCALIHDPDLL 165
Cdd:COG0410 82 YVPEG--RRIFPSLTVEENLLL-GAYARRDRAEVRADLERVYElfprLKERRRQRAGTLSGGEQQMLAIGRALMSRPKLL 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15600424 166 ILDEPTTGVDPLSRNQFWELIGRIRagREGMSVLV----ATAYMEEAERFdwlVAMDDGKVLATGTPQELRE 233
Cdd:COG0410 159 LLDEPSLGLAPLIVEEIFEIIRRLN--REGVTILLveqnARFALEIADRA---YVLERGRIVLEGTAAELLA 225
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
275-493 |
7.23e-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: 7.23e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 275 IEAEGLTCRFGDFVAVDHVSFRIERGEIFGFLGSNGCGKSTTMKMLTGLLPASEGTCALFGQPVDASDMATRRR--VGYM 352
Cdd:COG1137 4 LEAENLVKSYGKRTVVKDVSLEVNQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGRIFLDGEDITHLPMHKRARlgIGYL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 353 SQAFSLYAELSVRQNLVLHARLFHLPADGIPARVGEMLRRFDLEKVADELPNDLPLGIRQRLSLAVAVIHKPEILILDEP 432
Cdd:COG1137 84 PQEASIFRKLTVEDNILAVLELRKLSKKEREERLEELLEEFGITHLRKSKAYSLSGGERRRVEIARALATNPKFILLDEP 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15600424 433 TSGVDPVARDGFWELMVELSRRdGVTIFISTHFMNEAQR-CDRISLMHAGKVLASDTPDELV 493
Cdd:COG1137 164 FAGVDPIAVADIQKIIRHLKER-GIGVLITDHNVRETLGiCDRAYIISEGKVLAEGTPEEIL 224
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
260-492 |
1.19e-37 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 145.36 E-value: 1.19e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 260 VIP-PRPQSEGAPRIAIEAEGLTCRFGDFVAVDHVSFRIERGEIFGFLGSNGCGKSTTMKMLTGLLPASEGTCALFGQpv 338
Cdd:PRK11607 4 AIPrPQAKTRKALTPLLEIRNLTKSFDGQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGV-- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 339 DASDMATRRR-VGYMSQAFSLYAELSVRQNLVLHARLFHLPADGIPARVGEMLRRFDLEKVADELPNDLPLGIRQRLSLA 417
Cdd:PRK11607 82 DLSHVPPYQRpINMMFQSYALFPHMTVEQNIAFGLKQDKLPKAEIASRVNEMLGLVHMQEFAKRKPHQLSGGQRQRVALA 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15600424 418 VAVIHKPEILILDEPTSGVDPVARDGFWELMVELSRRDGVTIFISTHFMNEAQR-CDRISLMHAGKVLASDTPDEL 492
Cdd:PRK11607 162 RSLAKRPKLLLLDEPMGALDKKLRDRMQLEVVDILERVGVTCVMVTHDQEEAMTmAGRIAIMNRGKFVQIGEPEEI 237
|
|
| ABC2_membrane_3 |
pfam12698 |
ABC-2 family transporter protein; This family is related to the ABC-2 membrane transporter ... |
578-908 |
1.56e-37 |
|
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: 144.07 E-value: 1.56e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 578 MFIIGYGINmDVEDLSWAVLDRDQTTTSQAYALNIAGSRYFVEHAPITDPDDLDRRLRSGELSLAVEIPPNFGRDLKRGS 657
Cdd:pfam12698 19 GLIFSNAVN-DPEELPVAVVDEDNSSLSRQLVRALEASPTVNLVQYVDSEEEAKEALKNGKIDGLLVIPKGFSKDLLKGE 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 658 DPAIGVWIDGAMPTRANTVLGYVQGLHTSYLA-DLSRQAGGAEASAAASTEVRYRYNPDVESLKAMVPaVIPLLLIMIPA 736
Cdd:pfam12698 98 SATVTVYINSSNLLVSKLILNALQSLLQQLNAsALVLLLEALSTSAPIPVESTPLFNPQSGYAYYLVG-LILMIIILIGA 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 737 MLTALGVVREKELGSITNLYVTPVTRLEFLVGKQLPYVAMGMINFLLMLVLAIVVFrVPLKGSFLALtIGAFLYVVTSTG 816
Cdd:pfam12698 177 AIIAVSIVEEKESRIKERLLVSGVSPLQYWLGKILGDFLVGLLQLLIILLLLFGIG-IPFGNLGLLL-LLFLLYGLAYIA 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 817 LGLFLSTFMRSQIAAVFGVAIATMIPAIQFSGLIhPVSSLEGAAAWIGKLYPTSHFLVVSRgAFSKSLGLSDLWAYYLPL 896
Cdd:pfam12698 255 LGYLLGSLFKNSEDAQSIIGIVILLLSGFFGGLF-PLEDPPSFLQWIFSIIPFFSPIDGLL-RLIYGDSLWEIAPSLIIL 332
|
330
....*....|..
gi 15600424 897 AASIVVLTLLSV 908
Cdd:pfam12698 333 LLFAVVLLLLAL 344
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
11-231 |
1.86e-37 |
|
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; Phosphonates are a class of organophosphorus compounds characterized by a chemically stable carbon-to-phosphorus (C-P) bond. Phosphonates are widespread among naturally occurring compounds in all kingdoms of wildlife, but only prokaryotic microorganisms are able to cleave this bond. Certain bacteria such as E. coli can use alkylphosphonates as a phosphorus source. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213223 [Multi-domain] Cd Length: 241 Bit Score: 140.78 E-value: 1.86e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 11 LRGVSLRYGE-TRAVDDVSLEIPANRMVGLIGPDGVGKSSLLALLAGARKMQDGEIRVLDGDMRDRRHR--RAVCPRIAY 87
Cdd:cd03256 3 VENLSKTYPNgKKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGTDINKLKGKalRQLRRQIGM 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 88 MPQGLgkNLYPTLSVFENVdFFGRLFGH----------DKAERERRIAdLLQSTGLAPFAERPAGKLSGGMKQKLGLCCA 157
Cdd:cd03256 83 IFQQF--NLIERLSVLENV-LSGRLGRRstwrslfglfPKEEKQRALA-ALERVGLLDKAYQRADQLSGGQQQRVAIARA 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15600424 158 LIHDPDLLILDEPTTGVDPLSRNQFWELIGRIrAGREGMSVLVATAYMEEAERF-DWLVAMDDGKVLATGTPQEL 231
Cdd:cd03256 159 LMQQPKLILADEPVASLDPASSRQVMDLLKRI-NREEGITVIVSLHQVDLAREYaDRIVGLKDGRIVFDGPPAEL 232
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
275-483 |
1.96e-37 |
|
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: 140.33 E-value: 1.96e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 275 IEAEGLTCRF----GDFVAVDHVSFRIERGEIFGFLGSNGCGKSTTMKMLTGLLPASEGTCALFGQPV---DASDMATRR 347
Cdd:cd03257 2 LEVKNLSVSFptggGSVKALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGKDLlklSRRLRKIRR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 348 R-VGYMSQ--AFSLYAELSVRQnLVLHARLFHLPADG---IPARVGEMLRRFDL-EKVADELPNDLPLGIRQRLSLAVAV 420
Cdd:cd03257 82 KeIQMVFQdpMSSLNPRMTIGE-QIAEPLRIHGKLSKkeaRKEAVLLLLVGVGLpEEVLNRYPHELSGGQRQRVAIARAL 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15600424 421 IHKPEILILDEPTSGVDPVARDGFWELMVELSRRDGVTIFISTHFMNEAQR-CDRISLMHAGKV 483
Cdd:cd03257 161 ALNPKLLIADEPTSALDVSVQAQILDLLKKLQEELGLTLLFITHDLGVVAKiADRVAVMYAGKI 224
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
283-495 |
2.00e-37 |
|
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: 141.63 E-value: 2.00e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 283 RFGDFVAVDHVSFRIERGEIFGFLGSNGCGKSTTMKMLTGLLPASEGTCALFGQPVDASDMAT-----RRRVGYMSQAFS 357
Cdd:cd03294 33 KTGQTVGVNDVSLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGKVLIDGQDIAAMSRKElrelrRKKISMVFQSFA 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 358 LYAELSVRQNLVLHARLFHLPADGIPARVGEMLRRFDLEKVADELPNDLPLGIRQRLSLAVAVIHKPEILILDEPTSGVD 437
Cdd:cd03294 113 LLPHRTVLENVAFGLEVQGVPRAEREERAAEALELVGLEGWEHKYPDELSGGMQQRVGLARALAVDPDILLMDEAFSALD 192
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 15600424 438 PVARDGFWELMVELSRRDGVTIFISTHFMNEAQRC-DRISLMHAGKVLASDTPDELVRQ 495
Cdd:cd03294 193 PLIRREMQDELLRLQAELQKTIVFITHDLDEALRLgDRIAIMKDGRLVQVGTPEEILTN 251
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
24-172 |
4.37e-37 |
|
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: 136.24 E-value: 4.37e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 24 VDDVSLEIPANRMVGLIGPDGVGKSSLLALLAGARKMQDGEIRVLDGDM--RDRRHRRAvcpRIAYMPQGLgkNLYPTLS 101
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDLtdDERKSLRK---EIGYVFQDP--QLFPRLT 75
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15600424 102 VFENVDFFGRLFGHDKAERERRIADLLQSTGLAPFAERPAGK----LSGGMKQKLGLCCALIHDPDLLILDEPTT 172
Cdd:pfam00005 76 VRENLRLGLLLKGLSKREKDARAEEALEKLGLGDLADRPVGErpgtLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
10-234 |
5.29e-37 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 142.90 E-value: 5.29e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 10 SLRGVSLRYGETRAVDDVSLEIPANRMVGLIGPDGVGKSSLLALLAGARKMQDGEIRvLDGdmRDRRHRRAVCPRIAYMP 89
Cdd:COG3839 5 ELENVSKSYGGVEALKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAGLEDPTSGEIL-IGG--RDVTDLPPKDRNIAMVF 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 90 QGLGknLYPTLSVFENVDFFGRLFGHDKAERERRIADLLQSTGLAPFAERPAGKLSGGMKQKLGLCCALIHDPDLLILDE 169
Cdd:COG3839 82 QSYA--LYPHMTVYENIAFPLKLRKVPKAEIDRRVREAAELLGLEDLLDRKPKQLSGGQRQRVALGRALVREPKVFLLDE 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15600424 170 PTTGVDPLSRnqfWELIGRIRA--GREGMSVLVATAYMEEAERF-DWLVAMDDGKVLATGTPQELRER 234
Cdd:COG3839 160 PLSNLDAKLR---VEMRAEIKRlhRRLGTTTIYVTHDQVEAMTLaDRIAVMNDGRIQQVGTPEELYDR 224
|
|
| GldA_ABC_ATP |
TIGR03522 |
gliding motility-associated ABC transporter ATP-binding subunit GldA; Members of this protein ... |
14-244 |
2.36e-36 |
|
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: 139.52 E-value: 2.36e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 14 VSLRYGETRAVDDVSLEIPANRMVGLIGPDGVGKSSLLALLAGARKMQDGEIRVLDGDMRdrRHRRAVCPRIAYMPQGlg 93
Cdd:TIGR03522 8 LTKLYGTQNALDEVSFEAQKGRIVGFLGPNGAGKSTTMKIITGYLPPDSGSVQVCGEDVL--QNPKEVQRNIGYLPEH-- 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 94 KNLYPTLSVFENVDFFGRLFGHDKAERERRIADLLQSTGLAPFAERPAGKLSGGMKQKLGLCCALIHDPDLLILDEPTTG 173
Cdd:TIGR03522 84 NPLYLDMYVREYLQFIAGIYGMKGQLLKQRVEEMIELVGLRPEQHKKIGQLSKGYRQRVGLAQALIHDPKVLILDEPTTG 163
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15600424 174 VDPlsrNQFWELIGRIRAGREGMSVLVATAYMEEAERF-DWLVAMDDGKVLATGTPQELRERTGTQSLESAF 244
Cdd:TIGR03522 164 LDP---NQLVEIRNVIKNIGKDKTIILSTHIMQEVEAIcDRVIIINKGKIVADKKLDELSAANKKQVIEVEF 232
|
|
| LPS_export_lptB |
TIGR04406 |
LPS export ABC transporter ATP-binding protein; Members of this fmaily are LptB, the ... |
277-493 |
3.12e-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: 3.12e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 277 AEGLTCRFGDFVAVDHVSFRIERGEIFGFLGSNGCGKSTTMKMLTGLLPASEGTCALFGQPVDASDMATRRR--VGYMSQ 354
Cdd:TIGR04406 4 AENLIKSYKKRKVVNDVSLSVKSGEIVGLLGPNGAGKTTSFYMIVGLVRPDAGKILIDGQDITHLPMHERARlgIGYLPQ 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 355 AFSLYAELSVRQNL--VLHARlFHLPADGIPARVGEMLRRFDLEKVADELPNDLPLGIRQRLSLAVAVIHKPEILILDEP 432
Cdd:TIGR04406 84 EASIFRKLTVEENImaVLEIR-KDLDRAEREERLEALLEEFQISHLRDNKAMSLSGGERRRVEIARALATNPKFILLDEP 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15600424 433 TSGVDPVARDGFWELMVELSRRdGVTIFISTHFMNEAQR-CDRISLMHAGKVLASDTPDELV 493
Cdd:TIGR04406 163 FAGVDPIAVGDIKKIIKHLKER-GIGVLITDHNVRETLDiCDRAYIISDGKVLAEGTPAEIV 223
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
275-492 |
3.59e-36 |
|
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of the LIV-I bacterial ABC-type two-component transport system that imports neutral, branched-chain amino acids. The E. coli branched-chain amino acid transporter comprises a heterodimer of ABC transporters (LivF and LivG), a heterodimer of six-helix TM domains (LivM and LivH), and one of two alternative soluble periplasmic substrate binding proteins (LivK or LivJ). ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules.
Pssm-ID: 213191 [Multi-domain] Cd Length: 222 Bit Score: 136.41 E-value: 3.59e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 275 IEAEGLTCRFGDFVAVDHVSFRIERGEIFGFLGSNGCGKSTTMKMLTGLLPASEGTCALFGQPVD--ASDMATRRRVGYM 352
Cdd:cd03224 1 LEVENLNAGYGKSQILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDGRDITglPPHERARAGIGYV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 353 SQAFSLYAELSVRQNLVLHArlFHLPADGIPARVGEMLRRF-DLEKVADELPNDLPLGIRQRLSLAVAVIHKPEILILDE 431
Cdd:cd03224 81 PEGRRIFPELTVEENLLLGA--YARRRAKRKARLERVYELFpRLKERRKQLAGTLSGGEQQMLAIARALMSRPKLLLLDE 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15600424 432 PTSGVDPVARDGFWELMVELsRRDGVTIFISTHFMNEAQR-CDRISLMHAGKVLASDTPDEL 492
Cdd:cd03224 159 PSEGLAPKIVEEIFEAIREL-RDEGVTILLVEQNARFALEiADRAYVLERGRVVLEGTAAEL 219
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
290-434 |
9.72e-36 |
|
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: 132.39 E-value: 9.72e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 290 VDHVSFRIERGEIFGFLGSNGCGKSTTMKMLTGLLPASEGTCALFGQPVDASDM-ATRRRVGYMSQAFSLYAELSVRQNL 368
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDLTDDERkSLRKEIGYVFQDPQLFPRLTVRENL 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 369 VLHARLFHLPADGIPARVGEMLRRFDLEKVADELPNDLPL----GIRQRLSLAVAVIHKPEILILDEPTS 434
Cdd:pfam00005 81 RLGLLLKGLSKREKDARAEEALEKLGLGDLADRPVGERPGtlsgGQRQRVAIARALLTKPKLLLLDEPTA 150
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
10-221 |
1.38e-35 |
|
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213179 [Multi-domain] Cd Length: 157 Bit Score: 132.37 E-value: 1.38e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 10 SLRGVSLRYGETRAVDDVSLEIPANRMVGLIGPDGVGKSSLLALLAGARKMQDGEIRVLD---GDMRDRRHRRavcpRIA 86
Cdd:cd00267 1 EIENLSFRYGGRTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGkdiAKLPLEELRR----RIG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 87 YMPQglgknlyptlsvfenvdffgrlfghdkaererriadllqstglapfaerpagkLSGGMKQKLGLCCALIHDPDLLI 166
Cdd:cd00267 77 YVPQ-----------------------------------------------------LSGGQRQRVALARALLLNPDLLL 103
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 15600424 167 LDEPTTGVDPLSRNQFWELIGRIRagREGMSVLVATAYMEEAERF-DWLVAMDDGK 221
Cdd:cd00267 104 LDEPTSGLDPASRERLLELLRELA--EEGRTVIIVTHDPELAELAaDRVIVLKDGK 157
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
275-486 |
1.71e-35 |
|
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: 132.17 E-value: 1.71e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 275 IEAEGLTCRFGDFVAVDHVSFRIERGEIFGFLGSNGCGKSTTMKMLTGLLPASEGTCALFGQPVDASD--MATRRRVGYM 352
Cdd:cd03216 1 LELRGITKRFGGVKALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVDGKEVSFASprDARRAGIAMV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 353 SQafslyaelsvrqnlvlharlfhlpadgiparvgemlrrfdlekvadelpndLPLGIRQRLSLAVAVIHKPEILILDEP 432
Cdd:cd03216 81 YQ---------------------------------------------------LSVGERQMVEIARALARNARLLILDEP 109
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 15600424 433 TSGVDPVARDGFWELMVELsRRDGVT-IFIStHFMNEAQR-CDRISLMHAGKVLAS 486
Cdd:cd03216 110 TAALTPAEVERLFKVIRRL-RAQGVAvIFIS-HRLDEVFEiADRVTVLRDGRVVGT 163
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
10-483 |
3.62e-35 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 141.08 E-value: 3.62e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 10 SLRGVSLRYGETRAVDDVSLEIPANRMVGLIGPDGVGKSSLLALLAGARKMQDGEIRVLDGDMRDRRHRRAVCPRIAYMP 89
Cdd:PRK09700 7 SMAGIGKSFGPVHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNINYNKLDHKLAAQLGIGIIY 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 90 QGLgkNLYPTLSVFENVdFFGRL-----FGH---DKAERERRIADLLQSTGLAPFAERPAGKLSGGMKQKLGLCCALIHD 161
Cdd:PRK09700 87 QEL--SVIDELTVLENL-YIGRHltkkvCGVniiDWREMRVRAAMMLLRVGLKVDLDEKVANLSISHKQMLEIAKTLMLD 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 162 PDLLILDEPTTGVDPLSRNQFWELIGRIRagREGMSVLVATAYMEEAERF-DWLVAMDDGKVLATGTPQE------LRER 234
Cdd:PRK09700 164 AKVIIMDEPTSSLTNKEVDYLFLIMNQLR--KEGTAIVYISHKLAEIRRIcDRYTVMKDGSSVCSGMVSDvsnddiVRLM 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 235 TGtQSLESAFIALLPESKRAGHhrlvipprpqsegapRIAIEAEGLTCRfgDFVAVDHVSFRIERGEIFGFLGSNGCGKS 314
Cdd:PRK09700 242 VG-RELQNRFNAMKENVSNLAH---------------ETVFEVRNVTSR--DRKKVRDISFSVCRGEILGFAGLVGSGRT 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 315 TTMKMLTGLLPASEGTCALFGQ------PVDA--SDMA----TRRRVGYmsqafslYAELSVRQNLvlhARLFHLPADGI 382
Cdd:PRK09700 304 ELMNCLFGVDKRAGGEIRLNGKdisprsPLDAvkKGMAyiteSRRDNGF-------FPNFSIAQNM---AISRSLKDGGY 373
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 383 PARVGeMLRRFDLEKVADELPNDLPL--------------GIRQRLSLAVAVIHKPEILILDEPTSGVDPVARDGFWELM 448
Cdd:PRK09700 374 KGAMG-LFHEVDEQRTAENQRELLALkchsvnqnitelsgGNQQKVLISKWLCCCPEVIIFDEPTRGIDVGAKAEIYKVM 452
|
490 500 510
....*....|....*....|....*....|....*
gi 15600424 449 VELSRRDGVTIFISTHFMNEAQRCDRISLMHAGKV 483
Cdd:PRK09700 453 RQLADDGKVILMVSSELPEIITVCDRIAVFCEGRL 487
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
10-236 |
5.21e-35 |
|
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: 141.43 E-value: 5.21e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 10 SLRGVSLRYGETR-AVDDVSLEIPANRMVGLIGPDGVGKSSLLALLAGARKMQDGEIRVLDGDMR--DRRHRRAvcpRIA 86
Cdd:COG4988 338 ELEDVSFSYPGGRpALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPPYSGSILINGVDLSdlDPASWRR---QIA 414
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 87 YMPQGlgknlyPTL---SVFENVdffgrLFGHDKAERERrIADLLQSTGLAPFAER-PAG----------KLSGGMKQKL 152
Cdd:COG4988 415 WVPQN------PYLfagTIRENL-----RLGRPDASDEE-LEAALEAAGLDEFVAAlPDGldtplgeggrGLSGGQAQRL 482
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 153 GLCCALIHDPDLLILDEPTTGVDPLSRNQFWELIGRIRAGRegmSVLVATAYMEEAERFDWLVAMDDGKVLATGTPQELR 232
Cdd:COG4988 483 ALARALLRDAPLLLLDEPTAHLDAETEAEILQALRRLAKGR---TVILITHRLALLAQADRILVLDDGRIVEQGTHEELL 559
|
....
gi 15600424 233 ERTG 236
Cdd:COG4988 560 AKNG 563
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
276-483 |
6.97e-35 |
|
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: 132.00 E-value: 6.97e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 276 EAEGLTCRFGDFV-AVDHVSFRIERGEIFGFLGSNGCGKSTTMKMLTGLLPASEGTCALFGQPVDASDMatRRRVGYMSQ 354
Cdd:cd03226 1 RIENISFSYKKGTeILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLNGKPIKAKER--RKSIGYVMQ 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 355 --AFSLYAElSVRQNLVLHARlfhlPADGIPARVGEMLRRFDLEKVADELPNDLPLGIRQRLSLAVAVIHKPEILILDEP 432
Cdd:cd03226 79 dvDYQLFTD-SVREELLLGLK----ELDAGNEQAETVLKDLDLYALKERHPLSLSGGQKQRLAIAAALLSGKDLLIFDEP 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 15600424 433 TSGVDPVARDGFWELMVELSRRdGVTIFISTH---FMneAQRCDRISLMHAGKV 483
Cdd:cd03226 154 TSGLDYKNMERVGELIRELAAQ-GKAVIVITHdyeFL--AKVCDRVLLLANGAI 204
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
275-483 |
1.37e-34 |
|
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: 131.61 E-value: 1.37e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 275 IEAEGLTCRFGDFVAVDHVSFRIERGEIFGFLGSNGCGKSTTMKMLTGLLPASEGTCALFGQpvDASDM-ATRRRVGYMS 353
Cdd:cd03301 1 VELENVTKRFGNVTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGR--DVTDLpPKDRDIAMVF 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 354 QAFSLYAELSVRQNLVLHARLFHLPADGIPARVGEMLRRFDLEKVADELPNDLPLGIRQRLSLAVAVIHKPEILILDEPT 433
Cdd:cd03301 79 QNYALYPHMTVYDNIAFGLKLRKVPKDEIDERVREVAELLQIEHLLDRKPKQLSGGQRQRVALGRAIVREPKVFLMDEPL 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 15600424 434 SGVDPVARDGFWELMVELSRRDGVTIFISTHFMNEAQR-CDRISLMHAGKV 483
Cdd:cd03301 159 SNLDAKLRVQMRAELKRLQQRLGTTTIYVTHDQVEAMTmADRIAVMNDGQI 209
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
10-235 |
2.69e-34 |
|
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: 131.85 E-value: 2.69e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 10 SLRGVSLRYGE----TRAVDDVSLEIPANRMVGLIGPDGVGKSSLLALLAGARKMQDGEIRVLDGDMRDRRhRRAVCPRI 85
Cdd:COG1124 3 EVRNLSVSYGQggrrVPVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVTFDGRPVTRRR-RKAFRRRV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 86 AYMPQglgknlYPTLSV--FENVDffgRLFG-----HDKAERERRIADLLQSTGLAP-FAERPAGKLSGGMKQKLGLCCA 157
Cdd:COG1124 82 QMVFQ------DPYASLhpRHTVD---RILAeplriHGLPDREERIAELLEQVGLPPsFLDRYPHQLSGGQRQRVAIARA 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15600424 158 LIHDPDLLILDEPTTGVDPLSRNQFWELIGRIRAgREGMSVLVATAYMEEAERF-DWLVAMDDGKVLATGTPQELRERT 235
Cdd:COG1124 153 LILEPELLLLDEPTSALDVSVQAEILNLLKDLRE-ERGLTYLFVSHDLAVVAHLcDRVAVMQNGRIVEELTVADLLAGP 230
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
10-242 |
2.71e-34 |
|
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: 131.65 E-value: 2.71e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 10 SLRGVSLRYGETR-AVDDVSLEIPANRMVGLIGPDGVGKSSLLALLAGARKMQDGEIRVLDGDMRDR---RHRRavcpRI 85
Cdd:cd03295 2 EFENVTKRYGGGKkAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGEDIREQdpvELRR----KI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 86 AYMPQGLGknLYPTLSVFENVDFFGRLFGHDKAERERRIADLLQSTGLAP--FAERPAGKLSGGMKQKLGLCCALIHDPD 163
Cdd:cd03295 78 GYVIQQIG--LFPHMTVEENIALVPKLLKWPKEKIRERADELLALVGLDPaeFADRYPHELSGGQQQRVGVARALAADPP 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 164 LLILDEPTTGVDPLSRNQFWELIGRIRagRE-GMSVLVATAYMEEAERF-DWLVAMDDGKVLATGTPQELRERTGTQSLE 241
Cdd:cd03295 156 LLLMDEPFGALDPITRDQLQEEFKRLQ--QElGKTIVFVTHDIDEAFRLaDRIAIMKNGEIVQVGTPDEILRSPANDFVA 233
|
.
gi 15600424 242 S 242
Cdd:cd03295 234 E 234
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
11-500 |
4.75e-34 |
|
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: 137.65 E-value: 4.75e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 11 LRGVSLRYGETRAVDDVSLEIPANRMVGLIGPDGVGKSSLLALLAGARK--MQDGEIRVLDGDMRDRRHRRAVCPRIAYM 88
Cdd:TIGR02633 4 MKGIVKTFGGVKALDGIDLEVRPGECVGLCGENGAGKSTLMKILSGVYPhgTWDGEIYWSGSPLKASNIRDTERAGIVII 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 89 PQGLgkNLYPTLSVFENVdFFGRLFGH-----DKAERERRIADLLQSTGL-APFAERPAGKLSGGMKQKLGLCCALIHDP 162
Cdd:TIGR02633 84 HQEL--TLVPELSVAENI-FLGNEITLpggrmAYNAMYLRAKNLLRELQLdADNVTRPVGDYGGGQQQLVEIAKALNKQA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 163 DLLILDEPTTGvdpLSRNQFWELIGRIR-AGREGMSVLVATAYMEEAERF-DWLVAMDDGKVLATGTPQELRE-RTGTQS 239
Cdd:TIGR02633 161 RLLILDEPSSS---LTEKETEILLDIIRdLKAHGVACVYISHKLNEVKAVcDTICVIRDGQHVATKDMSTMSEdDIITMM 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 240 LESAFIALLPEskraghhrlvippRPQSEGapRIAIEAEGLTCRFGD---FVAVDHVSFRIERGEIFGFLGSNGCGKSTT 316
Cdd:TIGR02633 238 VGREITSLYPH-------------EPHEIG--DVILEARNLTCWDVInphRKRVDDVSFSLRRGEILGVAGLVGAGRTEL 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 317 MKMLTGLLP-ASEGTCALFGQPVDASDMAT------------RRRVGYMSQafslyaeLSVRQNLVL-----HARLFHLP 378
Cdd:TIGR02633 303 VQALFGAYPgKFEGNVFINGKPVDIRNPAQairagiamvpedRKRHGIVPI-------LGVGKNITLsvlksFCFKMRID 375
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 379 ADGIPARVGEMLRRFDLEKVADELP-NDLPLGIRQRLSLAVAVIHKPEILILDEPTSGVDPVARDGFWELMVELSRRDGV 457
Cdd:TIGR02633 376 AAAELQIIGSAIQRLKVKTASPFLPiGRLSGGNQQKAVLAKMLLTNPRVLILDEPTRGVDVGAKYEIYKLINQLAQEGVA 455
|
490 500 510 520
....*....|....*....|....*....|....*....|...
gi 15600424 458 TIFISTHFMNEAQRCDRISLMHAGKVLASDTPDELVRQRGLPT 500
Cdd:TIGR02633 456 IIVVSSELAEVLGLSDRVLVIGEGKLKGDFVNHALTQEQVLAA 498
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
10-231 |
8.56e-34 |
|
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: 130.01 E-value: 8.56e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 10 SLRGVSLRYGETR----AVDDVSLEIPANRMVGLIGPDGVGKSSLLALLAGARKMQDGEIRVLDGDM-----RDRRHRRA 80
Cdd:cd03258 3 ELKNVSKVFGDTGgkvtALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGSVLVDGTDLtllsgKELRKARR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 81 vcpRIAYMPQGLgkNLYPTLSVFENVDFFGRLFGHDKAERERRIADLLQSTGLAPFAERPAGKLSGGMKQKLGLCCALIH 160
Cdd:cd03258 83 ---RIGMIFQHF--NLLSSRTVFENVALPLEIAGVPKAEIEERVLELLELVGLEDKADAYPAQLSGGQKQRVGIARALAN 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15600424 161 DPDLLILDEPTTGVDPLSRNQFWELIGRIRAgREGMSVLVATAYMEEAERFDWLVA-MDDGKVLATGTPQEL 231
Cdd:cd03258 158 NPKVLLCDEATSALDPETTQSILALLRDINR-ELGLTIVLITHEMEVVKRICDRVAvMEKGEVVEEGTVEEV 228
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
11-221 |
1.22e-33 |
|
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is comprised of all BPD (Binding Protein Dependent) systems that are largely represented in archaea and eubacteria and are primarily involved in scavenging solutes from the environment. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213196 [Multi-domain] Cd Length: 178 Bit Score: 127.30 E-value: 1.22e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 11 LRGVSLRYGETRAVDDVSLEIPANRMVGLIGPDGVGKSSLLALLAGARKMQDGEIRVLDGD-MRDRRHRRAVCPRIAYMP 89
Cdd:cd03229 3 LKNVSKRYGQKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGEDlTDLEDELPPLRRRIGMVF 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 90 QGLgkNLYPTLSVFENVDFfgrlfghdkaererriadllqstglapfaerpagKLSGGMKQKLGLCCALIHDPDLLILDE 169
Cdd:cd03229 83 QDF--ALFPHLTVLENIAL----------------------------------GLSGGQQQRVALARALAMDPDVLLLDE 126
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 15600424 170 PTTGVDPLSRNQFWELIGRIRAgREGMSVLVATAYMEEAERF-DWLVAMDDGK 221
Cdd:cd03229 127 PTSALDPITRREVRALLKSLQA-QLGITVVLVTHDLDEAARLaDRVVVLRDGK 178
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
10-226 |
2.19e-33 |
|
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: 128.39 E-value: 2.19e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 10 SLRGVSLRY----GETRAVDDVSLEIPANRMVGLIGPDGVGKSSLLALLAGARKMQDGEIRVLDGDM--RDRRHRRAVCP 83
Cdd:cd03257 3 EVKNLSVSFptggGSVKALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGKDLlkLSRRLRKIRRK 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 84 RIAYMPQGLGKNLYPTLSVFENVD--FFGRLFGHDKAERERRIADLLQSTGLAP-FAERPAGKLSGGMKQKLGLCCALIH 160
Cdd:cd03257 83 EIQMVFQDPMSSLNPRMTIGEQIAepLRIHGKLSKKEARKEAVLLLLVGVGLPEeVLNRYPHELSGGQRQRVAIARALAL 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15600424 161 DPDLLILDEPTTGVDPLSRNQFWELIGRIRAGReGMSVLVAT------AYMeeAERfdwLVAMDDGKVLATG 226
Cdd:cd03257 163 NPKLLIADEPTSALDVSVQAQILDLLKKLQEEL-GLTLLFIThdlgvvAKI--ADR---VAVMYAGKIVEEG 228
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
275-483 |
2.22e-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: 128.03 E-value: 2.22e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 275 IEAEGLTCRFGDFVAVDHVSFRIERGEIFGFLGSNGCGKSTTMKMLTGLLPASEGTCALFGQPVDASD---MATRRRVGY 351
Cdd:cd03262 1 IEIKNLHKSFGDFHVLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIDGLKLTDDKkniNELRQKVGM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 352 MSQAFSLYAELSVRQNLVLHAR-LFHLPADGIPARVGEMLRRFDLEKVADELPNDLPLGIRQRLSLAVAVIHKPEILILD 430
Cdd:cd03262 81 VFQQFNLFPHLTVLENITLAPIkVKGMSKAEAEERALELLEKVGLADKADAYPAQLSGGQQQRVAIARALAMNPKVMLFD 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 15600424 431 EPTSGVDPVARDGFWELMVELSrRDGVTIFISTHFMNEAQR-CDRISLMHAGKV 483
Cdd:cd03262 161 EPTSALDPELVGEVLDVMKDLA-EEGMTMVVVTHEMGFAREvADRVIFMDDGRI 213
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
10-234 |
4.76e-33 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 131.04 E-value: 4.76e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 10 SLRGVSLRYGETRAVDDVSLEIPANRMVGLIGPDGVGKSSLLALLAGARKMQDGEIrVLDG-------DMRDRRhrravc 82
Cdd:COG1118 4 EVRNISKRFGSFTLLDDVSLEIASGELVALLGPSGSGKTTLLRIIAGLETPDSGRI-VLNGrdlftnlPPRERR------ 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 83 prIAYMPQglgkN--LYPTLSVFENVDFFGRLFGHDKAERERRIADLLQSTGLAPFAERPAGKLSGGMKQKLGLCCALIH 160
Cdd:COG1118 77 --VGFVFQ----HyaLFPHMTVAENIAFGLRVRPPSKAEIRARVEELLELVQLEGLADRYPSQLSGGQRQRVALARALAV 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15600424 161 DPDLLILDEPTTGVDPLSRNQFWELIGRIRAGREGMSVLVaTAYMEEAERF-DWLVAMDDGKVLATGTPQELRER 234
Cdd:COG1118 151 EPEVLLLDEPFGALDAKVRKELRRWLRRLHDELGGTTVFV-THDQEEALELaDRVVVMNQGRIEQVGTPDEVYDR 224
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
245-498 |
5.64e-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: 136.50 E-value: 5.64e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 245 IALLPESKRAGHHRLvipPRPQSEGApriaIEAEGLTCRFGDFV--AVDHVSFRIERGEIFGFLGSNGCGKSTTMKMLTG 322
Cdd:COG2274 451 ILDLPPEREEGRSKL---SLPRLKGD----IELENVSFRYPGDSppVLDNISLTIKPGERVAIVGRSGSGKSTLLKLLLG 523
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 323 LLPASEGTCALFGQPVDASDMAT-RRRVGYMSQAFSLYAElSVRQNLvlhaRLFHLPADgiPARVGEMLRRFDLEKVADE 401
Cdd:COG2274 524 LYEPTSGRILIDGIDLRQIDPASlRRQIGVVLQDVFLFSG-TIRENI----TLGDPDAT--DEEIIEAARLAGLHDFIEA 596
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 402 LPN-----------DLPLGIRQRLSLAVAVIHKPEILILDEPTSGVDPVARDGFWELMVELSRrdGVTIFISTHFMNEAQ 470
Cdd:COG2274 597 LPMgydtvvgeggsNLSGGQRQRLAIARALLRNPRILILDEATSALDAETEAIILENLRRLLK--GRTVIIIAHRLSTIR 674
|
250 260
....*....|....*....|....*...
gi 15600424 471 RCDRISLMHAGKVLASDTPDELVRQRGL 498
Cdd:COG2274 675 LADRIIVLDKGRIVEDGTHEELLARKGL 702
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
275-492 |
7.37e-33 |
|
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: 127.30 E-value: 7.37e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 275 IEAEGLTCRFGD-FVAVDHVSFRIERGEIFGFLGSNGCGKSTTMKMLTGLLPASEGTCALFGQPV----DASDMATRRRV 349
Cdd:cd03256 1 IEVENLSKTYPNgKKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGTDInklkGKALRQLRRQI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 350 GYMSQAFSLYAELSVRQNlVLHARLFHLP-----------ADGIPARvgEMLRRFDLEKVADELPNDLPLGIRQRLSLAV 418
Cdd:cd03256 81 GMIFQQFNLIERLSVLEN-VLSGRLGRRStwrslfglfpkEEKQRAL--AALERVGLLDKAYQRADQLSGGQQQRVAIAR 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15600424 419 AVIHKPEILILDEPTSGVDPVARDGFWELMVELSRRDGVTIFISTHFMNEAQR-CDRISLMHAGKVLASDTPDEL 492
Cdd:cd03256 158 ALMQQPKLILADEPVASLDPASSRQVMDLLKRINREEGITVIVSLHQVDLAREyADRIVGLKDGRIVFDGPPAEL 232
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
10-483 |
8.62e-33 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 133.50 E-value: 8.62e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 10 SLRGVSLRYGETRAVDDVSLEIPANRMVGLIGPDGVGKSSLLALLAGARKMQDGEIRVLDGDMRDRRHRRAVCPRIAYMP 89
Cdd:PRK11288 6 SFDGIGKTFPGVKALDDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSILIDGQEMRFASTTAALAAGVAIIY 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 90 QGLgkNLYPTLSVFENVdFFGRL---FGH-DKAERERRIADLLQSTGLAPFAERPAGKLSGGMKQKLGLCCALIHDPDLL 165
Cdd:PRK11288 86 QEL--HLVPEMTVAENL-YLGQLphkGGIvNRRLLNYEAREQLEHLGVDIDPDTPLKYLSIGQRQMVEIAKALARNARVI 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 166 ILDEPTTGVDPLSRNQFWELIGRIRAgrEGMSVLVATAYMEEAERF-DWLVAMDDGKvlatgtpqelrertgtqslesaF 244
Cdd:PRK11288 163 AFDEPTSSLSAREIEQLFRVIRELRA--EGRVILYVSHRMEEIFALcDAITVFKDGR----------------------Y 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 245 IALLPESKRAGHHRLV-------------IPPRPQSEgaprIAIEAEGLTcrfGDFVAVDhVSFRIERGEIFGFLGSNGC 311
Cdd:PRK11288 219 VATFDDMAQVDRDQLVqamvgreigdiygYRPRPLGE----VRLRLDGLK---GPGLREP-ISFSVRAGEIVGLFGLVGA 290
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 312 GKSTTMKMLTGLLPASEGTCALFGQPVDASDMATRRRVGYM-----SQAFSLYAELSVRQNLVLHARLFHLPADGI--PA 384
Cdd:PRK11288 291 GRSELMKLLYGATRRTAGQVYLDGKPIDIRSPRDAIRAGIMlcpedRKAEGIIPVHSVADNINISARRHHLRAGCLinNR 370
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 385 RVGEMLRRF-DLEKV----ADELPNDLPLGIRQRLSLAVAVIHKPEILILDEPTSGVDPVARDGFWELMVELSRRdGVTI 459
Cdd:PRK11288 371 WEAENADRFiRSLNIktpsREQLIMNLSGGNQQKAILGRWLSEDMKVILLDEPTRGIDVGAKHEIYNVIYELAAQ-GVAV 449
|
490 500
....*....|....*....|....*
gi 15600424 460 -FISTHFMNEAQRCDRISLMHAGKV 483
Cdd:PRK11288 450 lFVSSDLPEVLGVADRIVVMREGRI 474
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
275-492 |
9.88e-33 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 129.81 E-value: 9.88e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 275 IEAEGLTCRF----GDFVAVDHVSFRIERGEIFGFLGSNGCGKSTTMKMLTGLLPASEGTCALFGQPV---DASDM-ATR 346
Cdd:COG1135 2 IELENLSKTFptkgGPVTALDDVSLTIEKGEIFGIIGYSGAGKSTLIRCINLLERPTSGSVLVDGVDLtalSERELrAAR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 347 RRVGYMSQAFSLYAELSVRQNLVLHARLFHLPADGIPARVGEMLRRFDLEKVADELPNDLPLGIRQRLSLAVAVIHKPEI 426
Cdd:COG1135 82 RKIGMIFQHFNLLSSRTVAENVALPLEIAGVPKAEIRKRVAELLELVGLSDKADAYPSQLSGGQKQRVGIARALANNPKV 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15600424 427 LILDEPTSGVDPVARDGFWELMVELSRRDGVTIFISTHFMNEAQR-CDRISLMHAGKVLASDTPDEL 492
Cdd:COG1135 162 LLCDEATSALDPETTRSILDLLKDINRELGLTIVLITHEMDVVRRiCDRVAVLENGRIVEQGPVLDV 228
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
289-489 |
1.05e-32 |
|
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim protein) in eukaryotes. It is the member of ABC transporter superfamily. Rim protein is a membrane glycoprotein which is localized in the photoreceptor outer segment discs. Mutation/s in its genetic loci is implicated in the recessive Stargardt's disease. [Transport and binding proteins, Other]
Pssm-ID: 130324 [Multi-domain] Cd Length: 2272 Bit Score: 137.84 E-value: 1.05e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 289 AVDHVSFRIERGEIFGFLGSNGCGKSTTMKMLTGLLPASEGTCALFGQPVDASDMATRRRVGYMSQAFSLYAELSVRQNL 368
Cdd:TIGR01257 945 AVDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGKDIETNLDAVRQSLGMCPQHNILFHHLTVAEHI 1024
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 369 VLHARLFHLPADGIPARVGEMLRRFDLEKVADELPNDLPLGIRQRLSLAVAVIHKPEILILDEPTSGVDPVARDGFWELM 448
Cdd:TIGR01257 1025 LFYAQLKGRSWEEAQLEMEAMLEDTGLHHKRNEEAQDLSGGMQRKLSVAIAFVGDAKVVVLDEPTSGVDPYSRRSIWDLL 1104
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 15600424 449 veLSRRDGVTIFISTHFMNEAQRC-DRISLMHAGKVLASDTP 489
Cdd:TIGR01257 1105 --LKYRSGRTIIMSTHHMDEADLLgDRIAIISQGRLYCSGTP 1144
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
274-505 |
1.21e-32 |
|
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: 127.12 E-value: 1.21e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 274 AIEAEGLTCRFGDFVAVDHVSFRIERGEIFGFLGSNGCGKSTTMKMLTGLLPASEG-TCALFGQPVDASDMAT-RRRVGY 351
Cdd:COG1119 3 LLELRNVTVRRGGKTILDDISWTVKPGEHWAILGPNGAGKSTLLSLITGDLPPTYGnDVRLFGERRGGEDVWElRKRIGL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 352 MSQAFSLY--AELSVRqNLVLHAR-----LFHLPADGIPARVGEMLRRFDLEKVADELPNDLPLGIRQRLSLAVAVIHKP 424
Cdd:COG1119 83 VSPALQLRfpRDETVL-DVVLSGFfdsigLYREPTDEQRERARELLELLGLAHLADRPFGTLSQGEQRRVLIARALVKDP 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 425 EILILDEPTSGVDPVARDGFWELMVELSRRDGVTIFISTHFMNEAQRC-DRISLMHAGKVLASDTPDELVRQrglPTLEA 503
Cdd:COG1119 162 ELLILDEPTAGLDLGARELLLALLDKLAAEGAPTLVLVTHHVEEIPPGiTHVLLLKDGRVVAAGPKEEVLTS---ENLSE 238
|
..
gi 15600424 504 TF 505
Cdd:COG1119 239 AF 240
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
8-231 |
1.48e-32 |
|
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: 126.74 E-value: 1.48e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 8 VASLRGVSLRYGETRAVDDVSLEIPANRMVGLIGPDGVGKSSLLALLAG-ARKMQDGEIRVLD-----GDMRDRRhrrav 81
Cdd:COG1119 3 LLELRNVTVRRGGKTILDDISWTVKPGEHWAILGPNGAGKSTLLSLITGdLPPTYGNDVRLFGerrggEDVWELR----- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 82 cPRIAYMPQGLGKNLYPTLSVFENV--DFFG--RLFGHDKAERERRIADLLQSTGLAPFAERPAGKLSGGMKQKLGLCCA 157
Cdd:COG1119 78 -KRIGLVSPALQLRFPRDETVLDVVlsGFFDsiGLYREPTDEQRERARELLELLGLAHLADRPFGTLSQGEQRRVLIARA 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15600424 158 LIHDPDLLILDEPTTGVDPLSRNQFWELIGRIrAGREGMSVLVATAYMEEA-ERFDWLVAMDDGKVLATGTPQEL 231
Cdd:COG1119 157 LVKDPELLILDEPTAGLDLGARELLLALLDKL-AAEGAPTLVLVTHHVEEIpPGITHVLLLKDGRVVAAGPKEEV 230
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
10-236 |
4.39e-32 |
|
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase domain [Defense mechanisms];
Pssm-ID: 441875 [Multi-domain] Cd Length: 711 Bit Score: 133.81 E-value: 4.39e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 10 SLRGVSLRYGETR--AVDDVSLEIPANRMVGLIGPDGVGKSSLLALLAGARKMQDGEIRVlDG-DMR--DRRHRRAvcpR 84
Cdd:COG2274 475 ELENVSFRYPGDSppVLDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEPTSGRILI-DGiDLRqiDPASLRR---Q 550
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 85 IAYMPQGlgknlyPTL---SVFENVdffgrLFGHDKAERERrIADLLQSTGLAPFAER-PAG----------KLSGGMKQ 150
Cdd:COG2274 551 IGVVLQD------VFLfsgTIRENI-----TLGDPDATDEE-IIEAARLAGLHDFIEAlPMGydtvvgeggsNLSGGQRQ 618
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 151 KLGLCCALIHDPDLLILDEPTTGVDPLSRNQFWELIGRIRAGRegmSVLVATAYMEEAERFDWLVAMDDGKVLATGTPQE 230
Cdd:COG2274 619 RLAIARALLRNPRILILDEATSALDAETEAIILENLRRLLKGR---TVIIIAHRLSTIRLADRIIVLDKGRIVEDGTHEE 695
|
....*.
gi 15600424 231 LRERTG 236
Cdd:COG2274 696 LLARKG 701
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
15-230 |
4.40e-32 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 125.51 E-value: 4.40e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 15 SLRYGETRAVDDVSLEIPANRMVGLIGPDGVGKSSLLALLAGARKMQDGEIRVLDGDMR---DRRHRRavcpRIAYMPQG 91
Cdd:PRK11231 9 TVGYGTKRILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDKPISmlsSRQLAR----RLALLPQH 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 92 LgknLYPT-LSVFENV--------DFFGRLFGHDKAererRIADLLQSTGLAPFAERPAGKLSGGMKQKLGLCCALIHDP 162
Cdd:PRK11231 85 H---LTPEgITVRELVaygrspwlSLWGRLSAEDNA----RVNQAMEQTRINHLADRRLTDLSGGQRQRAFLAMVLAQDT 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15600424 163 DLLILDEPTTGVDPLSRNQFWELIGRIRAgrEGMSVLVATAYMEEAERF-DWLVAMDDGKVLATGTPQE 230
Cdd:PRK11231 158 PVVLLDEPTTYLDINHQVELMRLMRELNT--QGKTVVTVLHDLNQASRYcDHLVVLANGHVMAQGTPEE 224
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
10-231 |
5.53e-32 |
|
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: 124.60 E-value: 5.53e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 10 SLRGVSLRYGETRAVDDVSLEIPANRMVGLIGPDGVGKSSLLALLAGARKMQ-----DGEIRVLDGDMRDRRHRRAVCPR 84
Cdd:cd03260 2 ELRDLNVYYGDKHALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRLNDLIpgapdEGEVLLDGKDIYDLDVDVLELRR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 85 IAYM----PqglgkNLYPtLSVFENVDFFGRLFG-HDKAERERRIADLLQSTGLAPFAERP--AGKLSGGMKQKLGLCCA 157
Cdd:cd03260 82 RVGMvfqkP-----NPFP-GSIYDNVAYGLRLHGiKLKEELDERVEEALRKAALWDEVKDRlhALGLSGGQQQRLCLARA 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15600424 158 LIHDPDLLILDEPTTGVDPLSRNQFWELIGRIragREGMSVLVATAYMEEAERF-DWLVAMDDGKVLATGTPQEL 231
Cdd:cd03260 156 LANEPEVLLLDEPTSALDPISTAKIEELIAEL---KKEYTIVIVTHNMQQAARVaDRTAFLLNGRLVEFGPTEQI 227
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
270-497 |
6.37e-32 |
|
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: 131.80 E-value: 6.37e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 270 APRIAIEAEGLTCRFGD-FVAVDHVSFRIERGEIFGFLGSNGCGKSTTMKMLTGLLPASEGTCALFGQPVDASDMAT-RR 347
Cdd:COG4988 332 AGPPSIELEDVSFSYPGgRPALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPPYSGSILINGVDLSDLDPASwRR 411
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 348 RVGYMSQAFSLYAElSVRQNLvlhaRLFHLPADgiPARVGEMLRRFDLEKVADELPNDL--PL---------GIRQRLSL 416
Cdd:COG4988 412 QIAWVPQNPYLFAG-TIRENL----RLGRPDAS--DEELEAALEAAGLDEFVAALPDGLdtPLgeggrglsgGQAQRLAL 484
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 417 AVAVIHKPEILILDEPTSGVDPVARDGFWELMVELSRrdGVTIFISTHFMNEAQRCDRISLMHAGKVLASDTPDELVRQR 496
Cdd:COG4988 485 ARALLRDAPLLLLDEPTAHLDAETEAEILQALRRLAK--GRTVILITHRLALLAQADRILVLDDGRIVEQGTHEELLAKN 562
|
.
gi 15600424 497 G 497
Cdd:COG4988 563 G 563
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
10-234 |
6.74e-32 |
|
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: 124.27 E-value: 6.74e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 10 SLRGVSLRYGETRAVDDVSLEIPANRMVGLIGPDGVGKSSLLALLAGARKMQDGEIRVLDGDMRD----RRHRRAVCPRI 85
Cdd:cd03300 2 ELENVSKFYGGFVALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGKDITNlpphKRPVNTVFQNY 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 86 AympqglgknLYPTLSVFENVDFFGRLFGHDKAERERRIADLLQSTGLAPFAERPAGKLSGGMKQKLGLCCALIHDPDLL 165
Cdd:cd03300 82 A---------LFPHLTVFENIAFGLRLKKLPKAEIKERVAEALDLVQLEGYANRKPSQLSGGQQQRVAIARALVNEPKVL 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 166 ILDEPTTGVDPLSRNQFWELIGRIRAgREGMSVLVATAYMEEAERF-DWLVAMDDGKVLATGTPQELRER 234
Cdd:cd03300 153 LLDEPLGALDLKLRKDMQLELKRLQK-ELGITFVFVTHDQEEALTMsDRIAVMNKGKIQQIGTPEEIYEE 221
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
10-208 |
6.99e-32 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 125.36 E-value: 6.99e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 10 SLRGVSLRYG----ETRAVDDVSLEIPANRMVGLIGPDGVGKSSLLALLAGARKMQDGEIRvLDGdmrdrrhrRAVcpri 85
Cdd:COG4525 5 TVRHVSVRYPgggqPQPALQDVSLTIESGEFVVALGASGCGKTTLLNLIAGFLAPSSGEIT-LDG--------VPV---- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 86 aympQGLGKN---------LYPTLSVFENVDFFGRLFGHDKAERERRIADLLQSTGLAPFAERPAGKLSGGMKQKLGLCC 156
Cdd:COG4525 72 ----TGPGADrgvvfqkdaLLPWLNVLDNVAFGLRLRGVPKAERRARAEELLALVGLADFARRRIWQLSGGMRQRVGIAR 147
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 15600424 157 ALIHDPDLLILDEPTTGVDPLSRNQFWELIGRIRAgREGMSVLVATAYMEEA 208
Cdd:COG4525 148 ALAADPRFLLMDEPFGALDALTREQMQELLLDVWQ-RTGKGVFLITHSVEEA 198
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
10-222 |
9.35e-32 |
|
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: 123.14 E-value: 9.35e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 10 SLRGVSLRYGE-TRAVDDVSLEIPANRMVGLIGPDGVGKSSLLALLAGARKMQDGEIRvLDGDMRDRRHRRAvcpRIAYM 88
Cdd:cd03226 1 RIENISFSYKKgTEILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSIL-LNGKPIKAKERRK---SIGYV 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 89 PQGLGKNLYpTLSVFENVdffgRLFGHDKAERERRIADLLQSTGLAPFAERPAGKLSGGMKQKLGLCCALIHDPDLLILD 168
Cdd:cd03226 77 MQDVDYQLF-TDSVREEL----LLGLKELDAGNEQAETVLKDLDLYALKERHPLSLSGGQKQRLAIAAALLSGKDLLIFD 151
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 15600424 169 EPTTGVDPLSRNQFWELIGRIRAgrEGMSVLVATAYMEEAERF-DWLVAMDDGKV 222
Cdd:cd03226 152 EPTSGLDYKNMERVGELIRELAA--QGKAVIVITHDYEFLAKVcDRVLLLANGAI 204
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
275-495 |
1.08e-31 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 125.13 E-value: 1.08e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 275 IEAEGLTCRFGDF--VAVDHVSFRIERGEIFGFLGSNGCGKSTTMKMLTGLLPASEGTCALFGQPVD-ASDMATRRRVGY 351
Cdd:PRK13635 6 IRVEHISFRYPDAatYALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGGMVLSeETVWDVRRQVGM 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 352 MSQ-AFSLYAELSVRQNLVlharlFHLPADGIP-----ARVGEMLRRFDLEKVADELPNDLPLGIRQRLSLAVAVIHKPE 425
Cdd:PRK13635 86 VFQnPDNQFVGATVQDDVA-----FGLENIGVPreemvERVDQALRQVGMEDFLNREPHRLSGGQKQRVAIAGVLALQPD 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 426 ILILDEPTSGVDPVARDGFWELMVELSRRDGVTIFISTHFMNEAQRCDRISLMHAGKVLASDTPDELVRQ 495
Cdd:PRK13635 161 IIILDEATSMLDPRGRREVLETVRQLKEQKGITVLSITHDLDEAAQADRVIVMNKGEILEEGTPEEIFKS 230
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
289-482 |
1.08e-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: 121.72 E-value: 1.08e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 289 AVDHVSFRIERGEIFGFLGSNGCGKSTTMKMLTGLLPASEGTCALFGQPVDASDMAT-RRRVGYMSQAFSLYAElSVRQN 367
Cdd:cd03228 17 VLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGVDLRDLDLESlRKNIAYVPQDPFLFSG-TIREN 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 368 LvlharlfhlpadgiparvgemlrrfdlekvadelpndLPLGIRQRLSLAVAVIHKPEILILDEPTSGVDPVARDGFWEL 447
Cdd:cd03228 96 I-------------------------------------LSGGQRQRIAIARALLRDPPILILDEATSALDPETEALILEA 138
|
170 180 190
....*....|....*....|....*....|....*
gi 15600424 448 MveLSRRDGVTIFISTHFMNEAQRCDRISLMHAGK 482
Cdd:cd03228 139 L--RALAKGKTVIVIAHRLSTIRDADRIIVLDDGR 171
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
260-497 |
1.56e-31 |
|
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease components [Energy production and conversion, Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 444011 [Multi-domain] Cd Length: 569 Bit Score: 130.66 E-value: 1.56e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 260 VIPPRPQSEGAPRIAIEAEGLTCRF--GDFVAVDHVSFRIERGEIFGFLGSNGCGKSTTMKMLTGLLPASEGTCALFGQP 337
Cdd:COG4987 319 VTEPAEPAPAPGGPSLELEDVSFRYpgAGRPVLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFLDPQSGSITLGGVD 398
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 338 VDASDMAT-RRRVGYMSQAFSLYAElSVRQNLVLhARlfhlpADGIPARVGEMLRRFDLEKVADELPN--DLPLGI---- 410
Cdd:COG4987 399 LRDLDEDDlRRRIAVVPQRPHLFDT-TLRENLRL-AR-----PDATDEELWAALERVGLGDWLAALPDglDTWLGEggrr 471
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 411 -----RQRLSLAVAVIHKPEILILDEPTSGVDPVARDGFWELMVELSRRDGVtIFIsTHFMNEAQRCDRISLMHAGKVLA 485
Cdd:COG4987 472 lsggeRRRLALARALLRDAPILLLDEPTEGLDAATEQALLADLLEALAGRTV-LLI-THRLAGLERMDRILVLEDGRIVE 549
|
250
....*....|..
gi 15600424 486 SDTPDELVRQRG 497
Cdd:COG4987 550 QGTHEELLAQNG 561
|
|
| galliderm_ABC |
TIGR03740 |
gallidermin-class lantibiotic protection ABC transporter, ATP-binding subunit; Model TIGR03731 ... |
12-209 |
1.71e-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: 122.89 E-value: 1.71e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 12 RGVSLRYGETRAVDDVSLEIPANRMVGLIGPDGVGKSSLLALLAGARKMQDGEIrVLDGDMRDRRHRRAVCPRIAYMPqg 91
Cdd:TIGR03740 4 KNLSKRFGKQTAVNNISLTVPKNSVYGLLGPNGAGKSTLLKMITGILRPTSGEI-IFDGHPWTRKDLHKIGSLIESPP-- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 92 lgknLYPTLSVFENVDFFGRLFGHDkaerERRIADLLQSTGLAPFAERPAGKLSGGMKQKLGLCCALIHDPDLLILDEPT 171
Cdd:TIGR03740 81 ----LYENLTARENLKVHTTLLGLP----DSRIDEVLNIVDLTNTGKKKAKQFSLGMKQRLGIAIALLNHPKLLILDEPT 152
|
170 180 190
....*....|....*....|....*....|....*...
gi 15600424 172 TGVDPLSRNQFWELIGRIRagREGMSVLVATAYMEEAE 209
Cdd:TIGR03740 153 NGLDPIGIQELRELIRSFP--EQGITVILSSHILSEVQ 188
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
10-221 |
1.91e-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: 120.95 E-value: 1.91e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 10 SLRGVSLRYGET--RAVDDVSLEIPANRMVGLIGPDGVGKSSLLALLAGARKMQDGEIRVLDGDMR--DRRHRRAvcpRI 85
Cdd:cd03228 2 EFKNVSFSYPGRpkPVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGVDLRdlDLESLRK---NI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 86 AYMPQGlgknlyPTL---SVFENVdffgrlfghdkaererriadllqstglapfaerpagkLSGGMKQKLGLCCALIHDP 162
Cdd:cd03228 79 AYVPQD------PFLfsgTIRENI-------------------------------------LSGGQRQRIAIARALLRDP 115
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 15600424 163 DLLILDEPTTGVDPLSRNQFWELIGRIRAGRegmSVLVATAYMEEAERFDWLVAMDDGK 221
Cdd:cd03228 116 PILILDEATSALDPETEALILEALRALAKGK---TVIVIAHRLSTIRDADRIIVLDDGR 171
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
9-238 |
2.24e-31 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 125.58 E-value: 2.24e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 9 ASLRG-VSLRYGETRAVDDVSLEIPANRMVGLIGPDGVGKSSLLALLAGARKMQDGEIRVLDgdMRDRRHRRAVCPRIAY 87
Cdd:COG4586 22 GALKGlFRREYREVEAVDDISFTIEPGEIVGFIGPNGAGKSTTIKMLTGILVPTSGEVRVLG--YVPFKRRKEFARRIGV 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 88 -MPQglgKN-LYPTLSVFENVDFFGRLFGHDKAERERRIADLLQSTGLAPFAERPAGKLSGGMKQKLGLCCALIHDPDLL 165
Cdd:COG4586 100 vFGQ---RSqLWWDLPAIDSFRLLKAIYRIPDAEYKKRLDELVELLDLGELLDTPVRQLSLGQRMRCELAAALLHRPKIL 176
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15600424 166 ILDEPTTGVDPLSRNQFWELIGRIRAgREGMSVLVATAYMEEAERF-DWLVAMDDGKVLATGTPQELRERTGTQ 238
Cdd:COG4586 177 FLDEPTIGLDVVSKEAIREFLKEYNR-ERGTTILLTSHDMDDIEALcDRVIVIDHGRIIYDGSLEELKERFGPY 249
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
288-495 |
3.05e-31 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 124.04 E-value: 3.05e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 288 VAVDHVSFRIERGEIFGFLGSNGCGKSTTMKMLTGLLPASEGTCALFGqpVDASDMAT----RRRVGYMSQA--FSLYAE 361
Cdd:PRK13633 24 LALDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVYVDG--LDTSDEENlwdiRNKAGMVFQNpdNQIVAT 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 362 LsVRQNLVLHARLFHLPADGIPARVGEMLRRFDLEKVADELPNDLPLGIRQRLSLAVAVIHKPEILILDEPTSGVDPVAR 441
Cdd:PRK13633 102 I-VEEDVAFGPENLGIPPEEIRERVDESLKKVGMYEYRRHAPHLLSGGQKQRVAIAGILAMRPECIIFDEPTAMLDPSGR 180
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 15600424 442 DGFWELMVELSRRDGVTIFISTHFMNEAQRCDRISLMHAGKVLASDTPDELVRQ 495
Cdd:PRK13633 181 REVVNTIKELNKKYGITIILITHYMEEAVEADRIIVMDSGKVVMEGTPKEIFKE 234
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
283-495 |
3.61e-31 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 122.50 E-value: 3.61e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 283 RFGDFVAVDHVSFRIERGEIFGFLGSNGCGKSTTMKMLTGLLPASEGTCalfgqpvdasdmatrRRVGYMSQAFSL---- 358
Cdd:COG1134 35 RREEFWALKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTSGRV---------------EVNGRVSALLELgagf 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 359 YAELSVRQNLVLHARLFHLPADgiparvgEMLRRFDleKVAD--ELPN--DLPL-----GIRQRLSLAVAVIHKPEILIL 429
Cdd:COG1134 100 HPELTGRENIYLNGRLLGLSRK-------EIDEKFD--EIVEfaELGDfiDQPVktyssGMRARLAFAVATAVDPDILLV 170
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15600424 430 DEPTSGVDPVARDGFWELMVELsRRDGVTIFISTHFMNEAQR-CDRISLMHAGKVLASDTPDELVRQ 495
Cdd:COG1134 171 DEVLAVGDAAFQKKCLARIREL-RESGRTVIFVSHSMGAVRRlCDRAIWLEKGRLVMDGDPEEVIAA 236
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
5-236 |
9.65e-31 |
|
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease components [Energy production and conversion, Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 444011 [Multi-domain] Cd Length: 569 Bit Score: 128.35 E-value: 9.65e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 5 GSGVASLRGVSLRY-GETRAV-DDVSLEIPANRMVGLIGPDGVGKSSLLALLAGARKMQDGEIRVLDGDMR--DRRHRRA 80
Cdd:COG4987 330 GGPSLELEDVSFRYpGAGRPVlDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFLDPQSGSITLGGVDLRdlDEDDLRR 409
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 81 vcpRIAYMPQGlgknlyPTL---SVFENVdffgrLFGHDKAErERRIADLLQSTGLAPFAER-PAG----------KLSG 146
Cdd:COG4987 410 ---RIAVVPQR------PHLfdtTLRENL-----RLARPDAT-DEELWAALERVGLGDWLAAlPDGldtwlgeggrRLSG 474
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 147 GMKQKLGLCCALIHDPDLLILDEPTTGVDPLSRNQFWELIGRIRAGRegmSVLVATAYMEEAERFDWLVAMDDGKVLATG 226
Cdd:COG4987 475 GERRRLALARALLRDAPILLLDEPTEGLDAATEQALLADLLEALAGR---TVLLITHRLAGLERMDRILVLEDGRIVEQG 551
|
250
....*....|
gi 15600424 227 TPQELRERTG 236
Cdd:COG4987 552 THEELLAQNG 561
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
3-483 |
1.05e-30 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 127.47 E-value: 1.05e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 3 AGGSGVASLRGVSLRYGETRAVDDVSLEIPANRMVGLIGPDGVGKSSLLALLAGARKMQDGEIRVldgdmrDRRHRRAVC 82
Cdd:PRK15439 6 TTAPPLLCARSISKQYSGVEVLKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEI------GGNPCARLT 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 83 PRIAY------MPQGlgKNLYPTLSVFENVdffgrLFGHDK-AERERRIADLLQSTGLAPFAERPAGKLSGGMKQKLGLC 155
Cdd:PRK15439 80 PAKAHqlgiylVPQE--PLLFPNLSVKENI-----LFGLPKrQASMQKMKQLLAALGCQLDLDSSAGSLEVADRQIVEIL 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 156 CALIHDPDLLILDEPTTGVDPLSRNQfweLIGRIRAGR-EGMSVLVATAYMEEAERF-DWLVAMDDGKVLATGTPQELRE 233
Cdd:PRK15439 153 RGLMRDSRILILDEPTASLTPAETER---LFSRIRELLaQGVGIVFISHKLPEIRQLaDRISVMRDGTIALSGKTADLST 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 234 RTGTQSLESAFIAL-LPESKR-----AGHHRLvipprpQSEGAPRIAIE---AEGltcrfgdFVavdHVSFRIERGEIFG 304
Cdd:PRK15439 230 DDIIQAITPAAREKsLSASQKlwlelPGNRRQ------QAAGAPVLTVEdltGEG-------FR---NISLEVRAGEILG 293
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 305 FLGSNGCGKSTTMKMLTGLLPASEGTCALFGQPVDASDMATRRRVG--YMS---QAFSLYAELSVRQNLVlhARLFHLPA 379
Cdd:PRK15439 294 LAGVVGAGRTELAETLYGLRPARGGRIMLNGKEINALSTAQRLARGlvYLPedrQSSGLYLDAPLAWNVC--ALTHNRRG 371
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 380 DGI-PARVGEMLRRF---------DLEKVADELPNdlplGIRQRLSLAVAVIHKPEILILDEPTSGVDPVARDGFWELMV 449
Cdd:PRK15439 372 FWIkPARENAVLERYrralnikfnHAEQAARTLSG----GNQQKVLIAKCLEASPQLLIVDEPTRGVDVSARNDIYQLIR 447
|
490 500 510
....*....|....*....|....*....|....
gi 15600424 450 ELSRRDGVTIFISTHFMNEAQRCDRISLMHAGKV 483
Cdd:PRK15439 448 SIAAQNVAVLFISSDLEEIEQMADRVLVMHQGEI 481
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
266-492 |
1.21e-30 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 121.68 E-value: 1.21e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 266 QSEGAPRIAIEAEGLTCRFGDFVAVDHVSFRIERGEIFGFLGSNGCGKSTTMKML---TGLLPAS--EGTCALFGQPVDA 340
Cdd:COG1117 3 APASTLEPKIEVRNLNVYYGDKQALKDINLDIPENKVTALIGPSGCGKSTLLRCLnrmNDLIPGArvEGEILLDGEDIYD 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 341 SDM---ATRRRVGYMSQ---AFSlyaeLSVRQNLVLHARLFHLPADG-IPARVGEMLRRFDL-EKVADEL---PNDLPLG 409
Cdd:COG1117 83 PDVdvvELRRRVGMVFQkpnPFP----KSIYDNVAYGLRLHGIKSKSeLDEIVEESLRKAALwDEVKDRLkksALGLSGG 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 410 IRQRLSLAVAVIHKPEILILDEPTSGVDPVARDGFWELMVELSRRdgVTIFISTHFMNEAQRC-DRISLMHAGKVLASDT 488
Cdd:COG1117 159 QQQRLCIARALAVEPEVLLMDEPTSALDPISTAKIEELILELKKD--YTIVIVTHNMQQAARVsDYTAFFYLGELVEFGP 236
|
....
gi 15600424 489 PDEL 492
Cdd:COG1117 237 TEQI 240
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
10-235 |
1.40e-30 |
|
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440743 [Multi-domain] Cd Length: 239 Bit Score: 120.87 E-value: 1.40e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 10 SLRGVSLRYGETRAVDDVSLEIPANRMVGLIGPDGVGKSSLLALLAGARKMQDGEIRVLDGDM-RDRRHRRAVCPRIAYM 88
Cdd:COG1126 3 EIENLHKSFGDLEVLKGISLDVEKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTITVDGEDLtDSKKDINKLRRKVGMV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 89 PQGLgkNLYPTLSVFENVdFFG--RLFGHDKAERERRIADLLQSTGLAPFAERPAGKLSGGMKQKLGLCCALIHDPDLLI 166
Cdd:COG1126 83 FQQF--NLFPHLTVLENV-TLApiKVKKMSKAEAEERAMELLERVGLADKADAYPAQLSGGQQQRVAIARALAMEPKVML 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 167 LDEPTTGVDPlsrnqfwELIGRI-----RAGREGMSVLVATAYMEEAER-FDWLVAMDDGKVLATGTPQEL-----RERT 235
Cdd:COG1126 160 FDEPTSALDP-------ELVGEVldvmrDLAKEGMTMVVVTHEMGFAREvADRVVFMDGGRIVEEGPPEEFfenpqHERT 232
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
273-491 |
1.44e-30 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 121.42 E-value: 1.44e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 273 IAIEAEGLTCRFGDFVAVDHVSFRIERGEIFGFLGSNGCGKSTTMKMLTGLLPASEGTCALFGQPVD---ASDMATRRRV 349
Cdd:PRK13548 1 AMLEARNLSVRLGGRTLLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLNGRPLAdwsPAELARRRAV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 350 gyMSQAFSLYAELSVRQnLVLHARLFH-LPADGIPARVGEMLRRFDLEKVADELPNDLPLGIRQRLSLA-V-----AVIH 422
Cdd:PRK13548 81 --LPQHSSLSFPFTVEE-VVAMGRAPHgLSRAEDDALVAAALAQVDLAHLAGRDYPQLSGGEQQRVQLArVlaqlwEPDG 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15600424 423 KPEILILDEPTSGVDP--------VARdgfwelmvELSRRDGVTIFISTHFMNEAQR-CDRISLMHAGKVLASDTPDE 491
Cdd:PRK13548 158 PPRWLLLDEPTSALDLahqhhvlrLAR--------QLAHERGLAVIVVLHDLNLAARyADRIVLLHQGRLVADGTPAE 227
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
10-260 |
1.50e-30 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 123.65 E-value: 1.50e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 10 SLRGVSLRY----GETRAVDDVSLEIPANRMVGLIGPDGVGKSSLLALLAGARKMQDGEIRVLDGDMRD------RRHRR 79
Cdd:COG1135 3 ELENLSKTFptkgGPVTALDDVSLTIEKGEIFGIIGYSGAGKSTLIRCINLLERPTSGSVLVDGVDLTAlserelRAARR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 80 avcpRIAYMPQGLgkNLYPTLSVFENVDFFGRLFGHDKAERERRIADLLQSTGLAPFAER-PAgKLSGGMKQKLGLCCAL 158
Cdd:COG1135 83 ----KIGMIFQHF--NLLSSRTVAENVALPLEIAGVPKAEIRKRVAELLELVGLSDKADAyPS-QLSGGQKQRVGIARAL 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 159 IHDPDLLILDEPTTGVDPLSRNQFWELIGRIRAgREGMSVLVATAYMEE----AERfdwlVA-MDDGKVLATGTPQEL-- 231
Cdd:COG1135 156 ANNPKVLLCDEATSALDPETTRSILDLLKDINR-ELGLTIVLITHEMDVvrriCDR----VAvLENGRIVEQGPVLDVfa 230
|
250 260 270
....*....|....*....|....*....|....*..
gi 15600424 232 --RERTGTQSLESAFIALLPES------KRAGHHRLV 260
Cdd:COG1135 231 npQSELTRRFLPTVLNDELPEEllarlrEAAGGGRLV 267
|
|
| COG4559 |
COG4559 |
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism]; |
275-505 |
1.75e-30 |
|
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443620 [Multi-domain] Cd Length: 258 Bit Score: 120.99 E-value: 1.75e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 275 IEAEGLTCRFGDFVAVDHVSFRIERGEIFGFLGSNGCGKSTTMKMLTGLLPASEGTCALFGQPVDA---SDMATRRRVgy 351
Cdd:COG4559 2 LEAENLSVRLGGRTLLDDVSLTLRPGELTAIIGPNGAGKSTLLKLLTGELTPSSGEVRLNGRPLAAwspWELARRRAV-- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 352 MSQAFSLYAELSVRQnLVLHARLFH-LPADGIPARVGEMLRRFDLEKVADELPNDLPLGIRQRLSLA--VAVIHKPE--- 425
Cdd:COG4559 80 LPQHSSLAFPFTVEE-VVALGRAPHgSSAAQDRQIVREALALVGLAHLAGRSYQTLSGGEQQRVQLArvLAQLWEPVdgg 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 426 --ILILDEPTSGVDPVARDGFWELMVELSRRdGVTIFISTHFMN-EAQRCDRISLMHAGKVLASDTPDELVRQrglPTLE 502
Cdd:COG4559 159 prWLFLDEPTSALDLAHQHAVLRLARQLARR-GGGVVAVLHDLNlAAQYADRILLLHQGRLVAQGTPEEVLTD---ELLE 234
|
...
gi 15600424 503 ATF 505
Cdd:COG4559 235 RVY 237
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
17-231 |
3.15e-30 |
|
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: 120.83 E-value: 3.15e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 17 RYGETRAVDDVSLEIPANRMVGLIGPDGVGKSSLLALLAGARKMQDGEIrVLDGD----MRDRRHRRAVCPRIAYMPQGL 92
Cdd:cd03294 33 KTGQTVGVNDVSLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGKV-LIDGQdiaaMSRKELRELRRKKISMVFQSF 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 93 GknLYPTLSVFENVDFFGRLFGHDKAERERRIADLLQSTGLAPFAERPAGKLSGGMKQKLGLCCALIHDPDLLILDEPTT 172
Cdd:cd03294 112 A--LLPHRTVLENVAFGLEVQGVPRAEREERAAEALELVGLEGWEHKYPDELSGGMQQRVGLARALAVDPDILLMDEAFS 189
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 173 GVDPLSRNQFWELIGRIRAGREGMSVLVaTAYMEEAERF-DWLVAMDDGKVLATGTPQEL 231
Cdd:cd03294 190 ALDPLIRREMQDELLRLQAELQKTIVFI-THDLDEALRLgDRIAIMKDGRLVQVGTPEEI 248
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
10-222 |
3.60e-30 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 118.77 E-value: 3.60e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 10 SLRGVSLRYGETRAVDDVSLEIPANRMVGLIGPDGVGKSSLLALLAGARKMQDGEIRvLDGDMRDR----RHRRavcpRI 85
Cdd:COG4619 2 ELEGLSFRVGGKPILSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIY-LDGKPLSAmpppEWRR----QV 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 86 AYMPQglgknlYPTL---SVFENVDFfGRLFGHDKAERERrIADLLQSTGLAP-FAERPAGKLSGGMKQKLGLCCALIHD 161
Cdd:COG4619 77 AYVPQ------EPALwggTVRDNLPF-PFQLRERKFDRER-ALELLERLGLPPdILDKPVERLSGGERQRLALIRALLLQ 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15600424 162 PDLLILDEPTTGVDPLSRNQFWELIGRIRAgREGMSVLVATAYMEEAERF-DWLVAMDDGKV 222
Cdd:COG4619 149 PDVLLLDEPTSALDPENTRRVEELLREYLA-EEGRAVLWVSHDPEQIERVaDRVLTLEAGRL 209
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
10-231 |
4.83e-30 |
|
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: 119.18 E-value: 4.83e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 10 SLRGVSLRYGETRAVDDVSLEIPANRMVGLIGPDGVGKSSLLALLAGARKMQDGEIRVLDGDM-RDRRHRRAvcpR--IA 86
Cdd:cd03218 2 RAENLSKRYGKRKVVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDGQDItKLPMHKRA---RlgIG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 87 YMPQGlgKNLYPTLSVFENVDFFGRLFGHDKAERERRIADLLQSTGLAPFAERPAGKLSGGMKQKLGLCCALIHDPDLLI 166
Cdd:cd03218 79 YLPQE--ASIFRKLTVEENILAVLEIRGLSKKEREEKLEELLEEFHITHLRKSKASSLSGGERRRVEIARALATNPKFLL 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15600424 167 LDEPTTGVDPLSRNQFWELIGRIRAgrEGMSVL------------VATAYMeeaerfdwlvaMDDGKVLATGTPQEL 231
Cdd:cd03218 157 LDEPFAGVDPIAVQDIQKIIKILKD--RGIGVLitdhnvretlsiTDRAYI-----------IYEGKVLAEGTPEEI 220
|
|
| potA |
TIGR01187 |
spermidine/putrescine ABC transporter ATP-binding subunit; This model describes spermidine ... |
306-492 |
5.50e-30 |
|
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: 121.45 E-value: 5.50e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 306 LGSNGCGKSTTMKMLTGLLPASEGTCALFGqpVDASDMATRRR-VGYMSQAFSLYAELSVRQNLVLHARLFHLPADGIPA 384
Cdd:TIGR01187 2 LGPSGCGKTTLLRLLAGFEQPDSGSIMLDG--EDVTNVPPHLRhINMVFQSYALFPHMTVEENVAFGLKMRKVPRAEIKP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 385 RVGEMLRRFDLEKVADELPNDLPLGIRQRLSLAVAVIHKPEILILDEPTSGVDPVARDGFWELMVELSRRDGVTIFISTH 464
Cdd:TIGR01187 80 RVLEALRLVQLEEFADRKPHQLSGGQQQRVALARALVFKPKILLLDEPLSALDKKLRDQMQLELKTIQEQLGITFVFVTH 159
|
170 180
....*....|....*....|....*....
gi 15600424 465 FMNEA-QRCDRISLMHAGKVLASDTPDEL 492
Cdd:TIGR01187 160 DQEEAmTMSDRIAIMRKGKIAQIGTPEEI 188
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
1-241 |
5.78e-30 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 122.15 E-value: 5.78e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 1 MTAGGSGVASLRGVSLRYGETRAVDDVSLEIPANRMVGLIGPDGVgkssllallAGARKMQDGEIRVLDGDMRDRR---- 76
Cdd:NF000106 6 ISNGARNAVEVRGLVKHFGEVKAVDGVDLDVREGTVLGVLGP*GA---------A**RGALPAHV*GPDAGRRPWRf*tw 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 77 --HRRAVCPRIA-YMPQGLGKNlyPTLSVFENVDFFGRLFGHDKAERERRIADLLQSTGLAPFAERPAGKLSGGMKQKLG 153
Cdd:NF000106 77 caNRRALRRTIG*HRPVR*GRR--ESFSGRENLYMIGR*LDLSRKDARARADELLERFSLTEAAGRAAAKYSGGMRRRLD 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 154 LCCALIHDPDLLILDEPTTGVDPLSRNQFWELIGRIRagREGMSVLVATAYMEEAERF-DWLVAMDDGKVLATGTPQELR 232
Cdd:NF000106 155 LAASMIGRPAVLYLDEPTTGLDPRTRNEVWDEVRSMV--RDGATVLLTTQYMEEAEQLaHELTVIDRGRVIADGKVDELK 232
|
....*....
gi 15600424 233 ERTGTQSLE 241
Cdd:NF000106 233 TKVGGRTLQ 241
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
12-237 |
8.46e-30 |
|
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: 118.60 E-value: 8.46e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 12 RGVSLRYGETRAVDDVSLEIPANRMVGLIGPDGVGKSSLLALLAGARKMQDGEI-----RVLDGDMRDRrhrravcpRIA 86
Cdd:cd03296 6 RNVSKRFGDFVALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTIlfggeDATDVPVQER--------NVG 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 87 YMPQGLGknLYPTLSVFENVDfFG-----RLFGHDKAERERRIADLLQSTGLAPFAERPAGKLSGGMKQKLGLCCALIHD 161
Cdd:cd03296 78 FVFQHYA--LFRHMTVFDNVA-FGlrvkpRSERPPEAEIRAKVHELLKLVQLDWLADRYPAQLSGGQRQRVALARALAVE 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15600424 162 PDLLILDEPTTGVDPLSRNQFWELIGRIRAGREGMSVLVATAYMEEAERFDWLVAMDDGKVLATGTPQELRERTGT 237
Cdd:cd03296 155 PKVLLLDEPFGALDAKVRKELRRWLRRLHDELHVTTVFVTHDQEEALEVADRVVVMNKGRIEQVGTPDEVYDHPAS 230
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
288-502 |
1.23e-29 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 119.38 E-value: 1.23e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 288 VAVDHVSFRIERGEIFGFLGSNGCGKSTTMKMLTGLLPASEGTCALFG-----QPVDASDMatRRRVGYMSQ--AFSLYA 360
Cdd:PRK13637 21 KALDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDGvditdKKVKLSDI--RKKVGLVFQypEYQLFE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 361 ElSVRQNLVLHARLFHLPADGIPARVGEMLR--RFDLEKVADELPNDLPLGIRQRLSLAVAVIHKPEILILDEPTSGVDP 438
Cdd:PRK13637 99 E-TIEKDIAFGPINLGLSEEEIENRVKRAMNivGLDYEDYKDKSPFELSGGQKRRVAIAGVVAMEPKILILDEPTAGLDP 177
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15600424 439 VARDGFWELMVELSRRDGVTIFISTHFMNE-AQRCDRISLMHAGKVLASDTPDELVRQrgLPTLE 502
Cdd:PRK13637 178 KGRDEILNKIKELHKEYNMTIILVSHSMEDvAKLADRIIVMNKGKCELQGTPREVFKE--VETLE 240
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
275-495 |
1.43e-29 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 119.03 E-value: 1.43e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 275 IEAEGLTCRFGD-FVAVDHVSFRIERGEIFGFLGSNGCGKSTTMKMLTGLLPASEGTCALFGQPVD---ASDMATRRRVG 350
Cdd:PRK13639 2 LETRDLKYSYPDgTEALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIKGEPIKydkKSLLEVRKTVG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 351 YMSQA--FSLYAElSVRQNLVLHARLFHLPADGIPARVGEMLRRFDLEKVADELPNDLPLGIRQRLSLAVAVIHKPEILI 428
Cdd:PRK13639 82 IVFQNpdDQLFAP-TVEEDVAFGPLNLGLSKEEVEKRVKEALKAVGMEGFENKPPHHLSGGQKKRVAIAGILAMKPEIIV 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15600424 429 LDEPTSGVDPVARDGFWELMVELSRRdGVTIFISTHFMNEAQR-CDRISLMHAGKVLASDTPDELVRQ 495
Cdd:PRK13639 161 LDEPTSGLDPMGASQIMKLLYDLNKE-GITIIISTHDVDLVPVyADKVYVMSDGKIIKEGTPKEVFSD 227
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
26-226 |
2.41e-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: 116.24 E-value: 2.41e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 26 DVSLEIPANRmVGLIGPDGVGKSSLLALLAGARKMQDGEIRVLDGDMRDRR-------HRRavcpRIAYMPQGLGknLYP 98
Cdd:cd03297 16 KIDFDLNEEV-TGIFGASGAGKSTLLRCIAGLEKPDGGTIVLNGTVLFDSRkkinlppQQR----KIGLVFQQYA--LFP 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 99 TLSVFENVDFfgRLFGHDKAERERRIADLLQSTGLAPFAERPAGKLSGGMKQKLGLCCALIHDPDLLILDEPTTGVDPLS 178
Cdd:cd03297 89 HLNVRENLAF--GLKRKRNREDRISVDELLDLLGLDHLLNRYPAQLSGGEKQRVALARALAAQPELLLLDEPFSALDRAL 166
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 15600424 179 RNQFWELIGRIRAgREGMSVLVATAYMEEAERF-DWLVAMDDGKVLATG 226
Cdd:cd03297 167 RLQLLPELKQIKK-NLNIPVIFVTHDLSEAEYLaDRIVVMEDGRLQYIG 214
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
283-487 |
3.43e-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: 115.86 E-value: 3.43e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 283 RFGDFVAvdHVSFRIErGEIFGFLGSNGCGKSTTMKMLTGLLPASEGTCALFGQPVDASDMA-----TRRRVGYMSQAFS 357
Cdd:cd03297 9 RLPDFTL--KIDFDLN-EEVTGIFGASGAGKSTLLRCIAGLEKPDGGTIVLNGTVLFDSRKKinlppQQRKIGLVFQQYA 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 358 LYAELSVRQNLVLHARLFHLPADGIpaRVGEMLRRFDLEKVADELPNDLPLGIRQRLSLAVAVIHKPEILILDEPTSGVD 437
Cdd:cd03297 86 LFPHLNVRENLAFGLKRKRNREDRI--SVDELLDLLGLDHLLNRYPAQLSGGEKQRVALARALAAQPELLLLDEPFSALD 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 15600424 438 PVARDgfwELMVELSRR----DGVTIFIsTHFMNEAQR-CDRISLMHAGKVLASD 487
Cdd:cd03297 164 RALRL---QLLPELKQIkknlNIPVIFV-THDLSEAEYlADRIVVMEDGRLQYIG 214
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
15-277 |
3.55e-29 |
|
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding cassette (ABC) protein of the three subunit molybdate ABC transporter. The three proteins of this complex are homologous to proteins of the sulfate ABC transporter. Molybdenum may be used in nitrogenases of nitrogen-fixing bacteria and in molybdopterin cofactors. In some cases, molybdate may be transported by a sulfate transporter rather than by a specific molybdate transporter. [Transport and binding proteins, Anions]
Pssm-ID: 131197 [Multi-domain] Cd Length: 354 Bit Score: 119.83 E-value: 3.55e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 15 SLRYGETRAvdDVSLEIPANRMVGLIGPDGVGKSSLLALLAGARKMQDGEIrVLDG----DMRDRR----HRRavcpRIA 86
Cdd:TIGR02142 6 SKRLGDFSL--DADFTLPGQGVTAIFGRSGSGKTTLIRLIAGLTRPDEGEI-VLNGrtlfDSRKGIflppEKR----RIG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 87 YMPQGlgKNLYPTLSVFENVDF-FGRLFGHDKAERERRIADLLqstGLAPFAERPAGKLSGGMKQKLGLCCALIHDPDLL 165
Cdd:TIGR02142 79 YVFQE--ARLFPHLSVRGNLRYgMKRARPSERRISFERVIELL---GIGHLLGRLPGRLSGGEKQRVAIGRALLSSPRLL 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 166 ILDEPTTGVDPLSRNQFWELIGRIRAgREGMSVLVATAYMEEAERF-DWLVAMDDGKVLATGTPQELRERTGTQSLESAF 244
Cdd:TIGR02142 154 LMDEPLAALDDPRKYEILPYLERLHA-EFGIPILYVSHSLQEVLRLaDRVVVLEDGRVAAAGPIAEVWASPDLPWLARED 232
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 15600424 245 IALLPESKRAGHH-------------RLVIPPRPQSEGAP-RIAIEA 277
Cdd:TIGR02142 233 QGSLIEGVVAEHDqhygltalrlgggHLWVPENLGPTGARlRLRVPA 279
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
10-226 |
3.95e-29 |
|
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: 116.66 E-value: 3.95e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 10 SLRGVSLR-YGETRAVDDVSLEIPANRMVGLIGPDGVGKSSLLALLAGARKMQDGEIRVLDGDMRDRR--HRRavcpRIA 86
Cdd:cd03267 22 SLKSLFKRkYREVEALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRVAGLVPWKRRkkFLR----RIG 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 87 YMpQGLGKNLYPTLSVFENVDFFGRLFGHDKAE---RERRIADLLQstgLAPFAERPAGKLSGGMKQKLGLCCALIHDPD 163
Cdd:cd03267 98 VV-FGQKTQLWWDLPVIDSFYLLAAIYDLPPARfkkRLDELSELLD---LEELLDTPVRQLSLGQRMRAEIAAALLHEPE 173
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15600424 164 LLILDEPTTGVDPLSRNQFWELIGRIRAGReGMSVLVATAYMEEAERF-DWLVAMDDGKVLATG 226
Cdd:cd03267 174 ILFLDEPTIGLDVVAQENIRNFLKEYNRER-GTTVLLTSHYMKDIEALaRRVLVIDKGRLLYDG 236
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
275-464 |
4.04e-29 |
|
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: 115.97 E-value: 4.04e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 275 IEAEGLTCRF-GDFVAVDHVSFRIERGEIFGFLGSNGCGKSTTMKMLTGLLPASEGTCALFGQPV-DASDMAT---RRRV 349
Cdd:cd03292 1 IEFINVTKTYpNGTAALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQDVsDLRGRAIpylRRKI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 350 GYMSQAFSLYAELSVRQNLVLHARLFHLPADGIPARVGEMLRRFDLEKVADELPNDLPLGIRQRLSLAVAVIHKPEILIL 429
Cdd:cd03292 81 GVVFQDFRLLPDRNVYENVAFALEVTGVPPREIRKRVPAALELVGLSHKHRALPAELSGGEQQRVAIARAIVNSPTILIA 160
|
170 180 190
....*....|....*....|....*....|....*
gi 15600424 430 DEPTSGVDPVARDGFWELMVELSRRdGVTIFISTH 464
Cdd:cd03292 161 DEPTGNLDPDTTWEIMNLLKKINKA-GTTVVVATH 194
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
11-231 |
5.30e-29 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 119.44 E-value: 5.30e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 11 LRGVSLRYGETRAVDDVSLEIPANRMVGLIGPDGVGKSSLLALLAGARKMQDGEIrVLDG-DMRDRR-HRRAVCprIAYM 88
Cdd:PRK11432 9 LKNITKRFGSNTVIDNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQI-FIDGeDVTHRSiQQRDIC--MVFQ 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 89 PQGLgknlYPTLSVFENVDFFGRLFGHDKAERERRIADLLQSTGLAPFAERPAGKLSGGMKQKLGLCCALIHDPDLLILD 168
Cdd:PRK11432 86 SYAL----FPHMSLGENVGYGLKMLGVPKEERKQRVKEALELVDLAGFEDRYVDQISGGQQQRVALARALILKPKVLLFD 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15600424 169 EPTTGVDPLSRNQFWELIgRIRAGREGMSVLVATayMEEAERF---DWLVAMDDGKVLATGTPQEL 231
Cdd:PRK11432 162 EPLSNLDANLRRSMREKI-RELQQQFNITSLYVT--HDQSEAFavsDTVIVMNKGKIMQIGSPQEL 224
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
275-491 |
5.81e-29 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 119.67 E-value: 5.81e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 275 IEAEGLTCRFGDFVAVDHVSFRIERGEIFGFLGSNGCGKSTTMKMLTGLLPASEGTCALFGQpvDASDM-ATRRRVGYMS 353
Cdd:PRK09452 15 VELRGISKSFDGKEVISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLDGQ--DITHVpAENRHVNTVF 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 354 QAFSLYAELSVRQNLVLHARLFHLPADGIPARVGEMLRRFDLEKVADELPNDLPLGIRQRLSLAVAVIHKPEILILDEPT 433
Cdd:PRK09452 93 QSYALFPHMTVFENVAFGLRMQKTPAAEITPRVMEALRMVQLEEFAQRKPHQLSGGQQQRVAIARAVVNKPKVLLLDESL 172
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15600424 434 SGVDPVARDgfwELMVE---LSRRDGVT-IFIsTHFMNEA-QRCDRISLMHAGKVLASDTPDE 491
Cdd:PRK09452 173 SALDYKLRK---QMQNElkaLQRKLGITfVFV-THDQEEAlTMSDRIVVMRDGRIEQDGTPRE 231
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
275-483 |
8.81e-29 |
|
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: 117.85 E-value: 8.81e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 275 IEAEGLTCRF----GDFVAVDHVSFRIERGEIFGFLGSNGCGKSTTMKMLTGLLPA---SEGTCALFGQPV---DASDMA 344
Cdd:COG0444 2 LEVRNLKVYFptrrGVVKAVDGVSFDVRRGETLGLVGESGSGKSTLARAILGLLPPpgiTSGEILFDGEDLlklSEKELR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 345 TRR--RVGYMSQ-AF-SLYAELSVRQ----NLVLHarlFHLPADGIPARVGEMLRRFDL---EKVADELPNDLPLGIRQR 413
Cdd:COG0444 82 KIRgrEIQMIFQdPMtSLNPVMTVGDqiaePLRIH---GGLSKAEARERAIELLERVGLpdpERRLDRYPHELSGGMRQR 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15600424 414 LSLAVAVIHKPEILILDEPTSGVDPVARDGFWELMVELSRRDGVT-IFIsTHFMNE-AQRCDRISLMHAGKV 483
Cdd:COG0444 159 VMIARALALEPKLLIADEPTTALDVTIQAQILNLLKDLQRELGLAiLFI-THDLGVvAEIADRVAVMYAGRI 229
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
10-231 |
1.09e-28 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 115.13 E-value: 1.09e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 10 SLRGVSLRYGETRAVDDVSLEIPANRMVGLIGPDGVGKSSLLALLAGARKMQDGEIRvLDGD------MrdrrHRRAvcp 83
Cdd:COG1137 5 EAENLVKSYGKRTVVKDVSLEVNQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGRIF-LDGEdithlpM----HKRA--- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 84 R--IAYMPQ------GLgknlyptlSVFENVDFFGRLFGHDKAERERRIADLLQSTGLAPFAERPAGKLSGGMKQKLGLC 155
Cdd:COG1137 77 RlgIGYLPQeasifrKL--------TVEDNILAVLELRKLSKKEREERLEELLEEFGITHLRKSKAYSLSGGERRRVEIA 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 156 CALIHDPDLLILDEPTTGVDPLSRNQFWELIGRIRAgrEGMSVLVA------------TAYMeeaerfdwlvaMDDGKVL 223
Cdd:COG1137 149 RALATNPKFILLDEPFAGVDPIAVADIQKIIRHLKE--RGIGVLITdhnvretlgicdRAYI-----------ISEGKVL 215
|
....*...
gi 15600424 224 ATGTPQEL 231
Cdd:COG1137 216 AEGTPEEI 223
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
262-498 |
1.34e-28 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 121.81 E-value: 1.34e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 262 PPRPQSEGAPRIAIEAEGLTcrF---GDFVAVDHVSFRIERGEIFGFLGSNGCGKSTTMKMLTGLLPASEGTCALFGQPV 338
Cdd:COG1132 327 PPGAVPLPPVRGEIEFENVS--FsypGDRPVLKDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYDPTSGRILIDGVDI 404
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 339 DASDMAT-RRRVGYMSQAFSLYAElSVRQNLvlhaRLFHLPADgiPARVGEMLRRFDLEKVADELPN--DLPLGI----- 410
Cdd:COG1132 405 RDLTLESlRRQIGVVPQDTFLFSG-TIRENI----RYGRPDAT--DEEVEEAAKAAQAHEFIEALPDgyDTVVGErgvnl 477
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 411 ----RQRLSLAVAVIHKPEILILDEPTSGVDPVA----RDGFWELMvelsrrDGVTIFISTHFMNEAQRCDRISLMHAGK 482
Cdd:COG1132 478 sggqRQRIAIARALLKDPPILILDEATSALDTETealiQEALERLM------KGRTTIVIAHRLSTIRNADRILVLDDGR 551
|
250
....*....|....*.
gi 15600424 483 VLASDTPDELVRQRGL 498
Cdd:COG1132 552 IVEQGTHEELLARGGL 567
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
22-483 |
1.43e-28 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 120.88 E-value: 1.43e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 22 RAVDDVSLEIPANRMVGLIGPDGVGKSSLLALLAGARKMQDGEIRVLDGDMRDRRHRRAVCPRIAYMPQGLgkNLYPTLS 101
Cdd:PRK10762 18 KALSGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSILYLGKEVTFNGPKSSQEAGIGIIHQEL--NLIPQLT 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 102 VFENVdFFGR----LFGHDKAERERRIAD-LLQSTGLAPFAERPAGKLSGGMKQKLGLCCALIHDPDLLILDEPTTGVDP 176
Cdd:PRK10762 96 IAENI-FLGRefvnRFGRIDWKKMYAEADkLLARLNLRFSSDKLVGELSIGEQQMVEIAKVLSFESKVIIMDEPTDALTD 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 177 LSRNQFWELIGRIRAgrEGMSVLVATAYMEEA-ERFDWLVAMDDGKVLAtgtpqelrERTGTQSLESAFIALLpeskrAG 255
Cdd:PRK10762 175 TETESLFRVIRELKS--QGRGIVYISHRLKEIfEICDDVTVFRDGQFIA--------EREVADLTEDSLIEMM-----VG 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 256 hhrlvippRPQSEGAPRIAI-------EAEGLTcrfGDfvAVDHVSFRIERGEIFGFLGSNGCGKSTTMKMLTGLLPASE 328
Cdd:PRK10762 240 --------RKLEDQYPRLDKapgevrlKVDNLS---GP--GVNDVSFTLRKGEILGVSGLMGAGRTELMKVLYGALPRTS 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 329 GTCALFGQPVDASDMATRRRVG--YMSQ---AFSLYAELSVRQNLVLHArLFHLPADGIPAR-------VGEMLRRFDLE 396
Cdd:PRK10762 307 GYVTLDGHEVVTRSPQDGLANGivYISEdrkRDGLVLGMSVKENMSLTA-LRYFSRAGGSLKhadeqqaVSDFIRLFNIK 385
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 397 KVA-DELPNDLPLGIRQRLSLAVAVIHKPEILILDEPTSGVDPVARDGFWELMVELsRRDGVTIFISTHFMNEA-QRCDR 474
Cdd:PRK10762 386 TPSmEQAIGLLSGGNQQKVAIARGLMTRPKVLILDEPTRGVDVGAKKEIYQLINQF-KAEGLSIILVSSEMPEVlGMSDR 464
|
....*....
gi 15600424 475 ISLMHAGKV 483
Cdd:PRK10762 465 ILVMHEGRI 473
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
275-496 |
1.47e-28 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 116.10 E-value: 1.47e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 275 IEAEGLTCRFGDFV-AVDHVSFRIERGEIFGFLGSNGCGKSTTMKMLTGLLPASEGTCALFGQPVDASD---MATRRRVG 350
Cdd:PRK13636 6 LKVEELNYNYSDGThALKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGKPIDYSRkglMKLRESVG 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 351 YM-----SQAFSLyaelSVRQNLVLHARLFHLPADGIPARVGEMLRRFDLEKVADELPNDLPLGIRQRLSLAVAVIHKPE 425
Cdd:PRK13636 86 MVfqdpdNQLFSA----SVYQDVSFGAVNLKLPEDEVRKRVDNALKRTGIEHLKDKPTHCLSFGQKKRVAIAGVLVMEPK 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15600424 426 ILILDEPTSGVDPVARDGFWELMVELSRRDGVTIFISTHFMNE-AQRCDRISLMHAGKVLASDTPDELVRQR 496
Cdd:PRK13636 162 VLVLDEPTAGLDPMGVSEIMKLLVEMQKELGLTIIIATHDIDIvPLYCDNVFVMKEGRVILQGNPKEVFAEK 233
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
11-231 |
1.94e-28 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 114.47 E-value: 1.94e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 11 LRGVSLRYGETRAvdDVSLEIPANRMVGLIGPDGVGKSSLLALLAGARKMQDGEIRVLDGDMRDRR-HRRAVcpriAYMP 89
Cdd:COG3840 4 LDDLTYRYGDFPL--RFDLTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILWNGQDLTALPpAERPV----SMLF 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 90 QGlgKNLYPTLSVFENVDFfG-----RLfghDKAERERrIADLLQSTGLAPFAERPAGKLSGGMKQKLGLCCALIHDPDL 164
Cdd:COG3840 78 QE--NNLFPHLTVAQNIGL-GlrpglKL---TAEQRAQ-VEQALERVGLAGLLDRLPGQLSGGQRQRVALARCLVRKRPI 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15600424 165 LILDEPTTGVDPLSRNQFWELIGRIrAGREGMSVLVATAYMEEAERF-DWLVAMDDGKVLATGTPQEL 231
Cdd:COG3840 151 LLLDEPFSALDPALRQEMLDLVDEL-CRERGLTVLMVTHDPEDAARIaDRVLLVADGRIAADGPTAAL 217
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
19-462 |
1.96e-28 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 120.97 E-value: 1.96e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 19 GETR-AVDDVSLEIPANRMVGLIGPDGVGKS----SLLALL-AGARKMQDGEIR-----VLDGDMRDRRHRRAvcPRIAY 87
Cdd:PRK15134 19 QTVRtVVNDVSLQIEAGETLALVGESGSGKSvtalSILRLLpSPPVVYPSGDIRfhgesLLHASEQTLRGVRG--NKIAM 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 88 MPQ----------GLGKNLYPTLSVFenvdffgRLFGHDKAERErrIADLLQSTGLAPFAERPAG---KLSGGMKQKLGL 154
Cdd:PRK15134 97 IFQepmvslnplhTLEKQLYEVLSLH-------RGMRREAARGE--ILNCLDRVGIRQAAKRLTDyphQLSGGERQRVMI 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 155 CCALIHDPDLLILDEPTTGVDPLSRNQFWELIGRIRagRE-GMSVLVATAYMEEAERF-DWLVAMDDGKVLatgtpqelr 232
Cdd:PRK15134 168 AMALLTRPELLIADEPTTALDVSVQAQILQLLRELQ--QElNMGLLFITHNLSIVRKLaDRVAVMQNGRCV--------- 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 233 ERTGTQSLESA----FIALLPESKRAGHhrlvipPRPQSEGAPRIaIEAEGLTCRF-----------GDFVAVDHVSFRI 297
Cdd:PRK15134 237 EQNRAATLFSApthpYTQKLLNSEPSGD------PVPLPEPASPL-LDVEQLQVAFpirkgilkrtvDHNVVVKNISFTL 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 298 ERGEIFGFLGSNGCGKSTTMKMLTGLLpASEGTCALFGQPVDASD----MATRRRVGYMSQ--AFSLYAELSVRQ----N 367
Cdd:PRK15134 310 RPGETLGLVGESGSGKSTTGLALLRLI-NSQGEIWFDGQPLHNLNrrqlLPVRHRIQVVFQdpNSSLNPRLNVLQiieeG 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 368 LVLHARlfHLPADGIPARVGEMLRRFDLEKVA-DELPNDLPLGIRQRLSLAVAVIHKPEILILDEPTSGVDPVARDGFWE 446
Cdd:PRK15134 389 LRVHQP--TLSAAQREQQVIAVMEEVGLDPETrHRYPAEFSGGQRQRIAIARALILKPSLIILDEPTSSLDKTVQAQILA 466
|
490
....*....|....*..
gi 15600424 447 LMVELSRRDGVT-IFIS 462
Cdd:PRK15134 467 LLKSLQQKHQLAyLFIS 483
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
275-495 |
2.00e-28 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 115.09 E-value: 2.00e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 275 IEAEGLTCRFGDFVAVDHVSFRIERGEIFGFLGSNGCGKSTTMKMLTGLLPASEGTCALFGQPVD--ASDMATRRRVGYM 352
Cdd:PRK11300 6 LSVSGLMMRFGGLLAVNNVNLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTILLRGQHIEglPGHQIARMGVVRT 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 353 SQAFSLYAELSVRQNLV----------LHARLFHLPA------DGIpARVGEMLRRFDLEKVADELPNDLPLGIRQRLSL 416
Cdd:PRK11300 86 FQHVRLFREMTVIENLLvaqhqqlktgLFSGLLKTPAfrraesEAL-DRAATWLERVGLLEHANRQAGNLAYGQQRRLEI 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 417 AVAVIHKPEILILDEPTSGVDPVARDGFWELMVELSRRDGVTIFISTHFMNEAQR-CDRISLMHAGKVLASDTPDElVRQ 495
Cdd:PRK11300 165 ARCMVTQPEILMLDEPAAGLNPKETKELDELIAELRNEHNVTVLLIEHDMKLVMGiSDRIYVVNQGTPLANGTPEE-IRN 243
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
11-240 |
2.34e-28 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 114.42 E-value: 2.34e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 11 LRGVSLRYGETRAVDDVSLEIPANRMVGLIGPDGVGKSSLLALLAGARKMQDGEIRVLDGDMRDRRHRRAVCPRIAYMP- 89
Cdd:PRK09493 4 FKNVSKHFGPTQVLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGLKVNDPKVDERLIRQEAGMVf 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 90 QGLgkNLYPTLSVFENVdFFG--RLFGHDKAERERRIADLLQSTGLAPFAERPAGKLSGGMKQKLGLCCALIHDPDLLIL 167
Cdd:PRK09493 84 QQF--YLFPHLTALENV-MFGplRVRGASKEEAEKQARELLAKVGLAERAHHYPSELSGGQQQRVAIARALAVKPKLMLF 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15600424 168 DEPTTGVDPLSRNqfwELIGRIRA-GREGMSVLVATAYMEEAERF-DWLVAMDDGKVLATGTPQELRERTGTQSL 240
Cdd:PRK09493 161 DEPTSALDPELRH---EVLKVMQDlAEEGMTMVIVTHEIGFAEKVaSRLIFIDKGRIAEDGDPQVLIKNPPSQRL 232
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
275-491 |
4.34e-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: 113.58 E-value: 4.34e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 275 IEAEGLTCRFGDFVaVDHVSFRIERGEIFGFLGSNGCGKSTTMKMLTGLLPASEGTCALFGqpVDASDMA-TRRRVGYMS 353
Cdd:cd03299 1 LKVENLSKDWKEFK-LKNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNG--KDITNLPpEKRDISYVP 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 354 QAFSLYAELSVRQNLVLHARLFHLPADGIPARVGEMLRRFDLEKVADELPNDLPLGIRQRLSLAVAVIHKPEILILDEPT 433
Cdd:cd03299 78 QNYALFPHMTVYKNIAYGLKKRKVDKKEIERKVLEIAEMLGIDHLLNRKPETLSGGEQQRVAIARALVVNPKILLLDEPF 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 15600424 434 SGVDPVARDGFWELMVELSRRDGVTIFISTHFMNEAQR-CDRISLMHAGKVLASDTPDE 491
Cdd:cd03299 158 SALDVRTKEKLREELKKIRKEFGVTVLHVTHDFEEAWAlADKVAIMLNGKLIQVGKPEE 216
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
8-437 |
7.02e-28 |
|
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of the ABC transporter ATP-binding cassette, but are found outside the common ABC transporter operon structure that features integral membrane permease proteins and substrate-binding proteins encoded next to the ATP-binding cassette (ABC domain) protein. The member protein ChvD from Agrobacterium tumefaciens was identified as both a candidate to interact with VirB8, based on yeast two-hybrid analysis, and as an apparent regulator of VirG. The general function of this protein family is unknown.
Pssm-ID: 274744 [Multi-domain] Cd Length: 552 Bit Score: 119.27 E-value: 7.02e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 8 VASLRGVSLRYGETRAV-DDVSLEIPANRMVGLIGPDGVGKSSLLALLAGARKMQDGEIRVLDGdmrdrrhrravcPRIA 86
Cdd:TIGR03719 4 IYTMNRVSKVVPPKKEIlKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKDFNGEARPQPG------------IKVG 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 87 YMPQGlgKNLYPTLSVFENV--------DFFGRL------FG-----HDK-AERERRIADLLQSTGL------------- 133
Cdd:TIGR03719 72 YLPQE--PQLDPTKTVRENVeegvaeikDALDRFneisakYAepdadFDKlAAEQAELQEIIDAADAwdldsqleiamda 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 134 --APFAERPAGKLSGGMKQKLGLCCALIHDPDLLILDEPTTGVDPLSRNqfWelIGRIRAGREGMSVLV---------AT 202
Cdd:TIGR03719 150 lrCPPWDADVTKLSGGERRRVALCRLLLSKPDMLLLDEPTNHLDAESVA--W--LERHLQEYPGTVVAVthdryfldnVA 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 203 AYMEEAER----------FDWLVAMDdgKVLATGTPQEL-RERTGTQSLE-----------------SAFIALLPES--K 252
Cdd:TIGR03719 226 GWILELDRgrgipwegnySSWLEQKQ--KRLEQEEKEESaRQKTLKRELEwvrqspkgrqakskarlARYEELLSQEfqK 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 253 RAGHHRLVIPPrpqsegAPR---IAIEAEGLTCRFGDFVAVDHVSFRIERGEIFGFLGSNGCGKSTTMKMLTGLLPASEG 329
Cdd:TIGR03719 304 RNETAEIYIPP------GPRlgdKVIEAENLTKAFGDKLLIDDLSFKLPPGGIVGVIGPNGAGKSTLFRMITGQEQPDSG 377
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 330 TCALfGQPVdasdmatrrRVGYMSQAfslyaelsvRQNLVLHARLFHLPADG----------IPAR--VGemlrRF---- 393
Cdd:TIGR03719 378 TIEI-GETV---------KLAYVDQS---------RDALDPNKTVWEEISGGldiiklgkreIPSRayVG----RFnfkg 434
|
490 500 510 520
....*....|....*....|....*....|....*....|....*
gi 15600424 394 -DLEKVADELPNdlplGIRQRLSLAVAVIHKPEILILDEPTSGVD 437
Cdd:TIGR03719 435 sDQQKKVGQLSG----GERNRVHLAKTLKSGGNVLLLDEPTNDLD 475
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
11-202 |
1.18e-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: 111.73 E-value: 1.18e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 11 LRGVSLRY-GETRAVDDVSLEIPANRMVGLIGPDGVGKSSLLALLAGARKMQDGEIRVLDGDMRDRRHRRavcprIAYMP 89
Cdd:cd03292 3 FINVTKTYpNGTAALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQDVSDLRGRA-----IPYLR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 90 QGLG-----KNLYPTLSVFENVDFFGRLFGHDKAERERRIADLLQSTGLAPFAERPAGKLSGGMKQKLGLCCALIHDPDL 164
Cdd:cd03292 78 RKIGvvfqdFRLLPDRNVYENVAFALEVTGVPPREIRKRVPAALELVGLSHKHRALPAELSGGEQQRVAIARAIVNSPTI 157
|
170 180 190
....*....|....*....|....*....|....*...
gi 15600424 165 LILDEPTTGVDPLSRNQFWELIGRIRAgrEGMSVLVAT 202
Cdd:cd03292 158 LIADEPTGNLDPDTTWEIMNLLKKINK--AGTTVVVAT 193
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
275-503 |
1.51e-27 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 111.77 E-value: 1.51e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 275 IEAEGLTCRFGDFVAvdHVSFRIERGEIFGFLGSNGCGKSTTMKMLTGLLPASEGTCALFGQPVDASDMAtRRRVGYMSQ 354
Cdd:COG3840 2 LRLDDLTYRYGDFPL--RFDLTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILWNGQDLTALPPA-ERPVSMLFQ 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 355 AFSLYAELSVRQN--LVLHARLfHLPADGIpARVGEMLRRFDLEKVADELPNDLPLGIRQRLSLAVAVIHKPEILILDEP 432
Cdd:COG3840 79 ENNLFPHLTVAQNigLGLRPGL-KLTAEQR-AQVEQALERVGLAGLLDRLPGQLSGGQRQRVALARCLVRKRPILLLDEP 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15600424 433 TSGVDPVARDGFWELMVELSRRDGVTIFISTHFMNEAQR-CDRISLMHAGKVLASDTPDELVRQRGLPTLEA 503
Cdd:COG3840 157 FSALDPALRQEMLDLVDELCRERGLTVLMVTHDPEDAARiADRVLLVADGRIAADGPTAALLDGEPPPALAA 228
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
17-464 |
2.40e-27 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 117.04 E-value: 2.40e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 17 RYGETRAVDDVSLEIPANRMVGLIGPDGVGKSSLlallagARKMQdGEIRVLDGDMRDRRHRravCPRIAY------MPQ 90
Cdd:PRK10938 12 RLSDTKTLQLPSLTLNAGDSWAFVGANGSGKSAL------ARALA-GELPLLSGERQSQFSH---ITRLSFeqlqklVSD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 91 GLGKNLYPTLSVFEnvDFFGR------LFGHDKAERERRIADLLqstGLAPFAERPAGKLSGGMKQKLGLCCALIHDPDL 164
Cdd:PRK10938 82 EWQRNNTDMLSPGE--DDTGRttaeiiQDEVKDPARCEQLAQQF---GITALLDRRFKYLSTGETRKTLLCQALMSEPDL 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 165 LILDEPTTGVDPLSRNQFWELIGRIRAgrEGMS-VLVATAYMEEAERFDWLVAMDDGKVLATGTPQELrertgtqsLESA 243
Cdd:PRK10938 157 LILDEPFDGLDVASRQQLAELLASLHQ--SGITlVLVLNRFDEIPDFVQFAGVLADCTLAETGEREEI--------LQQA 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 244 FIALLPESKRAGHHRLVIPPRPQ-----SEGAPRiaIEAEGLTCRFGDFVAVDHVSFRIERGEIFGFLGSNGCGKSTTMK 318
Cdd:PRK10938 227 LVAQLAHSEQLEGVQLPEPDEPSarhalPANEPR--IVLNNGVVSYNDRPILHNLSWQVNPGEHWQIVGPNGAGKSTLLS 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 319 MLTGLLPAS-EGTCALFGqpvdasdmatRRR------------VGYMSQAFSL-Y-AELSVRqNLVLHA-----RLFHLP 378
Cdd:PRK10938 305 LITGDHPQGySNDLTLFG----------RRRgsgetiwdikkhIGYVSSSLHLdYrVSTSVR-NVILSGffdsiGIYQAV 373
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 379 ADGIPARVGEMLRRFDLEK-VADELPNDLPLGiRQRLSLAV-AVIHKPEILILDEPTSGVDPVARD---GFWELMVelsr 453
Cdd:PRK10938 374 SDRQQKLAQQWLDILGIDKrTADAPFHSLSWG-QQRLALIVrALVKHPTLLILDEPLQGLDPLNRQlvrRFVDVLI---- 448
|
490
....*....|...
gi 15600424 454 RDGVT--IFISTH 464
Cdd:PRK10938 449 SEGETqlLFVSHH 461
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
26-277 |
2.61e-27 |
|
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and metabolism]; ABC-type molybdate transport system, ATPase component ModC is part of the Pathway/BioSystem: Molybdopterin biosynthesis
Pssm-ID: 443319 [Multi-domain] Cd Length: 358 Bit Score: 114.43 E-value: 2.61e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 26 DVSLEIPANRMVGLIGPDGVGKSSLLALLAGARKMQDGEIRVLDGDMRDRRHRRAVCP---RIAYMPQGlgKNLYPTLSV 102
Cdd:COG4148 17 DVDFTLPGRGVTALFGPSGSGKTTLLRAIAGLERPDSGRIRLGGEVLQDSARGIFLPPhrrRIGYVFQE--ARLFPHLSV 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 103 FENVdffgrLFGHDKAERERR------IADLLqstGLAPFAERPAGKLSGGMKQKLGLCCALIHDPDLLILDEPTTGVDP 176
Cdd:COG4148 95 RGNL-----LYGRKRAPRAERrisfdeVVELL---GIGHLLDRRPATLSGGERQRVAIGRALLSSPRLLLMDEPLAALDL 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 177 LSRNQFWELIGRIRAgREGMSVLVATAYMEEAERF-DWLVAMDDGKVLATGTPQELRERTGTQSLESAFIA--LLpESKR 253
Cdd:COG4148 167 ARKAEILPYLERLRD-ELDIPILYVSHSLDEVARLaDHVVLLEQGRVVASGPLAEVLSRPDLLPLAGGEEAgsVL-EATV 244
|
250 260 270
....*....|....*....|....*....|....*...
gi 15600424 254 AGHH-------------RLVIPPRPQSEGAP-RIAIEA 277
Cdd:COG4148 245 AAHDpdygltrlalgggRLWVPRLDLPPGTRvRVRIRA 282
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
10-222 |
3.12e-27 |
|
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: 110.31 E-value: 3.12e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 10 SLRGVSLRYGETRAVDDVSLEIPANRMVGLIGPDGVGKSSLLALLAGARKMQDGEIRVlDGDMRDRRHRRavcprIAYMP 89
Cdd:cd03262 2 EIKNLHKSFGDFHVLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIII-DGLKLTDDKKN-----INELR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 90 QGLGK-----NLYPTLSVFENVDFFGR-LFGHDKAERERRIADLLQSTGLAPFAERPAGKLSGGMKQKLGLCCALIHDPD 163
Cdd:cd03262 76 QKVGMvfqqfNLFPHLTVLENITLAPIkVKGMSKAEAEERALELLEKVGLADKADAYPAQLSGGQQQRVAIARALAMNPK 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15600424 164 LLILDEPTTGVDPlsrnqfwELIGRI-----RAGREGMSVLVATAYMEEA-ERFDWLVAMDDGKV 222
Cdd:cd03262 156 VMLFDEPTSALDP-------ELVGEVldvmkDLAEEGMTMVVVTHEMGFArEVADRVIFMDDGRI 213
|
|
| LPS_export_lptB |
TIGR04406 |
LPS export ABC transporter ATP-binding protein; Members of this fmaily are LptB, the ... |
12-231 |
3.63e-27 |
|
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: 110.83 E-value: 3.63e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 12 RGVSLRYGETRAVDDVSLEIPANRMVGLIGPDGVGKSSLLALLAGARKMQDGEIRVLDGDMRDR-RHRRAvcpR--IAYM 88
Cdd:TIGR04406 5 ENLIKSYKKRKVVNDVSLSVKSGEIVGLLGPNGAGKTTSFYMIVGLVRPDAGKILIDGQDITHLpMHERA---RlgIGYL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 89 PQGlgKNLYPTLSVFENV----DFFGRLfghDKAERERRIADLLQSTGLAPFAERPAGKLSGGMKQKLGLCCALIHDPDL 164
Cdd:TIGR04406 82 PQE--ASIFRKLTVEENImavlEIRKDL---DRAEREERLEALLEEFQISHLRDNKAMSLSGGERRRVEIARALATNPKF 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15600424 165 LILDEPTTGVDPLSRNQFWELIGRIRAgrEGMSVLVATAYMEE----AERfDWLVAmdDGKVLATGTPQEL 231
Cdd:TIGR04406 157 ILLDEPFAGVDPIAVGDIKKIIKHLKE--RGIGVLITDHNVREtldiCDR-AYIIS--DGKVLAEGTPAEI 222
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
7-226 |
3.99e-27 |
|
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: 110.37 E-value: 3.99e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 7 GVASLRGVSLRY--GETRAVDDVSLEIPANRMVGLIGPDGVGKSSLLALLAGARKMQDGEIRvLDG------DMRDRRHR 78
Cdd:cd03245 1 GRIEFRNVSFSYpnQEIPALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVL-LDGtdirqlDPADLRRN 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 79 ravcprIAYMPQGlgknlyPTL---SVFENVDFfGRLFGHDkaERERRIADLlqsTGLAPFAER-PAG----------KL 144
Cdd:cd03245 80 ------IGYVPQD------VTLfygTLRDNITL-GAPLADD--ERILRAAEL---AGVTDFVNKhPNGldlqigergrGL 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 145 SGGMKQKLGLCCALIHDPDLLILDEPTTGVDPLSRNQFwelIGRIRAGREGMSVLVATAYMEEAERFDWLVAMDDGKVLA 224
Cdd:cd03245 142 SGGQRQAVALARALLNDPPILLLDEPTSAMDMNSEERL---KERLRQLLGDKTLIIITHRPSLLDLVDRIIVMDSGRIVA 218
|
..
gi 15600424 225 TG 226
Cdd:cd03245 219 DG 220
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
12-230 |
4.42e-27 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 111.40 E-value: 4.42e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 12 RGVSLRYGETRAVDDVSLEIPANRMVGLIGPDGVGKSSLLALLAGARKMQDGEIRVLDGDMRD-----RRHRRAVcpria 86
Cdd:PRK13548 6 RNLSVRLGGRTLLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLNGRPLADwspaeLARRRAV----- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 87 yMPQglgknlYPTLSvF----ENVDFFGRL-FGHDKAERERRIADLLQSTGLAPFAERPAGKLSGGMKQKLGLCCALI-- 159
Cdd:PRK13548 81 -LPQ------HSSLS-FpftvEEVVAMGRApHGLSRAEDDALVAAALAQVDLAHLAGRDYPQLSGGEQQRVQLARVLAql 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 160 ----HDPDLLILDEPTTGVDPlsRNQFWEL-IGRIRAGREGMSVLV-------ATAYmeeAERfdwLVAMDDGKVLATGT 227
Cdd:PRK13548 153 wepdGPPRWLLLDEPTSALDL--AHQHHVLrLARQLAHERGLAVIVvlhdlnlAARY---ADR---IVLLHQGRLVADGT 224
|
...
gi 15600424 228 PQE 230
Cdd:PRK13548 225 PAE 227
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
11-226 |
4.63e-27 |
|
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: 109.65 E-value: 4.63e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 11 LRGVSLRYGETRAVDDVSLEIPANRMVGLIGPDGVGKSSLLALLAGARKMQDGEIRVLDGDMRDRR--HRravcpRIAYM 88
Cdd:cd03301 3 LENVTKRFGNVTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGRDVTDLPpkDR-----DIAMV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 89 PQGLGknLYPTLSVFENVDFFGRLFGHDKAE---RERRIADLLQSTGLapfAERPAGKLSGGMKQKLGLCCALIHDPDLL 165
Cdd:cd03301 78 FQNYA--LYPHMTVYDNIAFGLKLRKVPKDEideRVREVAELLQIEHL---LDRKPKQLSGGQRQRVALGRAIVREPKVF 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15600424 166 ILDEPTTGVDPLSRNQFWELIGRIRAgREGMSVLVATAYMEEAERF-DWLVAMDDGKVLATG 226
Cdd:cd03301 153 LMDEPLSNLDAKLRVQMRAELKRLQQ-RLGTTTIYVTHDQVEAMTMaDRIAVMNDGQIQQIG 213
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
275-495 |
5.97e-27 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 113.28 E-value: 5.97e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 275 IEAEGLTCRFGDFVAVDHVSFRIERGEIFGFLGSNGCGKSTTMKMLTGLLPASEGTCALFGQPVDASDMaTRRRVGYMSQ 354
Cdd:PRK11432 7 VVLKNITKRFGSNTVIDNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIFIDGEDVTHRSI-QQRDICMVFQ 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 355 AFSLYAELSVRQNLVLHARLFHLPADGIPARVGEMLRRFDLEKVADELPNDLPLGIRQRLSLAVAVIHKPEILILDEPTS 434
Cdd:PRK11432 86 SYALFPHMSLGENVGYGLKMLGVPKEERKQRVKEALELVDLAGFEDRYVDQISGGQQQRVALARALILKPKVLLFDEPLS 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15600424 435 GVDPVARDGFWELMVELSRRDGVTIFISTHFMNEA-QRCDRISLMHAGKVLASDTPDELVRQ 495
Cdd:PRK11432 166 NLDANLRRSMREKIRELQQQFNITSLYVTHDQSEAfAVSDTVIVMNKGKIMQIGSPQELYRQ 227
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
8-484 |
6.19e-27 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 117.26 E-value: 6.19e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 8 VASLRGVSLRYGETR----AVDDVSLEIPANRMVGLIGPDGVGKS----SLLALL--AGARKMQDGEI------RVLD-G 70
Cdd:PRK10261 12 VLAVENLNIAFMQEQqkiaAVRNLSFSLQRGETLAIVGESGSGKSvtalALMRLLeqAGGLVQCDKMLlrrrsrQVIElS 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 71 DMRDRRHRRAVCPRIAYMPQGLGKNLYPTLSVFENVDFFGRL---FGHDKAERE-RRIADLLQSTGLAPFAERPAGKLSG 146
Cdd:PRK10261 92 EQSAAQMRHVRGADMAMIFQEPMTSLNPVFTVGEQIAESIRLhqgASREEAMVEaKRMLDQVRIPEAQTILSRYPHQLSG 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 147 GMKQKLGLCCALIHDPDLLILDEPTTGVDPLSRNQFWELIgRIRAGREGMSVLVATAYMEE-AERFDWLVAMDDGKVLAT 225
Cdd:PRK10261 172 GMRQRVMIAMALSCRPAVLIADEPTTALDVTIQAQILQLI-KVLQKEMSMGVIFITHDMGVvAEIADRVLVMYQGEAVET 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 226 GTPQELRERTG---TQSLESAfIALLPESKRAGHHR---LVIPPRPQS-----------EGAPriAIEAEGLTCRFG--- 285
Cdd:PRK10261 251 GSVEQIFHAPQhpyTRALLAA-VPQLGAMKGLDYPRrfpLISLEHPAKqeppieqdtvvDGEP--ILQVRNLVTRFPlrs 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 286 --------DFVAVDHVSFRIERGEIFGFLGSNGCGKSTTMKMLTGLLPASEGTCALFGQPVD---ASDM-ATRRRVGYMS 353
Cdd:PRK10261 328 gllnrvtrEVHAVEKVSFDLWPGETLSLVGESGSGKSTTGRALLRLVESQGGEIIFNGQRIDtlsPGKLqALRRDIQFIF 407
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 354 QafSLYAELSVRQNL---VLHARLFH--LPADGIPARVGEMLRRFDLE-KVADELPNDLPLGIRQRLSLAVAVIHKPEIL 427
Cdd:PRK10261 408 Q--DPYASLDPRQTVgdsIMEPLRVHglLPGKAAAARVAWLLERVGLLpEHAWRYPHEFSGGQRQRICIARALALNPKVI 485
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*...
gi 15600424 428 ILDEPTSGVDPVARDGFWELMVELSRRDGVTIFISTHFMNEAQRCD-RISLMHAGKVL 484
Cdd:PRK10261 486 IADEAVSALDVSIRGQIINLLLDLQRDFGIAYLFISHDMAVVERIShRVAVMYLGQIV 543
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
289-481 |
7.11e-27 |
|
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: 118.96 E-value: 7.11e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 289 AVDHVSFRIERGEIFGFLGSNGCGKSTTMKMLTGLLPASEGTCALFGQPVDASDMATRRRVGYMSQAFSLYAELSVRQNL 368
Cdd:TIGR01257 1954 AVDRLCVGVRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAGKSILTNISDVHQNMGYCPQFDAIDDLLTGREHL 2033
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 369 VLHARLFHLPADGIPARVGEMLRRFDLEKVADELPNDLPLGIRQRLSLAVAVIHKPEILILDEPTSGVDPVARDGFWELM 448
Cdd:TIGR01257 2034 YLYARLRGVPAEEIEKVANWSIQSLGLSLYADRLAGTYSGGNKRKLSTAIALIGCPPLVLLDEPTTGMDPQARRMLWNTI 2113
|
170 180 190
....*....|....*....|....*....|....
gi 15600424 449 VELSrRDGVTIFISTHFMNEAQR-CDRISLMHAG 481
Cdd:TIGR01257 2114 VSII-REGRAVVLTSHSMEECEAlCTRLAIMVKG 2146
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
11-234 |
1.25e-26 |
|
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: 109.35 E-value: 1.25e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 11 LRGVSLRYGETRaVDDVSLEIPANRMVGLIGPDGVGKSSLLALLAGARKMQDGEIRvLDG--------DMRDrrhrravc 82
Cdd:cd03299 3 VENLSKDWKEFK-LKNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKIL-LNGkditnlppEKRD-------- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 83 prIAYMPQGlgKNLYPTLSVFENVDFFGRLFGHDKAERERRIADLLQSTGLAPFAERPAGKLSGGMKQKLGLCCALIHDP 162
Cdd:cd03299 73 --ISYVPQN--YALFPHMTVYKNIAYGLKKRKVDKKEIERKVLEIAEMLGIDHLLNRKPETLSGGEQQRVAIARALVVNP 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15600424 163 DLLILDEPTTGVDPLSRNQFWELIGRIRAgREGMSVLVATAYMEEAERF-DWLVAMDDGKVLATGTPQELRER 234
Cdd:cd03299 149 KILLLDEPFSALDVRTKEKLREELKKIRK-EFGVTVLHVTHDFEEAWALaDKVAIMLNGKLIQVGKPEEVFKK 220
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
275-494 |
1.39e-26 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 114.88 E-value: 1.39e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 275 IEAEGLTCRFGDFVAVDHVSFRIERGEIFGFLGSNGCGKSTTMKMLTGLLPASEGTCALFGQPVDASD--MATRRRVGYM 352
Cdd:PRK09700 6 ISMAGIGKSFGPVHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNINYNKLDhkLAAQLGIGII 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 353 SQAFSLYAELSVRQNLVLhARLFHLPADGIP--------ARVGEMLRRFDLEKVADELPNDLPLGIRQRLSLAVAVIHKP 424
Cdd:PRK09700 86 YQELSVIDELTVLENLYI-GRHLTKKVCGVNiidwremrVRAAMMLLRVGLKVDLDEKVANLSISHKQMLEIAKTLMLDA 164
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15600424 425 EILILDEPTSGVDPVARDGFWELMVELsRRDGVTIFISTHFMNEAQR-CDRISLMHAGKVLASD-----TPDELVR 494
Cdd:PRK09700 165 KVIIMDEPTSSLTNKEVDYLFLIMNQL-RKEGTAIVYISHKLAEIRRiCDRYTVMKDGSSVCSGmvsdvSNDDIVR 239
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
11-226 |
1.53e-26 |
|
ATP-binding cassette domain of the thiamine transport system; Part of the binding-protein-dependent transport system tbpA-thiPQ for thiamine and TPP. Probably responsible for the translocation of thiamine across the membrane. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213265 [Multi-domain] Cd Length: 211 Bit Score: 108.35 E-value: 1.53e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 11 LRGVSLRYGETRAvdDVSLEIPANRMVGLIGPDGVGKSSLLALLAGARKMQDGEIrVLDGdmRDRRHRRAVCPRIAYMPQ 90
Cdd:cd03298 3 LDKIRFSYGEQPM--HFDLTFAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRV-LING--VDVTAAPPADRPVSMLFQ 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 91 GlgKNLYPTLSVFENVDFfGRLFG-HDKAERERRIADLLQSTGLAPFAERPAGKLSGGMKQKLGLCCALIHDPDLLILDE 169
Cdd:cd03298 78 E--NNLFAHLTVEQNVGL-GLSPGlKLTAEDRQAIEVALARVGLAGLEKRLPGELSGGERQRVALARVLVRDKPVLLLDE 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 15600424 170 PTTGVDPLSRNQFWELIGRIRAGReGMSVLVATAYMEEAER-FDWLVAMDDGKVLATG 226
Cdd:cd03298 155 PFAALDPALRAEMLDLVLDLHAET-KMTVLMVTHQPEDAKRlAQRVVFLDNGRIAAQG 211
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
273-493 |
2.03e-26 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 109.70 E-value: 2.03e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 273 IAIEAEGLTCRFGDFV--AVDHVSFRIERGEIFGFLGSNGCGKSTTMKMLTGLLPASEGTCALFGQPVDASDMA-TRRRV 349
Cdd:PRK13632 6 VMIKVENVSFSYPNSEnnALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIDGITISKENLKeIRKKI 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 350 GYMSQ---------------AFSLyaelsvrQNLvlharlfHLPADGIPARVGEMLRRFDLEKVADELPNDLPLGIRQRL 414
Cdd:PRK13632 86 GIIFQnpdnqfigatveddiAFGL-------ENK-------KVPPKKMKDIIDDLAKKVGMEDYLDKEPQNLSGGQKQRV 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 415 SLAVAVIHKPEILILDEPTSGVDPVARDGFWELMVELsRRDGVTIFIS-THFMNEAQRCDRISLMHAGKVLASDTPDELV 493
Cdd:PRK13632 152 AIASVLALNPEIIIFDESTSMLDPKGKREIKKIMVDL-RKTRKKTLISiTHDMDEAILADKVIVFSEGKLIAQGKPKEIL 230
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
267-502 |
2.22e-26 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 111.75 E-value: 2.22e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 267 SEGApRIAIEAEGLTCRFGDFVAVDHVSFRIERGEIFGFLGSNGCGKSTtmkmltGLLPASEGTCALFGQPVD-----AS 341
Cdd:NF000106 7 SNGA-RNAVEVRGLVKHFGEVKAVDGVDLDVREGTVLGVLGP*GAA**R------GALPAHV*GPDAGRRPWRf*twcAN 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 342 DMATRRRVG-YMSQAFSLYAELSVRQNLVLHARLFHLPADGIPARVGEMLRRFDLEKVADELPNDLPLGIRQRLSLAVAV 420
Cdd:NF000106 80 RRALRRTIG*HRPVR*GRRESFSGRENLYMIGR*LDLSRKDARARADELLERFSLTEAAGRAAAKYSGGMRRRLDLAASM 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 421 IHKPEILILDEPTSGVDPVARDGFWELMVELSrRDGVTIFISTHFMNEA-QRCDRISLMHAGKVLASDTPDELVRQRGLP 499
Cdd:NF000106 160 IGRPAVLYLDEPTTGLDPRTRNEVWDEVRSMV-RDGATVLLTTQYMEEAeQLAHELTVIDRGRVIADGKVDELKTKVGGR 238
|
...
gi 15600424 500 TLE 502
Cdd:NF000106 239 TLQ 241
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
282-487 |
2.28e-26 |
|
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: 108.00 E-value: 2.28e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 282 CRFGDFVAVDHVSFRIERGEIFGFLGSNGCGKSTTMKMLTGLLPASEGTCALFGQPVDASDMATrrrvgymsqafSLYAE 361
Cdd:cd03220 30 GEVGEFWALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVTVRGRVSSLLGLGG-----------GFNPE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 362 LSVRQNLVLHARLFHLPADGIPARVGEMLRRFDLEKVAdelpnDLPL-----GIRQRLSLAVAVIHKPEILILDEPTSGV 436
Cdd:cd03220 99 LTGRENIYLNGRLLGLSRKEIDEKIDEIIEFSELGDFI-----DLPVktyssGMKARLAFAIATALEPDILLIDEVLAVG 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 15600424 437 DPVARDGFWELMVELsRRDGVTIFISTHFMNEAQR-CDRISLMHAGKVLASD 487
Cdd:cd03220 174 DAAFQEKCQRRLREL-LKQGKTVILVSHDPSSIKRlCDRALVLEKGKIRFDG 224
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
275-483 |
2.40e-26 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 111.43 E-value: 2.40e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 275 IEAEGLTCRF----GDFVAVDHVSFRIERGEIFGFLGSNGCGKSTTMKMLTGLLPASEGTCALFGQPV---DASDM-ATR 346
Cdd:PRK11153 2 IELKNISKVFpqggRTIHALNNVSLHIPAGEIFGVIGASGAGKSTLIRCINLLERPTSGRVLVDGQDLtalSEKELrKAR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 347 RRVGYMSQAFSLYAELSVRQNLVLHARLFHLPADGIPARVGEMLRRFDLEKVADELPNDLPLGIRQRLSLAVAVIHKPEI 426
Cdd:PRK11153 82 RQIGMIFQHFNLLSSRTVFDNVALPLELAGTPKAEIKARVTELLELVGLSDKADRYPAQLSGGQKQRVAIARALASNPKV 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 15600424 427 LILDEPTSGVDPVARDGFWELMVELSRRDGVTIFISTHFMNEAQR-CDRISLMHAGKV 483
Cdd:PRK11153 162 LLCDEATSALDPATTRSILELLKDINRELGLTIVLITHEMDVVKRiCDRVAVIDAGRL 219
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
17-212 |
2.63e-26 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 106.93 E-value: 2.63e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 17 RYGETRAVDDVSLEIPANRMVGLIGPDGVGKSSLLALLAGARKMQDGEIRVLDGDmrdrrhrravcpRIAYMPQGLGKNL 96
Cdd:NF040873 1 GYGGRPVLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTVRRAGGA------------RVAYVPQRSEVPD 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 97 YPTLSVFENVD--FFGR--LFGHDKAERERRIADLLQSTGLAPFAERPAGKLSGGMKQKLGLCCALIHDPDLLILDEPTT 172
Cdd:NF040873 69 SLPLTVRDLVAmgRWARrgLWRRLTRDDRAAVDDALERVGLADLAGRQLGELSGGQRQRALLAQGLAQEADLLLLDEPTT 148
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 15600424 173 GVDPLSRNQFWELIGRIRAgrEGMSVLVATAYMEEAERFD 212
Cdd:NF040873 149 GLDAESRERIIALLAEEHA--RGATVVVVTHDLELVRRAD 186
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
277-493 |
4.60e-26 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 107.67 E-value: 4.60e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 277 AEGLTCRFGDFVAVDHVSFRIERGEIFGFLGSNGCGKSTTMKMLTGLLPASEGTCAlfgqpVDASDMA-------TRRRV 349
Cdd:PRK10895 6 AKNLAKAYKGRRVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNII-----IDDEDISllplharARRGI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 350 GYMSQAFSLYAELSVRQNL--VLHARLfHLPADGIPARVGEMLRRFDLEKVADELPNDLPLGIRQRLSLAVAVIHKPEIL 427
Cdd:PRK10895 81 GYLPQEASIFRRLSVYDNLmaVLQIRD-DLSAEQREDRANELMEEFHIEHLRDSMGQSLSGGERRRVEIARALAANPKFI 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15600424 428 ILDEPTSGVDPVARDGFWELMVELsRRDGVTIFISTHFMNEA-QRCDRISLMHAGKVLASDTPDELV 493
Cdd:PRK10895 160 LLDEPFAGVDPISVIDIKRIIEHL-RDSGLGVLITDHNVRETlAVCERAYIVSQGHLIAHGTPTEIL 225
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
274-505 |
5.98e-26 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 108.28 E-value: 5.98e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 274 AIEAEGLTCRFGDFV-AVDHVSFRIERGEIFGFLGSNGCGKSTTMKMLTGLLPASEGTCALFGQPVDASDMA-TRRRVGY 351
Cdd:PRK13647 4 IIEVEDLHFRYKDGTkALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGREVNAENEKwVRSKVGL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 352 M-----SQAFSLyaelSVRQNLVLHARLFHLPADGIPARVGEMLRRFDLEKVADELPNDLPLGIRQRLSLAVAVIHKPEI 426
Cdd:PRK13647 84 VfqdpdDQVFSS----TVWDDVAFGPVNMGLDKDEVERRVEEALKAVRMWDFRDKPPYHLSYGQKKRVAIAGVLAMDPDV 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 427 LILDEPTSGVDPVARDGFWELMVELSRRdGVTIFISTHFMN-EAQRCDRISLMHAGKVLASDTP-----DELVRQRGL-- 498
Cdd:PRK13647 160 IVLDEPMAYLDPRGQETLMEILDRLHNQ-GKTVIVATHDVDlAAEWADQVIVLKEGRVLAEGDKslltdEDIVEQAGLrl 238
|
....*..
gi 15600424 499 PTLEATF 505
Cdd:PRK13647 239 PLVAQIF 245
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
11-208 |
6.03e-26 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 107.86 E-value: 6.03e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 11 LRGVSLRYGETRAVDDVSLEIPANRMVGLIGPDGVGKSSLLALLAGARKMQDGEIRVLDGDMRDRRHRRAVcpriAYMPQ 90
Cdd:PRK11248 4 ISHLYADYGGKPALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDGKPVEGPGAERGV----VFQNE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 91 GLgknlYPTLSVFENVDFFGRLFGHDKAERERRIADLLQSTGLAPFAERPAGKLSGGMKQKLGLCCALIHDPDLLILDEP 170
Cdd:PRK11248 80 GL----LPWRNVQDNVAFGLQLAGVEKMQRLEIAHQMLKKVGLEGAEKRYIWQLSGGQRQRVGIARALAANPQLLLLDEP 155
|
170 180 190
....*....|....*....|....*....|....*...
gi 15600424 171 TTGVDPLSRNQFWELIGRIRAgREGMSVLVATAYMEEA 208
Cdd:PRK11248 156 FGALDAFTREQMQTLLLKLWQ-ETGKQVLLITHDIEEA 192
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
283-502 |
9.44e-26 |
|
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: 109.82 E-value: 9.44e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 283 RFGDFvAVDhVSFRIERGEIFGFLGSNGCGKSTTMKMLTGLLPASEGTCALFGQPVDASDM-----ATRRRVGYMSQAFS 357
Cdd:TIGR02142 8 RLGDF-SLD-ADFTLPGQGVTAIFGRSGSGKTTLIRLIAGLTRPDEGEIVLNGRTLFDSRKgiflpPEKRRIGYVFQEAR 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 358 LYAELSVRQNLVlHARLFHLPADGI--PARVGEMLrrfDLEKVADELPNDLPLGIRQRLSLAVAVIHKPEILILDEPTSG 435
Cdd:TIGR02142 86 LFPHLSVRGNLR-YGMKRARPSERRisFERVIELL---GIGHLLGRLPGRLSGGEKQRVAIGRALLSSPRLLLMDEPLAA 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15600424 436 VDPVARDGFWELMVELSRRDGVTIFISTHFMNEAQR-CDRISLMHAGKVLASDTPDELVRQRGLPTLE 502
Cdd:TIGR02142 162 LDDPRKYEILPYLERLHAEFGIPILYVSHSLQEVLRlADRVVVLEDGRVAAAGPIAEVWASPDLPWLA 229
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
11-496 |
1.71e-25 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 111.56 E-value: 1.71e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 11 LRGVSLRYGETRAVDDVSLEIPANRMVGLIGPDGVGKSSLLALLAGA--RKMQDGEIRVLDGDMRDRRHRRAVCPRIAYM 88
Cdd:PRK13549 8 MKNITKTFGGVKALDNVSLKVRAGEIVSLCGENGAGKSTLMKVLSGVypHGTYEGEIIFEGEELQASNIRDTERAGIAII 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 89 PQGLgkNLYPTLSVFENVdFFGRLFGH----DKAERERRIADLLQSTGLAPFAERPAGKLSGGMKQKLGLCCALIHDPDL 164
Cdd:PRK13549 88 HQEL--ALVKELSVLENI-FLGNEITPggimDYDAMYLRAQKLLAQLKLDINPATPVGNLGLGQQQLVEIAKALNKQARL 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 165 LILDEPTTgvdPLSRNQFWELIGRIRAGREGMsvlVATAYM-----EEAERFDWLVAMDDGKVLATGTPQELRE-RTGTQ 238
Cdd:PRK13549 165 LILDEPTA---SLTESETAVLLDIIRDLKAHG---IACIYIshklnEVKAISDTICVIRDGRHIGTRPAAGMTEdDIITM 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 239 SLESAFIALLPEskraghhrlvippRPQSEGapRIAIEAEGLTCRfgDFV-----AVDHVSFRIERGEIFGFLGSNGCGK 313
Cdd:PRK13549 239 MVGRELTALYPR-------------EPHTIG--EVILEVRNLTAW--DPVnphikRVDDVSFSLRRGEILGIAGLVGAGR 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 314 STTMKMLTGLLP-ASEGTCALFGQPVD--ASDMATRRRVGYMSQ---AFSLYAELSVRQNLVL-----HARLFHLPADGI 382
Cdd:PRK13549 302 TELVQCLFGAYPgRWEGEIFIDGKPVKirNPQQAIAQGIAMVPEdrkRDGIVPVMGVGKNITLaaldrFTGGSRIDDAAE 381
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 383 PARVGEMLRRFDLEKVADELP-NDLPLGIRQRLSLAVAVIHKPEILILDEPTSGVDPVARDGFWELMVELSRRDGVTIFI 461
Cdd:PRK13549 382 LKTILESIQRLKVKTASPELAiARLSGGNQQKAVLAKCLLLNPKILILDEPTRGIDVGAKYEIYKLINQLVQQGVAIIVI 461
|
490 500 510
....*....|....*....|....*....|....*
gi 15600424 462 STHFMNEAQRCDRISLMHAGKVLASDTPDELVRQR 496
Cdd:PRK13549 462 SSELPEVLGLSDRVLVMHEGKLKGDLINHNLTQEQ 496
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
11-236 |
2.00e-25 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 112.18 E-value: 2.00e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 11 LRGVSLRYGETRAV-DDVSLEIPANRMVGLIGPDGVGKSSLLALLAGARKMQDGEIRVlDG-DMRD------RRHrravc 82
Cdd:COG1132 342 FENVSFSYPGDRPVlKDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYDPTSGRILI-DGvDIRDltleslRRQ----- 415
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 83 prIAYMPQGlgknlyPTL---SVFENVdffgrLFGHDKAERErRIADLLQSTGLAPFAER-PAG----------KLSGGM 148
Cdd:COG1132 416 --IGVVPQD------TFLfsgTIRENI-----RYGRPDATDE-EVEEAAKAAQAHEFIEAlPDGydtvvgergvNLSGGQ 481
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 149 KQKLGLCCALIHDPDLLILDEPTTGVDPLSRNQFWELIGRIRAGRegMSVLVA----TaymeeAERFDWLVAMDDGKVLA 224
Cdd:COG1132 482 RQRIAIARALLKDPPILILDEATSALDTETEALIQEALERLMKGR--TTIVIAhrlsT-----IRNADRILVLDDGRIVE 554
|
250
....*....|..
gi 15600424 225 TGTPQELRERTG 236
Cdd:COG1132 555 QGTHEELLARGG 566
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
274-484 |
2.00e-25 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 106.46 E-value: 2.00e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 274 AIEAEGLTCRFGDFVAVDHVSFRIERGEIFGFLGSNGCGKSTTMKMLTGLLPAS-----EGTCALFGQPVDASDM---AT 345
Cdd:PRK14267 4 AIETVNLRVYYGSNHVIKGVDLKIPQNGVFALMGPSGCGKSTLLRTFNRLLELNeearvEGEVRLFGRNIYSPDVdpiEV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 346 RRRVGYMSQAFSLYAELSVRQNLVLHARLFHL--PADGIPARVGEMLRRFDL-EKVADEL---PNDLPLGIRQRLSLAVA 419
Cdd:PRK14267 84 RREVGMVFQYPNPFPHLTIYDNVAIGVKLNGLvkSKKELDERVEWALKKAALwDEVKDRLndyPSNLSGGQRQRLVIARA 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15600424 420 VIHKPEILILDEPTSGVDPVARDGFWELMVELsrRDGVTIFISTHFMNEAQR-CDRISLMHAGKVL 484
Cdd:PRK14267 164 LAMKPKILLMDEPTANIDPVGTAKIEELLFEL--KKEYTIVLVTHSPAQAARvSDYVAFLYLGKLI 227
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
10-199 |
2.46e-25 |
|
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid transport and metabolism, Inorganic ion transport and metabolism];
Pssm-ID: 440213 [Multi-domain] Cd Length: 320 Bit Score: 107.83 E-value: 2.46e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 10 SLRGVSLRY----GETRAVDDVSLEIPANRMVGLIGPDGVGKS----SLLALLAGARKMqDGEIRvLDG----DMRDRRH 77
Cdd:COG0444 3 EVRNLKVYFptrrGVVKAVDGVSFDVRRGETLGLVGESGSGKStlarAILGLLPPPGIT-SGEIL-FDGedllKLSEKEL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 78 RRAVCPRIAYMPQGLGKNLYPTLSVFENVDFFGRLFGH-DKAERERRIADLLQSTGLaPFAERPAGK----LSGGMKQKL 152
Cdd:COG0444 81 RKIRGREIQMIFQDPMTSLNPVMTVGDQIAEPLRIHGGlSKAEARERAIELLERVGL-PDPERRLDRypheLSGGMRQRV 159
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 15600424 153 GLCCALIHDPDLLILDEPTTGVDPLSRNQFWELIGRIRAgREGMSVL 199
Cdd:COG0444 160 MIARALALEPKLLIADEPTTALDVTIQAQILNLLKDLQR-ELGLAIL 205
|
|
| LolD_lipo_ex |
TIGR02211 |
lipoprotein releasing system, ATP-binding protein; This model represents LolD, a member of the ... |
275-483 |
3.45e-25 |
|
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: 104.74 E-value: 3.45e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 275 IEAEGLTCRF--GDF--VAVDHVSFRIERGEIFGFLGSNGCGKSTTMKMLTGLLPASEGTCALFGQPVDA---SDMATRR 347
Cdd:TIGR02211 2 LKCENLGKRYqeGKLdtRVLKGVSLSIGKGEIVAIVGSSGSGKSTLLHLLGGLDNPTSGEVLFNGQSLSKlssNERAKLR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 348 --RVGYMSQAFSLYAELSVRQNLVLHARLFHLPADGIPARVGEMLRRFDLEKVADELPNDLPLGIRQRLSLAVAVIHKPE 425
Cdd:TIGR02211 82 nkKLGFIYQFHHLLPDFTALENVAMPLLIGKKSVKEAKERAYEMLEKVGLEHRINHRPSELSGGERQRVAIARALVNQPS 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 15600424 426 ILILDEPTSGVDPVARDGFWELMVELSRRDGVTIFISTHFMNEAQRCDRISLMHAGKV 483
Cdd:TIGR02211 162 LVLADEPTGNLDNNNAKIIFDLMLELNRELNTSFLVVTHDLELAKKLDRVLEMKDGQL 219
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
23-237 |
4.04e-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: 113.18 E-value: 4.04e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 23 AVDDVSLEIPANRMVGLIGPDGVGKSSLLALLAGARKMQDGEIRVLDGDMRDR----RHRRAVCPRiaympqglGKNLYP 98
Cdd:TIGR01257 945 AVDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGKDIETNldavRQSLGMCPQ--------HNILFH 1016
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 99 TLSVFENVDFFGRLFGHDKAERERRIADLLQSTGLAPFAERPAGKLSGGMKQKLGLCCALIHDPDLLILDEPTTGVDPLS 178
Cdd:TIGR01257 1017 HLTVAEHILFYAQLKGRSWEEAQLEMEAMLEDTGLHHKRNEEAQDLSGGMQRKLSVAIAFVGDAKVVVLDEPTSGVDPYS 1096
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 179 RNQFWELIGRIRAGRegmSVLVATAYMEEAERF-DWLVAMDDGKVLATGTPQELRERTGT 237
Cdd:TIGR01257 1097 RRSIWDLLLKYRSGR---TIIMSTHHMDEADLLgDRIAIISQGRLYCSGTPLFLKNCFGT 1153
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
8-210 |
4.90e-25 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 105.12 E-value: 4.90e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 8 VASLRGVSLRYGETRAVDDVSLEIPANRMVGLIGPDGVGKSSLL-------ALLAGARkmQDGEIRVLDGDMRDRR---- 76
Cdd:COG1117 11 KIEVRNLNVYYGDKQALKDINLDIPENKVTALIGPSGCGKSTLLrclnrmnDLIPGAR--VEGEILLDGEDIYDPDvdvv 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 77 -HRRavcpRIAYMPQglgK-NLYPTlSVFENVDFFGRLFG-HDKAERERRIADLLQSTGLapFAE------RPAGKLSGG 147
Cdd:COG1117 89 eLRR----RVGMVFQ---KpNPFPK-SIYDNVAYGLRLHGiKSKSELDEIVEESLRKAAL--WDEvkdrlkKSALGLSGG 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15600424 148 MKQKLglcC---ALIHDPDLLILDEPTTGVDPLSRNQFWELIGRIragREGMSVLVATAYMEEAER 210
Cdd:COG1117 159 QQQRL---CiarALAVEPEVLLMDEPTSALDPISTAKIEELILEL---KKDYTIVIVTHNMQQAAR 218
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
288-493 |
6.89e-25 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 108.20 E-value: 6.89e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 288 VAVDHVSFRIERGEIFGFLGSNGCGKSTTMKMLTGLLPASEGTCALFGqpVDASDMAT-------RRRVGYMSQAFSLYA 360
Cdd:PRK10070 42 LGVKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDG--VDIAKISDaelrevrRKKIAMVFQSFALMP 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 361 ELSVRQNLVLHARLFHLPADGIPARVGEMLRRFDLEKVADELPNDLPLGIRQRLSLAVAVIHKPEILILDEPTSGVDPVA 440
Cdd:PRK10070 120 HMTVLDNTAFGMELAGINAEERREKALDALRQVGLENYAHSYPDELSGGMRQRVGLARALAINPDILLMDEAFSALDPLI 199
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 15600424 441 RDGFWELMVELSRRDGVTIFISTHFMNEAQRC-DRISLMHAGKVLASDTPDELV 493
Cdd:PRK10070 200 RTEMQDELVKLQAKHQRTIVFISHDLDEAMRIgDRIAIMQNGEVVQVGTPDEIL 253
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
289-485 |
7.02e-25 |
|
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic bacteriocins of lactic acid bacteria are produced as precursors which have N-terminal leader peptides that share similarities in amino acid sequence and contain a conserved processing site of two glycine residues in positions -1 and -2. A dedicated ATP-binding cassette (ABC) transporter is responsible for the proteolytic cleavage of the leader peptides and subsequent translocation of the bacteriocins across the cytoplasmic membrane.
Pssm-ID: 213212 [Multi-domain] Cd Length: 220 Bit Score: 103.82 E-value: 7.02e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 289 AVDHVSFRIERGEIFGFLGSNGCGKSTTMKMLTGLLPASEGTCALFGQPVDASDMAT-RRRVGYMSQAFSLYAElSVRQN 367
Cdd:cd03245 19 ALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGTDIRQLDPADlRRNIGYVPQDVTLFYG-TLRDN 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 368 LVlharLFHLPADGipARVGEMLRRFDLEKVADELPNDLPL-----------GIRQRLSLAVAVIHKPEILILDEPTSGV 436
Cdd:cd03245 98 IT----LGAPLADD--ERILRAAELAGVTDFVNKHPNGLDLqigergrglsgGQRQAVALARALLNDPPILLLDEPTSAM 171
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 15600424 437 DPVARDGFWELMVELSRrdGVTIFISTHFMNEAQRCDRISLMHAGKVLA 485
Cdd:cd03245 172 DMNSEERLKERLRQLLG--DKTLIIITHRPSLLDLVDRIIVMDSGRIVA 218
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
10-231 |
8.29e-25 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 105.10 E-value: 8.29e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 10 SLRGVSLRYGET--RAVDDVSLEIPANRMVGLIGPDGVGKSSLLALLAGARKMQDGEIRVlDGDMRDRRH----RRAVcp 83
Cdd:PRK13635 7 RVEHISFRYPDAatYALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITV-GGMVLSEETvwdvRRQV-- 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 84 riaympqGLgknlyptlsVFENVD--FFGRLFGHDKA--------ERE---RRIADLLQSTGLAPFAERPAGKLSGGMKQ 150
Cdd:PRK13635 84 -------GM---------VFQNPDnqFVGATVQDDVAfglenigvPREemvERVDQALRQVGMEDFLNREPHRLSGGQKQ 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 151 KLGLCCALIHDPDLLILDEPTTGVDPLSRNQFWELIGRIRAgREGMSVLVATAYMEEAERFDWLVAMDDGKVLATGTPQE 230
Cdd:PRK13635 148 RVAIAGVLALQPDIIILDEATSMLDPRGRREVLETVRQLKE-QKGITVLSITHDLDEAAQADRVIVMNKGEILEEGTPEE 226
|
.
gi 15600424 231 L 231
Cdd:PRK13635 227 I 227
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
275-498 |
1.01e-24 |
|
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: 103.72 E-value: 1.01e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 275 IEAEGLTCRFG--DFVAVDHVSFRIERGEIFGFLGSNGCGKSTTMKMLTGLLPASEGTCAlfgqpVDASDMAT------R 346
Cdd:cd03252 1 ITFEHVRFRYKpdGPVILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVL-----VDGHDLALadpawlR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 347 RRVGYMSQAFSLYAElSVRQNLVLharlfhlpADGIPA--RVGEMLRRFDLEKVADELPN-----------DLPLGIRQR 413
Cdd:cd03252 76 RQVGVVLQENVLFNR-SIRDNIAL--------ADPGMSmeRVIEAAKLAGAHDFISELPEgydtivgeqgaGLSGGQRQR 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 414 LSLAVAVIHKPEILILDEPTSGVDPVARDGFWELMVELSrrDGVTIFISTHFMNEAQRCDRISLMHAGKVLASDTPDELV 493
Cdd:cd03252 147 IAIARALIHNPRILIFDEATSALDYESEHAIMRNMHDIC--AGRTVIIIAHRLSTVKNADRIIVMEKGRIVEQGSHDELL 224
|
....*
gi 15600424 494 RQRGL 498
Cdd:cd03252 225 AENGL 229
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
275-492 |
1.08e-24 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 104.79 E-value: 1.08e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 275 IEAEGLTCRF---GDFVAVDHVSFRIERGEIFGFLGSNGCGKSTTMKMLTGLLPASEGTCALFGQPVDASDMAT-RRRVG 350
Cdd:PRK13642 5 LEVENLVFKYekeSDVNQLNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDGELLTAENVWNlRRKIG 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 351 YMSQ-AFSLYAELSVRQNLVLHARLFHLPADGIPARVGEMLRRFDLEKVADELPNDLPLGIRQRLSLAVAVIHKPEILIL 429
Cdd:PRK13642 85 MVFQnPDNQFVGATVEDDVAFGMENQGIPREEMIKRVDEALLAVNMLDFKTREPARLSGGQKQRVAVAGIIALRPEIIIL 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15600424 430 DEPTSGVDPVARDGFWELMVELSRRDGVTIFISTHFMNEAQRCDRISLMHAGKVLASDTPDEL 492
Cdd:PRK13642 165 DESTSMLDPTGRQEIMRVIHEIKEKYQLTVLSITHDLDEAASSDRILVMKAGEIIKEAAPSEL 227
|
|
| anch_rpt_ABC |
TIGR03771 |
anchored repeat-type ABC transporter, ATP-binding subunit; This protein family is the ... |
295-492 |
1.14e-24 |
|
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: 103.39 E-value: 1.14e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 295 FRIERGEIFGFLGSNGCGKSTTMKMLTGLLPASEGTCALFGQPVDASdmatRRRVGYMSQ--AFSLYAELSVRQnLVLHA 372
Cdd:TIGR03771 1 LSADKGELLGLLGPNGAGKTTLLRAILGLIPPAKGTVKVAGASPGKG----WRHIGYVPQrhEFAWDFPISVAH-TVMSG 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 373 R-----LFHLPADGIPARVGEMLRRFDLEKVADELPNDLPLGIRQRLSLAVAVIHKPEILILDEPTSGVDPVARDGFWEL 447
Cdd:TIGR03771 76 RtghigWLRRPCVADFAAVRDALRRVGLTELADRPVGELSGGQRQRVLVARALATRPSVLLLDEPFTGLDMPTQELLTEL 155
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 15600424 448 MVELSrRDGVTIFISTHFMNEA-QRCDRISLMHaGKVLASDTPDEL 492
Cdd:TIGR03771 156 FIELA-GAGTAILMTTHDLAQAmATCDRVVLLN-GRVIADGTPQQL 199
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
10-217 |
1.17e-24 |
|
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family transporter in which each gene contains an N-terminal membrane-spanning domain (pfam00664) and a C-terminal ATP-binding domain (pfam00005). In E. coli these genes were discovered as mutants which caused the terminal heme-copper oxidase complex cytochrome bd to fail to assemble. Recent work has shown that the transporter is involved in export of redox-active thiol compounds such as cysteine and glutathione. The linkage to assembly of the cytochrome bd complex is further supported by the conserved operon structure found outside the gammaproteobacteria (cydABCD) containing both the transporter and oxidase genes components. The genes used as the seed members for this model are all either found in the gammproteobacterial context or the CydABCD context. All members of this family scoring above trusted at the time of its creation were from genomes which encode a cytochrome bd complex. Unfortunately, the gene symbol nomenclature adopted based on this operon in B. subtilis assigns cydC to the third gene in the operon where this gene is actually homologous to the E. coli cydD gene. We have chosen to name all homologs in this family in accordance with the precedence of publication of the E. coli name, CydD
Pssm-ID: 274323 [Multi-domain] Cd Length: 529 Bit Score: 109.30 E-value: 1.17e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 10 SLRGVSLRY-GETRAVDDVSLEIPANRMVGLIGPDGVGKSSLLALLAGARKMQDGEIRVLDGDMR--DRRHRRAvcpRIA 86
Cdd:TIGR02857 323 EFSGVSVAYpGRRPALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSIAVNGVPLAdaDADSWRD---QIA 399
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 87 YMPQglgknlYPTL---SVFENVdffgRLFGHDKAERErrIADLLQSTGLAPF-AERPAG----------KLSGGMKQKL 152
Cdd:TIGR02857 400 WVPQ------HPFLfagTIAENI----RLARPDASDAE--IREALERAGLDEFvAALPQGldtpigeggaGLSGGQAQRL 467
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15600424 153 GLCCALIHDPDLLILDEPTTGVDPLSRNqfwELIGRIRAGREGMSVLVATAYMEEAERFDWLVAM 217
Cdd:TIGR02857 468 ALARAFLRDAPLLLLDEPTAHLDAETEA---EVLEALRALAQGRTVLLVTHRLALAALADRIVVL 529
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
289-497 |
1.19e-24 |
|
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan exporter ATP-binding protein. In A. tumefaciens cyclic beta-1, 2-glucan must be transported into the periplasmic space to exert its action as a virulence factor. This subfamily belongs to the MRP-like family and is involved in drug, peptide, and lipid export. The MRP-like family, similar to all ABC proteins, have a common four-domain core structure constituted by two membrane-spanning domains each composed of six transmembrane (TM) helices and two nucleotide-binding domains (NBD). ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213221 [Multi-domain] Cd Length: 229 Bit Score: 103.46 E-value: 1.19e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 289 AVDHVSFRIERGEIFGFLGSNGCGKSTTMKMLTGLLPASEGTCALFGQPVDASDMAT-RRRVGYMSQAFSLYAElSVRQN 367
Cdd:cd03254 18 VLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGIDIRDISRKSlRSMIGVVLQDTFLFSG-TIMEN 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 368 LvlhaRLFHLPADgiPARVGEMLRRFDLEKVADELPN-----------DLPLGIRQRLSLAVAVIHKPEILILDEPTSGV 436
Cdd:cd03254 97 I----RLGRPNAT--DEEVIEAAKEAGAHDFIMKLPNgydtvlgenggNLSQGERQLLAIARAMLRDPKILILDEATSNI 170
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15600424 437 DPVA----RDGFWELMvelsrrDGVTIFISTHFMNEAQRCDRISLMHAGKVLASDTPDELVRQRG 497
Cdd:cd03254 171 DTETekliQEALEKLM------KGRTSIIIAHRLSTIKNADKILVLDDGKIIEEGTHDELLAKKG 229
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
8-222 |
1.44e-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: 101.74 E-value: 1.44e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 8 VASLRGVSLRygetRAVDDVSLEIPANRMVGLIGPDGVGKSSLLALLAGARKMQDGEIRVLDGDMRDRRHRRAVCPRIAY 87
Cdd:cd03215 4 VLEVRGLSVK----GAVRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITLDGKPVTRRSPRDAIRAGIAY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 88 MP---QGLGknLYPTLSVFENVdFFGRLfghdkaererriadllqstglapfaerpagkLSGGMKQKLGLCCALIHDPDL 164
Cdd:cd03215 80 VPedrKREG--LVLDLSVAENI-ALSSL-------------------------------LSGGNQQKVVLARWLARDPRV 125
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 15600424 165 LILDEPTTGVDPLSRNQFWELIGRIRAgrEGMSVLVATAYMEEAERF-DWLVAMDDGKV 222
Cdd:cd03215 126 LILDEPTRGVDVGAKAEIYRLIRELAD--AGKAVLLISSELDELLGLcDRILVMYEGRI 182
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
16-226 |
1.45e-24 |
|
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: 103.00 E-value: 1.45e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 16 LRYGETRAVDDVSLEIPANRMVGLIGPDGVGKSSLLALLAGARKMQDGEIRVldgdmrdrrhRRAVCPRIaympqGLGKN 95
Cdd:cd03220 30 GEVGEFWALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVTV----------RGRVSSLL-----GLGGG 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 96 LYPTLSVFENVDFFGRLFGHDKAERERRIADLLQSTGLAPFAERPAGKLSGGMKQKLGLCCALIHDPDLLILDEPTTGVD 175
Cdd:cd03220 95 FNPELTGRENIYLNGRLLGLSRKEIDEKIDEIIEFSELGDFIDLPVKTYSSGMKARLAFAIATALEPDILLIDEVLAVGD 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 15600424 176 PLSRNQFWELIGRIRAGreGMSVLVATAYMEEAERF-DWLVAMDDGKVLATG 226
Cdd:cd03220 175 AAFQEKCQRRLRELLKQ--GKTVILVSHDPSSIKRLcDRALVLEKGKIRFDG 224
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
11-280 |
1.73e-24 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 103.60 E-value: 1.73e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 11 LRGVSLRYGETRAVDDVSLEIPANRMVGLIGPDGVGKSSLLALLAGARKMQDGEIRVLDGDMRDRRHRravcprIAYMPQ 90
Cdd:PRK11247 15 LNAVSKRYGERTVLNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAGELLAGTAPLAEARED------TRLMFQ 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 91 GlgKNLYPTLSVFENVDFfgRLFGHDKAERERriadLLQSTGLAPFA-ERPAGkLSGGMKQKLGLCCALIHDPDLLILDE 169
Cdd:PRK11247 89 D--ARLLPWKKVIDNVGL--GLKGQWRDAALQ----ALAAVGLADRAnEWPAA-LSGGQKQRVALARALIHRPGLLLLDE 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 170 PTTGVDPLSRNQFWELIGRIrAGREGMSVLVATAYMEEAerfdwlVAMDDgKVlatgtpqelrertgtqslesafiaLLP 249
Cdd:PRK11247 160 PLGALDALTRIEMQDLIESL-WQQHGFTVLLVTHDVSEA------VAMAD-RV------------------------LLI 207
|
250 260 270
....*....|....*....|....*....|..
gi 15600424 250 ESKRAGHHRLVIPPRPQSEGAPRIA-IEAEGL 280
Cdd:PRK11247 208 EEGKIGLDLTVDLPRPRRRGSARLAeLEAEVL 239
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
21-234 |
1.95e-24 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 104.05 E-value: 1.95e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 21 TRAVDDVSLEIPANRMVGLIGPDGVGKSSLLALLAGARKMQDGEIRVLdGDMRDRRHRRAVCPRIAYMPQGLGKNLYpTL 100
Cdd:PRK13647 18 TKALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVM-GREVNAENEKWVRSKVGLVFQDPDDQVF-SS 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 101 SVFENVDFFGRLFGHDKAERERRIADLLQSTGLAPFAERPAGKLSGGMKQKLGLCCALIHDPDLLILDEPTTGVDPLSRN 180
Cdd:PRK13647 96 TVWDDVAFGPVNMGLDKDEVERRVEEALKAVRMWDFRDKPPYHLSYGQKKRVAIAGVLAMDPDVIVLDEPMAYLDPRGQE 175
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 15600424 181 QFWELIGRIRagREGMSVLVATAYME-EAERFDWLVAMDDGKVLATGTPQELRER 234
Cdd:PRK13647 176 TLMEILDRLH--NQGKTVIVATHDVDlAAEWADQVIVLKEGRVLAEGDKSLLTDE 228
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
275-505 |
2.09e-24 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 106.85 E-value: 2.09e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 275 IEAEGLTCRFGDFVAVDHVSFRIERGEIFGFLGSNGCGKSTTMKMLTGLLPASEGTCALFGQPVDASDMAT-RRRVGYMS 353
Cdd:PRK09536 4 IDVSDLSVEFGDTTVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGDDVEALSARAaSRRVASVP 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 354 QAFSLYAELSVRQnLVLHARLFHL-------PADgiPARVGEMLRRFDLEKVADELPNDLPLGIRQRLSLAVAVIHKPEI 426
Cdd:PRK09536 84 QDTSLSFEFDVRQ-VVEMGRTPHRsrfdtwtETD--RAAVERAMERTGVAQFADRPVTSLSGGERQRVLLARALAQATPV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 427 LILDEPTSGVDPVARDGFWELMVELSrRDGVTIFISTHFMNEAQR-CDRISLMHAGKVLASDTPDELVRQrglPTLEATF 505
Cdd:PRK09536 161 LLLDEPTASLDINHQVRTLELVRRLV-DDGKTAVAAIHDLDLAARyCDELVLLADGRVRAAGPPADVLTA---DTLRAAF 236
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
275-498 |
2.33e-24 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 103.17 E-value: 2.33e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 275 IEAEGLTCRFGDFVAVDHVSFRIERGEIFGFLGSNGCGKSTTMKMLTGLLPASEGTCALFGQPVDA-SDMATRRRVGYMS 353
Cdd:PRK11231 3 LRTENLTVGYGTKRILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDKPISMlSSRQLARRLALLP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 354 QAFSLYAELSVRQnLVLHARLFHLP-----ADGIPARVGEMLRRFDLEKVADELPNDLPLGIRQRLSLAVAVIHKPEILI 428
Cdd:PRK11231 83 QHHLTPEGITVRE-LVAYGRSPWLSlwgrlSAEDNARVNQAMEQTRINHLADRRLTDLSGGQRQRAFLAMVLAQDTPVVL 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15600424 429 LDEPTSGVDPVARDGFWELMVELsRRDGVTIFISTHFMNEAQR-CDRISLMHAGKVLASDTPDELVRQRGL 498
Cdd:PRK11231 162 LDEPTTYLDINHQVELMRLMREL-NTQGKTVVTVLHDLNQASRyCDHLVVLANGHVMAQGTPEEVMTPGLL 231
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
8-234 |
2.61e-24 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 105.80 E-value: 2.61e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 8 VASLRGVSLRYGETRAVDDVSLEIPANRMVGLIGPDGVGKSSLLALLAGARKMQDGEIrVLDG-DMRD----RRHRRAVC 82
Cdd:PRK09452 14 LVELRGISKSFDGKEVISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRI-MLDGqDITHvpaeNRHVNTVF 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 83 PRIAympqglgknLYPTLSVFENVDFFGRLFGHDKAERERRIADLLQSTGLAPFAERPAGKLSGGMKQKLGLCCALIHDP 162
Cdd:PRK09452 93 QSYA---------LFPHMTVFENVAFGLRMQKTPAAEITPRVMEALRMVQLEEFAQRKPHQLSGGQQQRVAIARAVVNKP 163
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15600424 163 DLLILDEPTTGVDPLSRNQFWELIGRIRagRE-GMSVLVATAYMEEAERF-DWLVAMDDGKVLATGTPQELRER 234
Cdd:PRK09452 164 KVLLLDESLSALDYKLRKQMQNELKALQ--RKlGITFVFVTHDQEEALTMsDRIVVMRDGRIEQDGTPREIYEE 235
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
280-501 |
2.66e-24 |
|
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: 105.57 E-value: 2.66e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 280 LTCRFGDFvAVDhVSFRIERGEIFGFLGSNGCGKSTTMKMLTGLLPASEGTCALFGQP-VDAS---DMAT-RRRVGYMSQ 354
Cdd:COG4148 7 FRLRRGGF-TLD-VDFTLPGRGVTALFGPSGSGKTTLLRAIAGLERPDSGRIRLGGEVlQDSArgiFLPPhRRRIGYVFQ 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 355 AFSLYAELSVRQNLvLHARlfhlpadgipARVGEMLRRFDLEKVADEL---------PNDLPLGIRQRLSLAVAVIHKPE 425
Cdd:COG4148 85 EARLFPHLSVRGNL-LYGR----------KRAPRAERRISFDEVVELLgighlldrrPATLSGGERQRVAIGRALLSSPR 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 426 ILILDEPTSGVDPVARDgfwELMVELSR-RD--GVTIFISTHFMNEAQR-CDRISLMHAGKVLASDTPDELVRQRGLPTL 501
Cdd:COG4148 154 LLLMDEPLAALDLARKA---EILPYLERlRDelDIPILYVSHSLDEVARlADHVVLLEQGRVVASGPLAEVLSRPDLLPL 230
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
274-469 |
3.16e-24 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 103.02 E-value: 3.16e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 274 AIEAEGLTCRFGDFV----AVDHVSFRIERGEIFGFLGSNGCGKSTTMKMLTGLLPASEGTCALFGQPVDASDmATRrrv 349
Cdd:COG4525 3 MLTVRHVSVRYPGGGqpqpALQDVSLTIESGEFVVALGASGCGKTTLLNLIAGFLAPSSGEITLDGVPVTGPG-ADR--- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 350 GYMSQAFSLYAELSVRQNLVLHARLFHLPADGIPARVGEMLRRFDLEKVADELPNDLPLGIRQRLSLAVAVIHKPEILIL 429
Cdd:COG4525 79 GVVFQKDALLPWLNVLDNVAFGLRLRGVPKAERRARAEELLALVGLADFARRRIWQLSGGMRQRVGIARALAADPRFLLM 158
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 15600424 430 DEPTSGVDPVARDGFWELMVELSRRDGVTIFISTHFMNEA 469
Cdd:COG4525 159 DEPFGALDALTREQMQELLLDVWQRTGKGVFLITHSVEEA 198
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
262-478 |
3.60e-24 |
|
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family transporter in which each gene contains an N-terminal membrane-spanning domain (pfam00664) and a C-terminal ATP-binding domain (pfam00005). In E. coli these genes were discovered as mutants which caused the terminal heme-copper oxidase complex cytochrome bd to fail to assemble. Recent work has shown that the transporter is involved in export of redox-active thiol compounds such as cysteine and glutathione. The linkage to assembly of the cytochrome bd complex is further supported by the conserved operon structure found outside the gammaproteobacteria (cydABCD) containing both the transporter and oxidase genes components. The genes used as the seed members for this model are all either found in the gammproteobacterial context or the CydABCD context. All members of this family scoring above trusted at the time of its creation were from genomes which encode a cytochrome bd complex. Unfortunately, the gene symbol nomenclature adopted based on this operon in B. subtilis assigns cydC to the third gene in the operon where this gene is actually homologous to the E. coli cydD gene. We have chosen to name all homologs in this family in accordance with the precedence of publication of the E. coli name, CydD
Pssm-ID: 274323 [Multi-domain] Cd Length: 529 Bit Score: 107.76 E-value: 3.60e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 262 PPRPQSEGAPRIAIEAEGLTCRFGD-FVAVDHVSFRIERGEIFGFLGSNGCGKSTTMKMLTGLLPASEGTCALFGQPVDA 340
Cdd:TIGR02857 309 AGKAPVTAAPASSLEFSGVSVAYPGrRPALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSIAVNGVPLAD 388
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 341 SDMAT-RRRVGYMSQAFSLYAElSVRQNlVLHARlfhlpADGIPARVGEMLRRFDLekvaDELPNDLPLGI--------- 410
Cdd:TIGR02857 389 ADADSwRDQIAWVPQHPFLFAG-TIAEN-IRLAR-----PDASDAEIREALERAGL----DEFVAALPQGLdtpigegga 457
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15600424 411 ------RQRLSLAVAVIHKPEILILDEPTSGVDPVARDGFWELMVELSRrdGVTIFISTHFMNEAQRCDRISLM 478
Cdd:TIGR02857 458 glsggqAQRLALARAFLRDAPLLLLDEPTAHLDAETEAEVLEALRALAQ--GRTVLLVTHRLALAALADRIVVL 529
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
275-498 |
3.97e-24 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 103.34 E-value: 3.97e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 275 IEAEGLTCRF-GDFVAVDHVSFRIERGEIFGFLGSNGCGKSTTMKMLTGLLPASEGTCALFGQPVDASDM-ATRRRVGYM 352
Cdd:PRK13652 4 IETRDLCYSYsGSKEALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIRGEPITKENIrEVRKFVGLV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 353 -----SQAFSLyaelSVRQNLVLHARLFHLPADGIPARVGEMLRRFDLEKVADELPNDLPLGIRQRLSLAVAVIHKPEIL 427
Cdd:PRK13652 84 fqnpdDQIFSP----TVEQDIAFGPINLGLDEETVAHRVSSALHMLGLEELRDRVPHHLSGGEKKRVAIAGVIAMEPQVL 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15600424 428 ILDEPTSGVDPVARDGFWELMVELSRRDGVTIFISTHFMN-EAQRCDRISLMHAGKVLASDTPDELVRQRGL 498
Cdd:PRK13652 160 VLDEPTAGLDPQGVKELIDFLNDLPETYGMTVIFSTHQLDlVPEMADYIYVMDKGRIVAYGTVEEIFLQPDL 231
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
283-478 |
6.50e-24 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 100.00 E-value: 6.50e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 283 RFGDFVAVDHVSFRIERGEIFGFLGSNGCGKSTTMKMLTGLLPASEGTCAlfgqpvdasdMATRRRVGYMSQAFSLYAEL 362
Cdd:NF040873 1 GYGGRPVLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTVR----------RAGGARVAYVPQRSEVPDSL 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 363 --SVRQNLVL----HARLFHLPADGIPARVGEMLRRFDLEKVADELPNDLPLGIRQRLSLAVAVIHKPEILILDEPTSGV 436
Cdd:NF040873 71 plTVRDLVAMgrwaRRGLWRRLTRDDRAAVDDALERVGLADLAGRQLGELSGGQRQRALLAQGLAQEADLLLLDEPTTGL 150
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 15600424 437 DPVARDGFWELMVELsRRDGVTIFISTHFMNEAQRCDRISLM 478
Cdd:NF040873 151 DAESRERIIALLAEE-HARGATVVVVTHDLELVRRADPCVLL 191
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
10-231 |
7.37e-24 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 101.70 E-value: 7.37e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 10 SLRGVSLRYGETRAVDDVSLEIPANRMVGLIGPDGVGKSSLLALLAGARKMQDGEIRVLDGDMRDRRhRRAVCPRIAYMP 89
Cdd:COG4604 3 EIKNVSKRYGGKVVLDDVSLTIPKGGITALIGPNGAGKSTLLSMISRLLPPDSGEVLVDGLDVATTP-SRELAKRLAILR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 90 QGLGKNLypTLSVFENVdFFGRlFGHDK----AERERRIADLLQSTGLAPFAERPAGKLSGGMKQKlglccALI-----H 160
Cdd:COG4604 82 QENHINS--RLTVRELV-AFGR-FPYSKgrltAEDREIIDEAIAYLDLEDLADRYLDELSGGQRQR-----AFIamvlaQ 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 161 DPDLLILDEPTTGVDPL-SRnqfwELIGRIR-AGRE-GMSVLV-------ATAYMeeaerfDWLVAMDDGKVLATGTPQE 230
Cdd:COG4604 153 DTDYVLLDEPLNNLDMKhSV----QMMKLLRrLADElGKTVVIvlhdinfASCYA------DHIVAMKDGRVVAQGTPEE 222
|
.
gi 15600424 231 L 231
Cdd:COG4604 223 I 223
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
289-492 |
7.94e-24 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 102.14 E-value: 7.94e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 289 AVDHVSFRIERGEIFGFLGSNGCGKSTTMKMLTGLLPASEGTCALFGQPVDASDMA-TRRRVGYMSQ-AFSLYAELSVRQ 366
Cdd:PRK13648 24 TLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIFYNNQAITDDNFEkLRKHIGIVFQnPDNQFVGSIVKY 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 367 NLVLHARLFHLPADGIPARVGEMLRRFDLEKVADELPNDLPLGIRQRLSLAVAVIHKPEILILDEPTSGVDPVARDGFWE 446
Cdd:PRK13648 104 DVAFGLENHAVPYDEMHRRVSEALKQVDMLERADYEPNALSGGQKQRVAIAGVLALNPSVIILDEATSMLDPDARQNLLD 183
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 15600424 447 LMVELSRRDGVTIFISTHFMNEAQRCDRISLMHAGKVLASDTPDEL 492
Cdd:PRK13648 184 LVRKVKSEHNITIISITHDLSEAMEADHVIVMNKGTVYKEGTPTEI 229
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
11-231 |
1.11e-23 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 101.14 E-value: 1.11e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 11 LRGVSLRYGETRAVDDVSLEIPANRMVGLIGPDGVGKSSLLALLAGARKMQ-----DGEIrVLDG------DMRDRRHRR 79
Cdd:PRK14247 6 IRDLKVSFGQVEVLDGVNLEIPDNTITALMGPSGSGKSTLLRVFNRLIELYpearvSGEV-YLDGqdifkmDVIELRRRV 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 80 AVCPRIAympqglgkNLYPTLSVFENVDFFGRL--FGHDKAERERRIADLLQSTGL-APFAER---PAGKLSGGMKQKLG 153
Cdd:PRK14247 85 QMVFQIP--------NPIPNLSIFENVALGLKLnrLVKSKKELQERVRWALEKAQLwDEVKDRldaPAGKLSGGQQQRLC 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15600424 154 LCCALIHDPDLLILDEPTTGVDPLSRNQFWELIGRIragREGMSVLVATAYMEEAERF-DWLVAMDDGKVLATGTPQEL 231
Cdd:PRK14247 157 IARALAFQPEVLLADEPTANLDPENTAKIESLFLEL---KKDMTIVLVTHFPQQAARIsDYVAFLYKGQIVEWGPTREV 232
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
20-231 |
1.18e-23 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 101.70 E-value: 1.18e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 20 ETRAVDDVSLEIPANRMVGLIGPDGVGKSSLLALLAGARKMQDGEIRVLDGDMRDRRHRRAVCPRIAYMPQGLGKNLYPT 99
Cdd:PRK13633 22 EKLALDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVYVDGLDTSDEENLWDIRNKAGMVFQNPDNQIVAT 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 100 LsVFENVDFFGRLFGHDKAERERRIADLLQSTGLAPFAERPAGKLSGGMKQKLGLCCALIHDPDLLILDEPTTGVDPLSR 179
Cdd:PRK13633 102 I-VEEDVAFGPENLGIPPEEIRERVDESLKKVGMYEYRRHAPHLLSGGQKQRVAIAGILAMRPECIIFDEPTAMLDPSGR 180
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 15600424 180 NQFWELIGRIRaGREGMSVLVATAYMEEAERFDWLVAMDDGKVLATGTPQEL 231
Cdd:PRK13633 181 REVVNTIKELN-KKYGITIILITHYMEEAVEADRIIVMDSGKVVMEGTPKEI 231
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
12-236 |
1.41e-23 |
|
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan exporter ATP-binding protein. In A. tumefaciens cyclic beta-1, 2-glucan must be transported into the periplasmic space to exert its action as a virulence factor. This subfamily belongs to the MRP-like family and is involved in drug, peptide, and lipid export. The MRP-like family, similar to all ABC proteins, have a common four-domain core structure constituted by two membrane-spanning domains each composed of six transmembrane (TM) helices and two nucleotide-binding domains (NBD). ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213221 [Multi-domain] Cd Length: 229 Bit Score: 100.38 E-value: 1.41e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 12 RGVSLRYGETR-AVDDVSLEIPANRMVGLIGPDGVGKSSLLALLAGARKMQDGEIrVLDG-DMRDRRhRRAVCPRIAYMP 89
Cdd:cd03254 6 ENVNFSYDEKKpVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQI-LIDGiDIRDIS-RKSLRSMIGVVL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 90 QGLGknLYPTlSVFENVDFfgrlfGHDKAERERrIADLLQSTGLAPFAER----------PAGK-LSGGMKQKLGLCCAL 158
Cdd:cd03254 84 QDTF--LFSG-TIMENIRL-----GRPNATDEE-VIEAAKEAGAHDFIMKlpngydtvlgENGGnLSQGERQLLAIARAM 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15600424 159 IHDPDLLILDEPTTGVDPLSRNQFWELIGRIRAGRegmSVLVATAYMEEAERFDWLVAMDDGKVLATGTPQELRERTG 236
Cdd:cd03254 155 LRDPKILILDEATSNIDTETEKLIQEALEKLMKGR---TSIIIAHRLSTIKNADKILVLDDGKIIEEGTHDELLAKKG 229
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
293-488 |
1.57e-23 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 100.28 E-value: 1.57e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 293 VSFRIERGEIFGFLGSNGCGKSTTMKMLTGLLPASEGTCALFGQPVDASDMATR-----RRVGYMSQAFSLYAELSVRQN 367
Cdd:PRK11629 28 VSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPMSKLSSAAKaelrnQKLGFIYQFHHLLPDFTALEN 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 368 LVLHARLFHLPADGIPARVGEMLRRFDLEKVADELPNDLPLGIRQRLSLAVAVIHKPEILILDEPTSGVDPVARDGFWEL 447
Cdd:PRK11629 108 VAMPLLIGKKKPAEINSRALEMLAAVGLEHRANHRPSELSGGERQRVAIARALVNNPRLVLADEPTGNLDARNADSIFQL 187
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 15600424 448 MVELSRRDGVTIFISTHFMNEAQRCDRISLMHAGKVLASDT 488
Cdd:PRK11629 188 LGELNRLQGTAFLVVTHDLQLAKRMSRQLEMRDGRLTAELS 228
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
10-202 |
2.12e-23 |
|
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: 98.58 E-value: 2.12e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 10 SLRGVSLRYGETRAVDDVSLEIPANRMVGLIGPDGVGKSSLLALLAGARKMQDGEIRVLDGDM---RDRRHRRavcprIA 86
Cdd:TIGR01189 2 AARNLACSRGERMLFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRWNGTPLaeqRDEPHEN-----IL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 87 YMpqGLGKNLYPTLSVFENVDFFGRLFGHDkaerERRIADLLQSTGLAPFAERPAGKLSGGMKQKLGLCCALIHDPDLLI 166
Cdd:TIGR01189 77 YL--GHLPGLKPELSALENLHFWAAIHGGA----QRTIEDALAAVGLTGFEDLPAAQLSAGQQRRLALARLWLSRRPLWI 150
|
170 180 190
....*....|....*....|....*....|....*.
gi 15600424 167 LDEPTTGVDPLSRNQFWELIgRIRAGREGMsVLVAT 202
Cdd:TIGR01189 151 LDEPTTALDKAGVALLAGLL-RAHLARGGI-VLLTT 184
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
10-244 |
2.31e-23 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 103.77 E-value: 2.31e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 10 SLRGVSLRYGETRAVDDVSLEIPANRMVGLIGPDGVGKSSLLALLAGARKMQDGEIRVlDGDMRDRRHRRAVCPRIAYMP 89
Cdd:PRK09536 5 DVSDLSVEFGDTTVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLV-AGDDVEALSARAASRRVASVP 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 90 QglGKNLYPTLSVFENVDF-----FGRLFGHDKAEReRRIADLLQSTGLAPFAERPAGKLSGGMKQKLGLCCALIHDPDL 164
Cdd:PRK09536 84 Q--DTSLSFEFDVRQVVEMgrtphRSRFDTWTETDR-AAVERAMERTGVAQFADRPVTSLSGGERQRVLLARALAQATPV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 165 LILDEPTTGVDPLSRNQFWELIGRIraGREGMSVLVATAYMEEAERF-DWLVAMDDGKVLATGTPQELrerTGTQSLESA 243
Cdd:PRK09536 161 LLLDEPTASLDINHQVRTLELVRRL--VDDGKTAVAAIHDLDLAARYcDELVLLADGRVRAAGPPADV---LTADTLRAA 235
|
.
gi 15600424 244 F 244
Cdd:PRK09536 236 F 236
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
13-231 |
3.00e-23 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 102.47 E-value: 3.00e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 13 GVSLRYGETRAVDDVSLEIPANRMVGLIGPDGVGKSSLLALLAGARKMQDGEIRVLDGDM-----RDRrhrravcpRIAY 87
Cdd:PRK10851 7 NIKKSFGRTQVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFHGTDVsrlhaRDR--------KVGF 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 88 MPQGLGknLYPTLSVFENVDF----FGRLFGHDKAERERRIADLLQSTGLAPFAERPAGKLSGGMKQKLGLCCALIHDPD 163
Cdd:PRK10851 79 VFQHYA--LFRHMTVFDNIAFgltvLPRRERPNAAAIKAKVTQLLEMVQLAHLADRYPAQLSGGQKQRVALARALAVEPQ 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15600424 164 LLILDEPTTGVDPLSRNqfwELIGRIRAGREGM---SVLVaTAYMEEA-ERFDWLVAMDDGKVLATGTPQEL 231
Cdd:PRK10851 157 ILLLDEPFGALDAQVRK---ELRRWLRQLHEELkftSVFV-THDQEEAmEVADRVVVMSQGNIEQAGTPDQV 224
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
20-230 |
3.49e-23 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 100.51 E-value: 3.49e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 20 ETRAVDDVSLEIPANRMVGLIGPDGVGKSSLLALLAGARKMQDGEIRVLDGDMRDRRHR-RAVCPRIAYMPQglgknlYP 98
Cdd:PRK13637 19 EKKALDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDGVDITDKKVKlSDIRKKVGLVFQ------YP 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 99 TLSVFE-----NVDFFGRLFGHDKAERERRIADLLQSTGLA--PFAERPAGKLSGGMKQKLGLCCALIHDPDLLILDEPT 171
Cdd:PRK13637 93 EYQLFEetiekDIAFGPINLGLSEEEIENRVKRAMNIVGLDyeDYKDKSPFELSGGQKRRVAIAGVVAMEPKILILDEPT 172
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 172 TGVDPLSRNQFWELIGRIRAgREGMSVLVATAYMEEAERF-DWLVAMDDGKVLATGTPQE 230
Cdd:PRK13637 173 AGLDPKGRDEILNKIKELHK-EYNMTIILVSHSMEDVAKLaDRIIVMNKGKCELQGTPRE 231
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
275-464 |
3.96e-23 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 98.41 E-value: 3.96e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 275 IEAEGLTCRFGDFVAVDHVSFRIERGEIFGFLGSNGCGKSTTMKMLTGLLPASEGTCALFGQPVDASDMATrrRVGYMSQ 354
Cdd:PRK13539 3 LEGEDLACVRGGRVLFSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDGGDIDDPDVAE--ACHYLGH 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 355 AFSLYAELSVRQNLVLHARLFhlpaDGIPARVGEMLRRFDLEKVADELPNDLPLGIRQRLSLA-VAVIHKPeILILDEPT 433
Cdd:PRK13539 81 RNAMKPALTVAENLEFWAAFL----GGEELDIAAALEAVGLAPLAHLPFGYLSAGQKRRVALArLLVSNRP-IWILDEPT 155
|
170 180 190
....*....|....*....|....*....|.
gi 15600424 434 SGVDPVARDGFWELMVELSRRDGvTIFISTH 464
Cdd:PRK13539 156 AALDAAAVALFAELIRAHLAQGG-IVIAATH 185
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
11-230 |
4.33e-23 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 99.39 E-value: 4.33e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 11 LRGVSLRYGETRAVDDVSLEIPANRMVGLIGPDGVGKSSLLALLAGARKMQDGEIRVlDGdmrdrrhrravcpRIAyMPQ 90
Cdd:COG1134 29 LRRRRTRREEFWALKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTSGRVEV-NG-------------RVS-ALL 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 91 GLGKNLYPTLSVFENVDFFGRLFGHDKAERERRIADLLQSTGLAPFAERPAGKLSGGMKQKLGLCCALIHDPDLLILDEP 170
Cdd:COG1134 94 ELGAGFHPELTGRENIYLNGRLLGLSRKEIDEKFDEIVEFAELGDFIDQPVKTYSSGMRARLAFAVATAVDPDILLVDEV 173
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15600424 171 TTGVDPLSRNQFWELIGRIRagREGMSVLVATAYMEEAERF-DWLVAMDDGKVLATGTPQE 230
Cdd:COG1134 174 LAVGDAAFQKKCLARIRELR--ESGRTVIFVSHSMGAVRRLcDRAIWLEKGRLVMDGDPEE 232
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
10-231 |
7.64e-23 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 101.26 E-value: 7.64e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 10 SLRGVSLRYGETRAVDDVSLEIPANRMVGLIGPDGVGKSSLLALLAGARKMQDGEIRVLDGDMRDrrhrraVCPriayMP 89
Cdd:PRK11000 5 TLRNVTKAYGDVVISKDINLDIHEGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLFIGEKRMND------VPP----AE 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 90 QGLGK-----NLYPTLSVFENVDFFGRLFGHDKAERERRI---ADLLQstgLAPFAERPAGKLSGGMKQKLGLCCALIHD 161
Cdd:PRK11000 75 RGVGMvfqsyALYPHLSVAENMSFGLKLAGAKKEEINQRVnqvAEVLQ---LAHLLDRKPKALSGGQRQRVAIGRTLVAE 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15600424 162 PDLLILDEPTTGVDPLSRNQFWELIGRIRAgREGMSVLVATAYMEEAERF-DWLVAMDDGKVLATGTPQEL 231
Cdd:PRK11000 152 PSVFLLDEPLSNLDAALRVQMRIEISRLHK-RLGRTMIYVTHDQVEAMTLaDKIVVLDAGRVAQVGKPLEL 221
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
21-231 |
7.90e-23 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 99.81 E-value: 7.90e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 21 TRAVDDVSLEIPANRMVGLIGPDGVGKSSLLALLAGARKMQDGEIRVLDGDMRDRRHRRAVCP---RIAYMPQGLGKNLY 97
Cdd:PRK13643 19 SRALFDIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVTVGDIVVSSTSKQKEIKPvrkKVGVVFQFPESQLF 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 98 PTlSVFENVDFFGRLFGHDKAERERRIADLLQSTGLAP-FAERPAGKLSGGMKQKLGLCCALIHDPDLLILDEPTTGVDP 176
Cdd:PRK13643 99 EE-TVLKDVAFGPQNFGIPKEKAEKIAAEKLEMVGLADeFWEKSPFELSGGQMRRVAIAGILAMEPEVLVLDEPTAGLDP 177
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 15600424 177 LSRNQFWELIGRIRagREGMSVLVATAYMEE-AERFDWLVAMDDGKVLATGTPQEL 231
Cdd:PRK13643 178 KARIEMMQLFESIH--QSGQTVVLVTHLMDDvADYADYVYLLEKGHIISCGTPSDV 231
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
265-471 |
9.52e-23 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 98.70 E-value: 9.52e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 265 PQSEGAPRIAIEAEGLTCRFGDFVAVDHVSFRIERGEIFGFLGSNGCGKSTTMK---MLTGLLPA--SEGTCALFGQPVD 339
Cdd:PRK14243 1 TSTLNGTETVLRTENLNVYYGSFLAVKNVWLDIPKNQITAFIGPSGCGKSTILRcfnRLNDLIPGfrVEGKVTFHGKNLY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 340 ASDM---ATRRRVGYMSQAFSLYAElSVRQNLVLHARLFHLPADgIPARVGEMLRRFDL-EKVADEL-PNDLPL--GIRQ 412
Cdd:PRK14243 81 APDVdpvEVRRRIGMVFQKPNPFPK-SIYDNIAYGARINGYKGD-MDELVERSLRQAALwDEVKDKLkQSGLSLsgGQQQ 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 15600424 413 RLSLAVAVIHKPEILILDEPTSGVDPVARDGFWELMVELSRRdgVTIFISTHFMNEAQR 471
Cdd:PRK14243 159 RLCIARAIAVQPEVILMDEPCSALDPISTLRIEELMHELKEQ--YTIIIVTHNMQQAAR 215
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
272-483 |
1.01e-22 |
|
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: 96.35 E-value: 1.01e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 272 RIAIEAEGLTCRfgdfVAVDHVSFRIERGEIFGFLGSNGCGKSTTMKMLTGLLPASEGTCALFGQPVDASD--MATRRRV 349
Cdd:cd03215 2 EPVLEVRGLSVK----GAVRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITLDGKPVTRRSprDAIRAGI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 350 GYMS---QAFSLYAELSVRQNLVLHARLfhlpaDGiparvgemlrrfdlekvadelpndlplGIRQRLSLAVAVIHKPEI 426
Cdd:cd03215 78 AYVPedrKREGLVLDLSVAENIALSSLL-----SG---------------------------GNQQKVVLARWLARDPRV 125
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 15600424 427 LILDEPTSGVDPVARDGFWELMVELSRRDGVTIFISTHfMNEAQR-CDRISLMHAGKV 483
Cdd:cd03215 126 LILDEPTRGVDVGAKAEIYRLIRELADAGKAVLLISSE-LDELLGlCDRILVMYEGRI 182
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
290-489 |
1.37e-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: 97.54 E-value: 1.37e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 290 VDHVSFRIERGEIFGFLGSNGCGKSTTMKMLTGLLPASEGTCALFGQPVDASdmATRRRVGYmsQAFSLYAELSVRQNLV 369
Cdd:TIGR01184 1 LKGVNLTIQQGEFISLIGHSGCGKSTLLNLISGLAQPTSGGVILEGKQITEP--GPDRMVVF--QNYSLLPWLTVRENIA 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 370 L--HARLFHLPADGIPARVGEMLRRFDLEKVADELPNDLPLGIRQRLSLAVAVIHKPEILILDEPTSGVDPVARDGFWEL 447
Cdd:TIGR01184 77 LavDRVLPDLSKSERRAIVEEHIALVGLTEAADKRPGQLSGGMKQRVAIARALSIRPKVLLLDEPFGALDALTRGNLQEE 156
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 15600424 448 MVELSRRDGVTIFISTHFMNEAQ-RCDRISLM------HAGKVLASDTP 489
Cdd:TIGR01184 157 LMQIWEEHRVTVLMVTHDVDEALlLSDRVVMLtngpaaNIGQILEVPFP 205
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
10-236 |
1.80e-22 |
|
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; MsbA is an essential ABC transporter, closely related to eukaryotic MDR proteins. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213218 [Multi-domain] Cd Length: 234 Bit Score: 97.30 E-value: 1.80e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 10 SLRGVSLRYGETR--AVDDVSLEIPANRMVGLIGPDGVGKSSLLALLAGARKMQDGEIRVLDGDMRD------RRHrrav 81
Cdd:cd03251 2 EFKNVTFRYPGDGppVLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDGHDVRDytlaslRRQ---- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 82 cprIAYMPQGLgkNLYPTlSVFENVdffgrLFGHDKAERERrIADLLQSTGLAPFAER-PAG----------KLSGGMKQ 150
Cdd:cd03251 78 ---IGLVSQDV--FLFND-TVAENI-----AYGRPGATREE-VEEAARAANAHEFIMElPEGydtvigergvKLSGGQRQ 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 151 KLGLCCALIHDPDLLILDEPTTGVDPLSRNQFWELIGRIRAGRegmSVLVATAYMEEAERFDWLVAMDDGKVLATGTPQE 230
Cdd:cd03251 146 RIAIARALLKDPPILILDEATSALDTESERLVQAALERLMKNR---TTFVIAHRLSTIENADRIVVLEDGKIVERGTHEE 222
|
....*.
gi 15600424 231 LRERTG 236
Cdd:cd03251 223 LLAQGG 228
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
293-484 |
1.96e-22 |
|
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ABC transporters homologous to the Drosophila white gene, which acts as a dimeric importer for eye pigment precursors. The eye pigmentation of Drosophila is developed from the synthesis and deposition in the cells of red pigments, which are synthesized from guanine, and brown pigments, which are synthesized from tryptophan. The pigment precursors are encoded by the white, brown, and scarlet genes, respectively. Evidence from genetic and biochemical studies suggest that the White and Brown proteins function as heterodimers to import guanine, while the White and Scarlet proteins function to import tryptophan. However, a recent study also suggests that White may be involved in the transport of a metabolite, such as 3-hydroxykynurenine, across intracellular membranes. Mammalian ABC transporters belonging to the White subfamily (ABCG1, ABCG5, and ABCG8) have been shown to be involved in the regulation of lipid-trafficking mechanisms in macrophages, hepatocytes, and intestinal mucosa cells. ABCG1 (ABC8), the human homolog of the Drosophila white gene is induced in monocyte-derived macrophages during cholesterol influx mediated by acetylated low-density lipoprotein. It is possible that human ABCG1 forms heterodimers with several heterologous partners.
Pssm-ID: 213201 [Multi-domain] Cd Length: 226 Bit Score: 96.96 E-value: 1.96e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 293 VSFRIERGEIFGFLGSNGCGKSTTMKMLTGLLP---ASEGTCALFGQPVDASDMatRRRVGYMSQAFSLYAELSVRQNL- 368
Cdd:cd03234 26 VSLHVESGQVMAILGSSGSGKTTLLDAISGRVEgggTTSGQILFNGQPRKPDQF--QKCVAYVRQDDILLPGLTVRETLt 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 369 -VLHARLFHLPADGIPARVGE--MLRRFDLEKVADELPNDLPLGIRQRLSLAVAVIHKPEILILDEPTSGVDPVARDGFW 445
Cdd:cd03234 104 yTAILRLPRKSSDAIRKKRVEdvLLRDLALTRIGGNLVKGISGGERRRVSIAVQLLWDPKVLILDEPTSGLDSFTALNLV 183
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 15600424 446 ELMVELSRRdGVTIFISTH------FmneaQRCDRISLMHAGKVL 484
Cdd:cd03234 184 STLSQLARR-NRIVILTIHqprsdlF----RLFDRILLLSSGEIV 223
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
10-250 |
2.00e-22 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 98.14 E-value: 2.00e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 10 SLRGVSLRYG--ETRAVDDVSLEIPANRMVGLIGPDGVGKSSLLALLAGARKMQDGEIRvLDGDMRDRRHrravcprIAY 87
Cdd:PRK13632 9 KVENVSFSYPnsENNALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIK-IDGITISKEN-------LKE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 88 MPQGLGknlyptlSVFENVD--FFGRL------FG-----HDKAERERRIADLLQSTGLAPFAERPAGKLSGGMKQKLGL 154
Cdd:PRK13632 81 IRKKIG-------IIFQNPDnqFIGATveddiaFGlenkkVPPKKMKDIIDDLAKKVGMEDYLDKEPQNLSGGQKQRVAI 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 155 CCALIHDPDLLILDEPTTGVDPLSRNQFWELIGRIRAGREgMSVLVATAYMEEAERFDWLVAMDDGKVLATGTPQEL--- 231
Cdd:PRK13632 154 ASVLALNPEIIIFDESTSMLDPKGKREIKKIMVDLRKTRK-KTLISITHDMDEAILADKVIVFSEGKLIAQGKPKEIlnn 232
|
250
....*....|....*....
gi 15600424 232 RERTGTQSLESAFIALLPE 250
Cdd:PRK13632 233 KEILEKAKIDSPFIYKLSK 251
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
289-483 |
2.04e-22 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 99.42 E-value: 2.04e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 289 AVDHVSFRIERGEIFGFLGSNGCGKSTTMKMLTGLLPASEGTCALFGQPV---DASDM-ATRRRVGYMSQafSLYAELSV 364
Cdd:COG4608 33 AVDGVSFDIRRGETLGLVGESGCGKSTLGRLLLRLEEPTSGEILFDGQDItglSGRELrPLRRRMQMVFQ--DPYASLNP 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 365 RQN--------LVLHaRLfhLPADGIPARVGEMLRRFDLEK-VADELPNDLPLGIRQRLSLAVAVIHKPEILILDEPTSG 435
Cdd:COG4608 111 RMTvgdiiaepLRIH-GL--ASKAERRERVAELLELVGLRPeHADRYPHEFSGGQRQRIGIARALALNPKLIVCDEPVSA 187
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 15600424 436 VDPVARDGFWELMVELSRRDGVT-IFIS------THFmneaqrCDRISLMHAGKV 483
Cdd:COG4608 188 LDVSIQAQVLNLLEDLQDELGLTyLFIShdlsvvRHI------SDRVAVMYLGKI 236
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
12-202 |
2.08e-22 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 96.10 E-value: 2.08e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 12 RGVSLRYGETRAVDDVSLEIPANRMVGLIGPDGVGKSSLLALLAGARKMQDGEIRVLDGDMRDRRHRravcPRIAYmpqg 91
Cdd:PRK13539 6 EDLACVRGGRVLFSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDGGDIDDPDVA----EACHY---- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 92 LG-KN-LYPTLSVFENVDFFGRLFGhdkaERERRIADLLQSTGLAPFAERPAGKLSGGMKQKLGLCCALIHDPDLLILDE 169
Cdd:PRK13539 78 LGhRNaMKPALTVAENLEFWAAFLG----GEELDIAAALEAVGLAPLAHLPFGYLSAGQKRRVALARLLVSNRPIWILDE 153
|
170 180 190
....*....|....*....|....*....|...
gi 15600424 170 PTTGVDPLSRNQFWELIgRIRAGREGMsVLVAT 202
Cdd:PRK13539 154 PTAALDAAAVALFAELI-RAHLAQGGI-VIAAT 184
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
289-505 |
2.53e-22 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 97.55 E-value: 2.53e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 289 AVDHVSFRIE-------------RGEIFGFLGSNGCGKSTTMKMLTGLLPASEGTCALFGQPVDA-SDMATRRRVGYMSQ 354
Cdd:PRK10575 13 ALRNVSFRVPgrtllhplsltfpAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPLESwSSKAFARKVAYLPQ 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 355 AFSLYAELSVRQnLVLHARlfhLPADGIPARVGEMLRR--------FDLEKVADELPNDLPLGIRQRLSLAVAVIHKPEI 426
Cdd:PRK10575 93 QLPAAEGMTVRE-LVAIGR---YPWHGALGRFGAADREkveeaislVGLKPLAHRLVDSLSGGERQRAWIAMLVAQDSRC 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 427 LILDEPTSGVDPVARDGFWELMVELSRRDGVTIFISTHFMNEAQR-CDRISLMHAGKVLASDTPDELVRQrglPTLEATF 505
Cdd:PRK10575 169 LLLDEPTSALDIAHQVDVLALVHRLSQERGLTVIAVLHDINMAARyCDYLVALRGGEMIAQGTPAELMRG---ETLEQIY 245
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
289-505 |
2.58e-22 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 98.17 E-value: 2.58e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 289 AVDHVSFRIERGEIFGFLGSNGCGKSTTMKMLTGLLPASEGTCALFGQPVDASDMAT-----RRRVGYM-----SQAFsl 358
Cdd:PRK13634 22 ALYDVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVTIGERVITAGKKNKklkplRKKVGIVfqfpeHQLF-- 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 359 yaELSVRQNLVLHARLFHLPADGIPARVGEMLRRFDL-EKVADELPNDLPLGIRQRLSLAVAVIHKPEILILDEPTSGVD 437
Cdd:PRK13634 100 --EETVEKDICFGPMNFGVSEEDAKQKAREMIELVGLpEELLARSPFELSGGQMRRVAIAGVLAMEPEVLVLDEPTAGLD 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 438 PVARDGFWELMVELSRRDGVTIFISTHFMNEAQR-CDRISLMHAGKVLASDTPDELVR--------QRGLPT-------L 501
Cdd:PRK13634 178 PKGRKEMMEMFYKLHKEKGLTTVLVTHSMEDAARyADQIVVMHKGTVFLQGTPREIFAdpdeleaiGLDLPEtvkfkraL 257
|
....
gi 15600424 502 EATF 505
Cdd:PRK13634 258 EEKF 261
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
10-232 |
2.66e-22 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 97.37 E-value: 2.66e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 10 SLRGVSLRYGETRAVDDVSLEIPANRMVGLIGPDGVGKSSLLALLAGARKMQDGEIRvLDGdmrdrrHRRAVCP--RIAY 87
Cdd:PRK11300 7 SVSGLMMRFGGLLAVNNVNLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTIL-LRG------QHIEGLPghQIAR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 88 MpqGLGKN-----LYPTLSVFENV----------DFFGRLF---GHDKAERE--RRIADLLQSTGLAPFAERPAGKLSGG 147
Cdd:PRK11300 80 M--GVVRTfqhvrLFREMTVIENLlvaqhqqlktGLFSGLLktpAFRRAESEalDRAATWLERVGLLEHANRQAGNLAYG 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 148 MKQKLGLCCALIHDPDLLILDEPTTGVDPLSRNQFWELIGRIRagRE-GMSVLV----ATAYMEEAERfdwLVAMDDGKV 222
Cdd:PRK11300 158 QQRRLEIARCMVTQPEILMLDEPAAGLNPKETKELDELIAELR--NEhNVTVLLiehdMKLVMGISDR---IYVVNQGTP 232
|
250
....*....|
gi 15600424 223 LATGTPQELR 232
Cdd:PRK11300 233 LANGTPEEIR 242
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
10-225 |
3.25e-22 |
|
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: 94.03 E-value: 3.25e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 10 SLRGVSLRYGETRAVDDVSLEIPANRMVGLIGPDGVGKSSLLALLAGARKMQDGEIRVlDGDMRDRRhrravCPRIAymp 89
Cdd:cd03216 2 ELRGITKRFGGVKALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILV-DGKEVSFA-----SPRDA--- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 90 qglgknlyptlsvfenvdffgrlfghdkaeRERRIADLLQstglapfaerpagkLSGGMKQKLGLCCALIHDPDLLILDE 169
Cdd:cd03216 73 ------------------------------RRAGIAMVYQ--------------LSVGERQMVEIARALARNARLLILDE 108
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 15600424 170 PTTGVDPLSRNQFWELIGRIRAgrEGMSVLVATAYMEEAERF-DWLVAMDDGKVLAT 225
Cdd:cd03216 109 PTAALTPAEVERLFKVIRRLRA--QGVAVIFISHRLDEVFEIaDRVTVLRDGRVVGT 163
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
21-231 |
3.40e-22 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 97.46 E-value: 3.40e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 21 TRAVDDVSLEIPANRMVGLIGPDGVGKSSLLALLAGARKMQDGEIrVLDGDmrdrrhrravcpRIAYMPQGLGKNLYPTL 100
Cdd:PRK13639 15 TEALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEV-LIKGE------------PIKYDKKSLLEVRKTVG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 101 SVFENVD------------FFGRL-FGHDKAERERRIADLLQSTGLAPFAERPAGKLSGGMKQKLGLCCALIHDPDLLIL 167
Cdd:PRK13639 82 IVFQNPDdqlfaptveedvAFGPLnLGLSKEEVEKRVKEALKAVGMEGFENKPPHHLSGGQKKRVAIAGILAMKPEIIVL 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15600424 168 DEPTTGVDPLSRNQFWELIGRIraGREGMSVLVATAYMEEAERF-DWLVAMDDGKVLATGTPQEL 231
Cdd:PRK13639 162 DEPTSGLDPMGASQIMKLLYDL--NKEGITIIISTHDVDLVPVYaDKVYVMSDGKIIKEGTPKEV 224
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
273-495 |
3.94e-22 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 99.00 E-value: 3.94e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 273 IAIEAEGLTCRFGDFVAVDHVSFRIERGEIFGFLGSNGCGKSTTMKMLTGLLPASEGTCALFGQpvDASDMATR-RRVGY 351
Cdd:PRK10851 1 MSIEIANIKKSFGRTQVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFHGT--DVSRLHARdRKVGF 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 352 MSQAFSLYAELSVRQNLVLHARLfhLP------ADGIPARVGEMLRRFDLEKVADELPNDLPLGIRQRLSLAVAVIHKPE 425
Cdd:PRK10851 79 VFQHYALFRHMTVFDNIAFGLTV--LPrrerpnAAAIKAKVTQLLEMVQLAHLADRYPAQLSGGQKQRVALARALAVEPQ 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15600424 426 ILILDEPTSGVDPVARDGFWELMVELSRRDGVTIFISTHFMNEAQR-CDRISLMHAGKVLASDTPDELVRQ 495
Cdd:PRK10851 157 ILLLDEPFGALDAQVRKELRRWLRQLHEELKFTSVFVTHDQEEAMEvADRVVVMSQGNIEQAGTPDQVWRE 227
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
275-486 |
3.97e-22 |
|
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: 101.05 E-value: 3.97e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 275 IEAEGLTCRFGDFVAVDHVSFRIERGEIFGFLGSNGCGKSTTMKMLTGLLPAS--EGTCALFGQPVDASDMATRRRVG-- 350
Cdd:TIGR02633 2 LEMKGIVKTFGGVKALDGIDLEVRPGECVGLCGENGAGKSTLMKILSGVYPHGtwDGEIYWSGSPLKASNIRDTERAGiv 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 351 YMSQAFSLYAELSVRQNLVLHARLFH----LPADGIPARVGEMLRRFDLEKVADELP-NDLPLGIRQRLSLAVAVIHKPE 425
Cdd:TIGR02633 82 IIHQELTLVPELSVAENIFLGNEITLpggrMAYNAMYLRAKNLLRELQLDADNVTRPvGDYGGGQQQLVEIAKALNKQAR 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15600424 426 ILILDEPTSGVDPVARDGFWELMVELSRRDGVTIFIStHFMNEAQR-CDRISLMHAGKVLAS 486
Cdd:TIGR02633 162 LLILDEPSSSLTEKETEILLDIIRDLKAHGVACVYIS-HKLNEVKAvCDTICVIRDGQHVAT 222
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
10-226 |
4.97e-22 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 96.10 E-value: 4.97e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 10 SLRGVSLRYGETRAVDDVSLEIPANRMVGLIGPDGVGKSSLLALLAGARKMQDGEIRVLDGDMRDRRHRRAVCPRIAYMP 89
Cdd:PRK11614 7 SFDKVSAHYGKIQALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDGKDITDWQTAKIMREAVAIVP 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 90 QglGKNLYPTLSVFENVDFFGrlFGHDKAERERRIADLLqstGLAP-FAERP---AGKLSGGMKQKLGLCCALIHDPDLL 165
Cdd:PRK11614 87 E--GRRVFSRMTVEENLAMGG--FFAERDQFQERIKWVY---ELFPrLHERRiqrAGTMSGGEQQMLAIGRALMSQPRLL 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15600424 166 ILDEPTTGVDPLSRNQFWELIGRIRAgrEGMSVLVATAYMEEAerfdwLVAMDDGKVLATG 226
Cdd:PRK11614 160 LLDEPSLGLAPIIIQQIFDTIEQLRE--QGMTIFLVEQNANQA-----LKLADRGYVLENG 213
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
11-235 |
5.01e-22 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 96.76 E-value: 5.01e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 11 LRGVSLRYGETRAVDDVSLEIPANRMVGLIGPDGVGKSSLLALLAGARKMQDGEIrVLDGD---MRDRRHRRAVCPRIAY 87
Cdd:PRK11831 10 MRGVSFTRGNRCIFDNISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEI-LFDGEnipAMSRSRLYTVRKRMSM 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 88 MPQglGKNLYPTLSVFENVDFFGRlfghdkaERERRIADLLQST--------GLAPFAERPAGKLSGGMKQKLGLCCALI 159
Cdd:PRK11831 89 LFQ--SGALFTDMNVFDNVAYPLR-------EHTQLPAPLLHSTvmmkleavGLRGAAKLMPSELSGGMARRAALARAIA 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15600424 160 HDPDLLILDEPTTGVDPLSRNQFWELIGRIRAGREGMSVLVATAYMEEAERFDWLVAMDDGKVLATGTPQELRERT 235
Cdd:PRK11831 160 LEPDLIMFDEPFVGQDPITMGVLVKLISELNSALGVTCVVVSHDVPEVLSIADHAYIVADKKIVAHGSAQALQANP 235
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
275-493 |
5.09e-22 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 95.93 E-value: 5.09e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 275 IEAEGLTCRFGDFVAVDHVSFRIERGEIFGFLGSNGCGKSTTMKMLTGLLPASEGTCALFGQPVD---ASDMATRRRVGY 351
Cdd:PRK09493 2 IEFKNVSKHFGPTQVLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGLKVNdpkVDERLIRQEAGM 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 352 MSQAFSLYAELSVRQNLV---LHARLFHLPADGIPARvgEMLRRFDLEKVADELPNDLPLGIRQRLSLAVAVIHKPEILI 428
Cdd:PRK09493 82 VFQQFYLFPHLTALENVMfgpLRVRGASKEEAEKQAR--ELLAKVGLAERAHHYPSELSGGQQQRVAIARALAVKPKLML 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15600424 429 LDEPTSGVDPVARDGFWELMVELSrRDGVTIFISTHFMNEAQRC-DRISLMHAGKVLASDTPDELV 493
Cdd:PRK09493 160 FDEPTSALDPELRHEVLKVMQDLA-EEGMTMVIVTHEIGFAEKVaSRLIFIDKGRIAEDGDPQVLI 224
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
253-495 |
5.18e-22 |
|
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: 101.36 E-value: 5.18e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 253 RAGHHRL-----VIPPRPQSEG--APRIAIEAEGLTCRF--GDFVAVDHVSFRIERGEIFGFLGSNGCGKSTTMKMLTGL 323
Cdd:COG4618 302 RQAYRRLnellaAVPAEPERMPlpRPKGRLSVENLTVVPpgSKRPILRGVSFSLEPGEVLGVIGPSGSGKSTLARLLVGV 381
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 324 LPASEGTCALFGQPVDASDMATR-RRVGYMSQAFSLYAElSVRQNLvlhARLfhlpADGIPARVGEMLRRFDLEKVADEL 402
Cdd:COG4618 382 WPPTAGSVRLDGADLSQWDREELgRHIGYLPQDVELFDG-TIAENI---ARF----GDADPEKVVAAAKLAGVHEMILRL 453
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 403 PN--DLPLGI---------RQRLSLAVAVIHKPEILILDEPTSGVDPVARDGFWELMVELsRRDGVTIFISTHFMNEAQR 471
Cdd:COG4618 454 PDgyDTRIGEggarlsggqRQRIGLARALYGDPRLVVLDEPNSNLDDEGEAALAAAIRAL-KARGATVVVITHRPSLLAA 532
|
250 260
....*....|....*....|....
gi 15600424 472 CDRISLMHAGKVLASDTPDELVRQ 495
Cdd:COG4618 533 VDKLLVLRDGRVQAFGPRDEVLAR 556
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
23-245 |
5.21e-22 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 99.14 E-value: 5.21e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 23 AVDDVSLEIPANRMVGLIGPDGVGKSSLLALLAGARKMQDGEIrVLDGdmRDRRHRRAVCPRIAYMPQGLGknLYPTLSV 102
Cdd:PRK11607 34 AVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQI-MLDG--VDLSHVPPYQRPINMMFQSYA--LFPHMTV 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 103 FENVDFFGRLFGHDKAERERRIADLLQSTGLAPFAERPAGKLSGGMKQKLGLCCALIHDPDLLILDEPTTGVDPLSRNQF 182
Cdd:PRK11607 109 EQNIAFGLKQDKLPKAEIASRVNEMLGLVHMQEFAKRKPHQLSGGQRQRVALARSLAKRPKLLLLDEPMGALDKKLRDRM 188
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15600424 183 -WELIGRIRagREGMSVLVATAYMEEAERFDWLVA-MDDGKVLATGTPQELRERTGTQsLESAFI 245
Cdd:PRK11607 189 qLEVVDILE--RVGVTCVMVTHDQEEAMTMAGRIAiMNRGKFVQIGEPEEIYEHPTTR-YSAEFI 250
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
292-485 |
5.57e-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: 95.25 E-value: 5.57e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 292 HVSFRIERGEIFGFLGSNGCGKSTTMKMLTGLLPASEGTCALFGQPVDASDMAtRRRVGYMSQAFSLYAELSVRQN--LV 369
Cdd:cd03298 16 HFDLTFAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLINGVDVTAAPPA-DRPVSMLFQENNLFAHLTVEQNvgLG 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 370 LHARLFHLPADgiPARVGEMLRRFDLEKVADELPNDLPLGIRQRLSLAVAVIHKPEILILDEPTSGVDPVARDGFWELMV 449
Cdd:cd03298 95 LSPGLKLTAED--RQAIEVALARVGLAGLEKRLPGELSGGERQRVALARVLVRDKPVLLLDEPFAALDPALRAEMLDLVL 172
|
170 180 190
....*....|....*....|....*....|....*..
gi 15600424 450 ELSRRDGVTIFISTHFMNEAQRC-DRISLMHAGKVLA 485
Cdd:cd03298 173 DLHAETKMTVLMVTHQPEDAKRLaQRVVFLDNGRIAA 209
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
3-231 |
6.05e-22 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 96.74 E-value: 6.05e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 3 AGGSGVASLRGVSLRY--GETRAVDDVSLEIPANRMVGLIGPDGVGKSSLLALLAGARKMQDGEI-----RVLDGDMRDR 75
Cdd:PRK13648 2 EDKNSIIVFKNVSFQYqsDASFTLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIfynnqAITDDNFEKL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 76 RHRRAVcpriaympqglgknlyptlsVFENVD--FFGRLFGHDKA-----------ERERRIADLLQSTGLAPFAERPAG 142
Cdd:PRK13648 82 RKHIGI--------------------VFQNPDnqFVGSIVKYDVAfglenhavpydEMHRRVSEALKQVDMLERADYEPN 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 143 KLSGGMKQKLGLCCALIHDPDLLILDEPTTGVDPLSRNQFWELIGRIRAGREgMSVLVATAYMEEAERFDWLVAMDDGKV 222
Cdd:PRK13648 142 ALSGGQKQRVAIAGVLALNPSVIILDEATSMLDPDARQNLLDLVRKVKSEHN-ITIISITHDLSEAMEADHVIVMNKGTV 220
|
....*....
gi 15600424 223 LATGTPQEL 231
Cdd:PRK13648 221 YKEGTPTEI 229
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
274-484 |
6.42e-22 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 95.85 E-value: 6.42e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 274 AIEAEGLTCRFGDFVAVDHVSFRIERGEIFGFLGSNGCGKSTTMKMLTGLLPASEGTCAL------FGQPVDASDMAT-R 346
Cdd:PRK11124 2 SIQLNGINCFYGAHQALFDITLDCPQGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLNIagnhfdFSKTPSDKAIRElR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 347 RRVGYMSQAFSLYAELSVRQNLVlHA--RLFHLPADGIPARVGEMLRRFDLEKVADELPNDLPLGIRQRLSLAVAVIHKP 424
Cdd:PRK11124 82 RNVGMVFQQYNLWPHLTVQQNLI-EApcRVLGLSKDQALARAEKLLERLRLKPYADRFPLHLSGGQQQRVAIARALMMEP 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15600424 425 EILILDEPTSGVDPVARDGFWELMVELSrRDGVTIFISTHFMNEAQR-CDRISLMHAGKVL 484
Cdd:PRK11124 161 QVLLFDEPTAALDPEITAQIVSIIRELA-ETGITQVIVTHEVEVARKtASRVVYMENGHIV 220
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
10-230 |
1.11e-21 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 94.09 E-value: 1.11e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 10 SLRGVSLRYGETRAVDDVSLEIPANRMVGLIGPDGVGKSSLLALLAGARKMQ---DGEIRvLDGDMRDRR--HRRavcpR 84
Cdd:COG4136 3 SLENLTITLGGRPLLAPLSLTVAPGEILTLMGPSGSGKSTLLAAIAGTLSPAfsaSGEVL-LNGRRLTALpaEQR----R 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 85 IAYMPQ-GLgknLYPTLSVFENVdffgrLFG----HDKAERERRIADLLQSTGLAPFAERPAGKLSGGMKQKLGLCCALI 159
Cdd:COG4136 78 IGILFQdDL---LFPHLSVGENL-----AFAlpptIGRAQRRARVEQALEEAGLAGFADRDPATLSGGQRARVALLRALL 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15600424 160 HDPDLLILDEPTTGVDPLSRNQFWELIgRIRAGREGMSVLVATAYMEEAErfdwlvamDDGKVLATGTPQE 230
Cdd:COG4136 150 AEPRALLLDEPFSKLDAALRAQFREFV-FEQIRQRGIPALLVTHDEEDAP--------AAGRVLDLGNWQH 211
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
290-492 |
1.15e-21 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 95.95 E-value: 1.15e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 290 VDHVSFRIERGEIFGFLGSNGCGKSTTMKMLTGLLPASEGTCALFGQPVDASDM-ATRRRVGYMSQ-AFSLYAELSVRQN 367
Cdd:PRK13650 23 LNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIIDGDLLTEENVwDIRHKIGMVFQnPDNQFVGATVEDD 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 368 LVlharlFHLPADGIP-----ARVGEMLRRFDLEKVADELPNDLPLGIRQRLSLAVAVIHKPEILILDEPTSGVDPVARD 442
Cdd:PRK13650 103 VA-----FGLENKGIPheemkERVNEALELVGMQDFKEREPARLSGGQKQRVAIAGAVAMRPKIIILDEATSMLDPEGRL 177
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 15600424 443 GFWELMVELSRRDGVTIFISTHFMNEAQRCDRISLMHAGKVLASDTPDEL 492
Cdd:PRK13650 178 ELIKTIKGIRDDYQMTVISITHDLDEVALSDRVLVMKNGQVESTSTPREL 227
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
289-492 |
1.19e-21 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 96.02 E-value: 1.19e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 289 AVDHVSFRIERGEIFGFLGSNGCGKSTTMKMLTGLL---PASEGTCALFGQPVDASDM-ATRRRVGYMSQ-AFSLYAELS 363
Cdd:PRK13640 22 ALNDISFSIPRGSWTALIGHNGSGKSTISKLINGLLlpdDNPNSKITVDGITLTAKTVwDIREKVGIVFQnPDNQFVGAT 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 364 VRQNLVlharlFHLPADGIPAR-----VGEMLRRFDLEKVADELPNDLPLGIRQRLSLAVAVIHKPEILILDEPTSGVDP 438
Cdd:PRK13640 102 VGDDVA-----FGLENRAVPRPemikiVRDVLADVGMLDYIDSEPANLSGGQKQRVAIAGILAVEPKIIILDESTSMLDP 176
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 15600424 439 VARDGFWELMVELSRRDGVTIFISTHFMNEAQRCDRISLMHAGKVLASDTPDEL 492
Cdd:PRK13640 177 AGKEQILKLIRKLKKKNNLTVISITHDIDEANMADQVLVLDDGKLLAQGSPVEI 230
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
23-250 |
1.26e-21 |
|
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: 101.63 E-value: 1.26e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 23 AVDDVSLEIPANRMVGLIGPDGVGKSSLLALLAGARKMQDGEIRV----LDGDMRDRRHRRAVCPRIAYMPQglgknlyp 98
Cdd:TIGR01257 1954 AVDRLCVGVRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVagksILTNISDVHQNMGYCPQFDAIDD-------- 2025
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 99 TLSVFENVDFFGRLFGHDKAERERRIADLLQSTGLAPFAERPAGKLSGGMKQKLGLCCALIHDPDLLILDEPTTGVDPLS 178
Cdd:TIGR01257 2026 LLTGREHLYLYARLRGVPAEEIEKVANWSIQSLGLSLYADRLAGTYSGGNKRKLSTAIALIGCPPLVLLDEPTTGMDPQA 2105
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15600424 179 RNQFWELIGRIRagREGMSVLVATAYMEEAERF-DWLVAMDDGKVLATGTPQELRERTG-----TQSLESAFIALLPE 250
Cdd:TIGR01257 2106 RRMLWNTIVSII--REGRAVVLTSHSMEECEALcTRLAIMVKGAFQCLGTIQHLKSKFGdgyivTMKIKSPKDDLLPD 2181
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
293-474 |
1.27e-21 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 94.46 E-value: 1.27e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 293 VSFRIERGEIFGFLGSNGCGKSTTMKMLTGLLPASEGTCALFGQPVDASDMATR-----RRVGYMSQAFSLYAELSVRQN 367
Cdd:PRK10584 29 VELVVKRGETIALIGESGSGKSTLLAILAGLDDGSSGEVSLVGQPLHQMDEEARaklraKHVGFVFQSFMLIPTLNALEN 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 368 LVLHARLFHLPADGIPARVGEMLRRFDLEKVADELPNDLPLGIRQRLSLAVAVIHKPEILILDEPTSGVDPVARDGFWEL 447
Cdd:PRK10584 109 VELPALLRGESSRQSRNGAKALLEQLGLGKRLDHLPAQLSGGEQQRVALARAFNGRPDVLFADEPTGNLDRQTGDKIADL 188
|
170 180
....*....|....*....|....*..
gi 15600424 448 MVELSRRDGVTIFISTHFMNEAQRCDR 474
Cdd:PRK10584 189 LFSLNREHGTTLILVTHDLQLAARCDR 215
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
20-231 |
1.51e-21 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 95.86 E-value: 1.51e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 20 ETRAVDDVSLEIPANRMVGLIGPDGVGKSSLLALLAGARKMQDGEIRVldGDMRDRRHRRAvcpriaympqglgKNL--- 96
Cdd:PRK13634 19 ERRALYDVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVTI--GERVITAGKKN-------------KKLkpl 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 97 ---------YPTLSVFENV---DF-FGRL-FGHDKAERERRIADLLQSTGLAP-FAERPAGKLSGGMKQKLGLCCALIHD 161
Cdd:PRK13634 84 rkkvgivfqFPEHQLFEETvekDIcFGPMnFGVSEEDAKQKAREMIELVGLPEeLLARSPFELSGGQMRRVAIAGVLAME 163
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15600424 162 PDLLILDEPTTGVDPLSRNQFWELIGRIRAgREGMSVLVATAYMEEAERF-DWLVAMDDGKVLATGTPQEL 231
Cdd:PRK13634 164 PEVLVLDEPTAGLDPKGRKEMMEMFYKLHK-EKGLTTVLVTHSMEDAARYaDQIVVMHKGTVFLQGTPREI 233
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
10-226 |
1.52e-21 |
|
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: 92.76 E-value: 1.52e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 10 SLRGVSLRYGE--TRAVDDVSLEIPANRMVGLIGPDGVGKSSLLALLAGARKMQDGEIrVLDGdmrdrrhrravcpriaY 87
Cdd:cd03247 2 SINNVSFSYPEqeQQVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEI-TLDG----------------V 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 88 MPQGLGKNLYPTLSVFENVDFfgrLFGhdkaererriADLLQSTGLapfaerpagKLSGGMKQKLGLCCALIHDPDLLIL 167
Cdd:cd03247 65 PVSDLEKALSSLISVLNQRPY---LFD----------TTLRNNLGR---------RFSGGERQRLALARILLQDAPIVLL 122
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 15600424 168 DEPTTGVDPLSRNQFWELIGRIragREGMSVLVATAYMEEAERFDWLVAMDDGKVLATG 226
Cdd:cd03247 123 DEPTVGLDPITERQLLSLIFEV---LKDKTLIWITHHLTGIEHMDKILFLENGKIIMQG 178
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
275-483 |
1.68e-21 |
|
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of the protease secretion system PrtD, a 60-kDa integral membrane protein sharing 37% identity with HlyB, the ABC component of the alpha-hemolysin secretion pathway, in the C-terminal domain. They export degradative enzymes by using a type I protein secretion system and lack an N-terminal signal peptide, but contain a C-terminal secretion signal. The Type I secretion apparatus is made up of three components, an ABC transporter, a membrane fusion protein (MFP), and an outer membrane protein (OMP). For the HlyA transporter complex, HlyB (ABC transporter) and HlyD (MFP) reside in the inner membrane of E. coli. The OMP component is TolC, which is thought to interact with the MFP to form a continuous channel across the periplasm from the cytoplasm to the exterior. HlyB belongs to the family of ABC transporters, which are ubiquitous, ATP-dependent transmembrane pumps or channels. The spectrum of transport substrates ranges from inorganic ions, nutrients such as amino acids, sugars, or peptides, hydrophobic drugs, to large polypeptides, such as HlyA.
Pssm-ID: 213213 [Multi-domain] Cd Length: 173 Bit Score: 92.66 E-value: 1.68e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 275 IEAEGLTCRFGDFVA--VDHVSFRIERGEIFGFLGSNGCGKSTTMKMLTGLLPASEGTCALFGQPVDASDMAT-RRRVGY 351
Cdd:cd03246 1 LEVENVSFRYPGAEPpvLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDGADISQWDPNElGDHVGY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 352 MSQAFSLYAElSVRQNLvlharlfhlpadgiparvgemlrrfdlekvadelpndLPLGIRQRLSLAVAVIHKPEILILDE 431
Cdd:cd03246 81 LPQDDELFSG-SIAENI-------------------------------------LSGGQRQRLGLARALYGNPRILVLDE 122
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 15600424 432 PTSGVDPVARDGFWELMVELSRRdGVTIFISTHFMNEAQRCDRISLMHAGKV 483
Cdd:cd03246 123 PNSHLDVEGERALNQAIAALKAA-GATRIVIAHRPETLASADRILVLEDGRV 173
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
275-484 |
1.70e-21 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 94.98 E-value: 1.70e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 275 IEAEGLTCRFGDFVAVDHVSFRIERGEIFGFLGSNGCGKSTTMKMLTGLL-----PASEGTCALFGQPVDASDMAT-RRR 348
Cdd:PRK14247 4 IEIRDLKVSFGQVEVLDGVNLEIPDNTITALMGPSGSGKSTLLRVFNRLIelypeARVSGEVYLDGQDIFKMDVIElRRR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 349 VGYMSQAFSLYAELSVRQNLVLHARLFHLPADG--IPARVGEMLRRFDL-EKVADEL---PNDLPLGIRQRLSLAVAVIH 422
Cdd:PRK14247 84 VQMVFQIPNPIPNLSIFENVALGLKLNRLVKSKkeLQERVRWALEKAQLwDEVKDRLdapAGKLSGGQQQRLCIARALAF 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15600424 423 KPEILILDEPTSGVDPVARDGFWELMVELSRRdgVTIFISTHFMNEAQRC-DRISLMHAGKVL 484
Cdd:PRK14247 164 QPEVLLADEPTANLDPENTAKIESLFLELKKD--MTIVLVTHFPQQAARIsDYVAFLYKGQIV 224
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
293-484 |
2.12e-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: 93.00 E-value: 2.12e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 293 VSFRIERGEIFGFLGSNGCGKSTTMKMLTGLL--PASEGTCALFGQPVDASDMatRRRVGYMSQAFSLYAELSVRQNLVL 370
Cdd:cd03213 28 VSGKAKPGELTAIMGPSGAGKSTLLNALAGRRtgLGVSGEVLINGRPLDKRSF--RKIIGYVPQDDILHPTLTVRETLMF 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 371 HARLfhlpaDGIPArvGEmlrrfdlekvadelpndlplgiRQRLSLAVAVIHKPEILILDEPTSGVDPV-ARDgfweLMV 449
Cdd:cd03213 106 AAKL-----RGLSG--GE----------------------RKRVSIALELVSNPSLLFLDEPTSGLDSSsALQ----VMS 152
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 15600424 450 ELSR--RDGVTIFISTH------FmneaQRCDRISLMHAGKVL 484
Cdd:cd03213 153 LLRRlaDTGRTIICSIHqpsseiF----ELFDKLLLLSQGRVI 191
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
283-482 |
2.14e-21 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 93.63 E-value: 2.14e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 283 RFGDFVAVDHVSFRIERGEIFGFLGSNGCGKSTTMKMLTGLLPASEGTCALFGQPVDA-SDMATRRRVGYMSQAFSLYAE 361
Cdd:PRK10247 16 LAGDAKILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFEGEDISTlKPEIYRQQVSYCAQTPTLFGD 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 362 lSVRQNLVLHARLFHLPADgiPARVGEMLRRFDL-EKVADELPNDLPLGIRQRLSLAVAVIHKPEILILDEPTSGVDPVA 440
Cdd:PRK10247 96 -TVYDNLIFPWQIRNQQPD--PAIFLDDLERFALpDTILTKNIAELSGGEKQRISLIRNLQFMPKVLLLDEITSALDESN 172
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 15600424 441 RDGFWELMVELSRRDGVTIFISTHFMNEAQRCDR-ISLM-HAGK 482
Cdd:PRK10247 173 KHNVNEIIHRYVREQNIAVLWVTHDKDEINHADKvITLQpHAGE 216
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
10-231 |
2.23e-21 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 94.85 E-value: 2.23e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 10 SLRGVSLRYGETRAVDDVSLEIPANRMVGLIGPDGVGKSSLLALLAGARKMQDGEIrVLDGDMRDRRHRRAVCPRIAYMP 89
Cdd:PRK10575 13 ALRNVSFRVPGRTLLHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEI-LLDAQPLESWSSKAFARKVAYLP 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 90 QGLgknlyPT---LSVFENVDFfGRL-----FGHDKAERERRIADLLQSTGLAPFAERPAGKLSGGMKQKLGLCCALIHD 161
Cdd:PRK10575 92 QQL-----PAaegMTVRELVAI-GRYpwhgaLGRFGAADREKVEEAISLVGLKPLAHRLVDSLSGGERQRAWIAMLVAQD 165
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15600424 162 PDLLILDEPTTGVDPLSRNQFWELIGRIRAGReGMSVLVATAYMEEAERF-DWLVAMDDGKVLATGTPQEL 231
Cdd:PRK10575 166 SRCLLLDEPTSALDIAHQVDVLALVHRLSQER-GLTVIAVLHDINMAARYcDYLVALRGGEMIAQGTPAEL 235
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
6-231 |
2.98e-21 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 94.91 E-value: 2.98e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 6 SGVASLRGVSLRYGE-TRAVDDVSLEIPANRMVGLIGPDGVGKSSLLALLAGARKMQDGEIrVLDGDMRDRRHRRAVCPR 84
Cdd:PRK13636 3 DYILKVEELNYNYSDgTHALKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRI-LFDGKPIDYSRKGLMKLR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 85 --IAYMPQGLGKNLYpTLSVFENVDFFGRLFGHDKAERERRIADLLQSTGLAPFAERPAGKLSGGMKQKLGLCCALIHDP 162
Cdd:PRK13636 82 esVGMVFQDPDNQLF-SASVYQDVSFGAVNLKLPEDEVRKRVDNALKRTGIEHLKDKPTHCLSFGQKKRVAIAGVLVMEP 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 163 DLLILDEPTTGVDPLSRNQFWELIGRIRAGReGMSVLVATAYMEEAERF-DWLVAMDDGKVLATGTPQEL 231
Cdd:PRK13636 161 KVLVLDEPTAGLDPMGVSEIMKLLVEMQKEL-GLTIIIATHDIDIVPLYcDNVFVMKEGRVILQGNPKEV 229
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
270-492 |
3.68e-21 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 94.90 E-value: 3.68e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 270 APRIAIEAEGLtcrfgdfvavDHVSFRIERGEIFGFLGSNGCGKSTTMKMLTGLLPASEGTCALFGQPVDASD-----MA 344
Cdd:PRK13641 13 SPGTPMEKKGL----------DNISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITIAGYHITPETgnknlKK 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 345 TRRRVGYMSQafslYAELSVRQNLVLH-----ARLFHLPADGIPARVGEMLRRFDL-EKVADELPNDLPLGIRQRLSLAV 418
Cdd:PRK13641 83 LRKKVSLVFQ----FPEAQLFENTVLKdvefgPKNFGFSEDEAKEKALKWLKKVGLsEDLISKSPFELSGGQMRRVAIAG 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15600424 419 AVIHKPEILILDEPTSGVDPVARDGFWELMVELsRRDGVTIFISTHFMNE-AQRCDRISLMHAGKVLASDTPDEL 492
Cdd:PRK13641 159 VMAYEPEILCLDEPAAGLDPEGRKEMMQLFKDY-QKAGHTVILVTHNMDDvAEYADDVLVLEHGKLIKHASPKEI 232
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
11-227 |
4.05e-21 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 95.64 E-value: 4.05e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 11 LRGVSLRY----GETRAVDDVSLEIPANRMVGLIGPDGVGKSSLLALLAGARKMQDGEIRVlDGdmRD---------RRH 77
Cdd:PRK11153 4 LKNISKVFpqggRTIHALNNVSLHIPAGEIFGVIGASGAGKSTLIRCINLLERPTSGRVLV-DG--QDltalsekelRKA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 78 RRavcpRIAYMPQGLgkNLYPTLSVFENVDFFGRLFGHDKAERERRIADLLQSTGLAPFAER-PAgKLSGGMKQKLGLCC 156
Cdd:PRK11153 81 RR----QIGMIFQHF--NLLSSRTVFDNVALPLELAGTPKAEIKARVTELLELVGLSDKADRyPA-QLSGGQKQRVAIAR 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15600424 157 ALIHDPDLLILDEPTTGVDPLSRNQFWELIGRIRagRE-GMSVLVATAYMEEAERF-DWLVAMDDGKVLATGT 227
Cdd:PRK11153 154 ALASNPKVLLCDEATSALDPATTRSILELLKDIN--RElGLTIVLITHEMDVVKRIcDRVAVIDAGRLVEQGT 224
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
8-437 |
6.26e-21 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 97.88 E-value: 6.26e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 8 VASLRGVSLRYGETRAV-DDVSLEIPANRMVGLIGPDGVGKSSLLALLAGARKMQDGEIRVLDGdmrdrrhrravcPRIA 86
Cdd:PRK11819 6 IYTMNRVSKVVPPKKQIlKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKEFEGEARPAPG------------IKVG 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 87 YMPQGlgKNLYPTLSVFENV--------DFFGRL------FGHDKA------ERERRIADLLQSTGLA------------ 134
Cdd:PRK11819 74 YLPQE--PQLDPEKTVRENVeegvaevkAALDRFneiyaaYAEPDAdfdalaAEQGELQEIIDAADAWdldsqleiamda 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 135 ---PFAERPAGKLSGGMKQKLGLCCALIHDPDLLILDEPTTGVDPLSRNqfW-EligRIRAGREGMSVLV---------A 201
Cdd:PRK11819 152 lrcPPWDAKVTKLSGGERRRVALCRLLLEKPDMLLLDEPTNHLDAESVA--WlE---QFLHDYPGTVVAVthdryfldnV 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 202 TAYMEEAER----------FDWLVAMDdgKVLATGTPQEL-RERTGTQSLE-----------------SAFIALLPES-- 251
Cdd:PRK11819 227 AGWILELDRgrgipwegnySSWLEQKA--KRLAQEEKQEAaRQKALKRELEwvrqspkarqakskarlARYEELLSEEyq 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 252 KRAGHHRLVIPPrpqsegAPR---IAIEAEGLTCRFGDFVAVDHVSFRIERGEIFGFLGSNGCGKSTTMKMLTGLLPASE 328
Cdd:PRK11819 305 KRNETNEIFIPP------GPRlgdKVIEAENLSKSFGDRLLIDDLSFSLPPGGIVGIIGPNGAGKSTLFKMITGQEQPDS 378
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 329 GTCALfGQPVdasdmatrrRVGYMSQAfslyaelsvRQNLVLHARLFHLPADG----------IPAR--VGemlrRF--- 393
Cdd:PRK11819 379 GTIKI-GETV---------KLAYVDQS---------RDALDPNKTVWEEISGGldiikvgnreIPSRayVG----RFnfk 435
|
490 500 510 520
....*....|....*....|....*....|....*....|....*.
gi 15600424 394 --DLEKVADELPNdlplGIRQRLSLAVAVIHKPEILILDEPTSGVD 437
Cdd:PRK11819 436 ggDQQKKVGVLSG----GERNRLHLAKTLKQGGNVLLLDEPTNDLD 477
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
10-222 |
6.36e-21 |
|
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of the protease secretion system PrtD, a 60-kDa integral membrane protein sharing 37% identity with HlyB, the ABC component of the alpha-hemolysin secretion pathway, in the C-terminal domain. They export degradative enzymes by using a type I protein secretion system and lack an N-terminal signal peptide, but contain a C-terminal secretion signal. The Type I secretion apparatus is made up of three components, an ABC transporter, a membrane fusion protein (MFP), and an outer membrane protein (OMP). For the HlyA transporter complex, HlyB (ABC transporter) and HlyD (MFP) reside in the inner membrane of E. coli. The OMP component is TolC, which is thought to interact with the MFP to form a continuous channel across the periplasm from the cytoplasm to the exterior. HlyB belongs to the family of ABC transporters, which are ubiquitous, ATP-dependent transmembrane pumps or channels. The spectrum of transport substrates ranges from inorganic ions, nutrients such as amino acids, sugars, or peptides, hydrophobic drugs, to large polypeptides, such as HlyA.
Pssm-ID: 213213 [Multi-domain] Cd Length: 173 Bit Score: 90.74 E-value: 6.36e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 10 SLRGVSLRYGETRA--VDDVSLEIPANRMVGLIGPDGVGKSSLLALLAGARKMQDGEIRvLDGDMRDRRHRRAVCPRIAY 87
Cdd:cd03246 2 EVENVSFRYPGAEPpvLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVR-LDGADISQWDPNELGDHVGY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 88 MPQGLgkNLYPTlSVFENVdffgrlfghdkaererriadllqstglapfaerpagkLSGGMKQKLGLCCALIHDPDLLIL 167
Cdd:cd03246 81 LPQDD--ELFSG-SIAENI-------------------------------------LSGGQRQRLGLARALYGNPRILVL 120
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 15600424 168 DEPTTGVDPLSRNQFWELIGRIRAGreGMSVLVATAYMEEAERFDWLVAMDDGKV 222
Cdd:cd03246 121 DEPNSHLDVEGERALNQAIAALKAA--GATRIVIAHRPETLASADRILVLEDGRV 173
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
8-171 |
6.51e-21 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 97.44 E-value: 6.51e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 8 VASLRGVSLRYGETRAVDDVSLEIPANRMVGLIGPDGVGKSSLLALLAGARKMQDGEIrvldgdmrdRRHRRAvcpRIAY 87
Cdd:COG0488 315 VLELEGLSKSYGDKTLLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPDSGTV---------KLGETV---KIGY 382
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 88 MPQGLgKNLYPTLSVFENVdffgRLFGHDKAERERRiaDLLQSTGLAP-FAERPAGKLSGGMKQKLGLCCALIHDPDLLI 166
Cdd:COG0488 383 FDQHQ-EELDPDKTVLDEL----RDGAPGGTEQEVR--GYLGRFLFSGdDAFKPVGVLSGGEKARLALAKLLLSPPNVLL 455
|
....*
gi 15600424 167 LDEPT 171
Cdd:COG0488 456 LDEPT 460
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
275-474 |
8.89e-21 |
|
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the bacterial CcmAB transporter. The CCM family is involved in bacterial cytochrome c biogenesis. Cytochrome c maturation in E. coli requires the ccm operon, which encodes eight membrane proteins (CcmABCDEFGH). CcmE is a periplasmic heme chaperon that binds heme covalently and transfers it onto apocytochrome c in the presence of CcmF, CcmG, and CcmH. The CcmAB proteins represent an ABC transporter and the CcmCD proteins participate in heme transfer to CcmE.
Pssm-ID: 213198 [Multi-domain] Cd Length: 201 Bit Score: 91.40 E-value: 8.89e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 275 IEAEGLTCRFGDFVAVDHVSFRIERGEIFGFLGSNGCGKSTTMKMLTGLLPASEGTCALFGQPVDASDMATRRRVGYMSQ 354
Cdd:cd03231 1 LEADELTCERDGRALFSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNGGPLDFQRDSIARGLLYLGH 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 355 AFSLYAELSVRQNLvlhaRLFHlpADGIPARVGEMLRRFDLEKVADELPNDLPLGIRQRLSLAVAVIHKPEILILDEPTS 434
Cdd:cd03231 81 APGIKTTLSVLENL----RFWH--ADHSDEQVEEALARVGLNGFEDRPVAQLSAGQQRRVALARLLLSGRPLWILDEPTT 154
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 15600424 435 GVDPVARDGFWELMVELSRRDGVTIFISTHFMNEAQRCDR 474
Cdd:cd03231 155 ALDKAGVARFAEAMAGHCARGGMVVLTTHQDLGLSEAGAR 194
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
8-231 |
1.01e-20 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 93.13 E-value: 1.01e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 8 VASLRG--VSLRYGETRAVDDVSLEIPANRMVGLIGPDGVGKSSLLALLAGARKMQDGEIrVLDGDMRDRRHRRAVCPRI 85
Cdd:PRK10253 5 VARLRGeqLTLGYGKYTVAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHV-WLDGEHIQHYASKEVARRI 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 86 AYMPQGLGKnlyPTLSVFENVDFFGR-----LFGHDKAERERRIADLLQSTGLAPFAERPAGKLSGGMKQKLGLCCALIH 160
Cdd:PRK10253 84 GLLAQNATT---PGDITVQELVARGRyphqpLFTRWRKEDEEAVTKAMQATGITHLADQSVDTLSGGQRQRAWIAMVLAQ 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15600424 161 DPDLLILDEPTTGVDPLSRNQFWELIGRIraGREGMSVLVATAY-MEEAERF-DWLVAMDDGKVLATGTPQEL 231
Cdd:PRK10253 161 ETAIMLLDEPTTWLDISHQIDLLELLSEL--NREKGYTLAAVLHdLNQACRYaSHLIALREGKIVAQGAPKEI 231
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
286-486 |
1.01e-20 |
|
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: 90.45 E-value: 1.01e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 286 DFVAVDHVSFRIERGEIFGFLGSNGCGKSTTMKMLTGLLPASEGTCALFGQPVDASDMATRRRVGYMSQAFSLYAElSVR 365
Cdd:cd03247 14 EQQVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDGVPVSDLEKALSSLISVLNQRPYLFDT-TLR 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 366 QNLvlharlfhlpadGIPARVGEmlrrfdlekvadelpndlplgiRQRLSLAVAVIHKPEILILDEPTSGVDPVARDGFW 445
Cdd:cd03247 93 NNL------------GRRFSGGE----------------------RQRLALARILLQDAPIVLLDEPTVGLDPITERQLL 138
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 15600424 446 ELMVELSRrdGVTIFISTHFMNEAQRCDRISLMHAGKVLAS 486
Cdd:cd03247 139 SLIFEVLK--DKTLIWITHHLTGIEHMDKILFLENGKIIMQ 177
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
286-495 |
1.05e-20 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 93.31 E-value: 1.05e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 286 DFVAVDHVSFRIERGEIFGFLGSNGCGKSTTMKMLTGLLPASEGTCALFGQPV-----DASDMATRRRVGYM-----SQA 355
Cdd:PRK13646 19 EHQAIHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVDDITIthktkDKYIRPVRKRIGMVfqfpeSQL 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 356 FslyaELSVRQNLVLHARLFHLPADGIPARVGEMLRRFDLEK-VADELPNDLPLGIRQRLSLAVAVIHKPEILILDEPTS 434
Cdd:PRK13646 99 F----EDTVEREIIFGPKNFKMNLDEVKNYAHRLLMDLGFSRdVMSQSPFQMSGGQMRKIAIVSILAMNPDIIVLDEPTA 174
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15600424 435 GVDPVARDGFWELMVELSRRDGVTIFISTHFMNE-AQRCDRISLMHAGKVLASDTPDELVRQ 495
Cdd:PRK13646 175 GLDPQSKRQVMRLLKSLQTDENKTIILVSHDMNEvARYADEVIVMKEGSIVSQTSPKELFKD 236
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
288-498 |
1.25e-20 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 92.30 E-value: 1.25e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 288 VAVDH----VSFRIERGEIFGFLGSNGCGKSTTMKMLTGLLPaSEGTCALFGQPV---DASDMATRRrvGYMSQAFSLYA 360
Cdd:PRK03695 6 VAVSTrlgpLSAEVRAGEILHLVGPNGAGKSTLLARMAGLLP-GSGSIQFAGQPLeawSAAELARHR--AYLSQQQTPPF 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 361 ELSVRQNLVLHaRLFHLPADGIPARVGEMLRRFDLEkvaDELP---NDLPLGIRQRLSLAVAV--IHkPEI------LIL 429
Cdd:PRK03695 83 AMPVFQYLTLH-QPDKTRTEAVASALNEVAEALGLD---DKLGrsvNQLSGGEWQRVRLAAVVlqVW-PDInpagqlLLL 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 430 DEPTSGVDpVARDGFWELMVELSRRDGVTIFISTHFMNE-AQRCDRISLMHAGKVLASDTPDELVRQRGL 498
Cdd:PRK03695 158 DEPMNSLD-VAQQAALDRLLSELCQQGIAVVMSSHDLNHtLRHADRVWLLKQGKLLASGRRDEVLTPENL 226
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
10-235 |
1.41e-20 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 92.94 E-value: 1.41e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 10 SLRGVSLRYGETR--AVDDVSLEIPANRMVGLIGPDGVGKSSLLALLAG---------ARKMQDGeIRVLDGDMRDRRHR 78
Cdd:PRK13640 7 EFKHVSFTYPDSKkpALNDISFSIPRGSWTALIGHNGSGKSTISKLINGlllpddnpnSKITVDG-ITLTAKTVWDIREK 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 79 RAVcpriaympqglgknlyptlsVFENVD--FFGRLFGHDKA-----------ERERRIADLLQSTGLAPFAERPAGKLS 145
Cdd:PRK13640 86 VGI--------------------VFQNPDnqFVGATVGDDVAfglenravprpEMIKIVRDVLADVGMLDYIDSEPANLS 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 146 GGMKQKLGLCCALIHDPDLLILDEPTTGVDPLSRNQFWELIGRIRAgREGMSVLVATAYMEEAERFDWLVAMDDGKVLAT 225
Cdd:PRK13640 146 GGQKQRVAIAGILAVEPKIIILDESTSMLDPAGKEQILKLIRKLKK-KNNLTVISITHDIDEANMADQVLVLDDGKLLAQ 224
|
250
....*....|
gi 15600424 226 GTPQELRERT 235
Cdd:PRK13640 225 GSPVEIFSKV 234
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
20-231 |
1.54e-20 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 93.76 E-value: 1.54e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 20 ETRAVDDVSLEIPANRMVGLIGPDGVGKSSLLALLAGARKMQDGEIRVldGDMRDRRHRRAVCPRIAYMPQGLG--KNLY 97
Cdd:PRK13631 38 ELVALNNISYTFEKNKIYFIIGNSGSGKSTLVTHFNGLIKSKYGTIQV--GDIYIGDKKNNHELITNPYSKKIKnfKELR 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 98 PTLS-VFENVDF------------FGRL-FGHDKAERERRIADLLQSTGL-APFAERPAGKLSGGMKQKLGLCCALIHDP 162
Cdd:PRK13631 116 RRVSmVFQFPEYqlfkdtiekdimFGPVaLGVKKSEAKKLAKFYLNKMGLdDSYLERSPFGLSGGQKRRVAIAGILAIQP 195
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 163 DLLILDEPTTGVDPLSRNQFWELIgrIRAGREGMSVLVATAYMEEA-ERFDWLVAMDDGKVLATGTPQEL 231
Cdd:PRK13631 196 EILIFDEPTAGLDPKGEHEMMQLI--LDAKANNKTVFVITHTMEHVlEVADEVIVMDKGKILKTGTPYEI 263
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
289-504 |
1.72e-20 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 92.36 E-value: 1.72e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 289 AVDHVSFRIERGEIFGFLGSNGCGKSTTMKMLTGLLPASEGTCALFGqpVDASDMA----TRRRVGYMSQ-AFSLYAELS 363
Cdd:PRK13644 17 ALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLVSG--IDTGDFSklqgIRKLVGIVFQnPETQFVGRT 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 364 VRQNLVLHARLFHLPADGIPARVGEMLRRFDLEKVADELPNDLPLGIRQRLSLAVAVIHKPEILILDEPTSGVDPVARDG 443
Cdd:PRK13644 95 VEEDLAFGPENLCLPPIEIRKRVDRALAEIGLEKYRHRSPKTLSGGQGQCVALAGILTMEPECLIFDEVTSMLDPDSGIA 174
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15600424 444 FWELMVELSRRdGVTIFISTHFMNEAQRCDRISLMHAGKVLASDTPDELVRQRGLPTLEAT 504
Cdd:PRK13644 175 VLERIKKLHEK-GKTIVYITHNLEELHDADRIIVMDRGKIVLEGEPENVLSDVSLQTLGLT 234
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
11-262 |
2.02e-20 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 92.36 E-value: 2.02e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 11 LRGVSLRYGE-TRAVDDVSLEIPANRMVGLIGPDGVGKSSLLALLAGARKMQDGEIRVLDGDMRDRRHRRAVCPRIAYmp 89
Cdd:PRK13644 4 LENVSYSYPDgTPALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLVSGIDTGDFSKLQGIRKLVGI-- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 90 qglgknlyptlsVFEN--VDFFGRLFGHDKA-----------ERERRIADLLQSTGLAPFAERPAGKLSGGMKQKLGLCC 156
Cdd:PRK13644 82 ------------VFQNpeTQFVGRTVEEDLAfgpenlclppiEIRKRVDRALAEIGLEKYRHRSPKTLSGGQGQCVALAG 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 157 ALIHDPDLLILDEPTTGVDPLSRNQFWELIGRIRagREGMSVLVATAYMEEAERFDWLVAMDDGKVLATGTPQELRERTG 236
Cdd:PRK13644 150 ILTMEPECLIFDEVTSMLDPDSGIAVLERIKKLH--EKGKTIVYITHNLEELHDADRIIVMDRGKIVLEGEPENVLSDVS 227
|
250 260
....*....|....*....|....*.
gi 15600424 237 TQSLESAFIALLPESKRAGHHRLVIP 262
Cdd:PRK13644 228 LQTLGLTPPSLIELAENLKMHGVVIP 253
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
10-227 |
2.05e-20 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 91.23 E-value: 2.05e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 10 SLRGVSLRYGETRAVDDVSLEIPANRMVGLIGPDGVGKSSLLALLAGARKMQDGEIRVLDG--DMRDRRHRRAvcprIAY 87
Cdd:COG4161 4 QLKNINCFYGSHQALFDINLECPSGETLVLLGPSGAGKSSLLRVLNLLETPDSGQLNIAGHqfDFSQKPSEKA----IRL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 88 MPQGLGK-----NLYPTLSVFEN-VDFFGRLFGHDKAERERRIADLLQSTGLAPFAERPAGKLSGGMKQKLGLCCALIHD 161
Cdd:COG4161 80 LRQKVGMvfqqyNLWPHLTVMENlIEAPCKVLGLSKEQAREKAMKLLARLRLTDKADRFPLHLSGGQQQRVAIARALMME 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15600424 162 PDLLILDEPTTGVDPLSRNQFWELIGRIraGREGMSVLVATAYMEEAERF-DWLVAMDDGKVLATGT 227
Cdd:COG4161 160 PQVLLFDEPTAALDPEITAQVVEIIREL--SQTGITQVIVTHEVEFARKVaSQVVYMEKGRIIEQGD 224
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
263-464 |
2.25e-20 |
|
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: 95.89 E-value: 2.25e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 263 PRPQSEGAPRIAIEAEGLTCRF-GDFVAVDHVSFRIERGEIFGFLGSNGCGKSTTMKMLTGLLPASEGTCALFGQPV-DA 340
Cdd:TIGR02868 323 PAAGAVGLGKPTLELRDLSAGYpGAPPVLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPLQGEVTLDGVPVsSL 402
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 341 SDMATRRRVGYMSQAFSLYAElSVRQNLVLhARlfhlpADGIPARVGEMLRRFDLEKVADELPNDLPL-----------G 409
Cdd:TIGR02868 403 DQDEVRRRVSVCAQDAHLFDT-TVRENLRL-AR-----PDATDEELWAALERVGLADWLRALPDGLDTvlgeggarlsgG 475
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 15600424 410 IRQRLSLAVAVIHKPEILILDEPTSGVDPVARDGFWELMveLSRRDGVTIFISTH 464
Cdd:TIGR02868 476 ERQRLALARALLADAPILLLDEPTEHLDAETADELLEDL--LAALSGRTVVLITH 528
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
258-492 |
2.80e-20 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 92.99 E-value: 2.80e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 258 RLVIPPRPQSEGaprIAIEAEGLTCRFGD-----FVAVDHVSFRIERGEIFGFLGSNGCGKSTTMKMLTGLLPASEGTCA 332
Cdd:PRK13631 8 KKLKVPNPLSDD---IILRVKNLYCVFDEkqeneLVALNNISYTFEKNKIYFIIGNSGSGKSTLVTHFNGLIKSKYGTIQ 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 333 L----FGQPVDASDMAT-------------RRRVGYMSQafslYAELSVRQNLVLHARLFHLPADGIPARVGEMLRRFDL 395
Cdd:PRK13631 85 VgdiyIGDKKNNHELITnpyskkiknfkelRRRVSMVFQ----FPEYQLFKDTIEKDIMFGPVALGVKKSEAKKLAKFYL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 396 EKVA------DELPNDLPLGIRQRLSLAVAVIHKPEILILDEPTSGVDPVARDGFWELMVElSRRDGVTIFISTHFM-NE 468
Cdd:PRK13631 161 NKMGlddsylERSPFGLSGGQKRRVAIAGILAIQPEILIFDEPTAGLDPKGEHEMMQLILD-AKANNKTVFVITHTMeHV 239
|
250 260
....*....|....*....|....
gi 15600424 469 AQRCDRISLMHAGKVLASDTPDEL 492
Cdd:PRK13631 240 LEVADEVIVMDKGKILKTGTPYEI 263
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
7-236 |
3.14e-20 |
|
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: 95.55 E-value: 3.14e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 7 GVASLRGVSLRYG--ETRAVDDVSLEIPANRMVGLIGPDGVGKSSLLALLAGARKMQDGEIrVLDGDmrDRRHRRAVCPR 84
Cdd:TIGR02203 329 GDVEFRNVTFRYPgrDRPALDSISLVIEPGETVALVGRSGSGKSTLVNLIPRFYEPDSGQI-LLDGH--DLADYTLASLR 405
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 85 --IAYMPQGLgknlypTL---SVFENVDFfGRLFGHDKAERERRIADL-LQS------TGLAPFAERPAGKLSGGMKQKL 152
Cdd:TIGR02203 406 rqVALVSQDV------VLfndTIANNIAY-GRTEQADRAEIERALAAAyAQDfvdklpLGLDTPIGENGVLLSGGQRQRL 478
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 153 GLCCALIHDPDLLILDEPTTGVDPLSRNQFWELIGRIRAGREGMSVLVATAYMEEAERfdwLVAMDDGKVLATGTPQELR 232
Cdd:TIGR02203 479 AIARALLKDAPILILDEATSALDNESERLVQAALERLMQGRTTLVIAHRLSTIEKADR---IVVMDDGRIVERGTHNELL 555
|
....
gi 15600424 233 ERTG 236
Cdd:TIGR02203 556 ARNG 559
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
17-231 |
3.27e-20 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 93.94 E-value: 3.27e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 17 RYGETRAVDDVSLEIPANRMVGLIGPDGVGKSSLLALLAGARKMQDGEI--------RVLDGDMRDRRHRRavcprIAYM 88
Cdd:PRK10070 37 KTGLSLGVKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVlidgvdiaKISDAELREVRRKK-----IAMV 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 89 PQGLGknLYPTLSVFENVDFFGRLFGHDKAERERRIADLLQSTGLAPFAERPAGKLSGGMKQKLGLCCALIHDPDLLILD 168
Cdd:PRK10070 112 FQSFA--LMPHMTVLDNTAFGMELAGINAEERREKALDALRQVGLENYAHSYPDELSGGMRQRVGLARALAINPDILLMD 189
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15600424 169 EPTTGVDPLSRNQFWELIGRIRAGREGMSVLVATAYMEEAERFDWLVAMDDGKVLATGTPQEL 231
Cdd:PRK10070 190 EAFSALDPLIRTEMQDELVKLQAKHQRTIVFISHDLDEAMRIGDRIAIMQNGEVVQVGTPDEI 252
|
|
| PvdE |
COG4615 |
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ... |
293-496 |
4.59e-20 |
|
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: 94.86 E-value: 4.59e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 293 VSFRIERGEIFGFLGSNGCGKSTTMKMLTGLLPASEGTCALFGQPVDASDMATRRrvgymsQAFSlyaelSVRQNLVLHA 372
Cdd:COG4615 351 IDLTIRRGELVFIVGGNGSGKSTLAKLLTGLYRPESGEILLDGQPVTADNREAYR------QLFS-----AVFSDFHLFD 419
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 373 RLFHLPADGIPARVGEMLRRFDLE-KVA---DELPN-DLPLGIRQRLSLAVAVIHKPEILILDEPTSGVDPVARDGFW-E 446
Cdd:COG4615 420 RLLGLDGEADPARARELLERLELDhKVSvedGRFSTtDLSQGQRKRLALLVALLEDRPILVFDEWAADQDPEFRRVFYtE 499
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 15600424 447 LMVELsRRDGVTIFISTH----FmneaQRCDRISLMHAGKvLASDTPDELVRQR 496
Cdd:COG4615 500 LLPEL-KARGKTVIAISHddryF----DLADRVLKMDYGK-LVELTGPAALAAS 547
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
10-221 |
4.76e-20 |
|
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: 89.07 E-value: 4.76e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 10 SLRGVSLRYGETR-----AVDDVSLEIPANRMVGLIGPDGVGKSSLL-ALLagarkmqdGEIRVLDGdmrdrrhRRAVCP 83
Cdd:cd03250 2 SVEDASFTWDSGEqetsfTLKDINLEVPKGELVAIVGPVGSGKSSLLsALL--------GELEKLSG-------SVSVPG 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 84 RIAYMPQglgknlYPTL---SVFENVdffgrLFGHDkaERERRIADLLQSTGLAP-FAERPAG----------KLSGGMK 149
Cdd:cd03250 67 SIAYVSQ------EPWIqngTIRENI-----LFGKP--FDEERYEKVIKACALEPdLEILPDGdlteigekgiNLSGGQK 133
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15600424 150 QKLGLCCALIHDPDLLILDEPTTGVDPLSRNQFWE--LIGRIRAGRegmSVLVATAYMEEAERFDWLVAMDDGK 221
Cdd:cd03250 134 QRISLARAVYSDADIYLLDDPLSAVDAHVGRHIFEncILGLLLNNK---TRILVTHQLQLLPHADQIVVLDNGR 204
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
274-469 |
5.16e-20 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 90.53 E-value: 5.16e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 274 AIEAEGLTCRFGDFVAVDHVSFRIERGEIFGFLGSNGCGKSTTMKMLTGLLPASEGTCALFGQPVDASDmATRrrvGYMS 353
Cdd:PRK11248 1 MLQISHLYADYGGKPALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDGKPVEGPG-AER---GVVF 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 354 QAFSLYAELSVRQNLVLHARLFHLPADGIPARVGEMLRRFDLEKVADELPNDLPLGIRQRLSLAVAVIHKPEILILDEPT 433
Cdd:PRK11248 77 QNEGLLPWRNVQDNVAFGLQLAGVEKMQRLEIAHQMLKKVGLEGAEKRYIWQLSGGQRQRVGIARALAANPQLLLLDEPF 156
|
170 180 190
....*....|....*....|....*....|....*.
gi 15600424 434 SGVDPVARDGFWELMVELSRRDGVTIFISTHFMNEA 469
Cdd:PRK11248 157 GALDAFTREQMQTLLLKLWQETGKQVLLITHDIEEA 192
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
275-493 |
5.45e-20 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 90.82 E-value: 5.45e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 275 IEAEGLTCRFGDFVAVDHVSFRIERGEIFGFLGSNGCGKSTTMKMLTGLLPASEGTCALFGQPVDA-SDMATRRRVGYMS 353
Cdd:PRK10253 8 LRGEQLTLGYGKYTVAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIQHyASKEVARRIGLLA 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 354 QAFSLYAELSVrQNLVLHARLFHLPA-----DGIPARVGEMLRRFDLEKVADELPNDLPLGIRQRLSLAVAVIHKPEILI 428
Cdd:PRK10253 88 QNATTPGDITV-QELVARGRYPHQPLftrwrKEDEEAVTKAMQATGITHLADQSVDTLSGGQRQRAWIAMVLAQETAIML 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15600424 429 LDEPTSGVDPVARDGFWELMVELSRRDGVTIFISTHFMNEAQR-CDRISLMHAGKVLASDTPDELV 493
Cdd:PRK10253 167 LDEPTTWLDISHQIDLLELLSELNREKGYTLAAVLHDLNQACRyASHLIALREGKIVAQGAPKEIV 232
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
293-493 |
5.54e-20 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 95.11 E-value: 5.54e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 293 VSFRIERGEIFGFLGSNGCGKSTTMKMLTGLLPAS---EGTCALFGQPVDASDMatRRRVGYMSQAFSLYAELSVRQNLV 369
Cdd:TIGR00955 44 VSGVAKPGELLAVMGSSGAGKTTLMNALAFRSPKGvkgSGSVLLNGMPIDAKEM--RAISAYVQQDDLFIPTLTVREHLM 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 370 LHARLF---HLPADGIPARVGEMLRRFDLEKVADEL---PND---LPLGIRQRLSLAVAVIHKPEILILDEPTSGVDPVA 440
Cdd:TIGR00955 122 FQAHLRmprRVTKKEKRERVDEVLQALGLRKCANTRigvPGRvkgLSGGERKRLAFASELLTDPPLLFCDEPTSGLDSFM 201
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15600424 441 RDGFWELMVELSRRdGVTIFISTH---------FmneaqrcDRISLMHAGKVLASDTPDELV 493
Cdd:TIGR00955 202 AYSVVQVLKGLAQK-GKTIICTIHqpsselfelF-------DKIILMAEGRVAYLGSPDQAV 255
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
10-231 |
5.87e-20 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 94.89 E-value: 5.87e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 10 SLRGVSLRY--GETRAVDDVSLEIPANRMVGLIGPDGVGKSSLLALLAGARKMQDGEIRvLDG----DMRDRRHRRAVC- 82
Cdd:PRK11160 340 TLNNVSFTYpdQPQPVLKGLSLQIKAGEKVALLGRTGCGKSTLLQLLTRAWDPQQGEIL-LNGqpiaDYSEAALRQAISv 418
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 83 --PRIAYMPQGLGKNLyptlsvfenvdffgrLFGHDKAERERrIADLLQSTGLAPFAERPAG----------KLSGGMKQ 150
Cdd:PRK11160 419 vsQRVHLFSATLRDNL---------------LLAAPNASDEA-LIEVLQQVGLEKLLEDDKGlnawlgeggrQLSGGEQR 482
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 151 KLGLCCALIHDPDLLILDEPTTGVDPLSRNQFWELIGRIRAGRegmSVLVATAYMEEAERFDWLVAMDDGKVLATGTPQE 230
Cdd:PRK11160 483 RLGIARALLHDAPLLLLDEPTEGLDAETERQILELLAEHAQNK---TVLMITHRLTGLEQFDRICVMDNGQIIEQGTHQE 559
|
.
gi 15600424 231 L 231
Cdd:PRK11160 560 L 560
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
275-492 |
7.11e-20 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 94.23 E-value: 7.11e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 275 IEAEGLTCRFGDFVAVDHVSFRIERGEIFGFLGSNGCGKSTTMKMLTGLLPAS--EGTCALFGQPVDASDMATRRRVG-- 350
Cdd:PRK13549 6 LEMKNITKTFGGVKALDNVSLKVRAGEIVSLCGENGAGKSTLMKVLSGVYPHGtyEGEIIFEGEELQASNIRDTERAGia 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 351 YMSQAFSLYAELSVRQNLVLHARLFH---LPADGIPARVGEMLRRFDLEKVADELPNDLPLGIRQRLSLAVAVIHKPEIL 427
Cdd:PRK13549 86 IIHQELALVKELSVLENIFLGNEITPggiMDYDAMYLRAQKLLAQLKLDINPATPVGNLGLGQQQLVEIAKALNKQARLL 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15600424 428 ILDEPTSGVDPVARDGFWELMVELSRRDGVTIFIStHFMNEAQR-CDRISLMHAGKVLASDTPDEL 492
Cdd:PRK13549 166 ILDEPTASLTESETAVLLDIIRDLKAHGIACIYIS-HKLNEVKAiSDTICVIRDGRHIGTRPAAGM 230
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
290-483 |
7.17e-20 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 90.52 E-value: 7.17e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 290 VDHVSFRIERGEIFGFLGSNGCGKSTTMKMLTGLLPASEGTCALFGQPV---DASDMATRRRVGYMSQAFSLYA---ELS 363
Cdd:PRK10419 28 LNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWRGEPLaklNRAQRKAFRRDIQMVFQDSISAvnpRKT 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 364 VRQNLVLHAR-LFHLPADGIPARVGEMLRRFDL-EKVADELPNDLPLGIRQRLSLAVAVIHKPEILILDEPTSGVDPVAR 441
Cdd:PRK10419 108 VREIIREPLRhLLSLDKAERLARASEMLRAVDLdDSVLDKRPPQLSGGQLQRVCLARALAVEPKLLILDEAVSNLDLVLQ 187
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 15600424 442 DGFWELMVELSRRDGVTIFISTHFMNEAQR-CDRISLMHAGKV 483
Cdd:PRK10419 188 AGVIRLLKKLQQQFGTACLFITHDLRLVERfCQRVMVMDNGQI 230
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
275-493 |
7.28e-20 |
|
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in methanogenesis, methyl coenzyme M reductase, contains alpha, beta, and gamma chains. In older literature, the complex of alpha, beta, and gamma chains was termed component C, while this single chain protein was termed methyl coenzyme M reductase system component A2. [Energy metabolism, Methanogenesis]
Pssm-ID: 132313 [Multi-domain] Cd Length: 520 Bit Score: 94.10 E-value: 7.28e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 275 IEAEGLTCRFGDFVAVDHVSFRIERGEIFGFLGSNGCGKSTTMKMLTGL------------------------------- 323
Cdd:TIGR03269 1 IEVKNLTKKFDGKEVLKNISFTIEEGEVLGILGRSGAGKSVLMHVLRGMdqyeptsgriiyhvalcekcgyverpskvge 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 324 -LPASEGTCAL----FGQPVDASDMATRRRVGYMSQ-AFSLYAELSVRQNLVLHARLFHLPADGIPARVGEMLRRFDLEK 397
Cdd:TIGR03269 81 pCPVCGGTLEPeevdFWNLSDKLRRRIRKRIAIMLQrTFALYGDDTVLDNVLEALEEIGYEGKEAVGRAVDLIEMVQLSH 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 398 VADELPNDLPLGIRQRLSLAVAVIHKPEILILDEPTSGVDPVARDGFWELMVELSRRDGVTIFISTHFMNE-AQRCDRIS 476
Cdd:TIGR03269 161 RITHIARDLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALEEAVKASGISMVLTSHWPEViEDLSDKAI 240
|
250
....*....|....*..
gi 15600424 477 LMHAGKVLASDTPDELV 493
Cdd:TIGR03269 241 WLENGEIKEEGTPDEVV 257
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
10-227 |
7.77e-20 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 89.69 E-value: 7.77e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 10 SLRGVSLRYGETRAVDDVSLEIPANRMVGLIGPDGVGKSSLLALLAGARKMQDGEIRVLDG--DMRDRRHRRAvcprIAY 87
Cdd:PRK11124 4 QLNGINCFYGAHQALFDITLDCPQGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLNIAGNhfDFSKTPSDKA----IRE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 88 MPQGLGK-----NLYPTLSVFEN-VDFFGRLFGHDKAERERRIADLLQSTGLAPFAERPAGKLSGGMKQKLGLCCALIHD 161
Cdd:PRK11124 80 LRRNVGMvfqqyNLWPHLTVQQNlIEAPCRVLGLSKDQALARAEKLLERLRLKPYADRFPLHLSGGQQQRVAIARALMME 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15600424 162 PDLLILDEPTTGVDPLSRNQFWELIGRIRAgrEGMSVLVATAYMEEAERF-DWLVAMDDGKVLATGT 227
Cdd:PRK11124 160 PQVLLFDEPTAALDPEITAQIVSIIRELAE--TGITQVIVTHEVEVARKTaSRVVYMENGHIVEQGD 224
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
11-202 |
9.60e-20 |
|
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family transporter in which each gene contains an N-terminal membrane-spanning domain (pfam00664) and a C-terminal ATP-binding domain (pfam00005). In E. coli these genes were discovered as mutants which caused the terminal heme-copper oxidase complex cytochrome bd to fail to assemble. Recent work has shown that the transporter is involved in export of redox-active thiol compounds such as cysteine and glutathione. The linkage to assembly of the cytochrome bd complex is further supported by the conserved operon structure found outside the gammaproteobacteria (cydABCD) containing both the transporter and oxidase genes components. The genes used as the seed members for this model are all either found in the gammproteobacterial context or the CydABCD context. All members of this family scoring above trusted at the time of its creation were from genomes which encode a cytochrome bd complex.
Pssm-ID: 274331 [Multi-domain] Cd Length: 530 Bit Score: 93.96 E-value: 9.60e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 11 LRGVSLRY-GETRAVDDVSLEIPANRMVGLIGPDGVGKSSLLALLAGARKMQDGEIrVLDGDMRDRRHRRAVCPRIAYMP 89
Cdd:TIGR02868 337 LRDLSAGYpGAPPVLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPLQGEV-TLDGVPVSSLDQDEVRRRVSVCA 415
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 90 QGlgKNLYPTlSVFENVdffgRLFGHDKAERErrIADLLQSTGLAPF-AERPAG----------KLSGGMKQKLGLCCAL 158
Cdd:TIGR02868 416 QD--AHLFDT-TVRENL----RLARPDATDEE--LWAALERVGLADWlRALPDGldtvlgeggaRLSGGERQRLALARAL 486
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 15600424 159 IHDPDLLILDEPTTGVDPLSRNqfwELIGRIRAGREGMSVLVAT 202
Cdd:TIGR02868 487 LADAPILLLDEPTEHLDAETAD---ELLEDLLAALSGRTVVLIT 527
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
20-231 |
1.12e-19 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 90.22 E-value: 1.12e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 20 ETRAVDDVSLEIPANRMVGLIGPDGVGKSSLLALLAGARKMQDGEIRVLDGDMRDR---RHRRAVCPRIAYMPQglgknl 96
Cdd:PRK13646 19 EHQAIHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVDDITITHKtkdKYIRPVRKRIGMVFQ------ 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 97 YPTLSVFEN-----VDFFGRLFGHDKAERERRIADLLQSTG-------LAPFaerpagKLSGGMKQKLGLCCALIHDPDL 164
Cdd:PRK13646 93 FPESQLFEDtvereIIFGPKNFKMNLDEVKNYAHRLLMDLGfsrdvmsQSPF------QMSGGQMRKIAIVSILAMNPDI 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15600424 165 LILDEPTTGVDPLSRNQFWELIGRIRAgREGMSVLVATAYMEEAERF-DWLVAMDDGKVLATGTPQEL 231
Cdd:PRK13646 167 IVLDEPTAGLDPQSKRQVMRLLKSLQT-DENKTIILVSHDMNEVARYaDEVIVMKEGSIVSQTSPKEL 233
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
11-234 |
1.27e-19 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 90.18 E-value: 1.27e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 11 LRGVSLRYG---ETRAVDDVSLEIPANRMVGLIGPDGVGKSSLLALLAGARKMQDGEIrVLDGDMR------DRRHRrav 81
Cdd:PRK13650 7 VKNLTFKYKedqEKYTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQI-IIDGDLLteenvwDIRHK--- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 82 cprIAYMPQGlGKNLYPTLSVFENVDFFGRLFGHDKAERERRIADLLQSTGLAPFAERPAGKLSGGMKQKLGLCCALIHD 161
Cdd:PRK13650 83 ---IGMVFQN-PDNQFVGATVEDDVAFGLENKGIPHEEMKERVNEALELVGMQDFKEREPARLSGGQKQRVAIAGAVAMR 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15600424 162 PDLLILDEPTTGVDPLSRnqfWELIGRIRAGRE--GMSVLVATAYMEEAERFDWLVAMDDGKVLATGTPQELRER 234
Cdd:PRK13650 159 PKIIILDEATSMLDPEGR---LELIKTIKGIRDdyQMTVISITHDLDEVALSDRVLVMKNGQVESTSTPRELFSR 230
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
293-495 |
1.50e-19 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 89.80 E-value: 1.50e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 293 VSFRIERGEIFGFLGSNGCGKSTTMKMLTGLLPASEGTCALFGQPVDASDM-----ATRRRVGYMSQafslYAELSVRQN 367
Cdd:PRK13649 26 VNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDDTLITSTSKnkdikQIRKKVGLVFQ----FPESQLFEE 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 368 LVLHARLFHLPADGIPARVGEMLRRFDL------EKVADELPNDLPLGIRQRLSLAVAVIHKPEILILDEPTSGVDPVAR 441
Cdd:PRK13649 102 TVLKDVAFGPQNFGVSQEEAEALAREKLalvgisESLFEKNPFELSGGQMRRVAIAGILAMEPKILVLDEPTAGLDPKGR 181
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 15600424 442 DGFWELMVELsRRDGVTIFISTHFMNE-AQRCDRISLMHAGKVLASDTPDELVRQ 495
Cdd:PRK13649 182 KELMTLFKKL-HQSGMTIVLVTHLMDDvANYADFVYVLEKGKLVLSGKPKDIFQD 235
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
14-248 |
1.62e-19 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 89.56 E-value: 1.62e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 14 VSLRYGETrAVDDVSLEIPANRMVGLIGPDGVGKSSLLALLAGARKMQDGEIRVLDGDMRDRRHRRAVcpriAYMPQGLG 93
Cdd:PRK15056 14 VTWRNGHT-ALRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKISILGQPTRQALQKNLV----AYVPQSEE 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 94 KNL-YPTLsvFENVDFFGRlFGH------DKAERERRIADLLQSTGLAPFAERPAGKLSGGMKQKLGLCCALIHDPDLLI 166
Cdd:PRK15056 89 VDWsFPVL--VEDVVMMGR-YGHmgwlrrAKKRDRQIVTAALARVDMVEFRHRQIGELSGGQKKRVFLARAIAQQGQVIL 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 167 LDEPTTGVDPLSRNQFWELIGRIRAgrEGMSVLVATAYMEEAERFDWLVAMDDGKVLATGTPqelrERTGT-QSLESAFI 245
Cdd:PRK15056 166 LDEPFTGVDVKTEARIISLLRELRD--EGKTMLVSTHNLGSVTEFCDYTVMVKGTVLASGPT----ETTFTaENLELAFS 239
|
...
gi 15600424 246 ALL 248
Cdd:PRK15056 240 GVL 242
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
19-231 |
1.73e-19 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 89.48 E-value: 1.73e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 19 GETRAVDDVSLEIPANRMVGLIGPDGVGKSSLLALLAGARKMQDGEIRVlDGDMRDRRHRRAVCPRIAYMPQGLGKNLYP 98
Cdd:PRK13652 15 GSKEALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLI-RGEPITKENIREVRKFVGLVFQNPDDQIFS 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 99 TlSVFENVDFFGRLFGHDKAERERRIADLLQSTGLAPFAERPAGKLSGGMKQKLGLCCALIHDPDLLILDEPTTGVDPLS 178
Cdd:PRK13652 94 P-TVEQDIAFGPINLGLDEETVAHRVSSALHMLGLEELRDRVPHHLSGGEKKRVAIAGVIAMEPQVLVLDEPTAGLDPQG 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 15600424 179 RNQFWELIGRIrAGREGMSVLVATAYME-EAERFDWLVAMDDGKVLATGTPQEL 231
Cdd:PRK13652 173 VKELIDFLNDL-PETYGMTVIFSTHQLDlVPEMADYIYVMDKGRIVAYGTVEEI 225
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
1-230 |
1.74e-19 |
|
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase component [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 443338 [Multi-domain] Cd Length: 233 Bit Score: 88.26 E-value: 1.74e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 1 MTAGGSGVASLRGVSLRYGETRAV----DDVSLEIPANRMVGLIGPDGVGKSSLLALLAGARKMQDGEIRV-------LD 69
Cdd:COG4181 1 MSSSSAPIIELRGLTKTVGTGAGEltilKGISLEVEAGESVAIVGASGSGKSTLLGLLAGLDRPTSGTVRLagqdlfaLD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 70 GDMRDRRHRRavcpRIAYMPQGLgkNLYPTLSVFENVDFFGRLFGHDKAerERRIADLLQSTGLapfAER----PAGkLS 145
Cdd:COG4181 81 EDARARLRAR----HVGFVFQSF--QLLPTLTALENVMLPLELAGRRDA--RARARALLERVGL---GHRldhyPAQ-LS 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 146 GGMKQKLGLCCALIHDPDLLILDEPTTGVDPLSRNQFWELIGRIRAgREGMSVLVATAYMEEAERFDWLVAMDDGKVLAT 225
Cdd:COG4181 149 GGEQQRVALARAFATEPAILFADEPTGNLDAATGEQIIDLLFELNR-ERGTTLVLVTHDPALAARCDRVLRLRAGRLVED 227
|
....*
gi 15600424 226 GTPQE 230
Cdd:COG4181 228 TAATA 232
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
289-498 |
1.79e-19 |
|
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: 88.44 E-value: 1.79e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 289 AVDHVSFRIERGEIFGFLGSNGCGKSTTMKMLTGLLPASEGTCALFGQPVDASDMAT-RRRVGYMSQAFSLYAElSVRQN 367
Cdd:cd03251 17 VLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDGHDVRDYTLASlRRQIGLVSQDVFLFND-TVAEN 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 368 lVLHARLfhlpaDGIPARVGEMLRRFDLEKVADELPN-----------DLPLGIRQRLSLAVAVIHKPEILILDEPTSGV 436
Cdd:cd03251 96 -IAYGRP-----GATREEVEEAARAANAHEFIMELPEgydtvigergvKLSGGQRQRIAIARALLKDPPILILDEATSAL 169
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15600424 437 DPVARDGFWELMVELSRrdGVTIFISTHFMNEAQRCDRISLMHAGKVLASDTPDELVRQRGL 498
Cdd:cd03251 170 DTESERLVQAALERLMK--NRTTFVIAHRLSTIENADRIVVLEDGKIVERGTHEELLAQGGV 229
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
35-437 |
2.49e-19 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 92.95 E-value: 2.49e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 35 RMVGLIGPDGVGKSSLLALLAGA------------------------------RKMQDGEIRVldgdmrdrrhrrAVCPR 84
Cdd:PRK13409 100 KVTGILGPNGIGKTTAVKILSGElipnlgdyeeepswdevlkrfrgtelqnyfKKLYNGEIKV------------VHKPQ 167
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 85 -IAYMPQGL-GKnlypTLSVFENVDffgrlfghdkaerERRIAD-LLQSTGLAPFAERPAGKLSGGMKQKLGLCCALIHD 161
Cdd:PRK13409 168 yVDLIPKVFkGK----VRELLKKVD-------------ERGKLDeVVERLGLENILDRDISELSGGELQRVAIAAALLRD 230
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 162 PDLLILDEPTTGVDplsrnqfwelIG-RIRAGR------EGMSVLV-----ATaymeeaerFDWLVamdDGKVLATGTPq 229
Cdd:PRK13409 231 ADFYFFDEPTSYLD----------IRqRLNVARlirelaEGKYVLVvehdlAV--------LDYLA---DNVHIAYGEP- 288
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 230 elrertgtqsleSAF-IALLPESKRAG-HHRL-------------------VIPPRPQSEGapRIAIEAEGLTCRFGDF- 287
Cdd:PRK13409 289 ------------GAYgVVSKPKGVRVGiNEYLkgylpeenmrirpepiefeERPPRDESER--ETLVEYPDLTKKLGDFs 354
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 288 VAVDHVSfrIERGEIFGFLGSNGCGKSTTMKMLTGLLPASEGtcalfgqpvdasDMATRRRVGYMSQAFSLYAELSVRQN 367
Cdd:PRK13409 355 LEVEGGE--IYEGEVIGIVGPNGIGKTTFAKLLAGVLKPDEG------------EVDPELKISYKPQYIKPDYDGTVEDL 420
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15600424 368 LvlharlfhlpaDGIPARVG------EMLRRFDLEKVADELPNDLPLGIRQRLSLAVAVIHKPEILILDEPTSGVD 437
Cdd:PRK13409 421 L-----------RSITDDLGssyyksEIIKPLQLERLLDKNVKDLSGGELQRVAIAACLSRDADLYLLDEPSAHLD 485
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
13-243 |
2.99e-19 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 88.91 E-value: 2.99e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 13 GVSLRYGETRAVDDVSLEIPANRMVGLIGPDGVGKSSLLALLAGARKMQDGEIrVLDGDMRD--RRHRRAVCPRIAYMPQ 90
Cdd:PRK13638 6 DLWFRYQDEPVLKGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLRPQKGAV-LWQGKPLDysKRGLLALRQQVATVFQ 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 91 GLGKNLYPTlSVFENVDFFGRLFGHDKAERERRIADLLQSTGLAPFAERPAGKLSGGMKQKLGLCCALIHDPDLLILDEP 170
Cdd:PRK13638 85 DPEQQIFYT-DIDSDIAFSLRNLGVPEAEITRRVDEALTLVDAQHFRHQPIQCLSHGQKKRVAIAGALVLQARYLLLDEP 163
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15600424 171 TTGVDPLSRNQFWELIGRIRAgrEGMSVLVATAYMEEA-ERFDWLVAMDDGKVLATGTPQELRERtgTQSLESA 243
Cdd:PRK13638 164 TAGLDPAGRTQMIAIIRRIVA--QGNHVIISSHDIDLIyEISDAVYVLRQGQILTHGAPGEVFAC--TEAMEQA 233
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
275-484 |
3.07e-19 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 88.53 E-value: 3.07e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 275 IEAEGLTCRFGDFVAVDHVSFRIERGEIFGFLGSNGCGKSTTMKMLTGLL---PASEGTCALFGQPVD-----ASDM-AT 345
Cdd:PRK09984 5 IRVEKLAKTFNQHQALHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGLItgdKSAGSHIELLGRTVQregrlARDIrKS 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 346 RRRVGYMSQAFSLYAELSVRQNLVLHA--------RLFHLPADGIPARVGEMLRRFDLEKVADELPNDLPLGIRQRLSLA 417
Cdd:PRK09984 85 RANTGYIFQQFNLVNRLSVLENVLIGAlgstpfwrTCFSWFTREQKQRALQALTRVGMVHFAHQRVSTLSGGQQQRVAIA 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15600424 418 VAVIHKPEILILDEPTSGVDPVARDGFWELMVELSRRDGVTIFISTHFMNEAQR-CDRISLMHAGKVL 484
Cdd:PRK09984 165 RALMQQAKVILADEPIASLDPESARIVMDTLRDINQNDGITVVVTLHQVDYALRyCERIVALRQGHVF 232
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
290-464 |
3.17e-19 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 87.15 E-value: 3.17e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 290 VDHVSFRIERGEIFGFLGSNGCGKSTTMKMLTGLLPA---SEGTCALFGQPVDASDMAtRRRVGYMSQAFSLYAELSVRQ 366
Cdd:COG4136 17 LAPLSLTVAPGEILTLMGPSGSGKSTLLAAIAGTLSPafsASGEVLLNGRRLTALPAE-QRRIGILFQDDLLFPHLSVGE 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 367 NLvlharLFHLPAdGIP-----ARVGEMLRRFDLEKVADELPNDLPLGIRQRLSLAVAVIHKPEILILDEPTSGVDPVAR 441
Cdd:COG4136 96 NL-----AFALPP-TIGraqrrARVEQALEEAGLAGFADRDPATLSGGQRARVALLRALLAEPRALLLDEPFSKLDAALR 169
|
170 180
....*....|....*....|...
gi 15600424 442 DGFWELMVELSRRDGVTIFISTH 464
Cdd:COG4136 170 AQFREFVFEQIRQRGIPALLVTH 192
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
11-483 |
3.29e-19 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 92.10 E-value: 3.29e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 11 LRGVSLRYGETRAVDDVSLEIPANRMVGLIGPDGVGKSSLLALLAGARKMQDGEIRVLDGDMRDRRHRRAVCPRIAYMPQ 90
Cdd:PRK10982 1 MSNISKSFPGVKALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEIDFKSSKEALENGISMVHQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 91 GLgkNLYPTLSVFENVdFFGR-----LF-GHDKAERE-RRIADLLqSTGLAPfaERPAGKLSGGMKQKLGLCCALIHDPD 163
Cdd:PRK10982 81 EL--NLVLQRSVMDNM-WLGRyptkgMFvDQDKMYRDtKAIFDEL-DIDIDP--RAKVATLSVSQMQMIEIAKAFSYNAK 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 164 LLILDEPTTGVDPLSRNQFWELIGRIRagREGMSVLVATAYMEEAERF-DWLVAMDDGKVLATgtpQELRERTGTQsles 242
Cdd:PRK10982 155 IVIMDEPTSSLTEKEVNHLFTIIRKLK--ERGCGIVYISHKMEEIFQLcDEITILRDGQWIAT---QPLAGLTMDK---- 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 243 aFIALLpeSKRAGHHRLviPPRPQSEGapRIAIEAEGLTCRfgDFVAVDHVSFRIERGEIFGFLGSNGCGKSTTMKMLTG 322
Cdd:PRK10982 226 -IIAMM--VGRSLTQRF--PDKENKPG--EVILEVRNLTSL--RQPSIRDVSFDLHKGEILGIAGLVGAKRTDIVETLFG 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 323 LLPASEGTCALFGQPVDASD----------MAT--RRRVGymsqafsLYAELSVRQNLVLHARLFHLPADGIPARvGEMl 390
Cdd:PRK10982 297 IREKSAGTITLHGKKINNHNaneainhgfaLVTeeRRSTG-------IYAYLDIGFNSLISNIRNYKNKVGLLDN-SRM- 367
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 391 rRFDLEKVADEL----PN------DLPLGIRQRLSLAVAVIHKPEILILDEPTSGVDPVARDGFWELMVELSRRDGVTIF 460
Cdd:PRK10982 368 -KSDTQWVIDSMrvktPGhrtqigSLSGGNQQKVIIGRWLLTQPEILMLDEPTRGIDVGAKFEIYQLIAELAKKDKGIII 446
|
490 500
....*....|....*....|...
gi 15600424 461 ISTHFMNEAQRCDRISLMHAGKV 483
Cdd:PRK10982 447 ISSEMPELLGITDRILVMSNGLV 469
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
275-492 |
3.46e-19 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 88.22 E-value: 3.46e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 275 IEAEGLTCRfGDFVAVDHVSFRIERGEIFGFLGSNGCGKSTTMKMLTGLLPA----SEGTCALFGQPVDASDMATRRRVG 350
Cdd:PRK10418 5 IELRNIALQ-AAQPLVHGVSLTLQRGRVLALVGGSGSGKSLTCAAALGILPAgvrqTAGRVLLDGKPVAPCALRGRKIAT 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 351 YMSQAFSLYAELsvrQNLVLHARLfHLPADGIPARVGEMLRRF------DLEKVADELPNDLPLGIRQRLSLAVAVIHKP 424
Cdd:PRK10418 84 IMQNPRSAFNPL---HTMHTHARE-TCLALGKPADDATLTAALeavgleNAARVLKLYPFEMSGGMLQRMMIALALLCEA 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15600424 425 EILILDEPTSGVDPVARDGFWELMVELSRRDGVTIFISTHFMNEAQRC-DRISLMHAGKVLASDTPDEL 492
Cdd:PRK10418 160 PFIIADEPTTDLDVVAQARILDLLESIVQKRALGMLLVTHDMGVVARLaDDVAVMSHGRIVEQGDVETL 228
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
275-464 |
5.06e-19 |
|
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein encoded by ccmA in bacteria. An exception is, an arabidopsis protein. Quite likely this is encoded by an organelle. Bacterial c-type cytocromes are located on the periplasmic side of the cytoplasmic membrane. Several gene products encoded in a locus designated as 'ccm' are implicated in the transport and assembly of the functional cytochrome C. This cluster includes genes: ccmA;B;C;D;E;F;G and H. The posttranslational pathway includes the transport of heme moiety, the secretion of the apoprotein and the covalent attachment of the heme with the apoprotein. The proteins ccmA and B represent an ABC transporter; ccmC and D participate in heme transfer to ccmE, which function as a periplasmic heme chaperone. The presence of ccmF, G and H is suggested to be obligatory for the final functional assembly of cytochrome c. [Protein fate, Protein and peptide secretion and trafficking, Transport and binding proteins, Other]
Pssm-ID: 273491 [Multi-domain] Cd Length: 198 Bit Score: 86.26 E-value: 5.06e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 275 IEAEGLTCRFGDFVAVDHVSFRIERGEIFGFLGSNGCGKSTTMKMLTGLLPASEGTCALFGQPVDASDMATRRRVGYMSQ 354
Cdd:TIGR01189 1 LAARNLACSRGERMLFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRWNGTPLAEQRDEPHENILYLGH 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 355 AFSLYAELSVRQNLVLHARlFHLPADGIPArvgEMLRRFDLEKVADELPNDLPLGIRQRLSLAVAVIHKPEILILDEPTS 434
Cdd:TIGR01189 81 LPGLKPELSALENLHFWAA-IHGGAQRTIE---DALAAVGLTGFEDLPAAQLSAGQQRRLALARLWLSRRPLWILDEPTT 156
|
170 180 190
....*....|....*....|....*....|
gi 15600424 435 GVDPVARDGFWELMVELSRRDGVTIfISTH 464
Cdd:TIGR01189 157 ALDKAGVALLAGLLRAHLARGGIVL-LTTH 185
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
292-471 |
5.48e-19 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 86.94 E-value: 5.48e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 292 HVSFRIERGEIFGFLGSNGCGKSTTMKMLTGLLPASEGTCALFGQPVDASDMAtRRRVGYMSQAFSLYAELSVRQN--LV 369
Cdd:PRK10771 17 RFDLTVERGERVAILGPSGAGKSTLLNLIAGFLTPASGSLTLNGQDHTTTPPS-RRPVSMLFQENNLFSHLTVAQNigLG 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 370 LHARLfHLPADGiPARVGEMLRRFDLEKVADELPNDLPLGIRQRLSLAVAVIHKPEILILDEPTSGVDPVARDGFWELMV 449
Cdd:PRK10771 96 LNPGL-KLNAAQ-REKLHAIARQMGIEDLLARLPGQLSGGQRQRVALARCLVREQPILLLDEPFSALDPALRQEMLTLVS 173
|
170 180
....*....|....*....|..
gi 15600424 450 ELSRRDGVTIFISTHFMNEAQR 471
Cdd:PRK10771 174 QVCQERQLTLLMVSHSLEDAAR 195
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
28-437 |
5.53e-19 |
|
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: 91.77 E-value: 5.53e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 28 SLEIP-ANRMVGLIGPDGVGKSSLLALLAGA------------------------------RKMQDGEIRVldgdmrdrr 76
Cdd:COG1245 92 GLPVPkKGKVTGILGPNGIGKSTALKILSGElkpnlgdydeepswdevlkrfrgtelqdyfKKLANGEIKV--------- 162
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 77 hrravcpriAYMPQ----------GLGKNLyptlsvFENVDFFGRLfghdkaereRRIADLLqstGLAPFAERPAGKLSG 146
Cdd:COG1245 163 ---------AHKPQyvdlipkvfkGTVREL------LEKVDERGKL---------DELAEKL---GLENILDRDISELSG 215
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 147 GMKQKLGLCCALIHDPDLLILDEPTTGVDplsrnqfwelIG-RIRAGR-------EGMSVLV-----ATaymeeaerFDW 213
Cdd:COG1245 216 GELQRVAIAAALLRDADFYFFDEPSSYLD----------IYqRLNVARlirelaeEGKYVLVvehdlAI--------LDY 277
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 214 LVamdDGKVLATGTPqelrertgtqsleSAF-IALLPESKRAG-HHRL-------------------VIPPRPQSEGAPr 272
Cdd:COG1245 278 LA---DYVHILYGEP-------------GVYgVVSKPKSVRVGiNQYLdgylpeenvrirdepiefeVHAPRREKEEET- 340
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 273 iAIEAEGLTCRFGDF-VAVDhvSFRIERGEIFGFLGSNGCGKSTTMKMLTGLLPASEGtcalfgqpvdasDMATRRRVGY 351
Cdd:COG1245 341 -LVEYPDLTKSYGGFsLEVE--GGEIREGEVLGIVGPNGIGKTTFAKILAGVLKPDEG------------EVDEDLKISY 405
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 352 MSQAFSLYAELSVRQNLvlharlfhlpADGIPARVG------EMLRRFDLEKVADELPNDLPLGIRQRLSLAVAVIHKPE 425
Cdd:COG1245 406 KPQYISPDYDGTVEEFL----------RSANTDDFGssyyktEIIKPLGLEKLLDKNVKDLSGGELQRVAIAACLSRDAD 475
|
490
....*....|..
gi 15600424 426 ILILDEPTSGVD 437
Cdd:COG1245 476 LYLLDEPSAHLD 487
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
22-226 |
9.07e-19 |
|
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: 86.17 E-value: 9.07e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 22 RAVDDVSLEIPANRMVGLIGPDGVGKSSLLALLAG---ARKMQDGEIrVLDGDmrdRRHRRAVCPRIAYMPQGlgKNLYP 98
Cdd:cd03234 21 RILNDVSLHVESGQVMAILGSSGSGKTTLLDAISGrveGGGTTSGQI-LFNGQ---PRKPDQFQKCVAYVRQD--DILLP 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 99 TLSVFENVDFFGRLFGH---DKAERERRIAD-LLQSTGLAPFAERPAGKLSGGMKQKLGLCCALIHDPDLLILDEPTTGV 174
Cdd:cd03234 95 GLTVRETLTYTAILRLPrksSDAIRKKRVEDvLLRDLALTRIGGNLVKGISGGERRRVSIAVQLLWDPKVLILDEPTSGL 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 15600424 175 DPLSRNQFWELIGRIraGREGMSVLVaTAYMEEAE---RFDWLVAMDDGKVLATG 226
Cdd:cd03234 175 DSFTALNLVSTLSQL--ARRNRIVIL-TIHQPRSDlfrLFDRILLLSSGEIVYSG 226
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
2-210 |
9.17e-19 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 87.14 E-value: 9.17e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 2 TAGGSGVASLRGVSLRYGETRAVDDVSLEIPANRMVGLIGPDGVGKSSLLA-------LLAGARKmqDGEIRVLDGDMRD 74
Cdd:PRK14243 4 LNGTETVLRTENLNVYYGSFLAVKNVWLDIPKNQITAFIGPSGCGKSTILRcfnrlndLIPGFRV--EGKVTFHGKNLYA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 75 RR-HRRAVCPRIAYMPQglGKNLYPTlSVFENVDFFGRLFGH-----DKAERERRIA-------DLLQSTGLApfaerpa 141
Cdd:PRK14243 82 PDvDPVEVRRRIGMVFQ--KPNPFPK-SIYDNIAYGARINGYkgdmdELVERSLRQAalwdevkDKLKQSGLS------- 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15600424 142 gkLSGGMKQKLGLCCALIHDPDLLILDEPTTGVDPLSRNQFWELIGRIragREGMSVLVATAYMEEAER 210
Cdd:PRK14243 152 --LSGGQQQRLCIARAIAVQPEVILMDEPCSALDPISTLRIEELMHEL---KEQYTIIIVTHNMQQAAR 215
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
291-498 |
1.17e-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: 86.05 E-value: 1.17e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 291 DHVSFRIERGEIFGFLGSNGCGKSTTMKMLTGLLPASEGTCALFGQpvDASDMA---TRRRVGYMSQAFSLYAeLSVRQN 367
Cdd:cd03249 20 KGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEILLDGV--DIRDLNlrwLRSQIGLVSQEPVLFD-GTIAEN 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 368 LVLharlfhlpadGIPARVGEMLRRFDLEKVADELPNDLPLGI---------------RQRLSLAVAVIHKPEILILDEP 432
Cdd:cd03249 97 IRY----------GKPDATDEEVEEAAKKANIHDFIMSLPDGYdtlvgergsqlsggqKQRIAIARALLRNPKILLLDEA 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15600424 433 TSGVDPVArdgfwELMVE--LSR-RDGVTIFISTHFMNEAQRCDRISLMHAGKVLASDTPDELVRQRGL 498
Cdd:cd03249 167 TSALDAES-----EKLVQeaLDRaMKGRTTIVIAHRLSTIRNADLIAVLQNGQVVEQGTHDELMAQKGV 230
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
26-231 |
1.18e-18 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 90.88 E-value: 1.18e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 26 DVSLEIPANRMVGLIGPDGVGKSSLLALLAGaRKMQDGEI---RVLDGDMRDRRHRRAVCpriAYMPQGlgKNLYPTLSV 102
Cdd:TIGR00955 43 NVSGVAKPGELLAVMGSSGAGKTTLMNALAF-RSPKGVKGsgsVLLNGMPIDAKEMRAIS---AYVQQD--DLFIPTLTV 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 103 FENVDFFGRLFGHD---KAERERRIADLLQSTGLAPFAERPAGK------LSGGMKQKLGLCCALIHDPDLLILDEPTTG 173
Cdd:TIGR00955 117 REHLMFQAHLRMPRrvtKKEKRERVDEVLQALGLRKCANTRIGVpgrvkgLSGGERKRLAFASELLTDPPLLFCDEPTSG 196
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15600424 174 VDPLSRNQFWELIGRIraGREGMSVLV------ATAYmeeaERFDWLVAMDDGKVLATGTPQEL 231
Cdd:TIGR00955 197 LDSFMAYSVVQVLKGL--AQKGKTIICtihqpsSELF----ELFDKIILMAEGRVAYLGSPDQA 254
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
278-503 |
1.58e-18 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 86.27 E-value: 1.58e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 278 EGLTCRFGDFVAVDHVSFRIERGEIFGFLGSNGCGKSTTMKMLTGLLPASEGTCALFGQPVDASDMATRrrvgYMSQAFS 357
Cdd:PRK11247 16 NAVSKRYGERTVLNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAGELLAGTAPLAEAREDTR----LMFQDAR 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 358 LYAELSVRQNLVLHARLFHLPAdgipARvgEMLRRFDLEKVADELPNDLPLGIRQRLSLAVAVIHKPEILILDEPTSGVD 437
Cdd:PRK11247 92 LLPWKKVIDNVGLGLKGQWRDA----AL--QALAAVGLADRANEWPAALSGGQKQRVALARALIHRPGLLLLDEPLGALD 165
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15600424 438 PVARDGFWELMVELSRRDGVTIFISTHFMNEA-QRCDRISLMHAGKV---LASDTPDElvRQRG---LPTLEA 503
Cdd:PRK11247 166 ALTRIEMQDLIESLWQQHGFTVLLVTHDVSEAvAMADRVLLIEEGKIgldLTVDLPRP--RRRGsarLAELEA 236
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
18-231 |
1.85e-18 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 85.72 E-value: 1.85e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 18 YGETRAVDDVSLEIPANRMVGLIGPDGVGKSSLLALLAGARKMQDGEIRVLDGDMR----DRRHRRAvcprIAYMPQglG 93
Cdd:PRK10895 13 YKGRRVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEDISllplHARARRG----IGYLPQ--E 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 94 KNLYPTLSVFENVDFFGRLFGHDKAE-RERRIADLLQSTGLAPFAERPAGKLSGGMKQKLGLCCALIHDPDLLILDEPTT 172
Cdd:PRK10895 87 ASIFRRLSVYDNLMAVLQIRDDLSAEqREDRANELMEEFHIEHLRDSMGQSLSGGERRRVEIARALAANPKFILLDEPFA 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15600424 173 GVDPLSRNQFWELIGRIRagREGMSVLVATAYMEEA----ERfDWLVAmdDGKVLATGTPQEL 231
Cdd:PRK10895 167 GVDPISVIDIKRIIEHLR--DSGLGVLITDHNVRETlavcER-AYIVS--QGHLIAHGTPTEI 224
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
17-231 |
1.94e-18 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 86.18 E-value: 1.94e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 17 RYGETRAVDDVSLEIPANRMVGLIGPDGVGKSSLLALLAGARKMQDGEIRVLDGDMR------------DRRHRRAVCPR 84
Cdd:PRK10619 14 RYGEHEVLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNGQTINlvrdkdgqlkvaDKNQLRLLRTR 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 85 IAYMPQGLgkNLYPTLSVFENV-DFFGRLFGHDKAERERRIADLLQSTGLApfaERPAGK----LSGGMKQKLGLCCALI 159
Cdd:PRK10619 94 LTMVFQHF--NLWSHMTVLENVmEAPIQVLGLSKQEARERAVKYLAKVGID---ERAQGKypvhLSGGQQQRVSIARALA 168
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15600424 160 HDPDLLILDEPTTGVDPlsrnqfwELIGRI-----RAGREGMSVLVATAYMEEAERF-DWLVAMDDGKVLATGTPQEL 231
Cdd:PRK10619 169 MEPEVLLFDEPTSALDP-------ELVGEVlrimqQLAEEGKTMVVVTHEMGFARHVsSHVIFLHQGKIEEEGAPEQL 239
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
24-220 |
2.28e-18 |
|
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits of nitrate transport in bacteria and archaea. This protein belongs to the ATP-binding cassette (ABC) superfamily. It is thought that the two subunits encoded by ntrC and ntrD form the binding surface for interaction with ATP. This model is restricted in identifying ATP binding subunit associated with the nitrate transport. Nitrate assimilation is aided by other proteins derived from the operon which among others include products of ntrA - a regulatory protein; ntrB - a hydropbobic transmembrane permease and narB - a reductase. [Transport and binding proteins, Anions, Transport and binding proteins, Other]
Pssm-ID: 130252 [Multi-domain] Cd Length: 230 Bit Score: 85.21 E-value: 2.28e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 24 VDDVSLEIPANRMVGLIGPDGVGKSSLLALLAGARKMQDGEIRvLDGDMRDRrhrravcPRIAYMPQGLGKNLYPTLSVF 103
Cdd:TIGR01184 1 LKGVNLTIQQGEFISLIGHSGCGKSTLLNLISGLAQPTSGGVI-LEGKQITE-------PGPDRMVVFQNYSLLPWLTVR 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 104 ENVDFFGRLFGHDKAERERR--IADLLQSTGLAPFAERPAGKLSGGMKQKLGLCCALIHDPDLLILDEPTTGVDPLSRNQ 181
Cdd:TIGR01184 73 ENIALAVDRVLPDLSKSERRaiVEEHIALVGLTEAADKRPGQLSGGMKQRVAIARALSIRPKVLLLDEPFGALDALTRGN 152
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 15600424 182 FWELIGRIrAGREGMSVLVATAYMEEAERF-DWLVAMDDG 220
Cdd:TIGR01184 153 LQEELMQI-WEEHRVTVLMVTHDVDEALLLsDRVVMLTNG 191
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
11-231 |
2.46e-18 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 86.60 E-value: 2.46e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 11 LRGVSLRYG-----ETRAVDDVSLEIPANRMVGLIGPDGVGKSSLLALLAGARKMQDGEIRVLD----GDMRDRRHRRAV 81
Cdd:PRK13645 9 LDNVSYTYAkktpfEFKALNNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGLIISETGQTIVGDyaipANLKKIKEVKRL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 82 CPRIAYMPQglgknlYPTLSVFENV---DF-FGRL-FGHDKAERERRIADLLQSTGLA-PFAERPAGKLSGGMKQKLGLC 155
Cdd:PRK13645 89 RKEIGLVFQ------FPEYQLFQETiekDIaFGPVnLGENKQEAYKKVPELLKLVQLPeDYVKRSPFELSGGQKRRVALA 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15600424 156 CALIHDPDLLILDEPTTGVDPLSRNQFWELIGRIRAgREGMSVLVATAYMEEAERF-DWLVAMDDGKVLATGTPQEL 231
Cdd:PRK13645 163 GIIAMDGNTLVLDEPTGGLDPKGEEDFINLFERLNK-EYKKRIIMVTHNMDQVLRIaDEVIVMHEGKVISIGSPFEI 238
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
288-483 |
3.38e-18 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 85.52 E-value: 3.38e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 288 VAVDHVSFRIERGEIFGFLGSNGCGKSTTMKMLTGLLPASEGTCALFGQpvDASDMATRRRVGYMSQAF-------SlyA 360
Cdd:COG1101 20 RALDGLNLTIEEGDFVTVIGSNGAGKSTLLNAIAGSLPPDSGSILIDGK--DVTKLPEYKRAKYIGRVFqdpmmgtA--P 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 361 ELSVRQNLVL-----HARLFHLpadGIP----ARVGEMLRRFDLekvadELPNDL--PLGI-----RQRLSLAVAVIHKP 424
Cdd:COG1101 96 SMTIEENLALayrrgKRRGLRR---GLTkkrrELFRELLATLGL-----GLENRLdtKVGLlsggqRQALSLLMATLTKP 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 425 EILILDEPTSGVDPVARDGFWELMVELSRRDGVTIFISTHFMNEAQRC-DRISLMHAGKV 483
Cdd:COG1101 168 KLLLLDEHTAALDPKTAALVLELTEKIVEENNLTTLMVTHNMEQALDYgNRLIMMHEGRI 227
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
10-231 |
3.63e-18 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 85.57 E-value: 3.63e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 10 SLRGVSLRYG-----ETRAVDDVSLEIPANRMVGLIGPDGVGKSSLLALLAGARKMQDGEIRVLDGDMRDRRHRRAVCP- 83
Cdd:PRK13649 4 NLQNVSYTYQagtpfEGRALFDVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDDTLITSTSKNKDIKQi 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 84 --RIAYMPQGLGKNLYPTlSVFENVDFFGRLFGHDKAERERRIADLLQSTGLAP-FAERPAGKLSGGMKQKLGLCCALIH 160
Cdd:PRK13649 84 rkKVGLVFQFPESQLFEE-TVLKDVAFGPQNFGVSQEEAEALAREKLALVGISEsLFEKNPFELSGGQMRRVAIAGILAM 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15600424 161 DPDLLILDEPTTGVDPLSRNQFWELIGRIRagREGMSVLVATAYMEE-AERFDWLVAMDDGKVLATGTPQEL 231
Cdd:PRK13649 163 EPKILVLDEPTAGLDPKGRKELMTLFKKLH--QSGMTIVLVTHLMDDvANYADFVYVLEKGKLVLSGKPKDI 232
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
286-492 |
4.05e-18 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 85.83 E-value: 4.05e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 286 DFVAVDHVSFRIERGEIFGFLGSNGCGKSTTMKMLTGLLPASEGTCAL--FGQPVDASDMAT----RRRVGYMSQ--AFS 357
Cdd:PRK13645 23 EFKALNNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGLIISETGQTIVgdYAIPANLKKIKEvkrlRKEIGLVFQfpEYQ 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 358 LYAElSVRQNLVLHArlFHLPADGIPA--RVGEMLRRFDL-EKVADELPNDLPLGIRQRLSLAVAVIHKPEILILDEPTS 434
Cdd:PRK13645 103 LFQE-TIEKDIAFGP--VNLGENKQEAykKVPELLKLVQLpEDYVKRSPFELSGGQKRRVALAGIIAMDGNTLVLDEPTG 179
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 15600424 435 GVDPVARDGFWELMVELSRRDGVTIFISTHFMNEAQR-CDRISLMHAGKVLASDTPDEL 492
Cdd:PRK13645 180 GLDPKGEEDFINLFERLNKEYKKRIIMVTHNMDQVLRiADEVIVMHEGKVISIGSPFEI 238
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
10-236 |
4.05e-18 |
|
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a central component of the secretion machinery that translocates the toxin, hemolysin A, in a Sec-independent fashion across both membranes of E. coli. The hemolysin A (HlyA) transport machinery is composed of the ATP-binding cassette (ABC) transporter HlyB located in the inner membrane, hemolysin D (HlyD), also anchored in the inner membrane, and TolC, which resides in the outer membrane. HlyD apparently forms a continuous channel that bridges the entire periplasm, interacting with TolC and HlyB. This arrangement prevents the appearance of periplasmic intermediates of HlyA during substrate transport. Little is known about the molecular details of HlyA transport, but it is evident that ATP-hydrolysis by the ABC-transporter HlyB is a necessary source of energy.
Pssm-ID: 213219 [Multi-domain] Cd Length: 237 Bit Score: 84.46 E-value: 4.05e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 10 SLRGVSLRYG--ETRAVDDVSLEIPANRMVGLIGPDGVGKSSLLALLAGARKMQDGEIrVLDG-DMR--DRRHRRAvcpR 84
Cdd:cd03252 2 TFEHVRFRYKpdGPVILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRV-LVDGhDLAlaDPAWLRR---Q 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 85 IAYMPQglgKNLYPTLSVFENVDFfgrlfgHDKAERERRIADLLQSTGLAPF------------AERPAGkLSGGMKQKL 152
Cdd:cd03252 78 VGVVLQ---ENVLFNRSIRDNIAL------ADPGMSMERVIEAAKLAGAHDFiselpegydtivGEQGAG-LSGGQRQRI 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 153 GLCCALIHDPDLLILDEPTTGVDPLSRNQFWELIGRIRAGRegmSVLVATAYMEEAERFDWLVAMDDGKVLATGTPQELR 232
Cdd:cd03252 148 AIARALIHNPRILIFDEATSALDYESEHAIMRNMHDICAGR---TVIIIAHRLSTVKNADRIIVMEKGRIVEQGSHDELL 224
|
....
gi 15600424 233 ERTG 236
Cdd:cd03252 225 AENG 228
|
|
| nickel_nikE |
TIGR02769 |
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a ... |
24-266 |
4.08e-18 |
|
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: 85.24 E-value: 4.08e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 24 VDDVSLEIPANRMVGLIGPDGVGKSSLLALLAGARKMQDGEIRVLDGDMR--DRRHRRAVCPRIAYMPQGLGKNLYPTLS 101
Cdd:TIGR02769 27 LTNVSLSIEEGETVGLLGRSGCGKSTLARLLLGLEKPAQGTVSFRGQDLYqlDRKQRRAFRRDVQLVFQDSPSAVNPRMT 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 102 VFENV-DFFGRLFGHDKAERERRIADLLQSTGLAP-FAERPAGKLSGGMKQKLGLCCALIHDPDLLILDEPTTGVDPLSR 179
Cdd:TIGR02769 107 VRQIIgEPLRHLTSLDESEQKARIAELLDMVGLRSeDADKLPRQLSGGQLQRINIARALAVKPKLIVLDEAVSNLDMVLQ 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 180 NQFWELIGRIRAgREGMSVLVATAYMEEAERF-DWLVAMDDGKVLatgtpqELRERTGTQSLESAFIALLPESkraghhr 258
Cdd:TIGR02769 187 AVILELLRKLQQ-AFGTAYLFITHDLRLVQSFcQRVAVMDKGQIV------EECDVAQLLSFKHPAGRNLQSA------- 252
|
....*...
gi 15600424 259 lVIPPRPQ 266
Cdd:TIGR02769 253 -VLPEHPV 259
|
|
| thiQ |
TIGR01277 |
thiamine ABC transporter, ATP-binding protein; This model describes the energy-transducing ... |
294-483 |
4.25e-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: 83.76 E-value: 4.25e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 294 SFRIERGEIFGFLGSNGCGKSTTMKMLTGLLPASEGTCALFGQPVDASdMATRRRVGYMSQAFSLYAELSVRQNLVLHAR 373
Cdd:TIGR01277 18 DLNVADGEIVAIMGPSGAGKSTLLNLIAGFIEPASGSIKVNDQSHTGL-APYQRPVSMLFQENNLFAHLTVRQNIGLGLH 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 374 lfhlPADGIPA----RVGEMLRRFDLEKVADELPNDLPLGIRQRLSLAVAVIHKPEILILDEPTSGVDPVARDGFWELMV 449
Cdd:TIGR01277 97 ----PGLKLNAeqqeKVVDAAQQVGIADYLDRLPEQLSGGQRQRVALARCLVRPNPILLLDEPFSALDPLLREEMLALVK 172
|
170 180 190
....*....|....*....|....*....|....*
gi 15600424 450 ELSRRDGVTIFISTHFMNEAQR-CDRISLMHAGKV 483
Cdd:TIGR01277 173 QLCSERQRTLLMVTHHLSDARAiASQIAVVSQGKI 207
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
289-492 |
4.60e-18 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 86.30 E-value: 4.60e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 289 AVDHVSFRIERGEIFGFLGSNGCGKSTTMKMLTGLLPASEGTCALFGQpvDASDM------ATRRRVGYMSQ--AFSLYA 360
Cdd:PRK15079 36 AVDGVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGEVAWLGK--DLLGMkddewrAVRSDIQMIFQdpLASLNP 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 361 ELSVRQNLVLHARLFH--LPADGIPARVGEMLRRFDL-EKVADELPNDLPLGIRQRLSLAVAVIHKPEILILDEPTSGVD 437
Cdd:PRK15079 114 RMTIGEIIAEPLRTYHpkLSRQEVKDRVKAMMLKVGLlPNLINRYPHEFSGGQCQRIGIARALILEPKLIICDEPVSALD 193
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 15600424 438 PVARDGFWELMVELSRRDGVT-IFISTHFMNEAQRCDRISLMHAGKVLASDTPDEL 492
Cdd:PRK15079 194 VSIQAQVVNLLQQLQREMGLSlIFIAHDLAVVKHISDRVLVMYLGHAVELGTYDEV 249
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
11-236 |
4.69e-18 |
|
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC transporter that is expressed in the mitochondria. Although the specific function of ATM1 is unknown, its disruption results in the accumulation of excess mitochondrial iron, loss of mitochondrial cytochromes, oxidative damage to mitochondrial DNA, and decreased levels of cytosolic heme proteins. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213220 [Multi-domain] Cd Length: 236 Bit Score: 84.20 E-value: 4.69e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 11 LRGVSLRYGETRAV-DDVSLEIPANRMVGLIGPDGVGKSSLLALLAGARKMQDGEIRVLDGDMRD------RRHrravcp 83
Cdd:cd03253 3 FENVTFAYDPGRPVlKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDGQDIREvtldslRRA------ 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 84 rIAYMPQGLgkNLYPTlSVFENVDFfGRLFGHD----KAERERRIADLLQSTglaPFA------ERpaG-KLSGGMKQKL 152
Cdd:cd03253 77 -IGVVPQDT--VLFND-TIGYNIRY-GRPDATDeeviEAAKAAQIHDKIMRF---PDGydtivgER--GlKLSGGEKQRV 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 153 GLCCALIHDPDLLILDEPTTGVDPLSRNQFWELIGRIRAGRegmSVLVATAYMEEAERFDWLVAMDDGKVLATGTPQELR 232
Cdd:cd03253 147 AIARAILKNPPILLLDEATSALDTHTEREIQAALRDVSKGR---TTIVIAHRLSTIVNADKIIVLKDGRIVERGTHEELL 223
|
....
gi 15600424 233 ERTG 236
Cdd:cd03253 224 AKGG 227
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
284-492 |
5.51e-18 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 87.01 E-value: 5.51e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 284 FGDFVAVDHVSFRIERGEIFGFLGSNGCGKSTTMKMLTGLLPASEGTCALFGQPVDASDMAtRRRVGYMSQAFSLYAELS 363
Cdd:PRK11000 13 YGDVVISKDINLDIHEGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLFIGEKRMNDVPPA-ERGVGMVFQSYALYPHLS 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 364 VRQNLVLHARLFHLPADGIPARVGEMLRRFDLEKVADELPNDLPLGIRQRLSLAVAVIHKPEILILDEPTSGVDPVARdg 443
Cdd:PRK11000 92 VAENMSFGLKLAGAKKEEINQRVNQVAEVLQLAHLLDRKPKALSGGQRQRVAIGRTLVAEPSVFLLDEPLSNLDAALR-- 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 15600424 444 fWELMVELSR---RDGVTIFISTHFMNEAQR-CDRISLMHAGKVLASDTPDEL 492
Cdd:PRK11000 170 -VQMRIEISRlhkRLGRTMIYVTHDQVEAMTlADKIVVLDAGRVAQVGKPLEL 221
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
279-498 |
6.44e-18 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 84.67 E-value: 6.44e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 279 GLTCRFGDFVAVDHVSFRIERGEIFGFLGSNGCGKSTTMKMLTGLLPASEGTCALFGQPVDASD---MATRRRVGYMSQA 355
Cdd:PRK13638 6 DLWFRYQDEPVLKGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLRPQKGAVLWQGKPLDYSKrglLALRQQVATVFQD 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 356 FS---LYAELSvrQNLVLHARLFHLPADGIPARVGEMLRRFDLEKVADELPNDLPLGIRQRLSLAVAVIHKPEILILDEP 432
Cdd:PRK13638 86 PEqqiFYTDID--SDIAFSLRNLGVPEAEITRRVDEALTLVDAQHFRHQPIQCLSHGQKKRVAIAGALVLQARYLLLDEP 163
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15600424 433 TSGVDPVARdgfwELMVELSRR---DGVTIFISTHFMNEA-QRCDRISLMHAGKVLASDTP------DELVRQRGL 498
Cdd:PRK13638 164 TAGLDPAGR----TQMIAIIRRivaQGNHVIISSHDIDLIyEISDAVYVLRQGQILTHGAPgevfacTEAMEQAGL 235
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
20-231 |
7.77e-18 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 84.88 E-value: 7.77e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 20 ETRAVDDVSLEIPANRMVGLIGPDGVGKSSLLALLAGARKMQDGEIRVLD-------GDMRDRRHRRAVCPRIAYMPQGL 92
Cdd:PRK13641 19 EKKGLDNISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITIAGyhitpetGNKNLKKLRKKVSLVFQFPEAQL 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 93 GKNlyptlSVFENVDFFGRLFGHDKAERERRIADLLQSTGLAP-FAERPAGKLSGGMKQKLGLCCALIHDPDLLILDEPT 171
Cdd:PRK13641 99 FEN-----TVLKDVEFGPKNFGFSEDEAKEKALKWLKKVGLSEdLISKSPFELSGGQMRRVAIAGVMAYEPEILCLDEPA 173
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15600424 172 TGVDPLSRNQFWELIGRIRagREGMSVLVATAYMEE-AERFDWLVAMDDGKVLATGTPQEL 231
Cdd:PRK13641 174 AGLDPEGRKEMMQLFKDYQ--KAGHTVILVTHNMDDvAEYADDVLVLEHGKLIKHASPKEI 232
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
275-482 |
9.80e-18 |
|
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: 80.57 E-value: 9.80e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 275 IEAEGLTCRFGDFVAVDHVSFRIERGEIFGFLGSNGCGKSTTMKMLTGLLPASEGTCALfGQPVdasdmatrrRVGYMSQ 354
Cdd:cd03221 1 IELENLSKTYGGKLLLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIVTW-GSTV---------KIGYFEQ 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 355 afslyaeLSvrqnlvlharlfhlpadGiparvGEmlrrfdlekvadelpndlplgiRQRLSLAVAVIHKPEILILDEPTS 434
Cdd:cd03221 71 -------LS-----------------G-----GE----------------------KMRLALAKLLLENPNLLLLDEPTN 99
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 15600424 435 GVDPVARDgfWeLMVELSRRDGVTIFIS--THFMNEAqrCDRISLMHAGK 482
Cdd:cd03221 100 HLDLESIE--A-LEEALKEYPGTVILVShdRYFLDQV--ATKIIELEDGK 144
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
6-190 |
1.01e-17 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 83.62 E-value: 1.01e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 6 SGVASLRGVSLRYGETRAVDDVSLEIPANRMVGLIGPDGVGKSSLLALLAGARKMQDGEIRvldgdmrdrrhrRAVCPRI 85
Cdd:PRK09544 2 TSLVSLENVSVSFGQRRVLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIK------------RNGKLRI 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 86 AYMPQGLgkNLYPTLSVfeNVDFFGRLfghDKAERERRIADLLQSTGLAPFAERPAGKLSGGMKQKLGLCCALIHDPDLL 165
Cdd:PRK09544 70 GYVPQKL--YLDTTLPL--TVNRFLRL---RPGTKKEDILPALKRVQAGHLIDAPMQKLSGGETQRVLLARALLNRPQLL 142
|
170 180
....*....|....*....|....*
gi 15600424 166 ILDEPTTGVDPLSRNQFWELIGRIR 190
Cdd:PRK09544 143 VLDEPTQGVDVNGQVALYDLIDQLR 167
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
293-482 |
1.09e-17 |
|
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This subfamily is also known as MRP (multidrug resistance-associated protein). Some of the MRP members have five additional transmembrane segments in their N-terminus, but the function of these additional membrane-spanning domains is not clear. The MRP was found in the multidrug-resisting lung cancer cell in which p-glycoprotein was not overexpressed. MRP exports glutathione by drug stimulation, as well as, certain substrates in conjugated forms with anions, such as glutathione, glucuronate, and sulfate.
Pssm-ID: 213217 [Multi-domain] Cd Length: 204 Bit Score: 82.52 E-value: 1.09e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 293 VSFRIERGEIFGFLGSNGCGKSTTMKMLTGLLPASEGTCALFGqpvdasdmatrrRVGYMSQ-AFSLYAelSVRQNLvlh 371
Cdd:cd03250 24 INLEVPKGELVAIVGPVGSGKSSLLSALLGELEKLSGSVSVPG------------SIAYVSQePWIQNG--TIRENI--- 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 372 arLFHLPADgiPARVGEMLRRFDLEKVADELPN-DLPL----GI------RQRLSLAVAVIHKPEILILDEPTSGVDP-V 439
Cdd:cd03250 87 --LFGKPFD--EERYEKVIKACALEPDLEILPDgDLTEigekGInlsggqKQRISLARAVYSDADIYLLDDPLSAVDAhV 162
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 15600424 440 ARDGFWELMVELsRRDGVTIFISTHFMNEAQRCDRISLMHAGK 482
Cdd:cd03250 163 GRHIFENCILGL-LLNNKTRILVTHQLQLLPHADQIVVLDNGR 204
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
1-231 |
1.51e-17 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 83.56 E-value: 1.51e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 1 MTAGGSG--VASLRGVSLRYGETRAVDDVSLEIPANRMVGLIGPDGVGKSSLLALLAGARKMQDGEIRVlDGDM----RD 74
Cdd:PRK14246 1 MEAGKSAedVFNISRLYLYINDKAILKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLIEIYDSKIKV-DGKVlyfgKD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 75 RRHRRAVCPRIAYMPQGLGKNLYPTLSVFENVDFFGRLFG-HDKAERERRIADLLQSTGL-APFAER---PAGKLSGGMK 149
Cdd:PRK14246 80 IFQIDAIKLRKEVGMVFQQPNPFPHLSIYDNIAYPLKSHGiKEKREIKKIVEECLRKVGLwKEVYDRlnsPASQLSGGQQ 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 150 QKLGLCCALIHDPDLLILDEPTTGVDPLSRNQFWELIGRIRagREGMSVLVATAYMEEAERFDWLVAMDDGKVLATGTPQ 229
Cdd:PRK14246 160 QRLTIARALALKPKVLLMDEPTSMIDIVNSQAIEKLITELK--NEIAIVIVSHNPQQVARVADYVAFLYNGELVEWGSSN 237
|
..
gi 15600424 230 EL 231
Cdd:PRK14246 238 EI 239
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
24-223 |
1.54e-17 |
|
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: 81.83 E-value: 1.54e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 24 VDDVSLEIPANRMVGLIGPDGVGKSSLLALLAGARKMQ--DGEIRVlDGDMRDRRHRRAvcpRIAYMPQGLgkNLYPTLS 101
Cdd:cd03213 25 LKNVSGKAKPGELTAIMGPSGAGKSTLLNALAGRRTGLgvSGEVLI-NGRPLDKRSFRK---IIGYVPQDD--ILHPTLT 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 102 VFENVDFfgrlfghdkaererriADLLQStglapfaerpagkLSGGMKQKLGLCCALIHDPDLLILDEPTTGVDPLSRNQ 181
Cdd:cd03213 99 VRETLMF----------------AAKLRG-------------LSGGERKRVSIALELVSNPSLLFLDEPTSGLDSSSALQ 149
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 15600424 182 FWELIGRIR-AGREGMSVLVATAYmEEAERFDWLVAMDDGKVL 223
Cdd:cd03213 150 VMSLLRRLAdTGRTIICSIHQPSS-EIFELFDKLLLLSQGRVI 191
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
289-484 |
1.64e-17 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 83.69 E-value: 1.64e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 289 AVDHVSFRIERGEIFGFLGSNGCGKSTTMKMLTGLLPASEGTCALFGQPVDASDMATRR---RVGYMSQAFSLYAELSVR 365
Cdd:PRK15112 28 AVKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDHPLHFGDYSYRSqriRMIFQDPSTSLNPRQRIS 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 366 QNLVLHARL-FHLPADGIPARVGEMLRRFDL-EKVADELPNDLPLGIRQRLSLAVAVIHKPEILILDEPTSGVDPVARDG 443
Cdd:PRK15112 108 QILDFPLRLnTDLEPEQREKQIIETLRQVGLlPDHASYYPHMLAPGQKQRLGLARALILRPKVIIADEALASLDMSMRSQ 187
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 15600424 444 FWELMVELSRRDGVT-IFISTHFMNEAQRCDRISLMHAGKVL 484
Cdd:PRK15112 188 LINLMLELQEKQGISyIYVTQHLGMMKHISDQVLVMHQGEVV 229
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
5-235 |
1.65e-17 |
|
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: 86.78 E-value: 1.65e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 5 GSGVASLRGVSLRY-----GETRAVDDVSLEIPANRMVGLIGPDGVGKSSLLALLAGARKMQDGEIRVLDG----DMRDR 75
Cdd:TIGR03269 276 GEPIIKVRNVSKRYisvdrGVVKAVDNVSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGEVNVRVGdewvDMTKP 355
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 76 R--HRRAVCPRIAYMPQGLGknLYPTLSVFENV-DFFGRLFGHDKAERERRIAdlLQSTGlapFAERPA--------GKL 144
Cdd:TIGR03269 356 GpdGRGRAKRYIGILHQEYD--LYPHRTVLDNLtEAIGLELPDELARMKAVIT--LKMVG---FDEEKAeeildkypDEL 428
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 145 SGGMKQKLGLCCALIHDPDLLILDEPTTGVDPLSRNQFWELIGRIRAGREGMSVLVATAYMEEAERFDWLVAMDDGKVLA 224
Cdd:TIGR03269 429 SEGERHRVALAQVLIKEPRIVILDEPTGTMDPITKVDVTHSILKAREEMEQTFIIVSHDMDFVLDVCDRAALMRDGKIVK 508
|
250
....*....|..
gi 15600424 225 TGTPQE-LRERT 235
Cdd:TIGR03269 509 IGDPEEiVEELT 520
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
17-222 |
1.99e-17 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 82.56 E-value: 1.99e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 17 RYGE----TRAVDDVSLEIPANRMVGLIGPDGVGKSSLLALLAGARKMQDGEIrVLDGDMRDRRHRRAvcpRIAYMPQGL 92
Cdd:PRK11629 14 RYQEgsvqTDVLHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDV-IFNGQPMSKLSSAA---KAELRNQKL 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 93 G-----KNLYPTLSVFENVDFFGRLFGHDKAERERRIADLLQSTGLAPFAERPAGKLSGGMKQKLGLCCALIHDPDLLIL 167
Cdd:PRK11629 90 GfiyqfHHLLPDFTALENVAMPLLIGKKKPAEINSRALEMLAAVGLEHRANHRPSELSGGERQRVAIARALVNNPRLVLA 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 15600424 168 DEPTTGVDPLSRNQFWELIGRIRAgREGMSVLVATAYMEEAERFDWLVAMDDGKV 222
Cdd:PRK11629 170 DEPTGNLDARNADSIFQLLGELNR-LQGTAFLVVTHDLQLAKRMSRQLEMRDGRL 223
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
283-502 |
2.30e-17 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 82.71 E-value: 2.30e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 283 RFGDFVAVDHVSFRIERGEIFGFLGSNGCGKSTTMKMLTGLLPASEGTCALFGQPV-------------DASDMAT-RRR 348
Cdd:PRK10619 14 RYGEHEVLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNGQTInlvrdkdgqlkvaDKNQLRLlRTR 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 349 VGYMSQAFSLYAELSVRQNlVLHA--RLFHLPADGIPARVGEMLRRFDL-EKVADELPNDLPLGIRQRLSLAVAVIHKPE 425
Cdd:PRK10619 94 LTMVFQHFNLWSHMTVLEN-VMEApiQVLGLSKQEARERAVKYLAKVGIdERAQGKYPVHLSGGQQQRVSIARALAMEPE 172
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15600424 426 ILILDEPTSGVDPVARDGFWELMVELSrRDGVTIFISTHFMNEAQRC-DRISLMHAGKVLASDTPDELVRQRGLPTLE 502
Cdd:PRK10619 173 VLLFDEPTSALDPELVGEVLRIMQQLA-EEGKTMVVVTHEMGFARHVsSHVIFLHQGKIEEEGAPEQLFGNPQSPRLQ 249
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
289-495 |
2.58e-17 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 83.63 E-value: 2.58e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 289 AVDHVSFRIERGEIFGFLGSNGCGKSTTMKMLTGLLPASEGTCALFGQPVDASDMA-----TRRRVGYMSQafslYAELS 363
Cdd:PRK13643 21 ALFDIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVTVGDIVVSSTSKQkeikpVRKKVGVVFQ----FPESQ 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 364 VRQNLVLHARLFHLPADGIPARVGEMLRRFDLEKVA------DELPNDLPLGIRQRLSLAVAVIHKPEILILDEPTSGVD 437
Cdd:PRK13643 97 LFEETVLKDVAFGPQNFGIPKEKAEKIAAEKLEMVGladefwEKSPFELSGGQMRRVAIAGILAMEPEVLVLDEPTAGLD 176
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 15600424 438 PVARDGFWELMvELSRRDGVTIFISTHFMNE-AQRCDRISLMHAGKVLASDTPDELVRQ 495
Cdd:PRK13643 177 PKARIEMMQLF-ESIHQSGQTVVLVTHLMDDvADYADYVYLLEKGHIISCGTPSDVFQE 234
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
265-492 |
2.75e-17 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 85.87 E-value: 2.75e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 265 PQSEGAPRIAIEAEGLTCRFGDFVAVDHVSFRIERGEIFGFLGSNGCGKSTTMKMLTGLLPASEGTCALFGQPVDASDMA 344
Cdd:PRK15439 2 QTSDTTAPPLLCARSISKQYSGVEVLKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIGGNPCARLTPA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 345 TRRRVG-YM-SQAFSLYAELSVRQNLvlharLFHLPADGIP-ARVGEMLRRFDLEKVADELPNDLPLGIRQRLSLAVAVI 421
Cdd:PRK15439 82 KAHQLGiYLvPQEPLLFPNLSVKENI-----LFGLPKRQASmQKMKQLLAALGCQLDLDSSAGSLEVADRQIVEILRGLM 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15600424 422 HKPEILILDEPTSGVDPVARDGFWELMVELsRRDGVTIFISTHFMNEA-QRCDRISLMHAGKVLASDTPDEL 492
Cdd:PRK15439 157 RDSRILILDEPTASLTPAETERLFSRIREL-LAQGVGIVFISHKLPEIrQLADRISVMRDGTIALSGKTADL 227
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
27-199 |
2.75e-17 |
|
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the bacterial CcmAB transporter. The CCM family is involved in bacterial cytochrome c biogenesis. Cytochrome c maturation in E. coli requires the ccm operon, which encodes eight membrane proteins (CcmABCDEFGH). CcmE is a periplasmic heme chaperon that binds heme covalently and transfers it onto apocytochrome c in the presence of CcmF, CcmG, and CcmH. The CcmAB proteins represent an ABC transporter and the CcmCD proteins participate in heme transfer to CcmE.
Pssm-ID: 213198 [Multi-domain] Cd Length: 201 Bit Score: 81.39 E-value: 2.75e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 27 VSLEIPANRMVGLIGPDGVGKSSLLALLAGARKMQDGEIRV---LDGDMRDRRHRRavCPRIAYMPqglgkNLYPTLSVF 103
Cdd:cd03231 19 LSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLnggPLDFQRDSIARG--LLYLGHAP-----GIKTTLSVL 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 104 ENVDFFGRLFGHDKAErerriaDLLQSTGLAPFAERPAGKLSGGMKQKLGLCCALIHDPDLLILDEPTTGVDPLSRNQFW 183
Cdd:cd03231 92 ENLRFWHADHSDEQVE------EALARVGLNGFEDRPVAQLSAGQQRRVALARLLLSGRPLWILDEPTTALDKAGVARFA 165
|
170
....*....|....*.
gi 15600424 184 ELIgRIRAGREGMSVL 199
Cdd:cd03231 166 EAM-AGHCARGGMVVL 180
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
20-222 |
3.15e-17 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 82.44 E-value: 3.15e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 20 ETRAVDDVSLEIPANRMVGLIGPDGVGKSSLLALLAGARKMQDGEIRVLDGDM-RDRRHRRAvcPRIAYMPQGLGKNLYP 98
Cdd:COG1101 18 EKRALDGLNLTIEEGDFVTVIGSNGAGKSTLLNAIAGSLPPDSGSILIDGKDVtKLPEYKRA--KYIGRVFQDPMMGTAP 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 99 TLSVFENV-------DFFGRLFGHDKAERERrIADLLQSTGLApFAER---PAGKLSGGMKQKLGLCCALIHDPDLLILD 168
Cdd:COG1101 96 SMTIEENLalayrrgKRRGLRRGLTKKRREL-FRELLATLGLG-LENRldtKVGLLSGGQRQALSLLMATLTKPKLLLLD 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 15600424 169 EPTTGVDPLSRNQFWELIGRIrAGREGMSVLVATAYMEEAERF-DWLVAMDDGKV 222
Cdd:COG1101 174 EHTAALDPKTAALVLELTEKI-VEENNLTTLMVTHNMEQALDYgNRLIMMHEGRI 227
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
10-437 |
3.17e-17 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 86.54 E-value: 3.17e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 10 SLRGVSLRYGETRAVDDVSLEIPANRMVGLIGPDGVGKSSLLALLAGARKMQDGEIrVLDGDMRDRRHR----RAVCPRI 85
Cdd:PRK11147 5 SIHGAWLSFSDAPLLDNAELHIEDNERVCLVGRNGAGKSTLMKILNGEVLLDDGRI-IYEQDLIVARLQqdppRNVEGTV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 86 -AYMPQGL---GKNL--YPTLSvfenvdffgRLFGHDKAER--------------------ERRIADLLQSTGLAPfaER 139
Cdd:PRK11147 84 yDFVAEGIeeqAEYLkrYHDIS---------HLVETDPSEKnlnelaklqeqldhhnlwqlENRINEVLAQLGLDP--DA 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 140 PAGKLSGGMKQKLGLCCALIHDPDLLILDEPTTGVDPLSRNqfW------ELIGRI------RAGREGMS---------V 198
Cdd:PRK11147 153 ALSSLSGGWLRKAALGRALVSNPDVLLLDEPTNHLDIETIE--WlegflkTFQGSIifishdRSFIRNMAtrivdldrgK 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 199 LVA-----TAYM---EEAER--------FDWLVAMD---------------DGKVLA-TGTPQELRERTGTQSleSAFIA 246
Cdd:PRK11147 231 LVSypgnyDQYLlekEEALRveelqnaeFDRKLAQEevwirqgikarrtrnEGRVRAlKALRRERSERREVMG--TAKMQ 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 247 lLPESKRAGhhrlvipprpqsegapRIAIEAEGLTCRFGDFVAVDHVSFRIERGEIFGFLGSNGCGKSTTMKMLTGLLPA 326
Cdd:PRK11147 309 -VEEASRSG----------------KIVFEMENVNYQIDGKQLVKDFSAQVQRGDKIALIGPNGCGKTTLLKLMLGQLQA 371
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 327 SEGT--CalfgqpvdasdmATRRRVGYMSQ-AFSLYAELSVRQNLvlharlfhlpAD--------GIPARVGEMLRRFDL 395
Cdd:PRK11147 372 DSGRihC------------GTKLEVAYFDQhRAELDPEKTVMDNL----------AEgkqevmvnGRPRHVLGYLQDFLF 429
|
490 500 510 520
....*....|....*....|....*....|....*....|...
gi 15600424 396 E-KVADELPNDLPLGIRQRLSLAVAVIHKPEILILDEPTSGVD 437
Cdd:PRK11147 430 HpKRAMTPVKALSGGERNRLLLARLFLKPSNLLILDEPTNDLD 472
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
275-482 |
3.51e-17 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 85.79 E-value: 3.51e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 275 IEAEGLTCRFGD--FvAVDHVSFRIERGEIFGFLGSNGCGKSTTMKMLTGLLPASEGTCALFGQPVDASDMATRRRVgyM 352
Cdd:PRK10522 323 LELRNVTFAYQDngF-SVGPINLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKPVTAEQPEDYRKL--F 399
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 353 SQAFS---LYAELSVRQNlvlharlfhLPADgiPARVGEMLRRFDLE---KVADELPNDLPL--GIRQRLSLAVAVIHKP 424
Cdd:PRK10522 400 SAVFTdfhLFDQLLGPEG---------KPAN--PALVEKWLERLKMAhklELEDGRISNLKLskGQKKRLALLLALAEER 468
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 15600424 425 EILILDEPTSGVDPVARDGFWELMVELSRRDGVTIFISTHFMNEAQRCDRISLMHAGK 482
Cdd:PRK10522 469 DILLLDEWAADQDPHFRREFYQVLLPLLQEMGKTIFAISHDDHYFIHADRLLEMRNGQ 526
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
291-495 |
4.49e-17 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 85.93 E-value: 4.49e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 291 DHVSFRIERGEIFGFLGSNGCGKSTTMKMLTGLLPASEGTCALFGQPV---DASDMATRRR--VGYMSQAFSLYAELSVR 365
Cdd:PRK10535 25 KGISLDIYAGEMVAIVGASGSGKSTLMNILGCLDKPTSGTYRVAGQDVatlDADALAQLRRehFGFIFQRYHLLSHLTAA 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 366 QNLVLHARLFHLPADGIPARVGEMLRRFDLEKVADELPNDLPLGIRQRLSLAVAVIHKPEILILDEPTSGVDPVARDgfw 445
Cdd:PRK10535 105 QNVEVPAVYAGLERKQRLLRAQELLQRLGLEDRVEYQPSQLSGGQQQRVSIARALMNGGQVILADEPTGALDSHSGE--- 181
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 15600424 446 ELMVELS--RRDGVTIFISTHFMNEAQRCDRISLMHAGKVLaSDTPDELVRQ 495
Cdd:PRK10535 182 EVMAILHqlRDRGHTVIIVTHDPQVAAQAERVIEIRDGEIV-RNPPAQEKVN 232
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
275-489 |
5.90e-17 |
|
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: 80.53 E-value: 5.90e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 275 IEAEGLTCRFGDFV--AVDHVSFRIERGEIFGFLGSNGCGKSTTMKMLTGLLPASEGTCALFGQPVDASDMAT-RRRVGY 351
Cdd:cd03369 7 IEVENLSVRYAPDLppVLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDGIDISTIPLEDlRSSLTI 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 352 MSQAFSLYAElSVRQNLvlharlfhlpadgiparvgEMLRRFDLEKVADELP-----NDLPLGIRQRLSLAVAVIHKPEI 426
Cdd:cd03369 87 IPQDPTLFSG-TIRSNL-------------------DPFDEYSDEEIYGALRvseggLNLSQGQRQLLCLARALLKRPRV 146
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15600424 427 LILDEPTSGVDpVARDGfweLMVELSRRD--GVTIFISTHFMNEAQRCDRISLMHAGKVLASDTP 489
Cdd:cd03369 147 LVLDEATASID-YATDA---LIQKTIREEftNSTILTIAHRLRTIIDYDKILVMDAGEVKEYDHP 207
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
13-255 |
6.27e-17 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 81.66 E-value: 6.27e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 13 GVSLRYGETRAVDDVSLEIPANRMVGLIGPDGVGKSSLLALLAGARKMQDGEIRVLDGDMR--DRRHRRAVCPRIAYMPQ 90
Cdd:PRK10419 17 GLSGKHQHQTVLNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWRGEPLAklNRAQRKAFRRDIQMVFQ 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 91 GLGKNLYPTLSVFENVDFFGR-LFGHDKAERERRIADLLQSTGLAP-FAERPAGKLSGGMKQKLGLCCALIHDPDLLILD 168
Cdd:PRK10419 97 DSISAVNPRKTVREIIREPLRhLLSLDKAERLARASEMLRAVDLDDsVLDKRPPQLSGGQLQRVCLARALAVEPKLLILD 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 169 EPTTGVDPLSRNQFWELIGRIRAgREGMSVLVATAYMEEAERFDWLVA-MDDGKVL---ATGTPQELRERTGtQSLESAF 244
Cdd:PRK10419 177 EAVSNLDLVLQAGVIRLLKKLQQ-QFGTACLFITHDLRLVERFCQRVMvMDNGQIVetqPVGDKLTFSSPAG-RVLQNAV 254
|
250
....*....|.
gi 15600424 245 IALLPESKRAG 255
Cdd:PRK10419 255 LPAFPVRRRTT 265
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
10-181 |
6.40e-17 |
|
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: 78.26 E-value: 6.40e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 10 SLRGVSLRYGETRAVDDVSLEIPANRMVGLIGPDGVGKSSLLALLAGARKMQDGEIRVLDGdmrdrrhrravcPRIAYMP 89
Cdd:cd03221 2 ELENLSKTYGGKLLLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIVTWGST------------VKIGYFE 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 90 QglgknlyptlsvfenvdffgrlfghdkaererriadllqstglapfaerpagkLSGGMKQKLGLCCALIHDPDLLILDE 169
Cdd:cd03221 70 Q-----------------------------------------------------LSGGEKMRLALAKLLLENPNLLLLDE 96
|
170
....*....|..
gi 15600424 170 PTTGVDPLSRNQ 181
Cdd:cd03221 97 PTNHLDLESIEA 108
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
14-231 |
9.84e-17 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 81.21 E-value: 9.84e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 14 VSLRYGETRAVDDVSLEIPANRMVGLIGPDGVGKSSLLALLAG---ARKMQDGEIRVL------DGDM-RDRRHRRAvcp 83
Cdd:PRK09984 10 LAKTFNQHQALHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGlitGDKSAGSHIELLgrtvqrEGRLaRDIRKSRA--- 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 84 RIAYMPQGLgkNLYPTLSVFENV--------DFFGRLFGHDKAERERRIADLLQSTGLAPFAERPAGKLSGGMKQKLGLC 155
Cdd:PRK09984 87 NTGYIFQQF--NLVNRLSVLENVligalgstPFWRTCFSWFTREQKQRALQALTRVGMVHFAHQRVSTLSGGQQQRVAIA 164
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15600424 156 CALIHDPDLLILDEPTTGVDPLSRNQFWELIGRIRAgREGMSVLVATAYMEEAERF-DWLVAMDDGKVLATGTPQEL 231
Cdd:PRK09984 165 RALMQQAKVILADEPIASLDPESARIVMDTLRDINQ-NDGITVVVTLHQVDYALRYcERIVALRQGHVFYDGSSQQF 240
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
10-170 |
9.85e-17 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 82.97 E-value: 9.85e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 10 SLRGVSLRY-GETRAVDDVSLEIPANRMVGLIGPDGVGKSSLLALLAGARKMQDGEI-----RVLDGDMRDRRhrravcp 83
Cdd:PRK11650 5 KLQAVRKSYdGKTQVIKGIDLDVADGEFIVLVGPSGCGKSTLLRMVAGLERITSGEIwiggrVVNELEPADRD------- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 84 rIAYMPQglgkN--LYPTLSVFENVDFFGRLFGHDKAERERRIADLLQSTGLAPFAERPAGKLSGGMKQKLGLCCALIHD 161
Cdd:PRK11650 78 -IAMVFQ----NyaLYPHMSVRENMAYGLKIRGMPKAEIEERVAEAARILELEPLLDRKPRELSGGQRQRVAMGRAIVRE 152
|
....*....
gi 15600424 162 PDLLILDEP 170
Cdd:PRK11650 153 PAVFLFDEP 161
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
11-237 |
1.04e-16 |
|
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: 80.28 E-value: 1.04e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 11 LRGVSLRY---GETRAVDDVSLEIPANRMVGLIGPDGVGKSSLLALLAGARKMQDGEIrVLDG-DMRD---RRHRRavcp 83
Cdd:cd03249 3 FKNVSFRYpsrPDVPILKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEI-LLDGvDIRDlnlRWLRS---- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 84 RIAYMPQGlgknlyPTL---SVFENVdffgrLFGHDKAERERRIADLLQSTGLAPFAERPAG----------KLSGGMKQ 150
Cdd:cd03249 78 QIGLVSQE------PVLfdgTIAENI-----RYGKPDATDEEVEEAAKKANIHDFIMSLPDGydtlvgergsQLSGGQKQ 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 151 KLGLCCALIHDPDLLILDEPTTGVDPLSRNQFWELIGRIRAGRegmSVLVATAYMEEAERFDWLVAMDDGKVLATGTPQE 230
Cdd:cd03249 147 RIAIARALLRNPKILLLDEATSALDAESEKLVQEALDRAMKGR---TTIVIAHRLSTIRNADLIAVLQNGQVVEQGTHDE 223
|
....*..
gi 15600424 231 LRERTGT 237
Cdd:cd03249 224 LMAQKGV 230
|
|
| type_I_sec_PrtD |
TIGR01842 |
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in ... |
293-495 |
1.18e-16 |
|
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: 84.32 E-value: 1.18e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 293 VSFRIERGEIFGFLGSNGCGKSTTMKMLTGLLPASEGTCALFGQPVDASDMAT-RRRVGYMSQAFSLYAElSVRQNLvlh 371
Cdd:TIGR01842 337 ISFSLQAGEALAIIGPSGSGKSTLARLIVGIWPPTSGSVRLDGADLKQWDRETfGKHIGYLPQDVELFPG-TVAENI--- 412
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 372 ARlFHLPADgiPARVGEMLRRFDLEKVADELPN-----------DLPLGIRQRLSLAVAVIHKPEILILDEPTSGVDPVA 440
Cdd:TIGR01842 413 AR-FGENAD--PEKIIEAAKLAGVHELILRLPDgydtvigpggaTLSGGQRQRIALARALYGDPKLVVLDEPNSNLDEEG 489
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 15600424 441 RDGFWELMVELSRRDGVTIFIsTHFMNEAQRCDRISLMHAGKVLASDTPDELVRQ 495
Cdd:TIGR01842 490 EQALANAIKALKARGITVVVI-THRPSLLGCVDKILVLQDGRIARFGERDEVLAK 543
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
275-483 |
1.83e-16 |
|
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 443332 [Multi-domain] Cd Length: 533 Bit Score: 83.58 E-value: 1.83e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 275 IEAEGLTCRFGD----FVAVDHVSFRIERGEIFGFLGSNGCGKSTTMKMLTGLLPASEGTC---ALF-GQPVDASDMATR 346
Cdd:COG4172 7 LSVEDLSVAFGQgggtVEAVKGVSFDIAAGETLALVGESGSGKSVTALSILRLLPDPAAHPsgsILFdGQDLLGLSEREL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 347 RRV--GYMSQAF-----SLYAELSV-RQ---NLVLHARlfhLPADGIPARVGEMLRRF---DLEKVADELPNDLPLGIRQ 412
Cdd:COG4172 87 RRIrgNRIAMIFqepmtSLNPLHTIgKQiaeVLRLHRG---LSGAAARARALELLERVgipDPERRLDAYPHQLSGGQRQ 163
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15600424 413 RLSLAVAVIHKPEILILDEPTSGVDPVARDGFWELMVELSRRDGVTI-FIsTHFMNEAQR-CDRISLMHAGKV 483
Cdd:COG4172 164 RVMIAMALANEPDLLIADEPTTALDVTVQAQILDLLKDLQRELGMALlLI-THDLGVVRRfADRVAVMRQGEI 235
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
275-498 |
1.96e-16 |
|
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: 83.61 E-value: 1.96e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 275 IEAEGLTCRFG--DFVAVDHVSFRIERGEIFGFLGSNGCGKSTTMKMLTGLLPASEGTCALFGQPV-DASDMATRRRVGY 351
Cdd:TIGR02203 331 VEFRNVTFRYPgrDRPALDSISLVIEPGETVALVGRSGSGKSTLVNLIPRFYEPDSGQILLDGHDLaDYTLASLRRQVAL 410
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 352 MSQAFSLYAElSVRQNlVLHARlfhlPADGIPARVGEMLRRFDLEKVADELPN--DLPLGI---------RQRLSLAVAV 420
Cdd:TIGR02203 411 VSQDVVLFND-TIANN-IAYGR----TEQADRAEIERALAAAYAQDFVDKLPLglDTPIGEngvllsggqRQRLAIARAL 484
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 421 IHKPEILILDEPTSGVDP----VARDGFWELMvelsrrDGVTIFISTHFMNEAQRCDRISLMHAGKVLASDTPDELVRQR 496
Cdd:TIGR02203 485 LKDAPILILDEATSALDNeserLVQAALERLM------QGRTTLVIAHRLSTIEKADRIVVMDDGRIVERGTHNELLARN 558
|
..
gi 15600424 497 GL 498
Cdd:TIGR02203 559 GL 560
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
11-210 |
3.23e-16 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 79.70 E-value: 3.23e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 11 LRGVSLRYGETRAVDDVSLEIPANRMVGLIGPDGVGKSSLLALLAGARKMQdGEIRVlDGDM---------------RDR 75
Cdd:PRK14258 10 VNNLSFYYDTQKILEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLNRMNELE-SEVRV-EGRVeffnqniyerrvnlnRLR 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 76 RHRRAVCPRiaympqglgKNLYPtLSVFENVDFFGRLFG-HDKAERERRIADLLQSTGLAPFAE----RPAGKLSGGMKQ 150
Cdd:PRK14258 88 RQVSMVHPK---------PNLFP-MSVYDNVAYGVKIVGwRPKLEIDDIVESALKDADLWDEIKhkihKSALDLSGGQQQ 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 151 KLGLCCALIHDPDLLILDEPTTGVDPLSRNQFWELIGRIRAgREGMSVLVATAYMEEAER 210
Cdd:PRK14258 158 RLCIARALAVKPKVLLMDEPCFGLDPIASMKVESLIQSLRL-RSELTMVIVSHNLHQVSR 216
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
293-498 |
3.28e-16 |
|
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: 78.81 E-value: 3.28e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 293 VSFRIERGEIFGFLGSNGCGKSTTMKMLTGLLPASEGTCALFGQPVDASDMAT-RRRVGYMSQAFSL----------YAE 361
Cdd:cd03253 20 VSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDGQDIREVTLDSlRRAIGVVPQDTVLfndtigynirYGR 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 362 LSVRQNLV--------LHARLFHLPaDGIPARVGEM-LRrfdlekvadelpndLPLGIRQRLSLAVAVIHKPEILILDEP 432
Cdd:cd03253 100 PDATDEEVieaakaaqIHDKIMRFP-DGYDTIVGERgLK--------------LSGGEKQRVAIARAILKNPPILLLDEA 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15600424 433 TSGVDPVARDGFWELMVELSRRDgVTIFIsTHFMNEAQRCDRISLMHAGKVLASDTPDELVRQRGL 498
Cdd:cd03253 165 TSALDTHTEREIQAALRDVSKGR-TTIVI-AHRLSTIVNADKIIVLKDGRIVERGTHEELLAKGGL 228
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
286-492 |
3.35e-16 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 79.32 E-value: 3.35e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 286 DFVAVDHVSFRIERGEIFGFLGSNGCGKSTTMKMLTGLLP------ASEGTCALFGQPVDASD-MATRRRVGYMSQAFSL 358
Cdd:PRK14246 22 DKAILKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLIEiydskiKVDGKVLYFGKDIFQIDaIKLRKEVGMVFQQPNP 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 359 YAELSVRQNLVlharlFHLPADGIPAR------VGEMLRRFDLEK-VADEL---PNDLPLGIRQRLSLAVAVIHKPEILI 428
Cdd:PRK14246 102 FPHLSIYDNIA-----YPLKSHGIKEKreikkiVEECLRKVGLWKeVYDRLnspASQLSGGQQQRLTIARALALKPKVLL 176
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15600424 429 LDEPTSGVDPVARDGFWELMVELSRRdgVTIFISTHFMNEAQR-CDRISLMHAGKVLASDTPDEL 492
Cdd:PRK14246 177 MDEPTSMIDIVNSQAIEKLITELKNE--IAIVIVSHNPQQVARvADYVAFLYNGELVEWGSSNEI 239
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
270-497 |
3.54e-16 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 82.95 E-value: 3.54e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 270 APRIAIEAEGLTCRFGD--FVAVDHVSFRIERGEIFGFLGSNGCGKSTTMKMLTGLLPASEGTCALFGQPVDA-SDMATR 346
Cdd:PRK11160 334 ADQVSLTLNNVSFTYPDqpQPVLKGLSLQIKAGEKVALLGRTGCGKSTLLQLLTRAWDPQQGEILLNGQPIADySEAALR 413
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 347 RRVGYMSQAFSLYAElSVRQNLVLHArlfhlpADGIPARVGEMLRRFDLEKVADelpNDLPL------GIRQ-------R 413
Cdd:PRK11160 414 QAISVVSQRVHLFSA-TLRDNLLLAA------PNASDEALIEVLQQVGLEKLLE---DDKGLnawlgeGGRQlsggeqrR 483
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 414 LSLAVAVIHKPEILILDEPTSGVDPVARDGFWELMVELSRrdGVTIFISTHFMNEAQRCDRISLMHAGKVLASDTPDELV 493
Cdd:PRK11160 484 LGIARALLHDAPLLLLDEPTEGLDAETERQILELLAEHAQ--NKTVLMITHRLTGLEQFDRICVMDNGQIIEQGTHQELL 561
|
....
gi 15600424 494 RQRG 497
Cdd:PRK11160 562 AQQG 565
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
289-462 |
4.04e-16 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 80.39 E-value: 4.04e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 289 AVDHVSFRIERGEIFGFLGSNGCGKSTTMKMLTGLLPASEGTCALFGQPVDASDMAT----RRRVGYMSQafSLYAELSV 364
Cdd:PRK11308 30 ALDGVSFTLERGKTLAVVGESGCGKSTLARLLTMIETPTGGELYYQGQDLLKADPEAqkllRQKIQIVFQ--NPYGSLNP 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 365 RQN--------LVLHARlfhLPADGIPARVGEMLRRFDLE-KVADELPNDLPLGIRQRLSLAVAVIHKPEILILDEPTSG 435
Cdd:PRK11308 108 RKKvgqileepLLINTS---LSAAERREKALAMMAKVGLRpEHYDRYPHMFSGGQRQRIAIARALMLDPDVVVADEPVSA 184
|
170 180
....*....|....*....|....*...
gi 15600424 436 VDPVARDGFWELMVELSRRDGVT-IFIS 462
Cdd:PRK11308 185 LDVSVQAQVLNLMMDLQQELGLSyVFIS 212
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
22-175 |
4.65e-16 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 80.55 E-value: 4.65e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 22 RAVDDVSLEIPANRMVGLIGPDGVGKSSLLALLAGARKMQDGEIR-----VLDGDMRDRRHRRavcPRIAYM---PQGlg 93
Cdd:COG4608 32 KAVDGVSFDIRRGETLGLVGESGCGKSTLGRLLLRLEEPTSGEILfdgqdITGLSGRELRPLR---RRMQMVfqdPYA-- 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 94 kNLYPTLSVFENVDFFGRLFG-HDKAERERRIADLLQSTGLAP-FAERPAGKLSGGMKQKLGLCCALIHDPDLLILDEPT 171
Cdd:COG4608 107 -SLNPRMTVGDIIAEPLRIHGlASKAERRERVAELLELVGLRPeHADRYPHEFSGGQRQRIGIARALALNPKLIVCDEPV 185
|
....
gi 15600424 172 TGVD 175
Cdd:COG4608 186 SALD 189
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
276-482 |
6.11e-16 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 81.76 E-value: 6.11e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 276 EAEGLTCRFGDFVAVDHVSFRIERGEIFGFLGSNGCGKSTTMKMLTGLLPAS--EGTCALFGQPVDASDMATRRRVGY-- 351
Cdd:NF040905 3 EMRGITKTFPGVKALDDVNLSVREGEIHALCGENGAGKSTLMKVLSGVYPHGsyEGEILFDGEVCRFKDIRDSEALGIvi 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 352 MSQAFSLYAELSVRQNLVL---HARLFHLPADGIPARVGEMLRRFDLEKVADELPNDLPLGIRQRLSLAVAVIHKPEILI 428
Cdd:NF040905 83 IHQELALIPYLSIAENIFLgneRAKRGVIDWNETNRRARELLAKVGLDESPDTLVTDIGVGKQQLVEIAKALSKDVKLLI 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 15600424 429 LDEPTSGVDPVARDGFWELMVELsRRDGVT-IFIStHFMNE-AQRCDRISLMHAGK 482
Cdd:NF040905 163 LDEPTAALNEEDSAALLDLLLEL-KAQGITsIIIS-HKLNEiRRVADSITVLRDGR 216
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
279-495 |
7.08e-16 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 81.50 E-value: 7.08e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 279 GLTCRFGDFVAVDHVSFRIERGEIFGFLGSNGCGKSTTMKMLTGLLPASEGTCALFGQPV---DASDmATRRRVGYMSQA 355
Cdd:PRK11288 9 GIGKTFPGVKALDDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSILIDGQEMrfaSTTA-ALAAGVAIIYQE 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 356 FSLYAELSVRQNLVLHarlfHLPADG-------IPARVGEMLRRFDLEKVADELPNDLPLGIRQRLSLAVAVIHKPEILI 428
Cdd:PRK11288 88 LHLVPEMTVAENLYLG----QLPHKGgivnrrlLNYEAREQLEHLGVDIDPDTPLKYLSIGQRQMVEIAKALARNARVIA 163
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15600424 429 LDEPTSGVDPVARDGFWELMVELsRRDGVTIFISTHFMNEAQR-CDRISLMHAGKV------LASDTPDELVRQ 495
Cdd:PRK11288 164 FDEPTSSLSAREIEQLFRVIREL-RAEGRVILYVSHRMEEIFAlCDAITVFKDGRYvatfddMAQVDRDQLVQA 236
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
275-464 |
1.30e-15 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 76.38 E-value: 1.30e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 275 IEAEGLTCRFGDFVAVDHVSFRIERGEIFGFLGSNGCGKSTTMKMLTGLLPASEGTCALFGQPVDASDMATRRRVGYMSQ 354
Cdd:PRK13538 2 LEARNLACERDERILFSGLSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVLWQGEPIRRQRDEYHQDLLYLGH 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 355 AFSLYAELSVRQNLVLHARLFHLPADgipARVGEMLRRFDLEKVADELPNDLPLGIRQRLSLAVAVIHKPEILILDEPTS 434
Cdd:PRK13538 82 QPGIKTELTALENLRFYQRLHGPGDD---EALWEALAQVGLAGFEDVPVRQLSAGQQRRVALARLWLTRAPLWILDEPFT 158
|
170 180 190
....*....|....*....|....*....|
gi 15600424 435 GVDPVARDGFWELMVELSRRDGVTIFiSTH 464
Cdd:PRK13538 159 AIDKQGVARLEALLAQHAEQGGMVIL-TTH 187
|
|
| BtuD |
COG4138 |
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ... |
27-263 |
1.35e-15 |
|
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism];
Pssm-ID: 443313 [Multi-domain] Cd Length: 248 Bit Score: 77.57 E-value: 1.35e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 27 VSLEIPANRMVGLIGPDGVGKSSLLALLAGARKMQdGEIRVLDGDMRD------RRHRravcpriAYMPQglgkNLYPT- 99
Cdd:COG4138 15 ISAQVNAGELIHLIGPNGAGKSTLLARMAGLLPGQ-GEILLNGRPLSDwsaaelARHR-------AYLSQ----QQSPPf 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 100 -LSVFENVDFFGRLfGHDKAERERRIADLLQSTGLAPFAERPAGKLSGGMKQKLGLCCAL--IH---DPD--LLILDEPT 171
Cdd:COG4138 83 aMPVFQYLALHQPA-GASSEAVEQLLAQLAEALGLEDKLSRPLTQLSGGEWQRVRLAAVLlqVWptiNPEgqLLLLDEPM 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 172 TGVDPLSRNQFWELIGRIRAgrEGMSVLVATAYMEEAERF-D--WLvaMDDGKVLATGTPQE-LRERTGTQSLESAFIAL 247
Cdd:COG4138 162 NSLDVAQQAALDRLLRELCQ--QGITVVMSSHDLNHTLRHaDrvWL--LKQGKLVASGETAEvMTPENLSEVFGVKFRRL 237
|
250
....*....|....*.
gi 15600424 248 lpeskRAGHHRLVIPP 263
Cdd:COG4138 238 -----EVEGHRWLIPT 248
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
289-464 |
1.64e-15 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 76.45 E-value: 1.64e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 289 AVDHVSFRIERGEIFGFLGSNGCGKSTTMKMLTGLLPASEGTCALFGQpvDASDMAT------RRRVGYMSQAFSLYAEL 362
Cdd:PRK10908 17 ALQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGH--DITRLKNrevpflRRQIGMIFQDHHLLMDR 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 363 SVRQNLVLHARLFHLPADGIPARVGEMLRRFDLEKVADELPNDLPLGIRQRLSLAVAVIHKPEILILDEPTSGVDPVARD 442
Cdd:PRK10908 95 TVYDNVAIPLIIAGASGDDIRRRVSAALDKVGLLDKAKNFPIQLSGGEQQRVGIARAVVNKPAVLLADEPTGNLDDALSE 174
|
170 180
....*....|....*....|..
gi 15600424 443 GFWELMVELSRRdGVTIFISTH 464
Cdd:PRK10908 175 GILRLFEEFNRV-GVTVLMATH 195
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
12-233 |
1.98e-15 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 77.19 E-value: 1.98e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 12 RGVSLRYGETRAVDDVSLEIPANRMVGLIGPDGVGKSSLL-------ALLAGARkmQDGEIR-----VLDGDMRDRRHRR 79
Cdd:PRK14267 8 VNLRVYYGSNHVIKGVDLKIPQNGVFALMGPSGCGKSTLLrtfnrllELNEEAR--VEGEVRlfgrnIYSPDVDPIEVRR 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 80 AVCPRIAYmpqglgKNLYPTLSVFENVDFFGRLFG--HDKAERERRIADLLQSTGL-APFAER---PAGKLSGGMKQKLG 153
Cdd:PRK14267 86 EVGMVFQY------PNPFPHLTIYDNVAIGVKLNGlvKSKKELDERVEWALKKAALwDEVKDRlndYPSNLSGGQRQRLV 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 154 LCCALIHDPDLLILDEPTTGVDPLSRNQFWELIGRIRagREGMSVLVATAYMEEAERFDWLVAMDDGKVLATGTPQELRE 233
Cdd:PRK14267 160 IARALAMKPKILLMDEPTANIDPVGTAKIEELLFELK--KEYTIVLVTHSPAQAARVSDYVAFLYLGKLIEVGPTRKVFE 237
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
289-486 |
2.10e-15 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 77.62 E-value: 2.10e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 289 AVDHVSFRIERGEIFGFLGSNGCGKSTTMKMLTGLLPASEGTCALFGQPVDASdmATRRRVGYMSQ------AFSLYAEL 362
Cdd:PRK15056 22 ALRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKISILGQPTRQA--LQKNLVAYVPQseevdwSFPVLVED 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 363 SVRQNLVLHARLFHLPADGIPARVGEMLRRFDLEKVADELPNDLPLGIRQRLSLAVAVIHKPEILILDEPTSGVDPVARD 442
Cdd:PRK15056 100 VVMMGRYGHMGWLRRAKKRDRQIVTAALARVDMVEFRHRQIGELSGGQKKRVFLARAIAQQGQVILLDEPFTGVDVKTEA 179
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 15600424 443 GFWELMVELsRRDGVTIFISTHFMNEAQR-CDrISLMHAGKVLAS 486
Cdd:PRK15056 180 RIISLLREL-RDEGKTMLVSTHNLGSVTEfCD-YTVMVKGTVLAS 222
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
275-495 |
2.15e-15 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 77.50 E-value: 2.15e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 275 IEAEGLTCRFGDFVAVDHVSFRIERGEIFGFLGSNGCGKSTTMKMLTGLLPASEGTCALFGQPVDASD----MATRRRVG 350
Cdd:PRK11831 8 VDMRGVSFTRGNRCIFDNISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEILFDGENIPAMSrsrlYTVRKRMS 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 351 YMSQAFSLYAELSVRQNLVLHARLF-HLPADGIPARVGEMLRRFDLEKVADELPNDLPLGIRQRLSLAVAVIHKPEILIL 429
Cdd:PRK11831 88 MLFQSGALFTDMNVFDNVAYPLREHtQLPAPLLHSTVMMKLEAVGLRGAAKLMPSELSGGMARRAALARAIALEPDLIMF 167
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15600424 430 DEPTSGVDPVARDGFWELMVELSRRDGVTIFISTHFMNEAQR-CDRISLMHAGKVLASDTPDEL-------VRQ 495
Cdd:PRK11831 168 DEPFVGQDPITMGVLVKLISELNSALGVTCVVVSHDVPEVLSiADHAYIVADKKIVAHGSAQALqanpdprVRQ 241
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
274-471 |
2.62e-15 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 77.00 E-value: 2.62e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 274 AIEAEGLTCRFGDFVAVDHVSFRIERGEIFGFLGSNGCGKSTTMKMLTGLLPAS-----EGTCALFGQPVDASDMAT--- 345
Cdd:PRK14258 7 AIKVNNLSFYYDTQKILEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLNRMNELEsevrvEGRVEFFNQNIYERRVNLnrl 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 346 RRRVGYMSQAFSLYAeLSVRQNLVLHARLF----HLPADGIparVGEMLRRFDLekvADELPN-------DLPLGIRQRL 414
Cdd:PRK14258 87 RRQVSMVHPKPNLFP-MSVYDNVAYGVKIVgwrpKLEIDDI---VESALKDADL---WDEIKHkihksalDLSGGQQQRL 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 15600424 415 SLAVAVIHKPEILILDEPTSGVDPVARDGFWELMVELSRRDGVTIFISTHFMNEAQR 471
Cdd:PRK14258 160 CIARALAVKPKVLLMDEPCFGLDPIASMKVESLIQSLRLRSELTMVIVSHNLHQVSR 216
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
289-497 |
2.93e-15 |
|
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: 80.17 E-value: 2.93e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 289 AVDHVSFRIERGEIFGFLGSNGCGKSTTMKMLTGLLPASEGTCALFGQPVDASDMAT-RRRVGYMSQAFSLYAElSVRQN 367
Cdd:TIGR01193 489 ILSDISLTIKMNSKTTIVGMSGSGKSTLAKLLVGFFQARSGEILLNGFSLKDIDRHTlRQFINYLPQEPYIFSG-SILEN 567
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 368 LVLHARLfhlpadgiPARVGEMLRRFDLEKVADELPNdLPLGI---------------RQRLSLAVAVIHKPEILILDEP 432
Cdd:TIGR01193 568 LLLGAKE--------NVSQDEIWAACEIAEIKDDIEN-MPLGYqtelseegssisggqKQRIALARALLTDSKVLILDES 638
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15600424 433 TSGVDPVARDGFWELMVELsrRDGVTIFIStHFMNEAQRCDRISLMHAGKVLASDTPDELVRQRG 497
Cdd:TIGR01193 639 TSNLDTITEKKIVNNLLNL--QDKTIIFVA-HRLSVAKQSDKIIVLDHGKIIEQGSHDELLDRNG 700
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
7-228 |
3.62e-15 |
|
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: 75.61 E-value: 3.62e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 7 GVASLRGVSLRYGETR--AVDDVSLEIPANRMVGLIGPDGVGKSSL-LALLagaR--KMQDGEIRVlDG------DMRDR 75
Cdd:cd03244 1 GDIEFKNVSLRYRPNLppVLKNISFSIKPGEKVGIVGRTGSGKSSLlLALF---RlvELSSGSILI-DGvdiskiGLHDL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 76 RHRRAVCPRIAYMPQGlgknlyptlSVFENVDFFGRlfgHDKAErerrIADLLQSTGLAPFAERPAGKL----------- 144
Cdd:cd03244 77 RSRISIIPQDPVLFSG---------TIRSNLDPFGE---YSDEE----LWQALERVGLKEFVESLPGGLdtvveeggenl 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 145 SGGMKQKLGLCCALIHDPDLLILDEPTTGVDPLSRNQFWELIGRIRAGRegmSVLVAtaymeeAER------FDWLVAMD 218
Cdd:cd03244 141 SVGQRQLLCLARALLRKSKILVLDEATASVDPETDALIQKTIREAFKDC---TVLTI------AHRldtiidSDRILVLD 211
|
250
....*....|
gi 15600424 219 DGKVLATGTP 228
Cdd:cd03244 212 KGRVVEFDSP 221
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
24-243 |
4.09e-15 |
|
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose isomerase and xylulokinase enzymes for xylose utilization. Members of this protein family are the ATP-binding cassette (ABC) subunit of the known or predicted high-affinity xylose ABC transporter for xylose import. These genes, which closely resemble other sugar transport ABC transporter genes, typically are encoded near xylose utilization enzymes and regulatory proteins. Note that this form of the transporter contains two copies of the ABC transporter domain (pfam00005). [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 131681 [Multi-domain] Cd Length: 500 Bit Score: 79.10 E-value: 4.09e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 24 VDDVSLEIPANRMVGLIGPDGVGKSSLLALLAGARKMQ-DGEIrVLDGDMRDRRH-RRAVCPRIAYMPQ----------- 90
Cdd:TIGR02633 276 VDDVSFSLRRGEILGVAGLVGAGRTELVQALFGAYPGKfEGNV-FINGKPVDIRNpAQAIRAGIAMVPEdrkrhgivpil 354
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 91 GLGKNLypTLSVFENVDFFGRLfghDKAERERRIADLLQSTGLAPFA-ERPAGKLSGGMKQKLGLCCALIHDPDLLILDE 169
Cdd:TIGR02633 355 GVGKNI--TLSVLKSFCFKMRI---DAAAELQIIGSAIQRLKVKTASpFLPIGRLSGGNQQKAVLAKMLLTNPRVLILDE 429
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15600424 170 PTTGVDPLSRNQFWELIGRIraGREGMSVLVATAYMEEAERF-DWLVAMDDGKVLATGTPQELrerTGTQSLESA 243
Cdd:TIGR02633 430 PTRGVDVGAKYEIYKLINQL--AQEGVAIIVVSSELAEVLGLsDRVLVIGEGKLKGDFVNHAL---TQEQVLAAA 499
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
21-236 |
7.93e-15 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 78.73 E-value: 7.93e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 21 TRAVDDVSLEIPANRMVGLIGPDGVGKSSLLALLAGARKMQdGEIRVLDGDMRD------RRHrravcprIAYmpqgLGK 94
Cdd:PRK11174 363 KTLAGPLNFTLPAGQRIALVGPSGAGKTSLLNALLGFLPYQ-GSLKINGIELREldpeswRKH-------LSW----VGQ 430
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 95 NlyPTL---SVFENVdffgrLFGHDKAERERrIADLLQSTGLAPFAERP-----------AGKLSGGMKQKLGLCCALIH 160
Cdd:PRK11174 431 N--PQLphgTLRDNV-----LLGNPDASDEQ-LQQALENAWVSEFLPLLpqgldtpigdqAAGLSVGQAQRLALARALLQ 502
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15600424 161 DPDLLILDEPTTGVDPLSRNQFWELIGRIRAGRegmSVLVATAYMEEAERFDWLVAMDDGKVLATGTPQELRERTG 236
Cdd:PRK11174 503 PCQLLLLDEPTASLDAHSEQLVMQALNAASRRQ---TTLMVTHQLEDLAQWDQIWVMQDGQIVQQGDYAELSQAGG 575
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
293-483 |
8.48e-15 |
|
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: 74.43 E-value: 8.48e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 293 VSFRIERGEIFGFLGSNGCGKSTTMKMLTGLLPASEGTCALFGQPVDASDMA-TRRRVGYMSQAFSLYAElSVRQNLVLH 371
Cdd:cd03248 33 VSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDGKPISQYEHKyLHSKVSLVGQEPVLFAR-SLQDNIAYG 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 372 arLFHLPADGIPAR---------VGEMLRRFDLEkvADELPNDLPLGIRQRLSLAVAVIHKPEILILDEPTSGVDPVArd 442
Cdd:cd03248 112 --LQSCSFECVKEAaqkahahsfISELASGYDTE--VGEKGSQLSGGQKQRVAIARALIRNPQVLILDEATSALDAES-- 185
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 15600424 443 gfwELMVELSRRDGV---TIFISTHFMNEAQRCDRISLMHAGKV 483
Cdd:cd03248 186 ---EQQVQQALYDWPerrTVLVIAHRLSTVERADQILVLDGGRI 226
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
275-493 |
9.06e-15 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 74.92 E-value: 9.06e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 275 IEAEGLTCRFGDFVAVDHVSFRIERGEIFGFLGSNGCGKSTTMKMLTGLLPASEGTCALFGQpvDASDMAT----RRRVG 350
Cdd:PRK11614 6 LSFDKVSAHYGKIQALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDGK--DITDWQTakimREAVA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 351 YMSQAFSLYAELSVRQNLVLharlfhlpaDGIPARVGEMLRRfdLEKVADELP----------NDLPLGIRQRLSLAVAV 420
Cdd:PRK11614 84 IVPEGRRVFSRMTVEENLAM---------GGFFAERDQFQER--IKWVYELFPrlherriqraGTMSGGEQQMLAIGRAL 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15600424 421 IHKPEILILDEPTSGVDPVARDGFWELMVELsRRDGVTIFISTHFMNEAQR-CDRISLMHAGKVLASDTPDELV 493
Cdd:PRK11614 153 MSQPRLLLLDEPSLGLAPIIIQQIFDTIEQL-REQGMTIFLVEQNANQALKlADRGYVLENGHVVLEDTGDALL 225
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
7-222 |
9.32e-15 |
|
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: 74.43 E-value: 9.32e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 7 GVASLRGVSLRY---GETRAVDDVSLEIPANRMVGLIGPDGVGKSSLLALLAGARKMQDGEIrVLDG---DMRDRRHRRA 80
Cdd:cd03248 10 GIVKFQNVTFAYptrPDTLVLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQV-LLDGkpiSQYEHKYLHS 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 81 VCPRIAYMPQGLGKnlyptlSVFENVDF------FGRLF-GHDKAERERRIADLLQstGLAPFAERPAGKLSGGMKQKLG 153
Cdd:cd03248 89 KVSLVGQEPVLFAR------SLQDNIAYglqscsFECVKeAAQKAHAHSFISELAS--GYDTEVGEKGSQLSGGQKQRVA 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15600424 154 LCCALIHDPDLLILDEPTTGVDPLSRNQFWELigrIRAGREGMSVLVATAYMEEAERFDWLVAMDDGKV 222
Cdd:cd03248 161 IARALIRNPQVLILDEATSALDAESEQQVQQA---LYDWPERRTVLVIAHRLSTVERADQILVLDGGRI 226
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
277-486 |
1.05e-14 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 74.96 E-value: 1.05e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 277 AEGLTCRFGDFVAVDHVSFRIERGEIFGFLGSNGCGKSTTMKMLTGLLPASEGTcALF----GQPVDASDM--ATRRRVG 350
Cdd:PRK11701 9 VRGLTKLYGPRKGCRDVSFDLYPGEVLGIVGESGSGKTTLLNALSARLAPDAGE-VHYrmrdGQLRDLYALseAERRRLL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 351 YMSQAFslyaelsVRQNlvlharlfhlPADGIP------ARVGEML-----RRFD---------LEKVA------DELPN 404
Cdd:PRK11701 88 RTEWGF-------VHQH----------PRDGLRmqvsagGNIGERLmavgaRHYGdiratagdwLERVEidaariDDLPT 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 405 DLPLGIRQRLSLAVAVIHKPEILILDEPTSGVDPVARDGFWELMVELSRRDGVTIFISTHFMNEAQ-RCDRISLMHAGKV 483
Cdd:PRK11701 151 TFSGGMQQRLQIARNLVTHPRLVFMDEPTGGLDVSVQARLLDLLRGLVRELGLAVVIVTHDLAVARlLAHRLLVMKQGRV 230
|
...
gi 15600424 484 LAS 486
Cdd:PRK11701 231 VES 233
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
27-234 |
1.18e-14 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 74.79 E-value: 1.18e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 27 VSLEIPANRMVGLIGPDGVGKSSLLALLAGARKMQDGEIRVLDGDMRDRRHRRAVCPRIAYMPQGLGK-----NLYPTLS 101
Cdd:PRK11264 22 IDLEVKPGEVVAIIGPSGSGKTTLLRCINLLEQPEAGTIRVGDITIDTARSLSQQKGLIRQLRQHVGFvfqnfNLFPHRT 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 102 VFENVdFFGRLF--GHDKAERERRIADLLQSTGLAPFAERPAGKLSGGMKQKLGLCCALIHDPDLLILDEPTTGVDPlsr 179
Cdd:PRK11264 102 VLENI-IEGPVIvkGEPKEEATARARELLAKVGLAGKETSYPRRLSGGQQQRVAIARALAMRPEVILFDEPTSALDP--- 177
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15600424 180 nqfwELIGR----IRA-GREGMSVLVATAYMEEA-ERFDWLVAMDDGKVLATG-------TPQELRER 234
Cdd:PRK11264 178 ----ELVGEvlntIRQlAQEKRTMVIVTHEMSFArDVADRAIFMDQGRIVEQGpakalfaDPQQPRTR 241
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
20-231 |
1.20e-14 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 75.13 E-value: 1.20e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 20 ETRAVDDVSLEIPANRMVGLIGPDGVGKSSLLALLAGARKMQDGEIRVlDGDMRDRRHRRAVCPRIAYMPQGlGKNLYPT 99
Cdd:PRK13642 19 DVNQLNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKI-DGELLTAENVWNLRRKIGMVFQN-PDNQFVG 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 100 LSVFENVDFFGRLFGHDKAERERRIADLLQSTGLAPFAERPAGKLSGGMKQKLGLCCALIHDPDLLILDEPTTGVDPLSR 179
Cdd:PRK13642 97 ATVEDDVAFGMENQGIPREEMIKRVDEALLAVNMLDFKTREPARLSGGQKQRVAVAGIIALRPEIIILDESTSMLDPTGR 176
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 15600424 180 NQFWELIGRIRaGREGMSVLVATAYMEEAERFDWLVAMDDGKVLATGTPQEL 231
Cdd:PRK13642 177 QEIMRVIHEIK-EKYQLTVLSITHDLDEAASSDRILVMKAGEIIKEAAPSEL 227
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
275-489 |
1.21e-14 |
|
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: 74.07 E-value: 1.21e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 275 IEAEGLTCRFGD--FVAVDHVSFRIERGEIFGFLGSNGCGKSTTMKMLTGLLPASEGTCALFGqpVDASDMAT---RRRV 349
Cdd:cd03244 3 IEFKNVSLRYRPnlPPVLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSILIDG--VDISKIGLhdlRSRI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 350 GYMSQ---AFSlyaeLSVRQNLvlhaRLFHLPADgipARVGEMLRRFDLEKVADELPNDLPL-----------GIRQRLS 415
Cdd:cd03244 81 SIIPQdpvLFS----GTIRSNL----DPFGEYSD---EELWQALERVGLKEFVESLPGGLDTvveeggenlsvGQRQLLC 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15600424 416 LAVAVIHKPEILILDEPTSGVDPvARDgfwELMVEL--SRRDGVTIFISTHFMNEAQRCDRISLMHAGKVLASDTP 489
Cdd:cd03244 150 LARALLRKSKILVLDEATASVDP-ETD---ALIQKTirEAFKDCTVLTIAHRLDTIIDSDRILVLDKGRVVEFDSP 221
|
|
| SapD |
COG4170 |
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms]; |
285-495 |
1.82e-14 |
|
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms];
Pssm-ID: 443330 [Multi-domain] Cd Length: 331 Bit Score: 75.71 E-value: 1.82e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 285 GDFVAVDHVSFRIERGEIFGFLGSNGCGKSTTMKMLTGLLPASEGTCA--LFGQPVDASDMATRRRVGYMSQAFSLyael 362
Cdd:COG4170 18 GRVKAVDRVSLTLNEGEIRGLVGESGSGKSLIAKAICGITKDNWHVTAdrFRWNGIDLLKLSPRERRKIIGREIAM---- 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 363 sVRQN----LVLHARLFHLPADGIPA----------------RVGEMLRRF---DLEKVADELPNDLPLGIRQRLSLAVA 419
Cdd:COG4170 94 -IFQEpsscLDPSAKIGDQLIEAIPSwtfkgkwwqrfkwrkkRAIELLHRVgikDHKDIMNSYPHELTEGECQKVMIAMA 172
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15600424 420 VIHKPEILILDEPTSGVDPVARDGFWELMVELSRRDGVTI-FISTHFMNEAQRCDRISLMHAGKVLASDTPDELVRQ 495
Cdd:COG4170 173 IANQPRLLIADEPTNAMESTTQAQIFRLLARLNQLQGTSIlLISHDLESISQWADTITVLYCGQTVESGPTEQILKS 249
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
289-486 |
2.07e-14 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 76.69 E-value: 2.07e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 289 AVDHVSFRIERGEIFGFLGSNGCGKSTTMKMLTGLLPASEGTCALFGQPVD--ASDMATRRRVGYMSQAFSLYAELSVRQ 366
Cdd:PRK10982 13 ALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEIDfkSSKEALENGISMVHQELNLVLQRSVMD 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 367 NLVLHarlfHLPADGIPARVGEMLRrfDLEKVADEL-----PND----LPLGIRQRLSLAVAVIHKPEILILDEPTSGVD 437
Cdd:PRK10982 93 NMWLG----RYPTKGMFVDQDKMYR--DTKAIFDELdididPRAkvatLSVSQMQMIEIAKAFSYNAKIVIMDEPTSSLT 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 15600424 438 PVARDGFWELMVELSRRDGVTIFIStHFMNEA-QRCDRISLMHAGKVLAS 486
Cdd:PRK10982 167 EKEVNHLFTIIRKLKERGCGIVYIS-HKMEEIfQLCDEITILRDGQWIAT 215
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
11-238 |
2.49e-14 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 77.07 E-value: 2.49e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 11 LRGVSLRY----GETRAVDDVSLEIPANRMVGLIGPDGVGKSSLLALLAGARKMQDGEIRV-------LDGD----MRdR 75
Cdd:PRK10535 7 LKDIRRSYpsgeEQVEVLKGISLDIYAGEMVAIVGASGSGKSTLMNILGCLDKPTSGTYRVagqdvatLDADalaqLR-R 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 76 RHRRAVCPRIaympqglgkNLYPTLSVFENVDFFGRLFGHDKAERERRIADLLQSTGLAPFAERPAGKLSGGMKQKLGLC 155
Cdd:PRK10535 86 EHFGFIFQRY---------HLLSHLTAAQNVEVPAVYAGLERKQRLLRAQELLQRLGLEDRVEYQPSQLSGGQQQRVSIA 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 156 CALIHDPDLLILDEPTTGVDPLSRNQFWELIGRIRAgrEGMSVLVATAYMEEAERFDWLVAMDDGKVLATGTPQELRERT 235
Cdd:PRK10535 157 RALMNGGQVILADEPTGALDSHSGEEVMAILHQLRD--RGHTVIIVTHDPQVAAQAERVIEIRDGEIVRNPPAQEKVNVA 234
|
...
gi 15600424 236 GTQ 238
Cdd:PRK10535 235 GGT 237
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
14-236 |
2.54e-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: 2.54e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 14 VSLRYGETR-AVDDVSLEIPANRMVGLIGPDGVGKSSLLALLAGARKMQDGEIrVLDGDMRDRRHRRAVCPRIAYMPQGl 92
Cdd:TIGR01193 479 VSYSYGYGSnILSDISLTIKMNSKTTIVGMSGSGKSTLAKLLVGFFQARSGEI-LLNGFSLKDIDRHTLRQFINYLPQE- 556
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 93 gknlyPTL---SVFENVdffgrLFG------HDKAERERRIADLLQ-----STGLAPFAERPAGKLSGGMKQKLGLCCAL 158
Cdd:TIGR01193 557 -----PYIfsgSILENL-----LLGakenvsQDEIWAACEIAEIKDdienmPLGYQTELSEEGSSISGGQKQRIALARAL 626
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15600424 159 IHDPDLLILDEPTTGVDPLSRNQfweLIGRIRAGREGMSVLVATAyMEEAERFDWLVAMDDGKVLATGTPQELRERTG 236
Cdd:TIGR01193 627 LTDSKVLILDESTSNLDTITEKK---IVNNLLNLQDKTIIFVAHR-LSVAKQSDKIIVLDHGKIIEQGSHDELLDRNG 700
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
10-230 |
2.79e-14 |
|
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: 76.71 E-value: 2.79e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 10 SLRGVSLRY-GETRAV-DDVSLEIPANRMVGLIGPDGVGKSSLLALLAGARKMQDGEIRvLDGDMRDRRHRRAVCPRIAY 87
Cdd:COG4618 332 SVENLTVVPpGSKRPIlRGVSFSLEPGEVLGVIGPSGSGKSTLARLLVGVWPPTAGSVR-LDGADLSQWDREELGRHIGY 410
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 88 MPQGLGknLYPTlSVFENVdffGRLfghDKAERERRIA--------DLLQS------TGLAPFAERpagkLSGGMKQKLG 153
Cdd:COG4618 411 LPQDVE--LFDG-TIAENI---ARF---GDADPEKVVAaaklagvhEMILRlpdgydTRIGEGGAR----LSGGQRQRIG 477
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 154 LCCALIHDPDLLILDEPTTGVDPLSRNQFWELIGRIRAgrEGMSVLVAT---AYMEEAerfDWLVAMDDGKVLATGTPQE 230
Cdd:COG4618 478 LARALYGDPRLVVLDEPNSNLDDEGEAALAAAIRALKA--RGATVVVIThrpSLLAAV---DKLLVLRDGRVQAFGPRDE 552
|
|
| nickel_nikD |
TIGR02770 |
nickel import ATP-binding protein NikD; This family represents the NikD subunit of a ... |
23-243 |
3.14e-14 |
|
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: 73.17 E-value: 3.14e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 23 AVDDVSLEIPANRMVGLIGPDGVGKS----SLLALLAGARKMQDGEIRVLDGDMRDRRHR-RAVC-----PRIAYMP-QG 91
Cdd:TIGR02770 1 LVQDLNLSLKRGEVLALVGESGSGKSltclAILGLLPPGLTQTSGEILLDGRPLLPLSIRgRHIAtimqnPRTAFNPlFT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 92 LGKNLYPTLsvfenvdffgRLFGHDKAERERRIADLLQSTGLAPFAE---RPAGKLSGGMKQKLGLCCALIHDPDLLILD 168
Cdd:TIGR02770 81 MGNHAIETL----------RSLGKLSKQARALILEALEAVGLPDPEEvlkKYPFQLSGGMLQRVMIALALLLEPPFLIAD 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15600424 169 EPTTGVDPLSRNQFWELIGRIRAgREGMSVLVATAYMEE-AERFDWLVAMDDGKVLATGTPQELRER---TGTQSLESA 243
Cdd:TIGR02770 151 EPTTDLDVVNQARVLKLLRELRQ-LFGTGILLITHDLGVvARIADEVAVMDDGRIVERGTVKEIFYNpkhETTRKLLSA 228
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
294-498 |
3.22e-14 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 77.07 E-value: 3.22e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 294 SFRIERGEIFGFLGSNGCGKSTTMKMLTGLLPASEGTCALFGQPVDASD-MATRRRVGYMSQAFSLYAElSVRQNLVLHa 372
Cdd:TIGR00958 501 TFTLHPGEVVALVGPSGSGKSTVAALLQNLYQPTGGQVLLDGVPLVQYDhHYLHRQVALVGQEPVLFSG-SVRENIAYG- 578
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 373 rLFHLPADGIPAR---------VGEMLRRFDLEkvADELPNDLPLGIRQRLSLAVAVIHKPEILILDEPTSGVDPVARDG 443
Cdd:TIGR00958 579 -LTDTPDEEIMAAakaanahdfIMEFPNGYDTE--VGEKGSQLSGGQKQRIAIARALVRKPRVLILDEATSALDAECEQL 655
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 15600424 444 FWELMVELSRrdgvTIFISTHFMNEAQRCDRISLMHAGKVLASDTPDELVRQRGL 498
Cdd:TIGR00958 656 LQESRSRASR----TVLLIAHRLSTVERADQILVLKKGSVVEMGTHKQLMEDQGC 706
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
275-464 |
3.43e-14 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 73.22 E-value: 3.43e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 275 IEAEGLTCRFGDFVAVDHVSFRIERGEIFGFLGSNGCGKSTTMKMLTGLLPASEGTCALFGQpvdasdmatrRRVGYMSQ 354
Cdd:PRK09544 5 VSLENVSVSFGQRRVLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIKRNGK----------LRIGYVPQ 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 355 AFSLYAELSVRQNLVLHARLFHLPADGIPArvgemLRRFDLEKVADELPNDLPLGIRQRLSLAVAVIHKPEILILDEPTS 434
Cdd:PRK09544 75 KLYLDTTLPLTVNRFLRLRPGTKKEDILPA-----LKRVQAGHLIDAPMQKLSGGETQRVLLARALLNRPQLLVLDEPTQ 149
|
170 180 190
....*....|....*....|....*....|
gi 15600424 435 GVDPVARDGFWELMVELSRRDGVTIFISTH 464
Cdd:PRK09544 150 GVDVNGQVALYDLIDQLRRELDCAVLMVSH 179
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
28-231 |
4.08e-14 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 72.69 E-value: 4.08e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 28 SLEIPANRMVGLIGPDGVGKSSLLALLAGARKMQDGEIRVLDGDmrdrrHRRAVCPR--IAYMPQGlgKNLYPTLSVFEN 105
Cdd:PRK10771 19 DLTVERGERVAILGPSGAGKSTLLNLIAGFLTPASGSLTLNGQD-----HTTTPPSRrpVSMLFQE--NNLFSHLTVAQN 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 106 VDFfG-----RLfghdKAERERRIADLLQSTGLAPFAERPAGKLSGGMKQKLGLCCALIHDPDLLILDEPTTGVDPLSRN 180
Cdd:PRK10771 92 IGL-GlnpglKL----NAAQREKLHAIARQMGIEDLLARLPGQLSGGQRQRVALARCLVREQPILLLDEPFSALDPALRQ 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 15600424 181 QFWELIGRIRAGREgMSVLVATAYMEEAERF-DWLVAMDDGKVLATGTPQEL 231
Cdd:PRK10771 167 EMLTLVSQVCQERQ-LTLLMVSHSLEDAARIaPRSLVVADGRIAWDGPTDEL 217
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
274-484 |
5.13e-14 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 72.86 E-value: 5.13e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 274 AIEAEGLTCRFGDFVAVDHVSFRIERGEIFGFLGSNGCGKSTTMKMLTGLLPASEGTCALFGQPVDASD---------MA 344
Cdd:PRK11264 3 AIEVKNLVKKFHGQTVLHGIDLEVKPGEVVAIIGPSGSGKTTLLRCINLLEQPEAGTIRVGDITIDTARslsqqkgliRQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 345 TRRRVGYMSQAFSLYAELSVRQNLVLHARLFH-LPADGIPARVGEMLRRFDLEKVADELPNDLPLGIRQRLSLAVAVIHK 423
Cdd:PRK11264 83 LRQHVGFVFQNFNLFPHRTVLENIIEGPVIVKgEPKEEATARARELLAKVGLAGKETSYPRRLSGGQQQRVAIARALAMR 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15600424 424 PEILILDEPTSGVDPvardgfwELMVEL---------SRRdgvTIFISTHFMNEAQR-CDRISLMHAGKVL 484
Cdd:PRK11264 163 PEVILFDEPTSALDP-------ELVGEVlntirqlaqEKR---TMVIVTHEMSFARDvADRAIFMDQGRIV 223
|
|
| NosY |
COG1277 |
ABC-type transport system involved in multi-copper enzyme maturation, permease component ... |
726-841 |
6.10e-14 |
|
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: 71.38 E-value: 6.10e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 726 VIPLLLIMIPAMLTALGVVREKELGSITNLYVTPVTRLEFLVGKQLPYVAMGMINFLLMLVLAIVVFRVPLK------GS 799
Cdd:COG1277 56 LLSLLLPLLAPALGMDAISGERESGTLELLLTLPISRWEIVLGKFLGALLVLLLALLITFLLALLLGLLLFGspppdlGA 135
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 15600424 800 FLALTIGAFLYVVTSTGLGLFLSTFMRSQIAAvFGVAIATMI 841
Cdd:COG1277 136 ILGFYLGLLLLGLAFLAIGLFISALTRNQIVA-AILAIALWL 176
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
16-483 |
9.02e-14 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 75.21 E-value: 9.02e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 16 LRYGETRAVDDVSLEIPANRMVGLIGPDGVGKSSLLALLAGARKMQDGEIR------------------------VLDGD 71
Cdd:PRK10636 9 IRRGVRVLLDNATATINPGQKVGLVGKNGCGKSTLLALLKNEISADGGSYTfpgnwqlawvnqetpalpqpaleyVIDGD 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 72 mrdrRHRRAVCPRIAYMPQGLGKNLYPTLSvfenvdffGRLFGHDKAERERRIADLLQSTGLA-PFAERPAGKLSGGMKQ 150
Cdd:PRK10636 89 ----REYRQLEAQLHDANERNDGHAIATIH--------GKLDAIDAWTIRSRAASLLHGLGFSnEQLERPVSDFSGGWRM 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 151 KLGLCCALIHDPDLLILDEPTTGVDpLSRNQFWEligRIRAGREGMSVLVAtaymeeAERfDWLVAMDDgKVLATgTPQE 230
Cdd:PRK10636 157 RLNLAQALICRSDLLLLDEPTNHLD-LDAVIWLE---KWLKSYQGTLILIS------HDR-DFLDPIVD-KIIHI-EQQS 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 231 LRERTGT-----------------------------QSLESAFIALLPESKRAGHH-------RLVIPPR---P------ 265
Cdd:PRK10636 224 LFEYTGNyssfevqratrlaqqqamyesqqervahlQSYIDRFRAKATKAKQAQSRikmlermELIAPAHvdnPfhfsfr 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 266 QSEGAPRIAIEAEGLTCRFGDFVAVDHVSFRIERGEIFGFLGSNGCGKSTTMKMLTGLLPASEGTCALfgqpvdasdmAT 345
Cdd:PRK10636 304 APESLPNPLLKMEKVSAGYGDRIILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELAPVSGEIGL----------AK 373
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 346 RRRVGYMSQ---AFsLYAELSVRQNLvlhARLfhlpadgIPARVGEMLRR------FDLEKVADElPNDLPLGIRQRLSL 416
Cdd:PRK10636 374 GIKLGYFAQhqlEF-LRADESPLQHL---ARL-------APQELEQKLRDylggfgFQGDKVTEE-TRRFSGGEKARLVL 441
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15600424 417 AVAVIHKPEILILDEPTSGVDPVARDGFWELMVELsrrDGVTIFIS--THFMNEAQrcDRISLMHAGKV 483
Cdd:PRK10636 442 ALIVWQRPNLLLLDEPTNHLDLDMRQALTEALIDF---EGALVVVShdRHLLRSTT--DDLYLVHDGKV 505
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
20-230 |
9.56e-14 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 73.20 E-value: 9.56e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 20 ETRAVDDVSLEIPANRMVGLIGPDGVGKSSLL----ALL---AGA-----------RKMQDGEIRVLDGDMRDRRHRR-- 79
Cdd:PRK13651 19 ELKALDNVSVEINQGEFIAIIGQTGSGKTTFIehlnALLlpdTGTiewifkdeknkKKTKEKEKVLEKLVIQKTRFKKik 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 80 ---AVCPRIAYMPQGLGKNLYPTlSVFENVDFFGRLFGHDKAERERRIADLLQSTGL-APFAERPAGKLSGGMKQKLGLC 155
Cdd:PRK13651 99 kikEIRRRVGVVFQFAEYQLFEQ-TIEKDIIFGPVSMGVSKEEAKKRAAKYIELVGLdESYLQRSPFELSGGQKRRVALA 177
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15600424 156 CALIHDPDLLILDEPTTGVDPLSRNQFWELIGRIRagREGMSVLVATAYMEEA-ERFDWLVAMDDGKVLATGTPQE 230
Cdd:PRK13651 178 GILAMEPDFLVFDEPTAGLDPQGVKEILEIFDNLN--KQGKTIILVTHDLDNVlEWTKRTIFFKDGKIIKDGDTYD 251
|
|
| ABC2_membrane_2 |
pfam12679 |
ABC-2 family transporter protein; This family is related to the ABC-2 membrane transporter ... |
729-915 |
1.31e-13 |
|
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: 72.43 E-value: 1.31e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 729 LLLIMIPAMLTALGVVREKELGSITNLYVTPVTRLEFLVGKQLPYVAMGMINFLLMLVLAIVVFRVPLKGS--------- 799
Cdd:pfam12679 76 FLIPVIAALLGADAIAGERERGTIELLLSLPVSRSEILLGKFIGRLAIGLILAVALLAGVLLALAITLALGdpldlgdll 155
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 800 FLALTIGAFLYVVTSTGLGLFLSTFMRSQ---IAAVFGVAIATMIPAIQFSGLIHPVSSLEGAAAWIGKLY----PTSHF 872
Cdd:pfam12679 156 LLVAASVLLALALVFLSIGLLLSSVARSTrtaAAIALGLFFVLAILWPIVLYGLAELLAGPAPPQELLDFLlflnPTSPY 235
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 15600424 873 LVVSRGAFSKSLGLSDL--WAYYLPLAASIVVLTLLSVACLKKQE 915
Cdd:pfam12679 236 NTLLSTILAGSDLSLYGstATNLLILLAWIAVPLALAYVLFKRKD 280
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
285-506 |
1.35e-13 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 73.34 E-value: 1.35e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 285 GDFVAVDHVSFRIERGEIFGFLGSNGCGKSTTMKMLTGLLPASEGTCALFGQPVDasDMATRRRVGYMS-QAFSLYAELS 363
Cdd:PRK11650 15 GKTQVIKGIDLDVADGEFIVLVGPSGCGKSTLLRMVAGLERITSGEIWIGGRVVN--ELEPADRDIAMVfQNYALYPHMS 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 364 VRQNLVLHARLFHLPADGIPARVGEMLRRFDLEKVADELPNDLPLGIRQRLSLAVAVIHKPEILILDEPTSGVDpvARdg 443
Cdd:PRK11650 93 VRENMAYGLKIRGMPKAEIEERVAEAARILELEPLLDRKPRELSGGQRQRVAMGRAIVREPAVFLFDEPLSNLD--AK-- 168
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15600424 444 fweLMV-------ELSRRDGVTIFISTHFMNEAQR-CDRISLMHAGKVLASDTPDElVRQRGLPTLEATFI 506
Cdd:PRK11650 169 ---LRVqmrleiqRLHRRLKTTSLYVTHDQVEAMTlADRVVVMNGGVAEQIGTPVE-VYEKPASTFVASFI 235
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
19-237 |
1.37e-13 |
|
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: 75.37 E-value: 1.37e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 19 GETRAVDDVSLEIPANRMVGLIGPDGVGKSSLLALLAGARKMQDGEIrvldgdmrdrrhrrAVCPRIAYMPQglgKNLYP 98
Cdd:TIGR00957 649 DLPPTLNGITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEGHV--------------HMKGSVAYVPQ---QAWIQ 711
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 99 TLSVFENVdffgrLFGHdkAERERRIADLLQSTGLAPFAE-RPAG----------KLSGGMKQKLGLCCALIHDPDLLIL 167
Cdd:TIGR00957 712 NDSLRENI-----LFGK--ALNEKYYQQVLEACALLPDLEiLPSGdrteigekgvNLSGGQKQRVSLARAVYSNADIYLF 784
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15600424 168 DEPTTGVDP-LSRNQFWELIGRIRAGREGMSVLVaTAYMEEAERFDWLVAMDDGKVLATGTPQELRERTGT 237
Cdd:TIGR00957 785 DDPLSAVDAhVGKHIFEHVIGPEGVLKNKTRILV-THGISYLPQVDVIIVMSGGKISEMGSYQELLQRDGA 854
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
6-236 |
1.98e-13 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 74.23 E-value: 1.98e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 6 SGVASLRGVSLRYGETR-AVDDVSLEIPANRMVGLIGPDGVGKSSLLALLAGARKMQDGEIRVlDG-DMRD---RRHRRA 80
Cdd:PRK13657 332 KGAVEFDDVSFSYDNSRqGVEDVSFEAKPGQTVAIVGPTGAGKSTLINLLQRVFDPQSGRILI-DGtDIRTvtrASLRRN 410
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 81 vcprIAYMPQGLGknLYpTLSVFENVdffgRLFGHDKAERERRIA-------DLL--QSTGLAPFAERPAGKLSGGMKQK 151
Cdd:PRK13657 411 ----IAVVFQDAG--LF-NRSIEDNI----RVGRPDATDEEMRAAaeraqahDFIerKPDGYDTVVGERGRQLSGGERQR 479
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 152 LGLCCALIHDPDLLILDEPTTGVDPLSRNQFWELIGRIRAGREGMSVLVATAYMEEAERfdwLVAMDDGKVLATGTPQEL 231
Cdd:PRK13657 480 LAIARALLKDPPILILDEATSALDVETEAKVKAALDELMKGRTTFIIAHRLSTVRNADR---ILVFDNGRVVESGSFDEL 556
|
....*
gi 15600424 232 RERTG 236
Cdd:PRK13657 557 VARGG 561
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
23-191 |
2.29e-13 |
|
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: 70.54 E-value: 2.29e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 23 AVDDVSLEIPANRMVGLIGPDGVGKSSLLALLAGARKMQDGEIRVLDGD-------------MRDRRHR--------RAV 81
Cdd:COG4778 26 VLDGVSFSVAAGECVALTGPSGAGKSTLLKCIYGNYLPDSGSILVRHDGgwvdlaqaspreiLALRRRTigyvsqflRVI 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 82 cPRIaympqglgknlyPTLSVFENVdffGRLFGHDKAERERRIADLLQSTGLApfaER----PAGKLSGGMKQKLGLCCA 157
Cdd:COG4778 106 -PRV------------SALDVVAEP---LLERGVDREEARARARELLARLNLP---ERlwdlPPATFSGGEQQRVNIARG 166
|
170 180 190
....*....|....*....|....*....|....
gi 15600424 158 LIHDPDLLILDEPTTGVDPLSRNQFWELIGRIRA 191
Cdd:COG4778 167 FIADPPLLLLDEPTASLDAANRAVVVELIEEAKA 200
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
27-255 |
3.16e-13 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 73.02 E-value: 3.16e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 27 VSLEIPANRMVGLIGPDGVGKSSLLALLAGARKMQDGEIRvLDGDMRD-RRHRRAVCPRIAYMPQGLGKN-LYPTLSVFE 104
Cdd:PRK11288 272 ISFSVRAGEIVGLFGLVGAGRSELMKLLYGATRRTAGQVY-LDGKPIDiRSPRDAIRAGIMLCPEDRKAEgIIPVHSVAD 350
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 105 NVDF-------FGRLFGHDKAERE---RRIADLLQSTglaPFAERPAGKLSGGMKQKLGLCCALIHDPDLLILDEPTTGV 174
Cdd:PRK11288 351 NINIsarrhhlRAGCLINNRWEAEnadRFIRSLNIKT---PSREQLIMNLSGGNQQKAILGRWLSEDMKVILLDEPTRGI 427
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 175 DPLSRNQFWELIGRIRAGreGMSVLVATAYMEE----AERfdwLVAMDDGKVLAtgtpqelrERTGTQSLESAFIAL-LP 249
Cdd:PRK11288 428 DVGAKHEIYNVIYELAAQ--GVAVLFVSSDLPEvlgvADR---IVVMREGRIAG--------ELAREQATERQALSLaLP 494
|
....*.
gi 15600424 250 ESKRAG 255
Cdd:PRK11288 495 RTSAAV 500
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
19-199 |
3.29e-13 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 69.45 E-value: 3.29e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 19 GETRAVDDVSLEIPANRMVGLIGPDGVGKSSLLALLAGARKMQDGEIRVLDGDMRDRRH--RRAVCpriaYMPQGLGknL 96
Cdd:PRK13538 12 DERILFSGLSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVLWQGEPIRRQRDeyHQDLL----YLGHQPG--I 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 97 YPTLSVFENVDFFGRLfgHDKAERERrIADLLQSTGLAPFAERPAGKLSGGMKQKLGLCCALIHDPDLLILDEPTTGVDP 176
Cdd:PRK13538 86 KTELTALENLRFYQRL--HGPGDDEA-LWEALAQVGLAGFEDVPVRQLSAGQQRRVALARLWLTRAPLWILDEPFTAIDK 162
|
170 180
....*....|....*....|...
gi 15600424 177 LSRNQFWELIGRiRAGREGMSVL 199
Cdd:PRK13538 163 QGVARLEALLAQ-HAEQGGMVIL 184
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
289-485 |
3.62e-13 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 73.11 E-value: 3.62e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 289 AVDHVSFRIERGEIFGFLGSNGCGKSTTMKMLTGLLPASEGTCALFGQPVD-----ASDMATrrrVGYMSQAFSLYAELS 363
Cdd:PRK10762 19 ALSGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSILYLGKEVTfngpkSSQEAG---IGIIHQELNLIPQLT 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 364 VRQNLVLhARLFHLPADGIP-----ARVGEMLRRFDLEKVADELPNDLPLGIRQRLSLAVAVIHKPEILILDEPTSGVDP 438
Cdd:PRK10762 96 IAENIFL-GREFVNRFGRIDwkkmyAEADKLLARLNLRFSSDKLVGELSIGEQQMVEIAKVLSFESKVIIMDEPTDALTD 174
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 15600424 439 VARDGFWELMVELsRRDGVTIFISTHFMNEA-QRCDRISLMHAGKVLA 485
Cdd:PRK10762 175 TETESLFRVIREL-KSQGRGIVYISHRLKEIfEICDDVTVFRDGQFIA 221
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
285-484 |
3.67e-13 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 71.68 E-value: 3.67e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 285 GDFVAVDHVSFRIERGEIFGFLGSNGCGKSTTMKMLTGLLPAS---EGTCALFGQPV-DASDMATRR-RVGYMSQAF--- 356
Cdd:PRK09473 27 GDVTAVNDLNFSLRAGETLGIVGESGSGKSQTAFALMGLLAANgriGGSATFNGREIlNLPEKELNKlRAEQISMIFqdp 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 357 --SLYAELSVRQNLV----LHARLFHLPAdgiparVGEMLRRFDLEKVADE------LPNDLPLGIRQRLSLAVAVIHKP 424
Cdd:PRK09473 107 mtSLNPYMRVGEQLMevlmLHKGMSKAEA------FEESVRMLDAVKMPEArkrmkmYPHEFSGGMRQRVMIAMALLCRP 180
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15600424 425 EILILDEPTSGVDPVARDGFWELMVELSRRDGVTIFISTHFMN-EAQRCDRISLMHAGKVL 484
Cdd:PRK09473 181 KLLIADEPTTALDVTVQAQIMTLLNELKREFNTAIIMITHDLGvVAGICDKVLVMYAGRTM 241
|
|
| ABC2_membrane |
pfam01061 |
ABC-2 type transporter; |
729-879 |
3.77e-13 |
|
ABC-2 type transporter;
Pssm-ID: 426023 [Multi-domain] Cd Length: 204 Bit Score: 69.22 E-value: 3.77e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 729 LLLIMIPAMLTALGVVREKELGSITNLYVTPV-TRLEFLVGKQLPYVAMGMINFLLMLVLAIVVFRVPL-KGSFLALTIG 806
Cdd:pfam01061 53 SILFNAFSALSGISPVFEKERGVLYRELASPLySPSAYVLAKILSELPLSLLQSLIFLLIVYFMVGLPPsAGRFFLFLLV 132
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15600424 807 AFLYVVTSTGLGLFLSTFMRSQIAAVFgVAIATMIPAIQFSGLIHPVSSLEGAAAWIGKLYPTSHFLVVSRGA 879
Cdd:pfam01061 133 LLLTALAASSLGLFISALAPSFEDASQ-LGPLVLLPLLLLSGFFIPIDSMPVWWQWIYYLNPLTYAIEALRAN 204
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
289-497 |
4.69e-13 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 73.07 E-value: 4.69e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 289 AVDHVSFRIERGEIFGFLGSNGCGKSTTMKMLTGLLPASEGTCALFGqpVDASDM---ATRRRVGYMSQAFSLYAElSVR 365
Cdd:PRK13657 350 GVEDVSFEAKPGQTVAIVGPTGAGKSTLINLLQRVFDPQSGRILIDG--TDIRTVtraSLRRNIAVVFQDAGLFNR-SIE 426
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 366 QNLVL------HARLfhLPADGIPARVGEMLRRFD-LEKVADELPNDLPLGIRQRLSLAVAVIHKPEILILDEPTSGVDP 438
Cdd:PRK13657 427 DNIRVgrpdatDEEM--RAAAERAQAHDFIERKPDgYDTVVGERGRQLSGGERQRLAIARALLKDPPILILDEATSALDV 504
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 15600424 439 VARDGFWELMVELSRrdGVTIFISTHFMNEAQRCDRISLMHAGKVLASDTPDELVRQRG 497
Cdd:PRK13657 505 ETEAKVKAALDELMK--GRTTFIIAHRLSTVRNADRILVFDNGRVVESGSFDELVARGG 561
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
10-236 |
5.71e-13 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 72.70 E-value: 5.71e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 10 SLRGVSLRYGETR-AVDDVSLEIPANRMVGLIGPDGVGKSSLLALLAGARKMQDGEIRVlDGDMRDRRHRRAvcpriaym 88
Cdd:PRK10522 324 ELRNVTFAYQDNGfSVGPINLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILL-DGKPVTAEQPED-------- 394
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 89 pqglgknlYPTL--SVFENVDFFGRLFGHDKAERERRIADL-LQSTGLAPFAERPAG-----KLSGGMKQKLGLCCALIH 160
Cdd:PRK10522 395 --------YRKLfsAVFTDFHLFDQLLGPEGKPANPALVEKwLERLKMAHKLELEDGrisnlKLSKGQKKRLALLLALAE 466
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 161 DPDLLILDEPTTGVDPLSRNQFW-ELIGRIRAgrEGMSVLVAT---AYMEEAERfdwLVAMDDGkvlatgtpqELRERTG 236
Cdd:PRK10522 467 ERDILLLDEWAADQDPHFRREFYqVLLPLLQE--MGKTIFAIShddHYFIHADR---LLEMRNG---------QLSELTG 532
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
27-175 |
6.91e-13 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 69.04 E-value: 6.91e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 27 VSLEIPANRMVGLIGPDGVGKSSLLALLAGARKMQDGEIRVLDGDMR--DRRHRRAVCPR-IAYMPQGLgkNLYPTLSVF 103
Cdd:PRK10584 29 VELVVKRGETIALIGESGSGKSTLLAILAGLDDGSSGEVSLVGQPLHqmDEEARAKLRAKhVGFVFQSF--MLIPTLNAL 106
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15600424 104 ENVDFFGRLFGHDKAERERRIADLLQSTGLAPFAERPAGKLSGGMKQKLGLCCALIHDPDLLILDEPTTGVD 175
Cdd:PRK10584 107 ENVELPALLRGESSRQSRNGAKALLEQLGLGKRLDHLPAQLSGGEQQRVALARAFNGRPDVLFADEPTGNLD 178
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
27-244 |
9.60e-13 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 69.19 E-value: 9.60e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 27 VSLEIPANRMVGLIGPDGVGKSSLLALLAGArKMQDGEIRVLDGDMRDRRHRRAVCPRiAYMPQglGKNLYPTLSVFENV 106
Cdd:PRK03695 15 LSAEVRAGEILHLVGPNGAGKSTLLARMAGL-LPGSGSIQFAGQPLEAWSAAELARHR-AYLSQ--QQTPPFAMPVFQYL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 107 DffgrLFGHDKA---ERERRIADLLQSTGLAPFAERPAGKLSGGMKQKLGLCCALIH-DPD------LLILDEPTTGVDP 176
Cdd:PRK03695 91 T----LHQPDKTrteAVASALNEVAEALGLDDKLGRSVNQLSGGEWQRVRLAAVVLQvWPDinpagqLLLLDEPMNSLDV 166
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15600424 177 LSRNQFWELIGRIraGREGMSVLVAT----AYMEEAERFdWLVAmdDGKVLATGTPQE-LRERTGTQSLESAF 244
Cdd:PRK03695 167 AQQAALDRLLSEL--CQQGIAVVMSShdlnHTLRHADRV-WLLK--QGKLLASGRRDEvLTPENLAQVFGVNF 234
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
273-498 |
1.14e-12 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 71.80 E-value: 1.14e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 273 IAIEAEGLT-CRFGDFVAVDHVSFRIERGEIFGFLGSNGCGKSTTMKMLTGLLPaSEGTCALFGQPVDASDMAT-RRRVG 350
Cdd:PRK11174 348 VTIEAEDLEiLSPDGKTLAGPLNFTLPAGQRIALVGPSGAGKTSLLNALLGFLP-YQGSLKINGIELRELDPESwRKHLS 426
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 351 YMSQAFSLYAElSVRQNLVLHArlfhlpADGIPARVGEMLRRFDLEKVADELPN--DLPLGIR---------QRLSLAVA 419
Cdd:PRK11174 427 WVGQNPQLPHG-TLRDNVLLGN------PDASDEQLQQALENAWVSEFLPLLPQglDTPIGDQaaglsvgqaQRLALARA 499
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15600424 420 VIHKPEILILDEPTSGVDPVARDGFWELMVELSRrdGVTIFISTHFMNEAQRCDRISLMHAGKVLASDTPDELVRQRGL 498
Cdd:PRK11174 500 LLQPCQLLLLDEPTASLDAHSEQLVMQALNAASR--RQTTLMVTHQLEDLAQWDQIWVMQDGQIVQQGDYAELSQAGGL 576
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
278-494 |
1.59e-12 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 69.77 E-value: 1.59e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 278 EGLTCRFGD----FVAVDHVSFRIERGEIFGFLGSNGCGKSTTMKMLTGLL--PASEGTCALFGQPVDASDMATRRR--- 348
Cdd:PRK11022 7 DKLSVHFGDesapFRAVDRISYSVKQGEVVGIVGESGSGKSVSSLAIMGLIdyPGRVMAEKLEFNGQDLQRISEKERrnl 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 349 ----VGYMSQ------------AFSLYAELSVRQ---NLVLHARLFHLPAD-GIParvgemlrrfDLEKVADELPNDLPL 408
Cdd:PRK11022 87 vgaeVAMIFQdpmtslnpcytvGFQIMEAIKVHQggnKKTRRQRAIDLLNQvGIP----------DPASRLDVYPHQLSG 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 409 GIRQRLSLAVAVIHKPEILILDEPTSGVDPVARDGFWELMVELSRRDGVTIFISTHFMN-EAQRCDRISLMHAGKVLASD 487
Cdd:PRK11022 157 GMSQRVMIAMAIACRPKLLIADEPTTALDVTIQAQIIELLLELQQKENMALVLITHDLAlVAEAAHKIIVMYAGQVVETG 236
|
....*..
gi 15600424 488 TPDELVR 494
Cdd:PRK11022 237 KAHDIFR 243
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
5-175 |
1.62e-12 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 71.29 E-value: 1.62e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 5 GSGVASLRGVSLRYGETRAV-DDVSLEIPANRMVGLIGPDGVGKSSLLALLAGARKMQDGEIRvLDGDMRDRRHRRAVCP 83
Cdd:PRK10790 337 QSGRIDIDNVSFAYRDDNLVlQNINLSVPSRGFVALVGHTGSGKSTLASLLMGYYPLTEGEIR-LDGRPLSSLSHSVLRQ 415
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 84 RIAYMPQGlgknlyPTL---SVFENVDfFGRLFGhdkaerERRIADLLQSTGLAPFAER-PAG----------KLSGGMK 149
Cdd:PRK10790 416 GVAMVQQD------PVVladTFLANVT-LGRDIS------EEQVWQALETVQLAELARSlPDGlytplgeqgnNLSVGQK 482
|
170 180
....*....|....*....|....*.
gi 15600424 150 QKLGLCCALIHDPDLLILDEPTTGVD 175
Cdd:PRK10790 483 QLLALARVLVQTPQILILDEATANID 508
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
264-497 |
1.69e-12 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 71.93 E-value: 1.69e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 264 RPQSEGAPRIAIEAEGLTCRF-GDFVAVDH-VSFRIERGEIFGFLGSNGCGKSTTMKMLTGLLPASEGTCALFGQPVDAS 341
Cdd:PLN03232 1224 RPVSGWPSRGSIKFEDVHLRYrPGLPPVLHgLSFFVSPSEKVGVVGRTGAGKSSMLNALFRIVELEKGRIMIDDCDVAKF 1303
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 342 DMATRRRV-GYMSQAFSLYAElSVRQNLVLHARlfHLPADGIPA----RVGEMLRR--FDLEKVADELPNDLPLGIRQRL 414
Cdd:PLN03232 1304 GLTDLRRVlSIIPQSPVLFSG-TVRFNIDPFSE--HNDADLWEAleraHIKDVIDRnpFGLDAEVSEGGENFSVGQRQLL 1380
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 415 SLAVAVIHKPEILILDEPTSGVDpVARDGFWELMVELSRRDgVTIFISTHFMNEAQRCDRISLMHAGKVLASDTPDELVR 494
Cdd:PLN03232 1381 SLARALLRRSKILVLDEATASVD-VRTDSLIQRTIREEFKS-CTMLVIAHRLNTIIDCDKILVLSSGQVLEYDSPQELLS 1458
|
...
gi 15600424 495 QRG 497
Cdd:PLN03232 1459 RDT 1461
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
8-210 |
2.85e-12 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 67.88 E-value: 2.85e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 8 VASLRGVSLRYGETRAVDDVSLEIPANRMVGLIGPDGVGKSSLLALLagaRKMQDGEIRV-LDGDMRDRRHRrAVCPR-- 84
Cdd:PRK14239 5 ILQVSDLSVYYNKKKALNSVSLDFYPNEITALIGPSGSGKSTLLRSI---NRMNDLNPEVtITGSIVYNGHN-IYSPRtd 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 85 -------IAYMPQGlgKNLYPtLSVFENVDFFGRLFG-HDKA------ERERRIA-------DLLQSTGLApfaerpagk 143
Cdd:PRK14239 81 tvdlrkeIGMVFQQ--PNPFP-MSIYENVVYGLRLKGiKDKQvldeavEKSLKGAsiwdevkDRLHDSALG--------- 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15600424 144 LSGGMKQKLGLCCALIHDPDLLILDEPTTGVDPLSRNQFWELIGRIragREGMSVLVATAYMEEAER 210
Cdd:PRK14239 149 LSGGQQQRVCIARVLATSPKIILLDEPTSALDPISAGKIEETLLGL---KDDYTMLLVTRSMQQASR 212
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
10-186 |
2.93e-12 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 70.22 E-value: 2.93e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 10 SLRGVSLRYGETRA-VDDVSLEIPANRMVGLIGPDGVGKSSLLALLAGARKMQDGEIRVLDGDmrdrrhRRAVCPRIAYM 88
Cdd:COG4178 364 ALEDLTLRTPDGRPlLEDLSLSLKPGERLLITGPSGSGKSTLLRAIAGLWPYGSGRIARPAGA------RVLFLPQRPYL 437
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 89 PQG-----LgknLYPtlsvfenvdffgrlfGHDKAERERRIADLLQSTGLAPFAERP------AGKLSGGMKQKLGLCCA 157
Cdd:COG4178 438 PLGtlreaL---LYP---------------ATAEAFSDAELREALEAVGLGHLAERLdeeadwDQVLSLGEQQRLAFARL 499
|
170 180
....*....|....*....|....*....
gi 15600424 158 LIHDPDLLILDEPTTGVDPLSRNQFWELI 186
Cdd:COG4178 500 LLHKPDWLFLDEATSALDEENEAALYQLL 528
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
290-492 |
3.68e-12 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 69.73 E-value: 3.68e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 290 VDHVSFRIERGEIFGFLGSNGCGKSTTMKMLTGLLPAS-----EGTCALFGQPVDASDMATRRRV--GYMSQAF-----S 357
Cdd:PRK15134 25 VNDVSLQIEAGETLALVGESGSGKSVTALSILRLLPSPpvvypSGDIRFHGESLLHASEQTLRGVrgNKIAMIFqepmvS 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 358 LYAELSVRQNL--VLharLFHLPADGIPARvGEMLR---RFDLEKVADEL---PNDLPLGIRQRLSLAVAVIHKPEILIL 429
Cdd:PRK15134 105 LNPLHTLEKQLyeVL---SLHRGMRREAAR-GEILNcldRVGIRQAAKRLtdyPHQLSGGERQRVMIAMALLTRPELLIA 180
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15600424 430 DEPTSGVDPVARDGFWELMVELSRRDGVTIFISTHFMNEAQR-CDRISLMHAGKVLASDTPDEL 492
Cdd:PRK15134 181 DEPTTALDVSVQAQILQLLRELQQELNMGLLFITHNLSIVRKlADRVAVMQNGRCVEQNRAATL 244
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
287-484 |
3.82e-12 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 68.19 E-value: 3.82e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 287 FVAVDHVSFRIERGEIFGFLGSNGCGKSTTMKMLTGLLPASEGTCALF-------GQPVDASDMAT-------------- 345
Cdd:PRK13651 20 LKALDNVSVEINQGEFIAIIGQTGSGKTTFIEHLNALLLPDTGTIEWIfkdeknkKKTKEKEKVLEklviqktrfkkikk 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 346 ----RRRVGYMSQaFSLYA--ELSVRQNLVLHARLFHLPADGIPARVGEMLRRFDL-EKVADELPNDLPLGIRQRLSLAV 418
Cdd:PRK13651 100 ikeiRRRVGVVFQ-FAEYQlfEQTIEKDIIFGPVSMGVSKEEAKKRAAKYIELVGLdESYLQRSPFELSGGQKRRVALAG 178
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15600424 419 AVIHKPEILILDEPTSGVDPVARDGFWELMVELSrRDGVTIFISTHFMNEA-QRCDRISLMHAGKVL 484
Cdd:PRK13651 179 ILAMEPDFLVFDEPTAGLDPQGVKEILEIFDNLN-KQGKTIILVTHDLDNVlEWTKRTIFFKDGKII 244
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
11-483 |
5.15e-12 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 69.43 E-value: 5.15e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 11 LRGVSLRYGETRAVDDVSLEIPANRMVGLIGPDGVGKSSLLALLAG--ARKMQDGEIrVLDG------DMRDRRHRravc 82
Cdd:NF040905 4 MRGITKTFPGVKALDDVNLSVREGEIHALCGENGAGKSTLMKVLSGvyPHGSYEGEI-LFDGevcrfkDIRDSEAL---- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 83 pRIAYMPQGLGknLYPTLSVFENVdFFGRLFGH----DKAERERRIADLLQSTGLAPFAERPAGKLSGGMKQKLGLCCAL 158
Cdd:NF040905 79 -GIVIIHQELA--LIPYLSIAENI-FLGNERAKrgviDWNETNRRARELLAKVGLDESPDTLVTDIGVGKQQLVEIAKAL 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 159 IHDPDLLILDEPTTGV-DPLSRNqFWELIGRIRAgrEGMSVLVATAYMEEAERF-DWLVAMDDGKVLATgtpqeLRERTG 236
Cdd:NF040905 155 SKDVKLLILDEPTAALnEEDSAA-LLDLLLELKA--QGITSIIISHKLNEIRRVaDSITVLRDGRTIET-----LDCRAD 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 237 TQSlESAFIALLpeSKRAGHHRLviPPRpqsegAPRI---AIEAEGLTCR---FGDFVAVDHVSFRIERGEIFGFLGSNG 310
Cdd:NF040905 227 EVT-EDRIIRGM--VGRDLEDRY--PER-----TPKIgevVFEVKNWTVYhplHPERKVVDDVSLNVRRGEIVGIAGLMG 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 311 CGKsTTMKMltGLLPAS-----EGTCALFGQPVDASDM--ATRRRVGYMSQ---AFSLYAELSVRQNLVLhARLFHLPAD 380
Cdd:NF040905 297 AGR-TELAM--SVFGRSygrniSGTVFKDGKEVDVSTVsdAIDAGLAYVTEdrkGYGLNLIDDIKRNITL-ANLGKVSRR 372
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 381 GIPARVGEMlrrfdleKVADELPNDLPL---GIRQ---RLS--------LAVAVIHKPEILILDEPTSGVDPVARDGFWE 446
Cdd:NF040905 373 GVIDENEEI-------KVAEEYRKKMNIktpSVFQkvgNLSggnqqkvvLSKWLFTDPDVLILDEPTRGIDVGAKYEIYT 445
|
490 500 510
....*....|....*....|....*....|....*...
gi 15600424 447 LMVELSRRDGVTIFISTHfMNEA-QRCDRISLMHAGKV 483
Cdd:NF040905 446 IINELAAEGKGVIVISSE-LPELlGMCDRIYVMNEGRI 482
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
263-462 |
6.82e-12 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 69.07 E-value: 6.82e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 263 PRPQSEGAPRI------AIEAEGLTCRFGDF-VAVDHVSFRIERGEifGFL--GSNGCGKSTTMKMLTGLLPASEGTCAL 333
Cdd:COG4178 345 ADALPEAASRIetsedgALALEDLTLRTPDGrPLLEDLSLSLKPGE--RLLitGPSGSGKSTLLRAIAGLWPYGSGRIAR 422
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 334 fgqPVDASDMatrrrvgYMSQafSLYAEL-SVRQNLvlharLFHLPADGIP-ARVGEMLRRFDLEKVADEL------PND 405
Cdd:COG4178 423 ---PAGARVL-------FLPQ--RPYLPLgTLREAL-----LYPATAEAFSdAELREALEAVGLGHLAERLdeeadwDQV 485
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 15600424 406 LPLGIRQRLSLAVAVIHKPEILILDEPTSGVDPVARDGFWELMVElsRRDGVTIfIS 462
Cdd:COG4178 486 LSLGEQQRLAFARLLLHKPDWLFLDEATSALDEENEAALYQLLRE--ELPGTTV-IS 539
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
10-233 |
7.20e-12 |
|
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: 65.24 E-value: 7.20e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 10 SLRGVSLRYGETRAVDDVSLEIPANRMVGLIGPDGVGKSSLLALLAG--ARKMQDGEIRvLDG----DMR-DRRHRRavc 82
Cdd:cd03217 2 EIKDLHVSVGGKEILKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMGhpKYEVTEGEIL-FKGeditDLPpEERARL--- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 83 priaympqGLgknlypTLSVFENVDFFGRlfghdkaererRIADLLQSTGLapfaerpagKLSGGMKQKLGLCCALIHDP 162
Cdd:cd03217 78 --------GI------FLAFQYPPEIPGV-----------KNADFLRYVNE---------GFSGGEKKRNEILQLLLLEP 123
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15600424 163 DLLILDEPTTGVDPLSRNQFWELIGRIRagREGMSVLVATAYMEEAE--RFDWLVAMDDGKVLATGTPQELRE 233
Cdd:cd03217 124 DLAILDEPDSGLDIDALRLVAEVINKLR--EEGKSVLIITHYQRLLDyiKPDRVHVLYDGRIVKSGDKELALE 194
|
|
| PRK15093 |
PRK15093 |
peptide ABC transporter ATP-binding protein SapD; |
289-493 |
1.31e-11 |
|
peptide ABC transporter ATP-binding protein SapD;
Pssm-ID: 185049 [Multi-domain] Cd Length: 330 Bit Score: 66.75 E-value: 1.31e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 289 AVDHVSFRIERGEIFGFLGSNGCGKSTTMKMLTGLLPASEGTCA--LFGQPVDASDMATRRR---VGY-MSQAFS----- 357
Cdd:PRK15093 22 AVDRVSMTLTEGEIRGLVGESGSGKSLIAKAICGVTKDNWRVTAdrMRFDDIDLLRLSPRERrklVGHnVSMIFQepqsc 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 358 LYAELSVRQNLVlharlfhlpaDGIPA----------------RVGEMLRRF---DLEKVADELPNDLPLGIRQRLSLAV 418
Cdd:PRK15093 102 LDPSERVGRQLM----------QNIPGwtykgrwwqrfgwrkrRAIELLHRVgikDHKDAMRSFPYELTEGECQKVMIAI 171
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15600424 419 AVIHKPEILILDEPTSGVDPVARDGFWELMVELSRRDGVTIFISTHFMNE-AQRCDRISLMHAGKVLASDTPDELV 493
Cdd:PRK15093 172 ALANQPRLLIADEPTNAMEPTTQAQIFRLLTRLNQNNNTTILLISHDLQMlSQWADKINVLYCGQTVETAPSKELV 247
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
284-464 |
1.33e-11 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 64.59 E-value: 1.33e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 284 FGDFVAVDHVSFRIERGEIFGFLGSNGCGKSTTMKMLTGLLPASEGTCALFGQPVDASDMATRRRVGYMSQAFSLYAELS 363
Cdd:PRK13540 11 YHDQPLLQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEILFERQSIKKDLCTYQKQLCFVGHRSGINPYLT 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 364 VRQNLvlharLFHLPADGIPARVGEMLRRFDLEKVADELPNDLPLGIRQRLSLAVAVIHKPEILILDEPTSGVDPVARDG 443
Cdd:PRK13540 91 LRENC-----LYDIHFSPGAVGITELCRLFSLEHLIDYPCGLLSSGQKRQVALLRLWMSKAKLWLLDEPLVALDELSLLT 165
|
170 180
....*....|....*....|.
gi 15600424 444 FWElMVELSRRDGVTIFISTH 464
Cdd:PRK13540 166 IIT-KIQEHRAKGGAVLLTSH 185
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
23-231 |
1.39e-11 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 65.97 E-value: 1.39e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 23 AVDDVSLEIPANRMVGLIGPDGVGKSSLLALLAGARKMQDGEIRVLD-----GDMRDRRHrravcpRIAYMPQGLGKNLY 97
Cdd:PRK15112 28 AVKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDhplhfGDYSYRSQ------RIRMIFQDPSTSLN 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 98 PTLSVFENVDFFGRL-FGHDKAERERRIADLLQSTGLAP-FAERPAGKLSGGMKQKLGLCCALIHDPDLLILDEPTTGVD 175
Cdd:PRK15112 102 PRQRISQILDFPLRLnTDLEPEQREKQIIETLRQVGLLPdHASYYPHMLAPGQKQRLGLARALILRPKVIIADEALASLD 181
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 15600424 176 PLSRNQFWELIGRIRAgREGMSVLVATAYMEEAERF-DWLVAMDDGKVLATGTPQEL 231
Cdd:PRK15112 182 MSMRSQLINLMLELQE-KQGISYIYVTQHLGMMKHIsDQVLVMHQGEVVERGSTADV 237
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
22-266 |
1.90e-11 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 66.30 E-value: 1.90e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 22 RAVDDVSLEIPANRMVGLIGPDGVGKS-SLLALLA----GARKMQDGeirvLDGDMRD------RRHRRAVCPRIAYMPQ 90
Cdd:PRK11022 21 RAVDRISYSVKQGEVVGIVGESGSGKSvSSLAIMGlidyPGRVMAEK----LEFNGQDlqriseKERRNLVGAEVAMIFQ 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 91 GLGKNLYPTLSV-FENVDFFGRLFGHDKAERERRIADLLQSTGLAPFAER----PAgKLSGGMKQKLGLCCALIHDPDLL 165
Cdd:PRK11022 97 DPMTSLNPCYTVgFQIMEAIKVHQGGNKKTRRQRAIDLLNQVGIPDPASRldvyPH-QLSGGMSQRVMIAMAIACRPKLL 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 166 ILDEPTTGVDPLSRNQFWELIGRIRAgREGMSVLVATAYME-EAERFDWLVAMDDGKVLATGTPQELReRTGTQSLESAF 244
Cdd:PRK11022 176 IADEPTTALDVTIQAQIIELLLELQQ-KENMALVLITHDLAlVAEAAHKIIVMYAGQVVETGKAHDIF-RAPRHPYTQAL 253
|
250 260 270
....*....|....*....|....*....|
gi 15600424 245 IALLPESKrAGHHRL-----VIP---PRPQ 266
Cdd:PRK11022 254 LRALPEFA-QDKARLaslpgVVPgkyDRPN 282
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
275-495 |
2.62e-11 |
|
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: 63.70 E-value: 2.62e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 275 IEAEGLTCRFGDFVAVDHVSFRIERGEIFGFLGSNGCGKSTTMKMLTGLlPASE---GTCALFGQPVDASDMATRRRVG- 350
Cdd:cd03217 1 LEIKDLHVSVGGKEILKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMGH-PKYEvteGEILFKGEDITDLPPEERARLGi 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 351 YMSqafslyaelsvrqnlvlharlFHLPADgIPA-RVGEMLRrfdlekvadELPNDLPLGIRQRLSLAVAVIHKPEILIL 429
Cdd:cd03217 80 FLA---------------------FQYPPE-IPGvKNADFLR---------YVNEGFSGGEKKRNEILQLLLLEPDLAIL 128
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15600424 430 DEPTSGVDPVARDGFWELMVELsRRDGVTIFISTHF--MNEAQRCDRISLMHAGKVLASDtPDELVRQ 495
Cdd:cd03217 129 DEPDSGLDIDALRLVAEVINKL-REEGKSVLIITHYqrLLDYIKPDRVHVLYDGRIVKSG-DKELALE 194
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
265-494 |
3.28e-11 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 67.19 E-value: 3.28e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 265 PQSEGAP-RIAIEAEGLTCRF----GDFVAVDHVSFRIERGEIFGFLGSNGCGKSTTMKMLTGLLPASEGTcalfgqpVD 339
Cdd:PRK10261 2 PHSDELDaRDVLAVENLNIAFmqeqQKIAAVRNLSFSLQRGETLAIVGESGSGKSVTALALMRLLEQAGGL-------VQ 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 340 ASDMATRRR------VGYMSQA------------------FSLYAELSVRQNLV----LHARLFHLPADGIPARVGEMLR 391
Cdd:PRK10261 75 CDKMLLRRRsrqvieLSEQSAAqmrhvrgadmamifqepmTSLNPVFTVGEQIAesirLHQGASREEAMVEAKRMLDQVR 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 392 RFDLEKVADELPNDLPLGIRQRLSLAVAVIHKPEILILDEPTSGVDPVARDGFWELMVELSRRDGVTIFISTHFMN-EAQ 470
Cdd:PRK10261 155 IPEAQTILSRYPHQLSGGMRQRVMIAMALSCRPAVLIADEPTTALDVTIQAQILQLIKVLQKEMSMGVIFITHDMGvVAE 234
|
250 260
....*....|....*....|....
gi 15600424 471 RCDRISLMHAGKVLASDTPDELVR 494
Cdd:PRK10261 235 IADRVLVMYQGEAVETGSVEQIFH 258
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
292-493 |
4.06e-11 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 67.46 E-value: 4.06e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 292 HVSFRIERGEIFGFLGSNGCGKSTTMKMLTGLLPASEGTCAlfgqpVDASDMAT------RRRVGYMSQAFSLYAElSVR 365
Cdd:PLN03130 1257 GLSFEISPSEKVGIVGRTGAGKSSMLNALFRIVELERGRIL-----IDGCDISKfglmdlRKVLGIIPQAPVLFSG-TVR 1330
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 366 QNLVLHARlfHLPADGIP----ARVGEMLRR--FDLEKVADELPNDLPLGIRQRLSLAVAVIHKPEILILDEPTSGVDpV 439
Cdd:PLN03130 1331 FNLDPFNE--HNDADLWEslerAHLKDVIRRnsLGLDAEVSEAGENFSVGQRQLLSLARALLRRSKILVLDEATAAVD-V 1407
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 15600424 440 ARDGfweLMVELSRRD--GVTIFISTHFMNEAQRCDRISLMHAGKVLASDTPDELV 493
Cdd:PLN03130 1408 RTDA---LIQKTIREEfkSCTMLIIAHRLNTIIDCDRILVLDAGRVVEFDTPENLL 1460
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
24-247 |
5.54e-11 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 63.95 E-value: 5.54e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 24 VDDVSLEIPANRMVGLIGPDGVGKS-SLLALL----AGARKMQdGEIRvLDG------DMRDRrHRRAVC--PRIAYMP- 89
Cdd:PRK10418 19 VHGVSLTLQRGRVLALVGGSGSGKSlTCAAALgilpAGVRQTA-GRVL-LDGkpvapcALRGR-KIATIMqnPRSAFNPl 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 90 QGLGKNLYPTLSVFenvdffgrlfghDKAERERRIADLLQSTGLAP---FAERPAGKLSGGMKQKLGLCCALIHDPDLLI 166
Cdd:PRK10418 96 HTMHTHARETCLAL------------GKPADDATLTAALEAVGLENaarVLKLYPFEMSGGMLQRMMIALALLCEAPFII 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 167 LDEPTTGVDPLSRNQFWELIGRIRAGReGMSVLVATAYMEEAERF-DWLVAMDDGKVLATGTPQELRERTG---TQSLES 242
Cdd:PRK10418 164 ADEPTTDLDVVAQARILDLLESIVQKR-ALGMLLVTHDMGVVARLaDDVAVMSHGRIVEQGDVETLFNAPKhavTRSLVS 242
|
....*
gi 15600424 243 AFIAL 247
Cdd:PRK10418 243 AHLAL 247
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
274-492 |
5.64e-11 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 64.35 E-value: 5.64e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 274 AIEAEGLTCRFGDFVAVDHVSFRIERGEIFGFLGSNGCGKSTTMKMLTGLLPASEG-----TCALFGQPV-DASD-MATR 346
Cdd:PRK14271 21 AMAAVNLTLGFAGKTVLDQVSMGFPARAVTSLMGPTGSGKTTFLRTLNRMNDKVSGyrysgDVLLGGRSIfNYRDvLEFR 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 347 RRVGYMSQAFSLYAeLSVRQNLVLHARLFHL-PADGIPARVGEMLRRFDL-EKVADEL---PNDLPLGIRQRLSLAVAVI 421
Cdd:PRK14271 101 RRVGMLFQRPNPFP-MSIMDNVLAGVRAHKLvPRKEFRGVAQARLTEVGLwDAVKDRLsdsPFRLSGGQQQLLCLARTLA 179
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15600424 422 HKPEILILDEPTSGVDPVARDGFWELMVELSRRdgVTIFISTHFMNEAQR-CDRISLMHAGKVLASDTPDEL 492
Cdd:PRK14271 180 VNPEVLLLDEPTSALDPTTTEKIEEFIRSLADR--LTVIIVTHNLAQAARiSDRAALFFDGRLVEEGPTEQL 249
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
300-464 |
5.67e-11 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 66.44 E-value: 5.67e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 300 GEIFGFLGSNGCGKSTTMKMLTGLLPAS--EGTCALFGQPVDASDMatrRRVGYMSQAFSLYAELSVRQNLVLHArLFHL 377
Cdd:PLN03211 94 GEILAVLGPSGSGKSTLLNALAGRIQGNnfTGTILANNRKPTKQIL---KRTGFVTQDDILYPHLTVRETLVFCS-LLRL 169
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 378 P-----------ADGIPARVGemLRRFDLEKVADELPNDLPLGIRQRLSLAVAVIHKPEILILDEPTSGVDPVARDGFWE 446
Cdd:PLN03211 170 PksltkqekilvAESVISELG--LTKCENTIIGNSFIRGISGGERKRVSIAHEMLINPSLLILDEPTSGLDATAAYRLVL 247
|
170
....*....|....*...
gi 15600424 447 LMVELSRRdGVTIFISTH 464
Cdd:PLN03211 248 TLGSLAQK-GKTIVTSMH 264
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
7-228 |
7.38e-11 |
|
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type transporter 1). NFT1 belongs to the MRP (multidrug resistance-associated protein) family of ABC transporters. Some of the MRP members have five additional transmembrane segments in their N-terminus, but the function of these additional membrane-spanning domains is not clear. The MRP was found in the multidrug-resisting lung cancer cell in which p-glycoprotein was not overexpressed. MRP exports glutathione by drug stimulation, as well as, certain substrates in conjugated forms with anions such as glutathione, glucuronate, and sulfate.
Pssm-ID: 213269 [Multi-domain] Cd Length: 207 Bit Score: 62.81 E-value: 7.38e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 7 GVASLRGVSLRYGE--TRAVDDVSLEIPANRMVGLIGPDGVGKSSLLALLAGARKMQDGEIRVLDGDMRD---RRHRRav 81
Cdd:cd03369 5 GEIEVENLSVRYAPdlPPVLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDGIDISTiplEDLRS-- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 82 cpRIAYMPQGlgknlyPTL---SVFENVDFFGRLfghdkAERERRIADLLQSTGLapfaerpagKLSGGMKQKLGLCCAL 158
Cdd:cd03369 83 --SLTIIPQD------PTLfsgTIRSNLDPFDEY-----SDEEIYGALRVSEGGL---------NLSQGQRQLLCLARAL 140
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15600424 159 IHDPDLLILDEPTTGVDPLSRnqfwELIGR-IRAGREGMSVLVATAYMEEAERFDWLVAMDDGKVLATGTP 228
Cdd:cd03369 141 LKRPRVLVLDEATASIDYATD----ALIQKtIREEFTNSTILTIAHRLRTIIDYDKILVMDAGEVKEYDHP 207
|
|
| NatB |
COG1668 |
ABC-type Na+ efflux pump, permease component NatB [Energy production and conversion, Inorganic ... |
578-908 |
7.40e-11 |
|
ABC-type Na+ efflux pump, permease component NatB [Energy production and conversion, Inorganic ion transport and metabolism];
Pssm-ID: 441274 [Multi-domain] Cd Length: 402 Bit Score: 65.32 E-value: 7.40e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 578 MFIIGYGINMDVEDLSWAVLDRDQTTTSQAYALNIAGSryFVEHAPITDPDDLDRRLRSGELSLAVEIPPNFGRDlkrgS 657
Cdd:COG1668 37 GLGMLFMSGNDDEPLKVAVVDESGAPALAEALKEAAVN--FEVVPEVADEEEAEAAVEDGEIDAVLVIPEDFSLE----N 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 658 DPAIGVWIDGAMPTRANTVL-GYVQGLHTSYLAD---LSRQAGGAEASAAASTEVRYRYNPDVESLKAMVPAVIPLLL-- 731
Cdd:COG1668 111 PATVELYSDSSPDSSAVSRLeSALSQALLALRLAalgLDPEQLQALLAPVSVETVDLSKASPEEGAGYILGYLLPFLLym 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 732 -IMIPAMLTALGVVREKELGSITNLyVTPVTRLEFLVGKQLPYVAMGMINFLLMLVLAIVVFR------------VPLKG 798
Cdd:COG1668 191 fIFTYGSMIADSVAEEKESRTLEIL-LSSVSPRQLLLGKILGIGLVGLTQALLWLVGGLIGLLlasglglsalsgLNLSP 269
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 799 SFLALTI-----GAFLYVVTSTGLGLFLSTFMRSQiAAVFGVAIATMIPA-IQFSGLIHPVSSLEGAAAWIgklyP-TSH 871
Cdd:COG1668 270 GLLLLFLlffllGYLLYAALFAALGALASSFKEAQ-QYLSPLTLLLMIPFfVAMFVLSNPDGPLATVLSLI----PfTSP 344
|
330 340 350
....*....|....*....|....*....|....*..
gi 15600424 872 FLVVSRGAFSkSLGLSDLWAYYLPLAASIVVLTLLSV 908
Cdd:COG1668 345 ILMPLRLALG-EVPWWEILLSLALLLATAVLLLWLAA 380
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
288-494 |
8.09e-11 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 63.69 E-value: 8.09e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 288 VAVDHVSFRIERGEIFGFLGSNGCGKSTTMKMLTGLLPAS--------EGTCALFGQP---VDASDMATRRRVgyMSQAF 356
Cdd:PRK13547 15 AILRDLSLRIEPGRVTALLGRNGAGKSTLLKALAGDLTGGgaprgarvTGDVTLNGEPlaaIDAPRLARLRAV--LPQAA 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 357 SLYAELSVRQnLVLHARLFHLPADGIPAR-----VGEMLRRFDLEKVADELPNDLPLGIRQRLSLA--VAVIHK------ 423
Cdd:PRK13547 93 QPAFAFSARE-IVLLGRYPHARRAGALTHrdgeiAWQALALAGATALVGRDVTTLSGGELARVQFArvLAQLWPphdaaq 171
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15600424 424 -PEILILDEPTSGVDPVARDGFWELMVELSRRDGVTIFISTHFMNEAQR-CDRISLMHAGKVLASDTPDELVR 494
Cdd:PRK13547 172 pPRYLLLDEPTAALDLAHQHRLLDTVRRLARDWNLGVLAIVHDPNLAARhADRIAMLADGAIVAHGAPADVLT 244
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
264-438 |
9.10e-11 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 62.56 E-value: 9.10e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 264 RPQSEGAPRIAieAEGLTCRFGDFVAVDHVSFRIERGEIFGFLGSNGCGKSTTMKMLTGLLPASEGTCALFGQPVDASDM 343
Cdd:PRK13543 3 EPLHTAPPLLA--AHALAFSRNEEPVFGPLDFHVDAGEALLVQGDNGAGKTTLLRVLAGLLHVESGQIQIDGKTATRGDR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 344 AtrRRVGYMSQAFSLYAELSVRQNLVLHARLFHLPADGIParvGEMLRRFDLEKVADELPNDLPLGIRQRLSLAVAVIHK 423
Cdd:PRK13543 81 S--RFMAYLGHLPGLKADLSTLENLHFLCGLHGRRAKQMP---GSALAIVGLAGYEDTLVRQLSAGQKKRLALARLWLSP 155
|
170
....*....|....*
gi 15600424 424 PEILILDEPTSGVDP 438
Cdd:PRK13543 156 APLWLLDEPYANLDL 170
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
275-484 |
9.45e-11 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 63.26 E-value: 9.45e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 275 IEAEGLTCRFGDFVAVDHVSFRIERGEIFGFLGSNGCGKSTTMKMLT---GLLPASEGTCA-------LFGQPVDASDMa 344
Cdd:PRK14239 6 LQVSDLSVYYNKKKALNSVSLDFYPNEITALIGPSGSGKSTLLRSINrmnDLNPEVTITGSivynghnIYSPRTDTVDL- 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 345 tRRRVGYMSQAFSLYAeLSVRQNLVLHARLfhlpaDGIP------ARVGEMLRRFDL-EKVADELpNDLPLGI----RQR 413
Cdd:PRK14239 85 -RKEIGMVFQQPNPFP-MSIYENVVYGLRL-----KGIKdkqvldEAVEKSLKGASIwDEVKDRL-HDSALGLsggqQQR 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15600424 414 LSLAVAVIHKPEILILDEPTSGVDPVARDGFWELMVELsrRDGVTIFISTHFMNEAQR-CDRISLMHAGKVL 484
Cdd:PRK14239 157 VCIARVLATSPKIILLDEPTSALDPISAGKIEETLLGL--KDDYTMLLVTRSMQQASRiSDRTGFFLDGDLI 226
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
5-175 |
9.91e-11 |
|
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of the ABC transporter ATP-binding cassette, but are found outside the common ABC transporter operon structure that features integral membrane permease proteins and substrate-binding proteins encoded next to the ATP-binding cassette (ABC domain) protein. The member protein ChvD from Agrobacterium tumefaciens was identified as both a candidate to interact with VirB8, based on yeast two-hybrid analysis, and as an apparent regulator of VirG. The general function of this protein family is unknown.
Pssm-ID: 274744 [Multi-domain] Cd Length: 552 Bit Score: 65.34 E-value: 9.91e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 5 GSGVASLRGVSLRYGETRAVDDVSLEIPANRMVGLIGPDGVGKSSLLALLAGARKMQDGEIRVldGDmrdrrhrrAVcpR 84
Cdd:TIGR03719 319 GDKVIEAENLTKAFGDKLLIDDLSFKLPPGGIVGVIGPNGAGKSTLFRMITGQEQPDSGTIEI--GE--------TV--K 386
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 85 IAYMPQGLgKNLYPTLSVFE------------NVDFFGR----LFGHDKAERERRIadllqstglapfaerpaGKLSGGM 148
Cdd:TIGR03719 387 LAYVDQSR-DALDPNKTVWEeisggldiiklgKREIPSRayvgRFNFKGSDQQKKV-----------------GQLSGGE 448
|
170 180
....*....|....*....|....*..
gi 15600424 149 KQKLGLCCALIHDPDLLILDEPTTGVD 175
Cdd:TIGR03719 449 RNRVHLAKTLKSGGNVLLLDEPTNDLD 475
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
8-223 |
1.03e-10 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 62.67 E-value: 1.03e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 8 VASLRGVSLRYGETRAVDDVSLEIPANRMVGLIGPDGVGKSSLLALLAGARKMQD--GEIRVLDGDmrdrrhrravcpri 85
Cdd:COG2401 30 VLEAFGVELRVVERYVLRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGALKGTPvaGCVDVPDNQ-------------- 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 86 aympqglgknLYPTLSVFENVDFFGRLfgHDKAErerriadLLQSTGL--APFAERPAGKLSGGMKQKLGLCCALIHDPD 163
Cdd:COG2401 96 ----------FGREASLIDAIGRKGDF--KDAVE-------LLNAVGLsdAVLWLRRFKELSTGQKFRFRLALLLAERPK 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15600424 164 LLILDEPTTGVDP-----LSRNqfwelIGRIrAGREGMSVLVATAYME--EAERFDWLVAMDDGKVL 223
Cdd:COG2401 157 LLVIDEFCSHLDRqtakrVARN-----LQKL-ARRAGITLVVATHHYDviDDLQPDLLIFVGYGGVP 217
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
291-481 |
1.07e-10 |
|
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: 61.88 E-value: 1.07e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 291 DHVSFRIERGEIFGFLGSNGCGKSTTMKMLTGLLPAS--EGTCALFGQPVDASdmaTRRRVGYMSQAFSLYAELSVRQNL 368
Cdd:cd03232 24 NNISGYVKPGTLTALMGESGAGKTTLLDVLAGRKTAGviTGEILINGRPLDKN---FQRSTGYVEQQDVHSPNLTVREAL 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 369 VLHArlfhlpadgiparvgeMLRRFDLEKvadelpndlplgiRQRLSLAVAVIHKPEILILDEPTSGVDPVARdgfWELM 448
Cdd:cd03232 101 RFSA----------------LLRGLSVEQ-------------RKRLTIGVELAAKPSILFLDEPTSGLDSQAA---YNIV 148
|
170 180 190
....*....|....*....|....*....|....*..
gi 15600424 449 VELSR--RDGVTIFISTHFMNEA--QRCDRISLMHAG 481
Cdd:cd03232 149 RFLKKlaDSGQAILCTIHQPSASifEKFDRLLLLKRG 185
|
|
| tagH |
PRK13545 |
teichoic acids export protein ATP-binding subunit; Provisional |
289-483 |
1.62e-10 |
|
teichoic acids export protein ATP-binding subunit; Provisional
Pssm-ID: 184130 [Multi-domain] Cd Length: 549 Bit Score: 64.53 E-value: 1.62e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 289 AVDHVSFRIERGEIFGFLGSNGCGKSTTMKMLTGLLPASEGTcalfgqpVDASDMATRRRVGYmsqafSLYAELSVRQNL 368
Cdd:PRK13545 39 ALNNISFEVPEGEIVGIIGLNGSGKSTLSNLIAGVTMPNKGT-------VDIKGSAALIAISS-----GLNGQLTGIENI 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 369 VLHARLFHLPADGIPARVGEMLRRFDLEKVADELPNDLPLGIRQRLSLAVAVIHKPEILILDEPTSGVDPVARDGFWELM 448
Cdd:PRK13545 107 ELKGLMMGLTKEKIKEIIPEIIEFADIGKFIYQPVKTYSSGMKSRLGFAISVHINPDILVIDEALSVGDQTFTKKCLDKM 186
|
170 180 190
....*....|....*....|....*....|....*.
gi 15600424 449 VELsRRDGVTIFISTHFMNEAQR-CDRISLMHAGKV 483
Cdd:PRK13545 187 NEF-KEQGKTIFFISHSLSQVKSfCTKALWLHYGQV 221
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
26-226 |
2.04e-10 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 63.35 E-value: 2.04e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 26 DVSLEIPANRMVGLIGPDGVGKSSLLALLAGARKMQDGEIRVLDGDMRDRRHRRAVCP---RIAYMPQGlgKNLYPTLSV 102
Cdd:PRK11144 16 TVNLTLPAQGITAIFGRSGAGKTSLINAISGLTRPQKGRIVLNGRVLFDAEKGICLPPekrRIGYVFQD--ARLFPHYKV 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 103 FENVdffgrLFGHDKAERER--RIADLLqstGLAPFAERPAGKLSGGMKQKLGLCCALIHDPDLLILDEPTTGVDpLSRN 180
Cdd:PRK11144 94 RGNL-----RYGMAKSMVAQfdKIVALL---GIEPLLDRYPGSLSGGEKQRVAIGRALLTAPELLLMDEPLASLD-LPRK 164
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 15600424 181 QfwELIGRI-RAGRE-GMSVLVATAYMEEAERF-DWLVAMDDGKVLATG 226
Cdd:PRK11144 165 R--ELLPYLeRLAREiNIPILYVSHSLDEILRLaDRVVVLEQGKVKAFG 211
|
|
| tagH |
PRK13545 |
teichoic acids export protein ATP-binding subunit; Provisional |
23-169 |
2.20e-10 |
|
teichoic acids export protein ATP-binding subunit; Provisional
Pssm-ID: 184130 [Multi-domain] Cd Length: 549 Bit Score: 64.14 E-value: 2.20e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 23 AVDDVSLEIPANRMVGLIGPDGVGKSSLLALLAGARKMQDGEIRVldgdmrdrrhrRAVCPRIAympqgLGKNLYPTLSV 102
Cdd:PRK13545 39 ALNNISFEVPEGEIVGIIGLNGSGKSTLSNLIAGVTMPNKGTVDI-----------KGSAALIA-----ISSGLNGQLTG 102
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15600424 103 FENVDFFGRLFGHDKAERERRIADLLQSTGLAPFAERPAGKLSGGMKQKLGLCCALIHDPDLLILDE 169
Cdd:PRK13545 103 IENIELKGLMMGLTKEKIKEIIPEIIEFADIGKFIYQPVKTYSSGMKSRLGFAISVHINPDILVIDE 169
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
285-437 |
2.77e-10 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 64.36 E-value: 2.77e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 285 GDFVAVDHVSFRIERGEIFGFLGSNGCGKSTTMKML-----TGLLpaSEGTCALFGQPVDASdmaTRRRVGYMSQAFSLY 359
Cdd:TIGR00956 774 EKRVILNNVDGWVKPGTLTALMGASGAGKTTLLNVLaervtTGVI--TGGDRLVNGRPLDSS---FQRSIGYVQQQDLHL 848
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 360 AELSVRQNLVLHARLfHLPADgIPAR-----VGEMLRRFDLEKVADELPNDLPLGI----RQRLSLAVAVIHKPEILI-L 429
Cdd:TIGR00956 849 PTSTVRESLRFSAYL-RQPKS-VSKSekmeyVEEVIKLLEMESYADAVVGVPGEGLnveqRKRLTIGVELVAKPKLLLfL 926
|
....*...
gi 15600424 430 DEPTSGVD 437
Cdd:TIGR00956 927 DEPTSGLD 934
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
264-497 |
3.24e-10 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 63.97 E-value: 3.24e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 264 RPQSEGapRIAIEAEGLTCRfGDFVAVDHVSFRIERGEIFGFLGSNGCGKSTTMKMLTGLLPASEGTCALFGQPVDA-SD 342
Cdd:PRK10790 334 RPLQSG--RIDIDNVSFAYR-DDNLVLQNINLSVPSRGFVALVGHTGSGKSTLASLLMGYYPLTEGEIRLDGRPLSSlSH 410
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 343 MATRRRVGYMSQ-----AFSLYA---------ELSVRQNL--VLHARLFHLPADGIPARVGEMlrrfdlekvadelPNDL 406
Cdd:PRK10790 411 SVLRQGVAMVQQdpvvlADTFLAnvtlgrdisEEQVWQALetVQLAELARSLPDGLYTPLGEQ-------------GNNL 477
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 407 PLGIRQRLSLAVAVIHKPEILILDEPTSGVDPVARDGFWELMVELsrRDGVTIFISTHFMNEAQRCDRISLMHAGKVLAS 486
Cdd:PRK10790 478 SVGQKQLLALARVLVQTPQILILDEATANIDSGTEQAIQQALAAV--REHTTLVVIAHRLSTIVEADTILVLHRGQAVEQ 555
|
250
....*....|.
gi 15600424 487 DTPDELVRQRG 497
Cdd:PRK10790 556 GTHQQLLAAQG 566
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
7-236 |
3.33e-10 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 63.88 E-value: 3.33e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 7 GVASLRGVSLRY--GETRAVDDVSLEIPANRMVGLIGPDGVGKSSLLALLAGARKMQDGEIrVLDG-DMRDRRHRravcp 83
Cdd:PRK11176 340 GDIEFRNVTFTYpgKEVPALRNINFKIPAGKTVALVGRSGSGKSTIANLLTRFYDIDEGEI-LLDGhDLRDYTLA----- 413
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 84 riaympqglgkNLYPTLS-VFENVDFF------------GRLFGHDKAERERRIA---DLLQS--TGLAPFAERPAGKLS 145
Cdd:PRK11176 414 -----------SLRNQVAlVSQNVHLFndtianniayarTEQYSREQIEEAARMAyamDFINKmdNGLDTVIGENGVLLS 482
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 146 GGMKQKLGLCCALIHDPDLLILDEPTTGVDPLSRNQFWELIGRIRAGRegmSVLVATAYMEEAERFDWLVAMDDGKVLAT 225
Cdd:PRK11176 483 GGQRQRIAIARALLRDSPILILDEATSALDTESERAIQAALDELQKNR---TSLVIAHRLSTIEKADEILVVEDGEIVER 559
|
250
....*....|.
gi 15600424 226 GTPQELRERTG 236
Cdd:PRK11176 560 GTHAELLAQNG 570
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
185-498 |
3.51e-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: 64.20 E-value: 3.51e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 185 LIGR--IRAGREGMSV---LVATAYMeeaerfDWLVAMDDGKVLATGTPQELRERTGTQSlESAFIallpeskraghhrl 259
Cdd:TIGR00957 1211 VISRhsLSAGLVGLSVsysLQVTFYL------NWLVRMSSEMETNIVAVERLKEYSETEK-EAPWQ-------------- 1269
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 260 VIPPRPQSEGAPRIAIEAEGLTCRFG---DFVaVDHVSFRIERGEIFGFLGSNGCGKSTTMKMLTGLLPASEGTCALFGq 336
Cdd:TIGR00957 1270 IQETAPPSGWPPRGRVEFRNYCLRYRedlDLV-LRHINVTIHGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDG- 1347
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 337 pVDASDMAT---RRRVGYMSQ--------------AFSLYAELSVRQNLVL-HARLFhlpADGIPARvgemlrrfdLEKV 398
Cdd:TIGR00957 1348 -LNIAKIGLhdlRFKITIIPQdpvlfsgslrmnldPFSQYSDEEVWWALELaHLKTF---VSALPDK---------LDHE 1414
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 399 ADELPNDLPLGIRQRLSLAVAVIHKPEILILDEPTSGVDpVARDGFWELMVElSRRDGVTIFISTHFMNEAQRCDRISLM 478
Cdd:TIGR00957 1415 CAEGGENLSVGQRQLVCLARALLRKTKILVLDEATAAVD-LETDNLIQSTIR-TQFEDCTVLTIAHRLNTIMDYTRVIVL 1492
|
330 340
....*....|....*....|
gi 15600424 479 HAGKVLASDTPDELVRQRGL 498
Cdd:TIGR00957 1493 DKGEVAEFGAPSNLLQQRGI 1512
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
26-236 |
4.23e-10 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 63.59 E-value: 4.23e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 26 DVSLEIPANRMVGLIGPDGVGKSSLLALLAGARKMQDGEIrVLDG-DMRD------RRHRRAVcpriAYMPQGLGKnlyp 98
Cdd:TIGR00958 499 GLTFTLHPGEVVALVGPSGSGKSTVAALLQNLYQPTGGQV-LLDGvPLVQydhhylHRQVALV----GQEPVLFSG---- 569
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 99 tlSVFENVdffgrLFGHDKAERERRIADLLQSTGLAPFAERPAG----------KLSGGMKQKLGLCCALIHDPDLLILD 168
Cdd:TIGR00958 570 --SVRENI-----AYGLTDTPDEEIMAAAKAANAHDFIMEFPNGydtevgekgsQLSGGQKQRIAIARALVRKPRVLILD 642
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15600424 169 EPTTGVDPLSRNQFWELigrirAGREGMSVLVATAYMEEAERFDWLVAMDDGKVLATGTPQELRERTG 236
Cdd:TIGR00958 643 EATSALDAECEQLLQES-----RSRASRTVLLIAHRLSTVERADQILVLKKGSVVEMGTHKQLMEDQG 705
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
18-202 |
4.72e-10 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 59.96 E-value: 4.72e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 18 YGETRAVDDVSLEIPANRMVGLIGPDGVGKSSLLALLAGARKMQDGEIRVLDGDMrdRRHRRAVCPRIAYMPQGLGKNly 97
Cdd:PRK13540 11 YHDQPLLQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEILFERQSI--KKDLCTYQKQLCFVGHRSGIN-- 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 98 PTLSVFENVdffgrLFGHDKAERERRIADLLQSTGLAPFAERPAGKLSGGMKQKLGLCCALIHDPDLLILDEPTTGVDPL 177
Cdd:PRK13540 87 PYLTLRENC-----LYDIHFSPGAVGITELCRLFSLEHLIDYPCGLLSSGQKRQVALLRLWMSKAKLWLLDEPLVALDEL 161
|
170 180
....*....|....*....|....*.
gi 15600424 178 SrnqFWELIGRIRAGR-EGMSVLVAT 202
Cdd:PRK13540 162 S---LLTIITKIQEHRaKGGAVLLTS 184
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
14-231 |
6.09e-10 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 61.27 E-value: 6.09e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 14 VSLRYGETRAVDDVSLEIPANRMVGLIGPDGVGKSSLLALLagaRKMQD--------GEIRVLDGDMRDRRHRRAVCPRI 85
Cdd:PRK14271 27 LTLGFAGKTVLDQVSMGFPARAVTSLMGPTGSGKTTFLRTL---NRMNDkvsgyrysGDVLLGGRSIFNYRDVLEFRRRV 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 86 AYMPQGlgKNLYPtLSVFENVdfFGRLFGHDKAERE--RRIADL-LQSTGL----------APFaerpagKLSGGMKQKL 152
Cdd:PRK14271 104 GMLFQR--PNPFP-MSIMDNV--LAGVRAHKLVPRKefRGVAQArLTEVGLwdavkdrlsdSPF------RLSGGQQQLL 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 153 GLCCALIHDPDLLILDEPTTGVDPLSRNQFWELigrIRAGREGMSVLVATAYMEEAERF-DWLVAMDDGKVLATGTPQEL 231
Cdd:PRK14271 173 CLARTLAVNPEVLLLDEPTSALDPTTTEKIEEF---IRSLADRLTVIIVTHNLAQAARIsDRAALFFDGRLVEEGPTEQL 249
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
275-467 |
8.02e-10 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 62.22 E-value: 8.02e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 275 IEAEGLTCRFGDFVAVDHVSFRIERGEIFGFLGSNGCGKSTTMKMLTGLLPASEGTCALfgqpvDASDmatrrRVGYMSQ 354
Cdd:PRK15064 2 LSTANITMQFGAKPLFENISVKFGGGNRYGLIGANGCGKSTFMKILGGDLEPSAGNVSL-----DPNE-----RLGKLRQ 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 355 AFSLYAELSVRQNLVL-HA----------RLFHLP----ADGIpaRVGEMLRRF------DLEKVADELPndLPLGI--- 410
Cdd:PRK15064 72 DQFAFEEFTVLDTVIMgHTelwevkqerdRIYALPemseEDGM--KVADLEVKFaemdgyTAEARAGELL--LGVGIpee 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15600424 411 -------------RQRLSLAVAVIHKPEILILDEPTSGVD-PVARdgfWeLMVELSRRDGVTIFIS--THFMN 467
Cdd:PRK15064 148 qhyglmsevapgwKLRVLLAQALFSNPDILLLDEPTNNLDiNTIR---W-LEDVLNERNSTMIIIShdRHFLN 216
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
22-175 |
9.16e-10 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 61.26 E-value: 9.16e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 22 RAVDDVSLEIPANRMVGLIGPDGVGKSSLLALLAGARKMQDGEIRVLDGDMRDRRH--RRAVCPRIAYMPQGLGKNLYPT 99
Cdd:PRK15079 35 KAVDGVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGEVAWLGKDLLGMKDdeWRAVRSDIQMIFQDPLASLNPR 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 100 LSVFENV-----DFFGRLfghDKAERERRIADLLQSTGLAP-FAERPAGKLSGGMKQKLGLCCALIHDPDLLILDEPTTG 173
Cdd:PRK15079 115 MTIGEIIaeplrTYHPKL---SRQEVKDRVKAMMLKVGLLPnLINRYPHEFSGGQCQRIGIARALILEPKLIICDEPVSA 191
|
..
gi 15600424 174 VD 175
Cdd:PRK15079 192 LD 193
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
256-464 |
1.07e-09 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 59.59 E-value: 1.07e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 256 HHRLVIPPRPQSegapRIAIEAEGLTCRFGDFVAVDHVSFRIERGEIFGFLGSNGCGKSTTMKMLTGLLPASEGTCAlfg 335
Cdd:COG2401 16 VYSSVLDLSERV----AIVLEAFGVELRVVERYVLRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGALKGTPVAGC--- 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 336 qpVDASDMatrrrvgymsqafSLYAELSVRQNlVLHARLFHLpADGIPARVG-----EMLRRFdlekvaDELPNdlplGI 410
Cdd:COG2401 89 --VDVPDN-------------QFGREASLIDA-IGRKGDFKD-AVELLNAVGlsdavLWLRRF------KELST----GQ 141
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 15600424 411 RQRLSLAVAVIHKPEILILDEPTSGVDP-----VARDgfwelMVELSRRDGVTIFISTH 464
Cdd:COG2401 142 KFRFRLALLLAERPKLLVIDEFCSHLDRqtakrVARN-----LQKLARRAGITLVVATH 195
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
14-202 |
1.17e-09 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 59.50 E-value: 1.17e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 14 VSLRY-GETRAVDDVSLEIPANRMVGLIGPDGVGKSSLLALLAGARKMQDGEIRVLDGDMRDRRHRRavcprIAYMPQGL 92
Cdd:PRK10908 7 VSKAYlGGRQALQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDITRLKNRE-----VPFLRRQI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 93 G-----KNLYPTLSVFENVDFFGRLFGHDKAERERRIADLLQSTGLAPFAERPAGKLSGGMKQKLGLCCALIHDPDLLIL 167
Cdd:PRK10908 82 GmifqdHHLLMDRTVYDNVAIPLIIAGASGDDIRRRVSAALDKVGLLDKAKNFPIQLSGGEQQRVGIARAVVNKPAVLLA 161
|
170 180 190
....*....|....*....|....*....|....*..
gi 15600424 168 DEPTTGVDplsrNQFWELIGRI--RAGREGMSVLVAT 202
Cdd:PRK10908 162 DEPTGNLD----DALSEGILRLfeEFNRVGVTVLMAT 194
|
|
| PRK13546 |
PRK13546 |
teichoic acids export ABC transporter ATP-binding subunit TagH; |
23-169 |
1.30e-09 |
|
teichoic acids export ABC transporter ATP-binding subunit TagH;
Pssm-ID: 184131 [Multi-domain] Cd Length: 264 Bit Score: 59.83 E-value: 1.30e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 23 AVDDVSLEIPANRMVGLIGPDGVGKSSLLALLAGARKMQDGEIRvLDGDMRdrrhrravcprIAYMPQGLGKNLyptlSV 102
Cdd:PRK13546 39 ALDDISLKAYEGDVIGLVGINGSGKSTLSNIIGGSLSPTVGKVD-RNGEVS-----------VIAISAGLSGQL----TG 102
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15600424 103 FENVDFFGRLFGHDKAERERRIADLLQSTGLAPFAERPAGKLSGGMKQKLGLCCALIHDPDLLILDE 169
Cdd:PRK13546 103 IENIEFKMLCMGFKRKEIKAMTPKIIEFSELGEFIYQPVKKYSSGMRAKLGFSINITVNPDILVIDE 169
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
302-487 |
1.34e-09 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 61.04 E-value: 1.34e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 302 IFGFLGSngcGKSTTMKMLTGLLPASEGTCALFGQPVDASDMAT-----RRRVGYMSQAFSLYAELSVRQNLvlharlfh 376
Cdd:PRK11144 29 IFGRSGA---GKTSLINAISGLTRPQKGRIVLNGRVLFDAEKGIclppeKRRIGYVFQDARLFPHYKVRGNL-------- 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 377 lpadgipaRVG---EMLRRFD-------LEKVADELPNDLPLGIRQRLSLAVAVIHKPEILILDEPTSGVD-PVARdgfw 445
Cdd:PRK11144 98 --------RYGmakSMVAQFDkivallgIEPLLDRYPGSLSGGEKQRVAIGRALLTAPELLLMDEPLASLDlPRKR---- 165
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 15600424 446 ELMV---ELSRRDGVTIFISTHFMNEAQR-CDRISLMHAGKVLASD 487
Cdd:PRK11144 166 ELLPyleRLAREINIPILYVSHSLDEILRlADRVVVLEQGKVKAFG 211
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
11-202 |
1.45e-09 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 59.34 E-value: 1.45e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 11 LRGVSLRYGETRAVDDVSLEIPANRMVGLIGPDGVGKSSLLALLAGARKMQDGEIrVLDGD----MRDRRHRRAVcpriA 86
Cdd:PRK10247 10 LQNVGYLAGDAKILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTL-LFEGEdistLKPEIYRQQV----S 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 87 YMPQGlgknlyPTL---SVFENVdFFGRLFGHDKAERERRIADLLQSTGLAPFAERPAGKLSGGMKQKLGLCCALIHDPD 163
Cdd:PRK10247 85 YCAQT------PTLfgdTVYDNL-IFPWQIRNQQPDPAIFLDDLERFALPDTILTKNIAELSGGEKQRISLIRNLQFMPK 157
|
170 180 190
....*....|....*....|....*....|....*....
gi 15600424 164 LLILDEPTTGVDPLSRNQFWELIGRIrAGREGMSVLVAT 202
Cdd:PRK10247 158 VLLLDEITSALDESNKHNVNEIIHRY-VREQNIAVLWVT 195
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
25-175 |
1.79e-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: 59.34 E-value: 1.79e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 25 DDVSLEIPA-----NRMVGLIGPDGVGKSSLLALLAGARKMQDGEIRVLdgdmrdrrhrravCPRIAYMPQGLgKNLYPT 99
Cdd:cd03237 11 GEFTLEVEGgsiseSEVIGILGPNGIGKTTFIKMLAGVLKPDEGDIEIE-------------LDTVSYKPQYI-KADYEG 76
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15600424 100 lsvfeNVDFFGRLFGHDKAERERRIADLLQSTGLAPFAERPAGKLSGGMKQKLGLCCALIHDPDLLILDEPTTGVD 175
Cdd:cd03237 77 -----TVRDLLSSITKDFYTHPYFKTEIAKPLQIEQILDREVPELSGGELQRVAIAACLSKDADIYLLDEPSAYLD 147
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
297-437 |
3.12e-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: 3.12e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 297 IERGEIFGFLGSNGCGKSTTMKMLTGLLPASEGTCALFGQpvdasdmatrrRVGYMSQAFSLYAELSVRQNLVlharlfh 376
Cdd:cd03237 22 ISESEVIGILGPNGIGKTTFIKMLAGVLKPDEGDIEIELD-----------TVSYKPQYIKADYEGTVRDLLS------- 83
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15600424 377 lpadGIPARVG-------EMLRRFDLEKVADELPNDLPLGIRQRLSLAVAVIHKPEILILDEPTSGVD 437
Cdd:cd03237 84 ----SITKDFYthpyfktEIAKPLQIEQILDREVPELSGGELQRVAIAACLSKDADIYLLDEPSAYLD 147
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
10-175 |
3.60e-09 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 58.40 E-value: 3.60e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 10 SLRGVSLRYGETRAVDDVSLEIPANRMVGLIGPDGVGKSSLLALLAGARKMQDGEI--RVLDGDMRD------RRHRRAV 81
Cdd:PRK11701 8 SVRGLTKLYGPRKGCRDVSFDLYPGEVLGIVGESGSGKTTLLNALSARLAPDAGEVhyRMRDGQLRDlyalseAERRRLL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 82 CPRIAYMPQGLGKNLYPTLSVFENVdffG-RLF--GHDKAERERRIA-DLLQSTGLAP--FAERPAgKLSGGMKQKLGLC 155
Cdd:PRK11701 88 RTEWGFVHQHPRDGLRMQVSAGGNI---GeRLMavGARHYGDIRATAgDWLERVEIDAarIDDLPT-TFSGGMQQRLQIA 163
|
170 180
....*....|....*....|
gi 15600424 156 CALIHDPDLLILDEPTTGVD 175
Cdd:PRK11701 164 RNLVTHPRLVFMDEPTGGLD 183
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
289-497 |
4.28e-09 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 60.11 E-value: 4.28e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 289 AVDHVSFRIERGEIFGFLGSNGCGKSTTMKMLTGLLPASEGTCALFGQPVDASDM-ATRRRVGYMSQAFSLYAElSVRQN 367
Cdd:PRK10789 330 ALENVNFTLKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGDIRFHDIPLTKLQLdSWRSRLAVVSQTPFLFSD-TVANN 408
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 368 LVL-------------------HARLFHLPaDGIPARVGE---MLRRfdlekvadelpndlplGIRQRLSLAVAVIHKPE 425
Cdd:PRK10789 409 IALgrpdatqqeiehvarlasvHDDILRLP-QGYDTEVGErgvMLSG----------------GQKQRISIARALLLNAE 471
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15600424 426 ILILDEPTSGVDPVARdgfWELMVELSR-RDGVTIFISTHFMNEAQRCDRISLMHAGKVLASDTPDELVRQRG 497
Cdd:PRK10789 472 ILILDDALSAVDGRTE---HQILHNLRQwGEGRTVIISAHRLSALTEASEILVMQHGHIAQRGNHDQLAQQSG 541
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
290-462 |
5.41e-09 |
|
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: 56.01 E-value: 5.41e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 290 VDHVSFRIERGEIFGFLGSNGCGKSTTMKMLTGLLPASEGTCalfgqpvdasDMATRRRVGYMSQAfSLYAELSVRQNLV 369
Cdd:cd03223 17 LKDLSFEIKPGDRLLITGPSGTGKSSLFRALAGLWPWGSGRI----------GMPEGEDLLFLPQR-PYLPLGTLREQLI 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 370 LharlfhlPADGIparvgemlrrfdlekvadelpndLPLGIRQRLSLAVAVIHKPEILILDEPTSGVDPVARDGFWELMV 449
Cdd:cd03223 86 Y-------PWDDV-----------------------LSGGEQQRLAFARLLLHKPKFVFLDEATSALDEESEDRLYQLLK 135
|
170
....*....|...
gi 15600424 450 ELSrrdgvTIFIS 462
Cdd:cd03223 136 ELG-----ITVIS 143
|
|
| ABC_UvrA_II |
cd03271 |
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair ... |
26-228 |
5.81e-09 |
|
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: 58.01 E-value: 5.81e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 26 DVSLEIPANRMVGLIGPDGVGKSSL--------LALLAGARKMQDGE------------IRVLDGDMRDRRHR------- 78
Cdd:cd03271 13 NIDVDIPLGVLTCVTGVSGSGKSSLindtlypaLARRLHLKKEQPGNhdrieglehidkVIVIDQSPIGRTPRsnpatyt 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 79 ------RA----VCPRIAYMPQGL-----GKNLYPTL--SVFENVDFFgrlfghDKAERERRIADLLQSTGLAPFA-ERP 140
Cdd:cd03271 93 gvfdeiRElfceVCKGKRYNRETLevrykGKSIADVLdmTVEEALEFF------ENIPKIARKLQTLCDVGLGYIKlGQP 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 141 AGKLSGGMKQKLGLCCALiHDPD----LLILDEPTTGVDPLSRNQFWELIGRIRAGreGMSVLVATAYMEEAERFDWLVA 216
Cdd:cd03271 167 ATTLSGGEAQRIKLAKEL-SKRStgktLYILDEPTTGLHFHDVKKLLEVLQRLVDK--GNTVVVIEHNLDVIKCADWIID 243
|
250
....*....|....*...
gi 15600424 217 M------DDGKVLATGTP 228
Cdd:cd03271 244 LgpeggdGGGQVVASGTP 261
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
5-171 |
6.44e-09 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 59.36 E-value: 6.44e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 5 GSGVASLRGVSLRYGETRAVDDVSLEIPANRMVGLIGPDGVGKSSLLALLAGARKMQDGEIRVldGDmrdrrhrrAVcpR 84
Cdd:PRK11819 321 GDKVIEAENLSKSFGDRLLIDDLSFSLPPGGIVGIIGPNGAGKSTLFKMITGQEQPDSGTIKI--GE--------TV--K 388
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 85 IAYMPQGLGkNLYPTLSVFENV-DffgrlfGHD-----KAERERRiadllqsTGLAPFA------ERPAGKLSGGMKQKL 152
Cdd:PRK11819 389 LAYVDQSRD-ALDPNKTVWEEIsG------GLDiikvgNREIPSR-------AYVGRFNfkggdqQKKVGVLSGGERNRL 454
|
170
....*....|....*....
gi 15600424 153 GLCCALIHDPDLLILDEPT 171
Cdd:PRK11819 455 HLAKTLKQGGNVLLLDEPT 473
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
293-481 |
9.38e-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: 59.54 E-value: 9.38e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 293 VSFRIERGEIFGFLGSNGCGKSTTMKMLTGLLPASEGTCALFGqpvdasdmatrrRVGYMSQaFSLYAELSVRQNLvlha 372
Cdd:TIGR01271 445 ISFKLEKGQLLAVAGSTGSGKSSLLMMIMGELEPSEGKIKHSG------------RISFSPQ-TSWIMPGTIKDNI---- 507
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 373 rLFHLPADGIpaRVGEMLRRFDLEKVADELPN--DLPL---------GIRQRLSLAVAVIHKPEILILDEPTSGVDPVAR 441
Cdd:TIGR01271 508 -IFGLSYDEY--RYTSVIKACQLEEDIALFPEkdKTVLgeggitlsgGQRARISLARAVYKDADLYLLDSPFTHLDVVTE 584
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 15600424 442 DGFWE-----LMVELSRrdgvtiFISTHFMNEAQRCDRISLMHAG 481
Cdd:TIGR01271 585 KEIFEsclckLMSNKTR------ILVTSKLEHLKKADKILLLHEG 623
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
21-171 |
1.01e-08 |
|
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440858 [Multi-domain] Cd Length: 592 Bit Score: 59.03 E-value: 1.01e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 21 TRAVDDVSLEIPANRM-----VGLIGPDGVGKSSLLALLAGARKMQDGEIrvlDGDMRdrrhrravcprIAYMPQglgkn 95
Cdd:COG1245 348 TKSYGGFSLEVEGGEIregevLGIVGPNGIGKTTFAKILAGVLKPDEGEV---DEDLK-----------ISYKPQ----- 408
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15600424 96 lYPTLSVFENVDFFgrLFGHDKAERERRI--ADLLQSTGLAPFAERPAGKLSGGMKQKLGLCCALIHDPDLLILDEPT 171
Cdd:COG1245 409 -YISPDYDGTVEEF--LRSANTDDFGSSYykTEIIKPLGLEKLLDKNVKDLSGGELQRVAIAACLSRDADLYLLDEPS 483
|
|
| SapD |
COG4170 |
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms]; |
19-199 |
1.02e-08 |
|
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms];
Pssm-ID: 443330 [Multi-domain] Cd Length: 331 Bit Score: 57.99 E-value: 1.02e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 19 GETRAVDDVSLEIPANRMVGLIGPDGVGKSSLLALLAGARK---------MQDGEIRVLDGDMRDRRhrRAVCPRIAYMP 89
Cdd:COG4170 18 GRVKAVDRVSLTLNEGEIRGLVGESGSGKSLIAKAICGITKdnwhvtadrFRWNGIDLLKLSPRERR--KIIGREIAMIF 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 90 QGLGKNLYPTLSVFENV------DFFGRLFGHDKAERERRIADLLQSTGLA---------PFaerpagKLSGGMKQKLGL 154
Cdd:COG4170 96 QEPSSCLDPSAKIGDQLieaipsWTFKGKWWQRFKWRKKRAIELLHRVGIKdhkdimnsyPH------ELTEGECQKVMI 169
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 15600424 155 CCALIHDPDLLILDEPTTGVDPLSRNQFWELIGRIRAGReGMSVL 199
Cdd:COG4170 170 AMAIANQPRLLIADEPTNAMESTTQAQIFRLLARLNQLQ-GTSIL 213
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
22-175 |
1.06e-08 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 58.05 E-value: 1.06e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 22 RAVDDVSLEIPANRMVGLIGPDGVGKSSLLALLAGARKMQDGEIR-----VLDGDMRDRRHRR------------AVCPR 84
Cdd:PRK11308 29 KALDGVSFTLERGKTLAVVGESGCGKSTLARLLTMIETPTGGELYyqgqdLLKADPEAQKLLRqkiqivfqnpygSLNPR 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 85 iaympQGLGKNLYPTLSVfeNVDFfgrlfghDKAERERRIADLLQSTGLAP-FAERPAGKLSGGMKQKLGLCCALIHDPD 163
Cdd:PRK11308 109 -----KKVGQILEEPLLI--NTSL-------SAAERREKALAMMAKVGLRPeHYDRYPHMFSGGQRQRIAIARALMLDPD 174
|
170
....*....|..
gi 15600424 164 LLILDEPTTGVD 175
Cdd:PRK11308 175 VVVADEPVSALD 186
|
|
| CP_lyasePhnK |
TIGR02323 |
phosphonate C-P lyase system protein PhnK; Members of this family are the PhnK protein of C-P ... |
10-226 |
1.43e-08 |
|
phosphonate C-P lyase system protein PhnK; Members of this family are the PhnK protein of C-P lyase systems for utilization of phosphonates. These systems resemble phosphonatase-based systems in having a three component ABC transporter, where TIGR01097 is the permease, TIGR01098 is the phosphonates binding protein, and TIGR02315 is the ATP-binding cassette (ABC) protein. They differ, however, in having, typically, ten or more additional genes, many of which are believed to form a membrane-associated complex. This protein (PhnK) and the adjacent-encoded PhnL resemble transporter ATP-binding proteins but are suggested, based on mutatgenesis studies, to be part of this complex rather than part of a transporter per se. [Central intermediary metabolism, Phosphorus compounds]
Pssm-ID: 188208 [Multi-domain] Cd Length: 253 Bit Score: 56.76 E-value: 1.43e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 10 SLRGVSLRYGETRAVDDVSLEIPANRMVGLIGPDGVGKSSLLALLAGARKMQDGEIRVLDGD--------MRDRRHRRAV 81
Cdd:TIGR02323 5 QVSGLSKSYGGGKGCRDVSFDLYPGEVLGIVGESGSGKSTLLGCLAGRLAPDHGTATYIMRSgaelelyqLSEAERRRLM 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 82 CPRIAYMPQGLGKNLYPTLSVFENV-----DFFGRLFGHDKAERErriaDLLQSTGLAP--FAERPAgKLSGGMKQKLGL 154
Cdd:TIGR02323 85 RTEWGFVHQNPRDGLRMRVSAGANIgerlmAIGARHYGNIRATAQ----DWLEEVEIDPtrIDDLPR-AFSGGMQQRLQI 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15600424 155 CCALIHDPDLLILDEPTTGVDPLSRNQFWELIGRIRagRE-GMSVLVATAYMEEAERF-DWLVAMDDGKVLATG 226
Cdd:TIGR02323 160 ARNLVTRPRLVFMDEPTGGLDVSVQARLLDLLRGLV--RDlGLAVIIVTHDLGVARLLaQRLLVMQQGRVVESG 231
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
21-248 |
1.52e-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: 1.52e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 21 TRAVDDVSLEIPANRMVGLIGPDGVGKSSLLALLAGARKMQDGEIRvldgdmrdRRHRRAVCPRIAY-MPQGLGKNLypt 99
Cdd:TIGR01271 439 TPVLKNISFKLEKGQLLAVAGSTGSGKSSLLMMIMGELEPSEGKIK--------HSGRISFSPQTSWiMPGTIKDNI--- 507
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 100 lsvfenvdffgrLFGHDKAE-RERRIADLLQ-STGLAPFAER---PAGK----LSGGMKQKLGLCCALIHDPDLLILDEP 170
Cdd:TIGR01271 508 ------------IFGLSYDEyRYTSVIKACQlEEDIALFPEKdktVLGEggitLSGGQRARISLARAVYKDADLYLLDSP 575
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 171 TTGVDPLSRNQFWE------LIGRIRagregmsvLVATAYMEEAERFDWLVAMDDGKVLATGTPQELrertgtQSLESAF 244
Cdd:TIGR01271 576 FTHLDVVTEKEIFEsclcklMSNKTR--------ILVTSKLEHLKKADKILLLHEGVCYFYGTFSEL------QAKRPDF 641
|
....
gi 15600424 245 IALL 248
Cdd:TIGR01271 642 SSLL 645
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
6-175 |
1.83e-08 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 58.04 E-value: 1.83e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 6 SG--VASLRGVSLRYGETRAVDDVSLEIPANRMVGLIGPDGVGKSSLLALLAGARKMQDGEIRV---LDgdmrdrrhrra 80
Cdd:PRK11147 315 SGkiVFEMENVNYQIDGKQLVKDFSAQVQRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRIHCgtkLE----------- 383
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 81 vcprIAYMPQgLGKNLYPTLSVFENVdffgrlfGHDKAE-----RERRIADLLQSTGLAPF-AERPAGKLSGGMKQKLGL 154
Cdd:PRK11147 384 ----VAYFDQ-HRAELDPEKTVMDNL-------AEGKQEvmvngRPRHVLGYLQDFLFHPKrAMTPVKALSGGERNRLLL 451
|
170 180
....*....|....*....|.
gi 15600424 155 CCALIHDPDLLILDEPTTGVD 175
Cdd:PRK11147 452 ARLFLKPSNLLILDEPTNDLD 472
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
258-492 |
1.91e-08 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 58.60 E-value: 1.91e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 258 RLVIPPRPQSEGAPRIAIeaegltcRFGDFV--------AVDHVSFRIERGEIFGFLGSNGCGKSTTMKMLTGLLPA-SE 328
Cdd:PLN03130 600 RVLLPNPPLEPGLPAISI-------KNGYFSwdskaerpTLSNINLDVPVGSLVAIVGSTGEGKTSLISAMLGELPPrSD 672
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 329 GTCALfgqpvdasdmatRRRVGYMSQAfSLYAELSVRQNLvlharLFHLPADgiPARVGEMLRRFDLEKVADELPN---- 404
Cdd:PLN03130 673 ASVVI------------RGTVAYVPQV-SWIFNATVRDNI-----LFGSPFD--PERYERAIDVTALQHDLDLLPGgdlt 732
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 405 -------DLPLGIRQRLSLAVAVIHKPEILILDEPTSGVDP-VARDGFWE-LMVELSRRDGVTIFISTHFMNeaqRCDRI 475
Cdd:PLN03130 733 eigergvNISGGQKQRVSMARAVYSNSDVYIFDDPLSALDAhVGRQVFDKcIKDELRGKTRVLVTNQLHFLS---QVDRI 809
|
250
....*....|....*..
gi 15600424 476 SLMHAGKVLASDTPDEL 492
Cdd:PLN03130 810 ILVHEGMIKEEGTYEEL 826
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
5-220 |
2.07e-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: 2.07e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 5 GSGVASLRGVSLRygetravddvsleIPANRMVGLIGPDGVGKSSLLALLAGARKMQDGEI-------RVLDGDMRDRRH 77
Cdd:cd03290 11 GSGLATLSNINIR-------------IPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVhwsnkneSEPSFEATRSRN 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 78 RRAVcpriAYMPQglgKNLYPTLSVFENVDfFGRLFGHDKAERERRIADLLQSTGLAPFAERP-----AGKLSGGMKQKL 152
Cdd:cd03290 78 RYSV----AYAAQ---KPWLLNATVEENIT-FGSPFNKQRYKAVTDACSLQPDIDLLPFGDQTeigerGINLSGGQRQRI 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15600424 153 GLCCALIHDPDLLILDEPTTGVD-PLSRNQFWELIGRIRAGREGMSVLVaTAYMEEAERFDWLVAMDDG 220
Cdd:cd03290 150 CVARALYQNTNIVFLDDPFSALDiHLSDHLMQEGILKFLQDDKRTLVLV-THKLQYLPHADWIIAMKDG 217
|
|
| PRK13546 |
PRK13546 |
teichoic acids export ABC transporter ATP-binding subunit TagH; |
286-483 |
2.14e-08 |
|
teichoic acids export ABC transporter ATP-binding subunit TagH;
Pssm-ID: 184131 [Multi-domain] Cd Length: 264 Bit Score: 56.36 E-value: 2.14e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 286 DFVAVDHVSFRIERGEIFGFLGSNGCGKSTTMKMLTGLLPASEGTCALFGQpvdasdmatrrrVGYMSQAFSLYAELSVR 365
Cdd:PRK13546 36 TFFALDDISLKAYEGDVIGLVGINGSGKSTLSNIIGGSLSPTVGKVDRNGE------------VSVIAISAGLSGQLTGI 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 366 QNLVLHARLFHLPADGIPARVGEMLRRFDLEKVADELPNDLPLGIRQRLSLAVAVIHKPEILILDEPTSGVDPVARDGFW 445
Cdd:PRK13546 104 ENIEFKMLCMGFKRKEIKAMTPKIIEFSELGEFIYQPVKKYSSGMRAKLGFSINITVNPDILVIDEALSVGDQTFAQKCL 183
|
170 180 190
....*....|....*....|....*....|....*....
gi 15600424 446 ELMVELSRRDGvTIFISTHFMNEAQR-CDRISLMHAGKV 483
Cdd:PRK13546 184 DKIYEFKEQNK-TIFFVSHNLGQVRQfCTKIAWIEGGKL 221
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
6-237 |
2.30e-08 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 58.45 E-value: 2.30e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 6 SGVASLRGVSLRY--GETRAVDDVSLEIPANRMVGLIGPDGVGKSSLLALLAGARKMQDGEIRVLDGD-----MRDRRHR 78
Cdd:PLN03232 1232 RGSIKFEDVHLRYrpGLPPVLHGLSFFVSPSEKVGVVGRTGAGKSSMLNALFRIVELEKGRIMIDDCDvakfgLTDLRRV 1311
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 79 RAVCPRIAYMPQGlgknlyptlSVFENVDFFGRLFGHD--KAERERRIADLLQSTGLAPFAERPAG--KLSGGMKQKLGL 154
Cdd:PLN03232 1312 LSIIPQSPVLFSG---------TVRFNIDPFSEHNDADlwEALERAHIKDVIDRNPFGLDAEVSEGgeNFSVGQRQLLSL 1382
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 155 CCALIHDPDLLILDEPTTGVDPLSRNqfweLIGR-IRAGREGMSVLVATAYMEEAERFDWLVAMDDGKVLATGTPQELRE 233
Cdd:PLN03232 1383 ARALLRRSKILVLDEATASVDVRTDS----LIQRtIREEFKSCTMLVIAHRLNTIIDCDKILVLSSGQVLEYDSPQELLS 1458
|
....
gi 15600424 234 RTGT 237
Cdd:PLN03232 1459 RDTS 1462
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
278-498 |
2.68e-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: 58.00 E-value: 2.68e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 278 EGLTCRF--GDFVAVDHVSFRIERGEIFGFLGSNGCGKSTTMKMLTGLLpASEGTCALFGQPVDASDMAT-RRRVGYMSQ 354
Cdd:TIGR01271 1221 QGLTAKYteAGRAVLQDLSFSVEGGQRVGLLGRTGSGKSTLLSALLRLL-STEGEIQIDGVSWNSVTLQTwRKAFGVIPQ 1299
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 355 AFSLYAElSVRQNLVLHARLfhlpADGIPARVGEmlrRFDLEKVADELPNDLPL-----------GIRQRLSLAVAVIHK 423
Cdd:TIGR01271 1300 KVFIFSG-TFRKNLDPYEQW----SDEEIWKVAE---EVGLKSVIEQFPDKLDFvlvdggyvlsnGHKQLMCLARSILSK 1371
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 424 PEILILDEPTSGVDPVArdgfwelmVELSRR------DGVTIFISTHFMNEAQRCDRISLMHAGKVLASDTPDELVRQRG 497
Cdd:TIGR01271 1372 AKILLLDEPSAHLDPVT--------LQIIRKtlkqsfSNCTVILSEHRVEALLECQQFLVIEGSSVKQYDSIQKLLNETS 1443
|
.
gi 15600424 498 L 498
Cdd:TIGR01271 1444 L 1444
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
30-171 |
2.80e-08 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 57.51 E-value: 2.80e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 30 EIPANRMVGLIGPDGVGKSSLLALLAGARKMQDGEIrvlDGDmrdrrhrravcPRIAYMPQglgknlYPTLSVFENVDFF 109
Cdd:PRK13409 361 EIYEGEVIGIVGPNGIGKTTFAKLLAGVLKPDEGEV---DPE-----------LKISYKPQ------YIKPDYDGTVEDL 420
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15600424 110 grLfghdkaereRRIADLLQST----------GLAPFAERPAGKLSGGMKQKLGLCCALIHDPDLLILDEPT 171
Cdd:PRK13409 421 --L---------RSITDDLGSSyykseiikplQLERLLDKNVKDLSGGELQRVAIAACLSRDADLYLLDEPS 481
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
10-222 |
5.18e-08 |
|
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette transporters; The pleiotropic drug resistance (PDR) is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. This PDR subfamily represents domain I of its (ABC-IM)2 organization. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds including sugars, ions, peptides, and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213200 [Multi-domain] Cd Length: 202 Bit Score: 54.19 E-value: 5.18e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 10 SLRGVSLRYGETRA----VDDVSLEIPANRMVGLIGPDGVGKSSLLALLAGARKMQ---DGEIRV--LDGDMRDRRHRRa 80
Cdd:cd03233 5 SWRNISFTTGKGRSkipiLKDFSGVVKPGEMVLVLGRPGSGCSTLLKALANRTEGNvsvEGDIHYngIPYKEFAEKYPG- 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 81 vcpRIAYMPQglGKNLYPTLSVFENVDFFGRLFGHDKAErerriadllqstglapfaerpagKLSGGMKQKLGLCCALIH 160
Cdd:cd03233 84 ---EIIYVSE--EDVHFPTLTVRETLDFALRCKGNEFVR-----------------------GISGGERKRVSIAEALVS 135
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15600424 161 DPDLLILDEPTTGVDPLSRNQFWELIgRIRAGREGMSVLVAT--AYMEEAERFDWLVAMDDGKV 222
Cdd:cd03233 136 RASVLCWDNSTRGLDSSTALEILKCI-RTMADVLKTTTFVSLyqASDEIYDLFDKVLVLYEGRQ 198
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
26-255 |
6.63e-08 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 56.71 E-value: 6.63e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 26 DVSLEIPANRMVGLIGPDGVGKSSLLALLAGARKMQDGEIrvldgdMRDRrhrravcpRIAYMPQglgKNLYPTLSVFEN 105
Cdd:PTZ00243 678 DVSVSVPRGKLTVVLGATGSGKSTLLQSLLSQFEISEGRV------WAER--------SIAYVPQ---QAWIMNATVRGN 740
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 106 VDFFgrlfghdKAERERRIADLLQSTGL-APFAERPAG----------KLSGGMKQKLGLCCALIHDPDLLILDEPTTGV 174
Cdd:PTZ00243 741 ILFF-------DEEDAARLADAVRVSQLeADLAQLGGGleteigekgvNLSGGQKARVSLARAVYANRDVYLLDDPLSAL 813
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 175 DPLSRNQFWE--LIGRIRagreGMSVLVATAYMEEAERFDWLVAMDDGKVLATGTPQELRErtgtQSLESAFIALLPESK 252
Cdd:PTZ00243 814 DAHVGERVVEecFLGALA----GKTRVLATHQVHVVPRADYVVALGDGRVEFSGSSADFMR----TSLYATLAAELKENK 885
|
...
gi 15600424 253 RAG 255
Cdd:PTZ00243 886 DSK 888
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
272-437 |
7.00e-08 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 56.05 E-value: 7.00e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 272 RIAIEAEGLTCRFGDFVAVDHVSFRIERGEIFGFLGSNGCGKSTTMKMLTGLLPASEGTcalfgqpVDASDMAtrrRVGY 351
Cdd:PRK15064 317 RNALEVENLTKGFDNGPLFKNLNLLLEAGERLAIIGENGVGKTTLLRTLVGELEPDSGT-------VKWSENA---NIGY 386
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 352 MSQafSLYAELSVRQNLVLHARLFHLPADG---IPARVGEMLrrF---DLEKVADELPNdlplGIRQRLSLAVAVIHKPE 425
Cdd:PRK15064 387 YAQ--DHAYDFENDLTLFDWMSQWRQEGDDeqaVRGTLGRLL--FsqdDIKKSVKVLSG----GEKGRMLFGKLMMQKPN 458
|
170
....*....|..
gi 15600424 426 ILILDEPTSGVD 437
Cdd:PRK15064 459 VLVMDEPTNHMD 470
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
41-176 |
7.52e-08 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 54.08 E-value: 7.52e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 41 GPDGVGKSSLLALLAGARKMQDGEIRVlDGDMRDRRHRRAVCPRIAYMPqglgkNLYPTLSVFENVDFFGRLFGHdkaeR 120
Cdd:PRK13543 44 GDNGAGKTTLLRVLAGLLHVESGQIQI-DGKTATRGDRSRFMAYLGHLP-----GLKADLSTLENLHFLCGLHGR----R 113
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 15600424 121 ERRI-ADLLQSTGLAPFAERPAGKLSGGMKQKLGLCCALIHDPDLLILDEPTTGVDP 176
Cdd:PRK13543 114 AKQMpGSALAIVGLAGYEDTLVRQLSAGQKKRLALARLWLSPAPLWLLDEPYANLDL 170
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
10-186 |
7.61e-08 |
|
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: 52.93 E-value: 7.61e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 10 SLRGVSLRYGETRA-VDDVSLEIPANRMVGLIGPDGVGKSSLLALLAGARKMQDGEIRvldgdmRDRRHRRAVCPRIAYM 88
Cdd:cd03223 2 ELENLSLATPDGRVlLKDLSFEIKPGDRLLITGPSGTGKSSLFRALAGLWPWGSGRIG------MPEGEDLLFLPQRPYL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 89 PQGlgknlypTLsvfenvdffgrlfghdkaeRERRIadllqstglapfaeRPAGK-LSGGMKQKLGLCCALIHDPDLLIL 167
Cdd:cd03223 76 PLG-------TL-------------------REQLI--------------YPWDDvLSGGEQQRLAFARLLLHKPKFVFL 115
|
170
....*....|....*....
gi 15600424 168 DEPTTGVDPLSRNQFWELI 186
Cdd:cd03223 116 DEATSALDEESEDRLYQLL 134
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
293-496 |
8.52e-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: 8.52e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 293 VSFRIERGEIFGFLGSNGCGKSTTMKMLTGLLPASEGTCALFGqpvdasdmatrrRVGYMSQaFSLYAELSVRQNLVlha 372
Cdd:cd03291 56 INLKIEKGEMLAITGSTGSGKTSLLMLILGELEPSEGKIKHSG------------RISFSSQ-FSWIMPGTIKENII--- 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 373 rlFHLPADgiPARVGEMLRRFDLEKVADELPN-----------DLPLGIRQRLSLAVAVIHKPEILILDEPTSGVDPVAR 441
Cdd:cd03291 120 --FGVSYD--EYRYKSVVKACQLEEDITKFPEkdntvlgeggiTLSGGQRARISLARAVYKDADLYLLDSPFGYLDVFTE 195
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 442 DGFWE-----LMVELSRrdgvtiFISTHFMNEAQRCDRISLMHAGKVLASDTPDELVRQR 496
Cdd:cd03291 196 KEIFEscvckLMANKTR------ILVTSKMEHLKKADKILILHEGSSYFYGTFSELQSLR 249
|
|
| 3a01203 |
TIGR00954 |
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ... |
288-464 |
8.68e-08 |
|
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: 55.91 E-value: 8.68e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 288 VAVDHVSFRIERGEIFGFLGSNGCGKSTTMKMLTGLLPASEGT------CALFGQPvdasdmatrrRVGYMSQAfslyae 361
Cdd:TIGR00954 466 VLIESLSFEVPSGNNLLICGPNGCGKSSLFRILGELWPVYGGRltkpakGKLFYVP----------QRPYMTLG------ 529
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 362 lSVRQNLVLharlfhlpadgiPARVGEMLRR----FDLEKVADELPND------------------LPLGIRQRLSLAVA 419
Cdd:TIGR00954 530 -TLRDQIIY------------PDSSEDMKRRglsdKDLEQILDNVQLThilereggwsavqdwmdvLSGGEKQRIAMARL 596
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 15600424 420 VIHKPEILILDEPTSGVDPVARDGfwelMVELSRRDGVTIFISTH 464
Cdd:TIGR00954 597 FYHKPQFAILDECTSAVSVDVEGY----MYRLCREFGITLFSVSH 637
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
261-497 |
1.06e-07 |
|
multi drug resistance-associated protein (MRP); This model describes multi drug resistance-associated protein (MRP) in eukaryotes. The multidrug resistance-associated protein is an integral membrane protein that causes multidrug resistance when overexpressed in mammalian cells. It belongs to ABC transporter superfamily. The protein topology and function was experimentally demonstrated by epitope tagging and immunofluorescence. Insertion of tags in the critical regions associated with drug efflux, abrogated its function. The C-terminal domain seem to highly conserved. [Transport and binding proteins, Other]
Pssm-ID: 188098 [Multi-domain] Cd Length: 1522 Bit Score: 56.11 E-value: 1.06e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 261 IPPRPQSEGAPR-IAIEAEGLTCRFGDFVAVDHVSFRIERGEIFGFLGSNGCGKSTTMKMLTGLLPASEGTCALFGQpvd 339
Cdd:TIGR00957 624 IERRTIKPGEGNsITVHNATFTWARDLPPTLNGITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVHMKGS--- 700
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 340 asdmatrrrVGYMSQAfSLYAELSVRQNLVLHARLFH------LPADGIPARVgEMLRRFDLEKVADELPNdLPLGIRQR 413
Cdd:TIGR00957 701 ---------VAYVPQQ-AWIQNDSLRENILFGKALNEkyyqqvLEACALLPDL-EILPSGDRTEIGEKGVN-LSGGQKQR 768
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 414 LSLAVAVIHKPEILILDEPTSGVDP-VARDGFWELMVELSRRDGVTIFISTHFMNEAQRCDRISLMHAGKVLASDTPDEL 492
Cdd:TIGR00957 769 VSLARAVYSNADIYLFDDPLSAVDAhVGKHIFEHVIGPEGVLKNKTRILVTHGISYLPQVDVIIVMSGGKISEMGSYQEL 848
|
....*
gi 15600424 493 VRQRG 497
Cdd:TIGR00957 849 LQRDG 853
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
280-437 |
1.50e-07 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 55.18 E-value: 1.50e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 280 LTCRFGDFVAVDHVSFRIERGEIFGFLGSNGCGKSTTMKMLTGLLPASEGTCALFG--------QPVDASDMATRRRVGY 351
Cdd:PRK10636 7 LQIRRGVRVLLDNATATINPGQKVGLVGKNGCGKSTLLALLKNEISADGGSYTFPGnwqlawvnQETPALPQPALEYVID 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 352 MSQAF-SLYAELSV--RQN-----LVLHARLFHLPADGIPARVGEMLRRFDLEKVADELP-NDLPLGIRQRLSLAVAVIH 422
Cdd:PRK10636 87 GDREYrQLEAQLHDanERNdghaiATIHGKLDAIDAWTIRSRAASLLHGLGFSNEQLERPvSDFSGGWRMRLNLAQALIC 166
|
170
....*....|....*
gi 15600424 423 KPEILILDEPTSGVD 437
Cdd:PRK10636 167 RSDLLLLDEPTNHLD 181
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
14-175 |
1.60e-07 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 55.18 E-value: 1.60e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 14 VSLRYGETRAVDDVSLE-IPANRmVGLIGPDGVGKSSLLALLAGARKMQDGEIRVLDGdmrdrrhrravcPRIAYMPQGL 92
Cdd:PRK10636 318 VSAGYGDRIILDSIKLNlVPGSR-IGLLGRNGAGKSTLIKLLAGELAPVSGEIGLAKG------------IKLGYFAQHQ 384
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 93 GKNLYPTLSVFENVdffGRLfghDKAERERRIADLLQSTGL-APFAERPAGKLSGGMKQKLGLCCALIHDPDLLILDEPT 171
Cdd:PRK10636 385 LEFLRADESPLQHL---ARL---APQELEQKLRDYLGGFGFqGDKVTEETRRFSGGEKARLVLALIVWQRPNLLLLDEPT 458
|
....
gi 15600424 172 TGVD 175
Cdd:PRK10636 459 NHLD 462
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
275-498 |
1.65e-07 |
|
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: 53.70 E-value: 1.65e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 275 IEAEGLTCRF--GDFVAVDHVSFRIERGEIFGFLGSNGCGKSTTMKMLTGLLpASEGTCALFGQPVDASDMAT-RRRVGY 351
Cdd:cd03289 3 MTVKDLTAKYteGGNAVLENISFSISPGQRVGLLGRTGSGKSTLLSAFLRLL-NTEGDIQIDGVSWNSVPLQKwRKAFGV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 352 MSQAFSLYAElSVRQNLVLHARLfhlpADGIPARVGEmlrRFDLEKVADELPNDLPL-----------GIRQRLSLAVAV 420
Cdd:cd03289 82 IPQKVFIFSG-TFRKNLDPYGKW----SDEEIWKVAE---EVGLKSVIEQFPGQLDFvlvdggcvlshGHKQLMCLARSV 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 421 IHKPEILILDEPTSGVDPVArdgfwelmVELSRR------DGVTIFISTHFMNEAQRCDRISLMHAGKVLASDTPDELVR 494
Cdd:cd03289 154 LSKAKILLLDEPSAHLDPIT--------YQVIRKtlkqafADCTVILSEHRIEAMLECQRFLVIEENKVRQYDSIQKLLN 225
|
....
gi 15600424 495 QRGL 498
Cdd:cd03289 226 EKSH 229
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
26-248 |
1.84e-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: 53.71 E-value: 1.84e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 26 DVSLEIPANRMVGLIGPDGVGKSSLLALLAGARKMQDGEIRvldgdmrdRRHRRAVCPRIAYMPQGlgknlyptlSVFEN 105
Cdd:cd03291 55 NINLKIEKGEMLAITGSTGSGKTSLLMLILGELEPSEGKIK--------HSGRISFSSQFSWIMPG---------TIKEN 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 106 VdffgrLFGHDKAE-RERRIADLLQ-STGLAPFAER---PAGK----LSGGMKQKLGLCCALIHDPDLLILDEPTTGVDP 176
Cdd:cd03291 118 I-----IFGVSYDEyRYKSVVKACQlEEDITKFPEKdntVLGEggitLSGGQRARISLARAVYKDADLYLLDSPFGYLDV 192
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15600424 177 LSRNQFWE-LIGRIRAGRegMSVLVaTAYMEEAERFDWLVAMDDGKVLATGTPQELrertgtQSLESAFIALL 248
Cdd:cd03291 193 FTEKEIFEsCVCKLMANK--TRILV-TSKMEHLKKADKILILHEGSSYFYGTFSEL------QSLRPDFSSKL 256
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
22-231 |
2.68e-07 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 52.91 E-value: 2.68e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 22 RAVDDVSLEIPANRMVGLIGPDGVGKSSLLALLAG--ARKMQDGEIRV-----LDGD-MRDRRHRRAVCPRiAYMPQGlG 93
Cdd:PRK13547 15 AILRDLSLRIEPGRVTALLGRNGAGKSTLLKALAGdlTGGGAPRGARVtgdvtLNGEpLAAIDAPRLARLR-AVLPQA-A 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 94 KNLYPtLSVFENVdFFGRlFGHDK-----AERERRIAD-LLQSTGLAPFAERPAGKLSGGMKQKLGLCCAL--------- 158
Cdd:PRK13547 93 QPAFA-FSAREIV-LLGR-YPHARragalTHRDGEIAWqALALAGATALVGRDVTTLSGGELARVQFARVLaqlwpphda 169
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15600424 159 IHDPDLLILDEPTTGVDPLSRNQFWELIGRI-RAGREGMSVLVATAYMeEAERFDWLVAMDDGKVLATGTPQEL 231
Cdd:PRK13547 170 AQPPRYLLLDEPTAALDLAHQHRLLDTVRRLaRDWNLGVLAIVHDPNL-AARHADRIAMLADGAIVAHGAPADV 242
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
26-231 |
2.85e-07 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 54.60 E-value: 2.85e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 26 DVSLEIPANRMVGLIGPDGVGKSSLLALLAGARKMQDGEIRVLDGDmrdrrhrravcprIAYMPQglgKNLYPTLSVFEN 105
Cdd:PLN03232 635 DINLEIPVGSLVAIVGGTGEGKTSLISAMLGELSHAETSSVVIRGS-------------VAYVPQ---VSWIFNATVREN 698
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 106 VdffgrLFGHD-KAERERRIA---------DLLQSTGLAPFAERPAgKLSGGMKQKLGLCCALIHDPDLLILDEPTTGVD 175
Cdd:PLN03232 699 I-----LFGSDfESERYWRAIdvtalqhdlDLLPGRDLTEIGERGV-NISGGQKQRVSMARAVYSNSDIYIFDDPLSALD 772
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 15600424 176 PLSRNQFWEliGRIRAGREGMSVLVATAYMEEAERFDWLVAMDDGKVLATGTPQEL 231
Cdd:PLN03232 773 AHVAHQVFD--SCMKDELKGKTRVLVTNQLHFLPLMDRIILVSEGMIKEEGTFAEL 826
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
6-236 |
3.34e-07 |
|
multi drug resistance-associated protein (MRP); This model describes multi drug resistance-associated protein (MRP) in eukaryotes. The multidrug resistance-associated protein is an integral membrane protein that causes multidrug resistance when overexpressed in mammalian cells. It belongs to ABC transporter superfamily. The protein topology and function was experimentally demonstrated by epitope tagging and immunofluorescence. Insertion of tags in the critical regions associated with drug efflux, abrogated its function. The C-terminal domain seem to highly conserved. [Transport and binding proteins, Other]
Pssm-ID: 188098 [Multi-domain] Cd Length: 1522 Bit Score: 54.57 E-value: 3.34e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 6 SGVASLRGVSLRYGETR--AVDDVSLEIPANRMVGLIGPDGVGKSSLLALLAGARKMQDGEIRVlDG------DMRDRRH 77
Cdd:TIGR00957 1282 RGRVEFRNYCLRYREDLdlVLRHINVTIHGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIII-DGlniakiGLHDLRF 1360
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 78 RRAVCPRIAYMPQGlgknlyptlSVFENVDFFGRLfghdkaeRERRIADLLQSTGLAPF-AERPAG----------KLSG 146
Cdd:TIGR00957 1361 KITIIPQDPVLFSG---------SLRMNLDPFSQY-------SDEEVWWALELAHLKTFvSALPDKldhecaeggeNLSV 1424
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 147 GMKQKLGLCCALIHDPDLLILDEPTTGVDPLSRNqfweLI-GRIRAGREGMSVLVATAYMEEAERFDWLVAMDDGKVLAT 225
Cdd:TIGR00957 1425 GQRQLVCLARALLRKTKILVLDEATAAVDLETDN----LIqSTIRTQFEDCTVLTIAHRLNTIMDYTRVIVLDKGEVAEF 1500
|
250
....*....|.
gi 15600424 226 GTPQELRERTG 236
Cdd:TIGR00957 1501 GAPSNLLQQRG 1511
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
284-462 |
5.84e-07 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 53.42 E-value: 5.84e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 284 FGDFVAVDHVSFRIERGEIFGFLGSNGCGKSTTMKMLTGLLPASEgtcalfGQPVDASDMATRRR--------------- 348
Cdd:PRK11147 13 FSDAPLLDNAELHIEDNERVCLVGRNGAGKSTLMKILNGEVLLDD------GRIIYEQDLIVARLqqdpprnvegtvydf 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 349 ----VGYMSQAFSLYAELSVR-------QNL----VLHARLFHLPADGIPARVGEMLRRFDLEkvADELPNDLPLGIRQR 413
Cdd:PRK11147 87 vaegIEEQAEYLKRYHDISHLvetdpseKNLnelaKLQEQLDHHNLWQLENRINEVLAQLGLD--PDAALSSLSGGWLRK 164
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 15600424 414 LSLAVAVIHKPEILILDEPTSGVDPVARDGFWELMVELSrrdGVTIFIS 462
Cdd:PRK11147 165 AALGRALVSNPDVLLLDEPTNHLDIETIEWLEGFLKTFQ---GSIIFIS 210
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
19-231 |
6.48e-07 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 53.59 E-value: 6.48e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 19 GETRAVDDVSLEIPANRMVGLIGPDGVGKSSLL-ALLAGARKMQDGEIrVLDGdmrdrrhrravcpRIAYMPQglgKNLY 97
Cdd:PLN03130 628 AERPTLSNINLDVPVGSLVAIVGSTGEGKTSLIsAMLGELPPRSDASV-VIRG-------------TVAYVPQ---VSWI 690
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 98 PTLSVFENVdFFGRLFGHDKAERERRIA------DLLQSTGLAPFAERPAgKLSGGMKQKLGLCCALIHDPDLLILDEPT 171
Cdd:PLN03130 691 FNATVRDNI-LFGSPFDPERYERAIDVTalqhdlDLLPGGDLTEIGERGV-NISGGQKQRVSMARAVYSNSDVYIFDDPL 768
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15600424 172 TGVDPLSRNQFW------ELIGRIRagregmsVLVaTAYMEEAERFDWLVAMDDGKVLATGTPQEL 231
Cdd:PLN03130 769 SALDAHVGRQVFdkcikdELRGKTR-------VLV-TNQLHFLSQVDRIILVHEGMIKEEGTYEEL 826
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
23-243 |
7.44e-07 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 52.79 E-value: 7.44e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 23 AVDDVSLEIPANRMVGLIGPDGVGKSSLLALLAGARKMQDGEIRVLDGDMRDRR--HRRAvcpRIAYMPQglgknlYPTL 100
Cdd:PRK10789 330 ALENVNFTLKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGDIRFHDIPLTKLQldSWRS---RLAVVSQ------TPFL 400
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 101 ---SVFENVdffgrLFGHDKA-----ERERRIA----DLLQstgLAPFAERPAGK----LSGGMKQKLGLCCALIHDPDL 164
Cdd:PRK10789 401 fsdTVANNI-----ALGRPDAtqqeiEHVARLAsvhdDILR---LPQGYDTEVGErgvmLSGGQKQRISIARALLLNAEI 472
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 165 LILDEPTTGVDPLSRNQfweLIGRIRAGREGMSVLVATAYMEEAERFDWLVAMDDGKVLATGTPQELRERTG-------T 237
Cdd:PRK10789 473 LILDDALSAVDGRTEHQ---ILHNLRQWGEGRTVIISAHRLSALTEASEILVMQHGHIAQRGNHDQLAQQSGwyrdmyrY 549
|
....*.
gi 15600424 238 QSLESA 243
Cdd:PRK10789 550 QQLEAA 555
|
|
| PRK13541 |
PRK13541 |
cytochrome c biogenesis protein CcmA; Provisional |
292-464 |
1.27e-06 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184128 [Multi-domain] Cd Length: 195 Bit Score: 49.87 E-value: 1.27e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 292 HVSFRIERGEIFG----FL--------GSNGCGKSTTMKMLTGLLPASEGTcaLFGQPVDASDMAtRRRVGYMSQAFSLY 359
Cdd:PRK13541 6 QLQFNIEQKNLFDlsitFLpsaityikGANGCGKSSLLRMIAGIMQPSSGN--IYYKNCNINNIA-KPYCTYIGHNLGLK 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 360 AELSVRQNLVLHARLFHlPADGIPARVgemlRRFDLEKVADELPNDLPLGIRQRLSLAVAVIHKPEILILDEPTSGVDPV 439
Cdd:PRK13541 83 LEMTVFENLKFWSEIYN-SAETLYAAI----HYFKLHDLLDEKCYSLSSGMQKIVAIARLIACQSDLWLLDEVETNLSKE 157
|
170 180
....*....|....*....|....*
gi 15600424 440 ARDGFWELMVELSRRDGVtIFISTH 464
Cdd:PRK13541 158 NRDLLNNLIVMKANSGGI-VLLSSH 181
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
238-494 |
2.19e-06 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 51.90 E-value: 2.19e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 238 QSLESAFIAllpeskragHHRLVIPPRPQSEGAPRIAIEAegltcrfGDFV--------AVDHVSFRIERGEIFGFLGSN 309
Cdd:PLN03232 589 QRIEELLLS---------EERILAQNPPLQPGAPAISIKN-------GYFSwdsktskpTLSDINLEIPVGSLVAIVGGT 652
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 310 GCGKSTTMKMLTGLLPASEGTCALFgqpvdasdmatRRRVGYMSQAFSLYaELSVRQNLvlharLFHlpADGIPARVGEM 389
Cdd:PLN03232 653 GEGKTSLISAMLGELSHAETSSVVI-----------RGSVAYVPQVSWIF-NATVRENI-----LFG--SDFESERYWRA 713
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 390 LRRFDLEKVADELPN-----------DLPLGIRQRLSLAVAVIHKPEILILDEPTSGVDP-VARDGFWELMV-ELSRRDG 456
Cdd:PLN03232 714 IDVTALQHDLDLLPGrdlteigergvNISGGQKQRVSMARAVYSNSDIYIFDDPLSALDAhVAHQVFDSCMKdELKGKTR 793
|
250 260 270
....*....|....*....|....*....|....*...
gi 15600424 457 VTIFISTHFMNEAqrcDRISLMHAGKVLASDTPDELVR 494
Cdd:PLN03232 794 VLVTNQLHFLPLM---DRIILVSEGMIKEEGTFAELSK 828
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
36-175 |
2.72e-06 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 51.03 E-value: 2.72e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 36 MVGLIGPDGVGKSSLLALLAGARKMQDGEIRVLdgdMRDRRHRRAVCPRIAYMPQGlgKNLYPTLSVFENVDFFG--RLF 113
Cdd:PLN03211 96 ILAVLGPSGSGKSTLLNALAGRIQGNNFTGTIL---ANNRKPTKQILKRTGFVTQD--DILYPHLTVRETLVFCSllRLP 170
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15600424 114 GHDKAERERRIAD-LLQSTGLAPFAERPAGK-----LSGGMKQKLGLCCALIHDPDLLILDEPTTGVD 175
Cdd:PLN03211 171 KSLTKQEKILVAEsVISELGLTKCENTIIGNsfirgISGGERKRVSIAHEMLINPSLLILDEPTSGLD 238
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
109-437 |
2.76e-06 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 51.40 E-value: 2.76e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 109 FGRLFGHDKAERERRIADLLQSTGLAPFAERPAGK-LSGGMKQKLGLCCALIHDPDLLILDEPTTGVDplSRNQFW---- 183
Cdd:PLN03073 309 YKRLELIDAYTAEARAASILAGLSFTPEMQVKATKtFSGGWRMRIALARALFIEPDLLLLDEPTNHLD--LHAVLWlety 386
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 184 -----ELIGRIRAGREGMSVLVATAYMEEAER-------FDWLVAMDDGKVLATGTPQELRERtgTQSLESAFI------ 245
Cdd:PLN03073 387 llkwpKTFIVVSHAREFLNTVVTDILHLHGQKlvtykgdYDTFERTREEQLKNQQKAFESNER--SRSHMQAFIdkfryn 464
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 246 ---ALLPESK-----RAGHHRLVIP--------PRPQSEGAPRIAIEAEGLTCRFGDFVAVDHVSFRIERGEIFGFLGSN 309
Cdd:PLN03073 465 akrASLVQSRikaldRLGHVDAVVNdpdykfefPTPDDRPGPPIISFSDASFGYPGGPLLFKNLNFGIDLDSRIAMVGPN 544
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 310 GCGKSTTMKMLTGLLPASEGTC--------ALFGQ-PVDASDMATRRRVgYMSQAFSLYAELSVRQnlvlharlfHLPAD 380
Cdd:PLN03073 545 GIGKSTILKLISGELQPSSGTVfrsakvrmAVFSQhHVDGLDLSSNPLL-YMMRCFPGVPEQKLRA---------HLGSF 614
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*..
gi 15600424 381 GIPArvgemlrrfdleKVADELPNDLPLGIRQRLSLAVAVIHKPEILILDEPTSGVD 437
Cdd:PLN03073 615 GVTG------------NLALQPMYTLSGGQKSRVAFAKITFKKPHILLLDEPSNHLD 659
|
|
| 3a01203 |
TIGR00954 |
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ... |
24-176 |
2.87e-06 |
|
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: 51.29 E-value: 2.87e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 24 VDDVSLEIPANRMVGLIGPDGVGKSSLLALLAGARKMQDGEIRVldgdmrDRRHRRAVCPRIAYMPQGLGKN--LYPTlS 101
Cdd:TIGR00954 468 IESLSFEVPSGNNLLICGPNGCGKSSLFRILGELWPVYGGRLTK------PAKGKLFYVPQRPYMTLGTLRDqiIYPD-S 540
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 102 VFenvDFFgrlfghDKAERERRIADLLQSTGLAPFAERPAG---------KLSGGMKQKLGLCCALIHDPDLLILDEPTT 172
Cdd:TIGR00954 541 SE---DMK------RRGLSDKDLEQILDNVQLTHILEREGGwsavqdwmdVLSGGEKQRIAMARLFYHKPQFAILDECTS 611
|
....
gi 15600424 173 GVDP 176
Cdd:TIGR00954 612 AVSV 615
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
81-231 |
3.18e-06 |
|
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: 51.17 E-value: 3.18e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 81 VCPRIAYMPQGL-----GKNLYPTL--SVFENVDFFgrlfghDKAERERRIADLLQSTGLA--PFAeRPAGKLSGGMKQK 151
Cdd:TIGR00630 765 VCKGKRYNRETLevkykGKNIADVLdmTVEEAYEFF------EAVPSISRKLQTLCDVGLGyiRLG-QPATTLSGGEAQR 837
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 152 LGLCCALIHD---PDLLILDEPTTGVDPLSRNQFWELIGRIRAGreGMSVLVATAYMEEAERFDWLV------AMDDGKV 222
Cdd:TIGR00630 838 IKLAKELSKRstgRTLYILDEPTTGLHFDDIKKLLEVLQRLVDK--GNTVVVIEHNLDVIKTADYIIdlgpegGDGGGTV 915
|
....*....
gi 15600424 223 LATGTPQEL 231
Cdd:TIGR00630 916 VASGTPEEV 924
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
286-481 |
4.25e-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: 48.87 E-value: 4.25e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 286 DFVAVDHVSFRIERGEIFGFLGSNGCGKSTTMKMLTGLLPASEG-----TCALFGQPVDASDMATRRRVGYMSQAfSLYA 360
Cdd:cd03290 13 GLATLSNINIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGkvhwsNKNESEPSFEATRSRNRYSVAYAAQK-PWLL 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 361 ELSVRQNLVlharlFHLPADgiPARVGEMLRRFDLEKVADELPN-----------DLPLGIRQRLSLAVAVIHKPEILIL 429
Cdd:cd03290 92 NATVEENIT-----FGSPFN--KQRYKAVTDACSLQPDIDLLPFgdqteigergiNLSGGQRQRICVARALYQNTNIVFL 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 15600424 430 DEPTSGVDPVARDGFW-ELMVELSRRDGVTIFISTHFMNEAQRCDRISLMHAG 481
Cdd:cd03290 165 DDPFSALDIHLSDHLMqEGILKFLQDDKRTLVLVTHKLQYLPHADWIIAMKDG 217
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
290-437 |
6.01e-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: 48.03 E-value: 6.01e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 290 VDHVSFRIERGEIFGFLGSNGCGKSTTMKMLTGLLPAS---EGTCALFGQPVDASDMATRRRVGYMSQAFSLYAELSVRQ 366
Cdd:cd03233 23 LKDFSGVVKPGEMVLVLGRPGSGCSTLLKALANRTEGNvsvEGDIHYNGIPYKEFAEKYPGEIIYVSEEDVHFPTLTVRE 102
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15600424 367 NLVLHARLfhlpadgipaRVGEMLRRFDlekvadelpndlpLGIRQRLSLAVAVIHKPEILILDEPTSGVD 437
Cdd:cd03233 103 TLDFALRC----------KGNEFVRGIS-------------GGERKRVSIAEALVSRASVLCWDNSTRGLD 150
|
|
| PRK15093 |
PRK15093 |
peptide ABC transporter ATP-binding protein SapD; |
19-189 |
6.64e-06 |
|
peptide ABC transporter ATP-binding protein SapD;
Pssm-ID: 185049 [Multi-domain] Cd Length: 330 Bit Score: 49.03 E-value: 6.64e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 19 GETRAVDDVSLEIPANRMVGLIGPDGVGKSSLLALLAG---------ARKMQDGEIRVLDGDMRDRRhrRAVCPRIAYMP 89
Cdd:PRK15093 18 GWVKAVDRVSMTLTEGEIRGLVGESGSGKSLIAKAICGvtkdnwrvtADRMRFDDIDLLRLSPRERR--KLVGHNVSMIF 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 90 QGLGKNLYPTLSVFENV-------DFFGRLFGHDKAeRERRIADLLQSTGLA---------PFaerpagKLSGGMKQKLG 153
Cdd:PRK15093 96 QEPQSCLDPSERVGRQLmqnipgwTYKGRWWQRFGW-RKRRAIELLHRVGIKdhkdamrsfPY------ELTEGECQKVM 168
|
170 180 190
....*....|....*....|....*....|....*.
gi 15600424 154 LCCALIHDPDLLILDEPTTGVDPLSRNQFWELIGRI 189
Cdd:PRK15093 169 IAIALANQPRLLIADEPTNAMEPTTQAQIFRLLTRL 204
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
26-233 |
7.71e-06 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 50.11 E-value: 7.71e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 26 DVSLEIPANRMVGLIGPDGVGKSSLLALLA----GARKMQDGEIRvLDG----DMRdrRHRRAvcpRIAYMPQGlgKNLY 97
Cdd:TIGR00956 79 PMDGLIKPGELTVVLGRPGSGCSTLLKTIAsntdGFHIGVEGVIT-YDGitpeEIK--KHYRG---DVVYNAET--DVHF 150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 98 PTLSVFENVDFFGRL-------FGHDKAERERRIADLLQST-GLAPFAERPAGK-----LSGGMKQKLGLCCALIHDPDL 164
Cdd:TIGR00956 151 PHLTVGETLDFAARCktpqnrpDGVSREEYAKHIADVYMATyGLSHTRNTKVGNdfvrgVSGGERKRVSIAEASLGGAKI 230
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15600424 165 LILDEPTTGVDPLSRNQFweligrIRAGREGMSVLVATAYM------EEA-ERFDWLVAMDDGKVLATGTPQELRE 233
Cdd:TIGR00956 231 QCWDNATRGLDSATALEF------IRALKTSANILDTTPLVaiyqcsQDAyELFDKVIVLYEGYQIYFGPADKAKQ 300
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
300-440 |
8.04e-06 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 49.84 E-value: 8.04e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 300 GEIFGFLGSNGCGKSTTMKMLTGLLPAS--EGTCALFGQPVDASDMAtrRRVGYMSQAFSLYAELSVRQNLVLHARLfHL 377
Cdd:PLN03140 906 GVLTALMGVSGAGKTTLMDVLAGRKTGGyiEGDIRISGFPKKQETFA--RISGYCEQNDIHSPQVTVRESLIYSAFL-RL 982
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15600424 378 PADGIPAR----VGEMLRRFDLEKVADE---LPNDLPLGI--RQRLSLAVAVIHKPEILILDEPTSGVDPVA 440
Cdd:PLN03140 983 PKEVSKEEkmmfVDEVMELVELDNLKDAivgLPGVTGLSTeqRKRLTIAVELVANPSIIFMDEPTSGLDARA 1054
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
7-266 |
1.05e-05 |
|
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator (CFTR), the product of the gene mutated in patients with cystic fibrosis, has adapted the ABC transporter structural motif to form a tightly regulated anion channel at the apical surface of many epithelia. Use of the term assembly of a functional ion channel implies the coming together of subunits or at least smaller not-yet functional components of the active whole. In fact, on the basis of current knowledge only the CFTR polypeptide itself is required to form an ATP- and protein kinase A-dependent low-conductance chloride channel of the type present in the apical membrane of many epithelial cells. CFTR displays the typical organization (IM-ABC)2 and carries a characteristic hydrophilic R-domain that separates IM1-ABC1 from IM2-ABC2.
Pssm-ID: 213256 [Multi-domain] Cd Length: 275 Bit Score: 48.31 E-value: 1.05e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 7 GVASLRGVSLRYGE--TRAVDDVSLEIPANRMVGLIGPDGVGKSSLL-ALLagarKM--QDGEIRVlDG----DMRDRRH 77
Cdd:cd03289 1 GQMTVKDLTAKYTEggNAVLENISFSISPGQRVGLLGRTGSGKSTLLsAFL----RLlnTEGDIQI-DGvswnSVPLQKW 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 78 RRA--VCPRIAYMPQG-LGKNLYPtlsvfenvdffgrlFGHDKAERERRIADllqSTGLAPFAERPAGKL---------- 144
Cdd:cd03289 76 RKAfgVIPQKVFIFSGtFRKNLDP--------------YGKWSDEEIWKVAE---EVGLKSVIEQFPGQLdfvlvdggcv 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 145 -SGGMKQKLGLCCALIHDPDLLILDEPTTGVDPLSrnqfWELIGR-IRAGREGMSVLVATAYME---EAERFdwlVAMDD 219
Cdd:cd03289 139 lSHGHKQLMCLARSVLSKAKILLLDEPSAHLDPIT----YQVIRKtLKQAFADCTVILSEHRIEamlECQRF---LVIEE 211
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 15600424 220 GKVLATGTPQELRERTGT--QSLESA-FIALLPESKRAGHHRlviPPRPQ 266
Cdd:cd03289 212 NKVRQYDSIQKLLNEKSHfkQAISPSdRLKLFPRRNSSKSKR---KPRPQ 258
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
20-226 |
1.53e-05 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 48.70 E-value: 1.53e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 20 ETRAVDDVSLEIPANRMVGLIGPDGVGKSSLLALLAGARKMQDGEIrVLDG---DMRDRRHRRAVCPRIAYMPQGLGKNL 96
Cdd:PRK10261 336 EVHAVEKVSFDLWPGETLSLVGESGSGKSTTGRALLRLVESQGGEI-IFNGqriDTLSPGKLQALRRDIQFIFQDPYASL 414
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 97 YPTL----SVFENVDFFGRLFGHDKAereRRIADLLQSTGLAP-FAERPAGKLSGGMKQKLGLCCALIHDPDLLILDEPT 171
Cdd:PRK10261 415 DPRQtvgdSIMEPLRVHGLLPGKAAA---ARVAWLLERVGLLPeHAWRYPHEFSGGQRQRICIARALALNPKVIIADEAV 491
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 15600424 172 TGVDPLSRNQFWELIGRIRagRE-GMSVLVATAYMEEAERFDWLVA-MDDGKVLATG 226
Cdd:PRK10261 492 SALDVSIRGQIINLLLDLQ--RDfGIAYLFISHDMAVVERISHRVAvMYLGQIVEIG 546
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
19-175 |
1.58e-05 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 48.18 E-value: 1.58e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 19 GETRAVDDVSLEIPANRMVGLIGPDGVGKS----SLLALLA------GARKMQDGEIRvldgDMRDRRHRRAVCPRIAYM 88
Cdd:PRK09473 27 GDVTAVNDLNFSLRAGETLGIVGESGSGKSqtafALMGLLAangrigGSATFNGREIL----NLPEKELNKLRAEQISMI 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 89 PQGLGKNLYPTLSVFENVDFFGRLF-GHDKAERERRIADLLQSTGLaPFAERPAG----KLSGGMKQKLGLCCALIHDPD 163
Cdd:PRK09473 103 FQDPMTSLNPYMRVGEQLMEVLMLHkGMSKAEAFEESVRMLDAVKM-PEARKRMKmyphEFSGGMRQRVMIAMALLCRPK 181
|
170
....*....|..
gi 15600424 164 LLILDEPTTGVD 175
Cdd:PRK09473 182 LLIADEPTTALD 193
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
22-226 |
1.78e-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: 1.78e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 22 RAVDDVSLEIPANRMVGLIGPDGVGKSSLLalLAGARKmqdgeirvldgdmrdrrhrrAVCPRIAYMPQGLGKNlyPTLs 101
Cdd:cd03238 9 HNLQNLDVSIPLNVLVVVTGVSGSGKSTLV--NEGLYA--------------------SGKARLISFLPKFSRN--KLI- 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 102 vfenvdFFGRLfghdkaereRRIADLlqstGLAPFA-ERPAGKLSGGMKQKLGLCCALIHDPD--LLILDEPTTGVDPLS 178
Cdd:cd03238 64 ------FIDQL---------QFLIDV----GLGYLTlGQKLSTLSGGELQRVKLASELFSEPPgtLFILDEPSTGLHQQD 124
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 15600424 179 RNQFWELIGRIRagREGMSVLVATAYMEEAERFDWLVAM------DDGKVLATG 226
Cdd:cd03238 125 INQLLEVIKGLI--DLGNTVILIEHNLDVLSSADWIIDFgpgsgkSGGKVVFSG 176
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
6-231 |
2.53e-05 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 48.20 E-value: 2.53e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 6 SGVASLRGVSLRY-GETRAV-DDVSLEIPANRMVGLIGPDGVGKSSLLALLAGARKMQDGEIRVLDGD-----MRDRRHR 78
Cdd:PLN03130 1235 SGSIKFEDVVLRYrPELPPVlHGLSFEISPSEKVGIVGRTGAGKSSMLNALFRIVELERGRILIDGCDiskfgLMDLRKV 1314
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 79 RAVCPRIAYMPQGlgknlyptlSVFENVDFFGRlfgHDKAE----RER-RIADLLQSTGLAPFAERPAG--KLSGGMKQK 151
Cdd:PLN03130 1315 LGIIPQAPVLFSG---------TVRFNLDPFNE---HNDADlwesLERaHLKDVIRRNSLGLDAEVSEAgeNFSVGQRQL 1382
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 152 LGLCCALIHDPDLLILDEPTTGVDPLSRnqfwELIGR-IRAGREGMSVLVATAYMEEAERFDWLVAMDDGKVLATGTPQE 230
Cdd:PLN03130 1383 LSLARALLRRSKILVLDEATAAVDVRTD----ALIQKtIREEFKSCTMLIIAHRLNTIIDCDRILVLDAGRVVEFDTPEN 1458
|
.
gi 15600424 231 L 231
Cdd:PLN03130 1459 L 1459
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
7-178 |
2.84e-05 |
|
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis fibrosis transmembrane conductor regulator (CFTR) in eukaryotes. The principal role of this protein is chloride ion conductance. The protein is predicted to consist of 12 transmembrane domains. Mutations or lesions in the genetic loci have been linked to the aetiology of asthma, bronchiectasis, chronic obstructive pulmonary disease etc. Disease-causing mutations have been studied by 36Cl efflux assays in vitro cell cultures and electrophysiology, all of which point to the impairment of chloride channel stability and not the biosynthetic processing per se. [Transport and binding proteins, Anions]
Pssm-ID: 273530 [Multi-domain] Cd Length: 1490 Bit Score: 47.98 E-value: 2.84e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 7 GVASLRGVSLRYGET-RAV-DDVSLEIPANRMVGLIGPDGVGKSSLL-ALLAGARkmQDGEIRVlDG------DMRDRRH 77
Cdd:TIGR01271 1216 GQMDVQGLTAKYTEAgRAVlQDLSFSVEGGQRVGLLGRTGSGKSTLLsALLRLLS--TEGEIQI-DGvswnsvTLQTWRK 1292
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 78 RRAVCPRIAYMPQG-LGKNLYPtlsvfenvdffgrlfgHDKAERER--RIADllqSTGLAPFAERPAGK----------- 143
Cdd:TIGR01271 1293 AFGVIPQKVFIFSGtFRKNLDP----------------YEQWSDEEiwKVAE---EVGLKSVIEQFPDKldfvlvdggyv 1353
|
170 180 190
....*....|....*....|....*....|....*
gi 15600424 144 LSGGMKQKLGLCCALIHDPDLLILDEPTTGVDPLS 178
Cdd:TIGR01271 1354 LSNGHKQLMCLARSILSKAKILLLDEPSAHLDPVT 1388
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
294-437 |
4.07e-05 |
|
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440858 [Multi-domain] Cd Length: 592 Bit Score: 47.47 E-value: 4.07e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 294 SFRI------ERGEIFGFLGSNGCGKSTTMKMLTGLLPASEGTcalFGQPVDASDMATRRRVGYMSQAFSLYAELSVR-- 365
Cdd:COG1245 87 GFRLyglpvpKKGKVTGILGPNGIGKSTALKILSGELKPNLGD---YDEEPSWDEVLKRFRGTELQDYFKKLANGEIKva 163
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 366 ---QNLVLHARLFhlpaDGipaRVGEMLRRFDLEKVADELPNDLPLG------IR-------QRLSLAVAVIHKPEILIL 429
Cdd:COG1245 164 hkpQYVDLIPKVF----KG---TVRELLEKVDERGKLDELAEKLGLEnildrdISelsggelQRVAIAAALLRDADFYFF 236
|
....*...
gi 15600424 430 DEPTSGVD 437
Cdd:COG1245 237 DEPSSYLD 244
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
293-437 |
4.45e-05 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 47.72 E-value: 4.45e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 293 VSFRIERGEIFGFLGSNGCGKSTTMKMLTGLLPASEGTcALFGQPVDASDMAT---RRRVGYMSQAFSLYAElSVRQNLV 369
Cdd:PTZ00265 404 LNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGD-IIINDSHNLKDINLkwwRSKIGVVSQDPLLFSN-SIKNNIK 481
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 370 --------LHARLFHLPADGIPARVGEMLRRFDLEKVADE---------------------------------------- 401
Cdd:PTZ00265 482 yslyslkdLEALSNYYNEDGNDSQENKNKRNSCRAKCAGDlndmsnttdsneliemrknyqtikdsevvdvskkvlihdf 561
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 15600424 402 ---LPND-----------LPLGIRQRLSLAVAVIHKPEILILDEPTSGVD 437
Cdd:PTZ00265 562 vsaLPDKyetlvgsnaskLSGGQKQRISIARAIIRNPKILILDEATSSLD 611
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
143-217 |
4.87e-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: 4.87e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15600424 143 KLSGGMKQKLGLCCALIH----DPDLLILDEPTTGVDPLSRNQFWELIGRIRAGreGMSVLVATAYMEEAERFDWLVAM 217
Cdd:cd03227 77 QLSGGEKELSALALILALaslkPRPLYILDEIDRGLDPRDGQALAEAILEHLVK--GAQVIVITHLPELAELADKLIHI 153
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
260-496 |
5.57e-05 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 47.08 E-value: 5.57e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 260 VIPPRPQSEGAPRI----AIEAEGLTCRF--GDFVAVDHVSFRIERGEIFGFLGSNGCGKSTTMKMLTGLLPASEGTCAL 333
Cdd:PTZ00243 1290 VIEPASPTSAAPHPvqagSLVFEGVQMRYreGLPLVLRGVSFRIAPREKVGIVGRTGSGKSTLLLTFMRMVEVCGGEIRV 1369
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 334 FGQPVDASDMATRRRVGYMSQAFSLYAELSVRQNL--VLHARlfhlpadgiPARVGEMLRRFDL-EKVADELP------- 403
Cdd:PTZ00243 1370 NGREIGAYGLRELRRQFSMIPQDPVLFDGTVRQNVdpFLEAS---------SAEVWAALELVGLrERVASESEgidsrvl 1440
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 404 ---NDLPLGIRQRLSLAVAVIHKPEILIL-DEPTSGVDPvARDGFWELMVeLSRRDGVTIFISTHFMNEAQRCDRISLMH 479
Cdd:PTZ00243 1441 eggSNYSVGQRQLMCMARALLKKGSGFILmDEATANIDP-ALDRQIQATV-MSAFSAYTVITIAHRLHTVAQYDKIIVMD 1518
|
250
....*....|....*..
gi 15600424 480 AGKVLASDTPDELVRQR 496
Cdd:PTZ00243 1519 HGAVAEMGSPRELVMNR 1535
|
|
| PRK13541 |
PRK13541 |
cytochrome c biogenesis protein CcmA; Provisional |
20-186 |
7.57e-05 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184128 [Multi-domain] Cd Length: 195 Bit Score: 44.48 E-value: 7.57e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 20 ETRAVDDVSLEIPANRMVGLIGPDGVGKSSLLALLAGARKMQDGEIRVLDGDMRDRRHrravcPRIAYMPQGLGKNLypT 99
Cdd:PRK13541 12 EQKNLFDLSITFLPSAITYIKGANGCGKSSLLRMIAGIMQPSSGNIYYKNCNINNIAK-----PYCTYIGHNLGLKL--E 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 100 LSVFENVDFFGRLFGH----DKAERERRIADLLqstglapfaERPAGKLSGGMKQKLGLCCALIHDPDLLILDEPTTGVD 175
Cdd:PRK13541 85 MTVFENLKFWSEIYNSaetlYAAIHYFKLHDLL---------DEKCYSLSSGMQKIVAIARLIACQSDLWLLDEVETNLS 155
|
170
....*....|.
gi 15600424 176 PLSRNQFWELI 186
Cdd:PRK13541 156 KENRDLLNNLI 166
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
141-201 |
8.47e-05 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 46.56 E-value: 8.47e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15600424 141 AGKLSGGMKQKLGLCCALIHDPDLLILDEPTTGVDPLSRNQFWELIGRIRAGREGMSVLVA 201
Cdd:PTZ00265 577 ASKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQKTINNLKGNENRITIIIA 637
|
|
| ABCC_SUR2 |
cd03288 |
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The ... |
292-496 |
9.48e-05 |
|
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: 45.28 E-value: 9.48e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 292 HVSFRIERGEIFGFLGSNGCGKSTTMKMLTGLLPASEGTCALFGQPVDASDMAT-RRRVGYMSQAFSLYAElSVRQNLVL 370
Cdd:cd03288 39 HVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVIDGIDISKLPLHTlRSRLSIILQDPILFSG-SIRFNLDP 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 371 HARLfhlpadgIPARVGEMLRRFDLEKVADELPNDL-----------PLGIRQRLSLAVAVIHKPEILILDEPTSGVDPV 439
Cdd:cd03288 118 ECKC-------TDDRLWEALEIAQLKNMVKSLPGGLdavvteggenfSVGQRQLFCLARAFVRKSSILIMDEATASIDMA 190
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 15600424 440 ARDGFWE-LMVELSRRDGVTIfisTHFMNEAQRCDRISLMHAGKVLASDTPDELVRQR 496
Cdd:cd03288 191 TENILQKvVMTAFADRTVVTI---AHRVSTILDADLVLVLSRGILVECDTPENLLAQE 245
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
100-231 |
1.41e-04 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 45.79 E-value: 1.41e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 100 LSVFENVDFfgrlfGHDKAERE--RR------IADLLQS------TGLAPFAErpagKLSGGMKQKLGLCCALIHDPDLL 165
Cdd:PTZ00265 1310 MSIYENIKF-----GKEDATREdvKRackfaaIDEFIESlpnkydTNVGPYGK----SLSGGQKQRIAIARALLREPKIL 1380
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15600424 166 ILDEPTTGVDPLSRNQFWELIGRIRaGREGMSVLVATAYMEEAERFDWLVAMDDGK-----VLATGTPQEL 231
Cdd:PTZ00265 1381 LLDEATSSLDSNSEKLIEKTIVDIK-DKADKTIITIAHRIASIKRSDKIVVFNNPDrtgsfVQAHGTHEEL 1450
|
|
| ABC-2_lan_permease-like |
cd21809 |
lantibiotic immunity ABC transporter permease (also called ABC-2 transporter permease) subunit ... |
722-913 |
1.89e-04 |
|
lantibiotic immunity ABC transporter permease (also called ABC-2 transporter permease) subunit and similar proteins; This subfamily contains lantibiotic ABC transporter permease subunits which are highly hydrophobic, integral membrane proteins, and part of the bacitracin ABC transport system that confers resistance to the Gram-positive bacteria in which this system operates, particularly to type-A lantibiotics. Lantibiotics are small peptides, produced by Gram-positive bacteria, which are ribosomally-synthesized as pre-peptides and act by disrupting membrane integrity. Genes encoding the lantibiotic ABC transporter subunits are highly organized in operons containing all the genes required for maturation, transport, immunity, and synthesis. For example, in Lactococcus lactis, the lantibiotic nisin is active against other Gram-positive bacteria via various modes of actions; however, its self-protection against the pore-forming nisin is mediated by the ABC transporter composed of NisF, NisE and NisG; the NisG permease subunit transports nisin to the surface and expels it from the membrane. This family includes mostly uncharacterized transport permease subunits that transport lantibiotics to the surface and expel them from the membrane.
Pssm-ID: 409634 Cd Length: 235 Bit Score: 44.11 E-value: 1.89e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 722 MVPAVIPLLLIMIPAMLTALgVVR-EKELGSITNLYVTPVTRLEFLVGKQLPYVAMGMINFLLMLV--LAIVVFRVPLKG 798
Cdd:cd21809 50 VVLFYGLLFLPLLIGILASL-VCRiEHKNNGWKQLLALPVSRTQIYLAKFLVVLLLLALTQLLFLGaiILGGLLLGFGGP 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 799 SFLALTIGAFLYVVTST----GLGLFLSTFMRSQIAAVFGVAIATMIpaiqfsGLIhpvssleGAAAWIGKLYPTSHFLV 874
Cdd:cd21809 129 IPWLLILKSVLLGWIASlpliALQLWLSLRFKSFAAPLGIGILTLPA------GLI-------ANSSKLGPFYPWAYPIL 195
|
170 180 190
....*....|....*....|....*....|....*....
gi 15600424 875 VSRGAFSKSLGLSDLWAYYLPLAASIVVLTLLSVACLKK 913
Cdd:cd21809 196 AMLPGSGDGAFNVSLELFLIVSLGSFILFLLIGLRHFKR 234
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
293-483 |
1.90e-04 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 45.54 E-value: 1.90e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 293 VSFRIERGEIFGFLGSNGCGKSTTMKMLTGLLPASEGtcalfgqpvdasDMATRRRVGYM-SQAFSLYAelSVRQNLvlh 371
Cdd:PTZ00243 679 VSVSVPRGKLTVVLGATGSGKSTLLQSLLSQFEISEG------------RVWAERSIAYVpQQAWIMNA--TVRGNI--- 741
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 372 arLFHLPADgiPARVGEMLRRFDLEKVADELPN-----------DLPLGIRQRLSLAVAVIHKPEILILDEPTSGVDpvA 440
Cdd:PTZ00243 742 --LFFDEED--AARLADAVRVSQLEADLAQLGGgleteigekgvNLSGGQKARVSLARAVYANRDVYLLDDPLSALD--A 815
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 15600424 441 RDGfwELMVE---LSRRDGVTIFISTHFMNEAQRCDRISLMHAGKV 483
Cdd:PTZ00243 816 HVG--ERVVEecfLGALAGKTRVLATHQVHVVPRADYVVALGDGRV 859
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
299-464 |
3.55e-04 |
|
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: 41.98 E-value: 3.55e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 299 RGEIFGFLGSNGCGKSTTMKMLTGLLPASEGTCALFgqpvdasdmatrrrvgymsqafslyaelsvrqnlvlharlfhlp 378
Cdd:smart00382 1 PGEVILIVGPPGSGKTTLARALARELGPPGGGVIYI-------------------------------------------- 36
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 379 aDGIPARVGEMLRRFDLEKVADELPNDLPLGIRQRLSLAVAviHKPEILILDEPTSGVDPVARDGFWELMV-----ELSR 453
Cdd:smart00382 37 -DGEDILEEVLDQLLLIIVGGKKASGSGELRLRLALALARK--LKPDVLILDEITSLLDAEQEALLLLLEElrlllLLKS 113
|
170
....*....|.
gi 15600424 454 RDGVTIFISTH 464
Cdd:smart00382 114 EKNLTVILTTN 124
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
12-260 |
5.34e-04 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 44.00 E-value: 5.34e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 12 RGVSLRY--GETRAVDDVSLEIPANRMVGLIGPDGVGKSSLLALLAGARKMQDGEIRVldgDMRD------RRHRRavcp 83
Cdd:PTZ00243 1312 EGVQMRYreGLPLVLRGVSFRIAPREKVGIVGRTGSGKSTLLLTFMRMVEVCGGEIRV---NGREigayglRELRR---- 1384
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 84 RIAYMPQGlgknlyPTL---SVFENVDFFgrlfghdkaeRERRIADLLQSTGLAPFAERPAGK--------LSGGMKQKL 152
Cdd:PTZ00243 1385 QFSMIPQD------PVLfdgTVRQNVDPF----------LEASSAEVWAALELVGLRERVASEsegidsrvLEGGSNYSV 1448
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 153 G----LCCA---LIHDPDLLILDEPTTGVDP-LSRnqfweligRIRAgrEGMSVLVATAYMEEAER------FDWLVAMD 218
Cdd:PTZ00243 1449 GqrqlMCMAralLKKGSGFILMDEATANIDPaLDR--------QIQA--TVMSAFSAYTVITIAHRlhtvaqYDKIIVMD 1518
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 15600424 219 DGKVLATGTPQELRERtgTQSLESAFIALLPESKRAGHHRLV 260
Cdd:PTZ00243 1519 HGAVAEMGSPRELVMN--RQSIFHSMVEALGRSEAKRFLQLV 1558
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
409-493 |
5.50e-04 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 43.86 E-value: 5.50e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 409 GIRQRLSLAVAVIHKPEILILDEPTSGVDPVARDGFWELMVELSRRDGVTIFISTHFMNEAQRCDRISLMH-----AGKV 483
Cdd:PTZ00265 1362 GQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDIKDKADKTIITIAHRIASIKRSDKIVVFNnpdrtGSFV 1441
|
90
....*....|
gi 15600424 484 LASDTPDELV 493
Cdd:PTZ00265 1442 QAHGTHEELL 1451
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
139-231 |
9.16e-04 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 43.28 E-value: 9.16e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 139 RPAGKLSGGMKQKLGLCCALIH---DPDLLILDEPTTGvdpLSRNQFWELIGRIRA-GREGMSVLVATAYMEEAERFDWL 214
Cdd:PRK00635 805 RPLSSLSGGEIQRLKLAYELLApskKPTLYVLDEPTTG---LHTHDIKALIYVLQSlTHQGHTVVIIEHNMHVVKVADYV 881
|
90 100
....*....|....*....|...
gi 15600424 215 VAMD------DGKVLATGTPQEL 231
Cdd:PRK00635 882 LELGpeggnlGGYLLASCSPEEL 904
|
|
| ABC2_membrane_4 |
pfam12730 |
ABC-2 family transporter protein; This family is related to the ABC-2 membrane transporter ... |
726-832 |
1.74e-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: 40.26 E-value: 1.74e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 726 VIPLLLIMIPAMLtalgVVREKELGSITNLYVTPVTRLEFLVGKqlpYVAMGMINFLLMLVLAIVVFRVPLKGSFLALTI 805
Cdd:pfam12730 59 LLPIILGIIASYL----FFREYDNDTLKNLLTIPVSRRKLLFAK---LIVLLLLSVLFMLVTFLITVLFGLLSGFVGFSW 131
|
90 100 110
....*....|....*....|....*....|....*...
gi 15600424 806 GAFLYVV---TSTGLGLF--------LSTFMRSQIAAV 832
Cdd:pfam12730 132 GLILYLLkkcLEIGLLVFfavlpiiaLALLFKGYVLPV 169
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
294-465 |
2.15e-03 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 41.54 E-value: 2.15e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 294 SFRIERGEIFGFLGSNGCGKSTTMKMLTGLLPASEGTCAL-FGQPVDASDMATRRRVgymSQAFS-----LYAE------ 361
Cdd:PRK10938 23 SLTLNAGDSWAFVGANGSGKSALARALAGELPLLSGERQSqFSHITRLSFEQLQKLV---SDEWQrnntdMLSPgeddtg 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 362 LSVRQNLVLHARlfhlpadgIPARVGEMLRRFDLEKVADELPNDLPLGIRQRLSLAVAVIHKPEILILDEPTSGVDPVAR 441
Cdd:PRK10938 100 RTTAEIIQDEVK--------DPARCEQLAQQFGITALLDRRFKYLSTGETRKTLLCQALMSEPDLLILDEPFDGLDVASR 171
|
170 180
....*....|....*....|....
gi 15600424 442 DGFWELMVELSRRDGVTIFISTHF 465
Cdd:PRK10938 172 QQLAELLASLHQSGITLVLVLNRF 195
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
99-233 |
2.62e-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: 41.54 E-value: 2.62e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 99 TLSVFENVDFFGRLfghDKAERERRIADL-----------LQSTGLAPFA-ERPAGKLSGGMKQKLGLC----CALIHdp 162
Cdd:TIGR00630 435 ELSIREAHEFFNQL---TLTPEEKKIAEEvlkeirerlgfLIDVGLDYLSlSRAAGTLSGGEAQRIRLAtqigSGLTG-- 509
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15600424 163 DLLILDEPTTGVDPlSRNQfwELIGRIRAGRE-GMSVLVATAYMEEAERFDWLVAM------DDGKVLATGTPQELRE 233
Cdd:TIGR00630 510 VLYVLDEPSIGLHQ-RDNR--RLINTLKRLRDlGNTLIVVEHDEDTIRAADYVIDIgpgageHGGEVVASGTPEEILA 584
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
19-175 |
2.66e-03 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 41.63 E-value: 2.66e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 19 GETRAV-DDVSLEIPANRMVGLIGPDGVGKSSLLALLAGARKMQ--DGEIRVLDGDMRDRRHRRavcpRIAYMPQglgKN 95
Cdd:TIGR00956 773 KEKRVIlNNVDGWVKPGTLTALMGASGAGKTTLLNVLAERVTTGviTGGDRLVNGRPLDSSFQR----SIGYVQQ---QD 845
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 96 LY-PTLSVFENVDF--FGRLFGH-DKAERERRIADLLQSTGLAPFAERPAGKLSGGM----KQKLGLCCALIHDPDLLI- 166
Cdd:TIGR00956 846 LHlPTSTVRESLRFsaYLRQPKSvSKSEKMEYVEEVIKLLEMESYADAVVGVPGEGLnveqRKRLTIGVELVAKPKLLLf 925
|
....*....
gi 15600424 167 LDEPTTGVD 175
Cdd:TIGR00956 926 LDEPTSGLD 934
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
400-503 |
3.48e-03 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 41.35 E-value: 3.48e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 400 DELPNDLPL-----GIRQRLSLA---VAVIHKPEILILDEPTSGVDPVARDGFWELMVELSRRdGVTIFISTHFMNEAQR 471
Cdd:PRK00635 799 DYLPLGRPLsslsgGEIQRLKLAyelLAPSKKPTLYVLDEPTTGLHTHDIKALIYVLQSLTHQ-GHTVVIIEHNMHVVKV 877
|
90 100 110
....*....|....*....|....*....|....*...
gi 15600424 472 CDRISLM------HAGKVLASDTPDELVrQRGLPTLEA 503
Cdd:PRK00635 878 ADYVLELgpeggnLGGYLLASCSPEELI-HLHTPTAKA 914
|
|
| RsgA_GTPase |
pfam03193 |
RsgA GTPase; RsgA (also known as EngC and YjeQ) represents a protein family whose members are ... |
33-79 |
3.98e-03 |
|
RsgA GTPase; RsgA (also known as EngC and YjeQ) represents a protein family whose members are broadly conserved in bacteria and are indispensable for growth. The GTPase domain of RsgA is very similar to several P-loop GTPases, but differs in having a circular permutation of the GTPase structure described by a G4-G1-G3 pattern.
Pssm-ID: 427191 [Multi-domain] Cd Length: 174 Bit Score: 39.06 E-value: 3.98e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 15600424 33 ANRMVGLIGPDGVGKSSLLALLAGARKMQDGEIRVLDGdmRDR---RHRR 79
Cdd:pfam03193 105 KGKTTVLAGQSGVGKSTLLNALLPELDLRTGEISEKLG--RGRhttTHVE 152
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
275-358 |
4.05e-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: 39.09 E-value: 4.05e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600424 275 IEAEGLTCRFGDFvavdHVSFR---IERGEIFGFLGSNGCGKSTTMKMLTGLLpasegtcalfgQPVDASDMATRRRVGY 351
Cdd:cd03222 1 QLYPDCVKRYGVF----FLLVElgvVKEGEVIGIVGPNGTGKTTAVKILAGQL-----------IPNGDNDEWDGITPVY 65
|
....*..
gi 15600424 352 MSQAFSL 358
Cdd:cd03222 66 KPQYIDL 72
|
|
| YjeQ_EngC |
cd01854 |
Ribosomal interacting GTPase YjeQ/EngC, a circularly permuted subfamily of the Ras GTPases; ... |
33-66 |
4.10e-03 |
|
Ribosomal interacting GTPase YjeQ/EngC, a circularly permuted subfamily of the Ras GTPases; YjeQ (YloQ in Bacillus subtilis) is a ribosomal small subunit-dependent GTPase; hence also known as RsgA. YjeQ is a late-stage ribosomal biogenesis factor involved in the 30S subunit maturation, and it represents a protein family whose members are broadly conserved in bacteria and have been shown to be essential to the growth of E. coli and B. subtilis. Proteins of the YjeQ family contain all sequence motifs typical of the vast class of P-loop-containing GTPases, but show a circular permutation, with a G4-G1-G3 pattern of motifs as opposed to the regular G1-G3-G4 pattern seen in most GTPases. All YjeQ family proteins display a unique domain architecture, which includes an N-terminal OB-fold RNA-binding domain, the central permuted GTPase domain, and a zinc knuckle-like C-terminal cysteine domain.
Pssm-ID: 206747 [Multi-domain] Cd Length: 211 Bit Score: 39.69 E-value: 4.10e-03
10 20 30
....*....|....*....|....*....|....
gi 15600424 33 ANRMVGLIGPDGVGKSSLLALLAGARKMQDGEIR 66
Cdd:cd01854 84 KGKTSVLVGQSGVGKSTLLNALLPELVLATGEIS 117
|
|
|