|
Name |
Accession |
Description |
Interval |
E-value |
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
6-989 |
0e+00 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 1775.05 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 6 VVRFSDVSLRYGKTVALDRITLDVPAGLTTGLIGPDGVGKSSLLALASGARALQTGGVDALGGDMRSRRHRERVCRRIAY 85
Cdd:NF033858 1 VARLEGVSHRYGKTVALDDVSLDIPAGCMVGLIGPDGVGKSSLLSLIAGARKIQQGRVEVLGGDMADARHRRAVCPRIAY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 86 MPQGLGKNLYPTLSVEENLQFFARLFGHDAGERRRRIDALTQSTGLFPFLSRPAGKLSGGMKQKLGLCCALIHDPDLLIL 165
Cdd:NF033858 81 MPQGLGKNLYPTLSVFENLDFFGRLFGQDAAERRRRIDELLRATGLAPFADRPAGKLSGGMKQKLGLCCALIHDPDLLIL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 166 DEPTTGVDPLARAQFWDLIARIRDERPTMSVIVATAYMDEAQRFDWLIAMDAGRVLATGAPAELLARTGCDSLEAAFIAL 245
Cdd:NF033858 161 DEPTTGVDPLSRRQFWELIDRIRAERPGMSVLVATAYMEEAERFDWLVAMDAGRVLATGTPAELLARTGADTLEAAFIAL 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 246 LPENERRGHKPVKIEPLRADARAGTAIEARGLTMRFGDFTAVDHVSFRIRRGEIFGFLGSNGCGKSTTMKMLTGLLPATE 325
Cdd:NF033858 241 LPEEKRRGHQPVVIPPRPADDDDEPAIEARGLTMRFGDFTAVDHVSFRIRRGEIFGFLGSNGCGKSTTMKMLTGLLPASE 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 326 GTAQLFGKEVDPKDINTRRRVGYMSQAFSLYSELTVRQNLVLHARLFGVPAAEIDARVDEMARRFGLADIYGMLPDSLPL 405
Cdd:NF033858 321 GEAWLFGQPVDAGDIATRRRVGYMSQAFSLYGELTVRQNLELHARLFHLPAAEIAARVAEMLERFDLADVADALPDSLPL 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 406 GMRQRLSLAVAMVHKPELLILDEPTSGVDPVARDSFWQLMIDLARRDLVTIFISTHFMNEAQRCDRISLMHAGRVLASDS 485
Cdd:NF033858 401 GIRQRLSLAVAVIHKPELLILDEPTSGVDPVARDMFWRLLIELSREDGVTIFISTHFMNEAERCDRISLMHAGRVLASDT 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 486 PAELVRARGAATLEDAFIGYLVDAsaqdadggagagagaadraaggapagrnatvdadaddaarahpaadvaaragdapa 565
Cdd:NF033858 481 PAALVAARGAATLEEAFIAYLEEA-------------------------------------------------------- 504
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 566 araEAGSEAGGESVTEAATASHpepnapaahaplaavprsSSALAEPPHRAFSAQRTLSYMWREMLELRRDPVRATLALI 645
Cdd:NF033858 505 ---AGAAAAPAAAAAPAAAAAA------------------PAAPAPAPRRRFSLRRLLAYARREALELLRDPIRLTFALL 563
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 646 GSLVLMCVIGIGISLDVEDLTYAVLDRDQTELSHDYALNLSGSRYFVERPPIADYAELDRRMRDGELSLAIEIPPNFARD 725
Cdd:NF033858 564 GSVILMFVMGYGISLDVENLTFAVLDRDQTPESRAYLLNFAGSRYFIEQPPIADYAELDRRMRSGELSLAIEIPPGFGRD 643
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 726 VERGAPAQIAMWIDGAMPQRAETIRGYAIGMHTMWLADKARHRLGVTLAPRAEVVTRYRYNPDVKSLPAMIPAVMPLLLL 805
Cdd:NF033858 644 LLRGRPPEVGAWIDGAMPFRAETIRGYVQGMHQQWLADLARERGGAAAASPATIETRYRYNPDFKSLPAMVPAVIPLLLM 723
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 806 MLPAMLTALAVVRERELGSILNLYVTPVTRTEFLIGKQVPYVVLAMLNFLLMTMLARIAFDVPVKGSFMTLLLAVLIFNV 885
Cdd:NF033858 724 LIPAMLTALSVVREKELGSITNLYVTPVTRLEFLLGKQLPYVALAMLNFLLLVLLAVFVFGVPLKGSFLALALGALLYVT 803
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 886 VATGIGLLASTFTRSQVAAIVMTIIGTMIPTVQFAGLLTPLSSLEGTGRFIGLVYPATYMLSISRGVFNKALSLQDLHSQ 965
Cdd:NF033858 804 ATTGLGLLISTFTRSQIAAIFGTAILTLIPAVQFSGLLDPVSSLEGAGRLIGRIFPATYFLTISRGTFTKGLGFADLWPS 883
|
970 980
....*....|....*....|....
gi 505416896 966 FWPLAASAPVILGATILLLKKQER 989
Cdd:NF033858 884 FLALAAFIPVLLGLSVLLLKKQER 907
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
272-506 |
8.35e-105 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 325.87 E-value: 8.35e-105
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 272 IEARGLTMRFGDFTAVDHVSFRIRRGEIFGFLGSNGCGKSTTMKMLTGLLPATEGTAQLFGKEVDPKDINTRRRVGYMSQ 351
Cdd:COG1131 1 IEVRGLTKRYGDKTALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRVLGEDVARDPAEVRRRIGYVPQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 352 AFSLYSELTVRQNLVLHARLFGVPAAEIDARVDEMARRFGLADIYGMLPDSLPLGMRQRLSLAVAMVHKPELLILDEPTS 431
Cdd:COG1131 81 EPALYPDLTVRENLRFFARLYGLPRKEARERIDELLELFGLTDAADRKVGTLSGGMKQRLGLALALLHDPELLILDEPTS 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 505416896 432 GVDPVARDSFWQLMIDLARRDlVTIFISTHFMNEAQR-CDRISLMHAGRVLASDSPAELVrargAATLEDAFIGYL 506
Cdd:COG1131 161 GLDPEARRELWELLRELAAEG-KTVLLSTHYLEEAERlCDRVAIIDKGRIVADGTPDELK----ARLLEDVFLELT 231
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
4-489 |
1.58e-90 |
|
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: 298.36 E-value: 1.58e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 4 SSVVRFSDVSLRY--GKTVALDRITLDVPAGLTTGLIGPDGVGKSSLLALASGA--RALQTGGVDALGGDMRSRRHRERV 79
Cdd:COG1123 2 TPLLEVRDLSVRYpgGDVPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGLlpHGGRISGEVLLDGRDLLELSEALR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 80 CRRIAYMPQGLGKNLYPtLSVEENLQFFARLFGHDAGERRRRIDALTQSTGLFPFLSRPAGKLSGGMKQKLGLCCALIHD 159
Cdd:COG1123 82 GRRIGMVFQDPMTQLNP-VTVGDQIAEALENLGLSRAEARARVLELLEAVGLERRLDRYPHQLSGGQRQRVAIAMALALD 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 160 PDLLILDEPTTGVDPLARAQFWDLIARIRDERpTMSVIVATAYMDE-AQRFDWLIAMDAGRVLATGAPAELLARTgcDSL 238
Cdd:COG1123 161 PDLLIADEPTTALDVTTQAEILDLLRELQRER-GTTVLLITHDLGVvAEIADRVVVMDDGRIVEDGPPEEILAAP--QAL 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 239 EAAfIALLPENERRGHKPVKIEPLradaragtaIEARGLTMRF-----GDFTAVDHVSFRIRRGEIFGFLGSNGCGKSTT 313
Cdd:COG1123 238 AAV-PRLGAARGRAAPAAAAAEPL---------LEVRNLSKRYpvrgkGGVRAVDDVSLTLRRGETLGLVGESGSGKSTL 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 314 MKMLTGLLPATEGTAQLFGKEVDPKDINT----RRRVGYMSQ--AFSLYSELTVRQNLVLHARLFGV-PAAEIDARVDEM 386
Cdd:COG1123 308 ARLLLGLLRPTSGSILFDGKDLTKLSRRSlrelRRRVQMVFQdpYSSLNPRMTVGDIIAEPLRLHGLlSRAERRERVAEL 387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 387 ARRFGL-ADIYGMLPDSLPLGMRQRLSLAVAMVHKPELLILDEPTSGVDPVARDSFWQLMIDLARRDLVT-IFIsTHFMN 464
Cdd:COG1123 388 LERVGLpPDLADRYPHELSGGQRQRVAIARALALEPKLLILDEPTSALDVSVQAQILNLLRDLQRELGLTyLFI-SHDLA 466
|
490 500
....*....|....*....|....*.
gi 505416896 465 EAQR-CDRISLMHAGRVLASDSPAEL 489
Cdd:COG1123 467 VVRYiADRVAVMYDGRIVEDGPTEEV 492
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
7-251 |
1.01e-80 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 261.92 E-value: 1.01e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 7 VRFSDVSLRYGKTVALDRITLDVPAGLTTGLIGPDGVGKSSLLALASGARALQTGGVDALGGDMRSRRHRERVCrrIAYM 86
Cdd:COG1131 1 IEVRGLTKRYGDKTALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRVLGEDVARDPAEVRRR--IGYV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 87 PQGLgkNLYPTLSVEENLQFFARLFGHDAGERRRRIDALTQSTGLFPFLSRPAGKLSGGMKQKLGLCCALIHDPDLLILD 166
Cdd:COG1131 79 PQEP--ALYPDLTVRENLRFFARLYGLPRKEARERIDELLELFGLTDAADRKVGTLSGGMKQRLGLALALLHDPELLILD 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 167 EPTTGVDPLARAQFWDLIARIRDERptMSVIVATAYMDEAQRF-DWLIAMDAGRVLATGAPAELLARTgcdsLEAAFIAL 245
Cdd:COG1131 157 EPTSGLDPEARRELWELLRELAAEG--KTVLLSTHYLEEAERLcDRVAIIDKGRIVADGTPDELKARL----LEDVFLEL 230
|
....*.
gi 505416896 246 LPENER 251
Cdd:COG1131 231 TGEEAR 236
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
271-499 |
3.86e-76 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 251.57 E-value: 3.86e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 271 AIEARGLTMRFGDFTAVDHVSFRIRRGEIFGFLGSNGCGKSTTMKMLTGLLPATEGTAQLFGKEVDPKDintRRRVGYMS 350
Cdd:COG4152 1 MLELKGLTKRFGDKTAVDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDSGEVLWDGEPLDPED---RRRIGYLP 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 351 QAFSLYSELTVRQNLVLHARLFGVPAAEIDARVDEMARRFGLADIYGMLPDSLPLGMRQRLSLAVAMVHKPELLILDEPT 430
Cdd:COG4152 78 EERGLYPKMKVGEQLVYLARLKGLSKAEAKRRADEWLERLGLGDRANKKVEELSKGNQQKVQLIAALLHDPELLILDEPF 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 431 SGVDPVARDSFWQLMIDLARRDlVTIFISTHFMNEAQR-CDRISLMHAGRVLASDSPAELVRARGAATLE 499
Cdd:COG4152 158 SGLDPVNVELLKDVIRELAAKG-TTVIFSSHQMELVEElCDRIVIINKGRKVLSGSVDEIRRQFGRNTLR 226
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
272-480 |
2.22e-75 |
|
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: 245.00 E-value: 2.22e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 272 IEARGLTMRFGDFTAVDHVSFRIRRGEIFGFLGSNGCGKSTTMKMLTGLLPATEGTAQLFGKEVDPKDINTRRRVGYMSQ 351
Cdd:cd03230 1 IEVRNLSKRYGKKTALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVLGKDIKKEPEEVKRRIGYLPE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 352 AFSLYSELTVRQNLvlharlfgvpaaeidarvdemarrfgladiygmlpdSLPLGMRQRLSLAVAMVHKPELLILDEPTS 431
Cdd:cd03230 81 EPSLYENLTVRENL------------------------------------KLSGGMKQRLALAQALLHDPELLILDEPTS 124
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 505416896 432 GVDPVARDSFWQLMIDLARRDlVTIFISTHFMNEAQR-CDRISLMHAGRV 480
Cdd:cd03230 125 GLDPESRREFWELLRELKKEG-KTILLSSHILEEAERlCDRVAILNNGRI 173
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
272-489 |
7.38e-75 |
|
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: 245.36 E-value: 7.38e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 272 IEARGLTMRFGDFTAVDHVSFRIRRGEIFGFLGSNGCGKSTTMKMLTGLLPATEGTAQLFGKEVDPKDINTRRRVGYMSQ 351
Cdd:cd03265 1 IEVENLVKKYGDFEAVRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATVAGHDVVREPREVRRRIGIVFQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 352 AFSLYSELTVRQNLVLHARLFGVPAAEIDARVDEMARRFGLADIYGMLPDSLPLGMRQRLSLAVAMVHKPELLILDEPTS 431
Cdd:cd03265 81 DLSVDDELTGWENLYIHARLYGVPGAERRERIDELLDFVGLLEAADRLVKTYSGGMRRRLEIARSLVHRPEVLFLDEPTI 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 505416896 432 GVDPVARDSFWQLMIDLARRDLVTIFISTHFMNEA-QRCDRISLMHAGRVLASDSPAEL 489
Cdd:cd03265 161 GLDPQTRAHVWEYIEKLKEEFGMTILLTTHYMEEAeQLCDRVAIIDHGRIIAEGTPEEL 219
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
272-503 |
2.84e-71 |
|
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: 236.29 E-value: 2.84e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 272 IEARGLTMRFGDFTAVDHVSFRIRRGEIFGFLGSNGCGKSTTMKMLTGLLPATEGTAQLFGKEVDPKDINTRRRVGYMSQ 351
Cdd:COG4555 2 IEVENLSKKYGKVPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIDGEDVRKEPREARRQIGVLPD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 352 AFSLYSELTVRQNLVLHARLFGVPAAEIDARVDEMARRFGLADIYGMLPDSLPLGMRQRLSLAVAMVHKPELLILDEPTS 431
Cdd:COG4555 82 ERGLYDRLTVRENIRYFAELYGLFDEELKKRIEELIELLGLEEFLDRRVGELSTGMKKKVALARALVHDPKVLLLDEPTN 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 505416896 432 GVDPVARDSFWQLMIDLARRDLvTIFISTHFMNEAQR-CDRISLMHAGRVLASDSPAELVRARGAATLEDAFI 503
Cdd:COG4555 162 GLDVMARRLLREILRALKKEGK-TVLFSSHIMQEVEAlCDRVVILHKGKVVAQGSLDELREEIGEENLEDAFV 233
|
|
| drrA |
TIGR01188 |
daunorubicin resistance ABC transporter ATP-binding subunit; This model describes daunorubicin ... |
280-499 |
6.20e-67 |
|
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: 226.50 E-value: 6.20e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 280 RFGDFTAVDHVSFRIRRGEIFGFLGSNGCGKSTTMKMLTGLLPATEGTAQLFGKEV--DPKDIntRRRVGYMSQAFSLYS 357
Cdd:TIGR01188 2 VYGDFKAVDGVNFKVREGEVFGFLGPNGAGKTTTIRMLTTLLRPTSGTARVAGYDVvrEPRKV--RRSIGIVPQYASVDE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 358 ELTVRQNLVLHARLFGVPAAEIDARVDEMARRFGLADIYGMLPDSLPLGMRQRLSLAVAMVHKPELLILDEPTSGVDPVA 437
Cdd:TIGR01188 80 DLTGRENLEMMGRLYGLPKDEAEERAEELLELFELGEAADRPVGTYSGGMRRRLDIAASLIHQPDVLFLDEPTTGLDPRT 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 505416896 438 RDSFWQLMIDLARRDlVTIFISTHFMNEA-QRCDRISLMHAGRVLASDSPAELVRARGAATLE 499
Cdd:TIGR01188 160 RRAIWDYIRALKEEG-VTILLTTHYMEEAdKLCDRIAIIDHGRIIAEGTPEELKRRLGKDTLE 221
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
272-489 |
2.30e-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: 222.00 E-value: 2.30e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 272 IEARGLTMRFGD--FTAVDHVSFRIRRGEIFGFLGSNGCGKSTTMKMLTGLLPATEGTAQLFGKEVDPKDINTRRRVGYM 349
Cdd:cd03263 1 LQIRNLTKTYKKgtKPAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYINGYSIRTDRKAARQSLGYC 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 350 SQAFSLYSELTVRQNLVLHARLFGVPAAEIDARVDEMARRFGLADIYGMLPDSLPLGMRQRLSLAVAMVHKPELLILDEP 429
Cdd:cd03263 81 PQFDALFDELTVREHLRFYARLKGLPKSEIKEEVELLLRVLGLTDKANKRARTLSGGMKRKLSLAIALIGGPSVLLLDEP 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 505416896 430 TSGVDPVARDSFWQLMIDLARRDlvTIFISTHFMNEAQR-CDRISLMHAGRVLASDSPAEL 489
Cdd:cd03263 161 TSGLDPASRRAIWDLILEVRKGR--SIILTTHSMDEAEAlCDRIAIMSDGKLRCIGSPQEL 219
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
272-482 |
2.01e-62 |
|
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: 210.60 E-value: 2.01e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 272 IEARGLTMRFGDFTAVDHVSFRIRRGEIFGFLGSNGCGKSTTMKMLTGLLPATEGTAQLFGKevdPKDINTRRRVGYMSQ 351
Cdd:cd03269 1 LEVENVTKRFGRVTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDGK---PLDIAARNRIGYLPE 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 352 AFSLYSELTVRQNLVLHARLFGVPAAEIDARVDEMARRFGLADIYGMLPDSLPLGMRQRLSLAVAMVHKPELLILDEPTS 431
Cdd:cd03269 78 ERGLYPKMKVIDQLVYLAQLKGLKKEEARRRIDEWLERLELSEYANKRVEELSKGNQQKVQFIAAVIHDPELLILDEPFS 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 505416896 432 GVDPVARDSFWQLMIDLARRDlVTIFISTHFMNEAQR-CDRISLMHAGRVLA 482
Cdd:cd03269 158 GLDPVNVELLKDVIRELARAG-KTVILSTHQMELVEElCDRVLLLNKGRAVL 208
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
272-483 |
1.45e-59 |
|
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: 202.45 E-value: 1.45e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 272 IEARGLTMRFGDFTAVDHVSFRIRRGEIFGFLGSNGCGKSTTMKMLTGLLPATEGTAQLFGKEVDpKDINTRRRVGYMSQ 351
Cdd:cd03268 1 LKTNDLTKTYGKKRVLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEITFDGKSYQ-KNIEALRRIGALIE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 352 AFSLYSELTVRQNLVLHARLFGVPaaeiDARVDEMARRFGLADIYGMLPDSLPLGMRQRLSLAVAMVHKPELLILDEPTS 431
Cdd:cd03268 80 APGFYPNLTARENLRLLARLLGIR----KKRIDEVLDVVGLKDSAKKKVKGFSLGMKQRLGIALALLGNPDLLILDEPTN 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 505416896 432 GVDPVARDSFWQLMIDLARRDlVTIFISTHFMNEAQR-CDRISLMHAGRVLAS 483
Cdd:cd03268 156 GLDPDGIKELRELILSLRDQG-ITVLISSHLLSEIQKvADRIGIINKGKLIEE 207
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
10-250 |
8.24e-57 |
|
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: 196.23 E-value: 8.24e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 10 SDVSLRYGKTVALDRITLDVPAGLTTGLIGPDGVGKSSLLALASGARALQTGGVDALGGDmrSRRHRERVCRRIAYMPQG 89
Cdd:COG4555 5 ENLSKKYGKVPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIDGED--VRKEPREARRQIGVLPDE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 90 LGknLYPTLSVEENLQFFARLFGHDAGERRRRIDALTQSTGLFPFLSRPAGKLSGGMKQKLGLCCALIHDPDLLILDEPT 169
Cdd:COG4555 83 RG--LYDRLTVRENIRYFAELYGLFDEELKKRIEELIELLGLEEFLDRRVGELSTGMKKKVALARALVHDPKVLLLDEPT 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 170 TGVDPLARAQFWDLIARIRDERPTmsVIVATAYMDEAQR-FDWLIAMDAGRVLATGAPAELLARTGCDSLEAAFIALLPE 248
Cdd:COG4555 161 NGLDVMARRLLREILRALKKEGKT--VLFSSHIMQEVEAlCDRVVILHKGKVVAQGSLDELREEIGEENLEDAFVALIGS 238
|
..
gi 505416896 249 NE 250
Cdd:COG4555 239 EE 240
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
268-489 |
1.73e-56 |
|
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: 195.20 E-value: 1.73e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 268 AGTAIEARGLTMRFGDFTAVDHVSFRIRRGEIFGFLGSNGCGKSTTMKMLTGLLPATEGTAQLFGKEV---DPKDINT-R 343
Cdd:COG1127 2 SEPMIEVRNLTKSFGDRVVLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEILVDGQDItglSEKELYElR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 344 RRVGYMSQAFSLYSELTVRQNLVL----HARLfgvPAAEIDARVDEMARRFGLADIYGMLPDSLPLGMRQRLSLAVAMVH 419
Cdd:COG1127 82 RRIGMLFQGGALFDSLTVFENVAFplreHTDL---SEAEIRELVLEKLELVGLPGAADKMPSELSGGMRKRVALARALAL 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 505416896 420 KPELLILDEPTSGVDPVARDSFWQLMIDLaRRDL-VTIFISTHFMNEAQR-CDRISLMHAGRVLASDSPAEL 489
Cdd:COG1127 159 DPEILLYDEPTAGLDPITSAVIDELIREL-RDELgLTSVVVTHDLDSAFAiADRVAVLADGKIIAEGTPEEL 229
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
272-493 |
2.05e-56 |
|
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: 194.47 E-value: 2.05e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 272 IEARGLTMRF-GDFTAVDHVSFRIRRGEIFGFLGSNGCGKSTTMKMLTGLLPATEGTAQLFGKEVDPKDINT-RRRVGYM 349
Cdd:COG1122 1 IELENLSFSYpGGTPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVDGKDITKKNLRElRRKVGLV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 350 -----SQAFslysELTVRQNLVLHARLFGVPAAEIDARVDEMARRFGLADIYGMLPDSLPLGMRQRLSLAVAMVHKPELL 424
Cdd:COG1122 81 fqnpdDQLF----APTVEEDVAFGPENLGLPREEIRERVEEALELVGLEHLADRPPHELSGGQKQRVAIAGVLAMEPEVL 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 425 ILDEPTSGVDPVARDSFWQLMIDLARRDlVTIFISTHFMNEAQR-CDRISLMHAGRVLASDSPAELVRAR 493
Cdd:COG1122 157 VLDEPTAGLDPRGRRELLELLKRLNKEG-KTVIIVTHDLDLVAElADRVIVLDDGRIVADGTPREVFSDY 225
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
268-492 |
1.36e-53 |
|
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: 187.55 E-value: 1.36e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 268 AGTAIEARGLTMRFGDFTAVDHVSFRIRRGEIFGFLGSNGCGKSTTMKMLTGLLPATEGTAQLFGKEVDPKDINTRRRVG 347
Cdd:COG0411 1 SDPLLEVRGLTKRFGGLVAVDDVSLEVERGEIVGLIGPNGAGKTTLFNLITGFYRPTSGRILFDGRDITGLPPHRIARLG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 348 yMSQAF---SLYSELTVRQNLVL--HAR--------LFGVPA-----AEIDARVDEMARRFGLADIYGMLPDSLPLGMRQ 409
Cdd:COG0411 81 -IARTFqnpRLFPELTVLENVLVaaHARlgrgllaaLLRLPRarreeREARERAEELLERVGLADRADEPAGNLSYGQQR 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 410 RLSLAVAMVHKPELLILDEPTSGVDPVARDSFWQLMIDLARRDLVTIFISTHFMNEAQR-CDRISLMHAGRVLASDSPAE 488
Cdd:COG0411 160 RLEIARALATEPKLLLLDEPAAGLNPEETEELAELIRRLRDERGITILLIEHDMDLVMGlADRIVVLDFGRVIAEGTPAE 239
|
....
gi 505416896 489 lVRA 492
Cdd:COG0411 240 -VRA 242
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
272-491 |
1.54e-51 |
|
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: 180.78 E-value: 1.54e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 272 IEARGLTMRFGDFTAVDHVSFRIRRGEIFGFLGSNGCGKSTTMKMLTGLLPATEGTAQLFGKEVDP----KDINTRRRVG 347
Cdd:cd03261 1 IELRGLTKSFGGRTVLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGEDISGlseaELYRLRRRMG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 348 YMSQAFSLYSELTVRQNLVL----HARLfgvPAAEIDARVDEMARRFGLADIYGMLPDSLPLGMRQRLSLAVAMVHKPEL 423
Cdd:cd03261 81 MLFQSGALFDSLTVFENVAFplreHTRL---SEEEIREIVLEKLEAVGLRGAEDLYPAELSGGMKKRVALARALALDPEL 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 505416896 424 LILDEPTSGVDPVARDSFWQLMIDLARRDLVTIFISTHFMNEAQR-CDRISLMHAGRVLASDSPAELVR 491
Cdd:cd03261 158 LLYDEPTAGLDPIASGVIDDLIRSLKKELGLTSIMVTHDLDTAFAiADRIAVLYDGKIVAEGTPEELRA 226
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
7-220 |
1.54e-51 |
|
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: 178.36 E-value: 1.54e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 7 VRFSDVSLRYGKTVALDRITLDVPAGLTTGLIGPDGVGKSSLLALASGARALQTGGVDALGGDMRSRRHRERVCrrIAYM 86
Cdd:cd03230 1 IEVRNLSKRYGKKTALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVLGKDIKKEPEEVKRR--IGYL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 87 PQGLGknLYPTLSVEENLqffarlfghdagerrrridaltqstglfpflsrpagKLSGGMKQKLGLCCALIHDPDLLILD 166
Cdd:cd03230 79 PEEPS--LYENLTVRENL------------------------------------KLSGGMKQRLALAQALLHDPELLILD 120
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 505416896 167 EPTTGVDPLARAQFWDLIARIRDERptMSVIVATAYMDEAQR-FDWLIAMDAGRV 220
Cdd:cd03230 121 EPTSGLDPESRREFWELLRELKKEG--KTILLSSHILEEAERlCDRVAILNNGRI 173
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
272-483 |
5.56e-51 |
|
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: 178.72 E-value: 5.56e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 272 IEARGLTMRFGD----FTAVDHVSFRIRRGEIFGFLGSNGCGKSTTMKMLTGLLPATEGTAQLFGKEVDPKDINTRRRVG 347
Cdd:cd03266 2 ITADALTKRFRDvkktVQAVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDGFDVVKEPAEARRRLG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 348 YMSQAFSLYSELTVRQNLVLHARLFGVPAAEIDARVDEMARRFGLADIYGMLPDSLPLGMRQRLSLAVAMVHKPELLILD 427
Cdd:cd03266 82 FVSDSTGLYDRLTARENLEYFAGLYGLKGDELTARLEELADRLGMEELLDRRVGGFSTGMRQKVAIARALVHDPPVLLLD 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 505416896 428 EPTSGVDPVARDSFWQLMIDLaRRDLVTIFISTHFMNEAQR-CDRISLMHAGRVLAS 483
Cdd:cd03266 162 EPTTGLDVMATRALREFIRQL-RALGKCILFSTHIMQEVERlCDRVVVLHRGRVVYE 217
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
268-489 |
1.08e-50 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 182.61 E-value: 1.08e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 268 AGTAIEARGLTMRFGDFTAVDHVSFRIRRGEIFGFLGSNGCGKSTTMKMLTGLLPATEGTAQLFGKEVDPKDINtRRRVG 347
Cdd:COG3842 2 AMPALELENVSKRYGDVTALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRILLDGRDVTGLPPE-KRNVG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 348 YMSQAFSLYSELTVRQNLVLHARLFGVPAAEIDARVDEMARRFGLADIYGMLPDSLPLGMRQRLSLAVAMVHKPELLILD 427
Cdd:COG3842 81 MVFQDYALFPHLTVAENVAFGLRMRGVPKAEIRARVAELLELVGLEGLADRYPHQLSGGQQQRVALARALAPEPRVLLLD 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 505416896 428 EPTSGVDPVARDSFWQLMIDLARR-DLVTIFIsTHFMNEAQR-CDRISLMHAGRVLASDSPAEL 489
Cdd:COG3842 161 EPLSALDAKLREEMREELRRLQRElGITFIYV-THDQEEALAlADRIAVMNDGRIEQVGTPEEI 223
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
272-491 |
1.11e-50 |
|
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: 178.40 E-value: 1.11e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 272 IEARGLTMRFGDFTAVDHVSFRIRRGEIFGFLGSNGCGKSTTMKMLTGLLPATEGTAQLFGKEVDPKDINTRRRVGyMSQ 351
Cdd:cd03219 1 LEVRGLTKRFGGLVALDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFDGEDITGLPPHEIARLG-IGR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 352 AF---SLYSELTVRQNLVLHARLFGVPA----------AEIDARVDEMARRFGLADIYGMLPDSLPLGMRQRLSLAVAMV 418
Cdd:cd03219 80 TFqipRLFPELTVLENVMVAAQARTGSGlllararreeREARERAEELLERVGLADLADRPAGELSYGQQRRLEIARALA 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 505416896 419 HKPELLILDEPTSGVDPVARDSFWQLMIDLARRDlVTIFISTHFMNEAQR-CDRISLMHAGRVLASDSPAELVR 491
Cdd:cd03219 160 TDPKLLLLDEPAAGLNPEETEELAELIRELRERG-ITVLLVEHDMDVVMSlADRVTVLDQGRVIAEGTPDEVRN 232
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
6-480 |
3.06e-50 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 185.61 E-value: 3.06e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 6 VVRFSDVSLRYGKTVALDRITLDVPAGLTTGLIGPDGVGKSSLLALASGARALQTGGVDALGGDMRSRRHRERVCRRIAY 85
Cdd:COG1129 4 LLEMRGISKSFGGVKALDGVSLELRPGEVHALLGENGAGKSTLMKILSGVYQPDSGEILLDGEPVRFRSPRDAQAAGIAI 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 86 MPQGLgkNLYPTLSVEENLqFFARLFGH----DAGERRRRIDALTQSTGL-FPfLSRPAGKLSGGMKQKLGLCCALIHDP 160
Cdd:COG1129 84 IHQEL--NLVPNLSVAENI-FLGREPRRggliDWRAMRRRARELLARLGLdID-PDTPVGDLSVAQQQLVEIARALSRDA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 161 DLLILDEPTTGVDPLARAQFWDLIARIRDERptMSVIVATAYMDEAQRF-DWLIAMDAGRVLATGAPAELLArtgcDSLE 239
Cdd:COG1129 160 RVLILDEPTASLTEREVERLFRIIRRLKAQG--VAIIYISHRLDEVFEIaDRVTVLRDGRLVGTGPVAELTE----DELV 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 240 AAFIallpenerrGHKPVKIEPLRADARAGTAIEARGLTMRfgdfTAVDHVSFRIRRGEIFGFLGSNGCGKSTTMKMLTG 319
Cdd:COG1129 234 RLMV---------GRELEDLFPKRAAAPGEVVLEVEGLSVG----GVVRDVSFSVRAGEILGIAGLVGAGRTELARALFG 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 320 LLPATEGTAQLFGKEVDPKDINT--RRRVGYMS---QAFSLYSELTVRQNLVL-----HARLFGVPAAEIDARVDEMARR 389
Cdd:COG1129 301 ADPADSGEIRLDGKPVRIRSPRDaiRAGIAYVPedrKGEGLVLDLSIRENITLasldrLSRGGLLDRRRERALAEEYIKR 380
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 390 FGL--ADIYgMLPDSLPLGMRQRLSLAVAMVHKPELLILDEPTSGVDPVARDSFWQLMIDLARRDLVTIFISTHfMNEAQ 467
Cdd:COG1129 381 LRIktPSPE-QPVGNLSGGNQQKVVLAKWLATDPKVLILDEPTRGIDVGAKAEIYRLIRELAAEGKAVIVISSE-LPELL 458
|
490
....*....|....
gi 505416896 468 R-CDRISLMHAGRV 480
Cdd:COG1129 459 GlSDRILVMREGRI 472
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
266-501 |
5.36e-50 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 177.59 E-value: 5.36e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 266 ARAGTAIEARGLTMRF----GDFTAVDHVSFRIRRGEIFGFLGSNGCGKSTTMKMLTGLLPATEGTAQLFGKEVDPKDin 341
Cdd:COG1116 2 SAAAPALELRGVSKRFptggGGVTALDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPTSGEVLVDGKPVTGPG-- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 342 trRRVGYMSQAFSLYSELTVRQNLVLHARLFGVPAAEIDARVDEMARRFGLADIYGMLPDSLPLGMRQRLSLAVAMVHKP 421
Cdd:COG1116 80 --PDRGVVFQEPALLPWLTVLDNVALGLELRGVPKAERRERARELLELVGLAGFEDAYPHQLSGGMRQRVAIARALANDP 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 422 ELLILDEPTSGVDPVARDSFWQLMIDLARRDLVTIFISTHFMNEAQR-CDRISLMHA--GRVLAsDSPAELVRARGAATL 498
Cdd:COG1116 158 EVLLMDEPFGALDALTRERLQDELLRLWQETGKTVLFVTHDVDEAVFlADRVVVLSArpGRIVE-EIDVDLPRPRDRELR 236
|
...
gi 505416896 499 EDA 501
Cdd:COG1116 237 TSP 239
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
272-482 |
5.84e-49 |
|
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: 173.04 E-value: 5.84e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 272 IEARGLTMRFGD----FTAVDHVSFRIRRGEIFGFLGSNGCGKSTTMKMLTGLLPATEGTAQLFGKEVDPkdinTRRRVG 347
Cdd:cd03293 1 LEVRNVSKTYGGgggaVTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVDGEPVTG----PGPDRG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 348 YMSQAFSLYSELTVRQNLVLHARLFGVPAAEIDARVDEMARRFGLADIYGMLPDSLPLGMRQRLSLAVAMVHKPELLILD 427
Cdd:cd03293 77 YVFQQDALLPWLTVLDNVALGLELQGVPKAEARERAEELLELVGLSGFENAYPHQLSGGMRQRVALARALAVDPDVLLLD 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 505416896 428 EPTSGVDPVARDSFWQLMIDLARRDLVTIFISTHFMNEAQR-CDRISLMHA--GRVLA 482
Cdd:cd03293 157 EPFSALDALTREQLQEELLDIWRETGKTVLLVTHDIDEAVFlADRVVVLSArpGRIVA 214
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
272-482 |
9.11e-49 |
|
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: 172.32 E-value: 9.11e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 272 IEARGLTMRFGDFTAVDHVSFRIRRGEIFGFLGSNGCGKSTTMKMLTGLLPATEGtaQLFgkeVDPKDINT----RRRVG 347
Cdd:cd03259 1 LELKGLSKTYGSVRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSG--EIL---IDGRDVTGvppeRRNIG 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 348 YMSQAFSLYSELTVRQNLVLHARLFGVPAAEIDARVDEMARRFGLADIYGMLPDSLPLGMRQRLSLAVAMVHKPELLILD 427
Cdd:cd03259 76 MVFQDYALFPHLTVAENIAFGLKLRGVPKAEIRARVRELLELVGLEGLLNRYPHELSGGQQQRVALARALAREPSLLLLD 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 505416896 428 EPTSGVDPVARDSFWQLMIDLARRDLVTIFISTHFMNEAQR-CDRISLMHAGRVLA 482
Cdd:cd03259 156 EPLSALDAKLREELREELKELQRELGITTIYVTHDQEEALAlADRIAVMNEGRIVQ 211
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
271-490 |
1.24e-48 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 175.38 E-value: 1.24e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 271 AIEARGLTMRFGDFTAVDHVSFRIRRGEIFGFLGSNGCGKSTTMKMLTGLLPATEGTAQLFGKEVDPKDINTRRRVGYMS 350
Cdd:PRK13537 7 PIDFRNVEKRYGDKLVVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCGEPVPSRARHARQRVGVVP 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 351 QAFSLYSELTVRQNLVLHARLFGVPAAEIDARVD---EMARRFGLADIYgmlPDSLPLGMRQRLSLAVAMVHKPELLILD 427
Cdd:PRK13537 87 QFDNLDPDFTVRENLLVFGRYFGLSAAAARALVPpllEFAKLENKADAK---VGELSGGMKRRLTLARALVNDPDVLVLD 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 505416896 428 EPTSGVDPVARDSFWQLMIDLARRDlVTIFISTHFMNEAQR-CDRISLMHAGRVLASDSPAELV 490
Cdd:PRK13537 164 EPTTGLDPQARHLMWERLRSLLARG-KTILLTTHFMEEAERlCDRLCVIEEGRKIAEGAPHALI 226
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
7-229 |
1.98e-48 |
|
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: 171.53 E-value: 1.98e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 7 VRFSDVSLRYGK--TVALDRITLDVPAGLTTGLIGPDGVGKSSLLALASGARALQTGGVDALGGDMRSRRHRERVCrrIA 84
Cdd:cd03263 1 LQIRNLTKTYKKgtKPAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYINGYSIRTDRKAARQS--LG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 85 YMPQGlgKNLYPTLSVEENLQFFARLFGHDAGERRRRIDALTQSTGLFPFLSRPAGKLSGGMKQKLGLCCALIHDPDLLI 164
Cdd:cd03263 79 YCPQF--DALFDELTVREHLRFYARLKGLPKSEIKEEVELLLRVLGLTDKANKRARTLSGGMKRKLSLAIALIGGPSVLL 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 505416896 165 LDEPTTGVDPLARAQFWDLIARIRDERptmSVIVATAYMDEAQRFDWLIA-MDAGRVLATGAPAEL 229
Cdd:cd03263 157 LDEPTSGLDPASRRAIWDLILEVRKGR---SIILTTHSMDEAEALCDRIAiMSDGKLRCIGSPQEL 219
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
272-480 |
7.33e-48 |
|
ATP-binding cassette domain of the transporters involved in export of lipoprotein and macrolide, and Cell division ATP-binding protein FtsE; This family is comprised of MJ0796 ATP-binding cassette, macrolide-specific ABC-type efflux carrier (MacAB), and proteins involved in cell division (FtsE), and release of lipoproteins from the cytoplasmic membrane (LolCDE). They are clustered together phylogenetically. MacAB is an exporter that confers resistance to macrolides, while the LolCDE system is not a transporter at all. The FtsEX complex resembles an ABC transporter, where FtsE is the ATPase and the membrane subunit FtsX resembles a permease subunit. But rather than transporting any substrate, the complex acts in cell division by undergoing conformational changes that alter the activity of cell wall hydrolases located outside the plasma membrane. The complex is widely conserved in bacteria, but also extremely divergent in sequence between different lineages. The LolCDE complex catalyzes the release of lipoproteins from the cytoplasmic membrane prior to their targeting to the outer membrane.
Pssm-ID: 213222 [Multi-domain] Cd Length: 218 Bit Score: 169.98 E-value: 7.33e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 272 IEARGLTMRFGD----FTAVDHVSFRIRRGEIFGFLGSNGCGKSTTMKMLTGLLPATEGTAQLFGKEVDPKDINT----- 342
Cdd:cd03255 1 IELKNLSKTYGGggekVQALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRVDGTDISKLSEKElaafr 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 343 RRRVGYMSQAFSLYSELTVRQNLVLHARLFGVPAAEIDARVDEMARRFGLADIYGMLPDSLPLGMRQRLSLAVAMVHKPE 422
Cdd:cd03255 81 RRHIGFVFQSFNLLPDLTALENVELPLLLAGVPKKERRERAEELLERVGLGDRLNHYPSELSGGQQQRVAIARALANDPK 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 505416896 423 LLILDEPTSGVDPVARDSFWQLMIDLARRDLVTIFISTHFMNEAQRCDRISLMHAGRV 480
Cdd:cd03255 161 IILADEPTGNLDSETGKEVMELLRELNKEAGTTIVVVTHDPELAEYADRIIELRDGKI 218
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
246-490 |
1.77e-47 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 173.09 E-value: 1.77e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 246 LPENERRGHKPVKIEPLRADARAGTAIEARGLTMRFGDFTAVDHVSFRIRRGEIFGFLGSNGCGKSTTMKMLTGLLPATE 325
Cdd:PRK13536 16 LSPIERKHQGISEAKASIPGSMSTVAIDLAGVSKSYGDKAVVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDA 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 326 GTAQLFGKEVDPKDINTRRRVGYMSQAFSLYSELTVRQNLVLHARLFGVPAAEIDARVD---EMARRFGLADIYgmlPDS 402
Cdd:PRK13536 96 GKITVLGVPVPARARLARARIGVVPQFDNLDLEFTVRENLLVFGRYFGMSTREIEAVIPsllEFARLESKADAR---VSD 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 403 LPLGMRQRLSLAVAMVHKPELLILDEPTSGVDPVARDSFWQLMIDLARRDLvTIFISTHFMNEAQR-CDRISLMHAGRVL 481
Cdd:PRK13536 173 LSGGMKRRLTLARALINDPQLLILDEPTTGLDPHARHLIWERLRSLLARGK-TILLTTHFMEEAERlCDRLCVLEAGRKI 251
|
....*....
gi 505416896 482 ASDSPAELV 490
Cdd:PRK13536 252 AEGRPHALI 260
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
273-479 |
4.04e-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: 167.26 E-value: 4.04e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 273 EARGLTMRFGDFT--AVDHVSFRIRRGEIFGFLGSNGCGKSTTMKMLTGLLPATEGTAQLFGKEVDPKDINT-RRRVGYM 349
Cdd:cd03225 1 ELKNLSFSYPDGArpALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDLTKLSLKElRRKVGLV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 350 SQ-AFSLYSELTVRQNLVLHARLFGVPAAEIDARVDEMARRFGLADIYGMLPDSLPLGMRQRLSLAVAMVHKPELLILDE 428
Cdd:cd03225 81 FQnPDDQFFGPTVEEEVAFGLENLGLPEEEIEERVEEALELVGLEGLRDRSPFTLSGGQKQRVAIAGVLAMDPDILLLDE 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 505416896 429 PTSGVDPVARDSFWQLMIDLaRRDLVTIFISTHFMNEAQR-CDRISLMHAGR 479
Cdd:cd03225 161 PTAGLDPAGRRELLELLKKL-KAEGKTIIIVTHDLDLLLElADRVIVLEDGK 211
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
272-483 |
4.58e-47 |
|
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: 167.37 E-value: 4.58e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 272 IEARGLTMRFGDFTAVDHVSFRIRRGeIFGFLGSNGCGKSTTMKMLTGLLPATEGTAQLFGKEVDPKDINTRRRVGYMSQ 351
Cdd:cd03264 1 LQLENLTKRYGKKRALDGVSLTLGPG-MYGLLGPNGAGKTTLMRILATLTPPSSGTIRIDGQDVLKQPQKLRRRIGYLPQ 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 352 AFSLYSELTVRQNLVLHARLFGVPAAEIDARVDEMARRFGLADIYGMLPDSLPLGMRQRLSLAVAMVHKPELLILDEPTS 431
Cdd:cd03264 80 EFGVYPNFTVREFLDYIAWLKGIPSKEVKARVDEVLELVNLGDRAKKKIGSLSGGMRRRVGIAQALVGDPSILIVDEPTA 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 505416896 432 GVDPVARDSFWQLMIDLARRdlVTIFISTHFMNE-AQRCDRISLMHAGRVLAS 483
Cdd:cd03264 160 GLDPEERIRFRNLLSELGED--RIVILSTHIVEDvESLCNQVAVLNKGKLVFE 210
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
272-491 |
1.11e-46 |
|
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: 167.48 E-value: 1.11e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 272 IEARGLTMRFGD-FTAVDHVSFRIRRGEIFGFLGSNGCGKSTTMKMLTGLLPATEGTAQLFGK---EVDPkdINTRRRVG 347
Cdd:cd03295 1 IEFENVTKRYGGgKKAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGEdirEQDP--VELRRKIG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 348 YMSQAFSLYSELTVRQNLVLHARLFGVPAAEIDARVDEMARRFGL-----ADIYgmlPDSLPLGMRQRLSLAVAMVHKPE 422
Cdd:cd03295 79 YVIQQIGLFPHMTVEENIALVPKLLKWPKEKIRERADELLALVGLdpaefADRY---PHELSGGQQQRVGVARALAADPP 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 423 LLILDEPTSGVDPVARDSFWQLMIDLARRDLVTIFISTHFMNEAQR-CDRISLMHAGRVLASDSPAELVR 491
Cdd:cd03295 156 LLLMDEPFGALDPITRDQLQEEFKRLQQELGKTIVFVTHDIDEAFRlADRIAIMKNGEIVQVGTPDEILR 225
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
271-502 |
1.51e-46 |
|
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: 167.53 E-value: 1.51e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 271 AIEARGLTMRFGDFTAVDHVSFRIRRGEIFGFLGSNGCGKSTTMKMLTGLLPATEGTAQLFGKEV---DPKDIntRRRVG 347
Cdd:COG1120 1 MLEAENLSVGYGGRPVLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDGRDLaslSRREL--ARRIA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 348 YMSQAFSLYSELTVRQnLVL-----HARLFGVPAAEIDARVDEMARRFGLADIYGMLPDSLPLGMRQRLSLAVAMVHKPE 422
Cdd:COG1120 79 YVPQEPPAPFGLTVRE-LVAlgrypHLGLFGRPSAEDREAVEEALERTGLEHLADRPVDELSGGERQRVLIARALAQEPP 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 423 LLILDEPTSGVDPVARDSFWQLMIDLARRDLVTIFISTHFMNEAQR-CDRISLMHAGRVLASDSPAELVRargAATLEDA 501
Cdd:COG1120 158 LLLLDEPTSHLDLAHQLEVLELLRRLARERGRTVVMVLHDLNLAARyADRLVLLKDGRIVAQGPPEEVLT---PELLEEV 234
|
.
gi 505416896 502 F 502
Cdd:COG1120 235 Y 235
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
270-489 |
2.53e-46 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 169.87 E-value: 2.53e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 270 TAIEARGLTMRFGDFTAVDHVSFRIRRGEIFGFLGSNGCGKSTTMKMLTGLLPATEGTAQLFGKEV---DPKDintrRRV 346
Cdd:COG3839 2 ASLELENVSKSYGGVEALKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAGLEDPTSGEILIGGRDVtdlPPKD----RNI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 347 GYMSQAFSLYSELTVRQNLVLHARLFGVPAAEIDARVDEMARRFGLADIYGMLPDSLPLGMRQRLSLAVAMVHKPELLIL 426
Cdd:COG3839 78 AMVFQSYALYPHMTVYENIAFPLKLRKVPKAEIDRRVREAAELLGLEDLLDRKPKQLSGGQRQRVALGRALVREPKVFLL 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 505416896 427 DEPTSGVDPVARdsfWQLMIDLAR--RDL-VTIFISTHFMNEAQR-CDRISLMHAGRVLASDSPAEL 489
Cdd:COG3839 158 DEPLSNLDAKLR---VEMRAEIKRlhRRLgTTTIYVTHDQVEAMTlADRIAVMNDGRIQQVGTPEEL 221
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
270-482 |
8.62e-46 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 164.06 E-value: 8.62e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 270 TAIEARGLTMRFGD----FTAVDHVSFRIRRGEIFGFLGSNGCGKSTTMKMLTGLLPATEGTAQLFGKEV---DPKDINT 342
Cdd:COG1136 3 PLLELRNLTKSYGTgegeVTALRGVSLSIEAGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVLIDGQDIsslSERELAR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 343 --RRRVGYMSQAFSLYSELTVRQNLVLHARLFGVPAAEIDARVDEMARRFGLADIYGMLPDSLPLGMRQRLSLAVAMVHK 420
Cdd:COG1136 83 lrRRHIGFVFQFFNLLPELTALENVALPLLLAGVSRKERRERARELLERVGLGDRLDHRPSQLSGGQQQRVAIARALVNR 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 505416896 421 PELLILDEPTSGVDPVARDSFWQLMIDLARRDLVTIFISTHFMNEAQRCDRISLMHAGRVLA 482
Cdd:COG1136 163 PKLILADEPTGNLDSKTGEEVLELLRELNRELGTTIVMVTHDPELAARADRVIRLRDGRIVS 224
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
271-491 |
3.29e-45 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 170.98 E-value: 3.29e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 271 AIEARGLTMRFGDFTAVDHVSFRIRRGEIFGFLGSNGCGKSTTMKMLTGLLPATEGTAQLFGKEV---DPKDINtRRRVG 347
Cdd:COG3845 5 ALELRGITKRFGGVVANDDVSLTVRPGEIHALLGENGAGKSTLMKILYGLYQPDSGEILIDGKPVrirSPRDAI-ALGIG 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 348 YMSQAFSLYSELTVRQNLVL---HARLFGVPAAEIDARVDEMARRFGLA-DiygmlPD----SLPLGMRQRLSLAVAMVH 419
Cdd:COG3845 84 MVHQHFMLVPNLTVAENIVLglePTKGGRLDRKAARARIRELSERYGLDvD-----PDakveDLSVGEQQRVEILKALYR 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 505416896 420 KPELLILDEPTSGVDPVARDSFWQLMIDLARRDLVTIFIsTHFMNEAQR-CDRISLMHAGRV-----LASDSPAELVR 491
Cdd:COG3845 159 GARILILDEPTAVLTPQEADELFEILRRLAAEGKSIIFI-THKLREVMAiADRVTVLRRGKVvgtvdTAETSEEELAE 235
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
270-502 |
6.58e-45 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 162.18 E-value: 6.58e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 270 TAIEARGLTMRFGDFTAVDHVSFRIRRGEIFGFLGSNGCGKSTTMKMLTGLLPATEGTAQLFGKEVDPKdintRRRVGYM 349
Cdd:COG1121 5 PAIELENLTVSYGGRPVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLFGKPPRRA----RRRIGYV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 350 SQAFSLYSE--LTVRQnLVL-----HARLFGVPAAEIDARVDEMARRFGLADIYGMLPDSLPLGMRQRLSLAVAMVHKPE 422
Cdd:COG1121 81 PQRAEVDWDfpITVRD-VVLmgrygRRGLFRRPSRADREAVDEALERVGLEDLADRPIGELSGGQQQRVLLARALAQDPD 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 423 LLILDEPTSGVDPVARDSFWQLMIDLARRDlVTIFISTHFMNEAQR-CDRISLMhAGRVLASDSPAELVRargAATLEDA 501
Cdd:COG1121 160 LLLLDEPFAGVDAATEEALYELLRELRREG-KTILVVTHDLGAVREyFDRVLLL-NRGLVAHGPPEEVLT---PENLSRA 234
|
.
gi 505416896 502 F 502
Cdd:COG1121 235 Y 235
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
272-479 |
1.20e-44 |
|
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: 159.27 E-value: 1.20e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 272 IEARGLTMRFGDFTAVDHVSFRIRRGEIFGFLGSNGCGKSTTMKMLTGLLPATEGTAQLFGKEVDPKDINT---RRRVGY 348
Cdd:cd03229 1 LELKNVSKRYGQKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGEDLTDLEDELpplRRRIGM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 349 MSQAFSLYSELTVRQNLVLhaRLFGvpaaeidarvdemarrfgladiygmlpdslplGMRQRLSLAVAMVHKPELLILDE 428
Cdd:cd03229 81 VFQDFALFPHLTVLENIAL--GLSG--------------------------------GQQQRVALARALAMDPDVLLLDE 126
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 505416896 429 PTSGVDPVARDSFWQLMIDLARRDLVTIFISTHFMNEAQR-CDRISLMHAGR 479
Cdd:cd03229 127 PTSALDPITRREVRALLKSLQAQLGITVVLVTHDLDEAARlADRVVVLRDGK 178
|
|
| drrA |
TIGR01188 |
daunorubicin resistance ABC transporter ATP-binding subunit; This model describes daunorubicin ... |
15-261 |
2.95e-44 |
|
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: 162.56 E-value: 2.95e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 15 RYGKTVALDRITLDVPAGLTTGLIGPDGVGKSSLLALASGARALQTGGVDALGGDMRSRRHRERVCrrIAYMPQGlgKNL 94
Cdd:TIGR01188 2 VYGDFKAVDGVNFKVREGEVFGFLGPNGAGKTTTIRMLTTLLRPTSGTARVAGYDVVREPRKVRRS--IGIVPQY--ASV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 95 YPTLSVEENLQFFARLFGHDAGERRRRIDALTQSTGLFPFLSRPAGKLSGGMKQKLGLCCALIHDPDLLILDEPTTGVDP 174
Cdd:TIGR01188 78 DEDLTGRENLEMMGRLYGLPKDEAEERAEELLELFELGEAADRPVGTYSGGMRRRLDIAASLIHQPDVLFLDEPTTGLDP 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 175 LARAQFWDLIARIRDERptMSVIVATAYMDEAQRF-DWLIAMDAGRVLATGAPAELLARTGCDSLEAAFIALLPENERRG 253
Cdd:TIGR01188 158 RTRRAIWDYIRALKEEG--VTILLTTHYMEEADKLcDRIAIIDHGRIIAEGTPEELKRRLGKDTLESRPRDIQSLKVEVS 235
|
....*...
gi 505416896 254 HKPVKIEP 261
Cdd:TIGR01188 236 MLIAELGE 243
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
285-491 |
5.21e-44 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 162.56 E-value: 5.21e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 285 TAVDHVSFRIRRGEIFGFLGSNGCGKSTTMKMLTGLLPATEGTAQLFGKevDPkdinTRRRVGY-------MSQAFSLYS 357
Cdd:COG4586 36 EAVDDISFTIEPGEIVGFIGPNGAGKSTTIKMLTGILVPTSGEVRVLGY--VP----FKRRKEFarrigvvFGQRSQLWW 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 358 ELTVRQNLVLHARLFGVPAAEIDARVDEMARRFGLADIYGMLPDSLPLGMRQRLSLAVAMVHKPELLILDEPTSGVDPVA 437
Cdd:COG4586 110 DLPAIDSFRLLKAIYRIPDAEYKKRLDELVELLDLGELLDTPVRQLSLGQRMRCELAAALLHRPKILFLDEPTIGLDVVS 189
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 505416896 438 RDSFWQLMIDLARRDLVTIFISTHFMNEAQR-CDRISLMHAGRVLASDSPAELVR 491
Cdd:COG4586 190 KEAIREFLKEYNRERGTTILLTSHDMDDIEAlCDRVIVIDHGRIIYDGSLEELKE 244
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
272-489 |
3.44e-43 |
|
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: 156.97 E-value: 3.44e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 272 IEARGLTMRFGD----FTAVDHVSFRIRRGEIFGFLGSNGCGKSTTMKMLTGLLPATEGTAQLFGKEV---DPKDI-NTR 343
Cdd:cd03258 2 IELKNVSKVFGDtggkVTALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGSVLVDGTDLtllSGKELrKAR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 344 RRVGYMSQAFSLYSELTVRQNLVLHARLFGVPAAEIDARVDEMARRFGLADIYGMLPDSLPLGMRQRLSLAVAMVHKPEL 423
Cdd:cd03258 82 RRIGMIFQHFNLLSSRTVFENVALPLEIAGVPKAEIEERVLELLELVGLEDKADAYPAQLSGGQKQRVGIARALANNPKV 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 505416896 424 LILDEPTSGVDPVARDSFWQLMIDLARRDLVTIFISTHFMNEAQR-CDRISLMHAGRVLASDSPAEL 489
Cdd:cd03258 162 LLCDEATSALDPETTQSILALLRDINRELGLTIVLITHEMEVVKRiCDRVAVMEKGEVVEEGTVEEV 228
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
272-474 |
8.07e-43 |
|
ABC-type transport system involved in cytochrome c biogenesis, ATPase component [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 443308 [Multi-domain] Cd Length: 206 Bit Score: 154.94 E-value: 8.07e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 272 IEARGLTMRFGDFTAVDHVSFRIRRGEIFGFLGSNGCGKSTTMKMLTGLLPATEGTAQLFGKEVDPKDINTRRRVGYMSQ 351
Cdd:COG4133 3 LEAENLSCRRGERLLFSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWNGEPIRDAREDYRRRLAYLGH 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 352 AFSLYSELTVRQNLVLHARLFGVPAAeiDARVDEMARRFGLADIYGMLPDSLPLGMRQRLSLAVAMVHKPELLILDEPTS 431
Cdd:COG4133 83 ADGLKPELTVRENLRFWAALYGLRAD--REAIDEALEAVGLAGLADLPVRQLSAGQKRRVALARLLLSPAPLWLLDEPFT 160
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 505416896 432 GVDPVARDSFWQLMIDLARRDlVTIFISTHFMNEAQRCDRISL 474
Cdd:COG4133 161 ALDAAGVALLAELIAAHLARG-GAVLLTTHQPLELAAARVLDL 202
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
9-430 |
8.75e-43 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 164.08 E-value: 8.75e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 9 FSDVSLRYGKTVALDRITLDVPAGLTTGLIGPDGVGKSSLLALASGARALQTGGVdALGGDMRsrrhrervcrrIAYMPQ 88
Cdd:COG0488 1 LENLSKSFGGRPLLDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEV-SIPKGLR-----------IGYLPQ 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 89 GLgkNLYPTLSV----------------------------EENLQFFARLFG----HDAGERRRRIDALTQSTGLFPF-L 135
Cdd:COG0488 69 EP--PLDDDLTVldtvldgdaelraleaeleeleaklaepDEDLERLAELQEefeaLGGWEAEARAEEILSGLGFPEEdL 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 136 SRPAGKLSGGMKQKLGLCCALIHDPDLLILDEPTTGVDplARAQFWdLIARIRDERPTMSVI---------VAT------ 200
Cdd:COG0488 147 DRPVSELSGGWRRRVALARALLSEPDLLLLDEPTNHLD--LESIEW-LEEFLKNYPGTVLVVshdryfldrVATrileld 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 201 ------------AYMDE-AQRFDWLIAMDAGRvlatgapAELLARtgcdslEAAFIALLPENERRGHKPV-------KIE 260
Cdd:COG0488 224 rgkltlypgnysAYLEQrAERLEQEAAAYAKQ-------QKKIAK------EEEFIRRFRAKARKAKQAQsrikaleKLE 290
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 261 PLRADARAGTA--------------IEARGLTMRFGDFTAVDHVSFRIRRGEIFGFLGSNGCGKSTTMKMLTGLLPATEG 326
Cdd:COG0488 291 REEPPRRDKTVeirfppperlgkkvLELEGLSKSYGDKTLLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPDSG 370
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 327 TAQLfGKEVdpkdintrrRVGYMSQAF-SLYSELTVRQNLvlhaRLFGVPAAEIDARvdEMARRFGL--ADIY------- 396
Cdd:COG0488 371 TVKL-GETV---------KIGYFDQHQeELDPDKTVLDEL----RDGAPGGTEQEVR--GYLGRFLFsgDDAFkpvgvls 434
|
490 500 510
....*....|....*....|....*....|....
gi 505416896 397 GmlpdslplGMRQRLSLAVAMVHKPELLILDEPT 430
Cdd:COG0488 435 G--------GEKARLALAKLLLSPPNVLLLDEPT 460
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
273-484 |
1.42e-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: 154.61 E-value: 1.42e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 273 EARGLTMRFGDFTAVDHVSFRIRRGEIFGFLGSNGCGKSTTMKMLTGLLPATEGTAQLFGKEVDpkdiNTRRRVGYMSQA 352
Cdd:cd03235 1 EVEDLTVSYGGHPVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFGKPLE----KERKRIGYVPQR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 353 FSL--YSELTVRQ----NLVLHARLFGVPAAEIDARVDEMARRFGLADIYGMLPDSLPLGMRQRLSLAVAMVHKPELLIL 426
Cdd:cd03235 77 RSIdrDFPISVRDvvlmGLYGHKGLFRRLSKADKAKVDEALERVGLSELADRQIGELSGGQQQRVLLARALVQDPDLLLL 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 505416896 427 DEPTSGVDPVARDSFWQLMIDLARRDLvTIFISTHFMNEAQR-CDRISLMhAGRVLASD 484
Cdd:cd03235 157 DEPFAGVDPKTQEDIYELLRELRREGM-TILVVTHDLGLVLEyFDRVLLL-NRTVVASG 213
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
270-492 |
1.84e-42 |
|
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: 163.15 E-value: 1.84e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 270 TAIEARGLTMRF--GDFTAVDHVSFRIRRGEIFGFLGSNGCGKSTTMKMLTGLLPAT---EGTAQLFGKEVDPKDINTR- 343
Cdd:COG1123 3 PLLEVRDLSVRYpgGDVPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGLLPHGgriSGEVLLDGRDLLELSEALRg 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 344 RRVGYMSQ-AFSLYSELTVRQNLVLHARLFGVPAAEIDARVDEMARRFGLADIYGMLPDSLPLGMRQRLSLAVAMVHKPE 422
Cdd:COG1123 83 RRIGMVFQdPMTQLNPVTVGDQIAEALENLGLSRAEARARVLELLEAVGLERRLDRYPHQLSGGQRQRVAIAMALALDPD 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 505416896 423 LLILDEPTSGVDPVARDSFWQLMIDLARRDLVTIFISTHFMNE-AQRCDRISLMHAGRVLASDSPAELVRA 492
Cdd:COG1123 163 LLIADEPTTALDVTTQAEILDLLRELQRERGTTVLLITHDLGVvAEIADRVVVMDDGRIVEDGPPEEILAA 233
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
272-488 |
6.99e-42 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 152.90 E-value: 6.99e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 272 IEARGLTMRF-GDFTAVDHVSFRIRRGEiFGFL-GSNGCGKSTTMKMLTGLLPATEGTAQLFGKEV---DPKDI-NTRRR 345
Cdd:COG2884 2 IRFENVSKRYpGGREALSDVSLEIEKGE-FVFLtGPSGAGKSTLLKLLYGEERPTSGQVLVNGQDLsrlKRREIpYLRRR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 346 VGYMSQAFSLYSELTVRQNLVLHARLFGVPAAEIDARVDEMARRFGLADIYGMLPDSLPLGMRQRLSLAVAMVHKPELLI 425
Cdd:COG2884 81 IGVVFQDFRLLPDRTVYENVALPLRVTGKSRKEIRRRVREVLDLVGLSDKAKALPHELSGGEQQRVAIARALVNRPELLL 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 505416896 426 LDEPTSGVDPVARDSFWQLMIDLARRDlVTIFISTH---FMNEAQRcdRISLMHAGRVLASDSPAE 488
Cdd:COG2884 161 ADEPTGNLDPETSWEIMELLEEINRRG-TTVLIATHdleLVDRMPK--RVLELEDGRLVRDEARGV 223
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
272-489 |
7.21e-42 |
|
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: 153.11 E-value: 7.21e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 272 IEARGLTMRFGDFTAVDHVSFRIRRGEIFGFLGSNGCGKSTTMKMLTGLLPA-----TEGTAQLFGKEVDPKDINT---R 343
Cdd:cd03260 1 IELRDLNVYYGDKHALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRLNDLipgapDEGEVLLDGKDIYDLDVDVlelR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 344 RRVGYMSQAFSLYSeLTVRQNLVLHARLFGV-PAAEIDARVDEMARRFGLADIYGMLPDSLPL--GMRQRLSLAVAMVHK 420
Cdd:cd03260 81 RRVGMVFQKPNPFP-GSIYDNVAYGLRLHGIkLKEELDERVEEALRKAALWDEVKDRLHALGLsgGQQQRLCLARALANE 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 421 PELLILDEPTSGVDPVARDSFWQLMIDLARRdlVTIFISTHFMNEAQRC-DRISLMHAGRVLASDSPAEL 489
Cdd:cd03260 160 PEVLLLDEPTSALDPISTAKIEELIAELKKE--YTIVIVTHNMQQAARVaDRTAFLLNGRLVEFGPTEQI 227
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
272-490 |
8.63e-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: 153.08 E-value: 8.63e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 272 IEARGLTMRFGDFTAVDHVSFRIRRGEIFGFLGSNGCGKSTTMKMLTGLLPATEGTAQLFGKEVDPKDINTRRR--VGYM 349
Cdd:cd03218 1 LRAENLSKRYGKRKVVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDGQDITKLPMHKRARlgIGYL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 350 SQAFSLYSELTVRQNLVLHARLFGVPAAEIDARVDEMARRFGLADIYGMLPDSLPLGMRQRLSLAVAMVHKPELLILDEP 429
Cdd:cd03218 81 PQEASIFRKLTVEENILAVLEIRGLSKKEREEKLEELLEEFHITHLRKSKASSLSGGERRRVEIARALATNPKFLLLDEP 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 505416896 430 TSGVDPVARDSFWQLMIDLARRDLvTIFISTHFMNEA-QRCDRISLMHAGRVLASDSPAELV 490
Cdd:cd03218 161 FAGVDPIAVQDIQKIIKILKDRGI-GVLITDHNVRETlSITDRAYIIYEGKVLAEGTPEEIA 221
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
1-480 |
8.99e-42 |
|
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 443332 [Multi-domain] Cd Length: 533 Bit Score: 161.39 E-value: 8.99e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 1 MNASSVVRFSDVSLRYGK----TVALDRITLDVPAGLTTGLIGPDGVGKS----SLLALASGARALQTGGVDALGGDMRS 72
Cdd:COG4172 1 MMSMPLLSVEDLSVAFGQgggtVEAVKGVSFDIAAGETLALVGESGSGKSvtalSILRLLPDPAAHPSGSILFDGQDLLG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 73 RRHRERVC---RRIAYMPQGLGKNLYPTLSVE----ENLQFFARLFGHDAgerRRRIDALTQSTGL---------FPFls 136
Cdd:COG4172 81 LSERELRRirgNRIAMIFQEPMTSLNPLHTIGkqiaEVLRLHRGLSGAAA---RARALELLERVGIpdperrldaYPH-- 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 137 rpagKLSGGMKQKLGLCCALIHDPDLLILDEPTTGVDPLARAQFWDLIARIRDERpTMSVIVATAYMDEAQRF-DWLIAM 215
Cdd:COG4172 156 ----QLSGGQRQRVMIAMALANEPDLLIADEPTTALDVTVQAQILDLLKDLQREL-GMALLLITHDLGVVRRFaDRVAVM 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 216 DAGRVLATGAPAELLAR-----TgcdsleAAFIALLPenerrghkpvKIEPLRADARAGTAIEARGLTMRF--------- 281
Cdd:COG4172 231 RQGEIVEQGPTAELFAApqhpyT------RKLLAAEP----------RGDPRPVPPDAPPLLEARDLKVWFpikrglfrr 294
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 282 --GDFTAVDHVSFRIRRGEIFGFLGSNGCGKSTTMKMLTGLLPaTEGTAQLFGKEVDPKDINT----RRRVgymsQA-F- 353
Cdd:COG4172 295 tvGHVKAVDGVSLTLRRGETLGLVGESGSGKSTLGLALLRLIP-SEGEIRFDGQDLDGLSRRAlrplRRRM----QVvFq 369
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 354 ----SLYSELTVRQ----NLVLHARlfGVPAAEIDARVDEMARRFGL-ADIYGMLPDSLPLGMRQRLSLAVAMVHKPELL 424
Cdd:COG4172 370 dpfgSLSPRMTVGQiiaeGLRVHGP--GLSAAERRARVAEALEEVGLdPAARHRYPHEFSGGQRQRIAIARALILEPKLL 447
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 505416896 425 ILDEPTSGVDPVARDSFWQLMIDL-ARRDLVTIFIStH------FMneaqrCDRISLMHAGRV 480
Cdd:COG4172 448 VLDEPTSALDVSVQAQILDLLRDLqREHGLAYLFIS-HdlavvrAL-----AHRVMVMKDGKV 504
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
10-224 |
1.56e-41 |
|
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: 151.58 E-value: 1.56e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 10 SDVSLRYGKTVALDRITLDVPAGLTtGLIGPDGVGKSSLLALASGARALQTGGVDALGGDMRSRRHRERVCrrIAYMPQG 89
Cdd:cd03264 4 ENLTKRYGKKRALDGVSLTLGPGMY-GLLGPNGAGKTTLMRILATLTPPSSGTIRIDGQDVLKQPQKLRRR--IGYLPQE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 90 LGknLYPTLSVEENLQFFARLFGHDAGERRRRIDALTQSTGLFPFLSRPAGKLSGGMKQKLGLCCALIHDPDLLILDEPT 169
Cdd:cd03264 81 FG--VYPNFTVREFLDYIAWLKGIPSKEVKARVDEVLELVNLGDRAKKKIGSLSGGMRRRVGIAQALVGDPSILIVDEPT 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 505416896 170 TGVDPLARAQFWDLIARIRDERptmSVIVATAYMDEAQRF-DWLIAMDAGRVLATG 224
Cdd:cd03264 159 AGLDPEERIRFRNLLSELGEDR---IVILSTHIVEDVESLcNQVAVLNKGKLVFEG 211
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
272-492 |
1.96e-41 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 155.69 E-value: 1.96e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 272 IEARGLTMRFGDFTAVDHVSFRIRRGEIFGFLGSNGCGKSTTMKMLTGLLPATEGTAQLFGKEVdpkDINT---RRRVGY 348
Cdd:COG1118 3 IEVRNISKRFGSFTLLDDVSLEIASGELVALLGPSGSGKTTLLRIIAGLETPDSGRIVLNGRDL---FTNLpprERRVGF 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 349 MSQAFSLYSELTVRQNLVLHARLFGVPAAEIDARVDEMARRFGLADIYGMLPDSLPLGMRQRLSLAVAMVHKPELLILDE 428
Cdd:COG1118 80 VFQHYALFPHMTVAENIAFGLRVRPPSKAEIRARVEELLELVQLEGLADRYPSQLSGGQRQRVALARALAVEPEVLLLDE 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 505416896 429 PTSGVDPVARDSFWQLMIDL-ARRDLVTIFIsTHFMNEAQR-CDRISLMHAGRVLASDSPAELVRA 492
Cdd:COG1118 160 PFGALDAKVRKELRRWLRRLhDELGGTTVFV-THDQEEALElADRVVVMNQGRIEQVGTPDEVYDR 224
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
287-431 |
2.21e-41 |
|
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: 148.56 E-value: 2.21e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 287 VDHVSFRIRRGEIFGFLGSNGCGKSTTMKMLTGLLPATEGTAQLFGKEVDPKDIN-TRRRVGYMSQAFSLYSELTVRQNL 365
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDLTDDERKsLRKEIGYVFQDPQLFPRLTVRENL 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 366 VLHARLFGVPAAEIDARVDEMARRFGLADIY----GMLPDSLPLGMRQRLSLAVAMVHKPELLILDEPTS 431
Cdd:pfam00005 81 RLGLLLKGLSKREKDARAEEALEKLGLGDLAdrpvGERPGTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
271-505 |
5.46e-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: 151.11 E-value: 5.46e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 271 AIEARGLTMRFG----DFTAVDHVSFRIRRGEIFGFLGSNGCGKSTTMKMLTGLLPATEGTAQLFGKEVDPKDI-NTRRR 345
Cdd:COG1124 1 MLEVRNLSVSYGqggrRVPVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVTFDGRPVTRRRRkAFRRR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 346 VGYMSQ--AFSLYSELTVRQNLVLHARLFGVPaaEIDARVDEMARRFGL-ADIYGMLPDSLPLGMRQRLSLAVAMVHKPE 422
Cdd:COG1124 81 VQMVFQdpYASLHPRHTVDRILAEPLRIHGLP--DREERIAELLEQVGLpPSFLDRYPHQLSGGQRQRVAIARALILEPE 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 423 LLILDEPTSGVDPVARDSFWQLMIDL-ARRDLVTIFIStHFMNEAQR-CDRISLMHAGRVLASDSPAELVR-ARGAAT-- 497
Cdd:COG1124 159 LLLLDEPTSALDVSVQAEILNLLKDLrEERGLTYLFVS-HDLAVVAHlCDRVAVMQNGRIVEELTVADLLAgPKHPYTre 237
|
....*...
gi 505416896 498 LEDAFIGY 505
Cdd:COG1124 238 LLAASLAF 245
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
15-229 |
6.41e-41 |
|
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: 150.21 E-value: 6.41e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 15 RYGKTVALDRITLDVPAGLTTGLIGPDGVGKSSLLALASGARALQTGGVDALGGDMRSRRHRERVCrrIAYMPQGLgkNL 94
Cdd:cd03265 9 KYGDFEAVRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATVAGHDVVREPREVRRR--IGIVFQDL--SV 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 95 YPTLSVEENLQFFARLFGHDAGERRRRIDALTQSTGLFPFLSRPAGKLSGGMKQKLGLCCALIHDPDLLILDEPTTGVDP 174
Cdd:cd03265 85 DDELTGWENLYIHARLYGVPGAERRERIDELLDFVGLLEAADRLVKTYSGGMRRRLEIARSLVHRPEVLFLDEPTIGLDP 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 505416896 175 LARAQFWDLIARIRDERpTMSVIVATAYMDEAQRF-DWLIAMDAGRVLATGAPAEL 229
Cdd:cd03265 165 QTRAHVWEYIEKLKEEF-GMTILLTTHYMEEAEQLcDRVAIIDHGRIIAEGTPEEL 219
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
272-490 |
6.89e-41 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 150.56 E-value: 6.89e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 272 IEARGLTMRFGDFTAVDHVSFRIRRGEIFGFLGSNGCGKSTTMKMLTGLLPATEGTAQLFGKEVDPKDINTRRR--VGYM 349
Cdd:COG1137 4 LEAENLVKSYGKRTVVKDVSLEVNQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGRIFLDGEDITHLPMHKRARlgIGYL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 350 SQAFSLYSELTVRQNLVLHARLFGVPAAEIDARVDEMARRFGLADIYGMLPDSLPLGMRQRLSLAVAMVHKPELLILDEP 429
Cdd:COG1137 84 PQEASIFRKLTVEDNILAVLELRKLSKKEREERLEELLEEFGITHLRKSKAYSLSGGERRRVEIARALATNPKFILLDEP 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 505416896 430 TSGVDPVARDSFWQLMIDLARRDLvTIFISTHFMNEAQR-CDRISLMHAGRVLASDSPAELV 490
Cdd:COG1137 164 FAGVDPIAVADIQKIIRHLKERGI-GVLITDHNVRETLGiCDRAYIISEGKVLAEGTPEEIL 224
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
272-489 |
8.19e-41 |
|
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: 150.08 E-value: 8.19e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 272 IEARGLTMRFGDFTAVDHVSFRIRRGEIFGFLGSNGCGKSTTMKMLTGLLPATEGTAQLFGKEVDPKDINtRRRVGYMSQ 351
Cdd:cd03300 1 IELENVSKFYGGFVALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGKDITNLPPH-KRPVNTVFQ 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 352 AFSLYSELTVRQNLVLHARLFGVPAAEIDARVDEMARRFGLADIYGMLPDSLPLGMRQRLSLAVAMVHKPELLILDEPTS 431
Cdd:cd03300 80 NYALFPHLTVFENIAFGLRLKKLPKAEIKERVAEALDLVQLEGYANRKPSQLSGGQQQRVAIARALVNEPKVLLLDEPLG 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 432 GVDPVARDSFwQLMIDLARRDL-VTIFISTHFMNEA-QRCDRISLMHAGRVLASDSPAEL 489
Cdd:cd03300 160 ALDLKLRKDM-QLELKRLQKELgITFVFVTHDQEEAlTMSDRIAVMNKGKIQQIGTPEEI 218
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
7-232 |
1.56e-40 |
|
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: 149.40 E-value: 1.56e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 7 VRFSDVSLRY-GKTVALDRITLDVPAGLTTGLIGPDGVGKSSLLALASGARALQTGGVDALGGDMRSRRHRERVCRrIAY 85
Cdd:COG1122 1 IELENLSFSYpGGTPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVDGKDITKKNLRELRRK-VGL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 86 MPQglgknlYP-----TLSVEENLQFFARLFGHDAGERRRRIDALTQSTGLFPFLSRPAGKLSGGMKQKLGLCCALIHDP 160
Cdd:COG1122 80 VFQ------NPddqlfAPTVEEDVAFGPENLGLPREEIRERVEEALELVGLEHLADRPPHELSGGQKQRVAIAGVLAMEP 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 505416896 161 DLLILDEPTTGVDPLARAQFWDLIARIRDERptMSVIVATAYMDEAQR-FDWLIAMDAGRVLATGAPAELLAR 232
Cdd:COG1122 154 EVLVLDEPTAGLDPRGRRELLELLKRLNKEG--KTVIIVTHDLDLVAElADRVIVLDDGRIVADGTPREVFSD 224
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
272-480 |
2.40e-40 |
|
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: 148.81 E-value: 2.40e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 272 IEARGLTMRF----GDFTAVDHVSFRIRRGEIFGFLGSNGCGKSTTMKMLTGLLPATEGTAQLFGKEVDPKDI----NTR 343
Cdd:cd03257 2 LEVKNLSVSFptggGSVKALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGKDLLKLSRrlrkIRR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 344 RRVGYMSQ--AFSLYSELTVRQNL--VLHARLFGVPAAEIDARVDEMARRFGL-ADIYGMLPDSLPLGMRQRLSLAVAMV 418
Cdd:cd03257 82 KEIQMVFQdpMSSLNPRMTIGEQIaePLRIHGKLSKKEARKEAVLLLLVGVGLpEEVLNRYPHELSGGQRQRVAIARALA 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 505416896 419 HKPELLILDEPTSGVDPVARDSFWQLMIDL-ARRDLVTIFIsTHFMNEAQR-CDRISLMHAGRV 480
Cdd:cd03257 162 LNPKLLIADEPTSALDVSVQAQILDLLKKLqEELGLTLLFI-THDLGVVAKiADRVAVMYAGKI 224
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
267-484 |
1.73e-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: 146.32 E-value: 1.73e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 267 RAGTAIEARGLTMR-FGDFTAVDHVSFRIRRGEIFGFLGSNGCGKSTTMKMLTGLLPATEGTAQLFGKEVDPKDINTRRR 345
Cdd:cd03267 16 EPGLIGSLKSLFKRkYREVEALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRVAGLVPWKRRKKFLRR 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 346 VGY-MSQAFSLYSELTVRQNLVLHARLFGVPAAEIDARVDEMARRFGLADIYGMLPDSLPLGMRQRLSLAVAMVHKPELL 424
Cdd:cd03267 96 IGVvFGQKTQLWWDLPVIDSFYLLAAIYDLPPARFKKRLDELSELLDLEELLDTPVRQLSLGQRMRAEIAAALLHEPEIL 175
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 505416896 425 ILDEPTSGVDPVARDSFWQLMIDLARRDLVTIFISTHFMNE-AQRCDRISLMHAGRVLASD 484
Cdd:cd03267 176 FLDEPTIGLDVVAQENIRNFLKEYNRERGTTVLLTSHYMKDiEALARRVLVIDKGRLLYDG 236
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
268-493 |
2.25e-39 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 153.64 E-value: 2.25e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 268 AGTAIEARGLTMRFGDFTAVDHVSFRIRRGEIFGFLGSNGCGKSTTMKMLTGLLPATEGTAQLFGKEVDPKDIN--TRRR 345
Cdd:COG1129 1 AEPLLEMRGISKSFGGVKALDGVSLELRPGEVHALLGENGAGKSTLMKILSGVYQPDSGEILLDGEPVRFRSPRdaQAAG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 346 VGYMSQAFSLYSELTVRQNLVLH---ARLFGVPAAEIDARVDEMARRFGLaDIygmLPD----SLPLGMRQRLSLAVAMV 418
Cdd:COG1129 81 IAIIHQELNLVPNLSVAENIFLGrepRRGGLIDWRAMRRRARELLARLGL-DI---DPDtpvgDLSVAQQQLVEIARALS 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 505416896 419 HKPELLILDEPTSGVDPVARDSFWQLMIDLARRDLVTIFIStHFMNEAQR-CDRISLMHAGRVLASDSPAELVRAR 493
Cdd:COG1129 157 RDARVLILDEPTASLTEREVERLFRIIRRLKAQGVAIIYIS-HRLDEVFEiADRVTVLRDGRLVGTGPVAELTEDE 231
|
|
| YadH |
COG0842 |
ABC-type multidrug transport system, permease component [Defense mechanisms]; |
791-989 |
2.52e-39 |
|
ABC-type multidrug transport system, permease component [Defense mechanisms];
Pssm-ID: 440604 [Multi-domain] Cd Length: 200 Bit Score: 144.57 E-value: 2.52e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 791 SLPAMIPAVMPLLLLMLPAMLTALAVVRERELGSILNLYVTPVTRTEFLIGKQVPYVVLAMLNFLLMTMLARIAFDVPVK 870
Cdd:COG0842 1 YLAFLVPGLLAMSLLFTALMLTALSIAREREQGTLERLLVTPVSRLEILLGKVLAYLLRGLLQALLVLLVALLFFGVPLR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 871 G-SFMTLLLAVLIFNVVATGIGLLASTFTRSQVAAIVMTIIgTMIPTVQFAGLLTPLSSLEGTGRFIGLVYPATYMLSIS 949
Cdd:COG0842 81 GlSLLLLLLVLLLFALAFSGLGLLISTLARSQEQASAISNL-VILPLTFLSGAFFPIESLPGWLQAIAYLNPLTYFVEAL 159
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 505416896 950 RGVFNKALSLQDLHSQFWPLAASAPVILGATILLLKKQER 989
Cdd:COG0842 160 RALFLGGAGLADVWPSLLVLLAFAVVLLALALRLFRRRLR 199
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
270-502 |
2.78e-39 |
|
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: 146.38 E-value: 2.78e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 270 TAIEARGLTMRFGDFTAVDHVSFRIRRGEIFGFLGSNGCGKSTTMKMLTGLLPATEG-TAQLFGKE---VDPKDIntRRR 345
Cdd:COG1119 2 PLLELRNVTVRRGGKTILDDISWTVKPGEHWAILGPNGAGKSTLLSLITGDLPPTYGnDVRLFGERrggEDVWEL--RKR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 346 VGYMSQAFSLY--SELTVRqNLVLHArLFGV------PAAEIDARVDEMARRFGLADIYGMLPDSLPLGMRQRLSLAVAM 417
Cdd:COG1119 80 IGLVSPALQLRfpRDETVL-DVVLSG-FFDSiglyrePTDEQRERARELLELLGLAHLADRPFGTLSQGEQRRVLIARAL 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 418 VHKPELLILDEPTSGVDPVARDSFWQLMIDLARRDLVTIFISTHFMNEAQRC-DRISLMHAGRVLASDSPAELVRargAA 496
Cdd:COG1119 158 VKDPELLILDEPTAGLDLGARELLLALLDKLAAEGAPTLVLVTHHVEEIPPGiTHVLLLKDGRVVAAGPKEEVLT---SE 234
|
....*.
gi 505416896 497 TLEDAF 502
Cdd:COG1119 235 NLSEAF 240
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
1-242 |
4.69e-39 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 145.62 E-value: 4.69e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 1 MNASSVVRFSDVSLRYGKTVALDRITLDVPAGLTTGLIGPDGVGKSSLLALASGARALQTGGVDALGGDMRsrrhreRVC 80
Cdd:COG1121 1 MMMMPAIELENLTVSYGGRPVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLFGKPPR------RAR 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 81 RRIAYMPQGLGKNLYPTLSVEE----NLQFFARLFGHDAGERRRRIDALTQSTGLFPFLSRPAGKLSGGMKQKLGLCCAL 156
Cdd:COG1121 75 RRIGYVPQRAEVDWDFPITVRDvvlmGRYGRRGLFRRPSRADREAVDEALERVGLEDLADRPIGELSGGQQQRVLLARAL 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 157 IHDPDLLILDEPTTGVDPLARAQFWDLIARIRDERptMSVIVATAYMDEAQR-FDWLIAMDaGRVLATGAPAELLARtgc 235
Cdd:COG1121 155 AQDPDLLLLDEPFAGVDAATEEALYELLRELRREG--KTILVVTHDLGAVREyFDRVLLLN-RGLVAHGPPEEVLTP--- 228
|
....*..
gi 505416896 236 DSLEAAF 242
Cdd:COG1121 229 ENLSRAY 235
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
272-483 |
5.87e-39 |
|
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: 142.18 E-value: 5.87e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 272 IEARGLTMRFGDFTAVDHVSFRIRRGEIFGFLGSNGCGKSTTMKMLTGLLPATEGTAQLFGKEVDPKDintrrrvgymsq 351
Cdd:cd03216 1 LELRGITKRFGGVKALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVDGKEVSFAS------------ 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 352 afslyseltvrqnlvlharlfgvPAAeidarvdemARRFGLADIYgmlpdSLPLGMRQRLSLAVAMVHKPELLILDEPTS 431
Cdd:cd03216 69 -----------------------PRD---------ARRAGIAMVY-----QLSVGERQMVEIARALARNARLLILDEPTA 111
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 505416896 432 GVDPVARDSFWQLMIDLARRDLVTIFIStHFMNEAQR-CDRISLMHAGRVLAS 483
Cdd:cd03216 112 ALTPAEVERLFKVIRRLRAQGVAVIFIS-HRLDEVFEiADRVTVLRDGRVVGT 163
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
273-479 |
8.61e-39 |
|
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: 141.61 E-value: 8.61e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 273 EARGLTMRFGDFTAVDHVSFRIRRGEIFGFLGSNGCGKSTTMKMLTGLLPATEGTAQLFGKEVDPKDINT-RRRVGYMSQ 351
Cdd:cd00267 1 EIENLSFRYGGRTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGKDIAKLPLEElRRRIGYVPQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 352 afslyseltvrqnlvlharlfgvpaaeidarvdemarrfgladiygmlpdsLPLGMRQRLSLAVAMVHKPELLILDEPTS 431
Cdd:cd00267 81 ---------------------------------------------------LSGGQRQRVALARALLLNPDLLLLDEPTS 109
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 505416896 432 GVDPVARDSFWQLMIDLARRDlVTIFISTHFMNEAQR-CDRISLMHAGR 479
Cdd:cd00267 110 GLDPASRERLLELLRELAEEG-RTVIIVTHDPELAELaADRVIVLKDGK 157
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
272-497 |
1.36e-38 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 147.15 E-value: 1.36e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 272 IEARGLTMRF----GDFTAVDHVSFRIRRGEIFGFLGSNGCGKSTTMKMLTGLLPATEGTAQLFGKEV---DPKDI-NTR 343
Cdd:COG1135 2 IELENLSKTFptkgGPVTALDDVSLTIEKGEIFGIIGYSGAGKSTLIRCINLLERPTSGSVLVDGVDLtalSERELrAAR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 344 RRVGYMSQAFSLYSELTVRQNLVLHARLFGVPAAEIDARVDEMARRFGLADIYGMLPDSLPLGMRQRLSLAVAMVHKPEL 423
Cdd:COG1135 82 RKIGMIFQHFNLLSSRTVAENVALPLEIAGVPKAEIRKRVAELLELVGLSDKADAYPSQLSGGQKQRVGIARALANNPKV 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 505416896 424 LILDEPTSGVDPVARDSFWQLMIDLaRRDL-VTIFISTHFMNEAQR-CDRISLMHAGRVLASDSPAELVRARGAAT 497
Cdd:COG1135 162 LLCDEATSALDPETTRSILDLLKDI-NRELgLTIVLITHEMDVVRRiCDRVAVLENGRIVEQGPVLDVFANPQSEL 236
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
8-219 |
3.72e-38 |
|
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: 141.84 E-value: 3.72e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 8 RFSDVSLRY--GKTVALDRITLDVPAGLTTGLIGPDGVGKSSLLALASGARALQTGGVDALGGDMRSRRHRERVCRrIAY 85
Cdd:cd03225 1 ELKNLSFSYpdGARPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDLTKLSLKELRRK-VGL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 86 MPQglgknlYP-----TLSVEENLQFFARLFGHDAGERRRRIDALTQSTGLFPFLSRPAGKLSGGMKQKLGLCCALIHDP 160
Cdd:cd03225 80 VFQ------NPddqffGPTVEEEVAFGLENLGLPEEEIEERVEEALELVGLEGLRDRSPFTLSGGQKQRVAIAGVLAMDP 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 161 DLLILDEPTTGVDPLARAQFWDLIARIRDERptMSVIVATAYMDEAQRF-DWLIAMDAGR 219
Cdd:cd03225 154 DILLLDEPTAGLDPAGRRELLELLKKLKAEG--KTIIIVTHDLDLLLELaDRVIVLEDGK 211
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
7-224 |
4.73e-38 |
|
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: 141.26 E-value: 4.73e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 7 VRFSDVSLRYGKTVALDRITLDVPAGLTTGLIGPDGVGKSSLLALASGARALQTGGVDALGGDMrsrrhRERVCRRIAYM 86
Cdd:cd03269 1 LEVENVTKRFGRVTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDGKPL-----DIAARNRIGYL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 87 PQGLGknLYPTLSVEENLQFFARLFGHDAGERRRRIDALTQSTGLFPFLSRPAGKLSGGMKQKLGLCCALIHDPDLLILD 166
Cdd:cd03269 76 PEERG--LYPKMKVIDQLVYLAQLKGLKKEEARRRIDEWLERLELSEYANKRVEELSKGNQQKVQFIAAVIHDPELLILD 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 505416896 167 EPTTGVDPLARAQFWDLIARIRDERPTmsVIVATAYMDEAQRF-DWLIAMDAGRVLATG 224
Cdd:cd03269 154 EPFSGLDPVNVELLKDVIRELARAGKT--VILSTHQMELVEELcDRVLLLNKGRAVLYG 210
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
272-480 |
6.01e-38 |
|
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: 141.24 E-value: 6.01e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 272 IEARGLTMRFGDFTAVDHVSFRIRRGEIFGFLGSNGCGKSTTMKMLTGLLPATEGTAQLFGKEV---DPKDintrRRVGY 348
Cdd:cd03301 1 VELENVTKRFGNVTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGRDVtdlPPKD----RDIAM 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 349 MSQAFSLYSELTVRQNLVLHARLFGVPAAEIDARVDEMARRFGLADIYGMLPDSLPLGMRQRLSLAVAMVHKPELLILDE 428
Cdd:cd03301 77 VFQNYALYPHMTVYDNIAFGLKLRKVPKDEIDERVREVAELLQIEHLLDRKPKQLSGGQRQRVALGRAIVREPKVFLMDE 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 505416896 429 PTSGVDPVARDSFWQLMIDLARRDLVTIFISTHFMNEAQR-CDRISLMHAGRV 480
Cdd:cd03301 157 PLSNLDAKLRVQMRAELKRLQQRLGTTTIYVTHDQVEAMTmADRIAVMNDGQI 209
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
11-232 |
6.38e-38 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 144.10 E-value: 6.38e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 11 DVSLRYGKTVALDRITLDVPAGLTTGLIGPDGVGKSSLLALASGARALQTGGVDALGGDMRsrrhrERVCRRIAYMPQGL 90
Cdd:COG4152 6 GLTKRFGDKTAVDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDSGEVLWDGEPLD-----PEDRRRIGYLPEER 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 91 GknLYPTLSVEENLQFFARLFGHDAGERRRRIDALTQSTGLFPFLSRPAGKLSGGMKQKLGLCCALIHDPDLLILDEPTT 170
Cdd:COG4152 81 G--LYPKMKVGEQLVYLARLKGLSKAEAKRRADEWLERLGLGDRANKKVEELSKGNQQKVQLIAALLHDPELLILDEPFS 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 505416896 171 GVDPLARAQFWDLIARIRDERPTmsVIVATAYMDEAQRF-DWLIAMDAGRVLATGAPAELLAR 232
Cdd:COG4152 159 GLDPVNVELLKDVIRELAAKGTT--VIFSSHQMELVEELcDRIVIINKGRKVLSGSVDEIRRQ 219
|
|
| LPS_export_lptB |
TIGR04406 |
LPS export ABC transporter ATP-binding protein; Members of this fmaily are LptB, the ... |
274-490 |
1.34e-37 |
|
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: 141.26 E-value: 1.34e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 274 ARGLTMRFGDFTAVDHVSFRIRRGEIFGFLGSNGCGKSTTMKMLTGLLPATEGTAQLFGKEVD--PKDINTRRRVGYMSQ 351
Cdd:TIGR04406 4 AENLIKSYKKRKVVNDVSLSVKSGEIVGLLGPNGAGKTTSFYMIVGLVRPDAGKILIDGQDIThlPMHERARLGIGYLPQ 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 352 AFSLYSELTVRQNL--VLHARlFGVPAAEIDARVDEMARRFGLADIYGMLPDSLPLGMRQRLSLAVAMVHKPELLILDEP 429
Cdd:TIGR04406 84 EASIFRKLTVEENImaVLEIR-KDLDRAEREERLEALLEEFQISHLRDNKAMSLSGGERRRVEIARALATNPKFILLDEP 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 505416896 430 TSGVDPVARDSFWQLMIDLARRDLvTIFISTHFMNEAQR-CDRISLMHAGRVLASDSPAELV 490
Cdd:TIGR04406 163 FAGVDPIAVGDIKKIIKHLKERGI-GVLITDHNVRETLDiCDRAYIISDGKVLAEGTPAEIV 223
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
271-489 |
1.59e-37 |
|
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: 140.94 E-value: 1.59e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 271 AIEARGLTMRFGDFTAVDHVSFRIRRGEIFGFLGSNGCGKSTTMKMLTGLLPATEGTAQLFGKEVDPKDINtRRRVGYMS 350
Cdd:cd03296 2 SIEVRNVSKRFGDFVALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGGEDATDVPVQ-ERNVGFVF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 351 QAFSLYSELTVRQN----LVLHARLFGVPAAEIDARVDEMARRFGLADIYGMLPDSLPLGMRQRLSLAVAMVHKPELLIL 426
Cdd:cd03296 81 QHYALFRHMTVFDNvafgLRVKPRSERPPEAEIRAKVHELLKLVQLDWLADRYPAQLSGGQRQRVALARALAVEPKVLLL 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 505416896 427 DEPTSGVDPVARDSFWQLMIDLARRDLVTIFISTHFMNEA-QRCDRISLMHAGRVLASDSPAEL 489
Cdd:cd03296 161 DEPFGALDAKVRKELRRWLRRLHDELHVTTVFVTHDQEEAlEVADRVVVMNKGRIEQVGTPDEV 224
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
10-231 |
2.32e-37 |
|
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: 139.88 E-value: 2.32e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 10 SDVSLRYGKTVALDRITLDVPAGLTTGLIGPDGVGKSSLLALASGARALQTGGVDALGGDMRSRRHRERVCRRIAYMPQG 89
Cdd:cd03224 4 ENLNAGYGKSQILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDGRDITGLPPHERARAGIGYVPEG 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 90 lgKNLYPTLSVEENLQFFARLFGHDagERRRRIDALTQstgLFP----FLSRPAGKLSGGMKQKLGLCCALIHDPDLLIL 165
Cdd:cd03224 84 --RRIFPELTVEENLLLGAYARRRA--KRKARLERVYE---LFPrlkeRRKQLAGTLSGGEQQMLAIARALMSRPKLLLL 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 505416896 166 DEPTTGVDPLARAQFWDLIARIRDERptMSVIVATAYMDEAQRF-DWLIAMDAGRVLATGAPAELLA 231
Cdd:cd03224 157 DEPSEGLAPKIVEEIFEAIRELRDEG--VTILLVEQNARFALEIaDRAYVLERGRVVLEGTAAELLA 221
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
5-239 |
5.21e-37 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 141.48 E-value: 5.21e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 5 SVVRFSDVSLRYGKTVALDRITLDVPAGLTTGLIGPDGVGKSSLLALASGARALQTGGVDALGGDMRSRRHRERVCrrIA 84
Cdd:PRK13537 6 APIDFRNVEKRYGDKLVVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCGEPVPSRARHARQR--VG 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 85 YMPQGlgKNLYPTLSVEENLQFFARLFGHDAGERRRRIDALTQSTGLFPFLSRPAGKLSGGMKQKLGLCCALIHDPDLLI 164
Cdd:PRK13537 84 VVPQF--DNLDPDFTVRENLLVFGRYFGLSAAAARALVPPLLEFAKLENKADAKVGELSGGMKRRLTLARALVNDPDVLV 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 165 LDEPTTGVDPLARAQFWD----LIARIRderptmSVIVATAYMDEAQRF-DWLIAMDAGRVLATGAPAELLAR-TGCDSL 238
Cdd:PRK13537 162 LDEPTTGLDPQARHLMWErlrsLLARGK------TILLTTHFMEEAERLcDRLCVIEEGRKIAEGAPHALIESeIGCDVI 235
|
.
gi 505416896 239 E 239
Cdd:PRK13537 236 E 236
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
253-491 |
2.98e-36 |
|
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: 138.16 E-value: 2.98e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 253 GHKPVKIEPLRADARAGTAIEARgltmrFGDFTAVDHVSFRIRRGEIFGFLGSNGCGKSTTMKMLTGLLPATEGTAqlfg 332
Cdd:cd03294 11 GKNPQKAFKLLAKGKSKEEILKK-----TGQTVGVNDVSLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGKV---- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 333 kEVDPKDINT----------RRRVGYMSQAFSLYSELTVRQNLVLHARLFGVPAAEIDARVDEMARRFGLADIYGMLPDS 402
Cdd:cd03294 82 -LIDGQDIAAmsrkelrelrRKKISMVFQSFALLPHRTVLENVAFGLEVQGVPRAEREERAAEALELVGLEGWEHKYPDE 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 403 LPLGMRQRLSLAVAMVHKPELLILDEPTSGVDPVARDSFWQLMIDLARRDLVTIFISTHFMNEAQRC-DRISLMHAGRVL 481
Cdd:cd03294 161 LSGGMQQRVGLARALAVDPDILLMDEAFSALDPLIRREMQDELLRLQAELQKTIVFITHDLDEALRLgDRIAIMKDGRLV 240
|
250
....*....|
gi 505416896 482 ASDSPAELVR 491
Cdd:cd03294 241 QVGTPEEILT 250
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
6-200 |
3.01e-36 |
|
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: 136.07 E-value: 3.01e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 6 VVRFSDVSLRYGKTVALDRITLDVPAGLTTGLIGPDGVGKSSLLALASGARALQTGGVDALGGDMRSRRHRERVCrrIAY 85
Cdd:COG4133 2 MLEAENLSCRRGERLLFSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWNGEPIRDAREDYRRR--LAY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 86 MPQGLGknLYPTLSVEENLQFFARLFGHDAGerRRRIDALTQSTGLFPFLSRPAGKLSGGMKQKLGLCCALIHDPDLLIL 165
Cdd:COG4133 80 LGHADG--LKPELTVRENLRFWAALYGLRAD--REAIDEALEAVGLAGLADLPVRQLSAGQKRRVALARLLLSPAPLWLL 155
|
170 180 190
....*....|....*....|....*....|....*
gi 505416896 166 DEPTTGVDPLARAQFWDLIARIRDERPTmsVIVAT 200
Cdd:COG4133 156 DEPFTALDAAGVALLAELIAAHLARGGA--VLLTT 188
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
7-491 |
3.05e-36 |
|
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: 144.56 E-value: 3.05e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 7 VRFSDVSLRYGKTVALDRITLDVPAGLTTGLIGPDGVGKSSLLALASG---------------ARALQTGGVD------- 64
Cdd:TIGR03269 1 IEVKNLTKKFDGKEVLKNISFTIEEGEVLGILGRSGAGKSVLMHVLRGmdqyeptsgriiyhvALCEKCGYVErpskvge 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 65 ---ALGGDMR---------SRRHRERVCRRIAYMPQGLGKnLYPTLSVEENLQFFARLFGHDAGERRRRIDALTQSTGLF 132
Cdd:TIGR03269 81 pcpVCGGTLEpeevdfwnlSDKLRRRIRKRIAIMLQRTFA-LYGDDTVLDNVLEALEEIGYEGKEAVGRAVDLIEMVQLS 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 133 PFLSRPAGKLSGGMKQKLGLCCALIHDPDLLILDEPTTGVDPL-ARAQFWDLIARIRDERPTMsviVATAYMDE--AQRF 209
Cdd:TIGR03269 160 HRITHIARDLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQtAKLVHNALEEAVKASGISM---VLTSHWPEviEDLS 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 210 DWLIAMDAGRVLATGAPAELLARtgcdsleaaFIALLPENERRGHKPVKiEPLradaragtaIEARGLTMRF-----GDF 284
Cdd:TIGR03269 237 DKAIWLENGEIKEEGTPDEVVAV---------FMEGVSEVEKECEVEVG-EPI---------IKVRNVSKRYisvdrGVV 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 285 TAVDHVSFRIRRGEIFGFLGSNGCGKSTTMKMLTGLLPATEGTAQ-LFGKE-VDPKDI------NTRRRVGYMSQAFSLY 356
Cdd:TIGR03269 298 KAVDNVSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGEVNvRVGDEwVDMTKPgpdgrgRAKRYIGILHQEYDLY 377
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 357 SELTVRQNLVLHARL-----FGVPAAEIDARV----DEMARrfglaDIYGMLPDSLPLGMRQRLSLAVAMVHKPELLILD 427
Cdd:TIGR03269 378 PHRTVLDNLTEAIGLelpdeLARMKAVITLKMvgfdEEKAE-----EILDKYPDELSEGERHRVALAQVLIKEPRIVILD 452
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 505416896 428 EPTSGVDPVARDSFWQLMIDlARRDL-VTIFISTH---FMNEAqrCDRISLMHAGRVLASDSPAELVR 491
Cdd:TIGR03269 453 EPTGTMDPITKVDVTHSILK-AREEMeQTFIIVSHdmdFVLDV--CDRAALMRDGKIVKIGDPEEIVE 517
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
280-492 |
5.85e-36 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 136.75 E-value: 5.85e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 280 RFGDFTAVDHVSFRIRRGEIFGFLGSNGCGKSTTMKMLTGLLPATEGTaqlfgkevdpkdINTRRRVGYM---SQAFSly 356
Cdd:COG1134 35 RREEFWALKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTSGR------------VEVNGRVSALlelGAGFH-- 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 357 SELTVRQNLVLHARLFGVPAAEIDARVDEMArRF-GLAD-IYgmlpdsLPL-----GMRQRLSLAVAMVHKPELLILDEP 429
Cdd:COG1134 101 PELTGRENIYLNGRLLGLSRKEIDEKFDEIV-EFaELGDfID------QPVktyssGMRARLAFAVATAVDPDILLVDEV 173
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 505416896 430 TSGVDPVARDSFWQLMIDLaRRDLVTIFISTHFMNEAQR-CDRISLMHAGRVLASDSPAELVRA 492
Cdd:COG1134 174 LAVGDAAFQKKCLARIREL-RESGRTVIFVSHSMGAVRRlCDRAIWLEKGRLVMDGDPEEVIAA 236
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
6-506 |
6.91e-36 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 143.24 E-value: 6.91e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 6 VVRFSDVSLRYGKTVALDRITLDVPAGLTTGLIGPDGVGKSSLLALASGA-RAlqTGGVDALGG---DMRSrrhrervcr 81
Cdd:COG3845 5 ALELRGITKRFGGVVANDDVSLTVRPGEIHALLGENGAGKSTLMKILYGLyQP--DSGEILIDGkpvRIRS--------- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 82 riaymPQ-----GLGK-----NLYPTLSVEENLQ------FFARLfghDAGERRRRIDALTQSTGLFPFLSRPAGKLSGG 145
Cdd:COG3845 74 -----PRdaialGIGMvhqhfMLVPNLTVAENIVlgleptKGGRL---DRKAARARIRELSERYGLDVDPDAKVEDLSVG 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 146 MKQKLGLCCALIHDPDLLILDEPTTGVDPLARAQFWDLIARIRDERptMSVIVATAYMDEAQRF-DWLIAMDAGRVLATG 224
Cdd:COG3845 146 EQQRVEILKALYRGARILILDEPTAVLTPQEADELFEILRRLAAEG--KSIIFITHKLREVMAIaDRVTVLRRGKVVGTV 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 225 APAEL----LAR--TGcdsleaafiallpenerrghKPVKIEPLRADARAG-TAIEARGLTMRFGD-FTAVDHVSFRIRR 296
Cdd:COG3845 224 DTAETseeeLAElmVG--------------------REVLLRVEKAPAEPGeVVLEVENLSVRDDRgVPALKDVSLEVRA 283
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 297 GEIFGFLGSNGCGKSTTMKMLTGLLPATEGTAQLFGKEVDPKDINTRRR--VGYMS---QAFSLYSELTVRQNLVLH--- 368
Cdd:COG3845 284 GEILGIAGVAGNGQSELAEALAGLRPPASGSIRLDGEDITGLSPRERRRlgVAYIPedrLGRGLVPDMSVAENLILGryr 363
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 369 ----ARLFGVPAAEIDARVDEMARRFglaDIygmLPDSLPLGMR-------QRLSLAVAMVHKPELLILDEPTSGVDPVA 437
Cdd:COG3845 364 rppfSRGGFLDRKAIRAFAEELIEEF---DV---RTPGPDTPARslsggnqQKVILARELSRDPKLLIAAQPTRGLDVGA 437
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 438 RDSFWQLMIDLARRDLVTIFISTHfMNEAQR-CDRISLMHAGRVLAsdspaelVRARGAATLEDafIGYL 506
Cdd:COG3845 438 IEFIHQRLLELRDAGAAVLLISED-LDEILAlSDRIAVMYEGRIVG-------EVPAAEATREE--IGLL 497
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
272-480 |
1.32e-35 |
|
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: 137.88 E-value: 1.32e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 272 IEARGLTMRF----GDFTAVDHVSFRIRRGEIFGFLGSNGCGKSTTMKMLTGLLPA---TEGTAQLFGKEV---DPKDIN 341
Cdd:COG0444 2 LEVRNLKVYFptrrGVVKAVDGVSFDVRRGETLGLVGESGSGKSTLARAILGLLPPpgiTSGEILFDGEDLlklSEKELR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 342 TRR--RVGYMSQ-AF-SLYSELTVRQ----NLVLHarlFGVPAAEIDARVDEMARRFGL---ADIYGMLPDSLPLGMRQR 410
Cdd:COG0444 82 KIRgrEIQMIFQdPMtSLNPVMTVGDqiaePLRIH---GGLSKAEARERAIELLERVGLpdpERRLDRYPHELSGGMRQR 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 505416896 411 LSLAVAMVHKPELLILDEPTSGVDPVARDSFWQLMIDLAR-RDLVTIFIsTHFMNE-AQRCDRISLMHAGRV 480
Cdd:COG0444 159 VMIARALALEPKLLIADEPTTALDVTIQAQILNLLKDLQReLGLAILFI-THDLGVvAEIADRVAVMYAGRI 229
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
8-224 |
1.40e-35 |
|
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: 134.80 E-value: 1.40e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 8 RFSDVSlryGKTVALDRITLDVPAGLTTGLIGPDGVGKSSLLALASGARALQTGGVDALGGDMRSRRHRERVCrrIAYMP 87
Cdd:cd03266 10 RFRDVK---KTVQAVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDGFDVVKEPAEARRR--LGFVS 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 88 QGLGknLYPTLSVEENLQFFARLFGHDAGERRRRIDALTQSTGLFPFLSRPAGKLSGGMKQKLGLCCALIHDPDLLILDE 167
Cdd:cd03266 85 DSTG--LYDRLTARENLEYFAGLYGLKGDELTARLEELADRLGMEELLDRRVGGFSTGMRQKVAIARALVHDPPVLLLDE 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 505416896 168 PTTGVDPLARAQFWDLIARIRDERPTmsVIVATAYMDEAQRF-DWLIAMDAGRVLATG 224
Cdd:cd03266 163 PTTGLDVMATRALREFIRQLRALGKC--ILFSTHIMQEVERLcDRVVVLHRGRVVYEG 218
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
272-480 |
2.37e-35 |
|
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: 133.81 E-value: 2.37e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 272 IEARGLTMRFGDFTAVDHVSFRIRRGEIFGFLGSNGCGKSTTMKMLTGLLPATEGTAQLFGKEV--DPKDINT-RRRVGY 348
Cdd:cd03262 1 IEIKNLHKSFGDFHVLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIDGLKLtdDKKNINElRQKVGM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 349 MSQAFSLYSELTVRQNLVLHAR-LFGVPAAEIDARVDEMARRFGLADIYGMLPDSLPLGMRQRLSLAVAMVHKPELLILD 427
Cdd:cd03262 81 VFQQFNLFPHLTVLENITLAPIkVKGMSKAEAEERALELLEKVGLADKADAYPAQLSGGQQQRVAIARALAMNPKVMLFD 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 505416896 428 EPTSGVDPVARDSFWQLMIDLARRDLvTIFISTHFMNEAQR-CDRISLMHAGRV 480
Cdd:cd03262 161 EPTSALDPELVGEVLDVMKDLAEEGM-TMVVVTHEMGFAREvADRVIFMDDGRI 213
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
10-231 |
2.49e-35 |
|
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: 134.34 E-value: 2.49e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 10 SDVSLRYGKTVALDRITLDVPAGLTTGLIGPDGVGKSSLLALASGARALQTGGVDALGGDMRSRRHRERVCRRIAYMPQG 89
Cdd:COG0410 7 ENLHAGYGGIHVLHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRSGSIRFDGEDITGLPPHRIARLGIGYVPEG 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 90 lgKNLYPTLSVEENLQFFARLfGHDAGERRRRIDALTQstgLFP----FLSRPAGKLSGGMKQKLGLCCALIHDPDLLIL 165
Cdd:COG0410 87 --RRIFPSLTVEENLLLGAYA-RRDRAEVRADLERVYE---LFPrlkeRRRQRAGTLSGGEQQMLAIGRALMSRPKLLLL 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 505416896 166 DEPTTGVDPLARAQFWDLIARIRDERptMSVIVATAYMDEAQRF-DWLIAMDAGRVLATGAPAELLA 231
Cdd:COG0410 161 DEPSLGLAPLIVEEIFEIIRRLNREG--VTILLVEQNARFALEIaDRAYVLERGRIVLEGTAAELLA 225
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
8-224 |
4.68e-35 |
|
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: 133.04 E-value: 4.68e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 8 RFSDVSLRYGKTVALDRITLDVPAGLTTGLIGPDGVGKSSLLALASGARALQTGGVDALGGDMRsrrhreRVCRRIAYMP 87
Cdd:cd03235 1 EVEDLTVSYGGHPVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFGKPLE------KERKRIGYVP 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 88 QGLGKNLYPTLSVEE----NLQFFARLFGHDAGERRRRIDALTQSTGLFPFLSRPAGKLSGGMKQKLGLCCALIHDPDLL 163
Cdd:cd03235 75 QRRSIDRDFPISVRDvvlmGLYGHKGLFRRLSKADKAKVDEALERVGLSELADRQIGELSGGQQQRVLLARALVQDPDLL 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 505416896 164 ILDEPTTGVDPLARAQFWDLIARIRDErpTMSVIVATAYMDEAQR-FDWLIAMDaGRVLATG 224
Cdd:cd03235 155 LLDEPFAGVDPKTQEDIYELLRELRRE--GMTILVVTHDLGLVLEyFDRVLLLN-RTVVASG 213
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
6-230 |
5.90e-35 |
|
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion transport and metabolism, Coenzyme transport and metabolism];
Pssm-ID: 440737 [Multi-domain] Cd Length: 254 Bit Score: 134.02 E-value: 5.90e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 6 VVRFSDVSLRYGKTVALDRITLDVPAGLTTGLIGPDGVGKSSLLALASGARALQTGGVDALGGDMRSrRHRERVCRRIAY 85
Cdd:COG1120 1 MLEAENLSVGYGGRPVLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDGRDLAS-LSRRELARRIAY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 86 MPQGLgkNLYPTLSVEENLQF----FARLFGHDAGERRRRIDALTQSTGLFPFLSRPAGKLSGGMKQKLGLCCALIHDPD 161
Cdd:COG1120 80 VPQEP--PAPFGLTVRELVALgrypHLGLFGRPSAEDREAVEEALERTGLEHLADRPVDELSGGERQRVLIARALAQEPP 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 162 LLILDEPTTGVDPLARAQFWDLIARIRDERPtMSVIVATAYMDEAQRF-DWLIAMDAGRVLATGAPAELL 230
Cdd:COG1120 158 LLLLDEPTSHLDLAHQLEVLELLRRLARERG-RTVVMVLHDLNLAARYaDRLVLLKDGRIVAQGPPEEVL 226
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
272-489 |
7.10e-35 |
|
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of the LIV-I bacterial ABC-type two-component transport system that imports neutral, branched-chain amino acids. The E. coli branched-chain amino acid transporter comprises a heterodimer of ABC transporters (LivF and LivG), a heterodimer of six-helix TM domains (LivM and LivH), and one of two alternative soluble periplasmic substrate binding proteins (LivK or LivJ). ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules.
Pssm-ID: 213191 [Multi-domain] Cd Length: 222 Bit Score: 132.56 E-value: 7.10e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 272 IEARGLTMRFGDFTAVDHVSFRIRRGEIFGFLGSNGCGKSTTMKMLTGLLPATEGTAQLFGKEVD---PKDINtRRRVGY 348
Cdd:cd03224 1 LEVENLNAGYGKSQILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDGRDITglpPHERA-RAGIGY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 349 MSQAFSLYSELTVRQNLVLHARLFgvPAAEIDARVDEMARRF-GLADIYGMLPDSLPLGMRQRLSLAVAMVHKPELLILD 427
Cdd:cd03224 80 VPEGRRIFPELTVEENLLLGAYAR--RRAKRKARLERVYELFpRLKERRKQLAGTLSGGEQQMLAIARALMSRPKLLLLD 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 505416896 428 EPTSGVDPVARDSFWQLMIDLARRDlVTIFISTHFMNEAQR-CDRISLMHAGRVLASDSPAEL 489
Cdd:cd03224 158 EPSEGLAPKIVEEIFEAIRELRDEG-VTILLVEQNARFALEiADRAYVLERGRVVLEGTAAEL 219
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
272-489 |
8.64e-35 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 137.27 E-value: 8.64e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 272 IEARGLTMRFGDFTAVDHVSFRIRRGEIFGFLGSNGCGKSTTMKMLTGLLPATEGTAQLFGKE---VDPkdinTRRRVGY 348
Cdd:PRK11607 20 LEIRNLTKSFDGQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVDlshVPP----YQRPINM 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 349 MSQAFSLYSELTVRQNLVLHARLFGVPAAEIDARVDEMARRFGLADIYGMLPDSLPLGMRQRLSLAVAMVHKPELLILDE 428
Cdd:PRK11607 96 MFQSYALFPHMTVEQNIAFGLKQDKLPKAEIASRVNEMLGLVHMQEFAKRKPHQLSGGQRQRVALARSLAKRPKLLLLDE 175
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 505416896 429 PTSGVDPVARDSFWQLMIDLARRDLVTIFISTHFMNEAQR-CDRISLMHAGRVLASDSPAEL 489
Cdd:PRK11607 176 PMGALDKKLRDRMQLEVVDILERVGVTCVMVTHDQEEAMTmAGRIAIMNRGKFVQIGEPEEI 237
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
7-224 |
2.23e-34 |
|
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: 131.10 E-value: 2.23e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 7 VRFSDVSLRYGKTVALDRITLDVPAGLTTGLIGPDGVGKSSLLALASGARALQTGGVdALGGdmRSRRHRERVCRRIAYM 86
Cdd:cd03259 1 LELKGLSKTYGSVRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEI-LIDG--RDVTGVPPERRNIGMV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 87 PQGLgkNLYPTLSVEENLQFFARLFGHDAGERRRRIDALTQSTGLFPFLSRPAGKLSGGMKQKLGLCCALIHDPDLLILD 166
Cdd:cd03259 78 FQDY--ALFPHLTVAENIAFGLKLRGVPKAEIRARVRELLELVGLEGLLNRYPHELSGGQQQRVALARALAREPSLLLLD 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 505416896 167 EPTTGVDPLARAQFWDLIARIRDERpTMSVIVATAYMDEAQRF-DWLIAMDAGRVLATG 224
Cdd:cd03259 156 EPLSALDAKLREELREELKELQREL-GITTIYVTHDQEEALALaDRIAVMNEGRIVQVG 213
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
272-489 |
4.45e-34 |
|
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: 131.15 E-value: 4.45e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 272 IEARGLTMRFGD-FTAVDHVSFRIRRGEIFGFLGSNGCGKSTTMKMLTGLLPATEGTAQLFGKEV---DPKDINT-RRRV 346
Cdd:cd03256 1 IEVENLSKTYPNgKKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGTDInklKGKALRQlRRQI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 347 GYMSQAFSLYSELTVRQNlVLHARL---------FG-VPAAEIdARVDEMARRFGLADIYGMLPDSLPLGMRQRLSLAVA 416
Cdd:cd03256 81 GMIFQQFNLIERLSVLEN-VLSGRLgrrstwrslFGlFPKEEK-QRALAALERVGLLDKAYQRADQLSGGQQQRVAIARA 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 505416896 417 MVHKPELLILDEPTSGVDPVARDSFWQLMIDLARRDLVTIFISTHFMNEAQR-CDRISLMHAGRVLASDSPAEL 489
Cdd:cd03256 159 LMQQPKLILADEPVASLDPASSRQVMDLLKRINREEGITVIVSLHQVDLAREyADRIVGLKDGRIVFDGPPAEL 232
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
273-483 |
4.65e-34 |
|
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: 128.71 E-value: 4.65e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 273 EARGLTMRFGDFTAVDHVSFRIRRGEIFGFLGSNGCGKSTTMKMLTGLLPATEGTAQLFGKEV---DPKDIntRRRVGYM 349
Cdd:cd03214 1 EVENLSVGYGGRTVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDGKDLaslSPKEL--ARKIAYV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 350 SQAFSLyseltvrqnlvlharlfgvpaaeidARVDEMARRFgladiYGMLPDslplGMRQRLSLAVAMVHKPELLILDEP 429
Cdd:cd03214 79 PQALEL-------------------------LGLAHLADRP-----FNELSG----GERQRVLLARALAQEPPILLLDEP 124
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 505416896 430 TSGVDPVARDSFWQLMIDLARRDLVTIFISTHFMNEAQR-CDRISLMHAGRVLAS 483
Cdd:cd03214 125 TSHLDIAHQIELLELLRRLARERGKTVVMVLHDLNLAARyADRVILLKDGRIVAQ 179
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
212-495 |
6.42e-34 |
|
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: 139.97 E-value: 6.42e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 212 LIA--MDAGRVLAtgaPAELLARTGcDSLEAAFIAL--------LPENERRGHKPVKIEPLRADaragtaIEARGLTMRF 281
Cdd:COG2274 414 LIAfnILSGRFLA---PVAQLIGLL-QRFQDAKIALerlddildLPPEREEGRSKLSLPRLKGD------IELENVSFRY 483
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 282 GDFT--AVDHVSFRIRRGEIFGFLGSNGCGKSTTMKMLTGLLPATEGTAQLFG---KEVDPKDIntRRRVGYMSQAFSLY 356
Cdd:COG2274 484 PGDSppVLDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEPTSGRILIDGidlRQIDPASL--RRQIGVVLQDVFLF 561
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 357 SElTVRQNLVLharlfGVPAAEiDARVDEMARRFGLADIYGMLPD-----------SLPLGMRQRLSLAVAMVHKPELLI 425
Cdd:COG2274 562 SG-TIRENITL-----GDPDAT-DEEIIEAARLAGLHDFIEALPMgydtvvgeggsNLSGGQRQRLAIARALLRNPRILI 634
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 426 LDEPTSGVDPVARDSFWQLMIDLARRdlVTIFISTHFMNEAQRCDRISLMHAGRVLASDSPAELVRARGA 495
Cdd:COG2274 635 LDEATSALDAETEAIILENLRRLLKG--RTVIIIAHRLSTIRLADRIIVLDKGRIVEDGTHEELLARKGL 702
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
1-239 |
7.82e-34 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 133.42 E-value: 7.82e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 1 MNASSV-VRFSDVSLRYGKTVALDRITLDVPAGLTTGLIGPDGVGKSSLLALASGARALQTGGVDALGGDMRSRRHRERV 79
Cdd:PRK13536 35 GSMSTVaIDLAGVSKSYGDKAVVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKITVLGVPVPARARLARA 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 80 CrrIAYMPQGlgKNLYPTLSVEENLQFFARLFGHDAgerrRRIDALTQSTGLFPFLSRPA----GKLSGGMKQKLGLCCA 155
Cdd:PRK13536 115 R--IGVVPQF--DNLDLEFTVRENLLVFGRYFGMST----REIEAVIPSLLEFARLESKAdarvSDLSGGMKRRLTLARA 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 156 LIHDPDLLILDEPTTGVDPLARAQFWD----LIARirderpTMSVIVATAYMDEAQRF-DWLIAMDAGRVLATGAPAELL 230
Cdd:PRK13536 187 LINDPQLLILDEPTTGLDPHARHLIWErlrsLLAR------GKTILLTTHFMEEAERLcDRLCVLEAGRKIAEGRPHALI 260
|
250
....*....|
gi 505416896 231 -ARTGCDSLE 239
Cdd:PRK13536 261 dEHIGCQVIE 270
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
2-499 |
9.56e-34 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 136.84 E-value: 9.56e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 2 NASSVVRFSDVSLRYGKTVALDRITLDVPAGLTTGLIGPDGVGKSSLLALASGARALQTGGVDALGGDMRSRRHRERVCR 81
Cdd:PRK09700 1 MATPYISMAGIGKSFGPVHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNINYNKLDHKLAAQL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 82 RIAYMPQGLgkNLYPTLSVEENLqFFARL-----FGH---DAGERRRRIDALTQSTGLFPFLSRPAGKLSGGMKQKLGLC 153
Cdd:PRK09700 81 GIGIIYQEL--SVIDELTVLENL-YIGRHltkkvCGVniiDWREMRVRAAMMLLRVGLKVDLDEKVANLSISHKQMLEIA 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 154 CALIHDPDLLILDEPTTGVDPLARAQFWDLIARIRDErpTMSVIVATAYMDEAQRF-DWLIAMDAGRVLATGAPAEL--- 229
Cdd:PRK09700 158 KTLMLDAKVIIMDEPTSSLTNKEVDYLFLIMNQLRKE--GTAIVYISHKLAEIRRIcDRYTVMKDGSSVCSGMVSDVsnd 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 230 -LAR--TGCDsLEAAFIALLPENERRGHKPVkieplradaragtaIEARGLTMRfgDFTAVDHVSFRIRRGEIFGFLGSN 306
Cdd:PRK09700 236 dIVRlmVGRE-LQNRFNAMKENVSNLAHETV--------------FEVRNVTSR--DRKKVRDISFSVCRGEILGFAGLV 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 307 GCGKSTTMKMLTGLLPATEGTAQLFGKEVDPKD--INTRRRVGYMSQA---FSLYSELTVRQNLVLHARL--------FG 373
Cdd:PRK09700 299 GSGRTELMNCLFGVDKRAGGEIRLNGKDISPRSplDAVKKGMAYITESrrdNGFFPNFSIAQNMAISRSLkdggykgaMG 378
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 374 VPAAEIDARVDEMARR---FGLADIYGMLPDsLPLGMRQRLSLAVAMVHKPELLILDEPTSGVDPVARDSFWQLMIDLAR 450
Cdd:PRK09700 379 LFHEVDEQRTAENQREllaLKCHSVNQNITE-LSGGNQQKVLISKWLCCCPEVIIFDEPTRGIDVGAKAEIYKVMRQLAD 457
|
490 500 510 520
....*....|....*....|....*....|....*....|....*....
gi 505416896 451 RDLVTIFISTHFMNEAQRCDRISLMHAGRVlasdspAELVRARGAATLE 499
Cdd:PRK09700 458 DGKVILMVSSELPEIITVCDRIAVFCEGRL------TQILTNRDDMSEE 500
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
272-480 |
1.39e-33 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 128.40 E-value: 1.39e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 272 IEARGLTMRFGDFTAVDHVSFRIRRGEIFGFLGSNGCGKSTTMKMLTGLLPATEGTAQLFGKEVDPKDINT-RRRVGYMS 350
Cdd:COG4619 1 LELEGLSFRVGGKPILSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIYLDGKPLSAMPPPEwRRQVAYVP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 351 QAFSLYSElTVRQNLVLHARLFGVPAAEidARVDEMARRFGL-ADIYGMLPDSLPLGMRQRLSLAVAMVHKPELLILDEP 429
Cdd:COG4619 81 QEPALWGG-TVRDNLPFPFQLRERKFDR--ERALELLERLGLpPDILDKPVERLSGGERQRLALIRALLLQPDVLLLDEP 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 505416896 430 TSGVDPVARDSFWQLMIDLARRDLVTIFISTHFMNEAQR-CDRISLMHAGRV 480
Cdd:COG4619 158 TSALDPENTRRVEELLREYLAEEGRAVLWVSHDPEQIERvADRVLTLEAGRL 209
|
|
| GldA_ABC_ATP |
TIGR03522 |
gliding motility-associated ABC transporter ATP-binding subunit GldA; Members of this protein ... |
7-231 |
2.88e-33 |
|
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: 130.66 E-value: 2.88e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 7 VRFSDVSLRYGKTVALDRITLDVPAGLTTGLIGPDGVGKSSLLALASGARALQTGGVDALGGDMrsRRHRERVCRRIAYM 86
Cdd:TIGR03522 3 IRVSSLTKLYGTQNALDEVSFEAQKGRIVGFLGPNGAGKSTTMKIITGYLPPDSGSVQVCGEDV--LQNPKEVQRNIGYL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 87 PQGlgKNLYPTLSVEENLQFFARLFGHDAGERRRRIDALTQSTGLFPFLSRPAGKLSGGMKQKLGLCCALIHDPDLLILD 166
Cdd:TIGR03522 81 PEH--NPLYLDMYVREYLQFIAGIYGMKGQLLKQRVEEMIELVGLRPEQHKKIGQLSKGYRQRVGLAQALIHDPKVLILD 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 505416896 167 EPTTGVDPLARAQFWDLIARIRDERptmSVIVATAYMDEAQRF-DWLIAMDAGRVLATGAPAELLA 231
Cdd:TIGR03522 159 EPTTGLDPNQLVEIRNVIKNIGKDK---TIILSTHIMQEVEAIcDRVIIINKGKIVADKKLDELSA 221
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
6-231 |
4.03e-33 |
|
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440744 [Multi-domain] Cd Length: 241 Bit Score: 128.17 E-value: 4.03e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 6 VVRFSDVSLRYGKTVALDRITLDVPAGLTTGLIGPDGVGKSSLLALASGARALQTGGVDALGGDMR--SRRHRERVCRRI 83
Cdd:COG1127 5 MIEVRNLTKSFGDRVVLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEILVDGQDITglSEKELYELRRRI 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 84 AYMPQGLGknLYPTLSVEENLQFFARLFGH-DAGERRRRIDALTQSTGLFPFLSRPAGKLSGGMKQKLGLCCALIHDPDL 162
Cdd:COG1127 85 GMLFQGGA--LFDSLTVFENVAFPLREHTDlSEAEIRELVLEKLELVGLPGAADKMPSELSGGMRKRVALARALALDPEI 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 163 LILDEPTTGVDPLARAQFWDLIARIRDERPTMSVIVaTAYMDEAQRF-DWLIAMDAGRVLATGAPAELLA 231
Cdd:COG1127 163 LLYDEPTAGLDPITSAVIDELIRELRDELGLTSVVV-THDLDSAFAIaDRVAVLADGKIIAEGTPEELLA 231
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
286-486 |
1.27e-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: 1.27e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 286 AVDHVSFRIRRGEIFGFLGSNGCGKSTTMKMLTGLLPATEGTAQLFGKEVDPKDINTRRRVGYMSQAFSLYSELTVRQNL 365
Cdd:TIGR01257 945 AVDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGKDIETNLDAVRQSLGMCPQHNILFHHLTVAEHI 1024
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 366 VLHARLFGVPAAEIDARVDEMARRFGLADIYGMLPDSLPLGMRQRLSLAVAMVHKPELLILDEPTSGVDPVARDSFWQLM 445
Cdd:TIGR01257 1025 LFYAQLKGRSWEEAQLEMEAMLEDTGLHHKRNEEAQDLSGGMQRKLSVAIAFVGDAKVVVLDEPTSGVDPYSRRSIWDLL 1104
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 505416896 446 idLARRDLVTIFISTHFMNEAQRC-DRISLMHAGRVLASDSP 486
Cdd:TIGR01257 1105 --LKYRSGRTIIMSTHHMDEADLLgDRIAIISQGRLYCSGTP 1144
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
273-480 |
2.28e-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: 125.06 E-value: 2.28e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 273 EARGLTMRFGDFT-AVDHVSFRIRRGEIFGFLGSNGCGKSTTMKMLTGLLPATEGTAQLFGKEVDPKDinTRRRVGYMSQ 351
Cdd:cd03226 1 RIENISFSYKKGTeILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLNGKPIKAKE--RRKSIGYVMQ 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 352 --AFSLYSElTVRQNLVLHARlfgvPAAEIDARVDEMARRFGLADIYGMLPDSLPLGMRQRLSLAVAMVHKPELLILDEP 429
Cdd:cd03226 79 dvDYQLFTD-SVREELLLGLK----ELDAGNEQAETVLKDLDLYALKERHPLSLSGGQKQRLAIAAALLSGKDLLIFDEP 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 505416896 430 TSGVDPVARDSFWQLMIDLARRDlVTIFISTH---FMneAQRCDRISLMHAGRV 480
Cdd:cd03226 154 TSGLDYKNMERVGELIRELAAQG-KAVIVITHdyeFL--AKVCDRVLLLANGAI 204
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
272-479 |
3.22e-32 |
|
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP (Multidrug Resistance Protein)-like transporters are involved in drug, peptide, and lipid export. They belong to the subfamily C of the ATP-binding cassette (ABC) superfamily of transport proteins. The ABCC subfamily contains transporters with a diverse functional spectrum that includes ion transport, cell surface receptor, and toxin secretion activities. The MRP-like family, similar to all ABC proteins, have a common four-domain core structure constituted by two membrane-spanning domains, each composed of six transmembrane (TM) helices, and two nucleotide-binding domains (NBD). ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213195 [Multi-domain] Cd Length: 171 Bit Score: 123.26 E-value: 3.22e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 272 IEARGLTMRFGDFT--AVDHVSFRIRRGEIFGFLGSNGCGKSTTMKMLTGLLPATEGTAQLFGKEVdpKDINT---RRRV 346
Cdd:cd03228 1 IEFKNVSFSYPGRPkpVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGVDL--RDLDLeslRKNI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 347 GYMSQAFSLYSElTVRQNLvlharlfgvpaaeidarvdemarrfgladiygmlpdsLPLGMRQRLSLAVAMVHKPELLIL 426
Cdd:cd03228 79 AYVPQDPFLFSG-TIRENI-------------------------------------LSGGQRQRIAIARALLRDPPILIL 120
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 505416896 427 DEPTSGVDPVARDSFWQLMIDLARRdlVTIFISTHFMNEAQRCDRISLMHAGR 479
Cdd:cd03228 121 DEATSALDPETEALILEALRALAKG--KTVIVIAHRLSTIRDADRIIVLDDGR 171
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
7-231 |
3.60e-32 |
|
ATP-binding cassette transport system involved in resistance to organic solvents; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213228 [Multi-domain] Cd Length: 235 Bit Score: 125.31 E-value: 3.60e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 7 VRFSDVSLRYGKTVALDRITLDVPAGLTTGLIGPDGVGKSSLLALASGARALQTGGVDALGGDMR--SRRHRERVCRRIA 84
Cdd:cd03261 1 IELRGLTKSFGGRTVLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGEDISglSEAELYRLRRRMG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 85 YMPQGLGknLYPTLSVEENLQFFARLFGHDAGERRRRIDALT-QSTGLFPFLSRPAGKLSGGMKQKLGLCCALIHDPDLL 163
Cdd:cd03261 81 MLFQSGA--LFDSLTVFENVAFPLREHTRLSEEEIREIVLEKlEAVGLRGAEDLYPAELSGGMKKRVALARALALDPELL 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 505416896 164 ILDEPTTGVDPLARAQFWDLIARIRDERPTMSVIVaTAYMDEAQRF-DWLIAMDAGRVLATGAPAELLA 231
Cdd:cd03261 159 LYDEPTAGLDPIASGVIDDLIRSLKKELGLTSIMV-THDLDTAFAIaDRIAVLYDGKIVAEGTPEELRA 226
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
264-495 |
3.89e-32 |
|
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: 132.97 E-value: 3.89e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 264 ADARAGTAIEARGLTMRF--GDFTAVDHVSFRIRRGEIFGFLGSNGCGKSTTMKMLTGLLPATEGTAQLFGKEVDPKDIN 341
Cdd:COG4987 326 APAPGGPSLELEDVSFRYpgAGRPVLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFLDPQSGSITLGGVDLRDLDED 405
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 342 T-RRRVGYMSQAFSLYSElTVRQNLvlharLFGVPAAEiDARVDEMARRFGLADIYGMLPDSL--PL---------GMRQ 409
Cdd:COG4987 406 DlRRRIAVVPQRPHLFDT-TLRENL-----RLARPDAT-DEELWAALERVGLGDWLAALPDGLdtWLgeggrrlsgGERR 478
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 410 RLSLAVAMVHKPELLILDEPTSGVDPVARDSFWQLMIDLARRDlvTIFISTHFMNEAQRCDRISLMHAGRVLASDSPAEL 489
Cdd:COG4987 479 RLALARALLRDAPILLLDEPTEGLDAATEQALLADLLEALAGR--TVLLITHRLAGLERMDRILVLEDGRIVEQGTHEEL 556
|
....*.
gi 505416896 490 VRARGA 495
Cdd:COG4987 557 LAQNGR 562
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
3-231 |
5.30e-32 |
|
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: 125.54 E-value: 5.30e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 3 ASSVVRFSDVSLRYGKTVALDRITLDVPAGLTTGLIGPDGVGKSSLLALASGARALQTGGVDALGGDmrsrrhrervcrr 82
Cdd:COG0411 1 SDPLLEVRGLTKRFGGLVAVDDVSLEVERGEIVGLIGPNGAGKTTLFNLITGFYRPTSGRILFDGRD------------- 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 83 IAYMP------QGLGK-----NLYPTLSVEENL-------------QFFARLFGHDAGER--RRRIDALTQSTGLFPFLS 136
Cdd:COG0411 68 ITGLPphriarLGIARtfqnpRLFPELTVLENVlvaaharlgrgllAALLRLPRARREEReaRERAEELLERVGLADRAD 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 137 RPAGKLSGGMKQKLGLCCALIHDPDLLILDEPTTGVDPLARAQFWDLIARIRDERPT--------MSVIVATAymdeaqr 208
Cdd:COG0411 148 EPAGNLSYGQQRRLEIARALATEPKLLLLDEPAAGLNPEETEELAELIRRLRDERGItilliehdMDLVMGLA------- 220
|
250 260
....*....|....*....|...
gi 505416896 209 fDWLIAMDAGRVLATGAPAELLA 231
Cdd:COG0411 221 -DRIVVLDFGRVIAEGTPAEVRA 242
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
7-224 |
6.23e-32 |
|
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: 123.87 E-value: 6.23e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 7 VRFSDVSLRYGKTVALDRITLDVPAGLTTGLIGPDGVGKSSLLALASGARALQTGGVDALGGDMRSRRHRERVCRRIAYM 86
Cdd:cd03268 1 LKTNDLTKTYGKKRVLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEITFDGKSYQKNIEALRRIGALIEA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 87 PqglgkNLYPTLSVEENLQFFARLFGhdagERRRRIDALTQSTGLFPFLSRPAGKLSGGMKQKLGLCCALIHDPDLLILD 166
Cdd:cd03268 81 P-----GFYPNLTARENLRLLARLLG----IRKKRIDEVLDVVGLKDSAKKKVKGFSLGMKQRLGIALALLGNPDLLILD 151
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 505416896 167 EPTTGVDPLARAQFWDLIARIRDErpTMSVIVATAYMDEAQRF-DWLIAMDAGRVLATG 224
Cdd:cd03268 152 EPTNGLDPDGIKELRELILSLRDQ--GITVLISSHLLSEIQKVaDRIGIINKGKLIEEG 208
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
268-491 |
1.77e-31 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 124.74 E-value: 1.77e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 268 AGTAIEARGLTMRFGDFT--AVDHVSFRIRRGEIFGFLGSNGCGKSTTMKMLTGLLPATEGTAQLFGKEVDPKDI-NTRR 344
Cdd:PRK13635 2 KEEIIRVEHISFRYPDAAtyALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGGMVLSEETVwDVRR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 345 RVGYMSQ-AFSLYSELTVRQNLVLHARLFGVPAAEIDARVDEMARRFGLADIYGMLPDSLPLGMRQRLSLAVAMVHKPEL 423
Cdd:PRK13635 82 QVGMVFQnPDNQFVGATVQDDVAFGLENIGVPREEMVERVDQALRQVGMEDFLNREPHRLSGGQKQRVAIAGVLALQPDI 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 505416896 424 LILDEPTSGVDPVARDSFWQLMIDLARRDLVTIFISTHFMNEAQRCDRISLMHAGRVLASDSPAELVR 491
Cdd:PRK13635 162 IILDEATSMLDPRGRREVLETVRQLKEQKGITVLSITHDLDEAAQADRVIVMNKGEILEEGTPEEIFK 229
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
1-206 |
2.01e-31 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 124.05 E-value: 2.01e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 1 MNASS-VVRFSDVSLRY----GKTVALDRITLDVPAGLTTGLIGPDGVGKSSLLALASGARALQTGGVDALGgdmrsrRH 75
Cdd:COG1116 1 MSAAApALELRGVSKRFptggGGVTALDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPTSGEVLVDG------KP 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 76 RERVCRRIAYMPQGLgkNLYPTLSVEENLQFFARLFGHDAGERRRRIDALTQSTGLFPFLSRPAGKLSGGMKQKLGLCCA 155
Cdd:COG1116 75 VTGPGPDRGVVFQEP--ALLPWLTVLDNVALGLELRGVPKAERRERARELLELVGLAGFEDAYPHQLSGGMRQRVAIARA 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 505416896 156 LIHDPDLLILDEPTTGVDPLARAQFWDLIARIRDERPTmSVIVATAYMDEA 206
Cdd:COG1116 153 LANDPEVLLMDEPFGALDALTRERLQDELLRLWQETGK-TVLFVTHDVDEA 202
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
264-494 |
2.96e-31 |
|
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease components [Energy production and conversion, Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 444012 [Multi-domain] Cd Length: 563 Bit Score: 130.26 E-value: 2.96e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 264 ADARAGTAIEARGLTMRFGD-FTAVDHVSFRIRRGEIFGFLGSNGCGKSTTMKMLTGLLPATEGTAQLFGKEVDPKDINT 342
Cdd:COG4988 329 LPAAGPPSIELEDVSFSYPGgRPALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPPYSGSILINGVDLSDLDPAS 408
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 343 -RRRVGYMSQAFSLYSElTVRQNLvlharLFGVPAAEiDARVDEMARRFGLADIYGMLPDSL--PL---------GMRQR 410
Cdd:COG4988 409 wRRQIAWVPQNPYLFAG-TIRENL-----RLGRPDAS-DEELEAALEAAGLDEFVAALPDGLdtPLgeggrglsgGQAQR 481
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 411 LSLAVAMVHKPELLILDEPTSGVDPVARDSFWQLMIDLARRdlVTIFISTHFMNEAQRCDRISLMHAGRVLASDSPAELV 490
Cdd:COG4988 482 LALARALLRDAPLLLLDEPTAHLDAETEAEILQALRRLAKG--RTVILITHRLALLAQADRILVLDDGRIVEQGTHEELL 559
|
....
gi 505416896 491 RARG 494
Cdd:COG4988 560 AKNG 563
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
272-488 |
4.09e-31 |
|
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: 122.44 E-value: 4.09e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 272 IEARGLTMRFGDFTaVDHVSFRIRRGEIFGFLGSNGCGKSTTMKMLTGLLPATEGTAQLFGKevdpkDINT----RRRVG 347
Cdd:cd03299 1 LKVENLSKDWKEFK-LKNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNGK-----DITNlppeKRDIS 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 348 YMSQAFSLYSELTVRQNLVLHARLFGVPAAEIDARVDEMARRFGLADIYGMLPDSLPLGMRQRLSLAVAMVHKPELLILD 427
Cdd:cd03299 75 YVPQNYALFPHMTVYKNIAYGLKKRKVDKKEIERKVLEIAEMLGIDHLLNRKPETLSGGEQQRVAIARALVVNPKILLLD 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 505416896 428 EPTSGVDPVARDSFWQLMIDLARRDLVTIFISTHFMNEAQR-CDRISLMHAGRVLASDSPAE 488
Cdd:cd03299 155 EPFSALDVRTKEKLREELKKIRKEFGVTVLHVTHDFEEAWAlADKVAIMLNGKLIQVGKPEE 216
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
286-478 |
4.30e-31 |
|
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: 132.83 E-value: 4.30e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 286 AVDHVSFRIRRGEIFGFLGSNGCGKSTTMKMLTGLLPATEGTAQLFGKEVDPKDINTRRRVGYMSQAFSLYSELTVRQNL 365
Cdd:TIGR01257 1954 AVDRLCVGVRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAGKSILTNISDVHQNMGYCPQFDAIDDLLTGREHL 2033
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 366 VLHARLFGVPAAEIDARVDEMARRFGLADIYGMLPDSLPLGMRQRLSLAVAMVHKPELLILDEPTSGVDPVARDSFWQLM 445
Cdd:TIGR01257 2034 YLYARLRGVPAEEIEKVANWSIQSLGLSLYADRLAGTYSGGNKRKLSTAIALIGCPPLVLLDEPTTGMDPQARRMLWNTI 2113
|
170 180 190
....*....|....*....|....*....|....
gi 505416896 446 IDLARRDLVTIfISTHFMNEAQR-CDRISLMHAG 478
Cdd:TIGR01257 2114 VSIIREGRAVV-LTSHSMEECEAlCTRLAIMVKG 2146
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
7-220 |
4.63e-31 |
|
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: 121.44 E-value: 4.63e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 7 VRFSDVSLRYG----KTVALDRITLDVPAGLTTGLIGPDGVGKSSLLALASGARALQTGGVDALGGDMRSRRHRERVC-- 80
Cdd:cd03255 1 IELKNLSKTYGgggeKVQALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRVDGTDISKLSEKELAAfr 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 81 -RRIAYMPQGLgkNLYPTLSVEENLQFFARLFGHDAGERRRRIDALTQSTGLFPFLSRPAGKLSGGMKQKLGLCCALIHD 159
Cdd:cd03255 81 rRHIGFVFQSF--NLLPDLTALENVELPLLLAGVPKKERRERAEELLERVGLGDRLNHYPSELSGGQQQRVAIARALAND 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 505416896 160 PDLLILDEPTTGVDPLARAQFWDLIARIRDERPTmSVIVATAYMDEAQRFDWLIAMDAGRV 220
Cdd:cd03255 159 PKIILADEPTGNLDSETGKEVMELLRELNKEAGT-TIVVVTHDPELAEYADRIIELRDGKI 218
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
280-484 |
5.92e-31 |
|
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: 121.49 E-value: 5.92e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 280 RFGDFTAVDHVSFRIRRGEIFGFLGSNGCGKSTTMKMLTGLLPATEGTAQLFGKEVDPKDINTrrrvgymsqafSLYSEL 359
Cdd:cd03220 31 EVGEFWALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVTVRGRVSSLLGLGG-----------GFNPEL 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 360 TVRQNLVLHARLFGVPAAEIDARVDEMARRFGLADIYgmlpdSLPL-----GMRQRLSLAVAMVHKPELLILDEPTSGVD 434
Cdd:cd03220 100 TGRENIYLNGRLLGLSRKEIDEKIDEIIEFSELGDFI-----DLPVktyssGMKARLAFAIATALEPDILLIDEVLAVGD 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 505416896 435 PVARDSFWQLMIDLaRRDLVTIFISTHFMNEAQR-CDRISLMHAGRVLASD 484
Cdd:cd03220 175 AAFQEKCQRRLREL-LKQGKTVILVSHDPSSIKRlCDRALVLEKGKIRFDG 224
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
285-489 |
6.50e-31 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 123.27 E-value: 6.50e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 285 TAVDHVSFRIRRGEIFGFLGSNGCGKSTTMKMLTGLLPATEGTaqLFGKEVDPKDINT----RRRVGYMSQAFSLYSELT 360
Cdd:PRK13633 24 LALDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGK--VYVDGLDTSDEENlwdiRNKAGMVFQNPDNQIVAT 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 361 -VRQNLVLHARLFGVPAAEIDARVDEMARRFGLADIYGMLPDSLPLGMRQRLSLAVAMVHKPELLILDEPTSGVDPVARD 439
Cdd:PRK13633 102 iVEEDVAFGPENLGIPPEEIRERVDESLKKVGMYEYRRHAPHLLSGGQKQRVAIAGILAMRPECIIFDEPTAMLDPSGRR 181
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 505416896 440 SFWQLMIDLARRDLVTIFISTHFMNEAQRCDRISLMHAGRVLASDSPAEL 489
Cdd:PRK13633 182 EVVNTIKELNKKYGITIILITHYMEEAVEADRIIVMDSGKVVMEGTPKEI 231
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
280-484 |
6.74e-31 |
|
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type transporter and the ATPase component of a molybdate transport system that also includes the periplasmic binding protein ModA and the membrane protein ModB. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213264 [Multi-domain] Cd Length: 214 Bit Score: 120.86 E-value: 6.74e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 280 RFGDFTAvdHVSFRIRrGEIFGFLGSNGCGKSTTMKMLTGLLPATEGTAQLFGKEVDP--KDIN---TRRRVGYMSQAFS 354
Cdd:cd03297 9 RLPDFTL--KIDFDLN-EEVTGIFGASGAGKSTLLRCIAGLEKPDGGTIVLNGTVLFDsrKKINlppQQRKIGLVFQQYA 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 355 LYSELTVRQNLVlharlFGVPA---AEIDARVDEMARRFGLADIYGMLPDSLPLGMRQRLSLAVAMVHKPELLILDEPTS 431
Cdd:cd03297 86 LFPHLNVRENLA-----FGLKRkrnREDRISVDELLDLLGLDHLLNRYPAQLSGGEKQRVALARALAAQPELLLLDEPFS 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 505416896 432 GVDPVARDsfwQLMIDLARR----DLVTIFIsTHFMNEAQR-CDRISLMHAGRVLASD 484
Cdd:cd03297 161 ALDRALRL---QLLPELKQIkknlNIPVIFV-THDLSEAEYlADRIVVMEDGRLQYIG 214
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
270-489 |
6.75e-31 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 122.45 E-value: 6.75e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 270 TAIEARGLTMRFGDFTAVDHVSFRIRRGEIFGFLGSNGCGKSTTMKML---TGLLP--ATEGTAQLFGKEVDPKDINT-- 342
Cdd:COG1117 10 PKIEVRNLNVYYGDKQALKDINLDIPENKVTALIGPSGCGKSTLLRCLnrmNDLIPgaRVEGEILLDGEDIYDPDVDVve 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 343 -RRRVGYMSQ-----AFSLYseltvrQNLVLHARLFGV-PAAEIDARVDEMARRFGL----ADIYGMLPDSLPLGMRQRL 411
Cdd:COG1117 90 lRRRVGMVFQkpnpfPKSIY------DNVAYGLRLHGIkSKSELDEIVEESLRKAALwdevKDRLKKSALGLSGGQQQRL 163
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 505416896 412 SLAVAMVHKPELLILDEPTSGVDPVARDSFWQLMIDLARRdlVTIFISTHFMNEAQRC-DRISLMHAGRVLASDSPAEL 489
Cdd:COG1117 164 CIARALAVEPEVLLMDEPTSALDPISTAKIEELILELKKD--YTIVIVTHNMQQAARVsDYTAFFYLGELVEFGPTEQI 240
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
7-206 |
1.74e-30 |
|
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ATP-binding subunits of the bacterial ABC-type nitrate and sulfonate transport systems, respectively. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213260 [Multi-domain] Cd Length: 220 Bit Score: 119.88 E-value: 1.74e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 7 VRFSDVSLRYG----KTVALDRITLDVPAGLTTGLIGPDGVGKSSLLALASGARALQTGGVDALGGDMRSRRHRervcrr 82
Cdd:cd03293 1 LEVRNVSKTYGggggAVTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVDGEPVTGPGPD------ 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 83 IAYMPQGlgKNLYPTLSVEENLQFFARLFGHDAGERRRRIDALTQSTGLFPFLSRPAGKLSGGMKQKLGLCCALIHDPDL 162
Cdd:cd03293 75 RGYVFQQ--DALLPWLTVLDNVALGLELQGVPKAEARERAEELLELVGLSGFENAYPHQLSGGMRQRVALARALAVDPDV 152
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 505416896 163 LILDEPTTGVDPLARAQFWDLIARI-RDERPTmsVIVATAYMDEA 206
Cdd:cd03293 153 LLLDEPFSALDALTREQLQEELLDIwRETGKT--VLLVTHDIDEA 195
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
10-231 |
2.93e-30 |
|
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: 119.85 E-value: 2.93e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 10 SDVSLRYGKTVALDRITLDVPAGLTTGLIGPDGVGKSSLLALASGARALQTGGVDALGGDmrsrrhrervcrrIAYMP-- 87
Cdd:cd03219 4 RGLTKRFGGLVALDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFDGED-------------ITGLPph 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 88 ----QGLGK-----NLYPTLSVEENLQ----------FFARLFGHDAGERRRRIDALTQSTGLFPFLSRPAGKLSGGMKQ 148
Cdd:cd03219 71 eiarLGIGRtfqipRLFPELTVLENVMvaaqartgsgLLLARARREEREARERAEELLERVGLADLADRPAGELSYGQQR 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 149 KLGLCCALIHDPDLLILDEPTTGVDPLARAQFWDLIARIRDERPT-------MSVIvatayMDEAQRfdwLIAMDAGRVL 221
Cdd:cd03219 151 RLEIARALATDPKLLLLDEPAAGLNPEETEELAELIRELRERGITvllvehdMDVV-----MSLADR---VTVLDQGRVI 222
|
250
....*....|
gi 505416896 222 ATGAPAELLA 231
Cdd:cd03219 223 AEGTPDEVRN 232
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
272-488 |
4.18e-30 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 122.60 E-value: 4.18e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 272 IEARGLTMRF----GDFTAVDHVSFRIRRGEIFGFLGSNGCGKSTTMKMLTGLLPATEGTAQLFGKEV---DPKDIN-TR 343
Cdd:PRK11153 2 IELKNISKVFpqggRTIHALNNVSLHIPAGEIFGVIGASGAGKSTLIRCINLLERPTSGRVLVDGQDLtalSEKELRkAR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 344 RRVGYMSQAFSLYSELTVRQNLVLHARLFGVPAAEIDARVDEMARRFGLADIYGMLPDSLPLGMRQRLSLAVAMVHKPEL 423
Cdd:PRK11153 82 RQIGMIFQHFNLLSSRTVFDNVALPLELAGTPKAEIKARVTELLELVGLSDKADRYPAQLSGGQKQRVAIARALASNPKV 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 505416896 424 LILDEPTSGVDPVARDSFWQLMIDLARRDLVTIFISTHFMNEAQR-CDRISLMHAGRVLASDSPAE 488
Cdd:PRK11153 162 LLCDEATSALDPATTRSILELLKDINRELGLTIVLITHEMDVVKRiCDRVAVIDAGRLVEQGTVSE 227
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
286-482 |
4.81e-30 |
|
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: 118.85 E-value: 4.81e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 286 AVDHVSFRIRRGEIFGFLGSNGCGKSTTMKMLTGLLPATEGTAQLFG---KEVDPKDIntRRRVGYMSQAFSLYSElTVR 362
Cdd:cd03245 19 ALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGtdiRQLDPADL--RRNIGYVPQDVTLFYG-TLR 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 363 QNLVLharlfGVPAAEiDARVDEMARRFGLADIYGMLPDSLPL-----------GMRQRLSLAVAMVHKPELLILDEPTS 431
Cdd:cd03245 96 DNITL-----GAPLAD-DERILRAAELAGVTDFVNKHPNGLDLqigergrglsgGQRQAVALARALLNDPPILLLDEPTS 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 505416896 432 GVDPVARDSFWQLMIDLARRDlvTIFISTHFMNEAQRCDRISLMHAGRVLA 482
Cdd:cd03245 170 AMDMNSEERLKERLRQLLGDK--TLIIITHRPSLLDLVDRIIVMDSGRIVA 218
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
271-490 |
1.00e-29 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 119.33 E-value: 1.00e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 271 AIEARGLTMRFGDFT--AVDHVSFRIRRGEIFGFLGSNGCGKSTTMKMLTGLLPATEGTAQLFGKEVDPKDIN-TRRRVG 347
Cdd:PRK13632 7 MIKVENVSFSYPNSEnnALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIDGITISKENLKeIRKKIG 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 348 YMSQ---------------AFSLYSELtvrqnlvlharlfgVPAAEIDARVDEMARRFGLADIYGMLPDSLPLGMRQRLS 412
Cdd:PRK13632 87 IIFQnpdnqfigatveddiAFGLENKK--------------VPPKKMKDIIDDLAKKVGMEDYLDKEPQNLSGGQKQRVA 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 505416896 413 LAVAMVHKPELLILDEPTSGVDPVARDSFWQLMIDLARRDLVTIFISTHFMNEAQRCDRISLMHAGRVLASDSPAELV 490
Cdd:PRK13632 153 IASVLALNPEIIIFDESTSMLDPKGKREIKKIMVDLRKTRKKTLISITHDMDEAILADKVIVFSEGKLIAQGKPKEIL 230
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
8-219 |
1.51e-29 |
|
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: 115.03 E-value: 1.51e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 8 RFSDVSLRYGKTVALDRITLDVPAGLTTGLIGPDGVGKSSLLalasgaRALqTGGVDALGGDmrsrrhrervcrrIAYMP 87
Cdd:cd00267 1 EIENLSFRYGGRTALDNVSLTLKAGEIVALVGPNGSGKSTLL------RAI-AGLLKPTSGE-------------ILIDG 60
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 88 QGLGKNLYPtlsveenlqffarlfghdagERRRRIDALTQstglfpflsrpagkLSGGMKQKLGLCCALIHDPDLLILDE 167
Cdd:cd00267 61 KDIAKLPLE--------------------ELRRRIGYVPQ--------------LSGGQRQRVALARALLLNPDLLLLDE 106
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 505416896 168 PTTGVDPLARAQFWDLIARIRDERPTmsVIVATAYMDEAQRF-DWLIAMDAGR 219
Cdd:cd00267 107 PTSGLDPASRERLLELLRELAEEGRT--VIIVTHDPELAELAaDRVIVLKDGK 157
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
7-239 |
3.04e-29 |
|
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: 117.02 E-value: 3.04e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 7 VRFSDVSLRYGK-TVALDRITLDVPAGLTTGLIGPDGVGKSSLLALASgaRALQ-TGGVDALGGDMRSRRHRERVCRRIA 84
Cdd:cd03295 1 IEFENVTKRYGGgKKAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMIN--RLIEpTSGEIFIDGEDIREQDPVELRRKIG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 85 YMPQGLGknLYPTLSVEENLQFFARLFGHDAGERRRRIDALTQSTGLFP--FLSRPAGKLSGGMKQKLGLCCALIHDPDL 162
Cdd:cd03295 79 YVIQQIG--LFPHMTVEENIALVPKLLKWPKEKIRERADELLALVGLDPaeFADRYPHELSGGQQQRVGVARALAADPPL 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 505416896 163 LILDEPTTGVDPLARAQFWDLIARIRDERPTMSVIVaTAYMDEAQRF-DWLIAMDAGRVLATGAPAELLARTGCDSLE 239
Cdd:cd03295 157 LLMDEPFGALDPITRDQLQEEFKRLQQELGKTIVFV-THDIDEAFRLaDRIAIMKNGEIVQVGTPDEILRSPANDFVA 233
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
270-502 |
3.16e-29 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 117.57 E-value: 3.16e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 270 TAIEARGLTMRFGDFTAVDHVSFRIRRGEIFGFLGSNGCGKSTTMKMLTGLLPATEGTAQLFGKEVD---PKDINTRRRV 346
Cdd:PRK13548 1 AMLEARNLSVRLGGRTLLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLNGRPLAdwsPAELARRRAV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 347 gyMSQAFSLYSELTVRQnLVLHARL-FGVPAAEIDARVDEMARRFGLADIYGMLPDSLPLGMRQRLSLAVAMV------H 419
Cdd:PRK13548 81 --LPQHSSLSFPFTVEE-VVAMGRApHGLSRAEDDALVAAALAQVDLAHLAGRDYPQLSGGEQQRVQLARVLAqlwepdG 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 420 KPELLILDEPTSGVDPVARDSFWQLMIDLARRDLVTIFISTHFMNEAQR-CDRISLMHAGRVLASDSPAELVRargAATL 498
Cdd:PRK13548 158 PPRWLLLDEPTSALDLAHQHHVLRLARQLAHERGLAVIVVLHDLNLAARyADRIVLLHQGRLVADGTPAEVLT---PETL 234
|
....
gi 505416896 499 EDAF 502
Cdd:PRK13548 235 RRVY 238
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
22-170 |
3.60e-29 |
|
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: 113.90 E-value: 3.60e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 22 LDRITLDVPAGLTTGLIGPDGVGKSSLLALASGARALQTGGVDALGGDMRSRRHRERVCRrIAYMPQGLgkNLYPTLSVE 101
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDLTDDERKSLRKE-IGYVFQDP--QLFPRLTVR 77
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 505416896 102 ENLQFFARLFGHDAGERRRRIDALTQSTGLFPFLSRPAGK----LSGGMKQKLGLCCALIHDPDLLILDEPTT 170
Cdd:pfam00005 78 ENLRLGLLLKGLSKREKDARAEEALEKLGLGDLADRPVGErpgtLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
|
|
| potA |
TIGR01187 |
spermidine/putrescine ABC transporter ATP-binding subunit; This model describes spermidine ... |
303-489 |
4.93e-29 |
|
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: 118.75 E-value: 4.93e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 303 LGSNGCGKSTTMKMLTGLLPATEGTAQLFGKEVD--PKDintRRRVGYMSQAFSLYSELTVRQNLVLHARLFGVPAAEID 380
Cdd:TIGR01187 2 LGPSGCGKTTLLRLLAGFEQPDSGSIMLDGEDVTnvPPH---LRHINMVFQSYALFPHMTVEENVAFGLKMRKVPRAEIK 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 381 ARVDEMARRFGLADIYGMLPDSLPLGMRQRLSLAVAMVHKPELLILDEPTSGVDPVARDSFWQLMIDLARRDLVTIFIST 460
Cdd:TIGR01187 79 PRVLEALRLVQLEEFADRKPHQLSGGQQQRVALARALVFKPKILLLDEPLSALDKKLRDQMQLELKTIQEQLGITFVFVT 158
|
170 180 190
....*....|....*....|....*....|
gi 505416896 461 HFMNEA-QRCDRISLMHAGRVLASDSPAEL 489
Cdd:TIGR01187 159 HDQEEAmTMSDRIAIMRKGKIAQIGTPEEI 188
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
272-500 |
5.03e-29 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 117.50 E-value: 5.03e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 272 IEARGLTMRF---GDFTAVDHVSFRIRRGEIFGFLGSNGCGKSTTMKMLTGLLPATEGTAQLFGKEVDPKDI-NTRRRVG 347
Cdd:PRK13642 5 LEVENLVFKYekeSDVNQLNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDGELLTAENVwNLRRKIG 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 348 YMSQ-AFSLYSELTVRQNLVLHARLFGVPAAEIDARVDEMARRFGLADIYGMLPDSLPLGMRQRLSLAVAMVHKPELLIL 426
Cdd:PRK13642 85 MVFQnPDNQFVGATVEDDVAFGMENQGIPREEMIKRVDEALLAVNMLDFKTREPARLSGGQKQRVAVAGIIALRPEIIIL 164
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 505416896 427 DEPTSGVDPVARDSFWQLMIDLARRDLVTIFISTHFMNEAQRCDRISLMHAGRVLASDSPAELVrargaATLED 500
Cdd:PRK13642 165 DESTSMLDPTGRQEIMRVIHEIKEKYQLTVLSITHDLDEAASSDRILVMKAGEIIKEAAPSELF-----ATSED 233
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
272-489 |
6.15e-29 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 116.63 E-value: 6.15e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 272 IEARGLTMRFGDFTAVDHVSFRIRRGEIFGFLGSNGCGKSTTMKMLTGLLPATEGTAQLFGKEVD--PKDINTRRRVGYM 349
Cdd:PRK11300 6 LSVSGLMMRFGGLLAVNNVNLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTILLRGQHIEglPGHQIARMGVVRT 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 350 SQAFSLYSELTVRQNLV----------LHARLFGVPA---AEIDA--RVDEMARRFGLADIYGMLPDSLPLGMRQRLSLA 414
Cdd:PRK11300 86 FQHVRLFREMTVIENLLvaqhqqlktgLFSGLLKTPAfrrAESEAldRAATWLERVGLLEHANRQAGNLAYGQQRRLEIA 165
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 505416896 415 VAMVHKPELLILDEPTSGVDPVARDSFWQLMIDLARRDLVTIFISTHFMNEAQR-CDRISLMHAGRVLASDSPAEL 489
Cdd:PRK11300 166 RCMVTQPEILMLDEPAAGLNPKETKELDELIAELRNEHNVTVLLIEHDMKLVMGiSDRIYVVNQGTPLANGTPEEI 241
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
2-232 |
6.40e-29 |
|
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: 122.32 E-value: 6.40e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 2 NASSVVRFSDVSLRY-----GKTVALDRITLDVPAGLTTGLIGPDGVGKSSLLALASGARALQTGGVDALGGDMRSRRHR 76
Cdd:COG1123 256 AAEPLLEVRNLSKRYpvrgkGGVRAVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRPTSGSILFDGKDLTKLSRR 335
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 77 ERVCR--RIAYMPQglgkN----LYPTLSVEENLQFFARLFGH-DAGERRRRIDALTQSTGLFP-FLSRPAGKLSGGMKQ 148
Cdd:COG1123 336 SLRELrrRVQMVFQ----DpyssLNPRMTVGDIIAEPLRLHGLlSRAERRERVAELLERVGLPPdLADRYPHELSGGQRQ 411
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 149 KLGLCCALIHDPDLLILDEPTTGVDPLARAQFWDLIARIRDERpTMSVIVATAYMDEAQRF-DWLIAMDAGRVLATGAPA 227
Cdd:COG1123 412 RVAIARALALEPKLLILDEPTSALDVSVQAQILNLLRDLQREL-GLTYLFISHDLAVVRYIaDRVAVMYDGRIVEDGPTE 490
|
....*
gi 505416896 228 ELLAR 232
Cdd:COG1123 491 EVFAN 495
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
256-500 |
8.68e-29 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 117.07 E-value: 8.68e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 256 PVKIEPLRADARAGTAIEARgltmrfgdftAVDHVSFRIRRGEIFGFLGSNGCGKSTTMKMLTGLLPATEGTAQLFG--- 332
Cdd:PRK13637 2 SIKIENLTHIYMEGTPFEKK----------ALDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDGvdi 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 333 --KEVDPKDIntRRRVGYMSQ--AFSLYSElTVRQNLVLHARLFGVPAAEIDARVDEMARRFGLA--DIYGMLPDSLPLG 406
Cdd:PRK13637 72 tdKKVKLSDI--RKKVGLVFQypEYQLFEE-TIEKDIAFGPINLGLSEEEIENRVKRAMNIVGLDyeDYKDKSPFELSGG 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 407 MRQRLSLAVAMVHKPELLILDEPTSGVDPVARDSFWQLMIDLARRDLVTIFISTHFMNE-AQRCDRISLMHAGRVLASDS 485
Cdd:PRK13637 149 QKRRVAIAGVVAMEPKILILDEPTAGLDPKGRDEILNKIKELHKEYNMTIILVSHSMEDvAKLADRIIVMNKGKCELQGT 228
|
250
....*....|....*
gi 505416896 486 PAELVRArgAATLED 500
Cdd:PRK13637 229 PREVFKE--VETLES 241
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
246-494 |
9.78e-29 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 122.58 E-value: 9.78e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 246 LPENERRGHKPVKIEPLRADaragtaIEARGLTMRF-GDFTAVDHVSFRIRRGEIFGFLGSNGCGKSTTMKMLTGLLPAT 324
Cdd:COG1132 320 EPPEIPDPPGAVPLPPVRGE------IEFENVSFSYpGDRPVLKDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYDPT 393
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 325 EGTAQLFGkeVDPKDINT---RRRVGYMSQAFSLYSElTVRQNLvlharLFGVPAAEiDARVDEMARRFGLADIYGMLPD 401
Cdd:COG1132 394 SGRILIDG--VDIRDLTLeslRRQIGVVPQDTFLFSG-TIRENI-----RYGRPDAT-DEEVEEAAKAAQAHEFIEALPD 464
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 402 -----------SLPLGMRQRLSLAVAMVHKPELLILDEPTSGVDPVA----RDSFWQLMidlARRdlvTIFISTHFMNEA 466
Cdd:COG1132 465 gydtvvgergvNLSGGQRQRIAIARALLKDPPILILDEATSALDTETealiQEALERLM---KGR---TTIVIAHRLSTI 538
|
250 260
....*....|....*....|....*...
gi 505416896 467 QRCDRISLMHAGRVLASDSPAELVRARG 494
Cdd:COG1132 539 RNADRILVLDDGRIVEQGTHEELLARGG 566
|
|
| COG4559 |
COG4559 |
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism]; |
272-502 |
1.17e-28 |
|
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443620 [Multi-domain] Cd Length: 258 Bit Score: 115.98 E-value: 1.17e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 272 IEARGLTMRFGDFTAVDHVSFRIRRGEIFGFLGSNGCGKSTTMKMLTGLLPATEGTAQLFGKEVD---PKDINTRRRVgy 348
Cdd:COG4559 2 LEAENLSVRLGGRTLLDDVSLTLRPGELTAIIGPNGAGKSTLLKLLTGELTPSSGEVRLNGRPLAawsPWELARRRAV-- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 349 MSQAFSLYSELTVRQnLVLHARL-FGVPAAEIDARVDEMARRFGLADIYGMLPDSLPLGMRQRLSLA--VAMVHKPE--- 422
Cdd:COG4559 80 LPQHSSLAFPFTVEE-VVALGRApHGSSAAQDRQIVREALALVGLAHLAGRSYQTLSGGEQQRVQLArvLAQLWEPVdgg 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 423 --LLILDEPTSGVDPvardsFWQLMI-----DLARRDL--VTIFistHFMN-EAQRCDRISLMHAGRVLASDSPAELVRa 492
Cdd:COG4559 159 prWLFLDEPTSALDL-----AHQHAVlrlarQLARRGGgvVAVL---HDLNlAAQYADRILLLHQGRLVAQGTPEEVLT- 229
|
250
....*....|
gi 505416896 493 rgAATLEDAF 502
Cdd:COG4559 230 --DELLERVY 237
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
272-488 |
1.25e-28 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 118.90 E-value: 1.25e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 272 IEARGLTMRFGDFTAVDHVSFRIRRGEIFGFLGSNGCGKSTTMKMLTGLLPATEGTAQLFGKEVD--PKDintRRRVGYM 349
Cdd:PRK09452 15 VELRGISKSFDGKEVISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLDGQDIThvPAE---NRHVNTV 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 350 SQAFSLYSELTVRQNLVLHARLFGVPAAEIDARVDEMARRFGLADIYGMLPDSLPLGMRQRLSLAVAMVHKPELLILDEP 429
Cdd:PRK09452 92 FQSYALFPHMTVFENVAFGLRMQKTPAAEITPRVMEALRMVQLEEFAQRKPHQLSGGQQQRVAIARAVVNKPKVLLLDES 171
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 505416896 430 TSGVDPVARDSFwQLMIDLARRDLVTIFI-STHFMNEA-QRCDRISLMHAGRVLASDSPAE 488
Cdd:PRK09452 172 LSALDYKLRKQM-QNELKALQRKLGITFVfVTHDQEEAlTMSDRIVVMRDGRIEQDGTPRE 231
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
272-504 |
1.30e-28 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 114.85 E-value: 1.30e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 272 IEARGLTMRFGDFTAvdHVSFRIRRGEIFGFLGSNGCGKSTTMKMLTGLLPATEGTAQLFGKEVDPKDINtRRRVGYMSQ 351
Cdd:COG3840 2 LRLDDLTYRYGDFPL--RFDLTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILWNGQDLTALPPA-ERPVSMLFQ 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 352 AFSLYSELTVRQN--LVLHARLfgVPAAEIDARVDEMARRFGLADIYGMLPDSLPLGMRQRLSLAVAMVHKPELLILDEP 429
Cdd:COG3840 79 ENNLFPHLTVAQNigLGLRPGL--KLTAEQRAQVEQALERVGLAGLLDRLPGQLSGGQRQRVALARCLVRKRPILLLDEP 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 505416896 430 TSGVDPVARDSFWQLMIDLARRDLVTIFISTHFMNEAQR-CDRISLMHAGRVLASDSPAELVRARGAATLeDAFIG 504
Cdd:COG3840 157 FSALDPALRQEMLDLVDELCRERGLTVLMVTHDPEDAARiADRVLLVADGRIAADGPTAALLDGEPPPAL-AAYLG 231
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
16-483 |
1.41e-28 |
|
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: 121.09 E-value: 1.41e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 16 YGKTVALDRITLDVPAGLTTGLIGPDGVGKSSLLALASGARALQT--GGVDALGGDMRSRRHRERVCRRIAYMPQGLgkN 93
Cdd:TIGR02633 11 FGGVKALDGIDLEVRPGECVGLCGENGAGKSTLMKILSGVYPHGTwdGEIYWSGSPLKASNIRDTERAGIVIIHQEL--T 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 94 LYPTLSVEENLqFFARLFGHDAG-----ERRRRIDALTQSTGLFPF-LSRPAGKLSGGMKQKLGLCCALIHDPDLLILDE 167
Cdd:TIGR02633 89 LVPELSVAENI-FLGNEITLPGGrmaynAMYLRAKNLLRELQLDADnVTRPVGDYGGGQQQLVEIAKALNKQARLLILDE 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 168 PTTGvdpLARAQFWDLIARIRD-ERPTMSVIVATAYMDEAQRF-DWLIAMDAGRVLATgAPAELLArtgcdslEAAFIAL 245
Cdd:TIGR02633 168 PSSS---LTEKETEILLDIIRDlKAHGVACVYISHKLNEVKAVcDTICVIRDGQHVAT-KDMSTMS-------EDDIITM 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 246 LPENERRGHKPVkiEPlradARAGTAI-EARGLTMRFGDFTA---VDHVSFRIRRGEIFGFLGSNGCGKSTTMKMLTGLL 321
Cdd:TIGR02633 237 MVGREITSLYPH--EP----HEIGDVIlEARNLTCWDVINPHrkrVDDVSFSLRRGEILGVAGLVGAGRTELVQALFGAY 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 322 P-ATEGTAQLFGKEVD---------------PKDintRRRVGYMSQafslyseLTVRQNLVLHA--RLFGV----PAAEI 379
Cdd:TIGR02633 311 PgKFEGNVFINGKPVDirnpaqairagiamvPED---RKRHGIVPI-------LGVGKNITLSVlkSFCFKmridAAAEL 380
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 380 DArVDEMARRFGLADIYGMLP-DSLPLGMRQRLSLAVAMVHKPELLILDEPTSGVDPVARDSFWQLMIDLARRDLVTIFI 458
Cdd:TIGR02633 381 QI-IGSAIQRLKVKTASPFLPiGRLSGGNQQKAVLAKMLLTNPRVLILDEPTRGVDVGAKYEIYKLINQLAQEGVAIIVV 459
|
490 500
....*....|....*....|....*
gi 505416896 459 STHFMNEAQRCDRISLMHAGRVLAS 483
Cdd:TIGR02633 460 SSELAEVLGLSDRVLVIGEGKLKGD 484
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
6-224 |
1.92e-28 |
|
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter subfamily specific for the transport of dipeptides, oligopeptides (OppD), and nickel (NikDE). The NikABCDE system of E. coli belongs to this family and is composed of the periplasmic binding protein NikA, two integral membrane components (NikB and NikC), and two ATPase (NikD and NikE). The NikABCDE transporter is synthesized under anaerobic conditions to meet the increased demand for nickel resulting from hydrogenase synthesis. The molecular mechanism of nickel uptake in many bacteria and most archaea is not known. Many other members of this ABC family are also involved in the uptake of dipeptides and oligopeptides. The oligopeptide transport system (Opp) is a five-component ABC transport composed of a membrane-anchored substrate binding proteins (SRP), OppA, two transmembrane proteins, OppB and OppC, and two ATP-binding domains, OppD and OppF.
Pssm-ID: 213224 [Multi-domain] Cd Length: 228 Bit Score: 114.53 E-value: 1.92e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 6 VVRFSDVSLRY----GKTVALDRITLDVPAGLTTGLIGPDGVGKSSLLALASGARALQTGGVDALGGDM--RSRRHRERV 79
Cdd:cd03257 1 LLEVKNLSVSFptggGSVKALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGKDLlkLSRRLRKIR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 80 CRRIAYMPQGLGKNLYPTLSVEENLQ--FFARLFGHDAGERRRRIDALTQSTGLFP-FLSRPAGKLSGGMKQKLGLCCAL 156
Cdd:cd03257 81 RKEIQMVFQDPMSSLNPRMTIGEQIAepLRIHGKLSKKEARKEAVLLLLVGVGLPEeVLNRYPHELSGGQRQRVAIARAL 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 505416896 157 IHDPDLLILDEPTTGVDPLARAQFWDLIARIRDERpTMSVIVATAYMDEAQRF-DWLIAMDAGRVLATG 224
Cdd:cd03257 161 ALNPKLLIADEPTSALDVSVQAQILDLLKKLQEEL-GLTLLFITHDLGVVAKIaDRVAVMYAGKIVEEG 228
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
272-489 |
3.95e-28 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 114.79 E-value: 3.95e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 272 IEARGLTMRFGDFT-AVDHVSFRIRRGEIFGFLGSNGCGKSTTMKMLTGLLPATEGTAQLFGKEV--DPKD-INTRRRVG 347
Cdd:PRK13639 2 LETRDLKYSYPDGTeALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIKGEPIkyDKKSlLEVRKTVG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 348 YM-----SQAFSLyselTVRQNLVLHARLFGVPAAEIDARVDEMARRFGLADIYGMLPDSLPLGMRQRLSLAVAMVHKPE 422
Cdd:PRK13639 82 IVfqnpdDQLFAP----TVEEDVAFGPLNLGLSKEEVEKRVKEALKAVGMEGFENKPPHHLSGGQKKRVAIAGILAMKPE 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 505416896 423 LLILDEPTSGVDPVARDSFWQLMIDLARRDlVTIFISTHFMNEAQR-CDRISLMHAGRVLASDSPAEL 489
Cdd:PRK13639 158 IIVLDEPTSGLDPMGASQIMKLLYDLNKEG-ITIIISTHDVDLVPVyADKVYVMSDGKIIKEGTPKEV 224
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
270-480 |
5.73e-28 |
|
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: 111.37 E-value: 5.73e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 270 TAIEARGLTMRfgdfTAVDHVSFRIRRGEIFGFLGSNGCGKSTTMKMLTGLLPATEGTAQLFGKEVDPKDINTRRR--VG 347
Cdd:cd03215 3 PVLEVRGLSVK----GAVRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITLDGKPVTRRSPRDAIRagIA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 348 YMS---QAFSLYSELTVRQNLVLHARLFGvpaaeidarvdemarrfgladiygmlpdslplGMRQRLSLAVAMVHKPELL 424
Cdd:cd03215 79 YVPedrKREGLVLDLSVAENIALSSLLSG--------------------------------GNQQKVVLARWLARDPRVL 126
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 505416896 425 ILDEPTSGVDPVARDSFWQLMIDLARRDLVTIFISTHfMNEAQR-CDRISLMHAGRV 480
Cdd:cd03215 127 ILDEPTRGVDVGAKAEIYRLIRELADAGKAVLLISSE-LDELLGlCDRILVMYEGRI 182
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
10-224 |
6.62e-28 |
|
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: 111.37 E-value: 6.62e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 10 SDVSLRYGKTVALDRITLDVPAGLTTGLIGPDGVGKSSLLALASGARALQTGGVDALGGDMRSRRHRERVCRrIAYMPQG 89
Cdd:cd03214 3 ENLSVGYGGRTVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDGKDLASLSPKELARK-IAYVPQA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 90 LgknlyptlsveenlqffarlfghdagerrrridaltQSTGLFPFLSRPAGKLSGGMKQKLGLCCALIHDPDLLILDEPT 169
Cdd:cd03214 82 L------------------------------------ELLGLAHLADRPFNELSGGERQRVLLARALAQEPPILLLDEPT 125
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 505416896 170 TGVDPLARAQFWDLIARIRDERPtMSVIVATAYMDEAQRF-DWLIAMDAGRVLATG 224
Cdd:cd03214 126 SHLDIAHQIELLELLRRLARERG-KTVVMVLHDLNLAARYaDRVILLKDGRIVAQG 180
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
121-461 |
7.13e-28 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 118.96 E-value: 7.13e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 121 RIDALTQSTGLFPFLSRPAGKLSGGMKQKLGLCCALIHDPDLLILDEPTTGVDPLARAQFWDLIARIRDERPTMSVIVat 200
Cdd:PRK10938 115 RCEQLAQQFGITALLDRRFKYLSTGETRKTLLCQALMSEPDLLILDEPFDGLDVASRQQLAELLASLHQSGITLVLVL-- 192
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 201 aymdeaQRFDWL--IAMDAGrVLA------TGAPAELLARtgcdsleaAFIALLPENERRG--HKPVKIEPLRADARAGT 270
Cdd:PRK10938 193 ------NRFDEIpdFVQFAG-VLAdctlaeTGEREEILQQ--------ALVAQLAHSEQLEgvQLPEPDEPSARHALPAN 257
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 271 A--IEARGLTMRFGDFTAVDHVSFRIRRGEIFGFLGSNGCGKSTTMKMLTGLLPatEGTAQ---LFGKEVDPK----DIn 341
Cdd:PRK10938 258 EprIVLNNGVVSYNDRPILHNLSWQVNPGEHWQIVGPNGAGKSTLLSLITGDHP--QGYSNdltLFGRRRGSGetiwDI- 334
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 342 tRRRVGYMSQAFSL-YSELTVRQNLVLHARL--FGVPAAEIDAR---VDEMARRFGLADIYGMLP-DSLPLGmRQRLSLA 414
Cdd:PRK10938 335 -KKHIGYVSSSLHLdYRVSTSVRNVILSGFFdsIGIYQAVSDRQqklAQQWLDILGIDKRTADAPfHSLSWG-QQRLALI 412
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|.
gi 505416896 415 V-AMVHKPELLILDEPTSGVDPVARD---SFWQLMIDLARRDLvtIFISTH 461
Cdd:PRK10938 413 VrALVKHPTLLILDEPLQGLDPLNRQlvrRFVDVLISEGETQL--LFVSHH 461
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
272-490 |
7.57e-28 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 112.88 E-value: 7.57e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 272 IEARGLTMRFGDFTAVDHVSFRIRRGEIFGFLGSNGCGKSTTMKMLTGLLPATEGTAQLFGKEV-DPK--DINTRRRVGY 348
Cdd:PRK09493 2 IEFKNVSKHFGPTQVLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGLKVnDPKvdERLIRQEAGM 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 349 MSQAFSLYSELTVRQNLV---LHARlfGVPAAEIDARVDEMARRFGLADIYGMLPDSLPLGMRQRLSLAVAMVHKPELLI 425
Cdd:PRK09493 82 VFQQFYLFPHLTALENVMfgpLRVR--GASKEEAEKQARELLAKVGLAERAHHYPSELSGGQQQRVAIARALAVKPKLML 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 505416896 426 LDEPTSGVDPVARDSFWQLMIDLARRDLvTIFISTHFMNEAQRC-DRISLMHAGRVLASDSPAELV 490
Cdd:PRK09493 160 FDEPTSALDPELRHEVLKVMQDLAEEGM-TMVIVTHEIGFAEKVaSRLIFIDKGRIAEDGDPQVLI 224
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
2-234 |
1.42e-27 |
|
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: 118.71 E-value: 1.42e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 2 NASSVVRFSDVSLRY-GKTVALDRITLDVPAGLTTGLIGPDGVGKSSLLALASGARALQTGGVdALGGDMRSRRHRERVC 80
Cdd:COG4988 332 AGPPSIELEDVSFSYpGGRPALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPPYSGSI-LINGVDLSDLDPASWR 410
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 81 RRIAYMPQGlgknlyPTL---SVEENLqffaRLFGHDAGERRrrIDALTQSTGLFPFLSR-PAG----------KLSGGM 146
Cdd:COG4988 411 RQIAWVPQN------PYLfagTIRENL----RLGRPDASDEE--LEAALEAAGLDEFVAAlPDGldtplgeggrGLSGGQ 478
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 147 KQKLGLCCALIHDPDLLILDEPTTGVDPLARAQFWDLIARIRDERptmSVIVATAYMDEAQRFDWLIAMDAGRVLATGAP 226
Cdd:COG4988 479 AQRLALARALLRDAPLLLLDEPTAHLDAETEAEILQALRRLAKGR---TVILITHRLALLAQADRILVLDDGRIVEQGTH 555
|
....*...
gi 505416896 227 AELLARTG 234
Cdd:COG4988 556 EELLAKNG 563
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
8-229 |
1.62e-27 |
|
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: 112.28 E-value: 1.62e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 8 RFSDVSLRYG-KTVALDRITLDVPAGLTTGLIGPDGVGKSSLLALASGARALQTGGVDALGGDMRSRRHRERVCR--RIA 84
Cdd:cd03256 2 EVENLSKTYPnGKKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGTDINKLKGKALRQLrrQIG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 85 YMPQGLgkNLYPTLSVEEN-----------LQFFARLFGhdAGERRRRIDALTQStGLFPFLSRPAGKLSGGMKQKLGLC 153
Cdd:cd03256 82 MIFQQF--NLIERLSVLENvlsgrlgrrstWRSLFGLFP--KEEKQRALAALERV-GLLDKAYQRADQLSGGQQQRVAIA 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 505416896 154 CALIHDPDLLILDEPTTGVDPLARAQFWDLIARIRDERpTMSVIVATAYMDEAQRF-DWLIAMDAGRVLATGAPAEL 229
Cdd:cd03256 157 RALMQQPKLILADEPVASLDPASSRQVMDLLKRINREE-GITVIVSLHQVDLAREYaDRIVGLKDGRIVFDGPPAEL 232
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
4-222 |
1.85e-27 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 111.29 E-value: 1.85e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 4 SSVVRFSDVSLRYG----KTVALDRITLDVPAGLTTGLIGPDGVGKSSLLALASGARALQTG-----GVD--ALGGDMRS 72
Cdd:COG1136 2 SPLLELRNLTKSYGtgegEVTALRGVSLSIEAGEFVAIVGPSGSGKSTLLNILGGLDRPTSGevlidGQDisSLSERELA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 73 RRHRERvcrrIAYMPQGLgkNLYPTLSVEENLQFFARLFGHDAGERRRRIDALTQSTGLFPFLSRPAGKLSGGMKQKLGL 152
Cdd:COG1136 82 RLRRRH----IGFVFQFF--NLLPELTALENVALPLLLAGVSRKERRERARELLERVGLGDRLDHRPSQLSGGQQQRVAI 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 153 CCALIHDPDLLILDEPTTGVDPLARAQFWDLIARIRDERpTMSVIVATAYMDEAQRFDWLIAMDAGRVLA 222
Cdd:COG1136 156 ARALVNRPKLILADEPTGNLDSKTGEEVLELLRELNREL-GTTIVMVTHDPELAARADRVIRLRDGRIVS 224
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
3-480 |
2.24e-27 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 117.32 E-value: 2.24e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 3 ASSVVRFSDVSLRYGKTVALDRITLDVPAGLTTGLIGPDGVGKSSLLALASGARALQTGGVDALGGDMRSRRHRERVCRR 82
Cdd:PRK11288 1 SSPYLSFDGIGKTFPGVKALDDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSILIDGQEMRFASTTAALAAG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 83 IAYMPQGLgkNLYPTLSVEENL---QFFARLFGHDAGERRRRIDALTQSTGLFPFLSRPAGKLSGGMKQKLGLCCALIHD 159
Cdd:PRK11288 81 VAIIYQEL--HLVPEMTVAENLylgQLPHKGGIVNRRLLNYEAREQLEHLGVDIDPDTPLKYLSIGQRQMVEIAKALARN 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 160 PDLLILDEPTTGVDPLARAQFWDLIARIRDErpTMSVIVATAYMDEAQRF-DWLIAMDAGRVLATgapAELLARTGCDSL 238
Cdd:PRK11288 159 ARVIAFDEPTSSLSAREIEQLFRVIRELRAE--GRVILYVSHRMEEIFALcDAITVFKDGRYVAT---FDDMAQVDRDQL 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 239 EAAFIAllpeneRR-----GHKPVKIEPLRADARagtAIEARGLTmrfgdftavDHVSFRIRRGEIFGFLGSNGCGKSTT 313
Cdd:PRK11288 234 VQAMVG------REigdiyGYRPRPLGEVRLRLD---GLKGPGLR---------EPISFSVRAGEIVGLFGLVGAGRSEL 295
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 314 MKMLTGLLPATEGTAQLFGKEVDPKDINTRRRVGYM-----SQAFSLYSELTVRQNLVLHARLFGVPAAEI--DARVDEM 386
Cdd:PRK11288 296 MKLLYGATRRTAGQVYLDGKPIDIRSPRDAIRAGIMlcpedRKAEGIIPVHSVADNINISARRHHLRAGCLinNRWEAEN 375
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 387 ARRFgLADIYGMLPD------SLPLGMRQRLSLAVAMVHKPELLILDEPTSGVDPVARDSFWQLMIDLARRDLVTIFIST 460
Cdd:PRK11288 376 ADRF-IRSLNIKTPSreqlimNLSGGNQQKAILGRWLSEDMKVILLDEPTRGIDVGAKHEIYNVIYELAAQGVAVLFVSS 454
|
490 500
....*....|....*....|
gi 505416896 461 HFMNEAQRCDRISLMHAGRV 480
Cdd:PRK11288 455 DLPEVLGVADRIVVMREGRI 474
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
4-242 |
4.48e-27 |
|
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: 110.94 E-value: 4.48e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 4 SSVVRFSDVSLRYGKTVALDRITLDVPAGLTTGLIGPDGVGKSSLLALASGaRALQTGGVDA------LGG----DMRSR 73
Cdd:COG1119 1 DPLLELRNVTVRRGGKTILDDISWTVKPGEHWAILGPNGAGKSTLLSLITG-DLPPTYGNDVrlfgerRGGedvwELRKR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 74 rhrervcrrIAYMPQGLGKNLYPTLSVEENLQ--FFA--RLFGHDAGERRRRIDALTQSTGLFPFLSRPAGKLSGGMKQK 149
Cdd:COG1119 80 ---------IGLVSPALQLRFPRDETVLDVVLsgFFDsiGLYREPTDEQRERARELLELLGLAHLADRPFGTLSQGEQRR 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 150 LGLCCALIHDPDLLILDEPTTGVDPLARAQFWDLIARIRDErPTMSVIVATAYMDEAQR-FDWLIAMDAGRVLATGAPAE 228
Cdd:COG1119 151 VLIARALVKDPELLILDEPTAGLDLGARELLLALLDKLAAE-GAPTLVLVTHHVEEIPPgITHVLLLKDGRVVAAGPKEE 229
|
250
....*....|....
gi 505416896 229 LLarTGcDSLEAAF 242
Cdd:COG1119 230 VL--TS-ENLSEAF 240
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
272-461 |
6.25e-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: 109.42 E-value: 6.25e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 272 IEARGLTMRF-GDFTAVDHVSFRIRRGEIFGFLGSNGCGKSTTMKMLTGLLPATEGTAQLFGKEV-DPKDINT---RRRV 346
Cdd:cd03292 1 IEFINVTKTYpNGTAALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQDVsDLRGRAIpylRRKI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 347 GYMSQAFSLYSELTVRQNLVLHARLFGVPAAEIDARVDEMARRFGLADIYGMLPDSLPLGMRQRLSLAVAMVHKPELLIL 426
Cdd:cd03292 81 GVVFQDFRLLPDRNVYENVAFALEVTGVPPREIRKRVPAALELVGLSHKHRALPAELSGGEQQRVAIARAIVNSPTILIA 160
|
170 180 190
....*....|....*....|....*....|....*..
gi 505416896 427 DEPTSGVDPvarDSFWQLMIDLARRDL--VTIFISTH 461
Cdd:cd03292 161 DEPTGNLDP---DTTWEIMNLLKKINKagTTVVVATH 194
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
21-480 |
7.47e-27 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 115.87 E-value: 7.47e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 21 ALDRITLDVPAGLTTGLIGPDGVGKSSLLALASGARALQTGGVDALGGDMRSRRHRERVCRRIAYMPQGLgkNLYPTLSV 100
Cdd:PRK10762 19 ALSGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSILYLGKEVTFNGPKSSQEAGIGIIHQEL--NLIPQLTI 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 101 EENLqFFARLFGHDAG-----ERRRRIDALTQSTGLfPFLS-RPAGKLSGGMKQKLGLCCALIHDPDLLILDEPTtgvDP 174
Cdd:PRK10762 97 AENI-FLGREFVNRFGridwkKMYAEADKLLARLNL-RFSSdKLVGELSIGEQQMVEIAKVLSFESKVIIMDEPT---DA 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 175 LARAQFWDLIARIRDERPTMSVIVATAY-MDEA-QRFDWLIAMDAGRVLATGAPAELLartgcdslEAAFIALLPenerr 252
Cdd:PRK10762 172 LTDTETESLFRVIRELKSQGRGIVYISHrLKEIfEICDDVTVFRDGQFIAEREVADLT--------EDSLIEMMV----- 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 253 GHKPVKIEPLRADARAGTAIEARGLTmrfGdfTAVDHVSFRIRRGEIFGFLGSNGCGKSTTMKMLTGLLPATEGTAQLFG 332
Cdd:PRK10762 239 GRKLEDQYPRLDKAPGEVRLKVDNLS---G--PGVNDVSFTLRKGEILGVSGLMGAGRTELMKVLYGALPRTSGYVTLDG 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 333 KEVDPKDINTRRRVG--YMSQ---AFSLYSELTVRQNLVLHA-RLFGVPAAEIDAR-----VDEMARRF-----GLADIY 396
Cdd:PRK10762 314 HEVVTRSPQDGLANGivYISEdrkRDGLVLGMSVKENMSLTAlRYFSRAGGSLKHAdeqqaVSDFIRLFniktpSMEQAI 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 397 GMLPDslplGMRQRLSLAVAMVHKPELLILDEPTSGVDPVARDSFWQLMIDLARRDLVTIFISTHfMNEA-QRCDRISLM 475
Cdd:PRK10762 394 GLLSG----GNQQKVAIARGLMTRPKVLILDEPTRGVDVGAKKEIYQLINQFKAEGLSIILVSSE-MPEVlGMSDRILVM 468
|
....*
gi 505416896 476 HAGRV 480
Cdd:PRK10762 469 HEGRI 473
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
272-491 |
8.63e-27 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 112.89 E-value: 8.63e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 272 IEARGLTMRFGDFTAVDHVSFRIRRGEIFGFLGSNGCGKSTTMKMLTGLLPATEGtaQLFgkeVDPKDINTR----RRVG 347
Cdd:PRK11432 7 VVLKNITKRFGSNTVIDNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEG--QIF---IDGEDVTHRsiqqRDIC 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 348 YMSQAFSLYSELTVRQNLVLHARLFGVPAAEIDARVDEMarrFGLADIYGM---LPDSLPLGMRQRLSLAVAMVHKPELL 424
Cdd:PRK11432 82 MVFQSYALFPHMSLGENVGYGLKMLGVPKEERKQRVKEA---LELVDLAGFedrYVDQISGGQQQRVALARALILKPKVL 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 505416896 425 ILDEPTSGVDPVARDSFWQLMIDLARRDLVTIFISTHFMNEA-QRCDRISLMHAGRVLASDSPAELVR 491
Cdd:PRK11432 159 LFDEPLSNLDANLRRSMREKIRELQQQFNITSLYVTHDQSEAfAVSDTVIVMNKGKIMQIGSPQELYR 226
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
7-219 |
1.89e-26 |
|
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: 106.89 E-value: 1.89e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 7 VRFSDVSLRYGKTVALDRITLDVPAGLTTGLIGPDGVGKSSLLALASGARALQTGGVDALGGD-MRSRRHRERVCRRIAY 85
Cdd:cd03229 1 LELKNVSKRYGQKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGEDlTDLEDELPPLRRRIGM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 86 MPQGLgkNLYPTLSVEENLQFfarlfghdagerrrridaltqstglfpflsrpagKLSGGMKQKLGLCCALIHDPDLLIL 165
Cdd:cd03229 81 VFQDF--ALFPHLTVLENIAL----------------------------------GLSGGQQQRVALARALAMDPDVLLL 124
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 505416896 166 DEPTTGVDPLARAQFWDLIARIRDERpTMSVIVATAYMDEAQRF-DWLIAMDAGR 219
Cdd:cd03229 125 DEPTSALDPITRREVRALLKSLQAQL-GITVVLVTHDLDEAARLaDRVVVLRDGK 178
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
7-229 |
2.25e-26 |
|
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of fundamental importance in the cell physiology of bacteria because phosphate is required as a nutrient. The Pst system of E. coli comprises four distinct subunits encoded by the pstS, pstA, pstB, and pstC genes. The PstS protein is a phosphate-binding protein located in the periplasmic space. PstA and PstC are hydrophobic and they form the transmembrane portion of the Pst system. PstB is the catalytic subunit, which couples the energy of ATP hydrolysis to the import of phosphate across cellular membranes through the Pst system, often referred as ABC-protein. PstB belongs to one of the largest superfamilies of proteins characterized by a highly conserved adenosine triphosphate (ATP) binding cassette (ABC), which is also a nucleotide binding domain (NBD).
Pssm-ID: 213227 [Multi-domain] Cd Length: 227 Bit Score: 108.42 E-value: 2.25e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 7 VRFSDVSLRYGKTVALDRITLDVPAGLTTGLIGPDGVGKSSLL-------ALASGARAlqTGGVDALGGDMRSRRHRERV 79
Cdd:cd03260 1 IELRDLNVYYGDKHALKDISLDIPKGEITALIGPSGCGKSTLLrllnrlnDLIPGAPD--EGEVLLDGKDIYDLDVDVLE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 80 CRRIAYM----PqglgkNLYPtLSVEENLQFFARLFG-HDAGERRRRIDALTQSTGLFPFLSRP--AGKLSGGMKQKLGL 152
Cdd:cd03260 79 LRRRVGMvfqkP-----NPFP-GSIYDNVAYGLRLHGiKLKEELDERVEEALRKAALWDEVKDRlhALGLSGGQQQRLCL 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 505416896 153 CCALIHDPDLLILDEPTTGVDPLARAQFWDLIARIRDErptMSVIVATAYMDEAQRF-DWLIAMDAGRVLATGAPAEL 229
Cdd:cd03260 153 ARALANEPEVLLLDEPTSALDPISTAKIEELIAELKKE---YTIVIVTHNMQQAARVaDRTAFLLNGRLVEFGPTEQI 227
|
|
| ABC2_membrane_3 |
pfam12698 |
ABC-2 family transporter protein; This family is related to the ABC-2 membrane transporter ... |
644-982 |
2.59e-26 |
|
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: 111.33 E-value: 2.59e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 644 LIGSLVLMCVIGIGISL-------DVEDLTYAVLDRDQTELSHDYALNLSGSRYFVERPPIADYAELDRRMRDGELSLAI 716
Cdd:pfam12698 4 LIITLLLPILLILLLGLifsnavnDPEELPVAVVDEDNSSLSRQLVRALEASPTVNLVQYVDSEEEAKEALKNGKIDGLL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 717 EIPPNFARDVERGAPAQIAMWIDGAMPQRAETIRGYAIGMHTMWLADKARHRLGVTLAPRA-EVVTRYRYNPDVKSLPAM 795
Cdd:pfam12698 84 VIPKGFSKDLLKGESATVTVYINSSNLLVSKLILNALQSLLQQLNASALVLLLEALSTSAPiPVESTPLFNPQSGYAYYL 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 796 IPAVmPLLLLMLPAMLTALAVVRERELGSILNLYVTPVTRTEFLIGKQVPYVVLAMLNFLLMTMLArIAFDVPVkGSFMT 875
Cdd:pfam12698 164 VGLI-LMIIILIGAAIIAVSIVEEKESRIKERLLVSGVSPLQYWLGKILGDFLVGLLQLLIILLLL-FGIGIPF-GNLGL 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 876 LLLAVLIFNVVATGIGLLASTFTRSQVAAIVMTIIGTMIPTVqFAGLLTPLSSLEGTGRFIGLVYPATYMlsisrGVFNK 955
Cdd:pfam12698 241 LLLLFLLYGLAYIALGYLLGSLFKNSEDAQSIIGIVILLLSG-FFGGLFPLEDPPSFLQWIFSIIPFFSP-----IDGLL 314
|
330 340 350
....*....|....*....|....*....|.
gi 505416896 956 ALSLQDLHSQFWP----LAASAPVILGATIL 982
Cdd:pfam12698 315 RLIYGDSLWEIAPsliiLLLFAVVLLLLALL 345
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
3-232 |
2.70e-26 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 111.34 E-value: 2.70e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 3 ASSVVRFSDVSLRYGKTVALDRITLDVPAGLTTGLIGPDGVGKSSLLALASGARALQTGGVdALGG-DM-------RSrr 74
Cdd:COG3842 2 AMPALELENVSKRYGDVTALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRI-LLDGrDVtglppekRN-- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 75 hrervcrrIAYMPQGLGknLYPTLSVEENLQFFARLFGHDAGERRRRIDALTQSTGLFPFLSRPAGKLSGGMKQKLGLCC 154
Cdd:COG3842 79 --------VGMVFQDYA--LFPHLTVAENVAFGLRMRGVPKAEIRARVAELLELVGLEGLADRYPHQLSGGQQQRVALAR 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 505416896 155 ALIHDPDLLILDEPTTGVDPLARAQFWDLIARIRDERPTmSVIVATAYMDEAQRF-DWLIAMDAGRVLATGAPAELLAR 232
Cdd:COG3842 149 ALAPEPRVLLLDEPLSALDAKLREEMREELRRLQRELGI-TFIYVTHDQEEALALaDRIAVMNDGRIEQVGTPEEIYER 226
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
268-499 |
2.71e-26 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 111.37 E-value: 2.71e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 268 AGTAIEARGLTMRFGDFTAVDHVSFRIRRGEIFGFLGSNGCGKSTtmkmltGLLPAtegtaQLFGKEVD--PKDINT--- 342
Cdd:NF000106 10 ARNAVEVRGLVKHFGEVKAVDGVDLDVREGTVLGVLGP*GAA**R------GALPA-----HV*GPDAGrrPWRF*Twca 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 343 -----RRRVG-YMSQAFSLYSELTVRQNLVLHARLFGVPAAEIDARVDEMARRFGLADIYGMLPDSLPLGMRQRLSLAVA 416
Cdd:NF000106 79 nrralRRTIG*HRPVR*GRRESFSGRENLYMIGR*LDLSRKDARARADELLERFSLTEAAGRAAAKYSGGMRRRLDLAAS 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 417 MVHKPELLILDEPTSGVDPVARDSFWQLMIDLArRDLVTIFISTHFMNEA-QRCDRISLMHAGRVLASDSPAELVRARGA 495
Cdd:NF000106 159 MIGRPAVLYLDEPTTGLDPRTRNEVWDEVRSMV-RDGATVLLTTQYMEEAeQLAHELTVIDRGRVIADGKVDELKTKVGG 237
|
....
gi 505416896 496 ATLE 499
Cdd:NF000106 238 RTLQ 241
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
272-504 |
3.08e-26 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 114.11 E-value: 3.08e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 272 IEARGLTMRFGDFTAVDHVSFRIRRGEIFGFLGSNGCGKSTTMKMLTGLLPATEGTAQLFGKE---VDPKdINTRRRVGY 348
Cdd:PRK09700 6 ISMAGIGKSFGPVHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNINynkLDHK-LAAQLGIGI 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 349 MSQAFSLYSELTVRQNL----VLHARLFGVPA---AEIDARVDEMARRFGLADIYGMLPDSLPLGMRQRLSLAVAMVHKP 421
Cdd:PRK09700 85 IYQELSVIDELTVLENLyigrHLTKKVCGVNIidwREMRVRAAMMLLRVGLKVDLDEKVANLSISHKQMLEIAKTLMLDA 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 422 ELLILDEPTSGVDPVARDSFWQLMIDLARRDLVTIFIStHFMNEAQR-CDRISLMHAG-----RVLASDSPAELVRARGA 495
Cdd:PRK09700 165 KVIIMDEPTSSLTNKEVDYLFLIMNQLRKEGTAIVYIS-HKLAEIRRiCDRYTVMKDGssvcsGMVSDVSNDDIVRLMVG 243
|
....*....
gi 505416896 496 ATLEDAFIG 504
Cdd:PRK09700 244 RELQNRFNA 252
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
272-480 |
3.26e-26 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 110.59 E-value: 3.26e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 272 IEARGLTMRF-----------GDFTAVDHVSFRIRRGEIFGFLGSNGCGKSTTMKMLTGLLPATEGTAQLFGKEV---DP 337
Cdd:COG4608 8 LEVRDLKKHFpvrgglfgrtvGVVKAVDGVSFDIRRGETLGLVGESGCGKSTLGRLLLRLEEPTSGEILFDGQDItglSG 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 338 KDINT-RRRVGYMSQ---AfSLYSELTVRQNLVLHARLFGV-PAAEIDARVDEMARRFGL-ADIYGMLPDSLPLGMRQRL 411
Cdd:COG4608 88 RELRPlRRRMQMVFQdpyA-SLNPRMTVGDIIAEPLRIHGLaSKAERRERVAELLELVGLrPEHADRYPHEFSGGQRQRI 166
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 505416896 412 SLAVAMVHKPELLILDEPTSGVDPVARDSFWQLMIDLARR-DLVTIFIS------THFmneaqrCDRISLMHAGRV 480
Cdd:COG4608 167 GIARALALNPKLIVCDEPVSALDVSIQAQVLNLLEDLQDElGLTYLFIShdlsvvRHI------SDRVAVMYLGKI 236
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
267-489 |
3.33e-26 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 109.55 E-value: 3.33e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 267 RAGTAIEARGLTMRFGDFT-AVDHVSFRIRRGEIFGFLGSNGCGKSTTMKMLTGLLPATEGTAQLFGKEVDPKD---INT 342
Cdd:PRK13636 1 MEDYILKVEELNYNYSDGThALKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGKPIDYSRkglMKL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 343 RRRVGYMSQA--FSLYSElTVRQNLVLHARLFGVPAAEIDARVDEMARRFGLADIYGMLPDSLPLGMRQRLSLAVAMVHK 420
Cdd:PRK13636 81 RESVGMVFQDpdNQLFSA-SVYQDVSFGAVNLKLPEDEVRKRVDNALKRTGIEHLKDKPTHCLSFGQKKRVAIAGVLVME 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 421 PELLILDEPTSGVDPVARDSFWQLMIDLARRDLVTIFISTHFMNE-AQRCDRISLMHAGRVLASDSPAEL 489
Cdd:PRK13636 160 PKVLVLDEPTAGLDPMGVSEIMKLLVEMQKELGLTIIIATHDIDIvPLYCDNVFVMKEGRVILQGNPKEV 229
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
268-489 |
4.04e-26 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 109.34 E-value: 4.04e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 268 AGTAIEARGLTmrfgdftavdHVSFRIRRGEIFGFLGSNGCGKSTTMKMLTGLLPATEGTAQLfGKEV-----DPKDINT 342
Cdd:PRK13634 14 YKTPFERRALY----------DVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVTI-GERVitagkKNKKLKP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 343 -RRRVGYM-----SQAFslysELTVRQNLVLHARLFGVPAAEIDARVDEMARRFGL-ADIYGMLPDSLPLGMRQRLSLAV 415
Cdd:PRK13634 83 lRKKVGIVfqfpeHQLF----EETVEKDICFGPMNFGVSEEDAKQKAREMIELVGLpEELLARSPFELSGGQMRRVAIAG 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 505416896 416 AMVHKPELLILDEPTSGVDPVARDSFWQLMIDLARRDLVTIFISTHFMNEAQR-CDRISLMHAGRVLASDSPAEL 489
Cdd:PRK13634 159 VLAMEPEVLVLDEPTAGLDPKGRKEMMEMFYKLHKEKGLTTVLVTHSMEDAARyADQIVVMHKGTVFLQGTPREI 233
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
1-480 |
4.24e-26 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 113.61 E-value: 4.24e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 1 MNASSVVRFSDVSLRYGKTVALDRITLDVPAGLTTGLIGPDGVGKSSLLALASGARALQTGGVDALGGDMRSRRHRERVC 80
Cdd:PRK15439 6 TTAPPLLCARSISKQYSGVEVLKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIGGNPCARLTPAKAHQ 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 81 RRIAYMPQGlgKNLYPTLSVEENLQFfaRLFGHDAGERRrrIDALTQSTGLFPFLSRPAGKLSGGMKQKLGLCCALIHDP 160
Cdd:PRK15439 86 LGIYLVPQE--PLLFPNLSVKENILF--GLPKRQASMQK--MKQLLAALGCQLDLDSSAGSLEVADRQIVEILRGLMRDS 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 161 DLLILDEPTTGVDPlarAQFWDLIARIRDERPTMSVIVATAY-MDEA-QRFDWLIAMDAGRVLATGAPAELlartgcdSL 238
Cdd:PRK15439 160 RILILDEPTASLTP---AETERLFSRIRELLAQGVGIVFISHkLPEIrQLADRISVMRDGTIALSGKTADL-------ST 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 239 EAAFIALLPENerRGHKPVKIEPLRADARAGTAIEARGLT-MRFGDFTA--VDHVSFRIRRGEIFGFLGSNGCGKSTTMK 315
Cdd:PRK15439 230 DDIIQAITPAA--REKSLSASQKLWLELPGNRRQQAAGAPvLTVEDLTGegFRNISLEVRAGEILGLAGVVGAGRTELAE 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 316 MLTGLLPATEGTAQLFGKEVDPKDINTRRRVG--YMS---QAFSLYSELTVRQNLV--LHAR--LFGVPAAEiDARVDEM 386
Cdd:PRK15439 308 TLYGLRPARGGRIMLNGKEINALSTAQRLARGlvYLPedrQSSGLYLDAPLAWNVCalTHNRrgFWIKPARE-NAVLERY 386
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 387 ARRFGLADIYGMLP-DSLPLGMRQRLSLAVAMVHKPELLILDEPTSGVDPVARDSFWQLMIDLARRDLVTIFISTHFMNE 465
Cdd:PRK15439 387 RRALNIKFNHAEQAaRTLSGGNQQKVLIAKCLEASPQLLIVDEPTRGVDVSARNDIYQLIRSIAAQNVAVLFISSDLEEI 466
|
490
....*....|....*
gi 505416896 466 AQRCDRISLMHAGRV 480
Cdd:PRK15439 467 EQMADRVLVMHQGEI 481
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
270-466 |
4.28e-26 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 108.41 E-value: 4.28e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 270 TAIEARGLTMRFGDF----TAVDHVSFRIRRGEIFGFLGSNGCGKSTTMKMLTGLLPATEGTAQLFGKEVDPKDinTRRR 345
Cdd:COG4525 2 SMLTVRHVSVRYPGGgqpqPALQDVSLTIESGEFVVALGASGCGKTTLLNLIAGFLAPSSGEITLDGVPVTGPG--ADRG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 346 VGYmsQAFSLYSELTVRQNLVLHARLFGVPAAEIDARVDEMARRFGLADIYGMLPDSLPLGMRQRLSLAVAMVHKPELLI 425
Cdd:COG4525 80 VVF--QKDALLPWLNVLDNVAFGLRLRGVPKAERRARAEELLALVGLADFARRRIWQLSGGMRQRVGIARALAADPRFLL 157
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 505416896 426 LDEPTSGVDPVARDSFWQLMIDLARRDLVTIFISTHFMNEA 466
Cdd:COG4525 158 MDEPFGALDALTREQMQELLLDVWQRTGKGVFLITHSVEEA 198
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
290-481 |
9.49e-26 |
|
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: 106.59 E-value: 9.49e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 290 VSFRIRRGEIFGFLGSNGCGKSTTMKMLTGLLP---ATEGTAQLFGKEVDPKdiNTRRRVGYMSQAFSLYSELTVRQNLV 366
Cdd:cd03234 26 VSLHVESGQVMAILGSSGSGKTTLLDAISGRVEgggTTSGQILFNGQPRKPD--QFQKCVAYVRQDDILLPGLTVRETLT 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 367 LHARLFG---VPAAEIDARVDEMA-RRFGLADIYGMLPDSLPLGMRQRLSLAVAMVHKPELLILDEPTSGVDPVARDSFW 442
Cdd:cd03234 104 YTAILRLprkSSDAIRKKRVEDVLlRDLALTRIGGNLVKGISGGERRRVSIAVQLLWDPKVLILDEPTSGLDSFTALNLV 183
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 505416896 443 QLMIDLARRD---LVTIF-----ISTHFmneaqrcDRISLMHAGRVL 481
Cdd:cd03234 184 STLSQLARRNrivILTIHqprsdLFRLF-------DRILLLSSGEIV 223
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
272-494 |
1.24e-25 |
|
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: 106.42 E-value: 1.24e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 272 IEARGLTMRFG--DFTAVDHVSFRIRRGEIFGFLGSNGCGKSTTMKMLTGLLPATEGTAQLFGKEVDPKDINT-RRRVGY 348
Cdd:cd03252 1 ITFEHVRFRYKpdGPVILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGHDLALADPAWlRRQVGV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 349 MSQAFSLYSElTVRQNLVLharlfGVPAAEIDaRVDEMARRFGLADIYGMLPD-----------SLPLGMRQRLSLAVAM 417
Cdd:cd03252 81 VLQENVLFNR-SIRDNIAL-----ADPGMSME-RVIEAAKLAGAHDFISELPEgydtivgeqgaGLSGGQRQRIAIARAL 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 505416896 418 VHKPELLILDEPTSGVDPVARDSFWQLMID-LARRdlvTIFISTHFMNEAQRCDRISLMHAGRVLASDSPAELVRARG 494
Cdd:cd03252 154 IHNPRILIFDEATSALDYESEHAIMRNMHDiCAGR---TVIIIAHRLSTVKNADRIIVMEKGRIVEQGSHDELLAENG 228
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
7-232 |
1.60e-25 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 109.01 E-value: 1.60e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 7 VRFSDVSLRYGKTVALDRITLDVPAGLTTGLIGPDGVGKSSLLALASGaraLQT--------GGVDALG---GDmRSrrh 75
Cdd:COG3839 4 LELENVSKSYGGVEALKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAG---LEDptsgeiliGGRDVTDlppKD-RN--- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 76 rervcrrIAYMPQGLGknLYPTLSVEENLQFFARLFGHDAGERRRRIDALTQSTGLFPFLSRPAGKLSGGMKQKLGLCCA 155
Cdd:COG3839 77 -------IAMVFQSYA--LYPHMTVYENIAFPLKLRKVPKAEIDRRVREAAELLGLEDLLDRKPKQLSGGQRQRVALGRA 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 505416896 156 LIHDPDLLILDEPTTGVDPLARAQFWDLIARIRDERPTMSVIVaTAYMDEAQRF-DWLIAMDAGRVLATGAPAELLAR 232
Cdd:COG3839 148 LVREPKVFLLDEPLSNLDAKLRVEMRAEIKRLHRRLGTTTIYV-THDQVEAMTLaDRIAVMNDGRIQQVGTPEELYDR 224
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
271-481 |
1.82e-25 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 106.46 E-value: 1.82e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 271 AIEARGLTMRFGDFTAVDHVSFRIRRGEIFGFLGSNGCGKSTTMKMLTGLL-----PATEGTAQLFGK-----EVDPkdI 340
Cdd:PRK14267 4 AIETVNLRVYYGSNHVIKGVDLKIPQNGVFALMGPSGCGKSTLLRTFNRLLelneeARVEGEVRLFGRniyspDVDP--I 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 341 NTRRRVGYMSQAFSLYSELTVRQNLVLHARLFGV--PAAEIDARVDEMARRFGLAD-IYGML---PDSLPLGMRQRLSLA 414
Cdd:PRK14267 82 EVRREVGMVFQYPNPFPHLTIYDNVAIGVKLNGLvkSKKELDERVEWALKKAALWDeVKDRLndyPSNLSGGQRQRLVIA 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 505416896 415 VAMVHKPELLILDEPTSGVDPVARDSFWQLMIDLarRDLVTIFISTHFMNEAQR-CDRISLMHAGRVL 481
Cdd:PRK14267 162 RALAMKPKILLMDEPTANIDPVGTAKIEELLFEL--KKEYTIVLVTHSPAQAARvSDYVAFLYLGKLI 227
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
12-459 |
2.38e-25 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 111.72 E-value: 2.38e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 12 VSLRYGKTV--ALDRITLDVPAGLTTGLIGPDGVGKSsLLALaSGARALQTGGVDALGGDMR----------SRRHRERV 79
Cdd:PRK15134 13 VAFRQQQTVrtVVNDVSLQIEAGETLALVGESGSGKS-VTAL-SILRLLPSPPVVYPSGDIRfhgesllhasEQTLRGVR 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 80 CRRIAYMPQ----------GLGKNLYPTLSVEenlqffaRLFGHDAGerRRRIDALTQSTGLFPFLSRPAG---KLSGGM 146
Cdd:PRK15134 91 GNKIAMIFQepmvslnplhTLEKQLYEVLSLH-------RGMRREAA--RGEILNCLDRVGIRQAAKRLTDyphQLSGGE 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 147 KQKLGLCCALIHDPDLLILDEPTTGVDPLARAQFWDLIARIRDERpTMSVIVATAYMDEAQRF-DWLIAMDAGRVLATGA 225
Cdd:PRK15134 162 RQRVMIAMALLTRPELLIADEPTTALDVSVQAQILQLLRELQQEL-NMGLLFITHNLSIVRKLaDRVAVMQNGRCVEQNR 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 226 PAELLARTgcdslEAAFIALLPENERRGhkpvkiEPLRADARAGTAIEARGLTMRF-----------GDFTAVDHVSFRI 294
Cdd:PRK15134 241 AATLFSAP-----THPYTQKLLNSEPSG------DPVPLPEPASPLLDVEQLQVAFpirkgilkrtvDHNVVVKNISFTL 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 295 RRGEIFGFLGSNGCGKSTTMKMLTGLLPAtEGTAQLFGKEVDPKD----INTRRRVGYMSQ--AFSLYSELTVRQ----N 364
Cdd:PRK15134 310 RPGETLGLVGESGSGKSTTGLALLRLINS-QGEIWFDGQPLHNLNrrqlLPVRHRIQVVFQdpNSSLNPRLNVLQiieeG 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 365 LVLHARlfGVPAAEIDARVDEMARRFGL-ADIYGMLPDSLPLGMRQRLSLAVAMVHKPELLILDEPTSGVDPVARDSFWQ 443
Cdd:PRK15134 389 LRVHQP--TLSAAQREQQVIAVMEEVGLdPETRHRYPAEFSGGQRQRIAIARALILKPSLIILDEPTSSLDKTVQAQILA 466
|
490
....*....|....*..
gi 505416896 444 LMIDL-ARRDLVTIFIS 459
Cdd:PRK15134 467 LLKSLqQKHQLAYLFIS 483
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
7-224 |
3.59e-25 |
|
ATP-binding cassette domain of the thiamine transport system; Part of the binding-protein-dependent transport system tbpA-thiPQ for thiamine and TPP. Probably responsible for the translocation of thiamine across the membrane. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213265 [Multi-domain] Cd Length: 211 Bit Score: 104.50 E-value: 3.59e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 7 VRFSDVSLRYGKTVAldRITLDVPAGLTTGLIGPDGVGKSSLLALASGARALQTGGVDALGGDMRSRRHRERVCRRIAYm 86
Cdd:cd03298 1 VRLDKIRFSYGEQPM--HFDLTFAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLINGVDVTAAPPADRPVSMLFQ- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 87 pqglGKNLYPTLSVEEN--LQFFARLfgHDAGERRRRIDALTQSTGLFPFLSRPAGKLSGGMKQKLGLCCALIHDPDLLI 164
Cdd:cd03298 78 ----ENNLFAHLTVEQNvgLGLSPGL--KLTAEDRQAIEVALARVGLAGLEKRLPGELSGGERQRVALARVLVRDKPVLL 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 505416896 165 LDEPTTGVDPLARAQFWDLIARIRDERpTMSVIVATAYMDEAQR-FDWLIAMDAGRVLATG 224
Cdd:cd03298 152 LDEPFAALDPALRAEMLDLVLDLHAET-KMTVLMVTHQPEDAKRlAQRVVFLDNGRIAAQG 211
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
10-233 |
4.85e-25 |
|
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: 105.27 E-value: 4.85e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 10 SDVSLRYGK----TVALDRITLDVPAGLTTGLIGPDGVGKSSLLALASGARALQTGGVDaLGGDMRSRRHRERVCRRIAY 85
Cdd:COG1124 5 RNLSVSYGQggrrVPVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVT-FDGRPVTRRRRKAFRRRVQM 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 86 MPQGLGKNLYPTLSVEENLQFFARLFGHDagERRRRIDALTQSTGLFP-FLSRPAGKLSGGMKQKLGLCCALIHDPDLLI 164
Cdd:COG1124 84 VFQDPYASLHPRHTVDRILAEPLRIHGLP--DREERIAELLEQVGLPPsFLDRYPHQLSGGQRQRVAIARALILEPELLL 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 165 LDEPTTGVDPLARAQFWDLIARIRDERpTMSVIVATAYMDEAQRF-DWLIAMDAGRVLATGAPAELLART 233
Cdd:COG1124 162 LDEPTSALDVSVQAEILNLLKDLREER-GLTYLFVSHDLAVVAHLcDRVAVMQNGRIVEELTVADLLAGP 230
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
280-475 |
8.37e-25 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 102.70 E-value: 8.37e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 280 RFGDFTAVDHVSFRIRRGEIFGFLGSNGCGKSTTMKMLTGLLPATEGTAqlfgkevdpkDINTRRRVGYMSQAFSLYSEL 359
Cdd:NF040873 1 GYGGRPVLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTV----------RRAGGARVAYVPQRSEVPDSL 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 360 --TVRQNLVL----HARLFGVPAAEIDARVDEMARRFGLADIYGMLPDSLPLGMRQRLSLAVAMVHKPELLILDEPTSGV 433
Cdd:NF040873 71 plTVRDLVAMgrwaRRGLWRRLTRDDRAAVDDALERVGLADLAGRQLGELSGGQRQRALLAQGLAQEADLLLLDEPTTGL 150
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 505416896 434 DPVARDSFWQLMIDLARRDlVTIFISTHFMNEAQRCDRISLM 475
Cdd:NF040873 151 DAESRERIIALLAEEHARG-ATVVVVTHDLELVRRADPCVLL 191
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
271-489 |
8.41e-25 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 105.27 E-value: 8.41e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 271 AIEARGLTMRFGDF--TAVDHVSFRIRRGEIFGFLGSNGCGKSTTMKMLTGLL---PATEGTAQLFGKEVDPKDI-NTRR 344
Cdd:PRK13640 5 IVEFKHVSFTYPDSkkPALNDISFSIPRGSWTALIGHNGSGKSTISKLINGLLlpdDNPNSKITVDGITLTAKTVwDIRE 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 345 RVGYMSQ-AFSLYSELTVRQNLVLHARLFGVPAAEIDARVDEMARRFGLADIYGMLPDSLPLGMRQRLSLAVAMVHKPEL 423
Cdd:PRK13640 85 KVGIVFQnPDNQFVGATVGDDVAFGLENRAVPRPEMIKIVRDVLADVGMLDYIDSEPANLSGGQKQRVAIAGILAVEPKI 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 505416896 424 LILDEPTSGVDPVARDSFWQLMIDLARRDLVTIFISTHFMNEAQRCDRISLMHAGRVLASDSPAEL 489
Cdd:PRK13640 165 IILDESTSMLDPAGKEQILKLIRKLKKKNNLTVISITHDIDEANMADQVLVLDDGKLLAQGSPVEI 230
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
275-489 |
8.75e-25 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 107.42 E-value: 8.75e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 275 RGLTMRFGDFTAVDHVSFRIRRGEIFGFLGSNGCGKSTTMKMLTGLLPATEGTAQLFGK---EVDPKDintrRRVGYMSQ 351
Cdd:PRK11000 7 RNVTKAYGDVVISKDINLDIHEGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLFIGEKrmnDVPPAE----RGVGMVFQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 352 AFSLYSELTVRQNLVLHARLFGVPAAEIDARVDEMARRFGLADIYGMLPDSLPLGMRQRLSLAVAMVHKPELLILDEPTS 431
Cdd:PRK11000 83 SYALYPHLSVAENMSFGLKLAGAKKEEINQRVNQVAEVLQLAHLLDRKPKALSGGQRQRVAIGRTLVAEPSVFLLDEPLS 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 505416896 432 GVDPVARdsfWQLMIDLAR---RDLVTIFISTHFMNEAQR-CDRISLMHAGRVLASDSPAEL 489
Cdd:PRK11000 163 NLDAALR---VQMRIEISRlhkRLGRTMIYVTHDQVEAMTlADKIVVLDAGRVAQVGKPLEL 221
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
286-490 |
8.77e-25 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 108.20 E-value: 8.77e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 286 AVDHVSFRIRRGEIFGFLGSNGCGKSTTMKMLTGLLPATEGTAQLFGkeVDPKDINT-------RRRVGYMSQAFSLYSE 358
Cdd:PRK10070 43 GVKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDG--VDIAKISDaelrevrRKKIAMVFQSFALMPH 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 359 LTVRQNLVLHARLFGVPAAEIDARVDEMARRFGLADIYGMLPDSLPLGMRQRLSLAVAMVHKPELLILDEPTSGVDPVAR 438
Cdd:PRK10070 121 MTVLDNTAFGMELAGINAEERREKALDALRQVGLENYAHSYPDELSGGMRQRVGLARALAINPDILLMDEAFSALDPLIR 200
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 505416896 439 DSFWQLMIDLARRDLVTIFISTHFMNEAQRC-DRISLMHAGRVLASDSPAELV 490
Cdd:PRK10070 201 TEMQDELVKLQAKHQRTIVFISHDLDEAMRIgDRIAIMQNGEVVQVGTPDEIL 253
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
8-246 |
1.12e-24 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 103.68 E-value: 1.12e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 8 RFSDVSLRYGKTVAldRITLDVPAGLTTGLIGPDGVGKSSLLALASGARALQTGGVDALGGDMRSRRhrervcrrIAYMP 87
Cdd:COG3840 3 RLDDLTYRYGDFPL--RFDLTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILWNGQDLTALP--------PAERP 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 88 -----QGlgKNLYPTLSVEENLqffarLFGHDAG-----ERRRRIDALTQSTGLFPFLSRPAGKLSGGMKQKLGLCCALI 157
Cdd:COG3840 73 vsmlfQE--NNLFPHLTVAQNI-----GLGLRPGlkltaEQRAQVEQALERVGLAGLLDRLPGQLSGGQRQRVALARCLV 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 158 HDPDLLILDEPTTGVDPLARAQFWDLIARIRDERPtMSVIVATAYMDEAQRF-DWLIAMDAGRVLATGAPAELLARTGcd 236
Cdd:COG3840 146 RKRPILLLDEPFSALDPALRQEMLDLVDELCRERG-LTVLMVTHDPEDAARIaDRVLLVADGRIAADGPTAALLDGEP-- 222
|
250
....*....|
gi 505416896 237 slEAAFIALL 246
Cdd:COG3840 223 --PPALAAYL 230
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
7-234 |
1.32e-24 |
|
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease components [Energy production and conversion, Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 444011 [Multi-domain] Cd Length: 569 Bit Score: 109.47 E-value: 1.32e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 7 VRFSDVSLRY--GKTVALDRITLDVPAGLTTGLIGPDGVGKSSLLALASGARALQTGGVdALGGDMRSRRHRERVCRRIA 84
Cdd:COG4987 334 LELEDVSFRYpgAGRPVLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFLDPQSGSI-TLGGVDLRDLDEDDLRRRIA 412
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 85 YMPQGlgknlyPTL---SVEENLqffaRLFGHDAGERRRRiDALTQsTGLFPFL-SRPAG----------KLSGGMKQKL 150
Cdd:COG4987 413 VVPQR------PHLfdtTLRENL----RLARPDATDEELW-AALER-VGLGDWLaALPDGldtwlgeggrRLSGGERRRL 480
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 151 GLCCALIHDPDLLILDEPTTGVDPLARAQFWDLIARIRDERptmSVIVATAYMDEAQRFDWLIAMDAGRVLATGAPAELL 230
Cdd:COG4987 481 ALARALLRDAPILLLDEPTEGLDAATEQALLADLLEALAGR---TVLLITHRLAGLERMDRILVLEDGRIVEQGTHEELL 557
|
....
gi 505416896 231 ARTG 234
Cdd:COG4987 558 AQNG 561
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
272-489 |
2.85e-24 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 103.73 E-value: 2.85e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 272 IEARGLTMRF-GDFTAVDHVSFRIRRGEIFGFLGSNGCGKSTTMKMLTGLLPATEGTAQLFGKEVDPKDIN-TRRRVGYM 349
Cdd:PRK13652 4 IETRDLCYSYsGSKEALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIRGEPITKENIReVRKFVGLV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 350 -----SQAFSLyselTVRQNLVLHARLFGVPAAEIDARVDEMARRFGLADIYGMLPDSLPLGMRQRLSLAVAMVHKPELL 424
Cdd:PRK13652 84 fqnpdDQIFSP----TVEQDIAFGPINLGLDEETVAHRVSSALHMLGLEELRDRVPHHLSGGEKKRVAIAGVIAMEPQVL 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 505416896 425 ILDEPTSGVDPVARDSFWQLMIDLARRDLVTIFISTHFMN-EAQRCDRISLMHAGRVLASDSPAEL 489
Cdd:PRK13652 160 VLDEPTAGLDPQGVKELIDFLNDLPETYGMTVIFSTHQLDlVPEMADYIYVMDKGRIVAYGTVEEI 225
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
11-232 |
3.00e-24 |
|
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: 105.58 E-value: 3.00e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 11 DVSLRYGKTvALDrITLDVPAGLTTGLIGPDGVGKSSLLALASGARALQTGGV---DALGGDMRSRRHRERVCRRIAYMP 87
Cdd:TIGR02142 4 RFSKRLGDF-SLD-ADFTLPGQGVTAIFGRSGSGKTTLIRLIAGLTRPDEGEIvlnGRTLFDSRKGIFLPPEKRRIGYVF 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 88 QGlgKNLYPTLSVEENLQFFARLfgHDAGERRRRIDALTQSTGLFPFLSRPAGKLSGGMKQKLGLCCALIHDPDLLILDE 167
Cdd:TIGR02142 82 QE--ARLFPHLSVRGNLRYGMKR--ARPSERRISFERVIELLGIGHLLGRLPGRLSGGEKQRVAIGRALLSSPRLLLMDE 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 505416896 168 PTTGVDPLARAQFWDLIARIRDERpTMSVIVATAYMDEAQRF-DWLIAMDAGRVLATGAPAELLAR 232
Cdd:TIGR02142 158 PLAALDDPRKYEILPYLERLHAEF-GIPILYVSHSLQEVLRLaDRVVVLEDGRVAAAGPIAEVWAS 222
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
6-228 |
3.16e-24 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 102.05 E-value: 3.16e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 6 VVRFSDVSLRY-GKTVALDRITLDVPAGLTTGLIGPDGVGKSSLLALASGARALQTGGVDALGGDMRSRRHRErvcrrIA 84
Cdd:COG2884 1 MIRFENVSKRYpGGREALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLVNGQDLSRLKRRE-----IP 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 85 YMPQGLG------KnLYPTLSVEENLQFFARLFGHDAGERRRRIDALTQSTGLFPFLSRPAGKLSGGMKQKLGLCCALIH 158
Cdd:COG2884 76 YLRRRIGvvfqdfR-LLPDRTVYENVALPLRVTGKSRKEIRRRVREVLDLVGLSDKAKALPHELSGGEQQRVAIARALVN 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 505416896 159 DPDLLILDEPTTGVDPLARAQFWDLIARIRDERPTmsVIVATAYMDEAQRFDW-LIAMDAGRVLATGAPAE 228
Cdd:COG2884 155 RPELLLADEPTGNLDPETSWEIMELLEEINRRGTT--VLIATHDLELVDRMPKrVLELEDGRLVRDEARGV 223
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
135-481 |
4.50e-24 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 108.40 E-value: 4.50e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 135 LSRPAGKLSGGMKQKLGLCCALIHDPDLLILDEPTTGVDPLARAQFWDLIARIRDERpTMSVIVATAYMD-EAQRFDWLI 213
Cdd:PRK10261 162 LSRYPHQLSGGMRQRVMIAMALSCRPAVLIADEPTTALDVTIQAQILQLIKVLQKEM-SMGVIFITHDMGvVAEIADRVL 240
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 214 AMDAGRVLATGApAELLARTGCDSLEAAFIALLPE-NERRGH------------KPVKIEPlraDARAGTAIEA------ 274
Cdd:PRK10261 241 VMYQGEAVETGS-VEQIFHAPQHPYTRALLAAVPQlGAMKGLdyprrfplisleHPAKQEP---PIEQDTVVDGepilqv 316
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 275 RGLTMRFG-----------DFTAVDHVSFRIRRGEIFGFLGSNGCGKSTTMKMLTGLLPATEGTAQLFGKEVDP----KD 339
Cdd:PRK10261 317 RNLVTRFPlrsgllnrvtrEVHAVEKVSFDLWPGETLSLVGESGSGKSTTGRALLRLVESQGGEIIFNGQRIDTlspgKL 396
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 340 INTRRRVGYMSQafSLYSELTVRQN--------LVLHARLFGVPAAeidARVDEMARRFGLADIYGM-LPDSLPLGMRQR 410
Cdd:PRK10261 397 QALRRDIQFIFQ--DPYASLDPRQTvgdsimepLRVHGLLPGKAAA---ARVAWLLERVGLLPEHAWrYPHEFSGGQRQR 471
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 505416896 411 LSLAVAMVHKPELLILDEPTSGVDPVARDSFWQLMIDLARR-DLVTIFIStHFMNEAQRCD-RISLMHAGRVL 481
Cdd:PRK10261 472 ICIARALALNPKVIIADEAVSALDVSIRGQIINLLLDLQRDfGIAYLFIS-HDMAVVERIShRVAVMYLGQIV 543
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
7-231 |
4.51e-24 |
|
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: 101.85 E-value: 4.51e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 7 VRFSDVSLRYGKTVALDRITLDVPAGLTTGLIGPDGVGKSSLLALASGARALQTGGVDALGGDMRSRRHRERVCRRIAYM 86
Cdd:cd03218 1 LRAENLSKRYGKRKVVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDGQDITKLPMHKRARLGIGYL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 87 PQGlgKNLYPTLSVEENLQFFARLFGHDAGERRRRIDALTQSTGLFPFLSRPAGKLSGGMKQKLGLCCALIHDPDLLILD 166
Cdd:cd03218 81 PQE--ASIFRKLTVEENILAVLEIRGLSKKEREEKLEELLEEFHITHLRKSKASSLSGGERRRVEIARALATNPKFLLLD 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 505416896 167 EPTTGVDPLARAQFWDLIARIRDE-----------RPTMSvIVATAYMdeaqrfdwliaMDAGRVLATGAPAELLA 231
Cdd:cd03218 159 EPFAGVDPIAVQDIQKIIKILKDRgigvlitdhnvRETLS-ITDRAYI-----------IYEGKVLAEGTPEEIAA 222
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
7-219 |
4.86e-24 |
|
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: 99.76 E-value: 4.86e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 7 VRFSDVSLRYG--KTVALDRITLDVPAGLTTGLIGPDGVGKSSLLALASGARALQTGGVdALGGDMRSRRHRERVCRRIA 84
Cdd:cd03228 1 IEFKNVSFSYPgrPKPVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEI-LIDGVDLRDLDLESLRKNIA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 85 YMPQGlgknlyPTL---SVEENLqffarlfghdagerrrridaltqstglfpflsrpagkLSGGMKQKLGLCCALIHDPD 161
Cdd:cd03228 80 YVPQD------PFLfsgTIRENI-------------------------------------LSGGQRQRIAIARALLRDPP 116
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 505416896 162 LLILDEPTTGVDPLARAQFWDLIARIRDERptmSVIVATAYMDEAQRFDWLIAMDAGR 219
Cdd:cd03228 117 ILILDEATSALDPETEALILEALRALAKGK---TVIVIAHRLSTIRDADRIIVLDDGR 171
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
271-491 |
4.96e-24 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 102.89 E-value: 4.96e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 271 AIEARGLTMRFGDFT-AVDHVSFRIRRGEIFGFLGSNGCGKSTTMKMLTGLLPATEGTAQLFGKEVDPKDIN-TRRRVGY 348
Cdd:PRK13647 4 IIEVEDLHFRYKDGTkALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGREVNAENEKwVRSKVGL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 349 M-----SQAFSLyselTVRQNLVLHARLFGVPAAEIDARVDEMARRFGLADIYGMLPDSLPLGMRQRLSLAVAMVHKPEL 423
Cdd:PRK13647 84 VfqdpdDQVFSS----TVWDDVAFGPVNMGLDKDEVERRVEEALKAVRMWDFRDKPPYHLSYGQKKRVAIAGVLAMDPDV 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 505416896 424 LILDEPTSGVDPVARDSFWQLMIDLARRDlVTIFISTHFMN-EAQRCDRISLMHAGRVLASDSPAELVR 491
Cdd:PRK13647 160 IVLDEPMAYLDPRGQETLMEILDRLHNQG-KTVIVATHDVDlAAEWADQVIVLKEGRVLAEGDKSLLTD 227
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
15-224 |
5.02e-24 |
|
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: 102.03 E-value: 5.02e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 15 RYGKTVALDRITLDVPAGLTTGLIGPDGVGKSSLLALASGARALQTGGVDALGgdMRSRRHRERVCRRIAYMpQGLGKNL 94
Cdd:cd03267 30 KYREVEALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRVAG--LVPWKRRKKFLRRIGVV-FGQKTQL 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 95 YPTLSVEENLQFFARLFGHDAGERRRRIDALTQSTGLFPFLSRPAGKLSGGMKQKLGLCCALIHDPDLLILDEPTTGVDP 174
Cdd:cd03267 107 WWDLPVIDSFYLLAAIYDLPPARFKKRLDELSELLDLEELLDTPVRQLSLGQRMRAEIAAALLHEPEILFLDEPTIGLDV 186
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 505416896 175 LARAQFWDLIARIRDERPTmSVIVATAYMDEAQRF-DWLIAMDAGRVLATG 224
Cdd:cd03267 187 VAQENIRNFLKEYNRERGT-TVLLTSHYMKDIEALaRRVLVIDKGRLLYDG 236
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
272-494 |
5.95e-24 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 102.89 E-value: 5.95e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 272 IEARGLTMRFG---DFTAVDHVSFRIRRGEIFGFLGSNGCGKSTTMKMLTGLLPATEGTAQLFGKEVDPKDI-NTRRRVG 347
Cdd:PRK13650 5 IEVKNLTFKYKedqEKYTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIIDGDLLTEENVwDIRHKIG 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 348 YMSQ-AFSLYSELTVRQNLVLHARLFGVPAAEIDARVDEMARRFGLADIYGMLPDSLPLGMRQRLSLAVAMVHKPELLIL 426
Cdd:PRK13650 85 MVFQnPDNQFVGATVEDDVAFGLENKGIPHEEMKERVNEALELVGMQDFKEREPARLSGGQKQRVAIAGAVAMRPKIIIL 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 505416896 427 DEPTSGVDPVARDSFWQLMIDLARRDLVTIFISTHFMNEAQRCDRISLMHAGRVLASDSPAELVrARG 494
Cdd:PRK13650 165 DEATSMLDPEGRLELIKTIKGIRDDYQMTVISITHDLDEVALSDRVLVMKNGQVESTSTPRELF-SRG 231
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
272-502 |
6.03e-24 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 102.08 E-value: 6.03e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 272 IEARGLTMRFGDFTAVDHVSFRIRRGEIFGFLGSNGCGKSTTMKMLTGLLPATEGTAQLFGKEVdpKDINTR---RRVGY 348
Cdd:COG4604 2 IEIKNVSKRYGGKVVLDDVSLTIPKGGITALIGPNGAGKSTLLSMISRLLPPDSGEVLVDGLDV--ATTPSRelaKRLAI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 349 MSQAFSLYSELTVRQnLVL-----HARlfGVPAAEIDARVDEMARRFGLADIYGMLPDSLPLGMRQRlslA-VAMV--HK 420
Cdd:COG4604 80 LRQENHINSRLTVRE-LVAfgrfpYSK--GRLTAEDREIIDEAIAYLDLEDLADRYLDELSGGQRQR---AfIAMVlaQD 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 421 PELLILDEPTSGVDPV-ARdsfwQLMIDLarRDLV-----TIFISTHFMNEAQR-CDRISLMHAGRVLASDSPAELVRar 493
Cdd:COG4604 154 TDYVLLDEPLNNLDMKhSV----QMMKLL--RRLAdelgkTVVIVLHDINFASCyADHIVAMKDGRVVAQGTPEEIIT-- 225
|
....*....
gi 505416896 494 gAATLEDAF 502
Cdd:COG4604 226 -PEVLSDIY 233
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
272-507 |
6.21e-24 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 105.31 E-value: 6.21e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 272 IEARGLTMRFGDFTAVDHVSFRIRRGEIFGFLGSNGCGKSTTMKMLTGLLPATEGTAQLFGKEVDPKDINT-RRRVGYMS 350
Cdd:PRK09536 4 IDVSDLSVEFGDTTVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGDDVEALSARAaSRRVASVP 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 351 QAFSLYSELTVRQNLVL----HARLFGVPAAEIDARVDEMARRFGLADIYGMLPDSLPLGMRQRLSLAVAMVHKPELLIL 426
Cdd:PRK09536 84 QDTSLSFEFDVRQVVEMgrtpHRSRFDTWTETDRAAVERAMERTGVAQFADRPVTSLSGGERQRVLLARALAQATPVLLL 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 427 DEPTSGVDPVARDSFWQLMIDLArRDLVTIFISTHFMNEAQR-CDRISLMHAGRVLASDSPAELVRargAATLEDAFIGY 505
Cdd:PRK09536 164 DEPTASLDINHQVRTLELVRRLV-DDGKTAVAAIHDLDLAARyCDELVLLADGRVRAAGPPADVLT---ADTLRAAFDAR 239
|
..
gi 505416896 506 LV 507
Cdd:PRK09536 240 TA 241
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
21-226 |
6.57e-24 |
|
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: 109.33 E-value: 6.57e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 21 ALDRITLDVPAGLTTGLIGPDGVGKSSLLALASGARALQTGGVDALGGDMRSRRHRERVCrrIAYMPQGlgKNLYPTLSV 100
Cdd:TIGR01257 945 AVDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGKDIETNLDAVRQS--LGMCPQH--NILFHHLTV 1020
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 101 EENLQFFARLFGHDAGERRRRIDALTQSTGLFPFLSRPAGKLSGGMKQKLGLCCALIHDPDLLILDEPTTGVDPLARAQF 180
Cdd:TIGR01257 1021 AEHILFYAQLKGRSWEEAQLEMEAMLEDTGLHHKRNEEAQDLSGGMQRKLSVAIAFVGDAKVVVLDEPTSGVDPYSRRSI 1100
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 505416896 181 WDLIARIRDERptmSVIVATAYMDEAQRF-DWLIAMDAGRVLATGAP 226
Cdd:TIGR01257 1101 WDLLLKYRSGR---TIIMSTHHMDEADLLgDRIAIISQGRLYCSGTP 1144
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
274-490 |
7.85e-24 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 101.51 E-value: 7.85e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 274 ARGLTMRFGDFTAVDHVSFRIRRGEIFGFLGSNGCGKSTTMKMLTGLLPATEGTAQLFGKEVD--PKDINTRRRVGYMSQ 351
Cdd:PRK10895 6 AKNLAKAYKGRRVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEDISllPLHARARRGIGYLPQ 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 352 AFSLYSELTVRQNL--VLHARLfGVPAAEIDARVDEMARRFGLADIYGMLPDSLPLGMRQRLSLAVAMVHKPELLILDEP 429
Cdd:PRK10895 86 EASIFRRLSVYDNLmaVLQIRD-DLSAEQREDRANELMEEFHIEHLRDSMGQSLSGGERRRVEIARALAANPKFILLDEP 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 505416896 430 TSGVDPVARDSFwQLMIDLARRDLVTIFISTHFMNEA-QRCDRISLMHAGRVLASDSPAELV 490
Cdd:PRK10895 165 FAGVDPISVIDI-KRIIEHLRDSGLGVLITDHNVRETlAVCERAYIVSQGHLIAHGTPTEIL 225
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
271-489 |
7.93e-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: 104.41 E-value: 7.93e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 271 AIEARgLTMRFGDFTaVDhVSFRIRRGEIFGFLGSNGCGKSTTMKMLTGLLPATEGTAQLFGkEV---DPKDINT---RR 344
Cdd:COG4148 2 MLEVD-FRLRRGGFT-LD-VDFTLPGRGVTALFGPSGSGKTTLLRAIAGLERPDSGRIRLGG-EVlqdSARGIFLpphRR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 345 RVGYMSQAFSLYSELTVRQNLvlharLFG---VPAAEIDARVDEMARRFGLADIYGMLPDSLPLGMRQRLSLAVAMVHKP 421
Cdd:COG4148 78 RIGYVFQEARLFPHLSVRGNL-----LYGrkrAPRAERRISFDEVVELLGIGHLLDRRPATLSGGERQRVAIGRALLSSP 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 505416896 422 ELLILDEPTSGVDPVARDsfwQLM--IDLARRDL-VTIFISTHFMNEAQR-CDRISLMHAGRVLASDSPAEL 489
Cdd:COG4148 153 RLLLMDEPLAALDLARKA---EILpyLERLRDELdIPILYVSHSLDEVARlADHVVLLEQGRVVASGPLAEV 221
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
269-489 |
8.45e-24 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 102.60 E-value: 8.45e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 269 GTAIEARGLtmrfgdftavDHVSFRIRRGEIFGFLGSNGCGKSTTMKMLTGLLPATEGTAQLFGKEVDPKDINT-----R 343
Cdd:PRK13641 15 GTPMEKKGL----------DNISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITIAGYHITPETGNKnlkklR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 344 RRVGYM-----SQAFslysELTVRQNLVLHARLFGVPAAEIDARVDEMARRFGLA-DIYGMLPDSLPLGMRQRLSLAVAM 417
Cdd:PRK13641 85 KKVSLVfqfpeAQLF----ENTVLKDVEFGPKNFGFSEDEAKEKALKWLKKVGLSeDLISKSPFELSGGQMRRVAIAGVM 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 505416896 418 VHKPELLILDEPTSGVDPVARDSFWQLMIDLARRDLVTIFIsTHFMNE-AQRCDRISLMHAGRVLASDSPAEL 489
Cdd:PRK13641 161 AYEPEILCLDEPAAGLDPEGRKEMMQLFKDYQKAGHTVILV-THNMDDvAEYADDVLVLEHGKLIKHASPKEI 232
|
|
| galliderm_ABC |
TIGR03740 |
gallidermin-class lantibiotic protection ABC transporter, ATP-binding subunit; Model TIGR03731 ... |
11-207 |
1.19e-23 |
|
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: 100.55 E-value: 1.19e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 11 DVSLRYGKTVALDRITLDVPAGLTTGLIGPDGVGKSSLLALASGArALQTGGVDALGGDMRSRRHRERVCRRIAYMPqgl 90
Cdd:TIGR03740 5 NLSKRFGKQTAVNNISLTVPKNSVYGLLGPNGAGKSTLLKMITGI-LRPTSGEIIFDGHPWTRKDLHKIGSLIESPP--- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 91 gknLYPTLSVEENLQFFARLFGHDagerRRRIDALTQSTGLFPFLSRPAGKLSGGMKQKLGLCCALIHDPDLLILDEPTT 170
Cdd:TIGR03740 81 ---LYENLTARENLKVHTTLLGLP----DSRIDEVLNIVDLTNTGKKKAKQFSLGMKQRLGIAIALLNHPKLLILDEPTN 153
|
170 180 190
....*....|....*....|....*....|....*..
gi 505416896 171 GVDPLARAQFWDLIARIRDErpTMSVIVATAYMDEAQ 207
Cdd:TIGR03740 154 GLDPIGIQELRELIRSFPEQ--GITVILSSHILSEVQ 188
|
|
| LolD_lipo_ex |
TIGR02211 |
lipoprotein releasing system, ATP-binding protein; This model represents LolD, a member of the ... |
272-480 |
1.38e-23 |
|
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: 100.12 E-value: 1.38e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 272 IEARGLTMRF--GDFT--AVDHVSFRIRRGEIFGFLGSNGCGKSTTMKMLTGLLPATEGTAQLFGKEVDPKDINTR---- 343
Cdd:TIGR02211 2 LKCENLGKRYqeGKLDtrVLKGVSLSIGKGEIVAIVGSSGSGKSTLLHLLGGLDNPTSGEVLFNGQSLSKLSSNERaklr 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 344 -RRVGYMSQAFSLYSELTVRQNLVLHARLFGVPAAEIDARVDEMARRFGLADIYGMLPDSLPLGMRQRLSLAVAMVHKPE 422
Cdd:TIGR02211 82 nKKLGFIYQFHHLLPDFTALENVAMPLLIGKKSVKEAKERAYEMLEKVGLEHRINHRPSELSGGERQRVAIARALVNQPS 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 505416896 423 LLILDEPTSGVDPVARDSFWQLMIDLaRRDLVTIF-ISTHFMNEAQRCDRISLMHAGRV 480
Cdd:TIGR02211 162 LVLADEPTGNLDNNNAKIIFDLMLEL-NRELNTSFlVVTHDLELAKKLDRVLEMKDGQL 219
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
7-234 |
2.38e-23 |
|
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: 106.46 E-value: 2.38e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 7 VRFSDVSLRYG--KTVALDRITLDVPAGLTTGLIGPDGVGKSSLLALASGARALQTGGVdALGG---------DMRSRrh 75
Cdd:COG2274 474 IELENVSFRYPgdSPPVLDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEPTSGRI-LIDGidlrqidpaSLRRQ-- 550
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 76 rervcrrIAYMPQGlgknlyPTL---SVEENLQFFARLFGHDagerrrRIDALTQSTGLFPFLSR-PAG----------K 141
Cdd:COG2274 551 -------IGVVLQD------VFLfsgTIRENITLGDPDATDE------EIIEAARLAGLHDFIEAlPMGydtvvgeggsN 611
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 142 LSGGMKQKLGLCCALIHDPDLLILDEPTTGVDPLARAQFWDLIARIRDERptmSVIVATAYMDEAQRFDWLIAMDAGRVL 221
Cdd:COG2274 612 LSGGQRQRLAIARALLRNPRILILDEATSALDAETEAIILENLRRLLKGR---TVIIIAHRLSTIRLADRIIVLDKGRIV 688
|
250
....*....|...
gi 505416896 222 ATGAPAELLARTG 234
Cdd:COG2274 689 EDGTHEELLARKG 701
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
290-481 |
3.21e-23 |
|
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette superfamily; ABCG transporters are involved in eye pigment (EP) precursor transport, regulation of lipid-trafficking mechanisms, and pleiotropic drug resistance (DR). DR is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. Compared to other members of the ABC transporter subfamilies, the ABCG transporter family is composed of proteins that have an ATP-binding cassette domain at the N-terminus and a TM (transmembrane) domain at the C-terminus.
Pssm-ID: 213180 [Multi-domain] Cd Length: 194 Bit Score: 98.39 E-value: 3.21e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 290 VSFRIRRGEIFGFLGSNGCGKSTTMKMLTGLL--PATEGTAQLFGKEVDPKDIntRRRVGYMSQAFSLYSELTVRQNLVL 367
Cdd:cd03213 28 VSGKAKPGELTAIMGPSGAGKSTLLNALAGRRtgLGVSGEVLINGRPLDKRSF--RKIIGYVPQDDILHPTLTVRETLMF 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 368 HARLFGVPAAEidarvdemarrfgladiygmlpdslplgmRQRLSLAVAMVHKPELLILDEPTSGVDPVARDSFWQLMID 447
Cdd:cd03213 106 AAKLRGLSGGE-----------------------------RKRVSIALELVSNPSLLFLDEPTSGLDSSSALQVMSLLRR 156
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 505416896 448 LArRDLVTIFISTH------FmneaQRCDRISLMHAGRVL 481
Cdd:cd03213 157 LA-DTGRTIICSIHqpsseiF----ELFDKLLLLSQGRVI 191
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
11-232 |
3.65e-23 |
|
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: 102.49 E-value: 3.65e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 11 DVSLRYGKTvALDrITLDVPAGLTTGLIGPDGVGKSSLLALASGARALQTGGVdALGG----DMRSRRHRERVCRRIAYM 86
Cdd:COG4148 6 DFRLRRGGF-TLD-VDFTLPGRGVTALFGPSGSGKTTLLRAIAGLERPDSGRI-RLGGevlqDSARGIFLPPHRRRIGYV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 87 PQGlgKNLYPTLSVEENLqffarLFGH---DAGERRRRIDALTQSTGLFPFLSRPAGKLSGGMKQKLGLCCALIHDPDLL 163
Cdd:COG4148 83 FQE--ARLFPHLSVRGNL-----LYGRkraPRAERRISFDEVVELLGIGHLLDRRPATLSGGERQRVAIGRALLSSPRLL 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 164 ILDEPTTGVDPLARAQFWDLIARIRDERpTMSVIVATAYMDEAQRF-DWLIAMDAGRVLATGAPAELLAR 232
Cdd:COG4148 156 LMDEPLAALDLARKAEILPYLERLRDEL-DIPILYVSHSLDEVARLaDHVVLLEQGRVVASGPLAEVLSR 224
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
272-489 |
3.75e-23 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 104.63 E-value: 3.75e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 272 IEARGLTMRFGDFTAVDHVSFRIRRGEIFGFLGSNGCGKSTTMKMLTGLLP--ATEGTAQLFGKEVDPKDINTRRRVG-- 347
Cdd:PRK13549 6 LEMKNITKTFGGVKALDNVSLKVRAGEIVSLCGENGAGKSTLMKVLSGVYPhgTYEGEIIFEGEELQASNIRDTERAGia 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 348 YMSQAFSLYSELTVRQNLVLHARLfgVPAAEID-----ARVDEMARRFGLaDIYGMLPDS-LPLGMRQRLSLAVAMVHKP 421
Cdd:PRK13549 86 IIHQELALVKELSVLENIFLGNEI--TPGGIMDydamyLRAQKLLAQLKL-DINPATPVGnLGLGQQQLVEIAKALNKQA 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 505416896 422 ELLILDEPTSGVDPVARDSFWQLMIDLARRDLVTIFIStHFMNEAQR-CDRISLMHAGRVLASDSPAEL 489
Cdd:PRK13549 163 RLLILDEPTASLTESETAVLLDIIRDLKAHGIACIYIS-HKLNEVKAiSDTICVIRDGRHIGTRPAAGM 230
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
25-224 |
3.81e-23 |
|
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: 98.52 E-value: 3.81e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 25 ITLDVPAGLTtGLIGPDGVGKSSLLALASGARALqTGGVDALGG----DMRSRRHRERVCRRIAYMPQGLGknLYPTLSV 100
Cdd:cd03297 17 IDFDLNEEVT-GIFGASGAGKSTLLRCIAGLEKP-DGGTIVLNGtvlfDSRKKINLPPQQRKIGLVFQQYA--LFPHLNV 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 101 EENLQFFARlfGHDAGERRRRIDALTQSTGLFPFLSRPAGKLSGGMKQKLGLCCALIHDPDLLILDEPTTGVDPLARAQF 180
Cdd:cd03297 93 RENLAFGLK--RKRNREDRISVDELLDLLGLDHLLNRYPAQLSGGEKQRVALARALAAQPELLLLDEPFSALDRALRLQL 170
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 505416896 181 WDLIARIRdERPTMSVIVATAYMDEAQRF-DWLIAMDAGRVLATG 224
Cdd:cd03297 171 LPELKQIK-KNLNIPVIFVTHDLSEAEYLaDRIVVMEDGRLQYIG 214
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
13-230 |
5.76e-23 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 99.32 E-value: 5.76e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 13 SLRYGKTVALDRITLDVPAGLTTGLIGPDGVGKSSLL-ALAsgaRAL--QTGGVdALGGDMRSRRHRERVCRRIAYMPQG 89
Cdd:PRK11231 9 TVGYGTKRILNDLSLSLPTGKITALIGPNGCGKSTLLkCFA---RLLtpQSGTV-FLGDKPISMLSSRQLARRLALLPQH 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 90 LgknLYPT-LSVEE--------NLQFFARLFGHDagerRRRIDALTQSTGLFPFLSRPAGKLSGGMKQKLGLCCALIHDP 160
Cdd:PRK11231 85 H---LTPEgITVRElvaygrspWLSLWGRLSAED----NARVNQAMEQTRINHLADRRLTDLSGGQRQRAFLAMVLAQDT 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 505416896 161 DLLILDEPTTGVDPLARAQFWDLIARIRDERPTmsVIVATAYMDEAQRF-DWLIAMDAGRVLATGAPAELL 230
Cdd:PRK11231 158 PVVLLDEPTTYLDINHQVELMRLMRELNTQGKT--VVTVLHDLNQASRYcDHLVVLANGHVMAQGTPEEVM 226
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
267-489 |
6.01e-23 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 99.82 E-value: 6.01e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 267 RAGTAIEARGLtmrFGdftavdhVSFRIRRGEIFGFLGSNGCGKSTTMKMLTGLLPATEGTAQLFGKEVDP----KDI-N 341
Cdd:PRK13649 13 QAGTPFEGRAL---FD-------VNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDDTLITStsknKDIkQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 342 TRRRVGYM-----SQAFslysELTVRQNLVLHARLFGVPAAEIDARVDEMARRFGLA-DIYGMLPDSLPLGMRQRLSLAV 415
Cdd:PRK13649 83 IRKKVGLVfqfpeSQLF----EETVLKDVAFGPQNFGVSQEEAEALAREKLALVGISeSLFEKNPFELSGGQMRRVAIAG 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 505416896 416 AMVHKPELLILDEPTSGVDPVARDSFWQLMIDLaRRDLVTIFISTHFMNE-AQRCDRISLMHAGRVLASDSPAEL 489
Cdd:PRK13649 159 ILAMEPKILVLDEPTAGLDPKGRKELMTLFKKL-HQSGMTIVLVTHLMDDvANYADFVYVLEKGKLVLSGKPKDI 232
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
287-478 |
1.03e-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: 97.92 E-value: 1.03e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 287 VDHVSFRIRRGEIFGFLGSNGCGKSTTMKMLTGLLPATEGTAQLFGKEVDpkDINTRRRVGYmsQAFSLYSELTVRQNLV 366
Cdd:TIGR01184 1 LKGVNLTIQQGEFISLIGHSGCGKSTLLNLISGLAQPTSGGVILEGKQIT--EPGPDRMVVF--QNYSLLPWLTVRENIA 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 367 L--HARLFGVPAAEIDARVDEMARRFGLADIYGMLPDSLPLGMRQRLSLAVAMVHKPELLILDEPTSGVDPVARDSFWQL 444
Cdd:TIGR01184 77 LavDRVLPDLSKSERRAIVEEHIALVGLTEAADKRPGQLSGGMKQRVAIARALSIRPKVLLLDEPFGALDALTRGNLQEE 156
|
170 180 190
....*....|....*....|....*....|....*
gi 505416896 445 MIDLARRDLVTIFISTHFMNEAQ-RCDRISLMHAG 478
Cdd:TIGR01184 157 LMQIWEEHRVTVLMVTHDVDEALlLSDRVVMLTNG 191
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
289-482 |
1.16e-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: 97.18 E-value: 1.16e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 289 HVSFRIRRGEIFGFLGSNGCGKSTTMKMLTGLLPATEGTAQLFGKEVDPKDInTRRRVGYMSQAFSLYSELTVRQNLVLh 368
Cdd:cd03298 16 HFDLTFAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLINGVDVTAAPP-ADRPVSMLFQENNLFAHLTVEQNVGL- 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 369 ARLFGVPAAEID-ARVDEMARRFGLADIYGMLPDSLPLGMRQRLSLAVAMVHKPELLILDEPTSGVDPVARDSFWQLMID 447
Cdd:cd03298 94 GLSPGLKLTAEDrQAIEVALARVGLAGLEKRLPGELSGGERQRVALARVLVRDKPVLLLDEPFAALDPALRAEMLDLVLD 173
|
170 180 190
....*....|....*....|....*....|....*.
gi 505416896 448 LARRDLVTIFISTHFMNEAQRC-DRISLMHAGRVLA 482
Cdd:cd03298 174 LHAETKMTVLMVTHQPEDAKRLaQRVVFLDNGRIAA 209
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
8-220 |
1.17e-22 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 97.19 E-value: 1.17e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 8 RFSDVSLRYGKTVALDRITLDVPAGLTTGLIGPDGVGKSSLLALASGARALQTGGVdALGGDMRSRRHRERVCRRIAYMP 87
Cdd:COG4619 2 ELEGLSFRVGGKPILSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEI-YLDGKPLSAMPPPEWRRQVAYVP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 88 QglgknlYPTL---SVEENLQFfARLFGHDAGERRRRIDALTQsTGLFP-FLSRPAGKLSGGMKQKLGLCCALIHDPDLL 163
Cdd:COG4619 81 Q------EPALwggTVRDNLPF-PFQLRERKFDRERALELLER-LGLPPdILDKPVERLSGGERQRLALIRALLLQPDVL 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 505416896 164 ILDEPTTGVDPLARAQFWDLIARIRDErPTMSVIVATAYMDEAQRF-DWLIAMDAGRV 220
Cdd:COG4619 153 LLDEPTSALDPENTRRVEELLREYLAE-EGRAVLWVSHDPEQIERVaDRVLTLEAGRL 209
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
288-495 |
1.24e-22 |
|
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: 98.00 E-value: 1.24e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 288 DHVSFRIRRGEIFGFLGSNGCGKSTTMKMLTGLLPATEGTAQLFGkeVDPKDIN---TRRRVGYMSQAFSLYSeLTVRQN 364
Cdd:cd03249 20 KGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEILLDG--VDIRDLNlrwLRSQIGLVSQEPVLFD-GTIAEN 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 365 LvlharLFGVPAAEiDARVDEMARRFGLADIYGMLPD-----------SLPLGMRQRLSLAVAMVHKPELLILDEPTSGV 433
Cdd:cd03249 97 I-----RYGKPDAT-DEEVEEAAKKANIHDFIMSLPDgydtlvgergsQLSGGQKQRIAIARALLRNPKILLLDEATSAL 170
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 505416896 434 DpVARDSFWQLMIDLARRDLVTIFIStHFMNEAQRCDRISLMHAGRVLASDSPAELVRARGA 495
Cdd:cd03249 171 D-AESEKLVQEALDRAMKGRTTIVIA-HRLSTIRNADLIAVLQNGQVVEQGTHDELMAQKGV 230
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
286-494 |
1.52e-22 |
|
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan exporter ATP-binding protein. In A. tumefaciens cyclic beta-1, 2-glucan must be transported into the periplasmic space to exert its action as a virulence factor. This subfamily belongs to the MRP-like family and is involved in drug, peptide, and lipid export. The MRP-like family, similar to all ABC proteins, have a common four-domain core structure constituted by two membrane-spanning domains each composed of six transmembrane (TM) helices and two nucleotide-binding domains (NBD). ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213221 [Multi-domain] Cd Length: 229 Bit Score: 97.30 E-value: 1.52e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 286 AVDHVSFRIRRGEIFGFLGSNGCGKSTTMKMLTGLLPATEGTAQLFGKEVDPKDINT-RRRVGYMSQAFSLYSElTVRQN 364
Cdd:cd03254 18 VLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGIDIRDISRKSlRSMIGVVLQDTFLFSG-TIMEN 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 365 LvlharLFGVPAAEiDARVDEMARRFGLADIYGMLPD-----------SLPLGMRQRLSLAVAMVHKPELLILDEPTSGV 433
Cdd:cd03254 97 I-----RLGRPNAT-DEEVIEAAKEAGAHDFIMKLPNgydtvlgenggNLSQGERQLLAIARAMLRDPKILILDEATSNI 170
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 505416896 434 DPVARDSFWQLMIDLarRDLVTIFISTHFMNEAQRCDRISLMHAGRVLASDSPAELVRARG 494
Cdd:cd03254 171 DTETEKLIQEALEKL--MKGRTSIIIAHRLSTIKNADKILVLDDGKIIEEGTHDELLAKKG 229
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
16-480 |
2.55e-22 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 101.93 E-value: 2.55e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 16 YGKTVALDRITLDVPAGLTTGLIGPDGVGKSSLLALASGARALQTGGVDAL--GGDMRSRRHRERVCRRIAYMPQGLGkn 93
Cdd:PRK13549 15 FGGVKALDNVSLKVRAGEIVSLCGENGAGKSTLMKVLSGVYPHGTYEGEIIfeGEELQASNIRDTERAGIAIIHQELA-- 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 94 LYPTLSVEENLqFFARLFGH----DAGERRRRIDALTQSTGLFPFLSRPAGKLSGGMKQKLGLCCALIHDPDLLILDEPT 169
Cdd:PRK13549 93 LVKELSVLENI-FLGNEITPggimDYDAMYLRAQKLLAQLKLDINPATPVGNLGLGQQQLVEIAKALNKQARLLILDEPT 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 170 TgvdPLARAQFWDLIARIRDERP--------------------TMSVI-----VATAYMDEAQRfDWLIAMDAGRVLATG 224
Cdd:PRK13549 172 A---SLTESETAVLLDIIRDLKAhgiaciyishklnevkaisdTICVIrdgrhIGTRPAAGMTE-DDIITMMVGRELTAL 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 225 APAELLArTGCDSLEAA-FIALLPENERRghkpvKIeplradaragtaieargltmrfgdftaVDHVSFRIRRGEIFGFL 303
Cdd:PRK13549 248 YPREPHT-IGEVILEVRnLTAWDPVNPHI-----KR---------------------------VDDVSFSLRRGEILGIA 294
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 304 GSNGCGKSTTMKMLTGLLP-ATEGTAQLFGKEVD---------------PKDintRRRVGymsqafsLYSELTVRQNLVL 367
Cdd:PRK13549 295 GLVGAGRTELVQCLFGAYPgRWEGEIFIDGKPVKirnpqqaiaqgiamvPED---RKRDG-------IVPVMGVGKNITL 364
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 368 HA----RLFGV--PAAEIDARVDEMAR-RFGLADIygMLP-DSLPLGMRQRLSLAVAMVHKPELLILDEPTSGVDPVARD 439
Cdd:PRK13549 365 AAldrfTGGSRidDAAELKTILESIQRlKVKTASP--ELAiARLSGGNQQKAVLAKCLLLNPKILILDEPTRGIDVGAKY 442
|
490 500 510 520
....*....|....*....|....*....|....*....|.
gi 505416896 440 SFWQLMIDLARRDLVTIFISTHFMNEAQRCDRISLMHAGRV 480
Cdd:PRK13549 443 EIYKLINQLVQQGVAIIVISSELPEVLGLSDRVLVMHEGKL 483
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
3-239 |
2.56e-22 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 99.81 E-value: 2.56e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 3 ASSVVRFSDVSLRYGKTVALDRITLDVPAGLTTGLIGPDGVgkssllALASGARALQTGGVDALGGDMR----SRRHRER 78
Cdd:NF000106 10 ARNAVEVRGLVKHFGEVKAVDGVDLDVREGTVLGVLGP*GA------A**RGALPAHV*GPDAGRRPWRf*twCANRRAL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 79 VCRRIAYMPQGLGKNlyPTLSVEENLQFFARLFGHDAGERRRRIDALTQSTGLFPFLSRPAGKLSGGMKQKLGLCCALIH 158
Cdd:NF000106 84 RRTIG*HRPVR*GRR--ESFSGRENLYMIGR*LDLSRKDARARADELLERFSLTEAAGRAAAKYSGGMRRRLDLAASMIG 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 159 DPDLLILDEPTTGVDPLARAQFWDLI-ARIRDerpTMSVIVATAYMDEAQRF-DWLIAMDAGRVLATGAPAELLARTGCD 236
Cdd:NF000106 162 RPAVLYLDEPTTGLDPRTRNEVWDEVrSMVRD---GATVLLTTQYMEEAEQLaHELTVIDRGRVIADGKVDELKTKVGGR 238
|
...
gi 505416896 237 SLE 239
Cdd:NF000106 239 TLQ 241
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
271-475 |
2.68e-22 |
|
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: 101.98 E-value: 2.68e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 271 AIEARGLTMRFGDFT-AVDHVSFRIRRGEIFGFLGSNGCGKSTTMKMLTGLLPATEGTAQLFGKEVDPKDINT-RRRVGY 348
Cdd:TIGR02857 321 SLEFSGVSVAYPGRRpALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSIAVNGVPLADADADSwRDQIAW 400
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 349 MSQAFSLYsELTVRQNLvlharLFGVPAAEiDARVDEMARRFGLADIYGMLPDSLPL-----------GMRQRLSLAVAM 417
Cdd:TIGR02857 401 VPQHPFLF-AGTIAENI-----RLARPDAS-DAEIREALERAGLDEFVAALPQGLDTpigeggaglsgGQAQRLALARAF 473
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 505416896 418 VHKPELLILDEPTSGVDPVARDSFWQLMIDLARRdlVTIFISTHFMNEAQRCDRISLM 475
Cdd:TIGR02857 474 LRDAPLLLLDEPTAHLDAETEAEVLEALRALAQG--RTVLLVTHRLALAALADRIVVL 529
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
280-509 |
3.17e-22 |
|
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: 99.42 E-value: 3.17e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 280 RFGDFTAvdHVSFRIRRGEIFGFLGSNGCGKSTTMKMLTGLLPATEGTAQLFGKEVDP--KDINT---RRRVGYMSQAFS 354
Cdd:TIGR02142 8 RLGDFSL--DADFTLPGQGVTAIFGRSGSGKTTLIRLIAGLTRPDEGEIVLNGRTLFDsrKGIFLppeKRRIGYVFQEAR 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 355 LYSELTVRQNLVLHARLfgVPAAEIDARVDEMARRFGLADIYGMLPDSLPLGMRQRLSLAVAMVHKPELLILDEPTSGVD 434
Cdd:TIGR02142 86 LFPHLSVRGNLRYGMKR--ARPSERRISFERVIELLGIGHLLGRLPGRLSGGEKQRVAIGRALLSSPRLLLMDEPLAALD 163
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 505416896 435 PVARDSFWQLMIDLARR-DLVTIFIStHFMNEAQR-CDRISLMHAGRVLASDSPAELVRARGAATLEDAFIGYLVDA 509
Cdd:TIGR02142 164 DPRKYEILPYLERLHAEfGIPILYVS-HSLQEVLRlADRVVVLEDGRVAAAGPIAEVWASPDLPWLAREDQGSLIEG 239
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
266-468 |
3.63e-22 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 97.16 E-value: 3.63e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 266 ARAGTAIEARGLTMRFGDFTAVDHVSFRIRRGEIFGFLGSNGCGKSTTMK---MLTGLLPA--TEGT-----AQLFGKEV 335
Cdd:PRK14243 5 NGTETVLRTENLNVYYGSFLAVKNVWLDIPKNQITAFIGPSGCGKSTILRcfnRLNDLIPGfrVEGKvtfhgKNLYAPDV 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 336 DPKDIntRRRVGYMSQAFSLYSElTVRQNLVLHARLFGVpAAEIDARVDEMARRFGLAD-IYGMLPDS---LPLGMRQRL 411
Cdd:PRK14243 85 DPVEV--RRRIGMVFQKPNPFPK-SIYDNIAYGARINGY-KGDMDELVERSLRQAALWDeVKDKLKQSglsLSGGQQQRL 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 505416896 412 SLAVAMVHKPELLILDEPTSGVDPVARDSFWQLMIDLARRdlVTIFISTHFMNEAQR 468
Cdd:PRK14243 161 CIARAIAVQPEVILMDEPCSALDPISTLRIEELMHELKEQ--YTIIIVTHNMQQAAR 215
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
277-490 |
4.72e-22 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 96.19 E-value: 4.72e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 277 LTMRFgdftavdhvSFRIRRGEIFGFLGSNGCGKSTTMKMLTGLLPATEGTAQLFGKE---VDPkdinTRRRVGYMSQAF 353
Cdd:PRK10771 14 LPMRF---------DLTVERGERVAILGPSGAGKSTLLNLIAGFLTPASGSLTLNGQDhttTPP----SRRPVSMLFQEN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 354 SLYSELTVRQN--LVLHA--RLfgvpAAEIDARVDEMARRFGLADIYGMLPDSLPLGMRQRLSLAVAMVHKPELLILDEP 429
Cdd:PRK10771 81 NLFSHLTVAQNigLGLNPglKL----NAAQREKLHAIARQMGIEDLLARLPGQLSGGQRQRVALARCLVREQPILLLDEP 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 505416896 430 TSGVDPVARDSFWQLMIDLARRDLVTIFISTHFMNEAQR-CDRISLMHAGRVLASDSPAELV 490
Cdd:PRK10771 157 FSALDPALRQEMLTLVSQVCQERQLTLLMVSHSLEDAARiAPRSLVVADGRIAWDGPTDELL 218
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
275-455 |
7.01e-22 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 94.86 E-value: 7.01e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 275 RGLTMRFGDFTAVDHVSFRIRRGEIFGFLGSNGCGKSTTMKMLTGLLPA---TEGTAQLFGKEVDPKDINtRRRVGYMSQ 351
Cdd:COG4136 5 ENLTITLGGRPLLAPLSLTVAPGEILTLMGPSGSGKSTLLAAIAGTLSPafsASGEVLLNGRRLTALPAE-QRRIGILFQ 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 352 AFSLYSELTVRQNLvlharLFGVPA----AEIDARVDEMARRFGLADIYGMLPDSLPLGMRQRLSLAVAMVHKPELLILD 427
Cdd:COG4136 84 DDLLFPHLSVGENL-----AFALPPtigrAQRRARVEQALEEAGLAGFADRDPATLSGGQRARVALLRALLAEPRALLLD 158
|
170 180 190
....*....|....*....|....*....|...
gi 505416896 428 EPTSGVDPVARDSFWQLMIDLARRD-----LVT 455
Cdd:COG4136 159 EPFSKLDAALRAQFREFVFEQIRQRgipalLVT 191
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
8-200 |
7.24e-22 |
|
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: 94.63 E-value: 7.24e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 8 RFSDVSLRYGK-TVALDRITLDVPAGLTTGLIGPDGVGKSSLLALASGARALQTGGVdALGGDMRSRRHRERVcrrIAYM 86
Cdd:cd03226 1 RIENISFSYKKgTEILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSI-LLNGKPIKAKERRKS---IGYV 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 87 PQGLGKNLYpTLSVEENLQFFARlfghDAGERRRRIDALTQSTGLFPFLSRPAGKLSGGMKQKLGLCCALIHDPDLLILD 166
Cdd:cd03226 77 MQDVDYQLF-TDSVREELLLGLK----ELDAGNEQAETVLKDLDLYALKERHPLSLSGGQKQRLAIAAALLSGKDLLIFD 151
|
170 180 190
....*....|....*....|....*....|....
gi 505416896 167 EPTTGVDPLARAQFWDLIARIRDErpTMSVIVAT 200
Cdd:cd03226 152 EPTSGLDYKNMERVGELIRELAAQ--GKAVIVIT 183
|
|
| thiQ |
TIGR01277 |
thiamine ABC transporter, ATP-binding protein; This model describes the energy-transducing ... |
291-480 |
1.07e-21 |
|
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: 94.54 E-value: 1.07e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 291 SFRIRRGEIFGFLGSNGCGKSTTMKMLTGLLPATEGTAQLFGKEVdPKDINTRRRVGYMSQAFSLYSELTVRQNLVLHAR 370
Cdd:TIGR01277 18 DLNVADGEIVAIMGPSGAGKSTLLNLIAGFIEPASGSIKVNDQSH-TGLAPYQRPVSMLFQENNLFAHLTVRQNIGLGLH 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 371 LFGVPAAEIDARVDEMARRFGLADIYGMLPDSLPLGMRQRLSLAVAMVHKPELLILDEPTSGVDPVARDSFWQLMIDLAR 450
Cdd:TIGR01277 97 PGLKLNAEQQEKVVDAAQQVGIADYLDRLPEQLSGGQRQRVALARCLVRPNPILLLDEPFSALDPLLREEMLALVKQLCS 176
|
170 180 190
....*....|....*....|....*....|.
gi 505416896 451 RDLVTIFISTHFMNEAQR-CDRISLMHAGRV 480
Cdd:TIGR01277 177 ERQRTLLMVTHHLSDARAiASQIAVVSQGKI 207
|
|
| LPS_export_lptB |
TIGR04406 |
LPS export ABC transporter ATP-binding protein; Members of this fmaily are LptB, the ... |
15-231 |
1.22e-21 |
|
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: 95.03 E-value: 1.22e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 15 RYGKTVALDRITLDVPAGLTTGLIGPDGVGKSSLLALASGARALQTGGVDALGGDMRSRRHRERVCRRIAYMPQGlgKNL 94
Cdd:TIGR04406 10 SYKKRKVVNDVSLSVKSGEIVGLLGPNGAGKTTSFYMIVGLVRPDAGKILIDGQDITHLPMHERARLGIGYLPQE--ASI 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 95 YPTLSVEEN----LQFFARLfghDAGERRRRIDALTQSTGLFPFLSRPAGKLSGGMKQKLGLCCALIHDPDLLILDEPTT 170
Cdd:TIGR04406 88 FRKLTVEENimavLEIRKDL---DRAEREERLEALLEEFQISHLRDNKAMSLSGGERRRVEIARALATNPKFILLDEPFA 164
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 505416896 171 GVDPLARAQFWDLIARIRDE-----------RPTMSvIVATAYMdeaqrfdwliaMDAGRVLATGAPAELLA 231
Cdd:TIGR04406 165 GVDPIAVGDIKKIIKHLKERgigvlitdhnvRETLD-ICDRAYI-----------ISDGKVLAEGTPAEIVA 224
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
15-210 |
1.28e-21 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 93.45 E-value: 1.28e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 15 RYGKTVALDRITLDVPAGLTTGLIGPDGVGKSSLLALASGARALQTGGVDALGGdmrsrrhrervcRRIAYMPQGLGKNL 94
Cdd:NF040873 1 GYGGRPVLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTVRRAGG------------ARVAYVPQRSEVPD 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 95 YPTLSVEE--NLQFFAR--LFGHDAGERRRRIDALTQSTGLFPFLSRPAGKLSGGMKQKLGLCCALIHDPDLLILDEPTT 170
Cdd:NF040873 69 SLPLTVRDlvAMGRWARrgLWRRLTRDDRAAVDDALERVGLADLAGRQLGELSGGQRQRALLAQGLAQEADLLLLDEPTT 148
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 505416896 171 GVDPLARAQFWDLIARIRDERPTmsVIVATAYMDEAQRFD 210
Cdd:NF040873 149 GLDAESRERIIALLAEEHARGAT--VVVVTHDLELVRRAD 186
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
6-232 |
1.90e-21 |
|
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: 94.18 E-value: 1.90e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 6 VVRFSDVSLRYG----KTVALDRITLDVPAGLTTGLIGPDGVGKSSLLALASGARALQTGGVDALGGDM--RSRRHRERV 79
Cdd:cd03258 1 MIELKNVSKVFGdtggKVTALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGSVLVDGTDLtlLSGKELRKA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 80 CRRIAYMPQGLgkNLYPTLSVEENLQFFARLFGHDAGERRRRIDALTQSTGLFPFLSRPAGKLSGGMKQKLGLCCALIHD 159
Cdd:cd03258 81 RRRIGMIFQHF--NLLSSRTVFENVALPLEIAGVPKAEIEERVLELLELVGLEDKADAYPAQLSGGQKQRVGIARALANN 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 505416896 160 PDLLILDEPTTGVDPLARAQFWDLIARIRDERpTMSVIVATAYMDEAQRF-DWLIAMDAGRVLATGAPAELLAR 232
Cdd:cd03258 159 PKVLLCDEATSALDPETTQSILALLRDINREL-GLTIVLITHEMEVVKRIcDRVAVMEKGEVVEEGTVEEVFAN 231
|
|
| anch_rpt_ABC |
TIGR03771 |
anchored repeat-type ABC transporter, ATP-binding subunit; This protein family is the ... |
292-489 |
2.01e-21 |
|
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: 93.76 E-value: 2.01e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 292 FRIRRGEIFGFLGSNGCGKSTTMKMLTGLLPATEGTAQLFGKEVDPKdintRRRVGYMSQ--AFSLYSELTVRQnLVLHA 369
Cdd:TIGR03771 1 LSADKGELLGLLGPNGAGKTTLLRAILGLIPPAKGTVKVAGASPGKG----WRHIGYVPQrhEFAWDFPISVAH-TVMSG 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 370 R-----LFGVPAAEIDARVDEMARRFGLADIYGMLPDSLPLGMRQRLSLAVAMVHKPELLILDEPTSGVDPVARDSFWQL 444
Cdd:TIGR03771 76 RtghigWLRRPCVADFAAVRDALRRVGLTELADRPVGELSGGQRQRVLVARALATRPSVLLLDEPFTGLDMPTQELLTEL 155
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 505416896 445 MIDLArRDLVTIFISTHFMNEA-QRCDRISLMHaGRVLASDSPAEL 489
Cdd:TIGR03771 156 FIELA-GAGTAILMTTHDLAQAmATCDRVVLLN-GRVIADGTPQQL 199
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
286-495 |
2.25e-21 |
|
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; MsbA is an essential ABC transporter, closely related to eukaryotic MDR proteins. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213218 [Multi-domain] Cd Length: 234 Bit Score: 94.22 E-value: 2.25e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 286 AVDHVSFRIRRGEIFGFLGSNGCGKSTTMKMLTGLLPATEGTAQLFGkeVDPKDI---NTRRRVGYMSQAFSLYSElTVR 362
Cdd:cd03251 17 VLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDG--HDVRDYtlaSLRRQIGLVSQDVFLFND-TVA 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 363 QNLvlharLFGVPAAEiDARVDEMARRFGLADIYGMLPD-----------SLPLGMRQRLSLAVAMVHKPELLILDEPTS 431
Cdd:cd03251 94 ENI-----AYGRPGAT-REEVEEAARAANAHEFIMELPEgydtvigergvKLSGGQRQRIAIARALLKDPPILILDEATS 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 505416896 432 GVDPVA----RDSFWQLMIDlaRrdlvTIFISTHFMNEAQRCDRISLMHAGRVLASDSPAELVRARGA 495
Cdd:cd03251 168 ALDTESerlvQAALERLMKN--R----TTFVIAHRLSTIENADRIVVLEDGKIVERGTHEELLAQGGV 229
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
272-483 |
2.38e-21 |
|
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: 98.74 E-value: 2.38e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 272 IEARGLTMRFGDFTAVDHVSFRIRRGEIFGFLGSNGCGKSTTMKMLTGLLP--ATEGTAQLFGKEVDPKDINTRRRVG-- 347
Cdd:TIGR02633 2 LEMKGIVKTFGGVKALDGIDLEVRPGECVGLCGENGAGKSTLMKILSGVYPhgTWDGEIYWSGSPLKASNIRDTERAGiv 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 348 YMSQAFSLYSELTVRQNLVLHARL----FGVPAAEIDARVDEMARRFGLADIygmlPDSLP-----LGMRQRLSLAVAMV 418
Cdd:TIGR02633 82 IIHQELTLVPELSVAENIFLGNEItlpgGRMAYNAMYLRAKNLLRELQLDAD----NVTRPvgdygGGQQQLVEIAKALN 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 505416896 419 HKPELLILDEPTSGVDPVARDSFWQLMIDLARRDLVTIFIStHFMNEAQR-CDRISLMHAGRVLAS 483
Cdd:TIGR02633 158 KQARLLILDEPSSSLTEKETEILLDIIRDLKAHGVACVYIS-HKLNEVKAvCDTICVIRDGQHVAT 222
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
272-481 |
2.81e-21 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 94.21 E-value: 2.81e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 272 IEARGLTMRFGDFTAVDHVSFRIRRGEIFGFLGSNGCGKSTTMKMLTGLL-----PATEGTAQLFGKEVDPKD-INTRRR 345
Cdd:PRK14247 4 IEIRDLKVSFGQVEVLDGVNLEIPDNTITALMGPSGSGKSTLLRVFNRLIelypeARVSGEVYLDGQDIFKMDvIELRRR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 346 VGYMSQAFSLYSELTVRQNLVLHARLFGV--PAAEIDARVDEMARRFGL----ADIYGMLPDSLPLGMRQRLSLAVAMVH 419
Cdd:PRK14247 84 VQMVFQIPNPIPNLSIFENVALGLKLNRLvkSKKELQERVRWALEKAQLwdevKDRLDAPAGKLSGGQQQRLCIARALAF 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 505416896 420 KPELLILDEPTSGVDPVARDSFWQLMIDLARRdlVTIFISTHFMNEAQRC-DRISLMHAGRVL 481
Cdd:PRK14247 164 QPEVLLADEPTANLDPENTAKIESLFLELKKD--MTIVLVTHFPQQAARIsDYVAFLYKGQIV 224
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
272-480 |
2.83e-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: 91.89 E-value: 2.83e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 272 IEARGLTMRFGDFTA--VDHVSFRIRRGEIFGFLGSNGCGKSTTMKMLTGLLPATEGTAQLFGKEVDPKDINT-RRRVGY 348
Cdd:cd03246 1 LEVENVSFRYPGAEPpvLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDGADISQWDPNElGDHVGY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 349 MSQAFSLYSElTVRQNLvlharlfgvpaaeidarvdemarrfgladiygmlpdsLPLGMRQRLSLAVAMVHKPELLILDE 428
Cdd:cd03246 81 LPQDDELFSG-SIAENI-------------------------------------LSGGQRQRLGLARALYGNPRILVLDE 122
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 505416896 429 PTSGVDPVARDSFWQLMIDLaRRDLVTIFISTHFMNEAQRCDRISLMHAGRV 480
Cdd:cd03246 123 PNSHLDVEGERALNQAIAAL-KAAGATRIVIAHRPETLASADRILVLEDGRV 173
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
282-481 |
3.29e-21 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 95.95 E-value: 3.29e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 282 GDFTAVDHVSFRIRRGEIFGFLGSNGCGKSTTMKMLTGLLPA---TEGTAQLFGKEV---DPKDINtRRRVGYMSQAF-- 353
Cdd:PRK09473 27 GDVTAVNDLNFSLRAGETLGIVGESGSGKSQTAFALMGLLAAngrIGGSATFNGREIlnlPEKELN-KLRAEQISMIFqd 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 354 ---SLYSELTVRQNLV----LHARLFGVPAAE-----IDA-RVDEMARRFGladiygMLPDSLPLGMRQRLSLAVAMVHK 420
Cdd:PRK09473 106 pmtSLNPYMRVGEQLMevlmLHKGMSKAEAFEesvrmLDAvKMPEARKRMK------MYPHEFSGGMRQRVMIAMALLCR 179
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 505416896 421 PELLILDEPTSGVDPVARDSFWQLMIDLARRDLVTIFISTHFMN-EAQRCDRISLMHAGRVL 481
Cdd:PRK09473 180 PKLLIADEPTTALDVTVQAQIMTLLNELKREFNTAIIMITHDLGvVAGICDKVLVMYAGRTM 241
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
6-232 |
3.51e-21 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 93.62 E-value: 3.51e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 6 VVRFSDVSLRYGKTVALDRITLDVPAGLTTGLIGPDGVGKSSLLALASGARALQTGGVDALGGDMRSRRHRERVCRRIAY 85
Cdd:PRK09493 1 MIEFKNVSKHFGPTQVLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGLKVNDPKVDERLIRQEAG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 86 MP-QGLgkNLYPTLSVEENLQFFA-RLFGHDAGERRRRIDALTQSTGLFPFLSRPAGKLSGGMKQKLGLCCALIHDPDLL 163
Cdd:PRK09493 81 MVfQQF--YLFPHLTALENVMFGPlRVRGASKEEAEKQARELLAKVGLAERAHHYPSELSGGQQQRVAIARALAVKPKLM 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 164 ILDEPTTGVDPLARAQFWDLIARIRDERPTMsvIVATAYMDEAQRF-DWLIAMDAGRVLATGAPAELLAR 232
Cdd:PRK09493 159 LFDEPTSALDPELRHEVLKVMQDLAEEGMTM--VIVTHEIGFAEKVaSRLIFIDKGRIAEDGDPQVLIKN 226
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
271-435 |
3.69e-21 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 93.54 E-value: 3.69e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 271 AIEARGLTMRFGDFTAVDHVSFRIRRGEIFGFLGSNGCGKSTTMKMLTGLLPATEGTAQL------FGKEVDPKDINT-R 343
Cdd:PRK11124 2 SIQLNGINCFYGAHQALFDITLDCPQGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLNIagnhfdFSKTPSDKAIRElR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 344 RRVGYMSQAFSLYSELTVRQNLVlHA--RLFGVPAAEIDARVDEMARRFGLADIYGMLPDSLPLGMRQRLSLAVAMVHKP 421
Cdd:PRK11124 82 RNVGMVFQQYNLWPHLTVQQNLI-EApcRVLGLSKDQALARAEKLLERLRLKPYADRFPLHLSGGQQQRVAIARALMMEP 160
|
170
....*....|....
gi 505416896 422 ELLILDEPTSGVDP 435
Cdd:PRK11124 161 QVLLFDEPTAALDP 174
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
6-231 |
4.40e-21 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 93.40 E-value: 4.40e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 6 VVRFSDVSLRYGKTVALDRITLDVPAGLTTGLIGPDGVGKSSLLALASGARALQTGGVDALGGDMRSRRHRERVCRRIAY 85
Cdd:PRK11614 5 MLSFDKVSAHYGKIQALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDGKDITDWQTAKIMREAVAI 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 86 MPQGlgKNLYPTLSVEENLQ---FFArlfghdagERRRRIDALTQSTGLFPFL----SRPAGKLSGGMKQKLGLCCALIH 158
Cdd:PRK11614 85 VPEG--RRVFSRMTVEENLAmggFFA--------ERDQFQERIKWVYELFPRLherrIQRAGTMSGGEQQMLAIGRALMS 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 505416896 159 DPDLLILDEPTTGVDPLARAQFWDLIARIRDErpTMSVIVATAYMDEAQRF-DWLIAMDAGRVLATGAPAELLA 231
Cdd:PRK11614 155 QPRLLLLDEPSLGLAPIIIQQIFDTIEQLREQ--GMTIFLVEQNANQALKLaDRGYVLENGHVVLEDTGDALLA 226
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
290-480 |
4.77e-21 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 92.96 E-value: 4.77e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 290 VSFRIRRGEIFGFLGSNGCGKSTTMKMLTGLLPATEGTAQLFGKEVDPKDINTR-----RRVGYMSQAFSLYSELTVRQN 364
Cdd:PRK11629 28 VSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPMSKLSSAAKaelrnQKLGFIYQFHHLLPDFTALEN 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 365 LVLHARLFGVPAAEIDARVDEMARRFGLADIYGMLPDSLPLGMRQRLSLAVAMVHKPELLILDEPTSGVDPVARDSFWQL 444
Cdd:PRK11629 108 VAMPLLIGKKKPAEINSRALEMLAAVGLEHRANHRPSELSGGERQRVAIARALVNNPRLVLADEPTGNLDARNADSIFQL 187
|
170 180 190
....*....|....*....|....*....|....*.
gi 505416896 445 MIDLARRDLVTIFISTHFMNEAQRCDRISLMHAGRV 480
Cdd:PRK11629 188 LGELNRLQGTAFLVVTHDLQLAKRMSRQLEMRDGRL 223
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
265-502 |
5.77e-21 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 93.70 E-value: 5.77e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 265 DARAGTAIEARGLTMRFGDFTAVDHVSFRIRRGEIFGFLGSNGCGKSTTMKMLTGLLPATEGTAQLFGKEVDPKDINT-R 343
Cdd:PRK10575 5 TNHSDTTFALRNVSFRVPGRTLLHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPLESWSSKAfA 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 344 RRVGYMSQAFSLYSELTVRQnLVLHARL-----FGVPAAEIDARVDEMARRFGLADIYGMLPDSLPLGMRQRLSLAVAMV 418
Cdd:PRK10575 85 RKVAYLPQQLPAAEGMTVRE-LVAIGRYpwhgaLGRFGAADREKVEEAISLVGLKPLAHRLVDSLSGGERQRAWIAMLVA 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 419 HKPELLILDEPTSGVDPVARDSFWQLMIDLARRDLVTIFISTHFMNEAQR-CDRISLMHAGRVLASDSPAELVRargAAT 497
Cdd:PRK10575 164 QDSRCLLLDEPTSALDIAHQVDVLALVHRLSQERGLTVIAVLHDINMAARyCDYLVALRGGEMIAQGTPAELMR---GET 240
|
....*
gi 505416896 498 LEDAF 502
Cdd:PRK10575 241 LEQIY 245
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
272-483 |
7.45e-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: 90.84 E-value: 7.45e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 272 IEARGLTMRFG--DFTAVDHVSFRIRRGEIFGFLGSNGCGKSTTMKMLTGLLPATEGTAQLFGKEVDPKDINTRRRVGYM 349
Cdd:cd03247 1 LSINNVSFSYPeqEQQVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDGVPVSDLEKALSSLISVL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 350 SQAFSLYSElTVRQNLvlharlfgvpaaeidarvdemARRFGladiyGmlpdslplGMRQRLSLAVAMVHKPELLILDEP 429
Cdd:cd03247 81 NQRPYLFDT-TLRNNL---------------------GRRFS-----G--------GERQRLALARILLQDAPIVLLDEP 125
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 505416896 430 TSGVDPVARDSFWQLMIDLARRDlvTIFISTHFMNEAQRCDRISLMHAGRVLAS 483
Cdd:cd03247 126 TVGLDPITERQLLSLIFEVLKDK--TLIWITHHLTGIEHMDKILFLENGKIIMQ 177
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
2-230 |
8.02e-21 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 93.52 E-value: 8.02e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 2 NASSVVRFSDVSLRYG--KTVALDRITLDVPAGLTTGLIGPDGVGKSSLLALASGARALQTGGVDALGGDMRSRRhrerv 79
Cdd:PRK13632 3 NKSVMIKVENVSFSYPnsENNALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIDGITISKEN----- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 80 crrIAYMPQGLG------KNLYPTLSVEENLQFFARLFGHDAGERRRRIDALTQSTGLFPFLSRPAGKLSGGMKQKLGLC 153
Cdd:PRK13632 78 ---LKEIRKKIGiifqnpDNQFIGATVEDDIAFGLENKKVPPKKMKDIIDDLAKKVGMEDYLDKEPQNLSGGQKQRVAIA 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 505416896 154 CALIHDPDLLILDEPTTGVDPLARAQFWDLIARIRDERpTMSVIVATAYMDEAQRFDWLIAMDAGRVLATGAPAELL 230
Cdd:PRK13632 155 SVLALNPEIIIFDESTSMLDPKGKREIKKIMVDLRKTR-KKTLISITHDMDEAILADKVIVFSEGKLIAQGKPKEIL 230
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
217-492 |
9.45e-21 |
|
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: 97.51 E-value: 9.45e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 217 AGRVLAtgaPAELL---------ARTGCDSLEAAFiALLPENERRGHKPvkieplradaRAGTAIEARGLTMRF--GDFT 285
Cdd:COG4618 281 MGRALA---PIEQAiggwkqfvsARQAYRRLNELL-AAVPAEPERMPLP----------RPKGRLSVENLTVVPpgSKRP 346
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 286 AVDHVSFRIRRGEIFGFLGSNGCGKSTTMKMLTGLLPATEGTAQLFGKEVDPKDINTR-RRVGYMSQAFSLYsELTVRQN 364
Cdd:COG4618 347 ILRGVSFSLEPGEVLGVIGPSGSGKSTLARLLVGVWPPTAGSVRLDGADLSQWDREELgRHIGYLPQDVELF-DGTIAEN 425
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 365 LvlhARLfgvpaAEID-ARVDEMARRFGLADIYGMLPD---------SLPL--GMRQRLSLAVAMVHKPELLILDEPTSG 432
Cdd:COG4618 426 I---ARF-----GDADpEKVVAAAKLAGVHEMILRLPDgydtrigegGARLsgGQRQRIGLARALYGDPRLVVLDEPNSN 497
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 433 VDPVARDSFWQlMIDLARRDLVTIFISTHFMNEAQRCDRISLMHAGRVLASDSPAELVRA 492
Cdd:COG4618 498 LDDEGEAALAA-AIRALKARGATVVVITHRPSLLAAVDKLLVLRDGRVQAFGPRDEVLAR 556
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
2-207 |
9.56e-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: 98.93 E-value: 9.56e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 2 NASSVVRFSDVSLRYGKTV--ALDRITLDVPAGLTTGLIGPDGVGKSSLLALASGARALQTGGVDALGGDMRSRRHRERV 79
Cdd:TIGR01257 1933 NKTDILRLNELTKVYSGTSspAVDRLCVGVRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAGKSILTNISDVHQ 2012
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 80 CrrIAYMPQGlgKNLYPTLSVEENLQFFARLFGHDAGERRRRIDALTQSTGLFPFLSRPAGKLSGGMKQKLGLCCALIHD 159
Cdd:TIGR01257 2013 N--MGYCPQF--DAIDDLLTGREHLYLYARLRGVPAEEIEKVANWSIQSLGLSLYADRLAGTYSGGNKRKLSTAIALIGC 2088
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 505416896 160 PDLLILDEPTTGVDPLARAQFWDLIAR-IRDERptmSVIVATAYMDEAQ 207
Cdd:TIGR01257 2089 PPLVLLDEPTTGMDPQARRMLWNTIVSiIREGR---AVVLTSHSMEECE 2134
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
10-231 |
1.66e-20 |
|
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This family comprises the glycine betaine/L-proline ATP binding subunit in bacteria and its equivalents in archaea. This transport system belong to the larger ATP-Binding Cassette (ABC) transporter superfamily. The characteristic feature of these transporters is the obligatory coupling of ATP hydrolysis to substrate translocation. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213261 [Multi-domain] Cd Length: 269 Bit Score: 92.32 E-value: 1.66e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 10 SDVSLRYGKTVALDRITLDVPAGLTTGLIGPDGVGKSSLLALASGARALQTGGVDALGGDMRSRRHRERVCR---RIAYM 86
Cdd:cd03294 28 EEILKKTGQTVGVNDVSLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGKVLIDGQDIAAMSRKELRELrrkKISMV 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 87 PQGLGknLYPTLSVEENLQFFARLFGHDAGERRRR-IDALTQsTGLFPFLSRPAGKLSGGMKQKLGLCCALIHDPDLLIL 165
Cdd:cd03294 108 FQSFA--LLPHRTVLENVAFGLEVQGVPRAEREERaAEALEL-VGLEGWEHKYPDELSGGMQQRVGLARALAVDPDILLM 184
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 505416896 166 DEPTTGVDPLARAQFWDLIARIRDERPTMSVIVaTAYMDEAQRFDWLIA-MDAGRVLATGAPAELLA 231
Cdd:cd03294 185 DEAFSALDPLIRREMQDELLRLQAELQKTIVFI-THDLDEALRLGDRIAiMKDGRLVQVGTPEEILT 250
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
7-229 |
1.93e-20 |
|
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: 91.63 E-value: 1.93e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 7 VRFSDVSLRYGKTVALDRITLDVPAGLTTGLIGPDGVGKSSLLALASGARALQTGGVdALGGdmRSRRHRERVCRRIAYM 86
Cdd:cd03296 3 IEVRNVSKRFGDFVALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTI-LFGG--EDATDVPVQERNVGFV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 87 PQGLGknLYPTLSVEENLQFFARL----FGHDAGERRRRIDALTQSTGLFPFLSRPAGKLSGGMKQKLGLCCALIHDPDL 162
Cdd:cd03296 80 FQHYA--LFRHMTVFDNVAFGLRVkprsERPPEAEIRAKVHELLKLVQLDWLADRYPAQLSGGQRQRVALARALAVEPKV 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 505416896 163 LILDEPTTGVDPLARAQFWDLIARIRDERPTMSVIVATAYMDEAQRFDWLIAMDAGRVLATGAPAEL 229
Cdd:cd03296 158 LLLDEPFGALDAKVRKELRRWLRRLHDELHVTTVFVTHDQEEALEVADRVVVMNKGRIEQVGTPDEV 224
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
270-493 |
2.47e-20 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 91.61 E-value: 2.47e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 270 TAIEARGLTMRFGDFTAVDHVSFRIRRGEIFGFLGSNGCGKSTTMKMLTGLLPATEGTAQLFGKevDPKDINTR---RRV 346
Cdd:PRK11231 1 MTLRTENLTVGYGTKRILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDK--PISMLSSRqlaRRL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 347 GYMSQAFSLYSELTVRQnLVLHAR-----LFGVPAAEIDARVDEMARRFGLADIYGMLPDSLPLGMRQRLSLAVAMVHKP 421
Cdd:PRK11231 79 ALLPQHHLTPEGITVRE-LVAYGRspwlsLWGRLSAEDNARVNQAMEQTRINHLADRRLTDLSGGQRQRAFLAMVLAQDT 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 505416896 422 ELLILDEPTSGVDPVARDSFWQLMIDLAR--RDLVTIFistHFMNEAQR-CDRISLMHAGRVLASDSPAELVRAR 493
Cdd:PRK11231 158 PVVLLDEPTTYLDINHQVELMRLMRELNTqgKTVVTVL---HDLNQASRyCDHLVVLANGHVMAQGTPEEVMTPG 229
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
273-503 |
3.35e-20 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 95.24 E-value: 3.35e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 273 EARGLTMRFGDFTAVDHVSFRIRRGEIFGFLGSNGCGKSTTMKMLTGLLPAT--EGTAQLFGKEVDPKDINTRRRVGY-- 348
Cdd:NF040905 3 EMRGITKTFPGVKALDDVNLSVREGEIHALCGENGAGKSTLMKVLSGVYPHGsyEGEILFDGEVCRFKDIRDSEALGIvi 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 349 MSQAFSLYSELTVRQNLVL---HARlFGVpaaeID-----ARVDEMARRFGLADIYGMLPDSLPLGMRQRLSLAVAMVHK 420
Cdd:NF040905 83 IHQELALIPYLSIAENIFLgneRAK-RGV----IDwnetnRRARELLAKVGLDESPDTLVTDIGVGKQQLVEIAKALSKD 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 421 PELLILDEPTSGVDpvARDS--FWQLMIDLARRDLVTIFIStHFMNE-AQRCDRISLMHAGRVLasdspaELVRARGAAT 497
Cdd:NF040905 158 VKLLILDEPTAALN--EEDSaaLLDLLLELKAQGITSIIIS-HKLNEiRRVADSITVLRDGRTI------ETLDCRADEV 228
|
....*.
gi 505416896 498 LEDAFI 503
Cdd:NF040905 229 TEDRII 234
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
277-492 |
4.26e-20 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 91.20 E-value: 4.26e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 277 LTMRFGDFTAVDHVSFRIRRGEIFGFLGSNGCGKSTTMKMLTGLLPATEGTAQLFGKEVD---PKDIntRRRVGYMSQAF 353
Cdd:PRK10253 13 LTLGYGKYTVAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIQhyaSKEV--ARRIGLLAQNA 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 354 SLYSELTVrQNLVLHAR-----LFGVPAAEIDARVDEMARRFGLADIYGMLPDSLPLGMRQRLSLAVAMVHKPELLILDE 428
Cdd:PRK10253 91 TTPGDITV-QELVARGRyphqpLFTRWRKEDEEAVTKAMQATGITHLADQSVDTLSGGQRQRAWIAMVLAQETAIMLLDE 169
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 505416896 429 PTSGVDPVARDSFWQLMIDLARRDLVTIFISTHFMNEAQR-CDRISLMHAGRVLASDSPAELVRA 492
Cdd:PRK10253 170 PTTWLDISHQIDLLELLSELNREKGYTLAAVLHDLNQACRyASHLIALREGKIVAQGAPKEIVTA 234
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
283-491 |
4.42e-20 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 91.76 E-value: 4.42e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 283 DFTAVDHVSFRIRRGEIFGFLGSNGCGKSTTMKMLTGLLPATEGTAQLFGKEVDPKDIN-----TRRRVGYM-----SQA 352
Cdd:PRK13646 19 EHQAIHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVDDITITHKTKDkyirpVRKRIGMVfqfpeSQL 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 353 FslysELTVRQNLVLHARLFGVPAAEIDARVDEMARRFGLA-DIYGMLPDSLPLGMRQRLSLAVAMVHKPELLILDEPTS 431
Cdd:PRK13646 99 F----EDTVEREIIFGPKNFKMNLDEVKNYAHRLLMDLGFSrDVMSQSPFQMSGGQMRKIAIVSILAMNPDIIVLDEPTA 174
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 505416896 432 GVDPVARDSFWQLMIDLARRDLVTIFISTHFMNE-AQRCDRISLMHAGRVLASDSPAELVR 491
Cdd:PRK13646 175 GLDPQSKRQVMRLLKSLQTDENKTIILVSHDMNEvARYADEVIVMKEGSIVSQTSPKELFK 235
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
5-187 |
5.06e-20 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 90.69 E-value: 5.06e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 5 SVVRFSDVSLRYGK----TVALDRITLDVPAGLTTGLIGPDGVGKSSLLALASGARALQTGGVdALGGDmrsrrhrervc 80
Cdd:COG4525 2 SMLTVRHVSVRYPGggqpQPALQDVSLTIESGEFVVALGASGCGKTTLLNLIAGFLAPSSGEI-TLDGV----------- 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 81 rriaymP-QGLGKN---------LYPTLSVEENLQFFARLFGHDAGERRRRIDALTQSTGLFPFLSRPAGKLSGGMKQKL 150
Cdd:COG4525 70 ------PvTGPGADrgvvfqkdaLLPWLNVLDNVAFGLRLRGVPKAERRARAEELLALVGLADFARRRIWQLSGGMRQRV 143
|
170 180 190
....*....|....*....|....*....|....*..
gi 505416896 151 GLCCALIHDPDLLILDEPTTGVDPLARAQFWDLIARI 187
Cdd:COG4525 144 GIARALAADPRFLLMDEPFGALDALTREQMQELLLDV 180
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
14-224 |
5.60e-20 |
|
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: 89.90 E-value: 5.60e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 14 LRYGKTVALDRITLDVPAGLTTGLIGPDGVGKSSLLALASGARALQTGGVDALGGdmrsrrhrervcrrIAYMPqGLGKN 93
Cdd:cd03220 30 GEVGEFWALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVTVRGR--------------VSSLL-GLGGG 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 94 LYPTLSVEENLQFFARLFGHDAGERRRRIDALTQSTGLFPFLSRPAGKLSGGMKQKLGLCCALIHDPDLLILDEPTTGVD 173
Cdd:cd03220 95 FNPELTGRENIYLNGRLLGLSRKEIDEKIDEIIEFSELGDFIDLPVKTYSSGMKARLAFAIATALEPDILLIDEVLAVGD 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 505416896 174 PLARAQFWDLIARIRdeRPTMSVIVATAYMDEAQRF-DWLIAMDAGRVLATG 224
Cdd:cd03220 175 AAFQEKCQRRLRELL--KQGKTVILVSHDPSSIKRLcDRALVLEKGKIRFDG 224
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
119-434 |
5.84e-20 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 95.26 E-value: 5.84e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 119 RRRIDALTQSTGLFPFLSRPAGKLSGGMKQKLGLCCALIHDPDLLILDEPTTGVDPLARAQFWDLIARIRDERPTMSV-- 196
Cdd:PRK13409 190 RGKLDEVVERLGLENILDRDISELSGGELQRVAIAAALLRDADFYFFDEPTSYLDIRQRLNVARLIRELAEGKYVLVVeh 269
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 197 --IVataymdeaqrFDWL---IamdagrVLATGAPA-------ELLARTGCDSLEAAFialLP-ENERRGHKPVKIE--P 261
Cdd:PRK13409 270 dlAV----------LDYLadnV------HIAYGEPGaygvvskPKGVRVGINEYLKGY---LPeENMRIRPEPIEFEerP 330
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 262 LRADARAGTAIEARGLTMRFGDFT-AVDHVSfrIRRGEIFGFLGSNGCGKSTTMKMLTGLLPATEGtaqlfgkevdpkDI 340
Cdd:PRK13409 331 PRDESERETLVEYPDLTKKLGDFSlEVEGGE--IYEGEVIGIVGPNGIGKTTFAKLLAGVLKPDEG------------EV 396
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 341 NTRRRVGYMSQAFSLYSELTVRQNLvlharlfgvpaAEIDARVD------EMARRFGLADIYGMLPDSLPLGMRQRLSLA 414
Cdd:PRK13409 397 DPELKISYKPQYIKPDYDGTVEDLL-----------RSITDDLGssyyksEIIKPLQLERLLDKNVKDLSGGELQRVAIA 465
|
330 340
....*....|....*....|
gi 505416896 415 VAMVHKPELLILDEPTSGVD 434
Cdd:PRK13409 466 ACLSRDADLYLLDEPSAHLD 485
|
|
| type_I_sec_PrtD |
TIGR01842 |
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in ... |
290-482 |
7.40e-20 |
|
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: 94.34 E-value: 7.40e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 290 VSFRIRRGEIFGFLGSNGCGKSTTMKMLTGLLPATEGTAQLFGKEVDPKDINT-RRRVGYMSQAFSLYSElTVRQNLvlh 368
Cdd:TIGR01842 337 ISFSLQAGEALAIIGPSGSGKSTLARLIVGIWPPTSGSVRLDGADLKQWDRETfGKHIGYLPQDVELFPG-TVAENI--- 412
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 369 ARlFG--------VPAAEIdARVDEMARRF--GLADIYGMLPDSLPLGMRQRLSLAVAMVHKPELLILDEPTSGVDPVAR 438
Cdd:TIGR01842 413 AR-FGenadpekiIEAAKL-AGVHELILRLpdGYDTVIGPGGATLSGGQRQRIALARALYGDPKLVVLDEPNSNLDEEGE 490
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 505416896 439 DSFWQLMIDLARRDLVTIFIsTHFMNEAQRCDRISLMHAGRVLA 482
Cdd:TIGR01842 491 QALANAIKALKARGITVVVI-THRPSLLGCVDKILVLQDGRIAR 533
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
272-492 |
8.35e-20 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 90.14 E-value: 8.35e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 272 IEARGLTMRfGDFTAVDHVSFRIRRGEIFGFLGSNGCGKSTTMKMLTGLLPA----TEGTAQLFGKEVDPKDINTRRRVG 347
Cdd:PRK10418 5 IELRNIALQ-AAQPLVHGVSLTLQRGRVLALVGGSGSGKSLTCAAALGILPAgvrqTAGRVLLDGKPVAPCALRGRKIAT 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 348 YMSQAFSLYSEL-TVRQNLVLHARLFGVPAAeiDARVDEMARRFGLAD---IYGMLPDSLPLGMRQRLSLAVAMVHKPEL 423
Cdd:PRK10418 84 IMQNPRSAFNPLhTMHTHARETCLALGKPAD--DATLTAALEAVGLENaarVLKLYPFEMSGGMLQRMMIALALLCEAPF 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 424 LILDEPTSGVDPVARDSFWQLMIDLARRDLVTIFISTHFMNEAQRC-DRISLMHAGRVLASDSPAELVRA 492
Cdd:PRK10418 162 IIADEPTTDLDVVAQARILDLLESIVQKRALGMLLVTHDMGVVARLaDDVAVMSHGRIVEQGDVETLFNA 231
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
286-489 |
9.02e-20 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 90.20 E-value: 9.02e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 286 AVDHVSFRIRRGEIFGFLGSNGCGKSTTMKMLTGLLPATEGTAQLFGKEVDPKDI-NTRRRVGYMSQ-AFSLYSELTVRQ 363
Cdd:PRK13648 24 TLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIFYNNQAITDDNFeKLRKHIGIVFQnPDNQFVGSIVKY 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 364 NLVLHARLFGVPAAEIDARVDEMARRFGLADIYGMLPDSLPLGMRQRLSLAVAMVHKPELLILDEPTSGVDPVARDSFWQ 443
Cdd:PRK13648 104 DVAFGLENHAVPYDEMHRRVSEALKQVDMLERADYEPNALSGGQKQRVAIAGVLALNPSVIILDEATSMLDPDARQNLLD 183
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 505416896 444 LMIDLARRDLVTIFISTHFMNEAQRCDRISLMHAGRVLASDSPAEL 489
Cdd:PRK13648 184 LVRKVKSEHNITIISITHDLSEAMEADHVIVMNKGTVYKEGTPTEI 229
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
22-232 |
1.01e-19 |
|
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: 89.32 E-value: 1.01e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 22 LDRITLDVPAGLTTGLIGPDGVGKSSLLALASGARALQTG-----GVD--ALGGDMRSrrhrervcrrIAYMPQGlgKNL 94
Cdd:cd03299 15 LKNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGkillnGKDitNLPPEKRD----------ISYVPQN--YAL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 95 YPTLSVEENLQFFARLFGHDAGERRRRIDALTQSTGLFPFLSRPAGKLSGGMKQKLGLCCALIHDPDLLILDEPTTGVDP 174
Cdd:cd03299 83 FPHMTVYKNIAYGLKKRKVDKKEIERKVLEIAEMLGIDHLLNRKPETLSGGEQQRVAIARALVVNPKILLLDEPFSALDV 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 505416896 175 LARAQFWDLIARIRDERPTmSVIVATAYMDEAqrfdWLIA-----MDAGRVLATGAPAELLAR 232
Cdd:cd03299 163 RTKEKLREELKKIRKEFGV-TVLHVTHDFEEA----WALAdkvaiMLNGKLIQVGKPEEVFKK 220
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
10-233 |
1.61e-19 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 89.68 E-value: 1.61e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 10 SDVSLRYGKTVALDRITLDVPAGLTTGLIGPDGVGKSSLLALASGARALQTGGVDALGGDMR-SRRHRERVCRRIAYMPQ 88
Cdd:PRK13638 5 SDLWFRYQDEPVLKGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLRPQKGAVLWQGKPLDySKRGLLALRQQVATVFQ 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 89 GLGKNLYPTlSVEENLQFFARLFGHDAGERRRRIDALTQSTGLFPFLSRPAGKLSGGMKQKLGLCCALIHDPDLLILDEP 168
Cdd:PRK13638 85 DPEQQIFYT-DIDSDIAFSLRNLGVPEAEITRRVDEALTLVDAQHFRHQPIQCLSHGQKKRVAIAGALVLQARYLLLDEP 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 505416896 169 TTGVDPLARAQFWDLIARIRDErpTMSVIVATAYMDEAQRF-DWLIAMDAGRVLATGAPAELLART 233
Cdd:PRK13638 164 TAGLDPAGRTQMIAIIRRIVAQ--GNHVIISSHDIDLIYEIsDAVYVLRQGQILTHGAPGEVFACT 227
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
2-232 |
1.84e-19 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 89.69 E-value: 1.84e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 2 NASSVVRFSDVSLRY--GKTVALDRITLDVPAGLTTGLIGPDGVGKSSLLALASGARALQTGGVDaLGGDMRSRRHRERV 79
Cdd:PRK13635 1 MKEEIIRVEHISFRYpdAATYALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTIT-VGGMVLSEETVWDV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 80 CRRIAYMPQGlGKNLYPTLSVEENLQFFARLFGHDAGERRRRIDALTQSTGLFPFLSRPAGKLSGGMKQKLGLCCALIHD 159
Cdd:PRK13635 80 RRQVGMVFQN-PDNQFVGATVQDDVAFGLENIGVPREEMVERVDQALRQVGMEDFLNREPHRLSGGQKQRVAIAGVLALQ 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 505416896 160 PDLLILDEPTTGVDPLARAQFWDLIARIRDERpTMSVIVATAYMDEAQRFDWLIAMDAGRVLATGAPAELLAR 232
Cdd:PRK13635 159 PDIIILDEATSMLDPRGRREVLETVRQLKEQK-GITVLSITHDLDEAAQADRVIVMNKGEILEEGTPEEIFKS 230
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
276-496 |
1.98e-19 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 89.30 E-value: 1.98e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 276 GLTMRFGDFTAVDHVSFRIRRGEIFGFLGSNGCGKSTTMKMLTGLLPATEGTAQLFGKevdPKDINTRRRVGYMSQAFSL 355
Cdd:PRK13638 6 DLWFRYQDEPVLKGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLRPQKGAVLWQGK---PLDYSKRGLLALRQQVATV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 356 YSE-------LTVRQNLVLHARLFGVPAAEIDARVDEM-----ARRFGLADIygmlpDSLPLGMRQRLSLAVAMVHKPEL 423
Cdd:PRK13638 83 FQDpeqqifyTDIDSDIAFSLRNLGVPEAEITRRVDEAltlvdAQHFRHQPI-----QCLSHGQKKRVAIAGALVLQARY 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 505416896 424 LILDEPTSGVDPVARDSfwqlMIDLARRDLVT---IFISTHFMNEA-QRCDRISLMHAGRVLASDSPAElVRARGAA 496
Cdd:PRK13638 158 LLLDEPTAGLDPAGRTQ----MIAIIRRIVAQgnhVIISSHDIDLIyEISDAVYVLRQGQILTHGAPGE-VFACTEA 229
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
270-481 |
2.08e-19 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 89.30 E-value: 2.08e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 270 TAIEARGLTMRFGDFTAVDHVSFRIRRGEIFGFLGSNGCGKSTTMKMLTGLL---PATEGTAQLFGKEVD-----PKDI- 340
Cdd:PRK09984 3 TIIRVEKLAKTFNQHQALHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGLItgdKSAGSHIELLGRTVQregrlARDIr 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 341 NTRRRVGYMSQAFSLYSELTVRQNLVLHArLFGVP---------AAEIDARVDEMARRFGLADIYGMLPDSLPLGMRQRL 411
Cdd:PRK09984 83 KSRANTGYIFQQFNLVNRLSVLENVLIGA-LGSTPfwrtcfswfTREQKQRALQALTRVGMVHFAHQRVSTLSGGQQQRV 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 505416896 412 SLAVAMVHKPELLILDEPTSGVDPVARDSFWQLMIDLARRDLVTIFISTHFMNEAQR-CDRISLMHAGRVL 481
Cdd:PRK09984 162 AIARALMQQAKVILADEPIASLDPESARIVMDTLRDINQNDGITVVVTLHQVDYALRyCERIVALRQGHVF 232
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
286-491 |
2.53e-19 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 89.41 E-value: 2.53e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 286 AVDHVSFRIRRGEIFGFLGSNGCGKSTTMKMLTGLLPATEGTAQLFG---------KEVDPkdinTRRRVGYMSQ--AFS 354
Cdd:PRK13643 21 ALFDIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVTVGDivvsstskqKEIKP----VRKKVGVVFQfpESQ 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 355 LYSElTVRQNLVLHARLFGVPAAEIDARVDEMARRFGLA-DIYGMLPDSLPLGMRQRLSLAVAMVHKPELLILDEPTSGV 433
Cdd:PRK13643 97 LFEE-TVLKDVAFGPQNFGIPKEKAEKIAAEKLEMVGLAdEFWEKSPFELSGGQMRRVAIAGILAMEPEVLVLDEPTAGL 175
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 505416896 434 DPVARDSFWQLMIDLARRDLvTIFISTHFMNE-AQRCDRISLMHAGRVLASDSPAELVR 491
Cdd:PRK13643 176 DPKARIEMMQLFESIHQSGQ-TVVLVTHLMDDvADYADYVYLLEKGHIISCGTPSDVFQ 233
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
272-486 |
2.89e-19 |
|
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C is also known as MRP (multidrug resistance-associated protein). Some of the MRP members have five additional transmembrane segments in their N-terminus, but the function of these additional membrane-spanning domains is not clear. The MRP was found in the multidrug-resistance lung cancer cell in which p-glycoprotein was not overexpressed. MRP exports glutathione by drug stimulation, as well as, certain substrates in conjugated forms with anions, such as glutathione, glucuronate, and sulfate.
Pssm-ID: 213211 [Multi-domain] Cd Length: 221 Bit Score: 87.55 E-value: 2.89e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 272 IEARGLTMRFGD--FTAVDHVSFRIRRGEIFGFLGSNGCGKSTTMKMLTGLLPATEGTAQlfgkeVDPKDINT------R 343
Cdd:cd03244 3 IEFKNVSLRYRPnlPPVLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSIL-----IDGVDISKiglhdlR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 344 RRVGYMSQAFSLYSElTVRQNLvlhaRLFGVPAaeiDARVDEMARRFGLADIYGMLPDSLPL-----------GMRQRLS 412
Cdd:cd03244 78 SRISIIPQDPVLFSG-TIRSNL----DPFGEYS---DEELWQALERVGLKEFVESLPGGLDTvveeggenlsvGQRQLLC 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 505416896 413 LAVAMVHKPELLILDEPTSGVDPvARDSFWQLMIDLARRDlVTIFISTHFMNEAQRCDRISLMHAGRVLASDSP 486
Cdd:cd03244 150 LARALLRKSKILVLDEATASVDP-ETDALIQKTIREAFKD-CTVLTIAHRLDTIIDSDRILVLDKGRVVEFDSP 221
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
6-229 |
3.71e-19 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 88.61 E-value: 3.71e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 6 VVRFSDVSLRYGK------TVALDRITLDVPAGLTTGLIGPDGVGKSSLlALASGARALQTGG---VDALggDMRSRRHR 76
Cdd:PRK13633 4 MIKCKNVSYKYESneesteKLALDDVNLEVKKGEFLVILGRNGSGKSTI-AKHMNALLIPSEGkvyVDGL--DTSDEENL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 77 ERVCRRIAYMPQGLGKNLYPTLsVEENLQFFARLFGHDAGERRRRIDALTQSTGLFPFLSRPAGKLSGGMKQKLGLCCAL 156
Cdd:PRK13633 81 WDIRNKAGMVFQNPDNQIVATI-VEEDVAFGPENLGIPPEEIRERVDESLKKVGMYEYRRHAPHLLSGGQKQRVAIAGIL 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 505416896 157 IHDPDLLILDEPTTGVDPLARAQFWDLIARIRDERpTMSVIVATAYMDEAQRFDWLIAMDAGRVLATGAPAEL 229
Cdd:PRK13633 160 AMRPECIIFDEPTAMLDPSGRREVVNTIKELNKKY-GITIILITHYMEEAVEADRIIVMDSGKVVMEGTPKEI 231
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
277-504 |
3.76e-19 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 88.18 E-value: 3.76e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 277 LTMRFGDFTAVDHVSFRIRRGEIFGFLGSNGCGKSTTMKMLTGLLP------ATEGTAQLFGKEVDPKD-INTRRRVGYM 349
Cdd:PRK14246 16 LYLYINDKAILKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLIEiydskiKVDGKVLYFGKDIFQIDaIKLRKEVGMV 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 350 SQAFSLYSELTVRQNLVLHARLFGVPAA-EIDARVDEMARRFGL-ADIYGML--PDS-LPLGMRQRLSLAVAMVHKPELL 424
Cdd:PRK14246 96 FQQPNPFPHLSIYDNIAYPLKSHGIKEKrEIKKIVEECLRKVGLwKEVYDRLnsPASqLSGGQQQRLTIARALALKPKVL 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 425 ILDEPTSGVDPVARDSFWQLMIDLARRdlVTIFISTHFMNEAQR-CDRISLMHAGRVLASDSPAELVRARGAATLEDAFI 503
Cdd:PRK14246 176 LMDEPTSMIDIVNSQAIEKLITELKNE--IAIVIVSHNPQQVARvADYVAFLYNGELVEWGSSNEIFTSPKNELTEKYVI 253
|
.
gi 505416896 504 G 504
Cdd:PRK14246 254 G 254
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
271-468 |
3.79e-19 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 88.17 E-value: 3.79e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 271 AIEARGLTMRFGDFTAVDHVSFRIRRGEIFGFLGSNGCGKSTTMKMLTGLLP-----ATEGTAQLFGKEVDPKDINT--- 342
Cdd:PRK14258 7 AIKVNNLSFYYDTQKILEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLNRMNElesevRVEGRVEFFNQNIYERRVNLnrl 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 343 RRRVGYMSQAFSLYSeLTVRQNLVLHARLFG-VPAAEIDARVDEMARRFGLAD-IYGMLPDS---LPLGMRQRLSLAVAM 417
Cdd:PRK14258 87 RRQVSMVHPKPNLFP-MSVYDNVAYGVKIVGwRPKLEIDDIVESALKDADLWDeIKHKIHKSaldLSGGQQQRLCIARAL 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 505416896 418 VHKPELLILDEPTSGVDPVARDSFWQLMIDLARRDLVTIFISTHFMNEAQR 468
Cdd:PRK14258 166 AVKPKVLLMDEPCFGLDPIASMKVESLIQSLRLRSELTMVIVSHNLHQVSR 216
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
286-486 |
3.84e-19 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 88.51 E-value: 3.84e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 286 AVDHVSFRIRRGEIFGFLGSNGCGKSTTMKMLTGLLPATEGTAQLFGKEV-DPKDI-NTRRRVGYMSQ-AFSLYSELTVR 362
Cdd:PRK13644 17 ALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLVSGIDTgDFSKLqGIRKLVGIVFQnPETQFVGRTVE 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 363 QNLVLHARLFGVPAAEIDARVDEMARRFGLADIYGMLPDSLPLGMRQRLSLAVAMVHKPELLILDEPTSGVDPVARDSFW 442
Cdd:PRK13644 97 EDLAFGPENLCLPPIEIRKRVDRALAEIGLEKYRHRSPKTLSGGQGQCVALAGILTMEPECLIFDEVTSMLDPDSGIAVL 176
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 505416896 443 QLMIDLARRDLVTIFIsTHFMNEAQRCDRISLMHAGRVLASDSP 486
Cdd:PRK13644 177 ERIKKLHEKGKTIVYI-THNLEELHDADRIIVMDRGKIVLEGEP 219
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
272-492 |
3.95e-19 |
|
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: 92.05 E-value: 3.95e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 272 IEARGLTMRFGD----FTAVDHVSFRIRRGEIFGFLGSNGCGKSTTMKMLTGLLPA----TEGTAQLFGKEV---DPKDI 340
Cdd:COG4172 7 LSVEDLSVAFGQgggtVEAVKGVSFDIAAGETLALVGESGSGKSVTALSILRLLPDpaahPSGSILFDGQDLlglSEREL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 341 NTRR--RVGY-----MSqafSLYSELTV-RQ---NLVLHarlFGVPAAEIDARVDEMARRFGLADIYGMLpDSLP--L-- 405
Cdd:COG4172 87 RRIRgnRIAMifqepMT---SLNPLHTIgKQiaeVLRLH---RGLSGAAARARALELLERVGIPDPERRL-DAYPhqLsg 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 406 GMRQRLSLAVAMVHKPELLILDEPTSGVDPVARDSFWQLMIDL-ARRDLVTIFIsTHFMNEAQR-CDRISLMHAGRVLAS 483
Cdd:COG4172 160 GQRQRVMIAMALANEPDLLIADEPTTALDVTVQAQILDLLKDLqRELGMALLLI-THDLGVVRRfADRVAVMRQGEIVEQ 238
|
....*....
gi 505416896 484 DSPAELVRA 492
Cdd:COG4172 239 GPTAELFAA 247
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
277-506 |
3.97e-19 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 88.10 E-value: 3.97e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 277 LTMRFGDFTAVDHVSFRIRRGEIFGFLGSNGCGKSTTMKMLTGLLPATEGTAQLFGKEV-------------DPKDINT- 342
Cdd:PRK10619 11 LHKRYGEHEVLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNGQTInlvrdkdgqlkvaDKNQLRLl 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 343 RRRVGYMSQAFSLYSELTVRQNlVLHA--RLFGVPAAEIDARVDEMARRFGLAD-IYGMLPDSLPLGMRQRLSLAVAMVH 419
Cdd:PRK10619 91 RTRLTMVFQHFNLWSHMTVLEN-VMEApiQVLGLSKQEARERAVKYLAKVGIDErAQGKYPVHLSGGQQQRVSIARALAM 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 420 KPELLILDEPTSGVDPVARDSFWQLMIDLARRDlVTIFISTHFMNEAQRC-DRISLMHAGRVLASDSPAELVRARGAATL 498
Cdd:PRK10619 170 EPEVLLFDEPTSALDPELVGEVLRIMQQLAEEG-KTMVVVTHEMGFARHVsSHVIFLHQGKIEEEGAPEQLFGNPQSPRL 248
|
....*...
gi 505416896 499 EDAFIGYL 506
Cdd:PRK10619 249 QQFLKGSL 256
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
272-486 |
4.31e-19 |
|
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: 86.70 E-value: 4.31e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 272 IEARGLTMRFG-DFTAVDH-VSFRIRRGEIFGFLGSNGCGKSTTMKMLTGLLPATEGTAqlfgkEVDPKDINT------R 343
Cdd:cd03369 7 IEVENLSVRYApDLPPVLKnVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKI-----EIDGIDISTipledlR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 344 RRVGYMSQAFSLYSElTVRQNLvlharlfgvpaaeidarvdEMARRFGLADIYGMLP-----DSLPLGMRQRLSLAVAMV 418
Cdd:cd03369 82 SSLTIIPQDPTLFSG-TIRSNL-------------------DPFDEYSDEEIYGALRvseggLNLSQGQRQLLCLARALL 141
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 505416896 419 HKPELLILDEPTSGVDpVARDSFWQLMIDLARRDlVTIFISTHFMNEAQRCDRISLMHAGRVLASDSP 486
Cdd:cd03369 142 KRPRVLVLDEATASID-YATDALIQKTIREEFTN-STILTIAHRLRTIIDYDKILVMDAGEVKEYDHP 207
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
15-234 |
4.91e-19 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 89.38 E-value: 4.91e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 15 RYGKTVALDRITLDVPAGLTTGLIGPDGVGKSSLLALASGAraLQ-TGG-VDALGgdmrsrrhrervcrriaYMPQ---- 88
Cdd:COG4586 31 EYREVEAVDDISFTIEPGEIVGFIGPNGAGKSTTIKMLTGI--LVpTSGeVRVLG-----------------YVPFkrrk 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 89 ------GL--G-KN-LYPTLSVEENLQFFARLFGHDAGERRRRIDALTQSTGLFPFLSRPAGKLSGGMKQKLGLCCALIH 158
Cdd:COG4586 92 efarriGVvfGqRSqLWWDLPAIDSFRLLKAIYRIPDAEYKKRLDELVELLDLGELLDTPVRQLSLGQRMRCELAAALLH 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 159 DPDLLILDEPTTGVDPLARAQFWDLIARIRDERPTmSVIVATAYMDE----AQRfdwLIAMDAGRVLATGAPAELLARTG 234
Cdd:COG4586 172 RPKILFLDEPTIGLDVVSKEAIREFLKEYNRERGT-TILLTSHDMDDiealCDR---VIVIDHGRIIYDGSLEELKERFG 247
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
7-224 |
5.72e-19 |
|
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: 86.87 E-value: 5.72e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 7 VRFSDVSLRY--GKTVALDRITLDVPAGLTTGLIGPDGVGKSSLLALASGARALQTGGVDALGGDMRsRRHRERVCRRIA 84
Cdd:cd03245 3 IEFRNVSFSYpnQEIPALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGTDIR-QLDPADLRRNIG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 85 YMPQGlgknlyPTL---SVEENLqffarLFGHDAGERRRRIDALTQStGLFPFLSR-PAG----------KLSGGMKQKL 150
Cdd:cd03245 82 YVPQD------VTLfygTLRDNI-----TLGAPLADDERILRAAELA-GVTDFVNKhPNGldlqigergrGLSGGQRQAV 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 505416896 151 GLCCALIHDPDLLILDEPTTGVDPLARAQFwdlIARIRDERPTMSVIVATAYMDEAQRFDWLIAMDAGRVLATG 224
Cdd:cd03245 150 ALARALLNDPPILLLDEPTSAMDMNSEERL---KERLRQLLGDKTLIIITHRPSLLDLVDRIIVMDSGRIVADG 220
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
268-498 |
6.76e-19 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 87.43 E-value: 6.76e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 268 AGTAIEARGLTMRFGDFTAVDHVSFRIRRGEIFGFLGSNGCGKSTTMKMLTGLLPATEGtaQLFGKEVDPKDINTRRRVg 347
Cdd:PRK11247 9 QGTPLLLNAVSKRYGERTVLNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAG--ELLAGTAPLAEAREDTRL- 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 348 yMSQAFSLYSELTVRQNLVLHARLFGVPAAEidarvdEMARRFGLADIYGMLPDSLPLGMRQRLSLAVAMVHKPELLILD 427
Cdd:PRK11247 86 -MFQDARLLPWKKVIDNVGLGLKGQWRDAAL------QALAAVGLADRANEWPAALSGGQKQRVALARALIHRPGLLLLD 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 505416896 428 EPTSGVDPVARDSFWQLMIDLARRDLVTIFISTHFMNEA-QRCDRISLMHAGRV---LASDSPAElvRARGAATL 498
Cdd:PRK11247 159 EPLGALDALTRIEMQDLIESLWQQHGFTVLLVTHDVSEAvAMADRVLLIEEGKIgldLTVDLPRP--RRRGSARL 231
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
285-471 |
7.32e-19 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 86.76 E-value: 7.32e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 285 TAVDHVsfrIRRGEIFGFLGSNGCGKSTTMKMLTGLLPATEGTAQLFGKEVDPKDINTR-----RRVGYMSQAFSLYSEL 359
Cdd:PRK10584 27 TGVELV---VKRGETIALIGESGSGKSTLLAILAGLDDGSSGEVSLVGQPLHQMDEEARaklraKHVGFVFQSFMLIPTL 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 360 TVRQNLVLHARLFGVPAAEIDARVDEMARRFGLADIYGMLPDSLPLGMRQRLSLAVAMVHKPELLILDEPTSGVDPVARD 439
Cdd:PRK10584 104 NALENVELPALLRGESSRQSRNGAKALLEQLGLGKRLDHLPAQLSGGEQQRVALARAFNGRPDVLFADEPTGNLDRQTGD 183
|
170 180 190
....*....|....*....|....*....|..
gi 505416896 440 SFWQLMIDLARRDLVTIFISTHFMNEAQRCDR 471
Cdd:PRK10584 184 KIADLLFSLNREHGTTLILVTHDLQLAARCDR 215
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
7-229 |
8.44e-19 |
|
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: 86.52 E-value: 8.44e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 7 VRFSDVSLRYGKTVALDRITLDVPAGLTTGLIGPDGVGKSSLLALASGARALQTGGVDALGGDMrsrrhrervcrriaym 86
Cdd:cd03300 1 IELENVSKFYGGFVALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGKDI---------------- 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 87 pQGLGKN------------LYPTLSVEENLQFFARLFGHDAGERRRRIDALTQSTGLFPFLSRPAGKLSGGMKQKLGLCC 154
Cdd:cd03300 65 -TNLPPHkrpvntvfqnyaLFPHLTVFENIAFGLRLKKLPKAEIKERVAEALDLVQLEGYANRKPSQLSGGQQQRVAIAR 143
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 505416896 155 ALIHDPDLLILDEPTTGVDPLARAQFWDLIARIRDERPTMSVIVaTAYMDEAQRF-DWLIAMDAGRVLATGAPAEL 229
Cdd:cd03300 144 ALVNEPKVLLLDEPLGALDLKLRKDMQLELKRLQKELGITFVFV-THDQEEALTMsDRIAVMNKGKIQQIGTPEEI 218
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
2-208 |
9.42e-19 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 87.01 E-value: 9.42e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 2 NASSVVRFSDVSLRYGKTVALDRITLDVPAGLTTGLIGPDGVGKSSLL-------ALASGARAlqTG-----GVDALGGD 69
Cdd:COG1117 7 TLEPKIEVRNLNVYYGDKQALKDINLDIPENKVTALIGPSGCGKSTLLrclnrmnDLIPGARV--EGeilldGEDIYDPD 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 70 M-----RSrrhrervcrRIAYMPQglgK-NLYPTlSVEENLQFFARLFG-HDAGERRRRI-DALTQStGLFP----FLSR 137
Cdd:COG1117 85 VdvvelRR---------RVGMVFQ---KpNPFPK-SIYDNVAYGLRLHGiKSKSELDEIVeESLRKA-ALWDevkdRLKK 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 505416896 138 PAGKLSGGMKQKLglcC---ALIHDPDLLILDEPTTGVDPLARAQFWDLIARIRDErptMSVIVATAYMDEAQR 208
Cdd:COG1117 151 SALGLSGGQQQRL---CiarALAVEPEVLLMDEPTSALDPISTAKIEELILELKKD---YTIVIVTHNMQQAAR 218
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
272-461 |
9.63e-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: 85.49 E-value: 9.63e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 272 IEARGLTMRFGDFTAVDHVSFRIRRGEIFGFLGSNGCGKSTTMKMLTGLLPATEGTAQLFGKEVDPKDINTRRRVGYMSQ 351
Cdd:TIGR01189 1 LAARNLACSRGERMLFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRWNGTPLAEQRDEPHENILYLGH 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 352 AFSLYSELTVRQNLVLHARLFGVPAAEIDARVDEMarrfGLADIYGMLPDSLPLGMRQRLSLAVAMVHKPELLILDEPTS 431
Cdd:TIGR01189 81 LPGLKPELSALENLHFWAAIHGGAQRTIEDALAAV----GLTGFEDLPAAQLSAGQQRRLALARLWLSRRPLWILDEPTT 156
|
170 180 190
....*....|....*....|....*....|
gi 505416896 432 GVDPVARDSFWQLMIDLARRDLVTIfISTH 461
Cdd:TIGR01189 157 ALDKAGVALLAGLLRAHLARGGIVL-LTTH 185
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
283-489 |
1.09e-18 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 87.76 E-value: 1.09e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 283 DFTAVDHVSFRIRRGEIFGFLGSNGCGKSTTMKMLTGLLpATEGTAQLFGKEVDPKDI-------NTRRRVGYMSQ--AF 353
Cdd:PRK13645 23 EFKALNNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGLI-ISETGQTIVGDYAIPANLkkikevkRLRKEIGLVFQfpEY 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 354 SLYSElTVRQNLVLHARLFGVPAAEIDARVDEMARRFGLADIYGML-PDSLPLGMRQRLSLAVAMVHKPELLILDEPTSG 432
Cdd:PRK13645 102 QLFQE-TIEKDIAFGPVNLGENKQEAYKKVPELLKLVQLPEDYVKRsPFELSGGQKRRVALAGIIAMDGNTLVLDEPTGG 180
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 505416896 433 VDPVARDSFWQLMIDLARRDLVTIFISTHFMNEAQR-CDRISLMHAGRVLASDSPAEL 489
Cdd:PRK13645 181 LDPKGEEDFINLFERLNKEYKKRIIMVTHNMDQVLRiADEVIVMHEGKVISIGSPFEI 238
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
272-459 |
1.24e-18 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 88.10 E-value: 1.24e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 272 IEARGLT----MRFGDFT------AVDHVSFRIRRGEIFGFLGSNGCGKSTTMKMLTGLLPATEGTAQLFGKEV---DPK 338
Cdd:PRK11308 6 LQAIDLKkhypVKRGLFKperlvkALDGVSFTLERGKTLAVVGESGCGKSTLARLLTMIETPTGGELYYQGQDLlkaDPE 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 339 DINTRRR-VGYMSQafSLYSELTVRQN--------LVLHARLfgvPAAEIDARVDEMARRFGL-ADIYGMLPDSLPLGMR 408
Cdd:PRK11308 86 AQKLLRQkIQIVFQ--NPYGSLNPRKKvgqileepLLINTSL---SAAERREKALAMMAKVGLrPEHYDRYPHMFSGGQR 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 505416896 409 QRLSLAVAMVHKPELLILDEPTSGVDPVARDSFWQLMIDLaRRDLVT--IFIS 459
Cdd:PRK11308 161 QRIAIARALMLDPDVVVADEPVSALDVSVQAQVLNLMMDL-QQELGLsyVFIS 212
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
4-215 |
1.27e-18 |
|
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family transporter in which each gene contains an N-terminal membrane-spanning domain (pfam00664) and a C-terminal ATP-binding domain (pfam00005). In E. coli these genes were discovered as mutants which caused the terminal heme-copper oxidase complex cytochrome bd to fail to assemble. Recent work has shown that the transporter is involved in export of redox-active thiol compounds such as cysteine and glutathione. The linkage to assembly of the cytochrome bd complex is further supported by the conserved operon structure found outside the gammaproteobacteria (cydABCD) containing both the transporter and oxidase genes components. The genes used as the seed members for this model are all either found in the gammproteobacterial context or the CydABCD context. All members of this family scoring above trusted at the time of its creation were from genomes which encode a cytochrome bd complex. Unfortunately, the gene symbol nomenclature adopted based on this operon in B. subtilis assigns cydC to the third gene in the operon where this gene is actually homologous to the E. coli cydD gene. We have chosen to name all homologs in this family in accordance with the precedence of publication of the E. coli name, CydD
Pssm-ID: 274323 [Multi-domain] Cd Length: 529 Bit Score: 90.42 E-value: 1.27e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 4 SSVVRFSDVSLRY-GKTVALDRITLDVPAGLTTGLIGPDGVGKSSLLALASGArALQTGGVDALGGDMRSRRHRERVCRR 82
Cdd:TIGR02857 319 ASSLEFSGVSVAYpGRRPALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGF-VDPTEGSIAVNGVPLADADADSWRDQ 397
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 83 IAYMPQglgknlYPTL---SVEENLQFfARLFGHDAGERR--RRIDALTQSTGLFPFLSRPAGK----LSGGMKQKLGLC 153
Cdd:TIGR02857 398 IAWVPQ------HPFLfagTIAENIRL-ARPDASDAEIREalERAGLDEFVAALPQGLDTPIGEggagLSGGQAQRLALA 470
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 505416896 154 CALIHDPDLLILDEPTTGVDPLARAQFWDLIARIRDERptmSVIVATAYMDEAQRFDWLIAM 215
Cdd:TIGR02857 471 RAFLRDAPLLLLDEPTAHLDAETEAEVLEALRALAQGR---TVLLVTHRLALAALADRIVVL 529
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
271-491 |
1.30e-18 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 88.60 E-value: 1.30e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 271 AIEARGLTMRFGDFTAVDHVSFRIRRGEIFGFLGSNGCGKSTTMKMLTGLLPATEGTAQLFGKEVD---PKDintrRRVG 347
Cdd:PRK10851 2 SIEIANIKKSFGRTQVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFHGTDVSrlhARD----RKVG 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 348 YMSQAFSLYSELTVRQNLVlharlFGVP---------AAEIDARVD---EMARRFGLADIYgmlPDSLPLGMRQRLSLAV 415
Cdd:PRK10851 78 FVFQHYALFRHMTVFDNIA-----FGLTvlprrerpnAAAIKAKVTqllEMVQLAHLADRY---PAQLSGGQKQRVALAR 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 416 AMVHKPELLILDEPTSGVDPVARDSF--W--QLMIDLarrDLVTIFIsTHFMNEAQR-CDRISLMHAGRVLASDSPAELV 490
Cdd:PRK10851 150 ALAVEPQILLLDEPFGALDAQVRKELrrWlrQLHEEL---KFTSVFV-THDQEEAMEvADRVVVMSQGNIEQAGTPDQVW 225
|
.
gi 505416896 491 R 491
Cdd:PRK10851 226 R 226
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
15-231 |
1.59e-18 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 85.85 E-value: 1.59e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 15 RYGKTVALDRITLDVPAGLTTGLIGPDGVGKSS-------LLALASGARALqtGGVD---------ALGGdmrsrrhrer 78
Cdd:COG1137 12 SYGKRTVVKDVSLEVNQGEIVGLLGPNGAGKTTtfymivgLVKPDSGRIFL--DGEDithlpmhkrARLG---------- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 79 vcrrIAYMPQ------GLgknlyptlSVEENLQFFARLFGHDAGERRRRIDALTQSTGLFPFLSRPAGKLSGGMKQKLGL 152
Cdd:COG1137 80 ----IGYLPQeasifrKL--------TVEDNILAVLELRKLSKKEREERLEELLEEFGITHLRKSKAYSLSGGERRRVEI 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 153 CCALIHDPDLLILDEPTTGVDPLARAQFWDLIARIRDE-----------RPTMSvIVATAYMdeaqrfdwliaMDAGRVL 221
Cdd:COG1137 148 ARALATNPKFILLDEPFAGVDPIAVADIQKIIRHLKERgigvlitdhnvRETLG-ICDRAYI-----------ISEGKVL 215
|
250
....*....|
gi 505416896 222 ATGAPAELLA 231
Cdd:COG1137 216 AEGTPEEILN 225
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
2-230 |
1.67e-18 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 86.38 E-value: 1.67e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 2 NASSVVRFSDVSLRYGKTVALDRITLDVPAGLTTGLIGPDGVGKSSLLALASGARALQTGGVdALGGDMRSRRHRERVCR 81
Cdd:PRK10575 7 HSDTTFALRNVSFRVPGRTLLHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEI-LLDAQPLESWSSKAFAR 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 82 RIAYMPQGLGKNlyPTLSVEEnLQFFARLFGHDA-----GERRRRIDALTQSTGLFPFLSRPAGKLSGGMKQKLGLCCAL 156
Cdd:PRK10575 86 KVAYLPQQLPAA--EGMTVRE-LVAIGRYPWHGAlgrfgAADREKVEEAISLVGLKPLAHRLVDSLSGGERQRAWIAMLV 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 505416896 157 IHDPDLLILDEPTTGVDPLARAQFWDLIARIRDERpTMSVIVATAYMDEAQRF-DWLIAMDAGRVLATGAPAELL 230
Cdd:PRK10575 163 AQDSRCLLLDEPTSALDIAHQVDVLALVHRLSQER-GLTVIAVLHDINMAARYcDYLVALRGGEMIAQGTPAELM 236
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
280-479 |
1.88e-18 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 85.54 E-value: 1.88e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 280 RFGDFTAVDHVSFRIRRGEIFGFLGSNGCGKSTTMKMLTGLLPATEGTAqLFgkevDPKDINT------RRRVGYMSQAF 353
Cdd:PRK10247 16 LAGDAKILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTL-LF----EGEDISTlkpeiyRQQVSYCAQTP 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 354 SLYSElTVRQNLVLHARLFGVpAAEIDARVDEMArRFGLADiyGMLPDS---LPLGMRQRLSLAVAMVHKPELLILDEPT 430
Cdd:PRK10247 91 TLFGD-TVYDNLIFPWQIRNQ-QPDPAIFLDDLE-RFALPD--TILTKNiaeLSGGEKQRISLIRNLQFMPKVLLLDEIT 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 505416896 431 SGVDPVARDSFWQLMIDLARRDLVTIFISTHFMNEAQRCDR-ISLM-HAGR 479
Cdd:PRK10247 166 SALDESNKHNVNEIIHRYVREQNIAVLWVTHDKDEINHADKvITLQpHAGE 216
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
6-232 |
2.12e-18 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 86.33 E-value: 2.12e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 6 VVRFSDVSLRYGK-TVALDRITLDVPAGLTTGLIGPDGVGKSSLLALASGARALQTGGVDALGGDMrSRRHRERVCRRIA 84
Cdd:PRK13647 4 IIEVEDLHFRYKDgTKALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGREV-NAENEKWVRSKVG 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 85 YMPQGLGKNLYpTLSVEENLQFFARLFGHDAGERRRRIDALTQSTGLFPFLSRPAGKLSGGMKQKLGLCCALIHDPDLLI 164
Cdd:PRK13647 83 LVFQDPDDQVF-SSTVWDDVAFGPVNMGLDKDEVERRVEEALKAVRMWDFRDKPPYHLSYGQKKRVAIAGVLAMDPDVIV 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 505416896 165 LDEPTTGVDPLARAQFWDLIARIRDERPTmsVIVATAYMD-EAQRFDWLIAMDAGRVLATGAPaELLAR 232
Cdd:PRK13647 162 LDEPMAYLDPRGQETLMEILDRLHNQGKT--VIVATHDVDlAAEWADQVIVLKEGRVLAEGDK-SLLTD 227
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
11-232 |
2.35e-18 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 87.89 E-value: 2.35e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 11 DVSLRYGKTVALDRITLDVPAGLTTGLIGPDGVGKSSLLALASGaraLQT--------GGVDALG----GDMRsrrhrer 78
Cdd:COG1118 7 NISKRFGSFTLLDDVSLEIASGELVALLGPSGSGKTTLLRIIAG---LETpdsgrivlNGRDLFTnlppRERR------- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 79 vcrrIAYMPQglgkN--LYPTLSVEENLQFFARLFGHDAGERRRRIDALTQSTGLFPFLSRPAGKLSGGMKQKLGLCCAL 156
Cdd:COG1118 77 ----VGFVFQ----HyaLFPHMTVAENIAFGLRVRPPSKAEIRARVEELLELVQLEGLADRYPSQLSGGQRQRVALARAL 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 505416896 157 IHDPDLLILDEPTTGVDPLARAQFWDLIARIRDERPTMSVIVaTAYMDEAQRF-DWLIAMDAGRVLATGAPAELLAR 232
Cdd:COG1118 149 AVEPEVLLLDEPFGALDAKVRKELRRWLRRLHDELGGTTVFV-THDQEEALELaDRVVVMNQGRIEQVGTPDEVYDR 224
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
271-466 |
3.19e-18 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 85.52 E-value: 3.19e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 271 AIEARGLTMRFGDFTAVDHVSFRIRRGEIFGFLGSNGCGKSTTMKMLTGLLPATEGTAQLFGKEVDpkDINTRRRVGYMS 350
Cdd:PRK11248 1 MLQISHLYADYGGKPALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDGKPVE--GPGAERGVVFQN 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 351 QAfsLYSELTVRQNLVLHARLFGVPAAEIDARVDEMARRFGLADIYGMLPDSLPLGMRQRLSLAVAMVHKPELLILDEPT 430
Cdd:PRK11248 79 EG--LLPWRNVQDNVAFGLQLAGVEKMQRLEIAHQMLKKVGLEGAEKRYIWQLSGGQRQRVGIARALAANPQLLLLDEPF 156
|
170 180 190
....*....|....*....|....*....|....*.
gi 505416896 431 SGVDPVARDSFWQLMIDLARRDLVTIFISTHFMNEA 466
Cdd:PRK11248 157 GALDAFTREQMQTLLLKLWQETGKQVLLITHDIEEA 192
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
7-229 |
4.48e-18 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 87.39 E-value: 4.48e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 7 VRFSDVSLRYGKTVALDRITLDVPAGLTTGLIGPDGVGKSSLLALASGARALQTGgvDALGGDMRsrrhrervCRRIAYM 86
Cdd:PRK11000 4 VTLRNVTKAYGDVVISKDINLDIHEGEFVVFVGPSGCGKSTLLRMIAGLEDITSG--DLFIGEKR--------MNDVPPA 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 87 PQGLGK-----NLYPTLSVEENLQFFARLFGHDAGERRRRIDALTQSTGLFPFLSRPAGKLSGGMKQKLGLCCALIHDPD 161
Cdd:PRK11000 74 ERGVGMvfqsyALYPHLSVAENMSFGLKLAGAKKEEINQRVNQVAEVLQLAHLLDRKPKALSGGQRQRVAIGRTLVAEPS 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 162 LLILDEPTTGVDPLARAQFWDLIARI-RDERPTMsvIVATAYMDEAQRF-DWLIAMDAGRVLATGAPAEL 229
Cdd:PRK11000 154 VFLLDEPLSNLDAALRVQMRIEISRLhKRLGRTM--IYVTHDQVEAMTLaDKIVVLDAGRVAQVGKPLEL 221
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
290-502 |
4.70e-18 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 84.60 E-value: 4.70e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 290 VSFRIRRGEIFGFLGSNGCGKSTTMKMLTGLLPAtEGTAQLFGKEVDPKDINT--RRRvGYMSQAFSLYSELTVRQNLVL 367
Cdd:PRK03695 15 LSAEVRAGEILHLVGPNGAGKSTLLARMAGLLPG-SGSIQFAGQPLEAWSAAElaRHR-AYLSQQQTPPFAMPVFQYLTL 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 368 HaRLFGVPAAEIDARVDEMARRFGLADIYGMLPDSLPLGMRQRLSLAVAM--VHK---PE--LLILDEPTSGVDPVARDS 440
Cdd:PRK03695 93 H-QPDKTRTEAVASALNEVAEALGLDDKLGRSVNQLSGGEWQRVRLAAVVlqVWPdinPAgqLLLLDEPMNSLDVAQQAA 171
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 505416896 441 FWQLMIDLARRDLvTIFISTHFMNE-AQRCDRISLMHAGRVLASDSPAELVRARgaaTLEDAF 502
Cdd:PRK03695 172 LDRLLSELCQQGI-AVVMSSHDLNHtLRHADRVWLLKQGKLLASGRRDEVLTPE---NLAQVF 230
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
7-248 |
5.06e-18 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 85.84 E-value: 5.06e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 7 VRFSDVSLRYGK-----TVALDRITLDVPAGLTTGLIGPDGVGKSSLLALASGAraLQ-TGGVDALGGDMRSrrhrervc 80
Cdd:PRK13634 3 ITFQKVEHRYQYktpfeRRALYDVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGL--LQpTSGTVTIGERVIT-------- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 81 rriaymPQGLGKNLYPTL-----------------SVEENLQFFARLFGHDAGERRRRIDALTQSTGLFP-FLSRPAGKL 142
Cdd:PRK13634 73 ------AGKKNKKLKPLRkkvgivfqfpehqlfeeTVEKDICFGPMNFGVSEEDAKQKAREMIELVGLPEeLLARSPFEL 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 143 SGGMKQKLGLCCALIHDPDLLILDEPTTGVDPLARAQFWDLIARIRDERpTMSVIVATAYMDEAQRF-DWLIAMDAGRVL 221
Cdd:PRK13634 147 SGGQMRRVAIAGVLAMEPEVLVLDEPTAGLDPKGRKEMMEMFYKLHKEK-GLTTVLVTHSMEDAARYaDQIVVMHKGTVF 225
|
250 260
....*....|....*....|....*...
gi 505416896 222 ATGAPAELLARTgcDSLEAafIAL-LPE 248
Cdd:PRK13634 226 LQGTPREIFADP--DELEA--IGLdLPE 249
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
283-495 |
5.15e-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: 5.15e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 283 DFTAVDHVSFRIRRGEIFGFLGSNGCGKSTTMKMLTGLLPATEGTAQLFGKEVDPKDINT-RRRVGYMSQAFSLYSElTV 361
Cdd:cd03253 13 GRPVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDGQDIREVTLDSlRRAIGVVPQDTVLFND-TI 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 362 RQNLvlharLFGVPAAEiDARVDEMARRFGLADIYGMLPDS-----------LPLGMRQRLSLAVAMVHKPELLILDEPT 430
Cdd:cd03253 92 GYNI-----RYGRPDAT-DEEVIEAAKAAQIHDKIMRFPDGydtivgerglkLSGGEKQRVAIARAILKNPPILLLDEAT 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 505416896 431 SGVDPVARDSFWQLMIDLARRDlVTIFIsTHFMNEAQRCDRISLMHAGRVLASDSPAELVRARGA 495
Cdd:cd03253 166 SALDTHTEREIQAALRDVSKGR-TTIVI-AHRLSTIVNADKIIVLKDGRIVERGTHEELLAKGGL 228
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
282-504 |
5.93e-18 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 86.82 E-value: 5.93e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 282 GDFTAVDHVSFRIRRGEIFGFLGSNGCGKSTTMKMLTGLLPATEGTAQLFGK---EVDPKDintrRRVGYMSQAFSLYSE 358
Cdd:PRK11650 15 GKTQVIKGIDLDVADGEFIVLVGPSGCGKSTLLRMVAGLERITSGEIWIGGRvvnELEPAD----RDIAMVFQNYALYPH 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 359 LTVRQNLVLHARLFGVPAAEIDARVDEMARRFGLADIYGMLPDSLPLGMRQRLSLAVAMVHKPELLILDEPTSGVDPVAR 438
Cdd:PRK11650 91 MSVRENMAYGLKIRGMPKAEIEERVAEAARILELEPLLDRKPRELSGGQRQRVAMGRAIVREPAVFLFDEPLSNLDAKLR 170
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 439 DsfwQLMID---LARRDLVTIFISTHFMNEAQR-CDRISLMHAGRVLASDSPAElVRARGAATLEDAFIG 504
Cdd:PRK11650 171 V---QMRLEiqrLHRRLKTTSLYVTHDQVEAMTlADRVVVMNGGVAEQIGTPVE-VYEKPASTFVASFIG 236
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
11-185 |
6.30e-18 |
|
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein encoded by ccmA in bacteria. An exception is, an arabidopsis protein. Quite likely this is encoded by an organelle. Bacterial c-type cytocromes are located on the periplasmic side of the cytoplasmic membrane. Several gene products encoded in a locus designated as 'ccm' are implicated in the transport and assembly of the functional cytochrome C. This cluster includes genes: ccmA;B;C;D;E;F;G and H. The posttranslational pathway includes the transport of heme moiety, the secretion of the apoprotein and the covalent attachment of the heme with the apoprotein. The proteins ccmA and B represent an ABC transporter; ccmC and D participate in heme transfer to ccmE, which function as a periplasmic heme chaperone. The presence of ccmF, G and H is suggested to be obligatory for the final functional assembly of cytochrome c. [Protein fate, Protein and peptide secretion and trafficking, Transport and binding proteins, Other]
Pssm-ID: 273491 [Multi-domain] Cd Length: 198 Bit Score: 83.18 E-value: 6.30e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 11 DVSLRYGKTVALDRITLDVPAGLTTGLIGPDGVGKSSLLALASGARALQTGGVDALGGDmrSRRHRERVCRRIAYMpqGL 90
Cdd:TIGR01189 5 NLACSRGERMLFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRWNGTP--LAEQRDEPHENILYL--GH 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 91 GKNLYPTLSVEENLQFFARLFGhdaGERRRRIDALTQsTGLFPFLSRPAGKLSGGMKQKLGLCCALIHDPDLLILDEPTT 170
Cdd:TIGR01189 81 LPGLKPELSALENLHFWAAIHG---GAQRTIEDALAA-VGLTGFEDLPAAQLSAGQQRRLALARLWLSRRPLWILDEPTT 156
|
170
....*....|....*
gi 505416896 171 GVDPLARAQFWDLIA 185
Cdd:TIGR01189 157 ALDKAGVALLAGLLR 171
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
276-480 |
6.76e-18 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 84.74 E-value: 6.76e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 276 GLTMRFGDFTAVDHVSFRIRRGEIFGFLGSNGCGKSTTMKMLTGLLPATEGT--------AQL-------FGKEVD---- 336
Cdd:PRK10419 17 GLSGKHQHQTVLNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNvswrgeplAKLnraqrkaFRRDIQmvfq 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 337 --PKDINTRRRVGYMsqafslyseltVRQNLvlhARLFGVPAAEIDARVDEMARRFGLAD-IYGMLPDSLPLGMRQRLSL 413
Cdd:PRK10419 97 dsISAVNPRKTVREI-----------IREPL---RHLLSLDKAERLARASEMLRAVDLDDsVLDKRPPQLSGGQLQRVCL 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 505416896 414 AVAMVHKPELLILDEPTSGVDPVARDSFWQLMIDL-ARRDLVTIFIsTHFMNEAQR-CDRISLMHAGRV 480
Cdd:PRK10419 163 ARALAVEPKLLILDEAVSNLDLVLQAGVIRLLKKLqQQFGTACLFI-THDLRLVERfCQRVMVMDNGQI 230
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
10-275 |
7.08e-18 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 87.20 E-value: 7.08e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 10 SDVSLRYGKTVALDRITLDVPAGLTTGLIGPDGVGKSSLLALASGARALQTGGVdALGGDMRSRRHRERVCRRIAYMPQg 89
Cdd:PRK09536 7 SDLSVEFGDTTVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTV-LVAGDDVEALSARAASRRVASVPQ- 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 90 lGKNLYPTLSVEENLQF-----FARLFGHDAGERRRRIDALTQsTGLFPFLSRPAGKLSGGMKQKLGLCCALIHDPDLLI 164
Cdd:PRK09536 85 -DTSLSFEFDVRQVVEMgrtphRSRFDTWTETDRAAVERAMER-TGVAQFADRPVTSLSGGERQRVLLARALAQATPVLL 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 165 LDEPTTGVDPLARAQFWDLIARIRDERPTmsVIVATAYMDEAQRF-DWLIAMDAGRVLATGAPAELLArtgCDSLEAAFI 243
Cdd:PRK09536 163 LDEPTASLDINHQVRTLELVRRLVDDGKT--AVAAIHDLDLAARYcDELVLLADGRVRAAGPPADVLT---ADTLRAAFD 237
|
250 260 270
....*....|....*....|....*....|..
gi 505416896 244 ALLPENERRGHKPVKIEPLRADARAGTAIEAR 275
Cdd:PRK09536 238 ARTAVGTDPATGAPTVTPLPDPDRTEAAADTR 269
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
272-489 |
7.94e-18 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 87.80 E-value: 7.94e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 272 IEARGLTMRFGDFTAVDHVSFRIRRGEIFGFLGSNGCGKSTTMKMLTGLLPATEGTAQLFGKEVDPKDINTRRRVG-YM- 349
Cdd:PRK15439 12 LCARSISKQYSGVEVLKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIGGNPCARLTPAKAHQLGiYLv 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 350 SQAFSLYSELTVRQNLvlharLFGVPAAEID-ARVDEMARRFGLADIYGMLPDSLPLGMRQRLSLAVAMVHKPELLILDE 428
Cdd:PRK15439 92 PQEPLLFPNLSVKENI-----LFGLPKRQASmQKMKQLLAALGCQLDLDSSAGSLEVADRQIVEILRGLMRDSRILILDE 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 505416896 429 PTSGVDPVARDSFWQLMIDLARRDLVTIFIStHFMNEA-QRCDRISLMHAGRVLASDSPAEL 489
Cdd:PRK15439 167 PTASLTPAETERLFSRIRELLAQGVGIVFIS-HKLPEIrQLADRISVMRDGTIALSGKTADL 227
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
5-232 |
8.24e-18 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 84.19 E-value: 8.24e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 5 SVVRFSDVSLRYGKTVALDRITLDVPAGLTTGLIGPDGVGKSSLL-------ALASGARAlqTGGVDALGGDM--RSRRH 75
Cdd:PRK14247 2 NKIEIRDLKVSFGQVEVLDGVNLEIPDNTITALMGPSGSGKSTLLrvfnrliELYPEARV--SGEVYLDGQDIfkMDVIE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 76 RERVCRRIAYMPqglgkNLYPTLSVEENLQFFARL--FGHDAGERRRRIDALTQSTGLFP----FLSRPAGKLSGGMKQK 149
Cdd:PRK14247 80 LRRRVQMVFQIP-----NPIPNLSIFENVALGLKLnrLVKSKKELQERVRWALEKAQLWDevkdRLDAPAGKLSGGQQQR 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 150 LGLCCALIHDPDLLILDEPTTGVDPLARAQFWDLIARIRDErptMSVIVATAYMDEAQRF-DWLIAMDAGRVLATGAPAE 228
Cdd:PRK14247 155 LCIARALAFQPEVLLADEPTANLDPENTAKIESLFLELKKD---MTIVLVTHFPQQAARIsDYVAFLYKGQIVEWGPTRE 231
|
....
gi 505416896 229 LLAR 232
Cdd:PRK14247 232 VFTN 235
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
10-480 |
8.31e-18 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 87.86 E-value: 8.31e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 10 SDVSLRYGKTVALDRITLDVPAGLTTGLIGPDGVGKSSLLALASGARALQTGGVDALGGDMRSRRHRERVCRRIAYMPQG 89
Cdd:PRK10982 2 SNISKSFPGVKALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEIDFKSSKEALENGISMVHQE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 90 LgkNLYPTLSVEENL---QFFARLFGHDAGERRRRIDALTQSTGLFPFLSRPAGKLSGGMKQKLGLCCALIHDPDLLILD 166
Cdd:PRK10982 82 L--NLVLQRSVMDNMwlgRYPTKGMFVDQDKMYRDTKAIFDELDIDIDPRAKVATLSVSQMQMIEIAKAFSYNAKIVIMD 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 167 EPTTGVDPLARAQFWDLIARIRDErpTMSVIVATAYMDEA-QRFDWLIAMDAGRVLATgapaELLARTGCDSLeaafIAL 245
Cdd:PRK10982 160 EPTSSLTEKEVNHLFTIIRKLKER--GCGIVYISHKMEEIfQLCDEITILRDGQWIAT----QPLAGLTMDKI----IAM 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 246 LPENERRGHKPVKI-EPlradarAGTAIEARGLTMRfgDFTAVDHVSFRIRRGEIFGFLGSNGCGKSTTMKMLTGLLPAT 324
Cdd:PRK10982 230 MVGRSLTQRFPDKEnKP------GEVILEVRNLTSL--RQPSIRDVSFDLHKGEILGIAGLVGAKRTDIVETLFGIREKS 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 325 EGTAQLFGKEVDPKDINTRrrvgyMSQAFSLYSEltVRQNLVLHARLfGVPAAEIDARVDEMARRFGLADIYGMLPD--- 401
Cdd:PRK10982 302 AGTITLHGKKINNHNANEA-----INHGFALVTE--ERRSTGIYAYL-DIGFNSLISNIRNYKNKVGLLDNSRMKSDtqw 373
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 402 -----------------SLPLGMRQRLSLAVAMVHKPELLILDEPTSGVDPVARDSFWQLMIDLARRDLVTIFISTHFMN 464
Cdd:PRK10982 374 vidsmrvktpghrtqigSLSGGNQQKVIIGRWLLTQPEILMLDEPTRGIDVGAKFEIYQLIAELAKKDKGIIIISSEMPE 453
|
490
....*....|....*.
gi 505416896 465 EAQRCDRISLMHAGRV 480
Cdd:PRK10982 454 LLGITDRILVMSNGLV 469
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
4-232 |
8.94e-18 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 84.90 E-value: 8.94e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 4 SSVVRFSDVSLRYGK-TVALDRITLDVPAGLTTGLIGPDGVGKSSLLALASGARALQTGGVDALGGDMR-SRRHRERVCR 81
Cdd:PRK13636 3 DYILKVEELNYNYSDgTHALKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGKPIDySRKGLMKLRE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 82 RIAYMPQGLGKNLYpTLSVEENLQFFARLFGHDAGERRRRIDALTQSTGLFPFLSRPAGKLSGGMKQKLGLCCALIHDPD 161
Cdd:PRK13636 83 SVGMVFQDPDNQLF-SASVYQDVSFGAVNLKLPEDEVRKRVDNALKRTGIEHLKDKPTHCLSFGQKKRVAIAGVLVMEPK 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 505416896 162 LLILDEPTTGVDPLARAQFWDLIARIRDERpTMSVIVATAYMDEAQRF-DWLIAMDAGRVLATGAPAELLAR 232
Cdd:PRK13636 162 VLVLDEPTAGLDPMGVSEIMKLLVEMQKEL-GLTIIIATHDIDIVPLYcDNVFVMKEGRVILQGNPKEVFAE 232
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
7-200 |
9.23e-18 |
|
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: 83.23 E-value: 9.23e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 7 VRFSDVSLRY-GKTVALDRITLDVPAGLTTGLIGPDGVGKSSLLALASGARALQTGGVDALGGDMrsrrhRERVCRRIAY 85
Cdd:cd03292 1 IEFINVTKTYpNGTAALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQDV-----SDLRGRAIPY 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 86 MPQGLG-----KNLYPTLSVEENLQFFARLFGHDAGERRRRIDALTQSTGLFPFLSRPAGKLSGGMKQKLGLCCALIHDP 160
Cdd:cd03292 76 LRRKIGvvfqdFRLLPDRNVYENVAFALEVTGVPPREIRKRVPAALELVGLSHKHRALPAELSGGEQQRVAIARAIVNSP 155
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 505416896 161 DLLILDEPTTGVDPLARAQFWDLIARIRDERPTmsVIVAT 200
Cdd:cd03292 156 TILIADEPTGNLDPDTTWEIMNLLKKINKAGTT--VVVAT 193
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
272-461 |
9.25e-18 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 83.00 E-value: 9.25e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 272 IEARGLTMRFGDFTAVDHVSFRIRRGEIFGFLGSNGCGKSTTMKMLTGLLPATEGTAQLFGKEVDpkDINTRRRVGYMSQ 351
Cdd:PRK13539 3 LEGEDLACVRGGRVLFSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDGGDID--DPDVAEACHYLGH 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 352 AFSLYSELTVRQNLVLHARLFGVPAAEIDARVDemarRFGLADI----YGMLPDslplGMRQRLSLAVAMVHKPELLILD 427
Cdd:PRK13539 81 RNAMKPALTVAENLEFWAAFLGGEELDIAAALE----AVGLAPLahlpFGYLSA----GQKRRVALARLLVSNRPIWILD 152
|
170 180 190
....*....|....*....|....*....|....
gi 505416896 428 EPTSGVDPVARDSFWQLMIDLARRDlVTIFISTH 461
Cdd:PRK13539 153 EPTAALDAAAVALFAELIRAHLAQG-GIVIAATH 185
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
6-251 |
1.45e-17 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 83.88 E-value: 1.45e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 6 VVRFSDVSLRYGK-TVALDRITLDVPAGLTTGLIGPDGVGKSSLLALASGARALQTG-----GVDAlgGDMRSRRHRERV 79
Cdd:PRK13644 1 MIRLENVSYSYPDgTPALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGkvlvsGIDT--GDFSKLQGIRKL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 80 CRRIAYMP--QGLGKnlyptlSVEENLQFFARLFGHDAGERRRRIDALTQSTGLFPFLSRPAGKLSGGMKQKLGLCCALI 157
Cdd:PRK13644 79 VGIVFQNPetQFVGR------TVEEDLAFGPENLCLPPIEIRKRVDRALAEIGLEKYRHRSPKTLSGGQGQCVALAGILT 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 158 HDPDLLILDEPTTGVDPLARAQFWDLIARIRDERPTmsVIVATAYMDEAQRFDWLIAMDAGRVLATGAPAELLARTGCDS 237
Cdd:PRK13644 153 MEPECLIFDEVTSMLDPDSGIAVLERIKKLHEKGKT--IVYITHNLEELHDADRIIVMDRGKIVLEGEPENVLSDVSLQT 230
|
250
....*....|....
gi 505416896 238 LEAAFIALLPENER 251
Cdd:PRK13644 231 LGLTPPSLIELAEN 244
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
288-499 |
1.77e-17 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 87.47 E-value: 1.77e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 288 DHVSFRIRRGEIFGFLGSNGCGKSTTMKMLTGLLPATEGTAQLFGKEV---DPKDINTRRR--VGYMSQAFSLYSELTVR 362
Cdd:PRK10535 25 KGISLDIYAGEMVAIVGASGSGKSTLMNILGCLDKPTSGTYRVAGQDVatlDADALAQLRRehFGFIFQRYHLLSHLTAA 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 363 QNLVLHARLFGVPAAEIDARVDEMARRFGLADIYGMLPDSLPLGMRQRLSLAVAMVHKPELLILDEPTSGVDPVARDSFW 442
Cdd:PRK10535 105 QNVEVPAVYAGLERKQRLLRAQELLQRLGLEDRVEYQPSQLSGGQQQRVSIARALMNGGQVILADEPTGALDSHSGEEVM 184
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 505416896 443 QLMIDLARRDLvTIFISTHFMNEAQRCDRISLMHAGRVLaSDSPAELVRARGAATLE 499
Cdd:PRK10535 185 AILHQLRDRGH-TVIIVTHDPQVAAQAERVIEIRDGEIV-RNPPAQEKVNVAGGTEP 239
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
259-489 |
2.32e-17 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 84.13 E-value: 2.32e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 259 IEPLRADaragTAIEARGLTMRFGD-----FTAVDHVSFRIRRGEIFGFLGSNGCGKSTTMKMLTGLLPATEGTAQL--- 330
Cdd:PRK13631 13 PNPLSDD----IILRVKNLYCVFDEkqeneLVALNNISYTFEKNKIYFIIGNSGSGKSTLVTHFNGLIKSKYGTIQVgdi 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 331 ----------FGKEVDPKDINT----RRRVGYMSQ--AFSLYSElTVRQNLVLHARLFGVPAAEIDARVDEMARRFGLAD 394
Cdd:PRK13631 89 yigdkknnheLITNPYSKKIKNfkelRRRVSMVFQfpEYQLFKD-TIEKDIMFGPVALGVKKSEAKKLAKFYLNKMGLDD 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 395 IY-GMLPDSLPLGMRQRLSLAVAMVHKPELLILDEPTSGVDPVARDSFWQLMIDlARRDLVTIFISTHFM-NEAQRCDRI 472
Cdd:PRK13631 168 SYlERSPFGLSGGQKRRVAIAGILAIQPEILIFDEPTAGLDPKGEHEMMQLILD-AKANNKTVFVITHTMeHVLEVADEV 246
|
250
....*....|....*..
gi 505416896 473 SLMHAGRVLASDSPAEL 489
Cdd:PRK13631 247 IVMDKGKILKTGTPYEI 263
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
10-200 |
2.65e-17 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 81.46 E-value: 2.65e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 10 SDVSLRYGKTVALDRITLDVPAGLTTGLIGPDGVGKSSLLALASGARALQTGGVDALGGDmrsrRHRERVCRRIAYmpqg 89
Cdd:PRK13539 6 EDLACVRGGRVLFSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDGGD----IDDPDVAEACHY---- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 90 LG-KN-LYPTLSVEENLQFFARLFghdaGERRRRIDALTQSTGLFPFLSRPAGKLSGGMKQKLGLCCALIHDPDLLILDE 167
Cdd:PRK13539 78 LGhRNaMKPALTVAENLEFWAAFL----GGEELDIAAALEAVGLAPLAHLPFGYLSAGQKRRVALARLLVSNRPIWILDE 153
|
170 180 190
....*....|....*....|....*....|...
gi 505416896 168 PTTGVDPLARAQFWDLIARiRDERPTMsVIVAT 200
Cdd:PRK13539 154 PTAALDAAAVALFAELIRA-HLAQGGI-VIAAT 184
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
290-479 |
2.81e-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: 81.36 E-value: 2.81e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 290 VSFRIRRGEIFGFLGSNGCGKSTTMKMLTGLLPATEGTAQLFGkevdpkdintrrRVGYMSQAFSLYSElTVRQNLvlha 369
Cdd:cd03250 24 INLEVPKGELVAIVGPVGSGKSSLLSALLGELEKLSGSVSVPG------------SIAYVSQEPWIQNG-TIRENI---- 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 370 rLFGVPaaeIDA-RVDEMARRFGL-ADIyGMLPD-----------SLPLGMRQRLSLAVAMVHKPELLILDEPTSGVDP- 435
Cdd:cd03250 87 -LFGKP---FDEeRYEKVIKACALePDL-EILPDgdlteigekgiNLSGGQKQRISLARAVYSDADIYLLDDPLSAVDAh 161
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 505416896 436 VARDSFWQLMIDLARRDlVTIFISTHFMNEAQRCDRISLMHAGR 479
Cdd:cd03250 162 VGRHIFENCILGLLLNN-KTRILVTHQLQLLPHADQIVVLDNGR 204
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
290-490 |
3.69e-17 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 86.25 E-value: 3.69e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 290 VSFRIRRGEIFGFLGSNGCGKSTTMKMLTGLLPA---TEGTAQLFGKEVDPKDIntRRRVGYMSQAFSLYSELTVRQNLV 366
Cdd:TIGR00955 44 VSGVAKPGELLAVMGSSGAGKTTLMNALAFRSPKgvkGSGSVLLNGMPIDAKEM--RAISAYVQQDDLFIPTLTVREHLM 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 367 LHARLF---GVPAAEIDARVDEMARRFGLAD----IYGMLPD--SLPLGMRQRLSLAVAMVHKPELLILDEPTSGVDPVA 437
Cdd:TIGR00955 122 FQAHLRmprRVTKKEKRERVDEVLQALGLRKcantRIGVPGRvkGLSGGERKRLAFASELLTDPPLLFCDEPTSGLDSFM 201
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 505416896 438 RDSFWQLMIDLARRDLvTIFISTH---------FmneaqrcDRISLMHAGRVLASDSPAELV 490
Cdd:TIGR00955 202 AYSVVQVLKGLAQKGK-TIICTIHqpsselfelF-------DKIILMAEGRVAYLGSPDQAV 255
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
7-224 |
4.10e-17 |
|
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: 80.05 E-value: 4.10e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 7 VRFSDVSLRYG--KTVALDRITLDVPAGLTTGLIGPDGVGKSSLLALASGARALQTGGVdALGGdmrsrrhrervcrria 84
Cdd:cd03247 1 LSINNVSFSYPeqEQQVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEI-TLDG---------------- 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 85 ympqglgknlYPTLSVEENLqffarlfghdagerRRRIDALTQSTGLF--PFLSRPAGKLSGGMKQKLGLCCALIHDPDL 162
Cdd:cd03247 64 ----------VPVSDLEKAL--------------SSLISVLNQRPYLFdtTLRNNLGRRFSGGERQRLALARILLQDAPI 119
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 505416896 163 LILDEPTTGVDPLARAQFWDLIARIRDERptmSVIVATAYMDEAQRFDWLIAMDAGRVLATG 224
Cdd:cd03247 120 VLLDEPTVGLDPITERQLLSLIFEVLKDK---TLIWITHHLTGIEHMDKILFLENGKIIMQG 178
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
270-481 |
4.15e-17 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 82.11 E-value: 4.15e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 270 TAIEARGLTMRFGDFTAVDHVSFRIRRGEIFGFLGSNGCGKSTTMKMLTGLLPATEGTAQLFGKEVD-PKDINT------ 342
Cdd:PRK11264 2 SAIEVKNLVKKFHGQTVLHGIDLEVKPGEVVAIIGPSGSGKTTLLRCINLLEQPEAGTIRVGDITIDtARSLSQqkglir 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 343 --RRRVGYMSQAFSLYSELTVRQNLVLHARLF-GVPAAEIDARVDEMARRFGLADIYGMLPDSLPLGMRQRLSLAVAMVH 419
Cdd:PRK11264 82 qlRQHVGFVFQNFNLFPHRTVLENIIEGPVIVkGEPKEEATARARELLAKVGLAGKETSYPRRLSGGQQQRVAIARALAM 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 505416896 420 KPELLILDEPTSGVDPVARDSFWQLMIDLA--RRDLVtifISTHFMNEAQR-CDRISLMHAGRVL 481
Cdd:PRK11264 162 RPEVILFDEPTSALDPELVGEVLNTIRQLAqeKRTMV---IVTHEMSFARDvADRAIFMDQGRIV 223
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
1-246 |
4.30e-17 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 82.62 E-value: 4.30e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 1 MNASSVVRFSDVSLRYGKTvALDRITLDVPAGLTTGLIGPDGVGKSSLLALASGARALQTGGVDALGGDMRSRRHRERvc 80
Cdd:PRK15056 3 QQAGIVVNDVTVTWRNGHT-ALRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKISILGQPTRQALQKNL-- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 81 rrIAYMPQGLGKNL-YPTLSveENLQFFARlFGHDAGER------RRRIDALTQSTGLFPFLSRPAGKLSGGMKQKLGLC 153
Cdd:PRK15056 80 --VAYVPQSEEVDWsFPVLV--EDVVMMGR-YGHMGWLRrakkrdRQIVTAALARVDMVEFRHRQIGELSGGQKKRVFLA 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 154 CALIHDPDLLILDEPTTGVDPLARAQFWDLIARIRDERPTMsvIVATAYMDEAQRFDWLIAMDAGRVLATGaPAELLART 233
Cdd:PRK15056 155 RAIAQQGQVILLDEPFTGVDVKTEARIISLLRELRDEGKTM--LVSTHNLGSVTEFCDYTVMVKGTVLASG-PTETTFTA 231
|
250
....*....|...
gi 505416896 234 gcDSLEAAFIALL 246
Cdd:PRK15056 232 --ENLELAFSGVL 242
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
272-461 |
4.92e-17 |
|
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family transporter in which each gene contains an N-terminal membrane-spanning domain (pfam00664) and a C-terminal ATP-binding domain (pfam00005). In E. coli these genes were discovered as mutants which caused the terminal heme-copper oxidase complex cytochrome bd to fail to assemble. Recent work has shown that the transporter is involved in export of redox-active thiol compounds such as cysteine and glutathione. The linkage to assembly of the cytochrome bd complex is further supported by the conserved operon structure found outside the gammaproteobacteria (cydABCD) containing both the transporter and oxidase genes components. The genes used as the seed members for this model are all either found in the gammproteobacterial context or the CydABCD context. All members of this family scoring above trusted at the time of its creation were from genomes which encode a cytochrome bd complex.
Pssm-ID: 274331 [Multi-domain] Cd Length: 530 Bit Score: 85.49 E-value: 4.92e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 272 IEARGLTMRF-GDFTAVDHVSFRIRRGEIFGFLGSNGCGKSTTMKMLTGLLPATEGTAQLFGKEVDPKDIN-TRRRVGYM 349
Cdd:TIGR02868 335 LELRDLSAGYpGAPPVLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPLQGEVTLDGVPVSSLDQDeVRRRVSVC 414
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 350 SQAFSLYSElTVRQNLvlharLFGVPAAEiDARVDEMARRFGLADIYGMLPD-----------SLPLGMRQRLSLAVAMV 418
Cdd:TIGR02868 415 AQDAHLFDT-TVRENL-----RLARPDAT-DEELWAALERVGLADWLRALPDgldtvlgeggaRLSGGERQRLALARALL 487
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 505416896 419 HKPELLILDEPTSGVDPVARDSFWQLMIDlARRDLVTIFISTH 461
Cdd:TIGR02868 488 ADAPILLLDEPTEHLDAETADELLEDLLA-ALSGRTVVLITHH 529
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
270-500 |
5.04e-17 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 82.14 E-value: 5.04e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 270 TAIEARGLTMRF----GDF-----TAVDHVSFRIRRGEIFGFLGSNGCGKSTTMKMLTGLLPATEGTAQLFGKEVDPKDI 340
Cdd:PRK15112 3 TLLEVRNLSKTFryrtGWFrrqtvEAVKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDHPLHFGDY 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 341 NTRR---RVGYMSQAFSLYSELTVRQNLVLHARL-FGVPAAEIDARVDEMARRFGL-ADIYGMLPDSLPLGMRQRLSLAV 415
Cdd:PRK15112 83 SYRSqriRMIFQDPSTSLNPRQRISQILDFPLRLnTDLEPEQREKQIIETLRQVGLlPDHASYYPHMLAPGQKQRLGLAR 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 416 AMVHKPELLILDEPTSGVDPVARDSFWQLMIDL-ARRDLVTIFISTHFMNEAQRCDRISLMHAGRVLASDSPAELVrarg 494
Cdd:PRK15112 163 ALILRPKVIIADEALASLDMSMRSQLINLMLELqEKQGISYIYVTQHLGMMKHISDQVLVMHQGEVVERGSTADVL---- 238
|
....*.
gi 505416896 495 AATLED 500
Cdd:PRK15112 239 ASPLHE 244
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
7-234 |
6.00e-17 |
|
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: 81.12 E-value: 6.00e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 7 VRFSDVSLRYGKTV--ALDRITLDVPAGLTTGLIGPDGVGKSSLLALASGARALQTGGVDALGGDMRsRRHRERVCRRIA 84
Cdd:cd03251 1 VEFKNVTFRYPGDGppVLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDGHDVR-DYTLASLRRQIG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 85 YMPQGLgkNLYPTlSVEENLQFFARlfghdaGERRRRIDALTQSTGLFPFLSR-PAG----------KLSGGMKQKLGLC 153
Cdd:cd03251 80 LVSQDV--FLFND-TVAENIAYGRP------GATREEVEEAARAANAHEFIMElPEGydtvigergvKLSGGQRQRIAIA 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 154 CALIHDPDLLILDEPTTGVDPLARAQFWDLIARIRDERPTMSVivataymdeAQRF------DWLIAMDAGRVLATGAPA 227
Cdd:cd03251 151 RALLKDPPILILDEATSALDTESERLVQAALERLMKNRTTFVI---------AHRLstienaDRIVVLEDGKIVERGTHE 221
|
....*..
gi 505416896 228 ELLARTG 234
Cdd:cd03251 222 ELLAQGG 228
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
286-479 |
6.45e-17 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 83.22 E-value: 6.45e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 286 AVDHVSFRIRRGEIFGFLGSNGCGKSTTMKMLTGLLPATEGTAQLFGKEVDPKDINTRRRVGYMSQAF------SLYSEL 359
Cdd:PRK15079 36 AVDGVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGEVAWLGKDLLGMKDDEWRAVRSDIQMIfqdplaSLNPRM 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 360 TVRQNLVLHARLF--GVPAAEIDARVDEMARRFGL-ADIYGMLPDSLPLGMRQRLSLAVAMVHKPELLILDEPTSGVDPV 436
Cdd:PRK15079 116 TIGEIIAEPLRTYhpKLSRQEVKDRVKAMMLKVGLlPNLINRYPHEFSGGQCQRIGIARALILEPKLIICDEPVSALDVS 195
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 505416896 437 ARDSFWQLMIDLARR-DLVTIFISTHFMNEAQRCDRISLMHAGR 479
Cdd:PRK15079 196 IQAQVVNLLQQLQREmGLSLIFIAHDLAVVKHISDRVLVMYLGH 239
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
10-230 |
6.54e-17 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 81.74 E-value: 6.54e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 10 SDVSLRYGKTVALDRITLDVPAGLTTGLIGPDGVGKSSLLALASGARALQTGGVDaLGGDMRSRRHRERVCRRIAYMPQg 89
Cdd:PRK13548 6 RNLSVRLGGRTLLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVR-LNGRPLADWSPAELARRRAVLPQ- 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 90 lgknlYPTLS----VEENLQFFARLFGHDAGERRRRIDALTQSTGLFPFLSRPAGKLSGGMKQKLGLCCALI------HD 159
Cdd:PRK13548 84 -----HSSLSfpftVEEVVAMGRAPHGLSRAEDDALVAAALAQVDLAHLAGRDYPQLSGGEQQRVQLARVLAqlwepdGP 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 505416896 160 PDLLILDEPTTGVDPLARAQFWDLIARIRDERPTMSVIV------ATAYMDEaqrfdwLIAMDAGRVLATGAPAELL 230
Cdd:PRK13548 159 PRWLLLDEPTSALDLAHQHHVLRLARQLAHERGLAVIVVlhdlnlAARYADR------IVLLHQGRLVADGTPAEVL 229
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
272-479 |
8.96e-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: 77.87 E-value: 8.96e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 272 IEARGLTMRFGDFTAVDHVSFRIRRGEIFGFLGSNGCGKSTTMKMLTGLLPATEGTAQLFGKEvdpkdintrrRVGYMSQ 351
Cdd:cd03221 1 IELENLSKTYGGKLLLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIVTWGSTV----------KIGYFEQ 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 352 aFSlyseltvrqnlvlharlfGvpaaeidarvdemarrfgladiygmlpdslplGMRQRLSLAVAMVHKPELLILDEPTS 431
Cdd:cd03221 71 -LS------------------G--------------------------------GEKMRLALAKLLLENPNLLLLDEPTN 99
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 505416896 432 GVDPVARDSFWQLMIDLARrdlvTIFISTH---FMNEAqrCDRISLMHAGR 479
Cdd:cd03221 100 HLDLESIEALEEALKEYPG----TVILVSHdryFLDQV--ATKIIELEDGK 144
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
7-232 |
9.49e-17 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 82.82 E-value: 9.49e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 7 VRFSDVSLRY----GKTVALDRITLDVPAGLTTGLIGPDGVGKSSLLALASGaraLQT--------GGVD--AL-GGDMR 71
Cdd:COG1135 2 IELENLSKTFptkgGPVTALDDVSLTIEKGEIFGIIGYSGAGKSTLIRCINL---LERptsgsvlvDGVDltALsERELR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 72 srrhreRVCRRIAYMPQGLgkNLYPTLSVEENLQFFARLFGHDAGERRRRIDALTQSTGLFPFL-SRPAgKLSGGMKQKL 150
Cdd:COG1135 79 ------AARRKIGMIFQHF--NLLSSRTVAENVALPLEIAGVPKAEIRKRVAELLELVGLSDKAdAYPS-QLSGGQKQRV 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 151 GLCCALIHDPDLLILDEPTTGVDPLARAQFWDLIARIRDERpTMSVIVATAYMDEAQRfdwlIA-----MDAGRVLATGA 225
Cdd:COG1135 150 GIARALANNPKVLLCDEATSALDPETTRSILDLLKDINREL-GLTIVLITHEMDVVRR----ICdrvavLENGRIVEQGP 224
|
....*..
gi 505416896 226 PAELLAR 232
Cdd:COG1135 225 VLDVFAN 231
|
|
| PvdE |
COG4615 |
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ... |
236-492 |
9.51e-17 |
|
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion transport and metabolism];
Pssm-ID: 443659 [Multi-domain] Cd Length: 547 Bit Score: 84.85 E-value: 9.51e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 236 DSLEAAFIALLPENERrghkpvkiEPLRADARAGTAIEARGLTMRFGD------FTaVDHVSFRIRRGEIFGFLGSNGCG 309
Cdd:COG4615 300 EELELALAAAEPAAAD--------AAAPPAPADFQTLELRGVTYRYPGedgdegFT-LGPIDLTIRRGELVFIVGGNGSG 370
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 310 KSTTMKMLTGLLPATEGTAQLFGKEVDPKDINTRRrvgymsQAFSlyselTVRQNLVLHARLFGVPAAEIDARVDEMARR 389
Cdd:COG4615 371 KSTLAKLLTGLYRPESGEILLDGQPVTADNREAYR------QLFS-----AVFSDFHLFDRLLGLDGEADPARARELLER 439
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 390 FGLADIY----GMLPD-SLPLGMRQRLSLAVAMVHKPELLILDEPTSGVDPVARDSFW-QLMIDLARRDlVTIFISTH-- 461
Cdd:COG4615 440 LELDHKVsvedGRFSTtDLSQGQRKRLALLVALLEDRPILVFDEWAADQDPEFRRVFYtELLPELKARG-KTVIAISHdd 518
|
250 260 270
....*....|....*....|....*....|...
gi 505416896 462 --FmneaQRCDRISLMHAGRVLASDSPAELVRA 492
Cdd:COG4615 519 ryF----DLADRVLKMDYGKLVELTGPAALAAS 547
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
245-494 |
9.56e-17 |
|
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The amino terminal domain (pfam03412) processes the N-terminal leader peptide from the bacteriocin while C-terminal domains resemble ABC transporter membrane protein and ATP-binding cassette domain. In general, bacteriocins are agents which are responsible for killing or inhibiting the closely related species or even different strains of the same species. Bacteriocins are usually encoded by bacterial plasmids. Bacteriocins are named after the species and hence in literature one encounters various names e.g., leucocin from Leuconostic geldium; pedicocin from Pedicoccus acidilactici; sakacin from Lactobacillus sake etc. [Protein fate, Protein and peptide secretion and trafficking, Protein fate, Protein modification and repair, Transport and binding proteins, Other]
Pssm-ID: 130261 [Multi-domain] Cd Length: 708 Bit Score: 85.18 E-value: 9.56e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 245 LLPENERRGHKPVKIEPLRADaragtaIEARGLTMRFG-DFTAVDHVSFRIRRGEIFGFLGSNGCGKSTTMKMLTGLLPA 323
Cdd:TIGR01193 453 LVDSEFINKKKRTELNNLNGD------IVINDVSYSYGyGSNILSDISLTIKMNSKTTIVGMSGSGKSTLAKLLVGFFQA 526
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 324 TEGTAQLFGKEVDPKDINT-RRRVGYMSQAFSLYSElTVRQNLVLHAR--------LFGVPAAEIDARVDEMARRFG--L 392
Cdd:TIGR01193 527 RSGEILLNGFSLKDIDRHTlRQFINYLPQEPYIFSG-SILENLLLGAKenvsqdeiWAACEIAEIKDDIENMPLGYQteL 605
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 393 ADIYGmlpdSLPLGMRQRLSLAVAMVHKPELLILDEPTSGVDPVARDSFWQLMIDLarRDLVTIFIStHFMNEAQRCDRI 472
Cdd:TIGR01193 606 SEEGS----SISGGQKQRIALARALLTDSKVLILDESTSNLDTITEKKIVNNLLNL--QDKTIIFVA-HRLSVAKQSDKI 678
|
250 260
....*....|....*....|..
gi 505416896 473 SLMHAGRVLASDSPAELVRARG 494
Cdd:TIGR01193 679 IVLDHGKIIEQGSHDELLDRNG 700
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
272-480 |
1.12e-16 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 80.90 E-value: 1.12e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 272 IEARGLTMRFG-----DFTAVDHVSFRIRRGEIFGFLGSNGCGKSTTMKMLTGLLPATEGTAQLFGKEVdpkdinTR--- 343
Cdd:COG1101 2 LELKNLSKTFNpgtvnEKRALDGLNLTIEEGDFVTVIGSNGAGKSTLLNAIAGSLPPDSGSILIDGKDV------TKlpe 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 344 -RRVGYMSQAF-------SlySELTVRQNLVLHAR-------LFGVPAAEIDaRVDEMARRFGLAdiygmLPD------- 401
Cdd:COG1101 76 yKRAKYIGRVFqdpmmgtA--PSMTIEENLALAYRrgkrrglRRGLTKKRRE-LFRELLATLGLG-----LENrldtkvg 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 402 SLPLGMRQRLSLAVAMVHKPELLILDEPTSGVDPvaRDSfwQLMIDLARR-----DLVTIFIsTHFMNEAQRC-DRISLM 475
Cdd:COG1101 148 LLSGGQRQALSLLMATLTKPKLLLLDEHTAALDP--KTA--ALVLELTEKiveenNLTTLMV-THNMEQALDYgNRLIMM 222
|
....*
gi 505416896 476 HAGRV 480
Cdd:COG1101 223 HEGRI 227
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
22-233 |
1.26e-16 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 81.29 E-value: 1.26e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 22 LDRITLDVPAGLTTGLIGPDGVGKSSLLALASGARAlQTGGVDALGGDMRSRRHRERVCRRIAYMPQGlGKNLYPTLSVE 101
Cdd:PRK13642 23 LNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFE-EFEGKVKIDGELLTAENVWNLRRKIGMVFQN-PDNQFVGATVE 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 102 ENLQFFARLFGHDAGERRRRIDALTQSTGLFPFLSRPAGKLSGGMKQKLGLCCALIHDPDLLILDEPTTGVDPLARAQFW 181
Cdd:PRK13642 101 DDVAFGMENQGIPREEMIKRVDEALLAVNMLDFKTREPARLSGGQKQRVAVAGIIALRPEIIILDESTSMLDPTGRQEIM 180
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 505416896 182 DLIARIRDeRPTMSVIVATAYMDEAQRFDWLIAMDAGRVLATGAPAELLART 233
Cdd:PRK13642 181 RVIHEIKE-KYQLTVLSITHDLDEAASSDRILVMKAGEIIKEAAPSELFATS 231
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
290-480 |
1.30e-16 |
|
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: 80.21 E-value: 1.30e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 290 VSFRIRRGEIFGFLGSNGCGKSTTMKMLTGLLPATEGTAQLFGKEV-DPKDINTRRRVGYMSQAFSLYSElTVRQNLVlh 368
Cdd:cd03248 33 VSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDGKPIsQYEHKYLHSKVSLVGQEPVLFAR-SLQDNIA-- 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 369 arlFGVPAAEIDaRVDEMARRFGLADIYGMLPDS-----------LPLGMRQRLSLAVAMVHKPELLILDEPTSGVDPVA 437
Cdd:cd03248 110 ---YGLQSCSFE-CVKEAAQKAHAHSFISELASGydtevgekgsqLSGGQKQRVAIARALIRNPQVLILDEATSALDAES 185
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 505416896 438 RDSFWQLMIDLARRDlvTIFISTHFMNEAQRCDRISLMHAGRV 480
Cdd:cd03248 186 EQQVQQALYDWPERR--TVLVIAHRLSTVERADQILVLDGGRI 226
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
7-234 |
1.32e-16 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 84.45 E-value: 1.32e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 7 VRFSDVSLRY-GKTVALDRITLDVPAGLTTGLIGPDGVGKSSLLALASGARALQTGGVdALGG---------DMRSrrhr 76
Cdd:COG1132 340 IEFENVSFSYpGDRPVLKDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYDPTSGRI-LIDGvdirdltleSLRR---- 414
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 77 ervcrRIAYMPQGlgknlyPTL---SVEENLqffaRLFGHDAGErrRRIDALTQSTGLFPFLSR-PAG----------KL 142
Cdd:COG1132 415 -----QIGVVPQD------TFLfsgTIRENI----RYGRPDATD--EEVEEAAKAAQAHEFIEAlPDGydtvvgergvNL 477
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 143 SGGMKQKLGLCCALIHDPDLLILDEPTTGVDPLARAQFWDLIARIRDERptMSVIVA----TaymdeAQRFDWLIAMDAG 218
Cdd:COG1132 478 SGGQRQRIAIARALLKDPPILILDEATSALDTETEALIQEALERLMKGR--TTIVIAhrlsT-----IRNADRILVLDDG 550
|
250
....*....|....*.
gi 505416896 219 RVLATGAPAELLARTG 234
Cdd:COG1132 551 RIVEQGTHEELLARGG 566
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
119-434 |
1.46e-16 |
|
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440858 [Multi-domain] Cd Length: 592 Bit Score: 84.45 E-value: 1.46e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 119 RRRIDALTQSTGLFPFLSRPAGKLSGGMKQKLGLCCALIHDPDLLILDEPTTGVDPLARAQfwdlIAR-IRDE-RPTMSV 196
Cdd:COG1245 190 RGKLDELAEKLGLENILDRDISELSGGELQRVAIAAALLRDADFYFFDEPSSYLDIYQRLN----VARlIRELaEEGKYV 265
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 197 IVAtaymdeaqRFDwLIAMD--AGRV-LATGAPA-------ELLARTGCDsleaAFIA-LLP-ENERRGHKPVKIE--PL 262
Cdd:COG1245 266 LVV--------EHD-LAILDylADYVhILYGEPGvygvvskPKSVRVGIN----QYLDgYLPeENVRIRDEPIEFEvhAP 332
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 263 RADARAGTAIEARGLTMRFGDFT-AVDhvSFRIRRGEIFGFLGSNGCGKSTTMKMLTGLLPATEGtaqlfgkEVDPKDin 341
Cdd:COG1245 333 RREKEEETLVEYPDLTKSYGGFSlEVE--GGEIREGEVLGIVGPNGIGKTTFAKILAGVLKPDEG-------EVDEDL-- 401
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 342 trrRVGYMSQAFSLYSELTVRQNlvlharLFGVPAAEIDARV--DEMARRFGLADIYGMLPDSLPLGMRQRLSLAVAMVH 419
Cdd:COG1245 402 ---KISYKPQYISPDYDGTVEEF------LRSANTDDFGSSYykTEIIKPLGLEKLLDKNVKDLSGGELQRVAIAACLSR 472
|
330
....*....|....*
gi 505416896 420 KPELLILDEPTSGVD 434
Cdd:COG1245 473 DADLYLLDEPSAHLD 487
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
4-232 |
1.56e-16 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 80.13 E-value: 1.56e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 4 SSVVRFSDVSLRY----------------------GKTVALDRITLDVPAGLTTGLIGPDGVGKSSLLALASGARALQTG 61
Cdd:COG1134 2 SSMIEVENVSKSYrlyhepsrslkelllrrrrtrrEEFWALKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTSG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 62 GVDAlggDMRsrrhrervcrrIAyMPQGLGKNLYPTLSVEENLQFFARLFGHDAGERRRRIDALTQSTGLFPFLSRPAGK 141
Cdd:COG1134 82 RVEV---NGR-----------VS-ALLELGAGFHPELTGRENIYLNGRLLGLSRKEIDEKFDEIVEFAELGDFIDQPVKT 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 142 LSGGMKQKLGLCCALIHDPDLLILDEPTTGVDPLARAQFWDLIARIRDERPTmsVIVATAYMDEAQRF-DWLIAMDAGRV 220
Cdd:COG1134 147 YSSGMRARLAFAVATAVDPDILLVDEVLAVGDAAFQKKCLARIRELRESGRT--VIFVSHSMGAVRRLcDRAIWLEKGRL 224
|
250
....*....|..
gi 505416896 221 LATGAPAELLAR 232
Cdd:COG1134 225 VMDGDPEEVIAA 236
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
7-224 |
1.64e-16 |
|
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: 79.22 E-value: 1.64e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 7 VRFSDVSLRYGKTVALDRITLDVPAGLTTGLIGPDGVGKSSLLALASGARALqTGGVDALGGdmRSRRHRERVCRRIAYM 86
Cdd:cd03301 1 VELENVTKRFGNVTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEP-TSGRIYIGG--RDVTDLPPKDRDIAMV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 87 PQGLGknLYPTLSVEENLQFFARLFGHDAGERRRRIDALTQSTGLFPFLSRPAGKLSGGMKQKLGLCCALIHDPDLLILD 166
Cdd:cd03301 78 FQNYA--LYPHMTVYDNIAFGLKLRKVPKDEIDERVREVAELLQIEHLLDRKPKQLSGGQRQRVALGRAIVREPKVFLMD 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 505416896 167 EPTTGVDPLARAQFWDLIARIRDERPTmSVIVATAYMDEAQRF-DWLIAMDAGRVLATG 224
Cdd:cd03301 156 EPLSNLDAKLRVQMRAELKRLQQRLGT-TTIYVTHDQVEAMTMaDRIAVMNDGQIQQIG 213
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
7-234 |
2.20e-16 |
|
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: 79.58 E-value: 2.20e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 7 VRFSDVSLRYGKTV-ALDRITLDVPAGLTTGLIGPDGVGKSSLLALASGARALQTGGVDALGGDMRSRRHRERVCRrIAY 85
Cdd:cd03254 3 IEFENVNFSYDEKKpVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGIDIRDISRKSLRSM-IGV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 86 MPQGLGknLYPTlSVEENLqffaRLFGHDAgeRRRRIDALTQSTGLFPFLSR----------PAGK-LSGGMKQKLGLCC 154
Cdd:cd03254 82 VLQDTF--LFSG-TIMENI----RLGRPNA--TDEEVIEAAKEAGAHDFIMKlpngydtvlgENGGnLSQGERQLLAIAR 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 155 ALIHDPDLLILDEPTTGVDPLARAQFWDLIARIRDERptMSVIVAtAYMDEAQRFDWLIAMDAGRVLATGAPAELLARTG 234
Cdd:cd03254 153 AMLRDPKILILDEATSNIDTETEKLIQEALEKLMKGR--TSIIIA-HRLSTIKNADKILVLDDGKIIEEGTHDELLAKKG 229
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
272-445 |
2.22e-16 |
|
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the bacterial CcmAB transporter. The CCM family is involved in bacterial cytochrome c biogenesis. Cytochrome c maturation in E. coli requires the ccm operon, which encodes eight membrane proteins (CcmABCDEFGH). CcmE is a periplasmic heme chaperon that binds heme covalently and transfers it onto apocytochrome c in the presence of CcmF, CcmG, and CcmH. The CcmAB proteins represent an ABC transporter and the CcmCD proteins participate in heme transfer to CcmE.
Pssm-ID: 213198 [Multi-domain] Cd Length: 201 Bit Score: 78.69 E-value: 2.22e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 272 IEARGLTMRFGDFTAVDHVSFRIRRGEIFGFLGSNGCGKSTTMKMLTGLLPATEGTAQLFGKEVDPKDINTRRRVGYMSQ 351
Cdd:cd03231 1 LEADELTCERDGRALFSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNGGPLDFQRDSIARGLLYLGH 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 352 AFSLYSELTVRQNLVLHARLFGvpaaeiDARVDEMARRFGLADIYGMLPDSLPLGMRQRLSLAVAMVHKPELLILDEPTS 431
Cdd:cd03231 81 APGIKTTLSVLENLRFWHADHS------DEQVEEALARVGLNGFEDRPVAQLSAGQQRRVALARLLLSGRPLWILDEPTT 154
|
170
....*....|....
gi 505416896 432 GVDPVARDSFWQLM 445
Cdd:cd03231 155 ALDKAGVARFAEAM 168
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
6-232 |
2.61e-16 |
|
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: 81.25 E-value: 2.61e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 6 VVRFSDVSLRY----GKTVALDRITLDVPAGLTTGLIGPDGVGKSSLlalasgARAL--------QTGG--------VDA 65
Cdd:COG0444 1 LLEVRNLKVYFptrrGVVKAVDGVSFDVRRGETLGLVGESGSGKSTL------ARAIlgllpppgITSGeilfdgedLLK 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 66 LGG-DMRSRRHRErvcrrIAYMPQGLGKNLYPTLSVEENLQFFARLFGH-DAGERRRRIDALTQSTGLFP---FLSRPAG 140
Cdd:COG0444 75 LSEkELRKIRGRE-----IQMIFQDPMTSLNPVMTVGDQIAEPLRIHGGlSKAEARERAIELLERVGLPDperRLDRYPH 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 141 KLSGGMKQKLGLCCALIHDPDLLILDEPTTGVDPLARAQFWDLIARIRDERpTMSVIVAT------AYMdeAQRfdwlIA 214
Cdd:COG0444 150 ELSGGMRQRVMIARALALEPKLLIADEPTTALDVTIQAQILNLLKDLQREL-GLAILFIThdlgvvAEI--ADR----VA 222
|
250
....*....|....*....
gi 505416896 215 -MDAGRVLATGAPAELLAR 232
Cdd:COG0444 223 vMYAGRIVEEGPVEELFEN 241
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
1-231 |
2.74e-16 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 80.44 E-value: 2.74e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 1 MNASSVVRFSDVSLRYGKTV-----ALDRITLDVPAGLTTGLIGPDGVGKSSLLALASGARALQTG----GVDALGGDMR 71
Cdd:PRK13645 1 FDFSKDIILDNVSYTYAKKTpfefkALNNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGLIISETGqtivGDYAIPANLK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 72 SRRHRERVCRRIAYMPQGLGKNLYPTlSVEENLQFFARLFGHDAGERRRRIDALTQSTGLfP--FLSRPAGKLSGGMKQK 149
Cdd:PRK13645 81 KIKEVKRLRKEIGLVFQFPEYQLFQE-TIEKDIAFGPVNLGENKQEAYKKVPELLKLVQL-PedYVKRSPFELSGGQKRR 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 150 LGLCCALIHDPDLLILDEPTTGVDPLARAQFWDLIARIRDERPTmSVIVATAYMDEAQRF-DWLIAMDAGRVLATGAPAE 228
Cdd:PRK13645 159 VALAGIIAMDGNTLVLDEPTGGLDPKGEEDFINLFERLNKEYKK-RIIMVTHNMDQVLRIaDEVIVMHEGKVISIGSPFE 237
|
...
gi 505416896 229 LLA 231
Cdd:PRK13645 238 IFS 240
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
263-494 |
3.29e-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: 83.23 E-value: 3.29e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 263 RADARAGTAIEARGLTMRFG--DFTAVDHVSFRIRRGEIFGFLGSNGCGKSTTMKMLTGLLPATEGTAQLFGKEV-DPKD 339
Cdd:TIGR02203 322 RAIERARGDVEFRNVTFRYPgrDRPALDSISLVIEPGETVALVGRSGSGKSTLVNLIPRFYEPDSGQILLDGHDLaDYTL 401
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 340 INTRRRVGYMSQAFSLYSElTVRQNlVLHARLFGVPAAEI-DARVDEMARRF------GLADIYGMLPDSLPLGMRQRLS 412
Cdd:TIGR02203 402 ASLRRQVALVSQDVVLFND-TIANN-IAYGRTEQADRAEIeRALAAAYAQDFvdklplGLDTPIGENGVLLSGGQRQRLA 479
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 413 LAVAMVHKPELLILDEPTSGVDP----VARDSFWQLMidlarRDLVTIFIStHFMNEAQRCDRISLMHAGRVLASDSPAE 488
Cdd:TIGR02203 480 IARALLKDAPILILDEATSALDNeserLVQAALERLM-----QGRTTLVIA-HRLSTIEKADRIVVMDDGRIVERGTHNE 553
|
....*.
gi 505416896 489 LVRARG 494
Cdd:TIGR02203 554 LLARNG 559
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
268-493 |
5.73e-16 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 81.88 E-value: 5.73e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 268 AGTAIEARGLTMRFGDFTAVDHVSFRIRRGEIFGFLGSNGCGKSTTMKMLTGLLPATEGTAQLFGKEVdpKDINTRRR-- 345
Cdd:PRK11288 1 SSPYLSFDGIGKTFPGVKALDDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSILIDGQEM--RFASTTAAla 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 346 --VGYMSQAFSLYSELTVRQNLVLhARL---FG-VPAAEIDARVDEMARRFGLaDIYGMLP-DSLPLGMRQRLSLAVAMV 418
Cdd:PRK11288 79 agVAIIYQELHLVPEMTVAENLYL-GQLphkGGiVNRRLLNYEAREQLEHLGV-DIDPDTPlKYLSIGQRQMVEIAKALA 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 505416896 419 HKPELLILDEPTSGVDPVARDSFWQLMIDLARRDLVTIFIStHFMNEAQR-CDRISLMHAGRVLAS-DSPAELVRAR 493
Cdd:PRK11288 157 RNARVIAFDEPTSSLSAREIEQLFRVIRELRAEGRVILYVS-HRMEEIFAlCDAITVFKDGRYVATfDDMAQVDRDQ 232
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
21-220 |
7.18e-16 |
|
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: 76.70 E-value: 7.18e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 21 ALDRITLDVPAGLTTGLIGPDGVGKSSLLALASGARALQTGGVDALGGDMRSRRHRERVCRRIAYMP---QGLGknLYPT 97
Cdd:cd03215 15 AVRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITLDGKPVTRRSPRDAIRAGIAYVPedrKREG--LVLD 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 98 LSVEENLqffarlfghdagerrrridALTQStglfpflsrpagkLSGGMKQKLGLCCALIHDPDLLILDEPTTGVDPLAR 177
Cdd:cd03215 93 LSVAENI-------------------ALSSL-------------LSGGNQQKVVLARWLARDPRVLILDEPTRGVDVGAK 140
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 505416896 178 AQFWDLIARIRDERptMSVIVATAYMDEAQRF-DWLIAMDAGRV 220
Cdd:cd03215 141 AEIYRLIRELADAG--KAVLLISSELDELLGLcDRILVMYEGRI 182
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
272-481 |
7.33e-16 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 79.36 E-value: 7.33e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 272 IEARGLTMRFG-----DFTAVDHVSFRIRRGEIFGFLGSNGCGKSTTMKMLTGLLPATEGTAQLF-----------GKEV 335
Cdd:PRK13651 3 IKVKNIVKIFNkklptELKALDNVSVEINQGEFIAIIGQTGSGKTTFIEHLNALLLPDTGTIEWIfkdeknkkktkEKEK 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 336 DPKDINT--------------RRRVGYMSQaFSLYS--ELTVRQNLVLHARLFGVPAAEIDARVDEMARRFGLADIYgmL 399
Cdd:PRK13651 83 VLEKLVIqktrfkkikkikeiRRRVGVVFQ-FAEYQlfEQTIEKDIIFGPVSMGVSKEEAKKRAAKYIELVGLDESY--L 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 400 PDS---LPLGMRQRLSLAVAMVHKPELLILDEPTSGVDPVARDSFWQLMIDLARRDlVTIFISTHFMNEA-QRCDRISLM 475
Cdd:PRK13651 160 QRSpfeLSGGQKRRVALAGILAMEPDFLVFDEPTAGLDPQGVKEILEIFDNLNKQG-KTIILVTHDLDNVlEWTKRTIFF 238
|
....*.
gi 505416896 476 HAGRVL 481
Cdd:PRK13651 239 KDGKII 244
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
4-221 |
1.60e-15 |
|
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: 76.05 E-value: 1.60e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 4 SSVVRFSDVSL-------RYGKTVaLDRITLDVPAGLTTGLIGPDGVGKSSLL-ALASGARALQTGGVDALGGDMRSRRH 75
Cdd:cd03213 1 GVTLSFRNLTVtvksspsKSGKQL-LKNVSGKAKPGELTAIMGPSGAGKSTLLnALAGRRTGLGVSGEVLINGRPLDKRS 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 76 RERVcrrIAYMPQGLgkNLYPTLSVEENLQFFARLFGHDAGERRRridaltqstglfpflsrpagklsggmkqkLGLCCA 155
Cdd:cd03213 80 FRKI---IGYVPQDD--ILHPTLTVRETLMFAAKLRGLSGGERKR-----------------------------VSIALE 125
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 505416896 156 LIHDPDLLILDEPTTGVDPLARAQFWDLIARIRDE-RPTMSVIVATAYMDEAQrFDWLIAMDAGRVL 221
Cdd:cd03213 126 LVSNPSLLFLDEPTSGLDSSSALQVMSLLRRLADTgRTIICSIHQPSSEIFEL-FDKLLLLSQGRVI 191
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
22-232 |
1.68e-15 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 77.85 E-value: 1.68e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 22 LDRITLDVPAGLTTGLIGPDGVGKSSLLALASGARALQTGGVdALGGDMRSRRHRERVCRRIAYMPQGlGKNLYPTLSVE 101
Cdd:PRK13650 23 LNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQI-IIDGDLLTEENVWDIRHKIGMVFQN-PDNQFVGATVE 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 102 ENLQFFARLFGHDAGERRRRIDALTQSTGLFPFLSRPAGKLSGGMKQKLGLCCALIHDPDLLILDEPTTGVDPLARAQFW 181
Cdd:PRK13650 101 DDVAFGLENKGIPHEEMKERVNEALELVGMQDFKEREPARLSGGQKQRVAIAGAVAMRPKIIILDEATSMLDPEGRLELI 180
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 505416896 182 DLIARIRDERpTMSVIVATAYMDEAQRFDWLIAMDAGRVLATGAPAELLAR 232
Cdd:PRK13650 181 KTIKGIRDDY-QMTVISITHDLDEVALSDRVLVMKNGQVESTSTPRELFSR 230
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
268-488 |
2.22e-15 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 77.44 E-value: 2.22e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 268 AGTAIEARGLTMRFGDFTAVDHVSFRIRRGEIFGFLGSNGCGKSTTMKMLTGLLPATEG-----TAQLFGKEV-DPKDI- 340
Cdd:PRK14271 18 AAPAMAAVNLTLGFAGKTVLDQVSMGFPARAVTSLMGPTGSGKTTFLRTLNRMNDKVSGyrysgDVLLGGRSIfNYRDVl 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 341 NTRRRVGYMSQAFSLYSeLTVRQNLVLHARLFG-VPAAEI----DARVDEMARRFGLADIYGMLPDSLPLGMRQRLSLAV 415
Cdd:PRK14271 98 EFRRRVGMLFQRPNPFP-MSIMDNVLAGVRAHKlVPRKEFrgvaQARLTEVGLWDAVKDRLSDSPFRLSGGQQQLLCLAR 176
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 505416896 416 AMVHKPELLILDEPTSGVDPVARDSFWQLMIDLARRdlVTIFISTHFMNEAQR-CDRISLMHAGRvLASDSPAE 488
Cdd:PRK14271 177 TLAVNPEVLLLDEPTSALDPTTTEKIEEFIRSLADR--LTVIIVTHNLAQAARiSDRAALFFDGR-LVEEGPTE 247
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
10-230 |
2.37e-15 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 77.05 E-value: 2.37e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 10 SDVSLRYGKTVALDRITLDVPAGLTTGLIGPDGVGKSSLLALASGARALQTGGVDALGGDmrsrrhrervcrrIAYMPqg 89
Cdd:COG4604 5 KNVSKRYGGKVVLDDVSLTIPKGGITALIGPNGAGKSTLLSMISRLLPPDSGEVLVDGLD-------------VATTP-- 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 90 lGKNLYPTLSV--EENlQFFARL-------FG---HDAG----ERRRRIDALTQSTGLFPFLSRPAGKLSGGMKQKLGLC 153
Cdd:COG4604 70 -SRELAKRLAIlrQEN-HINSRLtvrelvaFGrfpYSKGrltaEDREIIDEAIAYLDLEDLADRYLDELSGGQRQRAFIA 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 154 CALIHDPDLLILDEPTTGVDPLARAQFWDLIARIRDERPTMSVIV------ATAYMDEaqrfdwLIAMDAGRVLATGAPA 227
Cdd:COG4604 148 MVLAQDTDYVLLDEPLNNLDMKHSVQMMKLLRRLADELGKTVVIVlhdinfASCYADH------IVAMKDGRVVAQGTPE 221
|
...
gi 505416896 228 ELL 230
Cdd:COG4604 222 EII 224
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
277-492 |
2.39e-15 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 78.24 E-value: 2.39e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 277 LTMRFGD----FTAVDHVSFRIRRGEIFGFLGSNGCGKSTTMKMLTGL---------------------LPATEgTAQLF 331
Cdd:PRK11022 9 LSVHFGDesapFRAVDRISYSVKQGEVVGIVGESGSGKSVSSLAIMGLidypgrvmaeklefngqdlqrISEKE-RRNLV 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 332 GKEV-----DP-KDINTRRRVGY-MSQAFSLY---SELTVRQNLVLHARLFGVPAAEidARVDemarrfgladIYgmlPD 401
Cdd:PRK11022 88 GAEVamifqDPmTSLNPCYTVGFqIMEAIKVHqggNKKTRRQRAIDLLNQVGIPDPA--SRLD----------VY---PH 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 402 SLPLGMRQRLSLAVAMVHKPELLILDEPTSGVDPVARDSFWQLMIDLARRDLVTIFISTHFMN-EAQRCDRISLMHAGRV 480
Cdd:PRK11022 153 QLSGGMSQRVMIAMAIACRPKLLIADEPTTALDVTIQAQIIELLLELQQKENMALVLITHDLAlVAEAAHKIIVMYAGQV 232
|
250
....*....|..
gi 505416896 481 LASDSPAELVRA 492
Cdd:PRK11022 233 VETGKAHDIFRA 244
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
7-224 |
2.55e-15 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 76.59 E-value: 2.55e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 7 VRFSDVSLRYGKTVALDRITLDVPAGLTTGLIGPDGVGKSSLLalasgaRAL------QTGGVDALGG--DMRSRRHRER 78
Cdd:PRK11124 3 IQLNGINCFYGAHQALFDITLDCPQGETLVLLGPSGAGKSSLL------RVLnllempRSGTLNIAGNhfDFSKTPSDKA 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 79 vcrrIAYMPQGLGK-----NLYPTLSVEENL-QFFARLFGHDAGERRRRIDALTQSTGLFPFLSRPAGKLSGGMKQKLGL 152
Cdd:PRK11124 77 ----IRELRRNVGMvfqqyNLWPHLTVQQNLiEAPCRVLGLSKDQALARAEKLLERLRLKPYADRFPLHLSGGQQQRVAI 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 505416896 153 CCALIHDPDLLILDEPTTGVDPLARAQFWDLIARIRDERPTmSVIVaTAYMDEAQRF-DWLIAMDAGRVLATG 224
Cdd:PRK11124 153 ARALMMEPQVLLFDEPTAALDPEITAQIVSIIRELAETGIT-QVIV-THEVEVARKTaSRVVYMENGHIVEQG 223
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
21-232 |
2.84e-15 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 77.15 E-value: 2.84e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 21 ALDRITLDVPAGLTTGLIGPDGVGKSSLLALASGARALQTGGVdALGGDMRSRRHRERVCRRIAYMPQGLGKNLYPTlSV 100
Cdd:PRK13652 19 ALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSV-LIRGEPITKENIREVRKFVGLVFQNPDDQIFSP-TV 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 101 EENLQFFARLFGHDAGERRRRIDALTQSTGLFPFLSRPAGKLSGGMKQKLGLCCALIHDPDLLILDEPTTGVDPLARAqf 180
Cdd:PRK13652 97 EQDIAFGPINLGLDEETVAHRVSSALHMLGLEELRDRVPHHLSGGEKKRVAIAGVIAMEPQVLVLDEPTAGLDPQGVK-- 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 505416896 181 wDLIARIRD--ERPTMSVIVATAYMD-EAQRFDWLIAMDAGRVLATGAPAELLAR 232
Cdd:PRK13652 175 -ELIDFLNDlpETYGMTVIFSTHQLDlVPEMADYIYVMDKGRIVAYGTVEEIFLQ 228
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
10-187 |
3.14e-15 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 76.66 E-value: 3.14e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 10 SDVSLRYGKTVALDRITLDVPAGLTTGLIGPDGVGKSSLLALASGARALQTGGVdALGGdmrSRRHRERVCRRIAYMPQG 89
Cdd:PRK11248 5 SHLYADYGGKPALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSI-TLDG---KPVEGPGAERGVVFQNEG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 90 LgknlYPTLSVEENLQFFARLFGHDAGERRRRIDALTQSTGLFPFLSRPAGKLSGGMKQKLGLCCALIHDPDLLILDEPT 169
Cdd:PRK11248 81 L----LPWRNVQDNVAFGLQLAGVEKMQRLEIAHQMLKKVGLEGAEKRYIWQLSGGQRQRVGIARALAANPQLLLLDEPF 156
|
170
....*....|....*...
gi 505416896 170 TGVDPLARAQFWDLIARI 187
Cdd:PRK11248 157 GALDAFTREQMQTLLLKL 174
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
272-479 |
3.36e-15 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 79.63 E-value: 3.36e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 272 IEARGLTMRFGD--FtAVDHVSFRIRRGEIFGFLGSNGCGKSTTMKMLTGLLPATEGTAQLFGKEVDPKDINTRRRVgyM 349
Cdd:PRK10522 323 LELRNVTFAYQDngF-SVGPINLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKPVTAEQPEDYRKL--F 399
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 350 SQAFS---LYSELTVRQNlvlharlFGVPAAEIDARVD--EMARRFGLADiyGMLPD-SLPLGMRQRLSLAVAMVHKPEL 423
Cdd:PRK10522 400 SAVFTdfhLFDQLLGPEG-------KPANPALVEKWLErlKMAHKLELED--GRISNlKLSKGQKKRLALLLALAEERDI 470
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 505416896 424 LILDEPTSGVDPVARDSFWQLMIDLARRDLVTIFISTHFMNEAQRCDRISLMHAGR 479
Cdd:PRK10522 471 LLLDEWAADQDPHFRREFYQVLLPLLQEMGKTIFAISHDDHYFIHADRLLEMRNGQ 526
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
3-228 |
3.40e-15 |
|
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: 75.93 E-value: 3.40e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 3 ASSVVRFSDVSLRY----GKTVALDRITLDVPAGLTTGLIGPDGVGKSSLLALASGARALQTGGV-------DALGGDMR 71
Cdd:COG4181 5 SAPIIELRGLTKTVgtgaGELTILKGISLEVEAGESVAIVGASGSGKSTLLGLLAGLDRPTSGTVrlagqdlFALDEDAR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 72 SrrhrervcrriAYMPQGLG-----KNLYPTLSVEENLQFFARLFGH-DAGERRRridALTQSTGLFPFLS-RPAGkLSG 144
Cdd:COG4181 85 A-----------RLRARHVGfvfqsFQLLPTLTALENVMLPLELAGRrDARARAR---ALLERVGLGHRLDhYPAQ-LSG 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 145 GMKQKLGLCCALIHDPDLLILDEPTTGVDPLARAQFWDLIARIRDERPTMSVIVaTAYMDEAQRFDWLIAMDAGRVLATG 224
Cdd:COG4181 150 GEQQRVALARAFATEPAILFADEPTGNLDAATGEQIIDLLFELNRERGTTLVLV-THDPALAARCDRVLRLRAGRLVEDT 228
|
....
gi 505416896 225 APAE 228
Cdd:COG4181 229 AATA 232
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
274-483 |
3.62e-15 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 76.50 E-value: 3.62e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 274 ARGLTMRFGDFTAVDHVSFRIRRGEIFGFLGSNGCGKSTTMKMLTGLLPATEGTAQLFGKEVDPKDINT-----RRRV-- 346
Cdd:PRK11701 9 VRGLTKLYGPRKGCRDVSFDLYPGEVLGIVGESGSGKTTLLNALSARLAPDAGEVHYRMRDGQLRDLYAlseaeRRRLlr 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 347 ---GYMSQ--AFSLYSELTVRQNLVlhARLFGVPA----------------AEIDA-RVDEMARRFGladiyGmlpdslp 404
Cdd:PRK11701 89 tewGFVHQhpRDGLRMQVSAGGNIG--ERLMAVGArhygdiratagdwlerVEIDAaRIDDLPTTFS-----G------- 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 405 lGMRQRLSLAVAMVHKPELLILDEPTSGVDpV---ARdsfwqlMIDLARRdLVT-----IFISTHFMNEAQ-RCDRISLM 475
Cdd:PRK11701 155 -GMQQRLQIARNLVTHPRLVFMDEPTGGLD-VsvqAR------LLDLLRG-LVRelglaVVIVTHDLAVARlLAHRLLVM 225
|
....*...
gi 505416896 476 HAGRVLAS 483
Cdd:PRK11701 226 KQGRVVES 233
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
281-490 |
4.09e-15 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 76.07 E-value: 4.09e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 281 FGDFTAVDHVSFRIRRGEIFGFLGSNGCGKSTTMKMLTGLLPATEGTAQLFGKEVD--PKDINTRRRVGYMSQAFSLYSE 358
Cdd:PRK11614 15 YGKIQALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDGKDITdwQTAKIMREAVAIVPEGRRVFSR 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 359 LTVRQNLVLharlfGVPAAEIDARVDEMARrfgladIYGMLP----------DSLPLGMRQRLSLAVAMVHKPELLILDE 428
Cdd:PRK11614 95 MTVEENLAM-----GGFFAERDQFQERIKW------VYELFPrlherriqraGTMSGGEQQMLAIGRALMSQPRLLLLDE 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 505416896 429 PTSGVDPVARDSFWQLMIDLaRRDLVTIFISTHFMNEAQR-CDRISLMHAGRVLASDSPAELV 490
Cdd:PRK11614 164 PSLGLAPIIIQQIFDTIEQL-REQGMTIFLVEQNANQALKlADRGYVLENGHVVLEDTGDALL 225
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
7-234 |
4.34e-15 |
|
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: 75.99 E-value: 4.34e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 7 VRFSDVSLRYG--KTVALDRITLDVPAGLTTGLIGPDGVGKSSLLALASGARALQTGGVDALGGDMrSRRHRERVCRRIA 84
Cdd:cd03252 1 ITFEHVRFRYKpdGPVILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGHDL-ALADPAWLRRQVG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 85 YMPQglgKNLYPTLSVEENLQFfarlfgHDAGERRRRIDALTQSTGLFPFLSR-PAG----------KLSGGMKQKLGLC 153
Cdd:cd03252 80 VVLQ---ENVLFNRSIRDNIAL------ADPGMSMERVIEAAKLAGAHDFISElPEGydtivgeqgaGLSGGQRQRIAIA 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 154 CALIHDPDLLILDEPTTGVDPLARAQFWDLIARIRDERptmSVIVATAYMDEAQRFDWLIAMDAGRVLATGAPAELLART 233
Cdd:cd03252 151 RALIHNPRILIFDEATSALDYESEHAIMRNMHDICAGR---TVIIIAHRLSTVKNADRIIVMEKGRIVEQGSHDELLAEN 227
|
.
gi 505416896 234 G 234
Cdd:cd03252 228 G 228
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
1-229 |
4.43e-15 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 76.33 E-value: 4.43e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 1 MNASSVVRFSDVSLRYGKTVA--LDRITLDVPAGLTTGLIGPDGVGKSSLLALASGARALQTGGVdaLGGDMRSRRHREr 78
Cdd:PRK13648 2 EDKNSIIVFKNVSFQYQSDASftLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEI--FYNNQAITDDNF- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 79 vcrriaympQGLGKNLYPTLSVEENlQFFARLFGHDAG-----------ERRRRIDALTQSTGLFPFLSRPAGKLSGGMK 147
Cdd:PRK13648 79 ---------EKLRKHIGIVFQNPDN-QFVGSIVKYDVAfglenhavpydEMHRRVSEALKQVDMLERADYEPNALSGGQK 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 148 QKLGLCCALIHDPDLLILDEPTTGVDPLARAQFWDLIARIRDERpTMSVIVATAYMDEAQRFDWLIAMDAGRVLATGAPA 227
Cdd:PRK13648 149 QRVAIAGVLALNPSVIILDEATSMLDPDARQNLLDLVRKVKSEH-NITIISITHDLSEAMEADHVIVMNKGTVYKEGTPT 227
|
..
gi 505416896 228 EL 229
Cdd:PRK13648 228 EI 229
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
6-251 |
4.67e-15 |
|
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440743 [Multi-domain] Cd Length: 239 Bit Score: 75.80 E-value: 4.67e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 6 VVRFSDVSLRYGKTVALDRITLDVPAGLTTGLIGPDGVGKSSLLalasgaRALQ-----TGGVDALGGDmrsrrHRERVC 80
Cdd:COG1126 1 MIEIENLHKSFGDLEVLKGISLDVEKGEVVVIIGPSGSGKSTLL------RCINlleepDSGTITVDGE-----DLTDSK 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 81 RRIAYMPQGLG-----KNLYPTLSVEENLQfFA--RLFGHDAGERRRRIDALTQSTGLFPFLSRPAGKLSGGMKQKLGLC 153
Cdd:COG1126 70 KDINKLRRKVGmvfqqFNLFPHLTVLENVT-LApiKVKKMSKAEAEERAMELLERVGLADKADAYPAQLSGGQQQRVAIA 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 154 CALIHDPDLLILDEPTTGVDP------LaraqfwDLIARIRDERPTMsvIVATAYMDEAQR-FDWLIAMDAGRVLATGAP 226
Cdd:COG1126 149 RALAMEPKVMLFDEPTSALDPelvgevL------DVMRDLAKEGMTM--VVVTHEMGFAREvADRVVFMDGGRIVEEGPP 220
|
250 260
....*....|....*....|....*
gi 505416896 227 AELLARtgcdsleaafiallPENER 251
Cdd:COG1126 221 EEFFEN--------------PQHER 231
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
15-434 |
4.91e-15 |
|
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: 79.21 E-value: 4.91e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 15 RYGKTVA-----LDRITLDVPAGLTTGLIGPDGVGKSSLLALASGaralqtggVDA-LGGDMRsrrhrERVCRRIAYMPQ 88
Cdd:TIGR03719 9 RVSKVVPpkkeiLKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAG--------VDKdFNGEAR-----PQPGIKVGYLPQ 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 89 GlgKNLYPTLSVEENL---------------QFFARLFGHDA-----GERRRRIDALTQSTGLFPFLSR----------- 137
Cdd:TIGR03719 76 E--PQLDPTKTVRENVeegvaeikdaldrfnEISAKYAEPDAdfdklAAEQAELQEIIDAADAWDLDSQleiamdalrcp 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 138 ----PAGKLSGGMKQKLGLCCALIHDPDLLILDEPTTGVDplARAQFWdlIARIRDERPTmSVIVATA---YMDEAQrfD 210
Cdd:TIGR03719 154 pwdaDVTKLSGGERRRVALCRLLLSKPDMLLLDEPTNHLD--AESVAW--LERHLQEYPG-TVVAVTHdryFLDNVA--G 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 211 WLIAMDAGRvlatGAPAE----------------------LLARTGCDSLE-----------------AAFIALLPENER 251
Cdd:TIGR03719 227 WILELDRGR----GIPWEgnysswleqkqkrleqeekeesARQKTLKRELEwvrqspkgrqakskarlARYEELLSQEFQ 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 252 RGHKPVKIEPLRADARAGTAIEARGLTMRFGDFTAVDHVSFRIRRGEIFGFLGSNGCGKSTTMKMLTGLLPATEGTAQLf 331
Cdd:TIGR03719 303 KRNETAEIYIPPGPRLGDKVIEAENLTKAFGDKLLIDDLSFKLPPGGIVGVIGPNGAGKSTLFRMITGQEQPDSGTIEI- 381
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 332 GKEVdpkdintrrRVGYMSQAF-SLYSELTVRQNLVLHARLFGVPAAEIDARVDEMARRFGLADIYGMLpDSLPLGMRQR 410
Cdd:TIGR03719 382 GETV---------KLAYVDQSRdALDPNKTVWEEISGGLDIIKLGKREIPSRAYVGRFNFKGSDQQKKV-GQLSGGERNR 451
|
490 500
....*....|....*....|....
gi 505416896 411 LSLAVAMVHKPELLILDEPTSGVD 434
Cdd:TIGR03719 452 VHLAKTLKSGGNVLLLDEPTNDLD 475
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
1-229 |
5.85e-15 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 77.45 E-value: 5.85e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 1 MNASSVVRFSDVSLRYGKTVALDRITLDVPAGLTTGLIGPDGVGKSSLLALASGARALQTGGVDALGGDM--RSRRHRER 78
Cdd:PRK11432 1 MTQKNFVVLKNITKRFGSNTVIDNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIFIDGEDVthRSIQQRDI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 79 VCRRIAYMpqglgknLYPTLSVEENLQFFARLFGHDAGERRRRIDALTQSTGLFPFLSRPAGKLSGGMKQKLGLCCALIH 158
Cdd:PRK11432 81 CMVFQSYA-------LFPHMSLGENVGYGLKMLGVPKEERKQRVKEALELVDLAGFEDRYVDQISGGQQQRVALARALIL 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 505416896 159 DPDLLILDEPTTGVDPLARAQFWDliaRIRDERPTMSVIVATAYMDEAQRF---DWLIAMDAGRVLATGAPAEL 229
Cdd:PRK11432 154 KPKVLLFDEPLSNLDANLRRSMRE---KIRELQQQFNITSLYVTHDQSEAFavsDTVIVMNKGKIMQIGSPQEL 224
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
4-190 |
6.69e-15 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 75.54 E-value: 6.69e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 4 SSVVRFSDVSLRYGKTVALDRITLDVPAGLTTGLIGPDGVGKSSLLALASGARALQTGGVDALGGdmrsrrhrervcRRI 83
Cdd:PRK09544 2 TSLVSLENVSVSFGQRRVLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIKRNGK------------LRI 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 84 AYMPQGLgkNLYPTLSVeeNLQFFARLfghDAGERRRRIDALTQSTGLFPFLSRPAGKLSGGMKQKLGLCCALIHDPDLL 163
Cdd:PRK09544 70 GYVPQKL--YLDTTLPL--TVNRFLRL---RPGTKKEDILPALKRVQAGHLIDAPMQKLSGGETQRVLLARALLNRPQLL 142
|
170 180
....*....|....*....|....*..
gi 505416896 164 ILDEPTTGVDPLARAQFWDLIARIRDE 190
Cdd:PRK09544 143 VLDEPTQGVDVNGQVALYDLIDQLRRE 169
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
24-231 |
6.75e-15 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 75.00 E-value: 6.75e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 24 RITLDVPAGLTTGLIGPDGVGKSSLLALASGARALQTGGVDALGGDMRSRRhrervcrrIAYMPQGL---GKNLYPTLSV 100
Cdd:PRK10771 17 RFDLTVERGERVAILGPSGAGKSTLLNLIAGFLTPASGSLTLNGQDHTTTP--------PSRRPVSMlfqENNLFSHLTV 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 101 EENLQFfarlfGHDAG-----ERRRRIDALTQSTGLFPFLSRPAGKLSGGMKQKLGLCCALIHDPDLLILDEPTTGVDPL 175
Cdd:PRK10771 89 AQNIGL-----GLNPGlklnaAQREKLHAIARQMGIEDLLARLPGQLSGGQRQRVALARCLVREQPILLLDEPFSALDPA 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 505416896 176 ARAQFWDLIARIRDERPTMSVIVATAYMDEAQRFDWLIAMDAGRVLATGAPAELLA 231
Cdd:PRK10771 164 LRQEMLTLVSQVCQERQLTLLMVSHSLEDAARIAPRSLVVADGRIAWDGPTDELLS 219
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
6-169 |
7.54e-15 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 78.57 E-value: 7.54e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 6 VVRFSDVSLRYGKTVALDRITLDVPAGLTTGLIGPDGVGKSSLLALASGARALQTGGVDaLGGDMRsrrhrervcrrIAY 85
Cdd:COG0488 315 VLELEGLSKSYGDKTLLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPDSGTVK-LGETVK-----------IGY 382
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 86 MPQGLgKNLYPTLSVEENLQFFArlfghDAGERRRRIDALtqstGLFPF----LSRPAGKLSGGMKQKLGLCCALIHDPD 161
Cdd:COG0488 383 FDQHQ-EELDPDKTVLDELRDGA-----PGGTEQEVRGYL----GRFLFsgddAFKPVGVLSGGEKARLALAKLLLSPPN 452
|
....*...
gi 505416896 162 LLILDEPT 169
Cdd:COG0488 453 VLLLDEPT 460
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
5-233 |
1.24e-14 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 75.61 E-value: 1.24e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 5 SVVRFSDVSLRY--GKTVALDRITLDVPAGLTTGLIGPDGVGKSSLLALASG-------ARALQTggVDALGGDMRSRRH 75
Cdd:PRK13640 4 NIVEFKHVSFTYpdSKKPALNDISFSIPRGSWTALIGHNGSGKSTISKLINGlllpddnPNSKIT--VDGITLTAKTVWD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 76 RERVCRRIAYMPQglgkNLYPTLSVEENLQFFARLFGHDAGERRRRIDALTQSTGLFPFLSRPAGKLSGGMKQKLGLCCA 155
Cdd:PRK13640 82 IREKVGIVFQNPD----NQFVGATVGDDVAFGLENRAVPRPEMIKIVRDVLADVGMLDYIDSEPANLSGGQKQRVAIAGI 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 505416896 156 LIHDPDLLILDEPTTGVDPLARAQFWDLIARIRDERpTMSVIVATAYMDEAQRFDWLIAMDAGRVLATGAPAELLART 233
Cdd:PRK13640 158 LAVEPKIIILDESTSMLDPAGKEQILKLIRKLKKKN-NLTVISITHDIDEANMADQVLVLDDGKLLAQGSPVEIFSKV 234
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
7-220 |
1.33e-14 |
|
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: 73.72 E-value: 1.33e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 7 VRFSDVSLRYGKTVALDRITLDVPAGLTTGLIGPDGVGKSSLLalasgaRALQ-----TGGVDALGGDmrsrrHRERVCR 81
Cdd:cd03262 1 IEIKNLHKSFGDFHVLKGIDLTVKKGEVVVIIGPSGSGKSTLL------RCINlleepDSGTIIIDGL-----KLTDDKK 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 82 RIAYMPQGLGK-----NLYPTLSVEENLQFFAR-LFGHDAGERRRRIDALTQSTGLFPFLSRPAGKLSGGMKQKLGLCCA 155
Cdd:cd03262 70 NINELRQKVGMvfqqfNLFPHLTVLENITLAPIkVKGMSKAEAEERALELLEKVGLADKADAYPAQLSGGQQQRVAIARA 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 505416896 156 LIHDPDLLILDEPTTGVDPLARAQFWDLIARIRDERPTMsvIVATAYMDEAQRF-DWLIAMDAGRV 220
Cdd:cd03262 150 LAMNPKVMLFDEPTSALDPELVGEVLDVMKDLAEEGMTM--VVVTHEMGFAREVaDRVIFMDDGRI 213
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
11-228 |
1.38e-14 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 73.67 E-value: 1.38e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 11 DVSLRYGKTVALDRITLDVPAGLTTGLIGPDGVGKSSLLALASG--ARALQTGGVDALGGdmRSRRHRERVCRRIAYMPQ 88
Cdd:COG4136 6 NLTITLGGRPLLAPLSLTVAPGEILTLMGPSGSGKSTLLAAIAGtlSPAFSASGEVLLNG--RRLTALPAEQRRIGILFQ 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 89 -GLgknLYPTLSVEENLQF-FARLFGHdaGERRRRIDALTQSTGLFPFLSRPAGKLSGGMKQKLGLCCALIHDPDLLILD 166
Cdd:COG4136 84 dDL---LFPHLSVGENLAFaLPPTIGR--AQRRARVEQALEEAGLAGFADRDPATLSGGQRARVALLRALLAEPRALLLD 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 505416896 167 EPTTGVDPLARAQFWDLI-ARIRDERptMSVIVATAYMDEAQrfdwliamDAGRVLATGAPAE 228
Cdd:COG4136 159 EPFSKLDAALRAQFREFVfEQIRQRG--IPALLVTHDEEDAP--------AAGRVLDLGNWQH 211
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
281-480 |
1.48e-14 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 73.76 E-value: 1.48e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 281 FGDFTAVDHVSFRIRRGEIFGFLGSNGCGKSTTMKMLTGLLPATEGTAQLFGKEVDPKDINT----RRRVGYMSQAFSLY 356
Cdd:PRK10908 12 LGGRQALQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDITRLKNREvpflRRQIGMIFQDHHLL 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 357 SELTVRQNLVLHARLFGVPAAEIDARVDEMARRFGLADIYGMLPDSLPLGMRQRLSLAVAMVHKPELLILDEPTSGVDPV 436
Cdd:PRK10908 92 MDRTVYDNVAIPLIIAGASGDDIRRRVSAALDKVGLLDKAKNFPIQLSGGEQQRVGIARAVVNKPAVLLADEPTGNLDDA 171
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 505416896 437 ARDSFWQLMIDLARRDlVTIFISTHFMNE-AQRCDRISLMHAGRV 480
Cdd:PRK10908 172 LSEGILRLFEEFNRVG-VTVLMATHDIGLiSRRSYRMLTLSDGHL 215
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
2-234 |
1.57e-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: 78.24 E-value: 1.57e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 2 NASSVVRFSDVSLRYG-KTVALDRITLDVPAGLTTGLIGPDGVGKSSLLALASGARALQTGGVdALGGDMRSRRHRERVC 80
Cdd:TIGR01193 469 NLNGDIVINDVSYSYGyGSNILSDISLTIKMNSKTTIVGMSGSGKSTLAKLLVGFFQARSGEI-LLNGFSLKDIDRHTLR 547
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 81 RRIAYMPQglgKNLYPTLSVEENLQFFAR--------LFGHDAGERRRRIDALTQstGLFPFLSRPAGKLSGGMKQKLGL 152
Cdd:TIGR01193 548 QFINYLPQ---EPYIFSGSILENLLLGAKenvsqdeiWAACEIAEIKDDIENMPL--GYQTELSEEGSSISGGQKQRIAL 622
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 153 CCALIHDPDLLILDEPTTGVDPLARAQFWDLIARIRDErptmSVIVATAYMDEAQRFDWLIAMDAGRVLATGAPAELLAR 232
Cdd:TIGR01193 623 ARALLTDSKVLILDESTSNLDTITEKKIVNNLLNLQDK----TIIFVAHRLSVAKQSDKIIVLDHGKIIEQGSHDELLDR 698
|
..
gi 505416896 233 TG 234
Cdd:TIGR01193 699 NG 700
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
265-495 |
2.60e-14 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 77.19 E-value: 2.60e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 265 DARAGTAIEARGLTMRFGDFTA-VDHVSFRIRRGEIFGFLGSNGCGKSTTMKMLTGLLPaTEGTAQLFGKEVDPKDINT- 342
Cdd:PRK11174 343 ASNDPVTIEAEDLEILSPDGKTlAGPLNFTLPAGQRIALVGPSGAGKTSLLNALLGFLP-YQGSLKINGIELRELDPESw 421
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 343 RRRVGYMSQAFSLYsELTVRQNLVLharlfGVPAAEiDARVDEMARRFGLADIYGMLPDSL--PLGMR---------QRL 411
Cdd:PRK11174 422 RKHLSWVGQNPQLP-HGTLRDNVLL-----GNPDAS-DEQLQQALENAWVSEFLPLLPQGLdtPIGDQaaglsvgqaQRL 494
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 412 SLAVAMVHKPELLILDEPTSGVDpvaRDSFWQLMIDL--ARRDLVTIFIsTHFMNEAQRCDRISLMHAGRVLASDSPAEL 489
Cdd:PRK11174 495 ALARALLQPCQLLLLDEPTASLD---AHSEQLVMQALnaASRRQTTLMV-THQLEDLAQWDQIWVMQDGQIVQQGDYAEL 570
|
....*.
gi 505416896 490 VRARGA 495
Cdd:PRK11174 571 SQAGGL 576
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
7-233 |
2.75e-14 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 74.43 E-value: 2.75e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 7 VRFSDVSLRYGK-----TVALDRITLDVPAGLTTGLIGPDGVGKSSLLALASGARALQTGGVDAlgGDMRsrRHRERVCR 81
Cdd:PRK13646 3 IRFDNVSYTYQKgtpyeHQAIHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTV--DDIT--ITHKTKDK 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 82 RIAYMPQGLG-------KNLYPTlSVEENLQFFARLFGHDAGERRRRIDALTQSTGlFP--FLSRPAGKLSGGMKQKLGL 152
Cdd:PRK13646 79 YIRPVRKRIGmvfqfpeSQLFED-TVEREIIFGPKNFKMNLDEVKNYAHRLLMDLG-FSrdVMSQSPFQMSGGQMRKIAI 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 153 CCALIHDPDLLILDEPTTGVDPLARAQFWDLIARIRDERpTMSVIVATAYMDEAQRF-DWLIAMDAGRVLATGAPAELLA 231
Cdd:PRK13646 157 VSILAMNPDIIVLDEPTAGLDPQSKRQVMRLLKSLQTDE-NKTIILVSHDMNEVARYaDEVIVMKEGSIVSQTSPKELFK 235
|
..
gi 505416896 232 RT 233
Cdd:PRK13646 236 DK 237
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
4-175 |
3.69e-14 |
|
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: 72.69 E-value: 3.69e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 4 SSVVRFSDVSL---RYGKTV-ALDRITLDVPAGLTTGLIGPDGVGKSSLLALASGaRALQ---TGGVDALGGDMRSRRHR 76
Cdd:cd03234 1 QRVLPWWDVGLkakNWNKYArILNDVSLHVESGQVMAILGSSGSGKTTLLDAISG-RVEGggtTSGQILFNGQPRKPDQF 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 77 ERVcrrIAYMPQGlgKNLYPTLSVEENLQFFA--RLFGHDAGERRRRIDALTQSTGLFpfLSRPAGK----LSGGMKQKL 150
Cdd:cd03234 80 QKC---VAYVRQD--DILLPGLTVRETLTYTAilRLPRKSSDAIRKKRVEDVLLRDLA--LTRIGGNlvkgISGGERRRV 152
|
170 180
....*....|....*....|....*
gi 505416896 151 GLCCALIHDPDLLILDEPTTGVDPL 175
Cdd:cd03234 153 SIAVQLLWDPKVLILDEPTSGLDSF 177
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
7-234 |
3.73e-14 |
|
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC transporter that is expressed in the mitochondria. Although the specific function of ATM1 is unknown, its disruption results in the accumulation of excess mitochondrial iron, loss of mitochondrial cytochromes, oxidative damage to mitochondrial DNA, and decreased levels of cytosolic heme proteins. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213220 [Multi-domain] Cd Length: 236 Bit Score: 73.03 E-value: 3.73e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 7 VRFSDVSLRY--GKTVaLDRITLDVPAGLTTGLIGPDGVGKSSLLAL-------ASGAraLQTGGVDALGGDMRSRRHRe 77
Cdd:cd03253 1 IEFENVTFAYdpGRPV-LKDVSFTIPAGKKVAIVGPSGSGKSTILRLlfrfydvSSGS--ILIDGQDIREVTLDSLRRA- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 78 rvcrrIAYMPQG-------LGKNL-YPTLSVEENLQFFARL------------FGHDA--GERrrridaltqstGLfpfl 135
Cdd:cd03253 77 -----IGVVPQDtvlfndtIGYNIrYGRPDATDEEVIEAAKaaqihdkimrfpDGYDTivGER-----------GL---- 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 136 srpagKLSGGMKQKLGLCCALIHDPDLLILDEPTTGVDPLARAQFWDLIARIRDERPTmsVIVA---TAYMDEaqrfDWL 212
Cdd:cd03253 137 -----KLSGGEKQRVAIARAILKNPPILLLDEATSALDTHTEREIQAALRDVSKGRTT--IVIAhrlSTIVNA----DKI 205
|
250 260
....*....|....*....|..
gi 505416896 213 IAMDAGRVLATGAPAELLARTG 234
Cdd:cd03253 206 IVLKDGRIVERGTHEELLAKGG 227
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
288-478 |
3.89e-14 |
|
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: 71.89 E-value: 3.89e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 288 DHVSFRIRRGEIFGFLGSNGCGKSTTMKMLTGLLPA--TEGTAQLFGKevdPKDINTRRRVGYMSQAFSLYSELTVRQNL 365
Cdd:cd03232 24 NNISGYVKPGTLTALMGESGAGKTTLLDVLAGRKTAgvITGEILINGR---PLDKNFQRSTGYVEQQDVHSPNLTVREAL 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 366 VLHARLFGvpaaeidarvdemarrfgladiygmlpdsLPLGMRQRLSLAVAMVHKPELLILDEPTSGVDPVARDSFWQLM 445
Cdd:cd03232 101 RFSALLRG-----------------------------LSVEQRKRLTIGVELAAKPSILFLDEPTSGLDSQAAYNIVRFL 151
|
170 180 190
....*....|....*....|....*....|....*
gi 505416896 446 IDLARRDLvTIFISTHFMNEA--QRCDRISLMHAG 478
Cdd:cd03232 152 KKLADSGQ-AILCTIHQPSASifEKFDRLLLLKRG 185
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
15-242 |
3.99e-14 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 75.45 E-value: 3.99e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 15 RYGKTVALDRITLDVPAGLTTGLIGPDGVGKSSLLALASGARALQTGGVDALGGDM---RSRRHRERVCRRIAYMPQGLG 91
Cdd:PRK10070 37 KTGLSLGVKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIakiSDAELREVRRKKIAMVFQSFA 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 92 knLYPTLSVEENLQFFARLFGHDAGERRRR-IDALTQsTGLFPFLSRPAGKLSGGMKQKLGLCCALIHDPDLLILDEPTT 170
Cdd:PRK10070 117 --LMPHMTVLDNTAFGMELAGINAEERREKaLDALRQ-VGLENYAHSYPDELSGGMRQRVGLARALAINPDILLMDEAFS 193
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 505416896 171 GVDPLARAQFWDLIARIRdERPTMSVIVATAYMDEAQRF-DWLIAMDAGRVLATGAPAELLARTGCDSLEAAF 242
Cdd:PRK10070 194 ALDPLIRTEMQDELVKLQ-AKHQRTIVFISHDLDEAMRIgDRIAIMQNGEVVQVGTPDEILNNPANDYVRTFF 265
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
290-496 |
4.09e-14 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 77.32 E-value: 4.09e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 290 VSFRIRRGEIFGFLGSNGCGKSTTMKMLTGLLPATEGTAQLFGKEVDPKDINTRRRV-GYMSQAFSLYSElTVRQNLVlh 368
Cdd:PLN03232 1255 LSFFVSPSEKVGVVGRTGAGKSSMLNALFRIVELEKGRIMIDDCDVAKFGLTDLRRVlSIIPQSPVLFSG-TVRFNID-- 1331
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 369 arlfgvPAAEI-DARVDEMARRFGLADIYGMLP-----------DSLPLGMRQRLSLAVAMVHKPELLILDEPTSGVDpV 436
Cdd:PLN03232 1332 ------PFSEHnDADLWEALERAHIKDVIDRNPfgldaevseggENFSVGQRQLLSLARALLRRSKILVLDEATASVD-V 1404
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 437 ARDSFWQLMIDLARRDlVTIFISTHFMNEAQRCDRISLMHAGRVLASDSPAELVRARGAA 496
Cdd:PLN03232 1405 RTDSLIQRTIREEFKS-CTMLVIAHRLNTIIDCDKILVLSSGQVLEYDSPQELLSRDTSA 1463
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
270-453 |
4.55e-14 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 73.22 E-value: 4.55e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 270 TAIEARGLTMRFGDFTAVDHVSFRIRRGEIFGFLGSNGCGKSTTMKMLTGLLPATEGTAQLfgkevdpkdiNTRRRVGYM 349
Cdd:PRK09544 3 SLVSLENVSVSFGQRRVLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIKR----------NGKLRIGYV 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 350 SQAFSLYSE--LTVRQNLVLHArlfGVPAAEIDARVdemaRRFGLADIYGMLPDSLPLGMRQRLSLAVAMVHKPELLILD 427
Cdd:PRK09544 73 PQKLYLDTTlpLTVNRFLRLRP---GTKKEDILPAL----KRVQAGHLIDAPMQKLSGGETQRVLLARALLNRPQLLVLD 145
|
170 180
....*....|....*....|....*.
gi 505416896 428 EPTSGVDPVARDSFWQLmIDLARRDL 453
Cdd:PRK09544 146 EPTQGVDVNGQVALYDL-IDQLRREL 170
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
288-449 |
5.20e-14 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 76.69 E-value: 5.20e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 288 DHVSFRIRRGEIFGFLGSNGCGKSTTMKML-----TGLLpaTEGTAQLFGKevdPKDINTRRRVGYMSQAFSLYSELTVR 362
Cdd:TIGR00956 780 NNVDGWVKPGTLTALMGASGAGKTTLLNVLaervtTGVI--TGGDRLVNGR---PLDSSFQRSIGYVQQQDLHLPTSTVR 854
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 363 QNLVLHARLF---GVPAAEIDARVDEMARRFGL---AD-IYGMLPDSLPLGMRQRLSLAVAMVHKPELLI-LDEPTSGVD 434
Cdd:TIGR00956 855 ESLRFSAYLRqpkSVSKSEKMEYVEEVIKLLEMesyADaVVGVPGEGLNVEQRKRLTIGVELVAKPKLLLfLDEPTSGLD 934
|
170
....*....|....*
gi 505416896 435 PVARDSFWQLMIDLA 449
Cdd:TIGR00956 935 SQTAWSICKLMRKLA 949
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
7-223 |
7.16e-14 |
|
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: 70.15 E-value: 7.16e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 7 VRFSDVSLRYGKTVALDRITLDVPAGLTTGLIGPDGVGKSSLLALASGARALQTGgvdalggdmrsrrhrervcrriaym 86
Cdd:cd03216 1 LELRGITKRFGGVKALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSG------------------------- 55
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 87 pqglgknlypTLSVEENLQFFARLfgHDAgeRRRRIDALTQstglfpflsrpagkLSGGMKQKLGLCCALIHDPDLLILD 166
Cdd:cd03216 56 ----------EILVDGKEVSFASP--RDA--RRAGIAMVYQ--------------LSVGERQMVEIARALARNARLLILD 107
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 505416896 167 EPTTGVDPLARAQFWDLIARIRDErpTMSVIVATAYMDEAQRF-DWLIAMDAGRVLAT 223
Cdd:cd03216 108 EPTAALTPAEVERLFKVIRRLRAQ--GVAVIFISHRLDEVFEIaDRVTVLRDGRVVGT 163
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
10-229 |
7.34e-14 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 72.72 E-value: 7.34e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 10 SDVSLRYGKTVALDRITLDVPAGLTTGLIGPDGVGKSSLLALASGARAlQTGGVDALGGDmrsrrhrervcrRIAYMP-- 87
Cdd:PRK11300 9 SGLMMRFGGLLAVNNVNLEVREQEIVSLIGPNGAGKTTVFNCLTGFYK-PTGGTILLRGQ------------HIEGLPgh 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 88 ----QGLGKN-----LYPTLSVEENL----------QFFARLFgHDAGERRRRIDALTQST------GLFPFLSRPAGKL 142
Cdd:PRK11300 76 qiarMGVVRTfqhvrLFREMTVIENLlvaqhqqlktGLFSGLL-KTPAFRRAESEALDRAAtwlervGLLEHANRQAGNL 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 143 SGGMKQKLGLCCALIHDPDLLILDEPTTGVDPLARAQFWDLIARIRDERPT--------MSVIvatayMDEAQRfdwLIA 214
Cdd:PRK11300 155 AYGQQRRLEIARCMVTQPEILMLDEPAAGLNPKETKELDELIAELRNEHNVtvlliehdMKLV-----MGISDR---IYV 226
|
250
....*....|....*
gi 505416896 215 MDAGRVLATGAPAEL 229
Cdd:PRK11300 227 VNQGTPLANGTPEEI 241
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
22-206 |
1.08e-13 |
|
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: 71.73 E-value: 1.08e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 22 LDRITLDVPAGLTTGLIGPDGVGKSSLLALASGARALQTGGVDALGGDMRSRRHRErvcrriayMPQGLGKNLYPTLSVE 101
Cdd:TIGR01184 1 LKGVNLTIQQGEFISLIGHSGCGKSTLLNLISGLAQPTSGGVILEGKQITEPGPDR--------MVVFQNYSLLPWLTVR 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 102 ENLQFFARLFGHDA--GERRRRIDALTQSTGLFPFLSRPAGKLSGGMKQKLGLCCALIHDPDLLILDEPTTGVDPLARAQ 179
Cdd:TIGR01184 73 ENIALAVDRVLPDLskSERRAIVEEHIALVGLTEAADKRPGQLSGGMKQRVAIARALSIRPKVLLLDEPFGALDALTRGN 152
|
170 180
....*....|....*....|....*...
gi 505416896 180 FWDLIARIRDE-RPTmsVIVATAYMDEA 206
Cdd:TIGR01184 153 LQEELMQIWEEhRVT--VLMVTHDVDEA 178
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
7-234 |
1.16e-13 |
|
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 (also known as ABCB6) is a mitochondrial ATP-binding cassette protein involved in iron homeostasis and one of four ABC transporters expressed in the mitochondrial inner membrane, the other three being MDL1(ABC7), MDL2, and ATM1. In fact, the yeast MDL1 (multidrug resistance-like protein 1) and MDL2 (multidrug resistance-like protein 2) transporters are also included in this CD. MDL1 is an ATP-dependent permease that acts as a high-copy suppressor of ATM1 and is thought to have a role in resistance to oxidative stress. Interestingly, subfamily B is more closely related to the carboxyl-terminal component of subfamily C than the two halves of ABCC molecules are with one another.
Pssm-ID: 213216 [Multi-domain] Cd Length: 238 Bit Score: 71.80 E-value: 1.16e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 7 VRFSDVSLRY---GKTVALDRITLDVPAGLTTGLIGPDGVGKSSLLALasgaraLQ-----TGGVDALGGDMRSRRHRER 78
Cdd:cd03249 1 IEFKNVSFRYpsrPDVPILKGLSLTIPPGKTVALVGSSGCGKSTVVSL------LErfydpTSGEILLDGVDIRDLNLRW 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 79 VCRRIAYMPQGlgknlyPTL---SVEENLqffarLFGHDAGERRRRIDALTQSTGLFPFLSRPAG----------KLSGG 145
Cdd:cd03249 75 LRSQIGLVSQE------PVLfdgTIAENI-----RYGKPDATDEEVEEAAKKANIHDFIMSLPDGydtlvgergsQLSGG 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 146 MKQKLGLCCALIHDPDLLILDEPTTGVDPLARAQFWDLIARIRDERPTmsvIVATAYMDEAQRFDWLIAMDAGRVLATGA 225
Cdd:cd03249 144 QKQRIAIARALLRNPKILLLDEATSALDAESEKLVQEALDRAMKGRTT---IVIAHRLSTIRNADLIAVLQNGQVVEQGT 220
|
....*....
gi 505416896 226 PAELLARTG 234
Cdd:cd03249 221 HDELMAQKG 229
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
11-231 |
1.43e-13 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 72.03 E-value: 1.43e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 11 DVSLRYGK-TVALDRITLDVPAGLTTGLIGPDGVGKSSLLALASGARALQTGGVDALGGDMR-SRRHRERVCRRIAYMPQ 88
Cdd:PRK13639 6 DLKYSYPDgTEALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIKGEPIKyDKKSLLEVRKTVGIVFQ 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 89 GLGKNLY-PTlsVEENLQFFARLFGHDAGERRRRIDALTQSTGLFPFLSRPAGKLSGGMKQKLGLCCALIHDPDLLILDE 167
Cdd:PRK13639 86 NPDDQLFaPT--VEEDVAFGPLNLGLSKEEVEKRVKEALKAVGMEGFENKPPHHLSGGQKKRVAIAGILAMKPEIIVLDE 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 505416896 168 PTTGVDPLARAQFWDLIARIRDErpTMSVIVATAYMDEAQRF-DWLIAMDAGRVLATGAPAELLA 231
Cdd:PRK13639 164 PTSGLDPMGASQIMKLLYDLNKE--GITIIISTHDVDLVPVYaDKVYVMSDGKIIKEGTPKEVFS 226
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
267-461 |
1.80e-13 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 70.76 E-value: 1.80e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 267 RAGTAIEARGLTMRFGDFTAVDHVSFRIRRGEIFGFLGSNGCGKSTTMKMLTGLLPATEGTAqlfgkEVDPKDINtrrrv 346
Cdd:COG2401 26 RVAIVLEAFGVELRVVERYVLRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGALKGTPVAG-----CVDVPDNQ----- 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 347 gymsqafsLYSELTVRQNLvlhARLFGVPAA-EIDARVdemarrfGLADIYGML--PDSLPLGMRQRLSLAVAMVHKPEL 423
Cdd:COG2401 96 --------FGREASLIDAI---GRKGDFKDAvELLNAV-------GLSDAVLWLrrFKELSTGQKFRFRLALLLAERPKL 157
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 505416896 424 LILDEPTSGVDP-----VARDsfwqlMIDLARRDLVTIFISTH 461
Cdd:COG2401 158 LVIDEFCSHLDRqtakrVARN-----LQKLARRAGITLVVATH 195
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
272-489 |
2.02e-13 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 71.35 E-value: 2.02e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 272 IEARGLTMRFGDFTAVDHVSFRIRRGEIFGFLGSNGCGKSTTMKMLT---GLLP--ATEGTAQLFGKEVDPKDINT---R 343
Cdd:PRK14239 6 LQVSDLSVYYNKKKALNSVSLDFYPNEITALIGPSGSGKSTLLRSINrmnDLNPevTITGSIVYNGHNIYSPRTDTvdlR 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 344 RRVGYMSQA-----FSLYseltvrQNLVLHARLFGVPAAEI-DARVDEMARRFGLAD-IYGMLPDS---LPLGMRQRLSL 413
Cdd:PRK14239 86 KEIGMVFQQpnpfpMSIY------ENVVYGLRLKGIKDKQVlDEAVEKSLKGASIWDeVKDRLHDSalgLSGGQQQRVCI 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 505416896 414 AVAMVHKPELLILDEPTSGVDPVARDSFWQLMIDLarRDLVTIFISTHFMNEAQR-CDRISLMHAGRVLASDSPAEL 489
Cdd:PRK14239 160 ARVLATSPKIILLDEPTSALDPISAGKIEETLLGL--KDDYTMLLVTRSMQQASRiSDRTGFFLDGDLIEYNDTKQM 234
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
22-254 |
2.09e-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: 74.98 E-value: 2.09e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 22 LDRITLDVPAGLTTGLIGPDGVGKSSLLAlasgaralqtggvdALGGDMRSRRHRERVCRRIAYMPQglgKNLYPTLSVE 101
Cdd:TIGR00957 654 LNGITFSIPEGALVAVVGQVGCGKSSLLS--------------ALLAEMDKVEGHVHMKGSVAYVPQ---QAWIQNDSLR 716
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 102 ENLqffarLFGHDAGERRRRidALTQSTGLFPFLS-RPAG----------KLSGGMKQKLGLCCALIHDPDLLILDEPTT 170
Cdd:TIGR00957 717 ENI-----LFGKALNEKYYQ--QVLEACALLPDLEiLPSGdrteigekgvNLSGGQKQRVSLARAVYSNADIYLFDDPLS 789
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 171 GVDPLARAQFWDLIARIRDERPTMSVIVATAYMDEAQRFDWLIAMDAGRVLATGAPAELLARTGCdslEAAFIALLPENE 250
Cdd:TIGR00957 790 AVDAHVGKHIFEHVIGPEGVLKNKTRILVTHGISYLPQVDVIIVMSGGKISEMGSYQELLQRDGA---FAEFLRTYAPDE 866
|
....
gi 505416896 251 RRGH 254
Cdd:TIGR00957 867 QQGH 870
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
7-184 |
2.17e-13 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 70.81 E-value: 2.17e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 7 VRFSDVSLRYGKTVALDRITLDVPAGLTTGLIGPDGVGKSSLLalasgaRALQ-----TGGVDALGGDMRSRRHRERVCR 81
Cdd:COG4161 3 IQLKNINCFYGSHQALFDINLECPSGETLVLLGPSGAGKSSLL------RVLNlletpDSGQLNIAGHQFDFSQKPSEKA 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 82 RIAyMPQGLGK-----NLYPTLSVEENL-QFFARLFGHDAGERRRRIDALTQSTGLFPFLSRPAGKLSGGMKQKLGLCCA 155
Cdd:COG4161 77 IRL-LRQKVGMvfqqyNLWPHLTVMENLiEAPCKVLGLSKEQAREKAMKLLARLRLTDKADRFPLHLSGGQQQRVAIARA 155
|
170 180
....*....|....*....|....*....
gi 505416896 156 LIHDPDLLILDEPTTGVDPLARAQFWDLI 184
Cdd:COG4161 156 LMMEPQVLLFDEPTAALDPEITAQVVEII 184
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
266-506 |
2.20e-13 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 71.45 E-value: 2.20e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 266 ARAGTAIEARGLTMRFGDfTAVDHVSFRIRRGEIFGFLGSNGCGKSTTMKMLTGLLPATEGTAQLFGKEVdpKDINTRRR 345
Cdd:PRK15056 3 QQAGIVVNDVTVTWRNGH-TALRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKISILGQPT--RQALQKNL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 346 VGYMSQA------FSLYSELTVRQNLVLHARLFGVPAAEIDARVDEMARRFGLADIYGMLPDSLPLGMRQRLSLAVAMVH 419
Cdd:PRK15056 80 VAYVPQSeevdwsFPVLVEDVVMMGRYGHMGWLRRAKKRDRQIVTAALARVDMVEFRHRQIGELSGGQKKRVFLARAIAQ 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 420 KPELLILDEPTSGVDPVARDSFWQLMIDLaRRDLVTIFISTHFMNEAQR-CDrISLMHAGRVLASdSPAELVRArgAATL 498
Cdd:PRK15056 160 QGQVILLDEPFTGVDVKTEARIISLLREL-RDEGKTMLVSTHNLGSVTEfCD-YTVMVKGTVLAS-GPTETTFT--AENL 234
|
....*...
gi 505416896 499 EDAFIGYL 506
Cdd:PRK15056 235 ELAFSGVL 242
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
7-200 |
2.28e-13 |
|
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: 73.93 E-value: 2.28e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 7 VRFSDVSLRY-GKTVALDRITLDVPAGLTTGLIGPDGVGKSSLLALASGARALQTGGVdALGGDMRSRRHRERVCRRIAY 85
Cdd:TIGR02868 335 LELRDLSAGYpGAPPVLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPLQGEV-TLDGVPVSSLDQDEVRRRVSV 413
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 86 MPQGlgKNLYPTlSVEENLqffaRLFGHDAGE-------RRRRIDALTQST--GLFPFLSRPAGKLSGGMKQKLGLCCAL 156
Cdd:TIGR02868 414 CAQD--AHLFDT-TVRENL----RLARPDATDeelwaalERVGLADWLRALpdGLDTVLGEGGARLSGGERQRLALARAL 486
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 505416896 157 IHDPDLLILDEPTTGVDPLARAQfwdLIARIRDERPTMSVIVAT 200
Cdd:TIGR02868 487 LADAPILLLDEPTEHLDAETADE---LLEDLLAALSGRTVVLIT 527
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
286-489 |
2.63e-13 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 73.50 E-value: 2.63e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 286 AVDHVSFRIRRGEIFGFLGSNGCGKSTTMKMLTGLLPATEGTAQLFGKEVD---PKDiNTRRRVGYMSQAFSLYSELTVR 362
Cdd:PRK10762 19 ALSGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSILYLGKEVTfngPKS-SQEAGIGIIHQELNLIPQLTIA 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 363 QNLVLhARLFGVPAAEID-----ARVDEMARRFGLADIYGMLPDSLPLGMRQRLSLAVAMVHKPELLILDEPTSGVDPVA 437
Cdd:PRK10762 98 ENIFL-GREFVNRFGRIDwkkmyAEADKLLARLNLRFSSDKLVGELSIGEQQMVEIAKVLSFESKVIIMDEPTDALTDTE 176
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 505416896 438 RDSFWQLMIDLARRDLVTIFIStHFMNEA-QRCDRISLMHAGRVLASDSPAEL 489
Cdd:PRK10762 177 TESLFRVIRELKSQGRGIVYIS-HRLKEIfEICDDVTVFRDGQFIAEREVADL 228
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
2-208 |
2.97e-13 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 70.97 E-value: 2.97e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 2 NASSVVRFSDVSLRYGKTVALDRITLDVPAGLTTGLIGPDGVGKSSLLA-------LASGARA----------LQTGGVD 64
Cdd:PRK14243 6 GTETVLRTENLNVYYGSFLAVKNVWLDIPKNQITAFIGPSGCGKSTILRcfnrlndLIPGFRVegkvtfhgknLYAPDVD 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 65 ALggDMRSrrhrervcrRIAYMPQglGKNLYPTlSVEENLQFFARLFGHDAG-----ERRRR--------IDALTQStGL 131
Cdd:PRK14243 86 PV--EVRR---------RIGMVFQ--KPNPFPK-SIYDNIAYGARINGYKGDmdelvERSLRqaalwdevKDKLKQS-GL 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 505416896 132 fpflsrpagKLSGGMKQKLGLCCALIHDPDLLILDEPTTGVDPLARAQFWDLIARIRDErptMSVIVATAYMDEAQR 208
Cdd:PRK14243 151 ---------SLSGGQQQRLCIARAIAVQPEVILMDEPCSALDPISTLRIEELMHELKEQ---YTIIIVTHNMQQAAR 215
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
7-235 |
4.25e-13 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 73.32 E-value: 4.25e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 7 VRFSDVSLRY--GKTVALDRITLDVPAGLTTGLIGPDGVGKSSLLALASGARALQTGGVdALGGDMRSRRHRERVCRRIA 84
Cdd:PRK11160 339 LTLNNVSFTYpdQPQPVLKGLSLQIKAGEKVALLGRTGCGKSTLLQLLTRAWDPQQGEI-LLNGQPIADYSEAALRQAIS 417
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 85 YMPQGLgkNLYPTlSVEENLQFFArlfgHDAGERRRrIDALTQsTGLFPFLSRPAG----------KLSGGMKQKLGLCC 154
Cdd:PRK11160 418 VVSQRV--HLFSA-TLRDNLLLAA----PNASDEAL-IEVLQQ-VGLEKLLEDDKGlnawlgeggrQLSGGEQRRLGIAR 488
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 155 ALIHDPDLLILDEPTTGVDPLARAQFWDLIARIRDERptmSVIVATAYMDEAQRFDWLIAMDAGRVLATGAPAELLARTG 234
Cdd:PRK11160 489 ALLHDAPLLLLDEPTEGLDAETERQILELLAEHAQNK---TVLMITHRLTGLEQFDRICVMDNGQIIEQGTHQELLAQQG 565
|
.
gi 505416896 235 C 235
Cdd:PRK11160 566 R 566
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
272-489 |
4.52e-13 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 70.56 E-value: 4.52e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 272 IEARGLTMRFGDFTAVDHVSFRIRRGEIFGFLGSNGCGKSTTMKMLTGLLPATEGTAQLFGKEVDP----KDINTRRRVG 347
Cdd:PRK11831 8 VDMRGVSFTRGNRCIFDNISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEILFDGENIPAmsrsRLYTVRKRMS 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 348 YMSQAFSLYSELTVRQNLVL----HARLfgvPAAEIDARVDEMARRFGLADIYGMLPDSLPLGMRQRLSLAVAMVHKPEL 423
Cdd:PRK11831 88 MLFQSGALFTDMNVFDNVAYplreHTQL---PAPLLHSTVMMKLEAVGLRGAAKLMPSELSGGMARRAALARAIALEPDL 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 505416896 424 LILDEPTSGVDPVARDSFWQLMIDLARRDLVTIFISTHFMNEAQR-CDRISLMHAGRVLASDSPAEL 489
Cdd:PRK11831 165 IMFDEPFVGQDPITMGVLVKLISELNSALGVTCVVVSHDVPEVLSiADHAYIVADKKIVAHGSAQAL 231
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
261-492 |
4.82e-13 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 72.97 E-value: 4.82e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 261 PLRADARAGTAIEARGLTMRF----GDFTAVDHVSFRIRRGEIFGFLGSNGCGKSTTMKMLTGLLPATegtaqlfGKEVD 336
Cdd:PRK10261 2 PHSDELDARDVLAVENLNIAFmqeqQKIAAVRNLSFSLQRGETLAIVGESGSGKSVTALALMRLLEQA-------GGLVQ 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 337 PKDINTRRR------VGYMSQA------------------FSLYSELTVRQNLVLHARLF-GVPAAEIDARVDEMARRFG 391
Cdd:PRK10261 75 CDKMLLRRRsrqvieLSEQSAAqmrhvrgadmamifqepmTSLNPVFTVGEQIAESIRLHqGASREEAMVEAKRMLDQVR 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 392 LADIYGML---PDSLPLGMRQRLSLAVAMVHKPELLILDEPTSGVDPVARDSFWQLMIDLARR-DLVTIFIsTHFMNE-A 466
Cdd:PRK10261 155 IPEAQTILsryPHQLSGGMRQRVMIAMALSCRPAVLIADEPTTALDVTIQAQILQLIKVLQKEmSMGVIFI-THDMGVvA 233
|
250 260
....*....|....*....|....*.
gi 505416896 467 QRCDRISLMHAGRVLASDSPAELVRA 492
Cdd:PRK10261 234 EIADRVLVMYQGEAVETGSVEQIFHA 259
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
271-499 |
4.91e-13 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 73.62 E-value: 4.91e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 271 AIEARGLTMRF-GDFTAVDH-VSFRIRRGEIFGFLGSNGCGKSTtmkMLTGLLPATE-GTAQLFgkeVDPKDINT----- 342
Cdd:PLN03130 1237 SIKFEDVVLRYrPELPPVLHgLSFEISPSEKVGIVGRTGAGKSS---MLNALFRIVElERGRIL---IDGCDISKfglmd 1310
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 343 -RRRVGYMSQAFSLYSElTVRQNLVlharlfgvPAAE-IDARVDEMARRFGLADIYGMLP-----------DSLPLGMRQ 409
Cdd:PLN03130 1311 lRKVLGIIPQAPVLFSG-TVRFNLD--------PFNEhNDADLWESLERAHLKDVIRRNSlgldaevseagENFSVGQRQ 1381
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 410 RLSLAVAMVHKPELLILDEPTSGVDpVARDSFWQLMIdlaRRDL--VTIFISTHFMNEAQRCDRISLMHAGRVLASDSPA 487
Cdd:PLN03130 1382 LLSLARALLRRSKILVLDEATAAVD-VRTDALIQKTI---REEFksCTMLIIAHRLNTIIDCDRILVLDAGRVVEFDTPE 1457
|
250 260
....*....|....*....|...
gi 505416896 488 EL-----------VRARGAATLE 499
Cdd:PLN03130 1458 NLlsnegsafskmVQSTGAANAQ 1480
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
7-198 |
5.42e-13 |
|
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is a cytosolic protein required by fungal ribosomes for in vitro protein synthesis and for in vivo growth. EF-3 stimulates the binding of the EF-1: GTP: aa-tRNA ternary complex to the ribosomal A site by facilitated release of the deacylated tRNA from the E site. The reaction requires ATP hydrolysis. EF-3 contains two ATP nucleotide binding sequence (NBS) motifs. NBSI is sufficient for the intrinsic ATPase activity. NBSII is essential for the ribosome-stimulated functions.
Pssm-ID: 213188 [Multi-domain] Cd Length: 144 Bit Score: 67.09 E-value: 5.42e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 7 VRFSDVSLRYGKTVALDRITLDVPAGLTTGLIGPDGVGKSSLLALASGaRALQTGGVDALGGDMRsrrhrervcrrIAYM 86
Cdd:cd03221 1 IELENLSKTYGGKLLLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAG-ELEPDEGIVTWGSTVK-----------IGYF 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 87 PQglgknlyptlsveenlqffarlfghdagerrrridaltqstglfpflsrpagkLSGGMKQKLGLCCALIHDPDLLILD 166
Cdd:cd03221 69 EQ-----------------------------------------------------LSGGEKMRLALAKLLLENPNLLLLD 95
|
170 180 190
....*....|....*....|....*....|..
gi 505416896 167 EPTTGVDPLARAQfwdLIARIRDERPTMsVIV 198
Cdd:cd03221 96 EPTNHLDLESIEA---LEEALKEYPGTV-ILV 123
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
15-185 |
6.49e-13 |
|
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: 68.67 E-value: 6.49e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 15 RYGKTVaLDRITLDVPAGLTTGLIGPDGVGKSSLLALASGARALQTGGVDALG-GDMRSRRHRERVCRRIAYMPqglgkN 93
Cdd:cd03231 10 RDGRAL-FSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNGgPLDFQRDSIARGLLYLGHAP-----G 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 94 LYPTLSVEENLQFFARLFGHDAGErrrriDALTQsTGLFPFLSRPAGKLSGGMKQKLGLCCALIHDPDLLILDEPTTGVD 173
Cdd:cd03231 84 IKTTLSVLENLRFWHADHSDEQVE-----EALAR-VGLNGFEDRPVAQLSAGQQRRVALARLLLSGRPLWILDEPTTALD 157
|
170
....*....|..
gi 505416896 174 PLARAQFWDLIA 185
Cdd:cd03231 158 KAGVARFAEAMA 169
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
6-230 |
6.78e-13 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 70.53 E-value: 6.78e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 6 VVRFSDVSLRYG-----KTVALDRITLDVPAGLTTGLIGPDGVGKSSLLALASGARALQTGGV---DALGGDMRSRRHRE 77
Cdd:PRK13643 1 MIKFEKVNYTYQpnspfASRALFDIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVtvgDIVVSSTSKQKEIK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 78 RVCRRIAYMPQGLGKNLYPTlSVEENLQFFARLFGHDAGERRRRIDALTQSTGLFP-FLSRPAGKLSGGMKQKLGLCCAL 156
Cdd:PRK13643 81 PVRKKVGVVFQFPESQLFEE-TVLKDVAFGPQNFGIPKEKAEKIAAEKLEMVGLADeFWEKSPFELSGGQMRRVAIAGIL 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 505416896 157 IHDPDLLILDEPTTGVDPLARAQFWDLIARIRDERPTmsVIVATAYMDEAQRF-DWLIAMDAGRVLATGAPAELL 230
Cdd:PRK13643 160 AMEPEVLVLDEPTAGLDPKARIEMMQLFESIHQSGQT--VVLVTHLMDDVADYaDYVYLLEKGHIISCGTPSDVF 232
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
7-230 |
7.70e-13 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 69.63 E-value: 7.70e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 7 VRFSDVSLRYGKTVALDRITLDVPAGLTTGLIGPDGVGKSSLLALASGARALQTGGVdALGGDMRSRRHRERVCRRIAYM 86
Cdd:PRK10253 8 LRGEQLTLGYGKYTVAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHV-WLDGEHIQHYASKEVARRIGLL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 87 PQglGKNLYPTLSVEEnlqFFAR-------LFGHDAGERRRRIDALTQSTGLFPFLSRPAGKLSGGMKQKLGLCCALIHD 159
Cdd:PRK10253 87 AQ--NATTPGDITVQE---LVARgryphqpLFTRWRKEDEEAVTKAMQATGITHLADQSVDTLSGGQRQRAWIAMVLAQE 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 505416896 160 PDLLILDEPTTGVDPLARAQFWDLIARI-RDERPTMSVIVATayMDEAQRF-DWLIAMDAGRVLATGAPAELL 230
Cdd:PRK10253 162 TAIMLLDEPTTWLDISHQIDLLELLSELnREKGYTLAAVLHD--LNQACRYaSHLIALREGKIVAQGAPKEIV 232
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
7-219 |
8.23e-13 |
|
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: 68.26 E-value: 8.23e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 7 VRFSDVSLRYGKTV-----ALDRITLDVPAGLTTGLIGPDGVGKSSLLAlasgaralqtggvdALGGDMRSRRHRERVCR 81
Cdd:cd03250 1 ISVEDASFTWDSGEqetsfTLKDINLEVPKGELVAIVGPVGSGKSSLLS--------------ALLGELEKLSGSVSVPG 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 82 RIAYMPQglgknlYPTL---SVEENLqffarLFGHDAGERRRR--IDA--LTQSTGLFPflsrpAG----------KLSG 144
Cdd:cd03250 67 SIAYVSQ------EPWIqngTIRENI-----LFGKPFDEERYEkvIKAcaLEPDLEILP-----DGdlteigekgiNLSG 130
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 505416896 145 GMKQKLGLCCALIHDPDLLILDEPTTGVDPLARAQFWD--LIARIRDERptmSVIVATAYMDEAQRFDWLIAMDAGR 219
Cdd:cd03250 131 GQKQRISLARAVYSDADIYLLDDPLSAVDAHVGRHIFEncILGLLLNNK---TRILVTHQLQLLPHADQIVVLDNGR 204
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
10-220 |
8.72e-13 |
|
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: 67.63 E-value: 8.72e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 10 SDVSLRYG--KTVALDRITLDVPAGLTTGLIGPDGVGKSSLLALASGARALQTGGVDALGGDMRSRrhrervcrriaymp 87
Cdd:cd03246 4 ENVSFRYPgaEPPVLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDGADISQW-------------- 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 88 qglgknlyptlsveenlqffarlfghDAGERRRRIDALTQSTGLFPflsrpaGK-----LSGGMKQKLGLCCALIHDPDL 162
Cdd:cd03246 70 --------------------------DPNELGDHVGYLPQDDELFS------GSiaeniLSGGQRQRLGLARALYGNPRI 117
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 505416896 163 LILDEPTTGVDPLARAQFWDLIARIRDERPTmsVIVATAYMDEAQRFDWLIAMDAGRV 220
Cdd:cd03246 118 LVLDEPNSHLDVEGERALNQAIAALKAAGAT--RIVIAHRPETLASADRILVLEDGRV 173
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
2-261 |
9.42e-13 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 71.92 E-value: 9.42e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 2 NASSVVRFSDVSLRY-GKTVALDRITLDVPAGLTTGLIGPDGVGKSSLLALASGARALQTGGVDALGGDMRSRRHrervc 80
Cdd:PRK13657 330 RVKGAVEFDDVSFSYdNSRQGVEDVSFEAKPGQTVAIVGPTGAGKSTLINLLQRVFDPQSGRILIDGTDIRTVTR----- 404
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 81 rriaympQGLGKNLY-----PTL---SVEENLQF------FARLfgHDAGERRRRID-ALTQSTGLFPFLSRPAGKLSGG 145
Cdd:PRK13657 405 -------ASLRRNIAvvfqdAGLfnrSIEDNIRVgrpdatDEEM--RAAAERAQAHDfIERKPDGYDTVVGERGRQLSGG 475
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 146 MKQKLGLCCALIHDPDLLILDEPTTGVDPLARAQFWDLIARIRDERPTMSVIVATAYMDEAQRfdwLIAMDAGRVLATGA 225
Cdd:PRK13657 476 ERQRLAIARALLKDPPILILDEATSALDVETEAKVKAALDELMKGRTTFIIAHRLSTVRNADR---ILVFDNGRVVESGS 552
|
250 260 270
....*....|....*....|....*....|....*...
gi 505416896 226 PAELLARTG--CDSLEAAFiaLLPENERRGHKPVKIEP 261
Cdd:PRK13657 553 FDELVARGGrfAALLRAQG--MLQEDERRKQPAAEGAN 588
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
286-494 |
1.01e-12 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 71.78 E-value: 1.01e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 286 AVDHVSFRIRRGEIFGFLGSNGCGKSTTMKMLTGLLPATEGTAQLFGKEV-DPKDINTRRRVGYMSQAFSLYSElTVRQN 364
Cdd:PRK11160 355 VLKGLSLQIKAGEKVALLGRTGCGKSTLLQLLTRAWDPQQGEILLNGQPIaDYSEAALRQAISVVSQRVHLFSA-TLRDN 433
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 365 LVLHArlfgvPAAeIDARVDEMARRFGLADiygMLPDSLPL------GMRQ-------RLSLAVAMVHKPELLILDEPTS 431
Cdd:PRK11160 434 LLLAA-----PNA-SDEALIEVLQQVGLEK---LLEDDKGLnawlgeGGRQlsggeqrRLGIARALLHDAPLLLLDEPTE 504
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 505416896 432 GVDPVARDSFWQLMIDLARRDLVtIFIsTHFMNEAQRCDRISLMHAGRVLASDSPAELVRARG 494
Cdd:PRK11160 505 GLDAETERQILELLAEHAQNKTV-LMI-THRLTGLEQFDRICVMDNGQIIEQGTHQELLAQQG 565
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
271-494 |
1.11e-12 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 71.92 E-value: 1.11e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 271 AIEARGLTMRF-GDFTAVDHVSFRIRRGEIFGFLGSNGCGKSTTMKMLTGLLPATEGTAQLFGkeVDPKDINT---RRRV 346
Cdd:PRK13657 334 AVEFDDVSFSYdNSRQGVEDVSFEAKPGQTVAIVGPTGAGKSTLINLLQRVFDPQSGRILIDG--TDIRTVTRaslRRNI 411
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 347 GYMSQAFSLYSElTVRQNLVL------HARLfgVPAAEIDARVDEMARR-FGLADIYGMLPDSLPLGMRQRLSLAVAMVH 419
Cdd:PRK13657 412 AVVFQDAGLFNR-SIEDNIRVgrpdatDEEM--RAAAERAQAHDFIERKpDGYDTVVGERGRQLSGGERQRLAIARALLK 488
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 505416896 420 KPELLILDEPTSGVDpVARDSFWQLMIDLARRDLVTiFISTHFMNEAQRCDRISLMHAGRVLASDSPAELVRARG 494
Cdd:PRK13657 489 DPPILILDEATSALD-VETEAKVKAALDELMKGRTT-FIIAHRLSTVRNADRILVFDNGRVVESGSFDELVARGG 561
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
37-230 |
1.16e-12 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 72.00 E-value: 1.16e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 37 LIGPDGVGKSSLL-ALAS-GARALQTGGVDALGGDMRSRRHRERVCrriAYMPQGlgKNLYPTLSVEENLQFFARLFGHD 114
Cdd:TIGR00955 56 VMGSSGAGKTTLMnALAFrSPKGVKGSGSVLLNGMPIDAKEMRAIS---AYVQQD--DLFIPTLTVREHLMFQAHLRMPR 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 115 ---AGERRRRIDALTQSTGLfpflsRPAGK-----------LSGGMKQKLGLCCALIHDPDLLILDEPTTGVDPLARAQF 180
Cdd:TIGR00955 131 rvtKKEKRERVDEVLQALGL-----RKCANtrigvpgrvkgLSGGERKRLAFASELLTDPPLLFCDEPTSGLDSFMAYSV 205
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 505416896 181 WDLIARIRDERPTmsvIVATAYMDEAQ---RFDWLIAMDAGRVLATGAPAELL 230
Cdd:TIGR00955 206 VQVLKGLAQKGKT---IICTIHQPSSElfeLFDKIILMAEGRVAYLGSPDQAV 255
|
|
| PRK15093 |
PRK15093 |
peptide ABC transporter ATP-binding protein SapD; |
272-492 |
2.02e-12 |
|
peptide ABC transporter ATP-binding protein SapD;
Pssm-ID: 185049 [Multi-domain] Cd Length: 330 Bit Score: 69.45 E-value: 2.02e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 272 IEARGLTMRF----GDFTAVDHVSFRIRRGEIFGFLGSNGCGKSTTMKMLTGLLPAT-EGTAQLFG-KEVDPKDINTRRR 345
Cdd:PRK15093 4 LDIRNLTIEFktsdGWVKAVDRVSMTLTEGEIRGLVGESGSGKSLIAKAICGVTKDNwRVTADRMRfDDIDLLRLSPRER 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 346 ---VGY-MSQAFS-----LYSELTVRQNLVLharlfGVPAAEIDA-----------RVDEMARRFGLAD---IYGMLPDS 402
Cdd:PRK15093 84 rklVGHnVSMIFQepqscLDPSERVGRQLMQ-----NIPGWTYKGrwwqrfgwrkrRAIELLHRVGIKDhkdAMRSFPYE 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 403 LPLGMRQRLSLAVAMVHKPELLILDEPTSGVDPVARDSFWQLMIDLARRDLVTIFISTHFMNE-AQRCDRISLMHAGRVL 481
Cdd:PRK15093 159 LTEGECQKVMIAIALANQPRLLIADEPTNAMEPTTQAQIFRLLTRLNQNNNTTILLISHDLQMlSQWADKINVLYCGQTV 238
|
250
....*....|.
gi 505416896 482 ASDSPAELVRA 492
Cdd:PRK15093 239 ETAPSKELVTT 249
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
7-234 |
2.07e-12 |
|
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: 70.90 E-value: 2.07e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 7 VRFSDVSLRYGKT--VALDRITLDVPAGLTTGLIGPDGVGKSSLLALASgaR-ALQTGGVDALGGDMRSRRHRERVCRRI 83
Cdd:TIGR02203 331 VEFRNVTFRYPGRdrPALDSISLVIEPGETVALVGRSGSGKSTLVNLIP--RfYEPDSGQILLDGHDLADYTLASLRRQV 408
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 84 AYMPQGLgknlypTL---SVEENLQFFARLFGHDAGERRRRIDALTQS------TGLFPFLSRPAGKLSGGMKQKLGLCC 154
Cdd:TIGR02203 409 ALVSQDV------VLfndTIANNIAYGRTEQADRAEIERALAAAYAQDfvdklpLGLDTPIGENGVLLSGGQRQRLAIAR 482
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 155 ALIHDPDLLILDEPTTGVDPLARAQFWDLIARIRDERPTmsvIVATAYMDEAQRFDWLIAMDAGRVLATGAPAELLARTG 234
Cdd:TIGR02203 483 ALLKDAPILILDEATSALDNESERLVQAALERLMQGRTT---LVIAHRLSTIEKADRIVVMDDGRIVERGTHNELLARNG 559
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
6-231 |
2.31e-12 |
|
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: 70.60 E-value: 2.31e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 6 VVRFSDVSLRY-----GKTVALDRITLDVPAGLTTGLIGPDGVGKSSLLALASGARALQTGGVDALGG----DM--RSRR 74
Cdd:TIGR03269 279 IIKVRNVSKRYisvdrGVVKAVDNVSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGEVNVRVGdewvDMtkPGPD 358
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 75 HRERVCRRIAYMPQGLGknLYPTLSVEENLQFFARLFGHDAGERRRRIDALtQSTGL-----FPFLSRPAGKLSGGMKQK 149
Cdd:TIGR03269 359 GRGRAKRYIGILHQEYD--LYPHRTVLDNLTEAIGLELPDELARMKAVITL-KMVGFdeekaEEILDKYPDELSEGERHR 435
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 150 LGLCCALIHDPDLLILDEPTTGVDPLARAQFWDLIARIRDERPTMSVIVATAyMDEAQRF-DWLIAMDAGRVLATGAPAE 228
Cdd:TIGR03269 436 VALAQVLIKEPRIVILDEPTGTMDPITKVDVTHSILKAREEMEQTFIIVSHD-MDFVLDVcDRAALMRDGKIVKIGDPEE 514
|
...
gi 505416896 229 LLA 231
Cdd:TIGR03269 515 IVE 517
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
2-230 |
2.45e-12 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 68.15 E-value: 2.45e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 2 NASSVVRFSDVSLRYGKTVALDRITLDVPAGLTTGLIGPDGVGKSSLLALAS------GARALQTGGVDALGGDMRSRRH 75
Cdd:PRK14246 6 SAEDVFNISRLYLYINDKAILKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNrlieiyDSKIKVDGKVLYFGKDIFQIDA 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 76 RERVCRRIAYMPQglgKNLYPTLSVEENLQFFARLFG-HDAGERRRRIDALTQSTGL----FPFLSRPAGKLSGGMKQKL 150
Cdd:PRK14246 86 IKLRKEVGMVFQQ---PNPFPHLSIYDNIAYPLKSHGiKEKREIKKIVEECLRKVGLwkevYDRLNSPASQLSGGQQQRL 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 151 GLCCALIHDPDLLILDEPTTGVDPLARAQFWDLIARIRDErptMSVIVATAYMDEAQRF-DWLIAMDAGRVLATGAPAEL 229
Cdd:PRK14246 163 TIARALALKPKVLLMDEPTSMIDIVNSQAIEKLITELKNE---IAIVIVSHNPQQVARVaDYVAFLYNGELVEWGSSNEI 239
|
.
gi 505416896 230 L 230
Cdd:PRK14246 240 F 240
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
278-481 |
2.90e-12 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 70.68 E-value: 2.90e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 278 TMRFGDFTAVDHVSFRIRRGEIFGFLGSNGCGKSTTMKMLTGLLPATEGTAQLFGKEVDPKDiNTRRRVGYMSQAFSLYS 357
Cdd:PLN03211 75 TRQIQERTILNGVTGMASPGEILAVLGPSGSGKSTLLNALAGRIQGNNFTGTILANNRKPTK-QILKRTGFVTQDDILYP 153
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 358 ELTVRQNLVLHA--RLFGVPAAEIDARV-DEMARRFGLAD-----IYGMLPDSLPLGMRQRLSLAVAMVHKPELLILDEP 429
Cdd:PLN03211 154 HLTVRETLVFCSllRLPKSLTKQEKILVaESVISELGLTKcentiIGNSFIRGISGGERKRVSIAHEMLINPSLLILDEP 233
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 505416896 430 TSGVDPVARDSFWQLMIDLARRDlVTIFISTHFMNEA--QRCDRISLMHAGRVL 481
Cdd:PLN03211 234 TSGLDATAAYRLVLTLGSLAQKG-KTIVTSMHQPSSRvyQMFDSVLVLSEGRCL 286
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
21-268 |
2.96e-12 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 69.48 E-value: 2.96e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 21 ALDRITLDVPAGLTTGLIGPDGVGKSSLLALASGARALQTGGVDALGGDMrsrRHRERVCRRIAYMPQGLGknLYPTLSV 100
Cdd:PRK11607 34 AVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVDL---SHVPPYQRPINMMFQSYA--LFPHMTV 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 101 EENLQFFARLFGHDAGERRRRIDALTQSTGLFPFLSRPAGKLSGGMKQKLGLCCALIHDPDLLILDEPTTGVDPLARAQF 180
Cdd:PRK11607 109 EQNIAFGLKQDKLPKAEIASRVNEMLGLVHMQEFAKRKPHQLSGGQRQRVALARSLAKRPKLLLLDEPMGALDKKLRDRM 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 181 WDLIARIRdERPTMSVIVATAYMDEAQRFDWLIA-MDAGRVLATGAPAELLARTGCdSLEAAFIA-------LLPENERR 252
Cdd:PRK11607 189 QLEVVDIL-ERVGVTCVMVTHDQEEAMTMAGRIAiMNRGKFVQIGEPEEIYEHPTT-RYSAEFIGsvnvfegVLKERQED 266
|
250
....*....|....*....
gi 505416896 253 G---HKPVKIEPLRADARA 268
Cdd:PRK11607 267 GlviDSPGLVHPLKVDADA 285
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
263-459 |
3.02e-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: 3.02e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 263 RADARAGTAIEARGLTMRFGDFTA-VDHVSFRIRRGEifGFL--GSNGCGKSTTMKMLTGLLPATEGTAQLfgkevdPKD 339
Cdd:COG4178 354 RIETSEDGALALEDLTLRTPDGRPlLEDLSLSLKPGE--RLLitGPSGSGKSTLLRAIAGLWPYGSGRIAR------PAG 425
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 340 intrRRVGYMSQafSLYSEL-TVRQNLVLharlfgvPAAEI---DARVDEMARRFGLADIYGML------PDSLPLGMRQ 409
Cdd:COG4178 426 ----ARVLFLPQ--RPYLPLgTLREALLY-------PATAEafsDAELREALEAVGLGHLAERLdeeadwDQVLSLGEQQ 492
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 505416896 410 RLSLAVAMVHKPELLILDEPTSGVDPVARDSFWQLmidLARRDLVTIFIS 459
Cdd:COG4178 493 RLAFARLLLHKPDWLFLDEATSALDEENEAALYQL---LREELPGTTVIS 539
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
19-239 |
3.16e-12 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 68.15 E-value: 3.16e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 19 TVALDRITLDVPAGLTTGLIGPDGVGKSSLLALASGARALQTG-----GVDALGGDMRSRRHRERVCRRIAYMPQGLGKN 93
Cdd:PRK13637 20 KKALDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGkiiidGVDITDKKVKLSDIRKKVGLVFQYPEYQLFEE 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 94 lyptlSVEENLQFFARLFGHDAGERRRRIDALTQSTGLF--PFLSRPAGKLSGGMKQKLGLCCALIHDPDLLILDEPTTG 171
Cdd:PRK13637 100 -----TIEKDIAFGPINLGLSEEEIENRVKRAMNIVGLDyeDYKDKSPFELSGGQKRRVAIAGVVAMEPKILILDEPTAG 174
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 505416896 172 VDPLARAQFWDLIARIRDERpTMSVIVATAYMDEAQRF-DWLIAMDAGRVLATGAPAELLARTgcDSLE 239
Cdd:PRK13637 175 LDPKGRDEILNKIKELHKEY-NMTIILVSHSMEDVAKLaDRIIVMNKGKCELQGTPREVFKEV--ETLE 240
|
|
| ABC2_membrane |
pfam01061 |
ABC-2 type transporter; |
812-952 |
4.91e-12 |
|
ABC-2 type transporter;
Pssm-ID: 426023 [Multi-domain] Cd Length: 204 Bit Score: 66.14 E-value: 4.91e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 812 TALAVVRERELGSILNLYVTPV-TRTEFLIGKQVPYVVLAMLNFLLMTMLARIAFDVPV-KGSFMTLLLAVLIFNVVATG 889
Cdd:pfam01061 63 SGISPVFEKERGVLYRELASPLySPSAYVLAKILSELPLSLLQSLIFLLIVYFMVGLPPsAGRFFLFLLVLLLTALAASS 142
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 505416896 890 IGLLASTFTRSQVAAIVMTIIGTMiPTVQFAGLLTPLSSLEGTGRFIGLVYPATYMLSISRGV 952
Cdd:pfam01061 143 LGLFISALAPSFEDASQLGPLVLL-PLLLLSGFFIPIDSMPVWWQWIYYLNPLTYAIEALRAN 204
|
|
| BtuD |
COG4138 |
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ... |
22-230 |
6.04e-12 |
|
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism];
Pssm-ID: 443313 [Multi-domain] Cd Length: 248 Bit Score: 66.79 E-value: 6.04e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 22 LDRITLDVPAGLTTGLIGPDGVGKSSLLALASGARALQtGGVDALGGDMRSRRHRERVCRRiAYMPQglgkNLYPT--LS 99
Cdd:COG4138 12 LGPISAQVNAGELIHLIGPNGAGKSTLLARMAGLLPGQ-GEILLNGRPLSDWSAAELARHR-AYLSQ----QQSPPfaMP 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 100 VEENLQFFARLfGHDAGERRRRIDALTQSTGLFPFLSRPAGKLSGGMKQKLGLCCAL--IH---DPD--LLILDEPTTGV 172
Cdd:COG4138 86 VFQYLALHQPA-GASSEAVEQLLAQLAEALGLEDKLSRPLTQLSGGEWQRVRLAAVLlqVWptiNPEgqLLLLDEPMNSL 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 505416896 173 DPLARAQFWDLIARIRDErpTMSVIVAT-------AYMDEAqrfdWLiaMDAGRVLATGAPAELL 230
Cdd:COG4138 165 DVAQQAALDRLLRELCQQ--GITVVMSShdlnhtlRHADRV----WL--LKQGKLVASGETAEVM 221
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
20-229 |
6.60e-12 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 67.95 E-value: 6.60e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 20 VALDRITLDVPAGLTTGLIGPDGVGKSSLLALASGARALQTGGVDAlgGDMRSRRHRERVCRRIAYMPQGLG--KNLYPT 97
Cdd:PRK13631 40 VALNNISYTFEKNKIYFIIGNSGSGKSTLVTHFNGLIKSKYGTIQV--GDIYIGDKKNNHELITNPYSKKIKnfKELRRR 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 98 LS--------------VEENLQFFARLFGHDAGERRRRIDALTQSTGL-FPFLSRPAGKLSGGMKQKLGLCCALIHDPDL 162
Cdd:PRK13631 118 VSmvfqfpeyqlfkdtIEKDIMFGPVALGVKKSEAKKLAKFYLNKMGLdDSYLERSPFGLSGGQKRRVAIAGILAIQPEI 197
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 505416896 163 LILDEPTTGVDPLARAQFWDLIARIRDERPTmsVIVATAYMDEAQRF-DWLIAMDAGRVLATGAPAEL 229
Cdd:PRK13631 198 LIFDEPTAGLDPKGEHEMMQLILDAKANNKT--VFVITHTMEHVLEVaDEVIVMDKGKILKTGTPYEI 263
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
272-429 |
6.84e-12 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 65.60 E-value: 6.84e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 272 IEARGLTMRFGDFTAVDHVSFRIRRGEIFGFLGSNGCGKSTTMKMLTGLLPATEGTAQLFGKEVDPKDINTRRRVGYMSQ 351
Cdd:PRK13538 2 LEARNLACERDERILFSGLSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVLWQGEPIRRQRDEYHQDLLYLGH 81
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 505416896 352 AFSLYSELTVRQNLVLHARLFGVPAAeiDARVDEMArRFGLADiYGMLP-DSLPLGMRQRLSLAVAMVHKPELLILDEP 429
Cdd:PRK13538 82 QPGIKTELTALENLRFYQRLHGPGDD--EALWEALA-QVGLAG-FEDVPvRQLSAGQQRRVALARLWLTRAPLWILDEP 156
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
291-489 |
8.86e-12 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 68.98 E-value: 8.86e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 291 SFRIRRGEIFGFLGSNGCGKSTTMKMLTGLLPATEGTAQLFGKEVdpKDIN---TRRRVGYMSQAFSLYSElTVRQNLvl 367
Cdd:TIGR00958 501 TFTLHPGEVVALVGPSGSGKSTVAALLQNLYQPTGGQVLLDGVPL--VQYDhhyLHRQVALVGQEPVLFSG-SVRENI-- 575
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 368 harLFGVPAAEiDARVDEMARRFGLADIYGMLPDS-----------LPLGMRQRLSLAVAMVHKPELLILDEPTSGVDPV 436
Cdd:TIGR00958 576 ---AYGLTDTP-DEEIMAAAKAANAHDFIMEFPNGydtevgekgsqLSGGQKQRIAIARALVRKPRVLILDEATSALDAE 651
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 505416896 437 ARDSFWQLMidlARRDLvTIFISTHFMNEAQRCDRISLMHAGRVLASDSPAEL 489
Cdd:TIGR00958 652 CEQLLQESR---SRASR-TVLLIAHRLSTVERADQILVLKKGSVVEMGTHKQL 700
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
4-208 |
1.21e-11 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 65.95 E-value: 1.21e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 4 SSVVRFSDVSLRYGKTVALDRITLDVPAGLTTGLIGPDGVGKSSLLalasgaRALQ-----------TGGVDALGGDMRS 72
Cdd:PRK14239 3 EPILQVSDLSVYYNKKKALNSVSLDFYPNEITALIGPSGSGKSTLL------RSINrmndlnpevtiTGSIVYNGHNIYS 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 73 RRH-RERVCRRIAYMPQglGKNLYPtLSVEENLQFFARLFG-HDagerRRRIDALTQST--------GLFPFLSRPAGKL 142
Cdd:PRK14239 77 PRTdTVDLRKEIGMVFQ--QPNPFP-MSIYENVVYGLRLKGiKD----KQVLDEAVEKSlkgasiwdEVKDRLHDSALGL 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 505416896 143 SGGMKQKLGLCCALIHDPDLLILDEPTTGVDPLARAQFWDLIARIRDErptMSVIVATAYMDEAQR 208
Cdd:PRK14239 150 SGGQQQRVCIARVLATSPKIILLDEPTSALDPISAGKIEETLLGLKDD---YTMLLVTRSMQQASR 212
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
285-492 |
1.36e-11 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 68.19 E-value: 1.36e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 285 TAVDHVSFRIRRGEIFGFLGSNGCGKSTTMKMLTGLLPA-----TEGTAQLFGKEVDPKDINTRRRV--GYMSQAF---- 353
Cdd:PRK15134 23 TVVNDVSLQIEAGETLALVGESGSGKSVTALSILRLLPSppvvyPSGDIRFHGESLLHASEQTLRGVrgNKIAMIFqepm 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 354 -SLYSELTVRQNL----VLHARLFGVPA-AEIDARVDEM-----ARRfgLADiygmLPDSLPLGMRQRLSLAVAMVHKPE 422
Cdd:PRK15134 103 vSLNPLHTLEKQLyevlSLHRGMRREAArGEILNCLDRVgirqaAKR--LTD----YPHQLSGGERQRVMIAMALLTRPE 176
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 505416896 423 LLILDEPTSGVDPVARDSFWQLMIDLARR-DLVTIFIsTHFMNEAQR-CDRISLMHAGRVLASDSPAELVRA 492
Cdd:PRK15134 177 LLIADEPTTALDVSVQAQILQLLRELQQElNMGLLFI-THNLSIVRKlADRVAVMQNGRCVEQNRAATLFSA 247
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
21-248 |
1.39e-11 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 67.07 E-value: 1.39e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 21 ALDRITLDVPAGLTTGLIGPDGVGKS-SLLALAS--------GARALQTGGVDALggDMRSRRHRERVCRRIAYMPQGLG 91
Cdd:PRK11022 22 AVDRISYSVKQGEVVGIVGESGSGKSvSSLAIMGlidypgrvMAEKLEFNGQDLQ--RISEKERRNLVGAEVAMIFQDPM 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 92 KNLYPTLSVeeNLQFFARLFGHDAGERRRR----IDALTQsTGLFPFLSR----PAgKLSGGMKQKLGLCCALIHDPDLL 163
Cdd:PRK11022 100 TSLNPCYTV--GFQIMEAIKVHQGGNKKTRrqraIDLLNQ-VGIPDPASRldvyPH-QLSGGMSQRVMIAMAIACRPKLL 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 164 ILDEPTTGVDPLARAQFWDLIARIRdERPTMSVIVAT---AYMDEAQrfDWLIAMDAGRVLATGaPAELLARTGCDSLEA 240
Cdd:PRK11022 176 IADEPTTALDVTIQAQIIELLLELQ-QKENMALVLIThdlALVAEAA--HKIIVMYAGQVVETG-KAHDIFRAPRHPYTQ 251
|
....*...
gi 505416896 241 AFIALLPE 248
Cdd:PRK11022 252 ALLRALPE 259
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
277-437 |
1.46e-11 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 64.59 E-value: 1.46e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 277 LTMRFGDFTAVDHVSFRIRRGEIFGFLGSNGCGKSTTMKMLTGLLPATEGTAQLFGKEVDPKDINTRRRVGYMSQAFSLY 356
Cdd:PRK13540 7 LDFDYHDQPLLQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEILFERQSIKKDLCTYQKQLCFVGHRSGIN 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 357 SELTVRQNLvlharLFGVPAAEIDARVDEMARRFGLADIYGMLPDSLPLGMRQRLSLAVAMVHKPELLILDEPTSGVDPV 436
Cdd:PRK13540 87 PYLTLRENC-----LYDIHFSPGAVGITELCRLFSLEHLIDYPCGLLSSGQKRQVALLRLWMSKAKLWLLDEPLVALDEL 161
|
.
gi 505416896 437 A 437
Cdd:PRK13540 162 S 162
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
11-221 |
1.78e-11 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 65.47 E-value: 1.78e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 11 DVSLRYGKTVALDRITLDVPAGLTTGLIGPDGVGKSSLLALASGARalQTGGVDALGGdmrsRRHRERVCRRIAYMPQGl 90
Cdd:PRK11247 17 AVSKRYGERTVLNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLE--TPSAGELLAG----TAPLAEAREDTRLMFQD- 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 91 gKNLYPTLSVEENLQFfarlfGHDAGERRRRIDALtQSTGLFPFLSRPAGKLSGGMKQKLGLCCALIHDPDLLILDEPTT 170
Cdd:PRK11247 90 -ARLLPWKKVIDNVGL-----GLKGQWRDAALQAL-AAVGLADRANEWPAALSGGQKQRVALARALIHRPGLLLLDEPLG 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 505416896 171 GVDPLARAQFWDLIARIRDERpTMSVIVATAYMDEAqrfdwlIAMdAGRVL 221
Cdd:PRK11247 163 ALDALTRIEMQDLIESLWQQH-GFTVLLVTHDVSEA------VAM-ADRVL 205
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
272-491 |
2.21e-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: 64.09 E-value: 2.21e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 272 IEARGLTMRFGDFTAVDHVSFRIRRGEIFGFLGSNGCGKSTTMKMLTGLlPA---TEGTAQLFGKEVDPKDINTRRRVG- 347
Cdd:cd03217 1 LEIKDLHVSVGGKEILKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMGH-PKyevTEGEILFKGEDITDLPPEERARLGi 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 348 YMSqafslyseltvrqnlvlharlFGVPAaEIDA-RVDEMARRfgladiygmLPDSLPLGMRQRLSLAVAMVHKPELLIL 426
Cdd:cd03217 80 FLA---------------------FQYPP-EIPGvKNADFLRY---------VNEGFSGGEKKRNEILQLLLLEPDLAIL 128
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 505416896 427 DEPTSGVDPVARDSFWQLMIDLARRDlVTIFISTHF--MNEAQRCDRISLMHAGRVLASdSPAELVR 491
Cdd:cd03217 129 DEPDSGLDIDALRLVAEVINKLREEG-KSVLIITHYqrLLDYIKPDRVHVLYDGRIVKS-GDKELAL 193
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
7-208 |
2.84e-11 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 65.06 E-value: 2.84e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 7 VRFSDVSLRYGKTVALDRITLDVPAGLTTGLIGPDGVGKSSLLALASGARALQT-----GGVDALGGDM--RSRRHRERV 79
Cdd:PRK14258 8 IKVNNLSFYYDTQKILEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLNRMNELESevrveGRVEFFNQNIyeRRVNLNRLR 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 80 CRRIAYMPQglgKNLYPtLSVEENLQFFARLFG-HDAGERRRRIDALTQSTGLFP----FLSRPAGKLSGGMKQKLGLCC 154
Cdd:PRK14258 88 RQVSMVHPK---PNLFP-MSVYDNVAYGVKIVGwRPKLEIDDIVESALKDADLWDeikhKIHKSALDLSGGQQQRLCIAR 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 505416896 155 ALIHDPDLLILDEPTTGVDPLARAQFWDLIARIRdERPTMSVIVATAYMDEAQR 208
Cdd:PRK14258 164 ALAVKPKVLLMDEPCFGLDPIASMKVESLIQSLR-LRSELTMVIVSHNLHQVSR 216
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
5-225 |
3.12e-11 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 65.03 E-value: 3.12e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 5 SVVRFSDVSLRYGKTVALDRITLDVPAGLTTGLIGPDGVGKSSLLALASG---------------ARALQTGGvdALGGD 69
Cdd:PRK09984 3 TIIRVEKLAKTFNQHQALHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGlitgdksagshiellGRTVQREG--RLARD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 70 MRSRRHRErvcrriAYMPQGLgkNLYPTLSVEEN---------------LQFFARLfghdagERRRRIDALTQsTGLFPF 134
Cdd:PRK09984 81 IRKSRANT------GYIFQQF--NLVNRLSVLENvligalgstpfwrtcFSWFTRE------QKQRALQALTR-VGMVHF 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 135 LSRPAGKLSGGMKQKLGLCCALIHDPDLLILDEPTTGVDPLARAQFWDLIARIrDERPTMSVIVATAYMDEAQRF-DWLI 213
Cdd:PRK09984 146 AHQRVSTLSGGQQQRVAIARALMQQAKVILADEPIASLDPESARIVMDTLRDI-NQNDGITVVVTLHQVDYALRYcERIV 224
|
250
....*....|..
gi 505416896 214 AMDAGRVLATGA 225
Cdd:PRK09984 225 ALRQGHVFYDGS 236
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
9-480 |
3.61e-11 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 67.12 E-value: 3.61e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 9 FSDVSLRYGKTVALDRITLDVPAGLTTGLIGPDGVGKSSLLALASGARALQTGGVDALGGdmrsrrhrervcRRIAYMPQ 88
Cdd:PRK10636 4 FSSLQIRRGVRVLLDNATATINPGQKVGLVGKNGCGKSTLLALLKNEISADGGSYTFPGN------------WQLAWVNQ 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 89 GLgknlyPTLSV----------EENLQFFARLfgHDAGER---------------------RRRIDALTQSTGLF-PFLS 136
Cdd:PRK10636 72 ET-----PALPQpaleyvidgdREYRQLEAQL--HDANERndghaiatihgkldaidawtiRSRAASLLHGLGFSnEQLE 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 137 RPAGKLSGGMKQKLGLCCALIHDPDLLILDEPTTGVDplARAQFW------------DLIARIRD------------ERP 192
Cdd:PRK10636 145 RPVSDFSGGWRMRLNLAQALICRSDLLLLDEPTNHLD--LDAVIWlekwlksyqgtlILISHDRDfldpivdkiihiEQQ 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 193 TMSVIVATAYMDEAQRFDWL-------------IA-----MDAGRVLATGAPAellARTGCDSLE-AAFIAllpenerrg 253
Cdd:PRK10636 223 SLFEYTGNYSSFEVQRATRLaqqqamyesqqerVAhlqsyIDRFRAKATKAKQ---AQSRIKMLErMELIA--------- 290
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 254 hkPVKIE-PLRADARAGTAIEARGLTMR-----FGDFTAVDHVSFRIRRGEIFGFLGSNGCGKSTTMKMLTGLLPATEGT 327
Cdd:PRK10636 291 --PAHVDnPFHFSFRAPESLPNPLLKMEkvsagYGDRIILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELAPVSGE 368
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 328 AQLfgkevdPKDIntrrRVGYMSQ---AFsLYSELTVRQNLvlhARL---------------FGVPAaeidARVDEMARR 389
Cdd:PRK10636 369 IGL------AKGI----KLGYFAQhqlEF-LRADESPLQHL---ARLapqeleqklrdylggFGFQG----DKVTEETRR 430
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 390 FGladiygmlpdslpLGMRQRLSLAVAMVHKPELLILDEPTSGVDPVARDSFWQLMIDLaRRDLVTIFISTHFMNEAQrc 469
Cdd:PRK10636 431 FS-------------GGEKARLVLALIVWQRPNLLLLDEPTNHLDLDMRQALTEALIDF-EGALVVVSHDRHLLRSTT-- 494
|
570
....*....|.
gi 505416896 470 DRISLMHAGRV 480
Cdd:PRK10636 495 DDLYLVHDGKV 505
|
|
| NosY |
COG1277 |
ABC-type transport system involved in multi-copper enzyme maturation, permease component ... |
812-926 |
3.81e-11 |
|
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: 63.30 E-value: 3.81e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 812 TALAVVRERELGSILNLYVTPVTRTEFLIGK---QVPYVVLAML-NFLLMTMLARIAFDVPVK--GSFMTLLLAVLIFNV 885
Cdd:COG1277 69 GMDAISGERESGTLELLLTLPISRWEIVLGKflgALLVLLLALLiTFLLALLLGLLLFGSPPPdlGAILGFYLGLLLLGL 148
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 505416896 886 VATGIGLLASTFTRSQVAAIVMTIIGTMIPTVQFAGLLTPL 926
Cdd:COG1277 149 AFLAIGLFISALTRNQIVAAILAIALWLLLVILLAWIVLFL 189
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
272-464 |
3.96e-11 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 66.84 E-value: 3.96e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 272 IEARGLTMRFGDFTAVDHVSFRIRRGEIFGFLGSNGCGKSTTMKMLTGLLPATEGTAQLfgkevDPKDintrrRVGYMSQ 351
Cdd:PRK15064 2 LSTANITMQFGAKPLFENISVKFGGGNRYGLIGANGCGKSTFMKILGGDLEPSAGNVSL-----DPNE-----RLGKLRQ 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 352 ---AFSLYSELTVrqnlVL--HARLF-------------------GVPAAEIDARVDEM------ARRFGL---ADI--- 395
Cdd:PRK15064 72 dqfAFEEFTVLDT----VImgHTELWevkqerdriyalpemseedGMKVADLEVKFAEMdgytaeARAGELllgVGIpee 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 505416896 396 --YGMLPDSLPlGMRQRLSLAVAMVHKPELLILDEPTSGVDPvarDSFWQLMIDLARRDLVTIFIS--THFMN 464
Cdd:PRK15064 148 qhYGLMSEVAP-GWKLRVLLAQALFSNPDILLLDEPTNNLDI---NTIRWLEDVLNERNSTMIIIShdRHFLN 216
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
21-229 |
4.00e-11 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 64.77 E-value: 4.00e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 21 ALDRITLDVPAGLTTGLIGPDGVGKSSLLALASGARALQTGGV---------DALGGDMR--------------SRRHRE 77
Cdd:PRK13649 22 ALFDVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVrvddtlitsTSKNKDIKqirkkvglvfqfpeSQLFEE 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 78 RVCRRIAYMPQGLGknlyptLSVEENLQFfarlfghdageRRRRIDALTQSTGLF---PFlsrpagKLSGGMKQKLGLCC 154
Cdd:PRK13649 102 TVLKDVAFGPQNFG------VSQEEAEAL-----------AREKLALVGISESLFeknPF------ELSGGQMRRVAIAG 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 505416896 155 ALIHDPDLLILDEPTTGVDPLARAQFWDLIARIrdERPTMSVIVATAYMDEAQRF-DWLIAMDAGRVLATGAPAEL 229
Cdd:PRK13649 159 ILAMEPKILVLDEPTAGLDPKGRKELMTLFKKL--HQSGMTIVLVTHLMDDVANYaDFVYVLEKGKLVLSGKPKDI 232
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
1-229 |
4.74e-11 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 64.40 E-value: 4.74e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 1 MNASSVVRFSDVSLRYGKTVALDRITLDVPAGLTTGLIGPDGVGKSSLLALASGARALQTGGVDALGGDM----RSRRHR 76
Cdd:PRK11831 2 QSVANLVDMRGVSFTRGNRCIFDNISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEILFDGENIpamsRSRLYT 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 77 ERVCRRIAYMPQGlgknLYPTLSVEENLQFFARlfghdagERRRRIDALTQSTGLFPFLS---RPAGK-----LSGGMKQ 148
Cdd:PRK11831 82 VRKRMSMLFQSGA----LFTDMNVFDNVAYPLR-------EHTQLPAPLLHSTVMMKLEAvglRGAAKlmpseLSGGMAR 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 149 KLGLCCALIHDPDLLILDEPTTGVDPLARAQFWDLIARIRDERPTMSVIVATAYMDEAQRFDWLIAMDAGRVLATGAPAE 228
Cdd:PRK11831 151 RAALARAIALEPDLIMFDEPFVGQDPITMGVLVKLISELNSALGVTCVVVSHDVPEVLSIADHAYIVADKKIVAHGSAQA 230
|
.
gi 505416896 229 L 229
Cdd:PRK11831 231 L 231
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
7-232 |
5.07e-11 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 65.63 E-value: 5.07e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 7 VRFSDVSLRY-GKTVALDRITLDVPAGLTTGLIGPDGVGKSSLLALASGARALqTGGVDALGGdmRSRRHRERVCRRIAY 85
Cdd:PRK11650 4 LKLQAVRKSYdGKTQVIKGIDLDVADGEFIVLVGPSGCGKSTLLRMVAGLERI-TSGEIWIGG--RVVNELEPADRDIAM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 86 MPQglgkN--LYPTLSVEENLQFFARLFGHDAGERRRRIDALTQSTGLFPFLSRPAGKLSGGMKQKLGLCCALIHDPDLL 163
Cdd:PRK11650 81 VFQ----NyaLYPHMSVRENMAYGLKIRGMPKAEIEERVAEAARILELEPLLDRKPRELSGGQRQRVAMGRAIVREPAVF 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 505416896 164 ILDEPTTGVDPLARAQFWDLIARIRDERPTMSVIVA---TAYMDEAQRfdwLIAMDAGRVLATGAPAELLAR 232
Cdd:PRK11650 157 LFDEPLSNLDAKLRVQMRLEIQRLHRRLKTTSLYVThdqVEAMTLADR---VVVMNGGVAEQIGTPVEVYEK 225
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
22-198 |
5.12e-11 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 63.64 E-value: 5.12e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 22 LDRITLDVPAGLTTGLIGPDGVGKSSLLALASGARALQTGGVDALGGD---MRSRRHRERVCRRIAYMPQGLgkNLYPTL 98
Cdd:PRK10584 26 LTGVELVVKRGETIALIGESGSGKSTLLAILAGLDDGSSGEVSLVGQPlhqMDEEARAKLRAKHVGFVFQSF--MLIPTL 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 99 SVEENLQFFARLFGHDAGERRRRIDALTQSTGLFPFLSRPAGKLSGGMKQKLGLCCALIHDPDLLILDEPTTGVDPLARA 178
Cdd:PRK10584 104 NALENVELPALLRGESSRQSRNGAKALLEQLGLGKRLDHLPAQLSGGEQQRVALARAFNGRPDVLFADEPTGNLDRQTGD 183
|
170 180
....*....|....*....|
gi 505416896 179 QFWDLIARIRDERPTMSVIV 198
Cdd:PRK10584 184 KIADLLFSLNREHGTTLILV 203
|
|
| nickel_nikE |
TIGR02769 |
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a ... |
5-230 |
5.42e-11 |
|
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: 64.44 E-value: 5.42e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 5 SVVRFSDVSLRY---------GKTVALDRITLDVPAGLTTGLIGPDGVGKSSLLALASGARALQTGGVDALGGDM----R 71
Cdd:TIGR02769 1 SLLEVRDVTHTYrtgglfgakQRAPVLTNVSLSIEEGETVGLLGRSGCGKSTLARLLLGLEKPAQGTVSFRGQDLyqldR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 72 SRRHRERVCRRIAYmpQGLGKNLYPTLSVE----ENLQFFARLfghDAGERRRRIDALTQSTGLFP-FLSRPAGKLSGGM 146
Cdd:TIGR02769 81 KQRRAFRRDVQLVF--QDSPSAVNPRMTVRqiigEPLRHLTSL---DESEQKARIAELLDMVGLRSeDADKLPRQLSGGQ 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 147 KQKLGLCCALIHDPDLLILDEPTTGVDPLARAQFWDLIARIRDERPTMSVIVaTAYMDEAQRF-DWLIAMDAGRVLATGA 225
Cdd:TIGR02769 156 LQRINIARALAVKPKLIVLDEAVSNLDMVLQAVILELLRKLQQAFGTAYLFI-THDLRLVQSFcQRVAVMDKGQIVEECD 234
|
....*
gi 505416896 226 PAELL 230
Cdd:TIGR02769 235 VAQLL 239
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
17-231 |
6.43e-11 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 63.76 E-value: 6.43e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 17 GKTVALDrITLDVPAGLTTGLIGPDGVGKSSLLALASGARALQTGGVDALGGDMRSRRHRERVCRRIAYMPQGlgKNLYP 96
Cdd:PRK10895 15 GRRVVED-VSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEDISLLPLHARARRGIGYLPQE--ASIFR 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 97 TLSVEENLQFFARLFGHDAGERRR-RIDALTQSTGLFPFLSRPAGKLSGGMKQKLGLCCALIHDPDLLILDEPTTGVDPL 175
Cdd:PRK10895 92 RLSVYDNLMAVLQIRDDLSAEQREdRANELMEEFHIEHLRDSMGQSLSGGERRRVEIARALAANPKFILLDEPFAGVDPI 171
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 505416896 176 ARAQFWDLIARIRDE-----------RPTMSViVATAYMdeaqrfdwliaMDAGRVLATGAPAELLA 231
Cdd:PRK10895 172 SVIDIKRIIEHLRDSglgvlitdhnvRETLAV-CERAYI-----------VSQGHLIAHGTPTEILQ 226
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
6-232 |
1.20e-10 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 64.05 E-value: 1.20e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 6 VVRFSDVSLRY----GKTVALDRITLDVPAGLTTGLIGPDGVGKSSLLALASGaraLQ--TGG---VDalGGDMR--SRR 74
Cdd:PRK11153 1 MIELKNISKVFpqggRTIHALNNVSLHIPAGEIFGVIGASGAGKSTLIRCINL---LErpTSGrvlVD--GQDLTalSEK 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 75 HRERVCRRIAYMPQGLgkNLYPTLSVEENLQFFARLFGHDAGERRRRIDALTQSTGLFPFLSR-PAgKLSGGMKQKLGLC 153
Cdd:PRK11153 76 ELRKARRQIGMIFQHF--NLLSSRTVFDNVALPLELAGTPKAEIKARVTELLELVGLSDKADRyPA-QLSGGQKQRVAIA 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 154 CALIHDPDLLILDEPTTGVDPLARAQFWDLIARIrDERPTMSVIVATAYMDEAQRF-DWLIAMDAGRVLATGAPAELLAR 232
Cdd:PRK11153 153 RALASNPKVLLCDEATSALDPATTRSILELLKDI-NRELGLTIVLITHEMDVVKRIcDRVAVIDAGRLVEQGTVSEVFSH 231
|
|
| PRK13546 |
PRK13546 |
teichoic acids export ABC transporter ATP-binding subunit TagH; |
283-480 |
1.48e-10 |
|
teichoic acids export ABC transporter ATP-binding subunit TagH;
Pssm-ID: 184131 [Multi-domain] Cd Length: 264 Bit Score: 62.91 E-value: 1.48e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 283 DFTAVDHVSFRIRRGEIFGFLGSNGCGKSTTMKMLTGLLPATEGTAQLFGkEVDPKDINTrrrvgymsqafSLYSELTVR 362
Cdd:PRK13546 36 TFFALDDISLKAYEGDVIGLVGINGSGKSTLSNIIGGSLSPTVGKVDRNG-EVSVIAISA-----------GLSGQLTGI 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 363 QNLVLHARLFGVPAAEIDARVDEMARRFGLADIYGMLPDSLPLGMRQRLSLAVAMVHKPELLILDEPTSgvdpVARDSFW 442
Cdd:PRK13546 104 ENIEFKMLCMGFKRKEIKAMTPKIIEFSELGEFIYQPVKKYSSGMRAKLGFSINITVNPDILVIDEALS----VGDQTFA 179
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 505416896 443 QLMIDLA---RRDLVTIFISTHFMNEAQR-CDRISLMHAGRV 480
Cdd:PRK13546 180 QKCLDKIyefKEQNKTIFFVSHNLGQVRQfCTKIAWIEGGKL 221
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
6-220 |
1.60e-10 |
|
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: 62.10 E-value: 1.60e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 6 VVRFSDVSLRYGK---TVALDRITLDVPAGLTTGLIGPDGVGKSSLLALASGARALQTGGVdALGGDMRSRRHRERVCRR 82
Cdd:cd03248 11 IVKFQNVTFAYPTrpdTLVLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQV-LLDGKPISQYEHKYLHSK 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 83 IAYMPQglgknlYPTL---SVEENLQFFArlfghdAGERRRRIDALTQSTGLFPFLSRPA-----------GKLSGGMKQ 148
Cdd:cd03248 90 VSLVGQ------EPVLfarSLQDNIAYGL------QSCSFECVKEAAQKAHAHSFISELAsgydtevgekgSQLSGGQKQ 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 505416896 149 KLGLCCALIHDPDLLILDEPTTGVDPLARAQFWDLiarIRDERPTMSVIVATAYMDEAQRFDWLIAMDAGRV 220
Cdd:cd03248 158 RVAIARALIRNPQVLILDEATSALDAESEQQVQQA---LYDWPERRTVLVIAHRLSTVERADQILVLDGGRI 226
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
275-483 |
1.73e-10 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 64.37 E-value: 1.73e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 275 RGLTMRFGDFTAVDHVSFRIRRGEIFGFLGSNGCGKSTTMKMLTGLLPATEGTAQLFGKEVDPKDINT--RRRVGYMSQA 352
Cdd:PRK10982 2 SNISKSFPGVKALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEIDFKSSKEalENGISMVHQE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 353 FSLYSELTVRQNLVL-----------HARLFGVPAA---EIDARVDEmarRFGLADiygmlpdsLPLGMRQRLSLAVAMV 418
Cdd:PRK10982 82 LNLVLQRSVMDNMWLgryptkgmfvdQDKMYRDTKAifdELDIDIDP---RAKVAT--------LSVSQMQMIEIAKAFS 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 505416896 419 HKPELLILDEPTSGVDPVARDSFWQLMIDLARRDLVTIFIStHFMNEA-QRCDRISLMHAGRVLAS 483
Cdd:PRK10982 151 YNAKIVIMDEPTSSLTEKEVNHLFTIIRKLKERGCGIVYIS-HKMEEIfQLCDEITILRDGQWIAT 215
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
272-494 |
2.09e-10 |
|
multi drug resistance-associated protein (MRP); This model describes multi drug resistance-associated protein (MRP) in eukaryotes. The multidrug resistance-associated protein is an integral membrane protein that causes multidrug resistance when overexpressed in mammalian cells. It belongs to ABC transporter superfamily. The protein topology and function was experimentally demonstrated by epitope tagging and immunofluorescence. Insertion of tags in the critical regions associated with drug efflux, abrogated its function. The C-terminal domain seem to highly conserved. [Transport and binding proteins, Other]
Pssm-ID: 188098 [Multi-domain] Cd Length: 1522 Bit Score: 64.97 E-value: 2.09e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 272 IEARGLTMRFG---DFTaVDHVSFRIRRGEIFGFLGSNGCGKSTTMKMLTGLLPATEGTAQLFGkeVDPKDI---NTRRR 345
Cdd:TIGR00957 1285 VEFRNYCLRYRedlDLV-LRHINVTIHGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDG--LNIAKIglhDLRFK 1361
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 346 VGYMSQAFSLYSElTVRQNLvlhaRLFGVPAAEIDARVDEMARrfgLADIYGMLPD-----------SLPLGMRQRLSLA 414
Cdd:TIGR00957 1362 ITIIPQDPVLFSG-SLRMNL----DPFSQYSDEEVWWALELAH---LKTFVSALPDkldhecaeggeNLSVGQRQLVCLA 1433
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 415 VAMVHKPELLILDEPTSGVDpVARDSFWQLMIDlARRDLVTIFISTHFMNEAQRCDRISLMHAGRVLASDSPAELVRARG 494
Cdd:TIGR00957 1434 RALLRKTKILVLDEATAAVD-LETDNLIQSTIR-TQFEDCTVLTIAHRLNTIMDYTRVIVLDKGEVAEFGAPSNLLQQRG 1511
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
291-462 |
2.09e-10 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 64.27 E-value: 2.09e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 291 SFRIRRGEIFGFLGSNGCGKSTTMKMLTGLLPATEGTAQlfgkevdpkdiNTRRRVGYMS--QAFSLYSELTVRQN---L 365
Cdd:PRK10938 23 SLTLNAGDSWAFVGANGSGKSALARALAGELPLLSGERQ-----------SQFSHITRLSfeQLQKLVSDEWQRNNtdmL 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 366 VLHARLFGVPAAEI-------DARVDEMARRFGLADIYGMLPDSLPLGMRQRLSLAVAMVHKPELLILDEPTSGVDPVAR 438
Cdd:PRK10938 92 SPGEDDTGRTTAEIiqdevkdPARCEQLAQQFGITALLDRRFKYLSTGETRKTLLCQALMSEPDLLILDEPFDGLDVASR 171
|
170 180
....*....|....*....|....
gi 505416896 439 DSFWQLMIDLARRDLVTIFISTHF 462
Cdd:PRK10938 172 QQLAELLASLHQSGITLVLVLNRF 195
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
287-459 |
2.13e-10 |
|
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: 60.25 E-value: 2.13e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 287 VDHVSFRIRRGEIFGFLGSNGCGKSTTMKMLTGLLPATEGTAqlfgkevdpkDINTRRRVGYMSQAfSLYSELTVRQNLv 366
Cdd:cd03223 17 LKDLSFEIKPGDRLLITGPSGTGKSSLFRALAGLWPWGSGRI----------GMPEGEDLLFLPQR-PYLPLGTLREQL- 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 367 lharlfgvpaaeidarvdemarrfgladIYgmlP--DSLPLGMRQRLSLAVAMVHKPELLILDEPTSGVDPVARDSFWQL 444
Cdd:cd03223 85 ----------------------------IY---PwdDVLSGGEQQRLAFARLLLHKPKFVFLDEATSALDEESEDRLYQL 133
|
170
....*....|....*
gi 505416896 445 MidlarRDLVTIFIS 459
Cdd:cd03223 134 L-----KELGITVIS 143
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
268-493 |
2.38e-10 |
|
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis fibrosis transmembrane conductor regulator (CFTR) in eukaryotes. The principal role of this protein is chloride ion conductance. The protein is predicted to consist of 12 transmembrane domains. Mutations or lesions in the genetic loci have been linked to the aetiology of asthma, bronchiectasis, chronic obstructive pulmonary disease etc. Disease-causing mutations have been studied by 36Cl efflux assays in vitro cell cultures and electrophysiology, all of which point to the impairment of chloride channel stability and not the biosynthetic processing per se. [Transport and binding proteins, Anions]
Pssm-ID: 273530 [Multi-domain] Cd Length: 1490 Bit Score: 64.93 E-value: 2.38e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 268 AGTAIEARGLTMRF--GDFTAVDHVSFRIRRGEIFGFLGSNGCGKSTTMKMLTGLLpATEGTAQLFGKEVDPKDINT-RR 344
Cdd:TIGR01271 1214 SGGQMDVQGLTAKYteAGRAVLQDLSFSVEGGQRVGLLGRTGSGKSTLLSALLRLL-STEGEIQIDGVSWNSVTLQTwRK 1292
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 345 RVGYMSQAFSLYSElTVRQNLVLHARLfgvpaaeIDARVDEMARRFGLADIYGMLPDSLPL-----------GMRQRLSL 413
Cdd:TIGR01271 1293 AFGVIPQKVFIFSG-TFRKNLDPYEQW-------SDEEIWKVAEEVGLKSVIEQFPDKLDFvlvdggyvlsnGHKQLMCL 1364
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 414 AVAMVHKPELLILDEPTSGVDPVArdsfWQLMidlaRRDL------VTIFISTHFMNEAQRCDRISLMHAGRVLASDSPA 487
Cdd:TIGR01271 1365 ARSILSKAKILLLDEPSAHLDPVT----LQII----RKTLkqsfsnCTVILSEHRVEALLECQQFLVIEGSSVKQYDSIQ 1436
|
....*.
gi 505416896 488 ELVRAR 493
Cdd:TIGR01271 1437 KLLNET 1442
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
11-224 |
2.73e-10 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 61.78 E-value: 2.73e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 11 DVSLRYGKTVALDRITLDVPAGLTTGLIGPDGVGKSSLL-------ALASGARA---LQTGGVDALGGDMRSRRHRERVC 80
Cdd:PRK14267 9 NLRVYYGSNHVIKGVDLKIPQNGVFALMGPSGCGKSTLLrtfnrllELNEEARVegeVRLFGRNIYSPDVDPIEVRREVG 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 81 RRIAYmpqglgKNLYPTLSVEENLQFFARLFG--HDAGERRRRIDALTQSTGLFP----FLSRPAGKLSGGMKQKLGLCC 154
Cdd:PRK14267 89 MVFQY------PNPFPHLTIYDNVAIGVKLNGlvKSKKELDERVEWALKKAALWDevkdRLNDYPSNLSGGQRQRLVIAR 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 505416896 155 ALIHDPDLLILDEPTTGVDPLARAQFWDLIARIRDErptMSVIVATAYMDEAQRF-DWLIAMDAGRVLATG 224
Cdd:PRK14267 163 ALAMKPKILLMDEPTANIDPVGTAKIEELLFELKKE---YTIVLVTHSPAQAARVsDYVAFLYLGKLIEVG 230
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
294-434 |
3.15e-10 |
|
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: 61.66 E-value: 3.15e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 294 IRRGEIFGFLGSNGCGKSTTMKMLTGLLPATEGTAQLFGKEvdpkdintrrrVGYMSQAFSLYSELTVRQNLvlharlfg 373
Cdd:cd03237 22 ISESEVIGILGPNGIGKTTFIKMLAGVLKPDEGDIEIELDT-----------VSYKPQYIKADYEGTVRDLL-------- 82
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 505416896 374 vpaAEIDARV-------DEMARRFGLADIYGMLPDSLPLGMRQRLSLAVAMVHKPELLILDEPTSGVD 434
Cdd:cd03237 83 ---SSITKDFythpyfkTEIAKPLQIEQILDREVPELSGGELQRVAIAACLSKDADIYLLDEPSAYLD 147
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
272-493 |
3.62e-10 |
|
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: 61.79 E-value: 3.62e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 272 IEARGLTMRF--GDFTAVDHVSFRIRRGEIFGFLGSNGCGKSTTMKMLTGLLpATEGTAQLFGKEVDPKDINT-RRRVGY 348
Cdd:cd03289 3 MTVKDLTAKYteGGNAVLENISFSISPGQRVGLLGRTGSGKSTLLSAFLRLL-NTEGDIQIDGVSWNSVPLQKwRKAFGV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 349 MSQAFSLYSElTVRQNLVLHARlfgvpaaEIDARVDEMARRFGLADIYGMLPDSLPL-----------GMRQRLSLAVAM 417
Cdd:cd03289 82 IPQKVFIFSG-TFRKNLDPYGK-------WSDEEIWKVAEEVGLKSVIEQFPGQLDFvlvdggcvlshGHKQLMCLARSV 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 418 VHKPELLILDEPTSGVDPVArdsfwqlmIDLARRDL------VTIFISTHFMNEAQRCDRISLMHAGRVLASDSPAELVR 491
Cdd:cd03289 154 LSKAKILLLDEPSAHLDPIT--------YQVIRKTLkqafadCTVILSEHRIEAMLECQRFLVIEENKVRQYDSIQKLLN 225
|
..
gi 505416896 492 AR 493
Cdd:cd03289 226 EK 227
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
280-434 |
5.08e-10 |
|
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: 59.97 E-value: 5.08e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 280 RFGDFTAVDHVSFRIRRGEIFGFLGSNGCGKSTTMKMLTGLLP---ATEGTAQLFGKEVDPKDINTRRRVGYMSQAFSLY 356
Cdd:cd03233 16 GRSKIPILKDFSGVVKPGEMVLVLGRPGSGCSTLLKALANRTEgnvSVEGDIHYNGIPYKEFAEKYPGEIIYVSEEDVHF 95
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 505416896 357 SELTVRQNLVLHARLFGvpaaeidarvDEMARrfglaDIYGmlpdslplGMRQRLSLAVAMVHKPELLILDEPTSGVD 434
Cdd:cd03233 96 PTLTVRETLDFALRCKG----------NEFVR-----GISG--------GERKRVSIAEALVSRASVLCWDNSTRGLD 150
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
17-232 |
8.00e-10 |
|
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: 62.46 E-value: 8.00e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 17 GKTVALDRITLDVPAGLTTGLIGPDGVGKSSLLALASGARALQTGGV------------DALGgdmrsrrhrervcRRIA 84
Cdd:COG4618 343 SKRPILRGVSFSLEPGEVLGVIGPSGSGKSTLARLLVGVWPPTAGSVrldgadlsqwdrEELG-------------RHIG 409
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 85 YMPQGLGknLYPTlSVEENLqffARLFGHDAGE-----RRRRIDALTQStglFP-----FLSRPAGKLSGGMKQKLGLCC 154
Cdd:COG4618 410 YLPQDVE--LFDG-TIAENI---ARFGDADPEKvvaaaKLAGVHEMILR---LPdgydtRIGEGGARLSGGQRQRIGLAR 480
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 155 ALIHDPDLLILDEPTTGVDPLARAQFWDLIARIRdERPTMSVIVA--TAYMDEAqrfDWLIAMDAGRVLATGAPAELLAR 232
Cdd:COG4618 481 ALYGDPRLVVLDEPNSNLDDEGEAALAAAIRALK-ARGATVVVIThrPSLLAAV---DKLLVLRDGRVQAFGPRDEVLAR 556
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
10-229 |
8.62e-10 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 61.64 E-value: 8.62e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 10 SDVSLRYGKTVALDRITLDVPAGLTTGLIGPDGVGKSSLLALASGARALQTGGVDALGGDMrsrRHRERVCRRIAYMPQG 89
Cdd:PRK10851 6 ANIKKSFGRTQVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFHGTDV---SRLHARDRKVGFVFQH 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 90 LGknLYPTLSVEENLQFFARLFGH----DAGERRRRIDALTQSTGLFPFLSRPAGKLSGGMKQKLGLCCALIHDPDLLIL 165
Cdd:PRK10851 83 YA--LFRHMTVFDNIAFGLTVLPRrerpNAAAIKAKVTQLLEMVQLAHLADRYPAQLSGGQKQRVALARALAVEPQILLL 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 505416896 166 DEPTTGVDPLARAQFWDLIARIRDERPTMSVIVaTAYMDEAQRF-DWLIAMDAGRVLATGAPAEL 229
Cdd:PRK10851 161 DEPFGALDAQVRKELRRWLRQLHEELKFTSVFV-THDQEEAMEVaDRVVVMSQGNIEQAGTPDQV 224
|
|
| SapD |
COG4170 |
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms]; |
275-492 |
8.85e-10 |
|
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms];
Pssm-ID: 443330 [Multi-domain] Cd Length: 331 Bit Score: 61.46 E-value: 8.85e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 275 RGLTMRF----GDFTAVDHVSFRIRRGEIFGFLGSNGCGKSTTMKMLTGLL-PATEGTAQLF---GKEVDPKDINTRRRV 346
Cdd:COG4170 7 RNLTIEIdtpqGRVKAVDRVSLTLNEGEIRGLVGESGSGKSLIAKAICGITkDNWHVTADRFrwnGIDLLKLSPRERRKI 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 347 --GYMSQAF-----SLYSELTVRQNL--VLHARLFGVP----AAEIDARVDEMARRFGLAD---IYGMLPDSLPLGMRQR 410
Cdd:COG4170 87 igREIAMIFqepssCLDPSAKIGDQLieAIPSWTFKGKwwqrFKWRKKRAIELLHRVGIKDhkdIMNSYPHELTEGECQK 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 411 LSLAVAMVHKPELLILDEPTSGVDPVARDSFWQLMIDLARRDLVTI-FISTHFMNEAQRCDRISLMHAGRVLASDSPAEL 489
Cdd:COG4170 167 VMIAMAIANQPRLLIADEPTNAMESTTQAQIFRLLARLNQLQGTSIlLISHDLESISQWADTITVLYCGQTVESGPTEQI 246
|
...
gi 505416896 490 VRA 492
Cdd:COG4170 247 LKS 249
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
5-434 |
1.20e-09 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 62.28 E-value: 1.20e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 5 SVVRFSDVSLRYGKTVALDRITLDVPAGLTTGLIGPDGVGKSSLLALASGARALQTGGV----DALGGDMRSRRHRERVC 80
Cdd:PRK11147 2 SLISIHGAWLSFSDAPLLDNAELHIEDNERVCLVGRNGAGKSTLMKILNGEVLLDDGRIiyeqDLIVARLQQDPPRNVEG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 81 RRIAYMPQGL---GKNL--YPTLSV-------EENLQFFARLFG----HDAGERRRRIDALTQSTGLFPflSRPAGKLSG 144
Cdd:PRK11147 82 TVYDFVAEGIeeqAEYLkrYHDISHlvetdpsEKNLNELAKLQEqldhHNLWQLENRINEVLAQLGLDP--DAALSSLSG 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 145 GMKQKLGLCCALIHDPDLLILDEPTTGVDPLA---------------------RAQFWDLIARIRD-ERptmSVIVA--- 199
Cdd:PRK11147 160 GWLRKAALGRALVSNPDVLLLDEPTNHLDIETiewlegflktfqgsiifishdRSFIRNMATRIVDlDR---GKLVSypg 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 200 --TAYMD---EAQRFDWLIAMDAGRVLA-------TGAPAEllaRTGCDSLEAAFIALlpENERRGHKPV----KIEpLR 263
Cdd:PRK11147 237 nyDQYLLekeEALRVEELQNAEFDRKLAqeevwirQGIKAR---RTRNEGRVRALKAL--RRERSERREVmgtaKMQ-VE 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 264 ADARAGTAI-EARGLTMRFGDFTAVDHVSFRIRRGEIFGFLGSNGCGKSTTMKMLTGLLPATEGTAQlfgkevdpkdINT 342
Cdd:PRK11147 311 EASRSGKIVfEMENVNYQIDGKQLVKDFSAQVQRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRIH----------CGT 380
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 343 RRRVGYMSQ-AFSLYSELTVRQNLvlharlfgvpaAE--IDARVDEMARRfgladIYGMLPDSL--------PL-----G 406
Cdd:PRK11147 381 KLEVAYFDQhRAELDPEKTVMDNL-----------AEgkQEVMVNGRPRH-----VLGYLQDFLfhpkramtPVkalsgG 444
|
490 500
....*....|....*....|....*...
gi 505416896 407 MRQRLSLAVAMVHKPELLILDEPTSGVD 434
Cdd:PRK11147 445 ERNRLLLARLFLKPSNLLILDEPTNDLD 472
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
299-485 |
1.38e-09 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 61.04 E-value: 1.38e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 299 IFGFLGSngcGKSTTMKMLTGLLPATEGTAQLFGKE-VDP-KDIN---TRRRVGYMSQAFSLYSELTVRQNLvlharLFG 373
Cdd:PRK11144 29 IFGRSGA---GKTSLINAISGLTRPQKGRIVLNGRVlFDAeKGIClppEKRRIGYVFQDARLFPHYKVRGNL-----RYG 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 374 VpAAEIDARVDEMARRFGLADIYGMLPDSLPLGMRQRLSLAVAMVHKPELLILDEPTSGVD-PVARdsfwQLMI---DLA 449
Cdd:PRK11144 101 M-AKSMVAQFDKIVALLGIEPLLDRYPGSLSGGEKQRVAIGRALLTAPELLLMDEPLASLDlPRKR----ELLPyleRLA 175
|
170 180 190
....*....|....*....|....*....|....*..
gi 505416896 450 RRDLVTIFISTHFMNEAQR-CDRISLMHAGRVLASDS 485
Cdd:PRK11144 176 REINIPILYVSHSLDEILRlADRVVVLEQGKVKAFGP 212
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
17-231 |
1.74e-09 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 59.38 E-value: 1.74e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 17 GKTVaLDRITLDVPAGLTTGLIGPDGVGKSSLLalasgaRALQ-----TGGVDALGG-DMRSRRHRERVCRRIAYMPQGL 90
Cdd:PRK11264 15 GQTV-LHGIDLEVKPGEVVAIIGPSGSGKTTLL------RCINlleqpEAGTIRVGDiTIDTARSLSQQKGLIRQLRQHV 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 91 GK-----NLYPTLSVEENL---QFFARLFGHDAGERRRRidALTQSTGLfpflsrpAGK-------LSGGMKQKLGLCCA 155
Cdd:PRK11264 88 GFvfqnfNLFPHRTVLENIiegPVIVKGEPKEEATARAR--ELLAKVGL-------AGKetsyprrLSGGQQQRVAIARA 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 505416896 156 LIHDPDLLILDEPTTGVDPLARAQFWDLIARIRDERPTMsVIVaTAYMDEAQRF-DWLIAMDAGRVLATGAPAELLA 231
Cdd:PRK11264 159 LAMRPEVILFDEPTSALDPELVGEVLNTIRQLAQEKRTM-VIV-THEMSFARDVaDRAIFMDQGRIVEQGPAKALFA 233
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
7-226 |
2.73e-09 |
|
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C is also known as MRP (multidrug resistance-associated protein). Some of the MRP members have five additional transmembrane segments in their N-terminus, but the function of these additional membrane-spanning domains is not clear. The MRP was found in the multidrug-resistance lung cancer cell in which p-glycoprotein was not overexpressed. MRP exports glutathione by drug stimulation, as well as, certain substrates in conjugated forms with anions, such as glutathione, glucuronate, and sulfate.
Pssm-ID: 213211 [Multi-domain] Cd Length: 221 Bit Score: 58.27 E-value: 2.73e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 7 VRFSDVSLRYGKT--VALDRITLDVPAGLTTGLIGPDGVGKSSL-LAL------ASGAraLQTGGVD--ALG-GDMRSRr 74
Cdd:cd03244 3 IEFKNVSLRYRPNlpPVLKNISFSIKPGEKVGIVGRTGSGKSSLlLALfrlvelSSGS--ILIDGVDisKIGlHDLRSR- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 75 hrervcrrIAYMPQGlgknlyPTL---SVEENLQFFARlfgHDAGERrrrIDALtQSTGLFPFLSRPAGKL--------- 142
Cdd:cd03244 80 --------ISIIPQD------PVLfsgTIRSNLDPFGE---YSDEEL---WQAL-ERVGLKEFVESLPGGLdtvveegge 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 143 --SGGMKQKLGLCCALIHDPDLLILDEPTTGVDPLARAqfwdLIAR-IRDERPTMSVI-VA---TAYMDeaqrFDWLIAM 215
Cdd:cd03244 139 nlSVGQRQLLCLARALLRKSKILVLDEATASVDPETDA----LIQKtIREAFKDCTVLtIAhrlDTIID----SDRILVL 210
|
250
....*....|.
gi 505416896 216 DAGRVLATGAP 226
Cdd:cd03244 211 DKGRVVEFDSP 221
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
286-495 |
2.91e-09 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 60.80 E-value: 2.91e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 286 AVDHVSFRIRRGEIFGFLGSNGCGKSTTMKMLTGLLPATEGTAQLFGKEV-DPKDINTRRRVGYMSQAFSLYSElTVRQN 364
Cdd:PRK11176 358 ALRNINFKIPAGKTVALVGRSGSGKSTIANLLTRFYDIDEGEILLDGHDLrDYTLASLRNQVALVSQNVHLFND-TIANN 436
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 365 LVlHARLFGVPAAEIDaRVDEMARRF--------GLADIYGMLPDSLPLGMRQRLSLAVAMVHKPELLILDEPTSGVDPV 436
Cdd:PRK11176 437 IA-YARTEQYSREQIE-EAARMAYAMdfinkmdnGLDTVIGENGVLLSGGQRQRIAIARALLRDSPILILDEATSALDTE 514
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 505416896 437 ARDSFwQLMIDLARRDLVTIFIStHFMNEAQRCDRISLMHAGRVLASDSPAELVRARGA 495
Cdd:PRK11176 515 SERAI-QAALDELQKNRTSLVIA-HRLSTIEKADEILVVEDGEIVERGTHAELLAQNGV 571
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
18-231 |
2.92e-09 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 58.93 E-value: 2.92e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 18 KTVaLDRITLDVPAGLTTGLIGPDGVGKSSLLALASGARALQTGGVDALGGDMR--SRRHRERVCRRIAYMPQGLGKNLY 95
Cdd:PRK10419 25 QTV-LNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWRGEPLAklNRAQRKAFRRDIQMVFQDSISAVN 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 96 PTLSVEENLQFFAR-LFGHDAGERRRRIDALTQSTGLFP-FLSRPAGKLSGGMKQKLGLCCALIHDPDLLILDEPTTGVD 173
Cdd:PRK10419 104 PRKTVREIIREPLRhLLSLDKAERLARASEMLRAVDLDDsVLDKRPPQLSGGQLQRVCLARALAVEPKLLILDEAVSNLD 183
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 505416896 174 PLARAQFWDLIARIRDERPTMSVIVaTAYMDEAQRF-DWLIAMDAGRVLATGAPAELLA 231
Cdd:PRK10419 184 LVLQAGVIRLLKKLQQQFGTACLFI-THDLRLVERFcQRVMVMDNGQIVETQPVGDKLT 241
|
|
| nickel_nikD |
TIGR02770 |
nickel import ATP-binding protein NikD; This family represents the NikD subunit of a ... |
21-229 |
3.28e-09 |
|
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: 58.15 E-value: 3.28e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 21 ALDRITLDVPAGLTTGLIGPDGVGKSsLLALAS----GARALQTGGVDALGGdmRSRRHRERVCRRIAYMPQGLGKNLYP 96
Cdd:TIGR02770 1 LVQDLNLSLKRGEVLALVGESGSGKS-LTCLAIlgllPPGLTQTSGEILLDG--RPLLPLSIRGRHIATIMQNPRTAFNP 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 97 TLSVEENLQFFARLFGHDAGERRRRIDALTQSTGL---------FPFlsrpagKLSGGMKQKLGLCCALIHDPDLLILDE 167
Cdd:TIGR02770 78 LFTMGNHAIETLRSLGKLSKQARALILEALEAVGLpdpeevlkkYPF------QLSGGMLQRVMIALALLLEPPFLIADE 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 505416896 168 PTTGVDPLARAQFWDLIARIRDERPTmSVIVATAYMDE-AQRFDWLIAMDAGRVLATGAPAEL 229
Cdd:TIGR02770 152 PTTDLDVVNQARVLKLLRELRQLFGT-GILLITHDLGVvARIADEVAVMDDGRIVERGTVKEI 213
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
17-254 |
3.60e-09 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 58.95 E-value: 3.60e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 17 GKTVaLDRITLDVPAGLTTGLIGPDGVGKSSLLA----LASGARALQTGGVDALGG----DMRSRRHRERVCRRIAYMPq 88
Cdd:PRK14271 33 GKTV-LDQVSMGFPARAVTSLMGPTGSGKTTFLRtlnrMNDKVSGYRYSGDVLLGGrsifNYRDVLEFRRRVGMLFQRP- 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 89 glgkNLYPtLSVEENLqfFARLFGHDAGER---RRRIDALTQSTGLFPF----LSRPAGKLSGGMKQKLGLCCALIHDPD 161
Cdd:PRK14271 111 ----NPFP-MSIMDNV--LAGVRAHKLVPRkefRGVAQARLTEVGLWDAvkdrLSDSPFRLSGGQQQLLCLARTLAVNPE 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 162 LLILDEPTTGVDPLARAQFWDLIARIRDErptMSVIVATAYMDEAQRF-DWLIAMDAGRVLATGaPAELLARTGCDSLEA 240
Cdd:PRK14271 184 VLLLDEPTSALDPTTTEKIEEFIRSLADR---LTVIIVTHNLAQAARIsDRAALFFDGRLVEEG-PTEQLFSSPKHAETA 259
|
250
....*....|....*..
gi 505416896 241 AFIALLP---ENERRGH 254
Cdd:PRK14271 260 RYVAGLSgdvKDAKRGN 276
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
290-434 |
3.60e-09 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 61.20 E-value: 3.60e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 290 VSFRIRRGEIFGFLGSNGCGKSTTMKMLTGLLPATEGTAqLFGKEVDPKDINT---RRRVGYMSQ-------------AF 353
Cdd:PTZ00265 404 LNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDI-IINDSHNLKDINLkwwRSKIGVVSQdpllfsnsiknniKY 482
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 354 SLYS--EL-------------------------------------TVRQNLVLHARlfgvPAAEI--DARVDEMARRFGL 392
Cdd:PTZ00265 483 SLYSlkDLealsnyynedgndsqenknkrnscrakcagdlndmsnTTDSNELIEMR----KNYQTikDSEVVDVSKKVLI 558
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 505416896 393 ADIYGMLPD-----------SLPLGMRQRLSLAVAMVHKPELLILDEPTSGVD 434
Cdd:PTZ00265 559 HDFVSALPDkyetlvgsnasKLSGGQKQRISIARAIIRNPKILILDEATSSLD 611
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
99-231 |
3.92e-09 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 59.33 E-value: 3.92e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 99 SVEENLQFFARLFGHDAGERRRRIDALTQSTGL-FPFLSRPAGKLSGGMKQKLGLCCALIHDPDLLILDEPTTGVDPLAR 177
Cdd:PRK13651 122 TIEKDIIFGPVSMGVSKEEAKKRAAKYIELVGLdESYLQRSPFELSGGQKRRVALAGILAMEPDFLVFDEPTAGLDPQGV 201
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 505416896 178 AQFWDLIARIRDERPTmsVIVATAYMDEA-QRFDWLIAMDAGRVLATGAPAELLA 231
Cdd:PRK13651 202 KEILEIFDNLNKQGKT--IILVTHDLDNVlEWTKRTIFFKDGKIIKDGDTYDILS 254
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
138-327 |
4.00e-09 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 60.52 E-value: 4.00e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 138 PAGKLSGGMKQKLGLCCALIHDPDLLILDEPTTGVDplARAQFWdLIARIRDERPTmsVIVATA---YMDEAQrfDWLIA 214
Cdd:PRK11819 160 KVTKLSGGERRRVALCRLLLEKPDMLLLDEPTNHLD--AESVAW-LEQFLHDYPGT--VVAVTHdryFLDNVA--GWILE 232
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 215 MDAGRvlatGAP------------AELLA----------RTGCDSLE-----------------AAFIALLPENERRghk 255
Cdd:PRK11819 233 LDRGR----GIPwegnysswleqkAKRLAqeekqeaarqKALKRELEwvrqspkarqakskarlARYEELLSEEYQK--- 305
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 505416896 256 pvKIEPLR----ADARAG-TAIEARGLTMRFGDFTAVDHVSFRIRRGEIFGFLGSNGCGKSTTMKMLTGLLPATEGT 327
Cdd:PRK11819 306 --RNETNEifipPGPRLGdKVIEAENLSKSFGDRLLIDDLSFSLPPGGIVGIIGPNGAGKSTLFKMITGQEQPDSGT 380
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
10-231 |
4.27e-09 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 58.44 E-value: 4.27e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 10 SDVSLRYGKTVALDRITLDVPAGLTTGLIGPDGVGKSSLLALASGARALQTGGVDALGGDMR------------SRRHRE 77
Cdd:PRK10619 9 IDLHKRYGEHEVLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNGQTINlvrdkdgqlkvaDKNQLR 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 78 RVCRRIAYMPQGLgkNLYPTLSVEEN-LQFFARLFGHDAGERRRRIDALTQSTGLfpfLSRPAGK----LSGGMKQKLGL 152
Cdd:PRK10619 89 LLRTRLTMVFQHF--NLWSHMTVLENvMEAPIQVLGLSKQEARERAVKYLAKVGI---DERAQGKypvhLSGGQQQRVSI 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 153 CCALIHDPDLLILDEPTTGVDPLARAQFWDLIARIRDERPTMsvIVATAYMDEAQRF-DWLIAMDAGRVLATGAPAELLA 231
Cdd:PRK10619 164 ARALAMEPEVLLFDEPTSALDPELVGEVLRIMQQLAEEGKTM--VVVTHEMGFARHVsSHVIFLHQGKIEEEGAPEQLFG 241
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
7-231 |
4.51e-09 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 58.69 E-value: 4.51e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 7 VRFSDVSLRYG-----KTVALDRITLDVPAGLTTGLIGPDGVGKSSLLALASGARALQTGGVDALGGDMrsrrhrervcr 81
Cdd:PRK13641 3 IKFENVDYIYSpgtpmEKKGLDNISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITIAGYHI----------- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 82 riayMPQGLGKNL------------YPTL-----SVEENLQFFARLFGhdAGERRRRIDALT--QSTGLFP-FLSRPAGK 141
Cdd:PRK13641 72 ----TPETGNKNLkklrkkvslvfqFPEAqlfenTVLKDVEFGPKNFG--FSEDEAKEKALKwlKKVGLSEdLISKSPFE 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 142 LSGGMKQKLGLCCALIHDPDLLILDEPTTGVDPLARAQFWDLIARIrdERPTMSVIVATAYMDE-AQRFDWLIAMDAGRV 220
Cdd:PRK13641 146 LSGGQMRRVAIAGVMAYEPEILCLDEPAAGLDPEGRKEMMQLFKDY--QKAGHTVILVTHNMDDvAEYADDVLVLEHGKL 223
|
250
....*....|.
gi 505416896 221 LATGAPAELLA 231
Cdd:PRK13641 224 IKHASPKEIFS 234
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
25-224 |
5.62e-09 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 59.12 E-value: 5.62e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 25 ITLDVPAGLTTGLIGPDGVGKSSLLALASGARALQTGGVdALGG----DMRSRRHRERVCRRIAYMPQGlgKNLYPTLSV 100
Cdd:PRK11144 17 VNLTLPAQGITAIFGRSGAGKTSLINAISGLTRPQKGRI-VLNGrvlfDAEKGICLPPEKRRIGYVFQD--ARLFPHYKV 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 101 EENLQFfarlfGHdAGERRRRIDALTQSTGLFPFLSRPAGKLSGGMKQKLGLCCALIHDPDLLILDEPTTGVDpLARAQf 180
Cdd:PRK11144 94 RGNLRY-----GM-AKSMVAQFDKIVALLGIEPLLDRYPGSLSGGEKQRVAIGRALLTAPELLLMDEPLASLD-LPRKR- 165
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 505416896 181 wDLIARIrdERPTMSVIVATAY----MDEAQRF-DWLIAMDAGRVLATG 224
Cdd:PRK11144 166 -ELLPYL--ERLAREINIPILYvshsLDEILRLaDRVVVLEQGKVKAFG 211
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
3-234 |
5.63e-09 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 60.37 E-value: 5.63e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 3 ASSVVRFSDVSLRY--GKTVALDRITLDVPAGLTTGLIGPDGVGKSSLLALASGARALQTGGVDALGGDMrSRRHRERVC 80
Cdd:PLN03232 1231 SRGSIKFEDVHLRYrpGLPPVLHGLSFFVSPSEKVGVVGRTGAGKSSMLNALFRIVELEKGRIMIDDCDV-AKFGLTDLR 1309
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 81 RRIAYMPQGlgknlyPTL---SVEENLQFFARlfGHDAG-----ERRRRIDALTQST-GLFPFLSRPAGKLSGGMKQKLG 151
Cdd:PLN03232 1310 RVLSIIPQS------PVLfsgTVRFNIDPFSE--HNDADlwealERAHIKDVIDRNPfGLDAEVSEGGENFSVGQRQLLS 1381
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 152 LCCALIHDPDLLILDEPTTGVDPLARAqfwdLIAR-IRDERPTMSVIVATAYMDEAQRFDWLIAMDAGRVLATGAPAELL 230
Cdd:PLN03232 1382 LARALLRRSKILVLDEATASVDVRTDS----LIQRtIREEFKSCTMLVIAHRLNTIIDCDKILVLSSGQVLEYDSPQELL 1457
|
....
gi 505416896 231 ARTG 234
Cdd:PLN03232 1458 SRDT 1461
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
274-435 |
5.93e-09 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 57.17 E-value: 5.93e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 274 ARGLTMRFGDFTAVDHVSFRIRRGEIFGFLGSNGCGKSTTMKMLTGLLPATEGTAQLFGKEVDPKDinTRRRVGYMSQAF 353
Cdd:PRK13543 14 AHALAFSRNEEPVFGPLDFHVDAGEALLVQGDNGAGKTTLLRVLAGLLHVESGQIQIDGKTATRGD--RSRFMAYLGHLP 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 354 SLYSELTVRQNLVLHARLFGVPAAEIDARVDEMArrfGLADIYGMLPDSLPLGMRQRLSLAVAMVHKPELLILDEPTSGV 433
Cdd:PRK13543 92 GLKADLSTLENLHFLCGLHGRRAKQMPGSALAIV---GLAGYEDTLVRQLSAGQKKRLALARLWLSPAPLWLLDEPYANL 168
|
..
gi 505416896 434 DP 435
Cdd:PRK13543 169 DL 170
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
21-190 |
1.02e-08 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 58.18 E-value: 1.02e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 21 ALDRITLDVPAGLTTGLIGPDGVGKSSLlalasgARAL-----QTGG-VDALGGDMR--SRRHRERVCRRIAYMPQGLGK 92
Cdd:PRK15079 36 AVDGVTLRLYEGETLGVVGESGCGKSTF------ARAIiglvkATDGeVAWLGKDLLgmKDDEWRAVRSDIQMIFQDPLA 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 93 NLYPTLSV----EENLQ-FFARLfghDAGERRRRIDALTQSTGLFPFL-SRPAGKLSGGMKQKLGLCCALIHDPDLLILD 166
Cdd:PRK15079 110 SLNPRMTIgeiiAEPLRtYHPKL---SRQEVKDRVKAMMLKVGLLPNLiNRYPHEFSGGQCQRIGIARALILEPKLIICD 186
|
170 180
....*....|....*....|....
gi 505416896 167 EPTTGVDPLARAQFWDLIARIRDE 190
Cdd:PRK15079 187 EPVSALDVSIQAQVVNLLQQLQRE 210
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
22-218 |
1.52e-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: 56.19 E-value: 1.52e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 22 LDRITLDVPAGLTTGLIGPDGVGKSSLLALASGARALQTGGV---DALGGDMRSRRHRERVCRRIAYMPQglgKNLYPTL 98
Cdd:cd03290 17 LSNINIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVhwsNKNESEPSFEATRSRNRYSVAYAAQ---KPWLLNA 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 99 SVEENLqffarLFGHDAGERRRR--IDA--LTQSTGLFPF-----LSRPAGKLSGGMKQKLGLCCALIHDPDLLILDEPT 169
Cdd:cd03290 94 TVEENI-----TFGSPFNKQRYKavTDAcsLQPDIDLLPFgdqteIGERGINLSGGQRQRICVARALYQNTNIVFLDDPF 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 505416896 170 TGVDPLARAQFWD--LIARIRDERPTmsVIVATAYMDEAQRFDWLIAMDAG 218
Cdd:cd03290 169 SALDIHLSDHLMQegILKFLQDDKRT--LVLVTHKLQYLPHADWIIAMKDG 217
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
286-494 |
1.86e-08 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 58.19 E-value: 1.86e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 286 AVDHVSFRIRRGEIF-----------GFL---GSNGCGKSTTMKMLTGLLPATEGTAQLFGKEVDPKDINTRRRVGYMSQ 351
Cdd:PRK10790 342 DIDNVSFAYRDDNLVlqninlsvpsrGFValvGHTGSGKSTLASLLMGYYPLTEGEIRLDGRPLSSLSHSVLRQGVAMVQ 421
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 352 ------AFSLYSELTVRQNLVLHArlfgVPAAEIDARVDEMARRF--GLADIYGMLPDSLPLGMRQRLSLAVAMVHKPEL 423
Cdd:PRK10790 422 qdpvvlADTFLANVTLGRDISEEQ----VWQALETVQLAELARSLpdGLYTPLGEQGNNLSVGQKQLLALARVLVQTPQI 497
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 505416896 424 LILDEPTSGVDPVARDSFWQLMidLARRDLVTIFISTHFMNEAQRCDRISLMHAGRVLASDSPAELVRARG 494
Cdd:PRK10790 498 LILDEATANIDSGTEQAIQQAL--AAVREHTTLVVIAHRLSTIVEADTILVLHRGQAVEQGTHQQLLAAQG 566
|
|
| ABC2_membrane_2 |
pfam12679 |
ABC-2 family transporter protein; This family is related to the ABC-2 membrane transporter ... |
812-989 |
2.23e-08 |
|
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: 56.63 E-value: 2.23e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 812 TALAVVRERELGSILNLYVTPVTRTEFLIGKQVPY--VVLAMLNFLLMTMLARIAF-----DVPVKGSFMTLLLA--VLI 882
Cdd:pfam12679 86 GADAIAGERERGTIELLLSLPVSRSEILLGKFIGRlaIGLILAVALLAGVLLALAItlalgDPLDLGDLLLLVAAsvLLA 165
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 883 FNVVATGIGLLASTFTRSQVAA-------IVMTIIGTMIPTVQFAGLLTPLSSLEGTGRFIGLVYPATYMLSISRGVFnk 955
Cdd:pfam12679 166 LALVFLSIGLLLSSVARSTRTAaaialglFFVLAILWPIVLYGLAELLAGPAPPQELLDFLLFLNPTSPYNTLLSTIL-- 243
|
170 180 190
....*....|....*....|....*....|....*...
gi 505416896 956 ALSLQDLHSQFWPLAAS----APVILGATILLLKKQER 989
Cdd:pfam12679 244 AGSDLSLYGSTATNLLIllawIAVPLALAYVLFKRKDL 281
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
1-173 |
2.30e-08 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 57.26 E-value: 2.30e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 1 MNASSVVRFSDVSLRYGKTVALDRITLDVPAG--LTtgLIGPDGVGKSSLLALASGARALQTGGVDALGGDMRSRRhrer 78
Cdd:PRK09452 9 SSLSPLVELRGISKSFDGKEVISNLDLTINNGefLT--LLGPSGCGKTTVLRLIAGFETPDSGRIMLDGQDITHVP---- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 79 vcrriaymPQGLGKN-------LYPTLSVEENLQFFARLFGHDAGERRRRI-DALtQSTGLFPFLSRPAGKLSGGMKQKL 150
Cdd:PRK09452 83 --------AENRHVNtvfqsyaLFPHMTVFENVAFGLRMQKTPAAEITPRVmEAL-RMVQLEEFAQRKPHQLSGGQQQRV 153
|
170 180
....*....|....*....|...
gi 505416896 151 GLCCALIHDPDLLILDEPTTGVD 173
Cdd:PRK09452 154 AIARAVVNKPKVLLLDESLSALD 176
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
130-232 |
2.38e-08 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 56.25 E-value: 2.38e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 130 GLFPFlsrpagKLSGGMKQKLGLCCALIHDPDLLILDEPTTGVDPLARAQFWDLIARIRDERpTMSVIVATAYMDEAQRF 209
Cdd:PRK10418 135 KLYPF------EMSGGMLQRMMIALALLCEAPFIIADEPTTDLDVVAQARILDLLESIVQKR-ALGMLLVTHDMGVVARL 207
|
90 100
....*....|....*....|....
gi 505416896 210 -DWLIAMDAGRVLATGAPAELLAR 232
Cdd:PRK10418 208 aDDVAVMSHGRIVEQGDVETLFNA 231
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
290-478 |
2.73e-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: 2.73e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 290 VSFRIRRGEIFGFLGSNGCGKSTTMKMLTGLLPATEGTAQLFGkevdpkdintrrRVGYMSQaFSLYSELTVRQNLvlha 369
Cdd:TIGR01271 445 ISFKLEKGQLLAVAGSTGSGKSSLLMMIMGELEPSEGKIKHSG------------RISFSPQ-TSWIMPGTIKDNI---- 507
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 370 rLFGVPAAEIdaRVDEMARRFGLADIYGMLP--DSLPL---------GMRQRLSLAVAMVHKPELLILDEPTSGVDPVAR 438
Cdd:TIGR01271 508 -IFGLSYDEY--RYTSVIKACQLEEDIALFPekDKTVLgeggitlsgGQRARISLARAVYKDADLYLLDSPFTHLDVVTE 584
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 505416896 439 DSFWQ-----LMIDLARrdlvtiFISTHFMNEAQRCDRISLMHAG 478
Cdd:TIGR01271 585 KEIFEsclckLMSNKTR------ILVTSKLEHLKKADKILLLHEG 623
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
2-231 |
3.01e-08 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 55.95 E-value: 3.01e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 2 NASSVVRFSDVSLRYGKTVALDRITLDVPAGLTTGLIGPDGVGKSSLLALASGARAlQTGGVDALGGDMRSRRHRERVCR 81
Cdd:PRK15112 9 NLSKTFRYRTGWFRRQTVEAVKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIE-PTSGELLIDDHPLHFGDYSYRSQ 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 82 RIAYMPQGLGKNLYPTLSVEENLQFFARL-FGHDAGERRRRIDALTQSTGLFP-FLSRPAGKLSGGMKQKLGLCCALIHD 159
Cdd:PRK15112 88 RIRMIFQDPSTSLNPRQRISQILDFPLRLnTDLEPEQREKQIIETLRQVGLLPdHASYYPHMLAPGQKQRLGLARALILR 167
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 505416896 160 PDLLILDEPTTGVDPLARAQFWDLIARIRdERPTMSVIVATAYMDEAQRF-DWLIAMDAGRVLATGAPAELLA 231
Cdd:PRK15112 168 PKVIIADEALASLDMSMRSQLINLMLELQ-EKQGISYIYVTQHLGMMKHIsDQVLVMHQGEVVERGSTADVLA 239
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
21-190 |
3.66e-08 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 56.28 E-value: 3.66e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 21 ALDRITLDVPAGLTTGLIGPDGVGKSSLlalasgARAL-----QTGG------VDALGGDMRSRRHRERVCRRIAYMPQG 89
Cdd:COG4608 33 AVDGVSFDIRRGETLGLVGESGCGKSTL------GRLLlrleePTSGeilfdgQDITGLSGRELRPLRRRMQMVFQDPYA 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 90 lgkNLYPTLSVEENLQFFARLFG-HDAGERRRRIDALTQSTGLFP-FLSRPAGKLSGGMKQKLGLCCALIHDPDLLILDE 167
Cdd:COG4608 107 ---SLNPRMTVGDIIAEPLRIHGlASKAERRERVAELLELVGLRPeHADRYPHEFSGGQRQRIGIARALALNPKLIVCDE 183
|
170 180
....*....|....*....|...
gi 505416896 168 PTTGVDPLARAQFWDLIARIRDE 190
Cdd:COG4608 184 PVSALDVSIQAQVLNLLEDLQDE 206
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
20-220 |
4.06e-08 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 55.48 E-value: 4.06e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 20 VALDRITLDVPAG--LTtgLIGPDGVGKSSLLALASGARALQTGGVdALGGDmrsrrhrervcrRIAYMPQglgknlY-- 95
Cdd:COG1101 20 RALDGLNLTIEEGdfVT--VIGSNGAGKSTLLNAIAGSLPPDSGSI-LIDGK------------DVTKLPE------Ykr 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 96 ----------------PTLSVEENL-------QFFARLFGHDAGERRRRIDALTQ-STGLFPFLSRPAGKLSGGMKQKLG 151
Cdd:COG1101 79 akyigrvfqdpmmgtaPSMTIEENLalayrrgKRRGLRRGLTKKRRELFRELLATlGLGLENRLDTKVGLLSGGQRQALS 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 505416896 152 LCCALIHDPDLLILDEPTTGVDPLARAQFWDLIARIRDER--PTMSVivaTAYMDEAQRF-DWLIAMDAGRV 220
Cdd:COG1101 159 LLMATLTKPKLLLLDEHTAALDPKTAALVLELTEKIVEENnlTTLMV---THNMEQALDYgNRLIMMHEGRI 227
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
283-478 |
4.48e-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: 54.64 E-value: 4.48e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 283 DFTAVDHVSFRIRRGEIFGFLGSNGCGKSTTMKMLTGLLPATEGTAQLFGKEVDPK-----DINTRRRVGYMSQAFSLYS 357
Cdd:cd03290 13 GLATLSNINIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWSNKNESEPsfeatRSRNRYSVAYAAQKPWLLN 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 358 ElTVRQNLVlharlFGVP------AAEIDA---RVDEMARRFGLADIYGMLPDSLPLGMRQRLSLAVAMVHKPELLILDE 428
Cdd:cd03290 93 A-TVEENIT-----FGSPfnkqryKAVTDAcslQPDIDLLPFGDQTEIGERGINLSGGQRQRICVARALYQNTNIVFLDD 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 505416896 429 PTSGVDPVARDSFWQL-MIDLARRDLVTIFISTHFMNEAQRCDRISLMHAG 478
Cdd:cd03290 167 PFSALDIHLSDHLMQEgILKFLQDDKRTLVLVTHKLQYLPHADWIIAMKDG 217
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
287-491 |
5.51e-08 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 55.22 E-value: 5.51e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 287 VDHVSFRIRRGEIFGFLGSNGCGKSTTMKMLTGLLPAT--------EGTAQLFGK---EVDPKDINTRRRVgyMSQAFSL 355
Cdd:PRK13547 17 LRDLSLRIEPGRVTALLGRNGAGKSTLLKALAGDLTGGgaprgarvTGDVTLNGEplaAIDAPRLARLRAV--LPQAAQP 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 356 YSELTVRQNLVL----HARLFGVPAAEIDARVDEMARRFGLADIYGMLPDSLPLGMRQRLSLAVAMVH---------KPE 422
Cdd:PRK13547 95 AFAFSAREIVLLgrypHARRAGALTHRDGEIAWQALALAGATALVGRDVTTLSGGELARVQFARVLAQlwpphdaaqPPR 174
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 423 LLILDEPTSGVDPVARDSFWQLMIDLARRDLVTIFISTHFMNEAQR-CDRISLMHAGRVLASDSPAELVR 491
Cdd:PRK13547 175 YLLLDEPTAALDLAHQHRLLDTVRRLARDWNLGVLAIVHDPNLAARhADRIAMLADGAIVAHGAPADVLT 244
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
11-204 |
7.54e-08 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 53.80 E-value: 7.54e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 11 DVSLRYGKTVALDRITLDVPAGLTTGLIGPDGVGKSSLLALASGARALQTGGVDALGGDMRSRRHrervcrriAYMPQ-- 88
Cdd:PRK13540 6 ELDFDYHDQPLLQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEILFERQSIKKDLC--------TYQKQlc 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 89 --GLGKNLYPTLSVEENLQFFARLFGHDAGerrrrIDALTQSTGLFPFLSRPAGKLSGGMKQKLGLCCALIHDPDLLILD 166
Cdd:PRK13540 78 fvGHRSGINPYLTLRENCLYDIHFSPGAVG-----ITELCRLFSLEHLIDYPCGLLSSGQKRQVALLRLWMSKAKLWLLD 152
|
170 180 190
....*....|....*....|....*....|....*...
gi 505416896 167 EPTTGVDPLAraqFWDLIARIRDERPTMSVIVATAYMD 204
Cdd:PRK13540 153 EPLVALDELS---LLTIITKIQEHRAKGGAVLLTSHQD 187
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
6-235 |
7.71e-08 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 56.27 E-value: 7.71e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 6 VVRFSDVSLRY---GKTVALDRITLDVPAGLTTGLIGPDGVGKSSLLALasgaraLQ-----TGGVDALGGDMRSRRHRE 77
Cdd:TIGR00958 478 LIEFQDVSFSYpnrPDVPVLKGLTFTLHPGEVVALVGPSGSGKSTVAAL------LQnlyqpTGGQVLLDGVPLVQYDHH 551
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 78 RVCRRIAYMPQglgknlYPTL---SVEENLqffarLFGHDAGERRRrIDALTQSTGLFPFLSR----------PAG-KLS 143
Cdd:TIGR00958 552 YLHRQVALVGQ------EPVLfsgSVRENI-----AYGLTDTPDEE-IMAAAKAANAHDFIMEfpngydtevgEKGsQLS 619
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 144 GGMKQKLGLCCALIHDPDLLILDEPTTGVDPLARAQFWDLiarirDERPTMSVIVATAYMDEAQRFDWLIAMDAGRVLAT 223
Cdd:TIGR00958 620 GGQKQRIAIARALVRKPRVLILDEATSALDAECEQLLQES-----RSRASRTVLLIAHRLSTVERADQILVLKKGSVVEM 694
|
250
....*....|..
gi 505416896 224 GAPAELLARTGC 235
Cdd:TIGR00958 695 GTHKQLMEDQGC 706
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
283-494 |
7.88e-08 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 56.26 E-value: 7.88e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 283 DFTAVDHVSFRIRRGEIFGFLGSNGCGKSTTMKMLTGLLPATEGTAQLFGKEVDPKDINT-RRRVGYMSQAFSLYSElTV 361
Cdd:PRK10789 327 DHPALENVNFTLKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGDIRFHDIPLTKLQLDSwRSRLAVVSQTPFLFSD-TV 405
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 362 RQNLVLharlfGVPAAEiDARVDEMARRFGLADIYGMLPDS-----------LPLGMRQRLSLAVAMVHKPELLILDEPT 430
Cdd:PRK10789 406 ANNIAL-----GRPDAT-QQEIEHVARLASVHDDILRLPQGydtevgergvmLSGGQKQRISIARALLLNAEILILDDAL 479
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 505416896 431 SGVDpvARDSFwQLMIDLAR-RDLVTIFISTHFMNEAQRCDRISLMHAGRVLASDSPAELVRARG 494
Cdd:PRK10789 480 SAVD--GRTEH-QILHNLRQwGEGRTVIISAHRLSALTEASEILVMQHGHIAQRGNHDQLAQQSG 541
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
21-232 |
8.35e-08 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 55.36 E-value: 8.35e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 21 ALDRITLDVPAGLTTGLIGPDGVGKSSL---LAL----ASGAraLQTGGVDALGGDmRSRRHRERVCRRIAYmpqglgKN 93
Cdd:PRK11308 30 ALDGVSFTLERGKTLAVVGESGCGKSTLarlLTMietpTGGE--LYYQGQDLLKAD-PEAQKLLRQKIQIVF------QN 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 94 LYPTLS--------VEENLQFFARLfghDAGERRRRIDALTQSTGLFP-FLSRPAGKLSGGMKQKLGLCCALIHDPDLLI 164
Cdd:PRK11308 101 PYGSLNprkkvgqiLEEPLLINTSL---SAAERREKALAMMAKVGLRPeHYDRYPHMFSGGQRQRIAIARALMLDPDVVV 177
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 505416896 165 LDEPTTGVDPLARAQFWDLIARIRDERPT--------MSVIVATAymdeaqrfDWLIAMDAGRVLATGAPAELLAR 232
Cdd:PRK11308 178 ADEPVSALDVSVQAQVLNLMMDLQQELGLsyvfishdLSVVEHIA--------DEVMVMYLGRCVEKGTKEQIFNN 245
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
6-173 |
8.37e-08 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 56.33 E-value: 8.37e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 6 VVRFSDVSLRYGKTVALDRITLDVPAGLTTGLIGPDGVGKSSLLALASGARALQTGGVDALGGdmrsrrhrervcRRIAY 85
Cdd:PRK10636 312 LLKMEKVSAGYGDRIILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELAPVSGEIGLAKG------------IKLGY 379
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 86 MPQGLGKNLYPTlsvEENLQFFARLFGHDAGERRRriDALtqstGLFPF----LSRPAGKLSGGMKQKLGLCCALIHDPD 161
Cdd:PRK10636 380 FAQHQLEFLRAD---ESPLQHLARLAPQELEQKLR--DYL----GGFGFqgdkVTEETRRFSGGEKARLVLALIVWQRPN 450
|
170
....*....|..
gi 505416896 162 LLILDEPTTGVD 173
Cdd:PRK10636 451 LLLLDEPTNHLD 462
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
258-495 |
8.75e-08 |
|
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: 56.49 E-value: 8.75e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 258 KIEPLRADARAGTAIEARGLTMRFGDFT-------AVDHVSFRIRRGEIFGFLGSNGCGKSTTMKMLTGLLPATEGTAQL 330
Cdd:TIGR00957 618 ELEPDSIERRTIKPGEGNSITVHNATFTwardlppTLNGITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVHM 697
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 331 FGKevdpkdintrrrVGYMSQAFSLYSElTVRQNLvlharLFGVPAAEIDARVDEMARRFgLADIYgMLPD--------- 401
Cdd:TIGR00957 698 KGS------------VAYVPQQAWIQND-SLRENI-----LFGKALNEKYYQQVLEACAL-LPDLE-ILPSgdrteigek 757
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 402 --SLPLGMRQRLSLAVAMVHKPELLILDEPTSGVDP-VARDSFWQLMIDLARRDLVTIFISTHFMNEAQRCDRISLMHAG 478
Cdd:TIGR00957 758 gvNLSGGQKQRVSLARAVYSNADIYLFDDPLSAVDAhVGKHIFEHVIGPEGVLKNKTRILVTHGISYLPQVDVIIVMSGG 837
|
250
....*....|....*..
gi 505416896 479 RVLASDSPAELVRARGA 495
Cdd:TIGR00957 838 KISEMGSYQELLQRDGA 854
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
1-215 |
1.06e-07 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 53.56 E-value: 1.06e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 1 MNASSVVRFSDVSLRYGKTVALDRITLDVPAGLTTGLIGPDGVGKSSLLALASGARALQTGGVDALGGDMrSRRHRERVC 80
Cdd:PRK10247 2 QENSPLLQLQNVGYLAGDAKILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFEGEDI-STLKPEIYR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 81 RRIAYMPQGlgknlyPTL---SVEENLqFFARLFGHDAGERRRRIDALTQSTGLFPFLSRPAGKLSGGMKQKLGLCCALI 157
Cdd:PRK10247 81 QQVSYCAQT------PTLfgdTVYDNL-IFPWQIRNQQPDPAIFLDDLERFALPDTILTKNIAELSGGEKQRISLIRNLQ 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 505416896 158 HDPDLLILDEPTTGVDPLARAQFWDLIARIRDERpTMSVIVATAYMDEAQRFDWLIAM 215
Cdd:PRK10247 154 FMPKVLLLDEITSALDESNKHNVNEIIHRYVREQ-NIAVLWVTHDKDEINHADKVITL 210
|
|
| PRK13541 |
PRK13541 |
cytochrome c biogenesis protein CcmA; Provisional |
304-446 |
1.47e-07 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184128 [Multi-domain] Cd Length: 195 Bit Score: 52.95 E-value: 1.47e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 304 GSNGCGKSTTMKMLTGLLPATEGtaqlfgkEVDPKDINTRR----RVGYMSQAFSLYSELTVRQNLVLHARLFGvPAAEI 379
Cdd:PRK13541 33 GANGCGKSSLLRMIAGIMQPSSG-------NIYYKNCNINNiakpYCTYIGHNLGLKLEMTVFENLKFWSEIYN-SAETL 104
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 505416896 380 DARVdemaRRFGLADIYGMLPDSLPLGMRQRLSLAVAMVHKPELLILDEPTSGVDPVARDSFWQLMI 446
Cdd:PRK13541 105 YAAI----HYFKLHDLLDEKCYSLSSGMQKIVAIARLIACQSDLWLLDEVETNLSKENRDLLNNLIV 167
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
23-186 |
1.52e-07 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 52.88 E-value: 1.52e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 23 DRITLDVPAGLTTGLIGPDGVGKSSLLALASGARALQTGGVDALGGDMRSRRhrervcrriaymPQGLGKNLY------- 95
Cdd:PRK13538 18 SGLSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVLWQGEPIRRQR------------DEYHQDLLYlghqpgi 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 96 -PTLSVEENLQFFARLfgHDAGERRRRIDALTQsTGLFPFLSRPAGKLSGGMKQKLGLCCALIHDPDLLILDEPTTGVDP 174
Cdd:PRK13538 86 kTELTALENLRFYQRL--HGPGDDEALWEALAQ-VGLAGFEDVPVRQLSAGQQRRVALARLWLTRAPLWILDEPFTAIDK 162
|
170
....*....|..
gi 505416896 175 LARAQFWDLIAR 186
Cdd:PRK13538 163 QGVARLEALLAQ 174
|
|
| CP_lyasePhnK |
TIGR02323 |
phosphonate C-P lyase system protein PhnK; Members of this family are the PhnK protein of C-P ... |
6-224 |
1.53e-07 |
|
phosphonate C-P lyase system protein PhnK; Members of this family are the PhnK protein of C-P lyase systems for utilization of phosphonates. These systems resemble phosphonatase-based systems in having a three component ABC transporter, where TIGR01097 is the permease, TIGR01098 is the phosphonates binding protein, and TIGR02315 is the ATP-binding cassette (ABC) protein. They differ, however, in having, typically, ten or more additional genes, many of which are believed to form a membrane-associated complex. This protein (PhnK) and the adjacent-encoded PhnL resemble transporter ATP-binding proteins but are suggested, based on mutatgenesis studies, to be part of this complex rather than part of a transporter per se. [Central intermediary metabolism, Phosphorus compounds]
Pssm-ID: 188208 [Multi-domain] Cd Length: 253 Bit Score: 53.68 E-value: 1.53e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 6 VVRFSDVSLRYGKTVALDRITLDVPAGLTTGLIGPDGVGKSSLLALASGARALQTGGVdalGGDMRSRRHRErvcrrIAY 85
Cdd:TIGR02323 3 LLQVSGLSKSYGGGKGCRDVSFDLYPGEVLGIVGESGSGKSTLLGCLAGRLAPDHGTA---TYIMRSGAELE-----LYQ 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 86 MPQGLGKNLYPTL--SVEENLQFFARL---FGHDAGER-----RRRIDALTQSTGlfPFLSR---PAGKL-------SGG 145
Cdd:TIGR02323 75 LSEAERRRLMRTEwgFVHQNPRDGLRMrvsAGANIGERlmaigARHYGNIRATAQ--DWLEEveiDPTRIddlprafSGG 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 146 MKQKLGLCCALIHDPDLLILDEPTTGVDPLARAQFWDLIARIRDERpTMSVIVATAYMDEAQRF-DWLIAMDAGRVLATG 224
Cdd:TIGR02323 153 MQQRLQIARNLVTRPRLVFMDEPTGGLDVSVQARLLDLLRGLVRDL-GLAVIIVTHDLGVARLLaQRLLVMQQGRVVESG 231
|
|
| tagH |
PRK13545 |
teichoic acids export protein ATP-binding subunit; Provisional |
286-480 |
2.76e-07 |
|
teichoic acids export protein ATP-binding subunit; Provisional
Pssm-ID: 184130 [Multi-domain] Cd Length: 549 Bit Score: 54.51 E-value: 2.76e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 286 AVDHVSFRIRRGEIFGFLGSNGCGKSTTMKMLTGLLPATEGTaqlfgkevdpkdINTRRRVGYMSQAFSLYSELTVRQNL 365
Cdd:PRK13545 39 ALNNISFEVPEGEIVGIIGLNGSGKSTLSNLIAGVTMPNKGT------------VDIKGSAALIAISSGLNGQLTGIENI 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 366 VLHARLFGVPAAEIDARVDEMARrfgLADIYGMLPDSLPL---GMRQRLSLAVAMVHKPELLILDEPTSGVDPVARDSFW 442
Cdd:PRK13545 107 ELKGLMMGLTKEKIKEIIPEIIE---FADIGKFIYQPVKTyssGMKSRLGFAISVHINPDILVIDEALSVGDQTFTKKCL 183
|
170 180 190
....*....|....*....|....*....|....*....
gi 505416896 443 QLMIDLARRDlVTIFISTHFMNEAQR-CDRISLMHAGRV 480
Cdd:PRK13545 184 DKMNEFKEQG-KTIFFISHSLSQVKSfCTKALWLHYGQV 221
|
|
| PRK13546 |
PRK13546 |
teichoic acids export ABC transporter ATP-binding subunit TagH; |
21-167 |
2.97e-07 |
|
teichoic acids export ABC transporter ATP-binding subunit TagH;
Pssm-ID: 184131 [Multi-domain] Cd Length: 264 Bit Score: 52.90 E-value: 2.97e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 21 ALDRITLDVPAGLTTGLIGPDGVGKSSLLALASGARALQTGGVDALGgdmrsrrhrerVCRRIAyMPQGLGKNLyptlSV 100
Cdd:PRK13546 39 ALDDISLKAYEGDVIGLVGINGSGKSTLSNIIGGSLSPTVGKVDRNG-----------EVSVIA-ISAGLSGQL----TG 102
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 505416896 101 EENLQFFARLFGHdageRRRRIDALT----QSTGLFPFLSRPAGKLSGGMKQKLGLCCALIHDPDLLILDE 167
Cdd:PRK13546 103 IENIEFKMLCMGF----KRKEIKAMTpkiiEFSELGEFIYQPVKKYSSGMRAKLGFSINITVNPDILVIDE 169
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
287-499 |
3.98e-07 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 53.64 E-value: 3.98e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 287 VDHVSFRIRRGEIFGFLGSNGCGKsttmkmltgllpaTE---------------GTAQLFGKEVDpkdINTRRR-----V 346
Cdd:NF040905 276 VDDVSLNVRRGEIVGIAGLMGAGR-------------TElamsvfgrsygrnisGTVFKDGKEVD---VSTVSDaidagL 339
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 347 GYMSQ---AFSLYSELTVRQNLVLhARLFGVPAAEIdarVDEmARRFGLADIY-----------GMLPDSLPLGMRQRLS 412
Cdd:NF040905 340 AYVTEdrkGYGLNLIDDIKRNITL-ANLGKVSRRGV---IDE-NEEIKVAEEYrkkmniktpsvFQKVGNLSGGNQQKVV 414
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 413 LAVAMVHKPELLILDEPTSGVDPVARDSFWQLMIDLARRDLVTIFISTHfMNEA-QRCDRISLMHAGRVLasdspAELVR 491
Cdd:NF040905 415 LSKWLFTDPDVLILDEPTRGIDVGAKYEIYTIINELAAEGKGVIVISSE-LPELlGMCDRIYVMNEGRIT-----GELPR 488
|
....*...
gi 505416896 492 ARgaATLE 499
Cdd:NF040905 489 EE--ASQE 494
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
6-173 |
4.31e-07 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 51.80 E-value: 4.31e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 6 VVRFSDVSLRY-GKTVALDRITLDVPAGLTTGLIGPDGVGKSSLLALASGARALQTGGVDALGGDMrsrrhRERVCRRIA 84
Cdd:PRK10908 1 MIRFEHVSKAYlGGRQALQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDI-----TRLKNREVP 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 85 YMPQGLG-----KNLYPTLSVEENLQFFARLFGHDAGERRRRIDALTQSTGLFPFLSRPAGKLSGGMKQKLGLCCALIHD 159
Cdd:PRK10908 76 FLRRQIGmifqdHHLLMDRTVYDNVAIPLIIAGASGDDIRRRVSAALDKVGLLDKAKNFPIQLSGGEQQRVGIARAVVNK 155
|
170
....*....|....
gi 505416896 160 PDLLILDEPTTGVD 173
Cdd:PRK10908 156 PAVLLADEPTGNLD 169
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
17-224 |
4.46e-07 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 53.19 E-value: 4.46e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 17 GKTVALDRITLDVPAGLTTGLIGPDGVGKS----SLLAL-ASGARalqTGGVDALGG----DMRSRRHRERVCRRIAYMP 87
Cdd:PRK09473 27 GDVTAVNDLNFSLRAGETLGIVGESGSGKSqtafALMGLlAANGR---IGGSATFNGreilNLPEKELNKLRAEQISMIF 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 88 QGLGKNLYPTLSVEENL----QFFARLFGHDAGERR-RRIDALT-----QSTGLFPFlsrpagKLSGGMKQKLGLCCALI 157
Cdd:PRK09473 104 QDPMTSLNPYMRVGEQLmevlMLHKGMSKAEAFEESvRMLDAVKmpearKRMKMYPH------EFSGGMRQRVMIAMALL 177
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 505416896 158 HDPDLLILDEPTTGVDPLARAQFWDLIARIRDERPTmSVIVATAYMD-EAQRFDWLIAMDAGRVLATG 224
Cdd:PRK09473 178 CRPKLLIADEPTTALDVTVQAQIMTLLNELKREFNT-AIIMITHDLGvVAGICDKVLVMYAGRTMEYG 244
|
|
| tagH |
PRK13545 |
teichoic acids export protein ATP-binding subunit; Provisional |
21-167 |
4.62e-07 |
|
teichoic acids export protein ATP-binding subunit; Provisional
Pssm-ID: 184130 [Multi-domain] Cd Length: 549 Bit Score: 53.74 E-value: 4.62e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 21 ALDRITLDVPAGLTTGLIGPDGVGKSSLLALASGARALQTGGVDALGGdmrsrrhrervCRRIAympqgLGKNLYPTLSV 100
Cdd:PRK13545 39 ALNNISFEVPEGEIVGIIGLNGSGKSTLSNLIAGVTMPNKGTVDIKGS-----------AALIA-----ISSGLNGQLTG 102
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 505416896 101 EENLQFFARLFGHDAGERRRRIDALTQSTGLFPFLSRPAGKLSGGMKQKLGLCCALIHDPDLLILDE 167
Cdd:PRK13545 103 IENIELKGLMMGLTKEKIKEIIPEIIEFADIGKFIYQPVKTYSSGMKSRLGFAISVHINPDILVIDE 169
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
20-194 |
4.72e-07 |
|
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: 51.67 E-value: 4.72e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 20 VALDRITLDVPAGLTTGLIGPDGVGKSSLLA------LASGARAL---QTGGVDALGGDMRsrRHRERVCRRIAYMPQGL 90
Cdd:COG4778 25 PVLDGVSFSVAAGECVALTGPSGAGKSTLLKciygnyLPDSGSILvrhDGGWVDLAQASPR--EILALRRRTIGYVSQFL 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 91 gkNLYPTLS----VEENLqffaRLFGHDAGERRRRIDALtqstglfpfLSR----------PAGKLSGGMKQKLGLCCAL 156
Cdd:COG4778 103 --RVIPRVSaldvVAEPL----LERGVDREEARARAREL---------LARlnlperlwdlPPATFSGGEQQRVNIARGF 167
|
170 180 190
....*....|....*....|....*....|....*...
gi 505416896 157 IHDPDLLILDEPTTGVDPLARAQFWDLIARIRDERPTM 194
Cdd:COG4778 168 IADPPLLLLDEPTASLDAANRAVVVELIEEAKARGTAI 205
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
290-478 |
4.80e-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: 52.55 E-value: 4.80e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 290 VSFRIRRGEIFGFLGSNGCGKSTTMKMLTGLLPATEGTAQLFGkevdpkdintrrRVGYMSQaFSLYSELTVRQNLVlha 369
Cdd:cd03291 56 INLKIEKGEMLAITGSTGSGKTSLLMLILGELEPSEGKIKHSG------------RISFSSQ-FSWIMPGTIKENII--- 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 370 rlFGVPAAE------IDA-RVDEMARRFGLADIYGMLPDSLPL--GMRQRLSLAVAMVHKPELLILDEPTSGVDPVARDS 440
Cdd:cd03291 120 --FGVSYDEyryksvVKAcQLEEDITKFPEKDNTVLGEGGITLsgGQRARISLARAVYKDADLYLLDSPFGYLDVFTEKE 197
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 505416896 441 FWQ-----LMIDLARrdlvtiFISTHFMNEAQRCDRISLMHAG 478
Cdd:cd03291 198 IFEscvckLMANKTR------ILVTSKMEHLKKADKILILHEG 234
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
301-430 |
6.28e-07 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 53.20 E-value: 6.28e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 301 GFLGSNGCGKSTTMKMLTGLLPATEGTAQLfgkevdPKDIntrrRVGYMSQAFSLYSELTVRQN--------LVLHARL- 371
Cdd:PRK11819 37 GVLGLNGAGKSTLLRIMAGVDKEFEGEARP------APGI----KVGYLPQEPQLDPEKTVRENveegvaevKAALDRFn 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 372 -----FGVPAAEIDARVDEMARrfgLADIY--------------GM----LPD------SLPLGMRQRLSLAVAMVHKPE 422
Cdd:PRK11819 107 eiyaaYAEPDADFDALAAEQGE---LQEIIdaadawdldsqleiAMdalrCPPwdakvtKLSGGERRRVALCRLLLEKPD 183
|
....*...
gi 505416896 423 LLILDEPT 430
Cdd:PRK11819 184 MLLLDEPT 191
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
7-234 |
6.29e-07 |
|
multi drug resistance-associated protein (MRP); This model describes multi drug resistance-associated protein (MRP) in eukaryotes. The multidrug resistance-associated protein is an integral membrane protein that causes multidrug resistance when overexpressed in mammalian cells. It belongs to ABC transporter superfamily. The protein topology and function was experimentally demonstrated by epitope tagging and immunofluorescence. Insertion of tags in the critical regions associated with drug efflux, abrogated its function. The C-terminal domain seem to highly conserved. [Transport and binding proteins, Other]
Pssm-ID: 188098 [Multi-domain] Cd Length: 1522 Bit Score: 53.80 E-value: 6.29e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 7 VRFSDVSLRY--GKTVALDRITLDVPAGLTTGLIGPDGVGKSSL-LAL------ASGARALQTGGVDALG-GDMRSRrhr 76
Cdd:TIGR00957 1285 VEFRNYCLRYreDLDLVLRHINVTIHGGEKVGIVGRTGAGKSSLtLGLfrinesAEGEIIIDGLNIAKIGlHDLRFK--- 1361
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 77 ervcrrIAYMPQ-------GLGKNLYPTLSVEENLQFFARLFGHDAGERRRRIDALTQSTglfpflSRPAGKLSGGMKQK 149
Cdd:TIGR00957 1362 ------ITIIPQdpvlfsgSLRMNLDPFSQYSDEEVWWALELAHLKTFVSALPDKLDHEC------AEGGENLSVGQRQL 1429
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 150 LGLCCALIHDPDLLILDEPTTGVDplarAQFWDLI-ARIRDERPTMSVIVATAYMDEAQRFDWLIAMDAGRVLATGAPAE 228
Cdd:TIGR00957 1430 VCLARALLRKTKILVLDEATAAVD----LETDNLIqSTIRTQFEDCTVLTIAHRLNTIMDYTRVIVLDKGEVAEFGAPSN 1505
|
....*.
gi 505416896 229 LLARTG 234
Cdd:TIGR00957 1506 LLQQRG 1511
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
7-226 |
6.31e-07 |
|
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: 51.26 E-value: 6.31e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 7 VRFSDVSLRYGKTV--ALDRITLDVPAGLTTGLIGPDGVGKSSL-LALASGARAlQTGGVDALGGDMrSRRHRERVCRRI 83
Cdd:cd03369 7 IEVENLSVRYAPDLppVLKNVSFKVKAGEKIGIVGRTGAGKSTLiLALFRFLEA-EEGKIEIDGIDI-STIPLEDLRSSL 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 84 AYMPQGlgknlyPTL---SVEENLQFF-----ARLFGhdagerrrridALTQSTGlfpflsrpAGKLSGGMKQKLGLCCA 155
Cdd:cd03369 85 TIIPQD------PTLfsgTIRSNLDPFdeysdEEIYG-----------ALRVSEG--------GLNLSQGQRQLLCLARA 139
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 505416896 156 LIHDPDLLILDEPTTGVDPLARAqfwdLIAR-IRDERPTMSVIVATAYMDEAQRFDWLIAMDAGRVLATGAP 226
Cdd:cd03369 140 LLKRPRVLVLDEATASIDYATDA----LIQKtIREEFTNSTILTIAHRLRTIIDYDKILVMDAGEVKEYDHP 207
|
|
| ABC_UvrA_II |
cd03271 |
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair ... |
91-226 |
7.20e-07 |
|
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: 51.85 E-value: 7.20e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 91 GKNLYPTL--SVEENLQFFArlfghDAGERRRRIDALtQSTGL-FPFLSRPAGKLSGGMKQKLGLCCALiHDPD----LL 163
Cdd:cd03271 122 GKSIADVLdmTVEEALEFFE-----NIPKIARKLQTL-CDVGLgYIKLGQPATTLSGGEAQRIKLAKEL-SKRStgktLY 194
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 505416896 164 ILDEPTTGVDPLARAQFWDLIARIRDERPTmsVIVATAYMDEAQRFDWLIAM------DAGRVLATGAP 226
Cdd:cd03271 195 ILDEPTTGLHFHDVKKLLEVLQRLVDKGNT--VVVIEHNLDVIKCADWIIDLgpeggdGGGQVVASGTP 261
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
19-249 |
1.22e-06 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 52.54 E-value: 1.22e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 19 TVALDRITLDVPAGLTTGLIGPDGVGKSSLLALASGARALQtGGVDALGGDMRSRRHRERVCRrIAYmpqgLGKNlyPTL 98
Cdd:PRK11174 363 KTLAGPLNFTLPAGQRIALVGPSGAGKTSLLNALLGFLPYQ-GSLKINGIELRELDPESWRKH-LSW----VGQN--PQL 434
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 99 ---SVEENLqffaRLFGHDAGERRrrIDALTQSTGLFPFLSRP-----------AGKLSGGMKQKLGLCCALIHDPDLLI 164
Cdd:PRK11174 435 phgTLRDNV----LLGNPDASDEQ--LQQALENAWVSEFLPLLpqgldtpigdqAAGLSVGQAQRLALARALLQPCQLLL 508
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 165 LDEPTTGVDPLARAQFWDLIARIRDERPTMSVivaTAYMDEAQRFDWLIAMDAGRVLATGAPAELLARTGcdsleaAFIA 244
Cdd:PRK11174 509 LDEPTASLDAHSEQLVMQALNAASRRQTTLMV---THQLEDLAQWDQIWVMQDGQIVQQGDYAELSQAGG------LFAT 579
|
....*
gi 505416896 245 LLPEN 249
Cdd:PRK11174 580 LLAHR 584
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
25-230 |
1.25e-06 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 50.70 E-value: 1.25e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 25 ITLDVPAGLTTGLIGPDGVGKSSLLALASGARAlQTGGVDALGGDMRSRRHRERVCRRiAYMPQglGKNLYPTLSVEENL 104
Cdd:PRK03695 15 LSAEVRAGEILHLVGPNGAGKSTLLARMAGLLP-GSGSIQFAGQPLEAWSAAELARHR-AYLSQ--QQTPPFAMPVFQYL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 105 QffarLFGHD---AGERRRRIDALTQSTGLFPFLSRPAGKLSGGMKQKLGLCCALIH-DPD------LLILDEPTTGVDP 174
Cdd:PRK03695 91 T----LHQPDktrTEAVASALNEVAEALGLDDKLGRSVNQLSGGEWQRVRLAAVVLQvWPDinpagqLLLLDEPMNSLDV 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 175 LARAQFWDLIARIrdERPTMSVIVAT----AYMDEAQRFdWLIAmdAGRVLATGAPAELL 230
Cdd:PRK03695 167 AQQAALDRLLSEL--CQQGIAVVMSShdlnHTLRHADRV-WLLK--QGKLLASGRRDEVL 221
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
11-230 |
1.28e-06 |
|
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of iron-sulfur clusters (Fe-S) depends on multi-protein systems. The SUF system of E. coli and Erwinia chrysanthemi is important for Fe-S biogenesis under stressful conditions. The SUF system is made of six proteins: SufC is an atypical cytoplasmic ABC-ATPase, which forms a complex with SufB and SufD; SufA plays the role of a scaffold protein for assembly of iron-sulfur clusters and delivery to target proteins; SufS is a cysteine desulfurase which mobilizes the sulfur atom from cysteine and provides it to the cluster; SufE has no associated function yet.
Pssm-ID: 213184 [Multi-domain] Cd Length: 200 Bit Score: 50.22 E-value: 1.28e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 11 DVSLRYGKTVALDRITLDVPAGLTTGLIGPDGVGKSSLL-ALASGARALQTGGVDALGGDmrsrrhrervcrRIAYMPqg 89
Cdd:cd03217 5 DLHVSVGGKEILKGVNLTIKKGEVHALMGPNGSGKSTLAkTIMGHPKYEVTEGEILFKGE------------DITDLP-- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 90 lgknlyptlsVEENlqffARLFGHDAGERRRRIDALTQSTglfpFLsRPAGK-LSGGMKQKLGLCCALIHDPDLLILDEP 168
Cdd:cd03217 71 ----------PEER----ARLGIFLAFQYPPEIPGVKNAD----FL-RYVNEgFSGGEKKRNEILQLLLLEPDLAILDEP 131
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 505416896 169 TTGVDPLARAQFWDLIARIRDerPTMSVIVATAYmdeaQR-FDWLIA-----MDAGRVLATGaPAELL 230
Cdd:cd03217 132 DSGLDIDALRLVAEVINKLRE--EGKSVLIITHY----QRlLDYIKPdrvhvLYDGRIVKSG-DKELA 192
|
|
| ABCC_SUR2 |
cd03288 |
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The ... |
289-490 |
1.66e-06 |
|
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: 50.68 E-value: 1.66e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 289 HVSFRIRRGEIFGFLGSNGCGKSTTMKMLTGLLPATEGTAQLFGKEVDPKDINT-RRRVGYMSQAFSLYSElTVRQNL-- 365
Cdd:cd03288 39 HVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVIDGIDISKLPLHTlRSRLSIILQDPILFSG-SIRFNLdp 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 366 ---VLHARLFgvPAAEIdARVDEMARRF--GLADIYGMLPDSLPLGMRQRLSLAVAMVHKPELLILDEPTSGVDpVARDS 440
Cdd:cd03288 118 eckCTDDRLW--EALEI-AQLKNMVKSLpgGLDAVVTEGGENFSVGQRQLFCLARAFVRKSSILIMDEATASID-MATEN 193
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 505416896 441 FWQ--LMIDLARRDLVTIfisTHFMNEAQRCDRISLMHAGRVLASDSPAELV 490
Cdd:cd03288 194 ILQkvVMTAFADRTVVTI---AHRVSTILDADLVLVLSRGILVECDTPENLL 242
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
22-229 |
2.10e-06 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 51.90 E-value: 2.10e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 22 LDRITLDVPAGLTTGLIGPDGVGKSSLLALASGARA-LQTGGVDALGgdmrsrrhrervcrRIAYMPQglgKNLYPTLSV 100
Cdd:PLN03232 633 LSDINLEIPVGSLVAIVGGTGEGKTSLISAMLGELShAETSSVVIRG--------------SVAYVPQ---VSWIFNATV 695
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 101 EENLqffarLFGHDAGERR--RRID--ALTQSTGLFPFLSRP-----AGKLSGGMKQKLGLCCALIHDPDLLILDEPTTG 171
Cdd:PLN03232 696 RENI-----LFGSDFESERywRAIDvtALQHDLDLLPGRDLTeigerGVNISGGQKQRVSMARAVYSNSDIYIFDDPLSA 770
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 505416896 172 VDPLARAQFWDliARIRDERPTMSVIVATAYMDEAQRFDWLIAMDAGRVLATGAPAEL 229
Cdd:PLN03232 771 LDAHVAHQVFD--SCMKDELKGKTRVLVTNQLHFLPLMDRIILVSEGMIKEEGTFAEL 826
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
295-437 |
2.35e-06 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 51.77 E-value: 2.35e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 295 RRGEIFGFLGSNGCGKSTTMKMLTGLLPA--TEGTAQLFGKevdPKDINTRRRV-GYMSQAFSLYSELTVRQNLVLHARL 371
Cdd:PLN03140 904 RPGVLTALMGVSGAGKTTLMDVLAGRKTGgyIEGDIRISGF---PKKQETFARIsGYCEQNDIHSPQVTVRESLIYSAFL 980
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 505416896 372 ---FGVPAAEIDARVDEMARRFGLAD----IYGmLP--DSLPLGMRQRLSLAVAMVHKPELLILDEPTSGVDPVA 437
Cdd:PLN03140 981 rlpKEVSKEEKMMFVDEVMELVELDNlkdaIVG-LPgvTGLSTEQRKRLTIAVELVANPSIIFMDEPTSGLDARA 1054
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
6-173 |
2.36e-06 |
|
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of the ABC transporter ATP-binding cassette, but are found outside the common ABC transporter operon structure that features integral membrane permease proteins and substrate-binding proteins encoded next to the ATP-binding cassette (ABC domain) protein. The member protein ChvD from Agrobacterium tumefaciens was identified as both a candidate to interact with VirB8, based on yeast two-hybrid analysis, and as an apparent regulator of VirG. The general function of this protein family is unknown.
Pssm-ID: 274744 [Multi-domain] Cd Length: 552 Bit Score: 51.47 E-value: 2.36e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 6 VVRFSDVSLRYGKTVALDRITLDVPAGLTTGLIGPDGVGKSSLLALASGARALQTGGVdALGGDMRsrrhrervcrrIAY 85
Cdd:TIGR03719 322 VIEAENLTKAFGDKLLIDDLSFKLPPGGIVGVIGPNGAGKSTLFRMITGQEQPDSGTI-EIGETVK-----------LAY 389
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 86 MPQGLgKNLYPTLSVEENL---QFFARLFGHDAGERrrridaltQSTGLFPFL----SRPAGKLSGGMKQKLGLCCALIH 158
Cdd:TIGR03719 390 VDQSR-DALDPNKTVWEEIsggLDIIKLGKREIPSR--------AYVGRFNFKgsdqQKKVGQLSGGERNRVHLAKTLKS 460
|
170
....*....|....*
gi 505416896 159 DPDLLILDEPTTGVD 173
Cdd:TIGR03719 461 GGNVLLLDEPTNDLD 475
|
|
| 3a01203 |
TIGR00954 |
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ... |
287-461 |
2.58e-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: 2.58e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 287 VDHVSFRIRRGEIFGFLGSNGCGKSTTMKMLTGLLPATEGTaqlfgkevdpKDINTRRRVGYMSQAfSLYSELTVRQNLV 366
Cdd:TIGR00954 468 IESLSFEVPSGNNLLICGPNGCGKSSLFRILGELWPVYGGR----------LTKPAKGKLFYVPQR-PYMTLGTLRDQII 536
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 367 LHARLF-----GVPAAEIDARVDE-----MARRFGLADIYGMLPDSLPLGMRQRLSLAVAMVHKPELLILDEPTSGVDPV 436
Cdd:TIGR00954 537 YPDSSEdmkrrGLSDKDLEQILDNvqlthILEREGGWSAVQDWMDVLSGGEKQRIAMARLFYHKPQFAILDECTSAVSVD 616
|
170 180
....*....|....*....|....*
gi 505416896 437 ARDSfwqlMIDLARRDLVTIFISTH 461
Cdd:TIGR00954 617 VEGY----MYRLCREFGITLFSVSH 637
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
135-224 |
2.86e-06 |
|
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins, and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213205 [Multi-domain] Cd Length: 176 Bit Score: 48.47 E-value: 2.86e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 135 LSRPAGKLSGGMKQKLGLCCALIHDPD--LLILDEPTTGVDPLARAQFWDLIARIRDERPTMSVIVATAYMdeAQRFDWL 212
Cdd:cd03238 81 LGQKLSTLSGGELQRVKLASELFSEPPgtLFILDEPSTGLHQQDINQLLEVIKGLIDLGNTVILIEHNLDV--LSSADWI 158
|
90
....*....|....*...
gi 505416896 213 IAM------DAGRVLATG 224
Cdd:cd03238 159 IDFgpgsgkSGGKVVFSG 176
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
3-234 |
3.98e-06 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 51.28 E-value: 3.98e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 3 ASSVVRFSDVSLRYGKTV--ALDRITLDVPAGLTTGLIGPDGVGKSSLLALASGARALQTGGVDALGGDMRSRRHRERVC 80
Cdd:PLN03130 1234 SSGSIKFEDVVLRYRPELppVLHGLSFEISPSEKVGIVGRTGAGKSSMLNALFRIVELERGRILIDGCDISKFGLMDLRK 1313
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 81 RrIAYMPQGlgknlyPTL---SVEENLQFF-----ARLFghDAGERRRRIDALTQ-STGLFPFLSRPAGKLSGGMKQKLG 151
Cdd:PLN03130 1314 V-LGIIPQA------PVLfsgTVRFNLDPFnehndADLW--ESLERAHLKDVIRRnSLGLDAEVSEAGENFSVGQRQLLS 1384
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 152 LCCALIHDPDLLILDEPTTGVDPLARAqfwdLIAR-IRDE--RPTMSVIvataymdeAQRF------DWLIAMDAGRVLA 222
Cdd:PLN03130 1385 LARALLRRSKILVLDEATAAVDVRTDA----LIQKtIREEfkSCTMLII--------AHRLntiidcDRILVLDAGRVVE 1452
|
250
....*....|..
gi 505416896 223 TGAPAELLARTG 234
Cdd:PLN03130 1453 FDTPENLLSNEG 1464
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
17-222 |
4.13e-06 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 50.88 E-value: 4.13e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 17 GKTVALDRITLDVPAGLTTGLIGPDGVGKSSLLAL-------ASGARALQTGGVDALGGDmrsrRHRERVCRRIAYMPQG 89
Cdd:PRK10535 19 EQVEVLKGISLDIYAGEMVAIVGASGSGKSTLMNIlgcldkpTSGTYRVAGQDVATLDAD----ALAQLRREHFGFIFQR 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 90 LgkNLYPTLSVEENLQFFARLFGHDAGERRRRIDALTQSTGLFPFLSRPAGKLSGGMKQKLGLCCALIHDPDLLILDEPT 169
Cdd:PRK10535 95 Y--HLLSHLTAAQNVEVPAVYAGLERKQRLLRAQELLQRLGLEDRVEYQPSQLSGGQQQRVSIARALMNGGQVILADEPT 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 505416896 170 TGVDPLARAQFWDLIARIRDERPTmsVIVATAYMDEAQRFDWLIAMDAGRVLA 222
Cdd:PRK10535 173 GALDSHSGEEVMAILHQLRDRGHT--VIIVTHDPQVAAQAERVIEIRDGEIVR 223
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
85-229 |
4.33e-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: 50.78 E-value: 4.33e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 85 YMPQGL-----GKNLYPTL--SVEENLQFFArlfghDAGERRRRIDALTqSTGL-FPFLSRPAGKLSGGMKQKLGLCCAL 156
Cdd:TIGR00630 771 YNRETLevkykGKNIADVLdmTVEEAYEFFE-----AVPSISRKLQTLC-DVGLgYIRLGQPATTLSGGEAQRIKLAKEL 844
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 157 IHD---PDLLILDEPTTGVDPLARAQFWDLIARIRDERPTMSVIVATayMDEAQRFDWLI------AMDAGRVLATGAPA 227
Cdd:TIGR00630 845 SKRstgRTLYILDEPTTGLHFDDIKKLLEVLQRLVDKGNTVVVIEHN--LDVIKTADYIIdlgpegGDGGGTVVASGTPE 922
|
..
gi 505416896 228 EL 229
Cdd:TIGR00630 923 EV 924
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
141-215 |
5.70e-06 |
|
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems involved in cellular processes other than transport. These families are characterized by the fact that the ABC subunit is made up of duplicated, fused ABC modules (ABC2). No known transmembrane proteins or domains are associated with these proteins.
Pssm-ID: 213194 [Multi-domain] Cd Length: 162 Bit Score: 47.35 E-value: 5.70e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 505416896 141 KLSGGMKQKLGLCCALIH----DPDLLILDEPTTGVDPLARAQFWDLIARIRDERPTmsVIVATAYMDEAQRFDWLIAM 215
Cdd:cd03227 77 QLSGGEKELSALALILALaslkPRPLYILDEIDRGLDPRDGQALAEAILEHLVKGAQ--VIVITHLPELAELADKLIHI 153
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
7-234 |
5.95e-06 |
|
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 444078 [Multi-domain] Cd Length: 605 Bit Score: 50.20 E-value: 5.95e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 7 VRFSDVSLRY-GKTVALDRITLDVPAGLTTGLIGPDGVGKSSLLALASGARALQTGGVDALGGDMRSRRHRERVCRrIAY 85
Cdd:COG5265 358 VRFENVSFGYdPERPILKGVSFEVPAGKTVAIVGPSGAGKSTLARLLFRFYDVTSGRILIDGQDIRDVTQASLRAA-IGI 436
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 86 MPQGlgknlypTL----SVEENLQFfARLfghDAGE-------RRRRIDALTQSTglfpflsrPAG----------KLSG 144
Cdd:COG5265 437 VPQD-------TVlfndTIAYNIAY-GRP---DASEeeveaaaRAAQIHDFIESL--------PDGydtrvgerglKLSG 497
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 145 GMKQKLGLCCALIHDPDLLILDEPTTGVDPLARAQFWDLIARIRDERPTM------SVIVataymdEAqrfDWLIAMDAG 218
Cdd:COG5265 498 GEKQRVAIARTLLKNPPILIFDEATSALDSRTERAIQAALREVARGRTTLviahrlSTIV------DA---DEILVLEAG 568
|
250
....*....|....*.
gi 505416896 219 RVLATGAPAELLARTG 234
Cdd:COG5265 569 RIVERGTHAELLAQGG 584
|
|
| SapD |
COG4170 |
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms]; |
17-186 |
6.09e-06 |
|
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms];
Pssm-ID: 443330 [Multi-domain] Cd Length: 331 Bit Score: 49.52 E-value: 6.09e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 17 GKTVALDRITLDVPAGLTTGLIGPDGVGKSsLLALA----------SGARALQTGGVDALggDMRSRRHRERVCRRIAYM 86
Cdd:COG4170 18 GRVKAVDRVSLTLNEGEIRGLVGESGSGKS-LIAKAicgitkdnwhVTADRFRWNGIDLL--KLSPRERRKIIGREIAMI 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 87 PQGLGKNLYPTLSVEENLQ------FFARLFGHDAGERRRRIDALTQSTGL---------FPFlsrpagKLSGGMKQKLG 151
Cdd:COG4170 95 FQEPSSCLDPSAKIGDQLIeaipswTFKGKWWQRFKWRKKRAIELLHRVGIkdhkdimnsYPH------ELTEGECQKVM 168
|
170 180 190
....*....|....*....|....*....|....*
gi 505416896 152 LCCALIHDPDLLILDEPTTGVDPLARAQFWDLIAR 186
Cdd:COG4170 169 IAMAIANQPRLLIADEPTNAMESTTQAQIFRLLAR 203
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
257-493 |
7.58e-06 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 50.16 E-value: 7.58e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 257 VKIEPLRADARAGTAIEA-----RGLTMRF--GDFTAVDHVSFRIRRGEIFGFLGSNGCGKSTTMKMLTGLLPATEGTAQ 329
Cdd:PTZ00243 1289 VVIEPASPTSAAPHPVQAgslvfEGVQMRYreGLPLVLRGVSFRIAPREKVGIVGRTGSGKSTLLLTFMRMVEVCGGEIR 1368
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 330 LFGKEVDPKDINTRRRVGYMSQAFSLYSELTVRQNL--VLHA---------RLFGVP---AAE---IDARVDEMARRFGl 392
Cdd:PTZ00243 1369 VNGREIGAYGLRELRRQFSMIPQDPVLFDGTVRQNVdpFLEAssaevwaalELVGLRervASEsegIDSRVLEGGSNYS- 1447
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 393 adiygmlpdslpLGMRQRLSLAVAMVHKPELLIL-DEPTSGVDPvARDSFWQ--LMIDLARRDLVTIfisTHFMNEAQRC 469
Cdd:PTZ00243 1448 ------------VGQRQLMCMARALLKKGSGFILmDEATANIDP-ALDRQIQatVMSAFSAYTVITI---AHRLHTVAQY 1511
|
250 260
....*....|....*....|....
gi 505416896 470 DRISLMHAGRVLASDSPAELVRAR 493
Cdd:PTZ00243 1512 DKIIVMDHGAVAEMGSPRELVMNR 1535
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
2-197 |
7.81e-06 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 49.81 E-value: 7.81e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 2 NASSVVRFSDVSLR--YGKTVaLDRITLDVPAGLTTGLIGPDGVGKSSLL-ALA-------------SGARAL---QTgg 62
Cdd:COG4178 358 SEDGALALEDLTLRtpDGRPL-LEDLSLSLKPGERLLITGPSGSGKSTLLrAIAglwpygsgriarpAGARVLflpQR-- 434
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 63 vdalggdmrsrrhrervcrriAYMPQG-----LgknLYPtlsveenlqffarlFGHDAGERRRRIDALTQsTGLFPFLSR 137
Cdd:COG4178 435 ---------------------PYLPLGtlreaL---LYP--------------ATAEAFSDAELREALEA-VGLGHLAER 475
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 505416896 138 P------AGKLSGGMKQKLGLCCALIHDPDLLILDEPTTGVDPLARAQfwdLIARIRDERPTMSVI 197
Cdd:COG4178 476 LdeeadwDQVLSLGEQQRLAFARLLLHKPDWLFLDEATSALDEENEAA---LYQLLREELPGTTVI 538
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
133-173 |
1.12e-05 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 49.02 E-value: 1.12e-05
10 20 30 40
....*....|....*....|....*....|....*....|.
gi 505416896 133 PFLSRPAGKLSGGMKQKLGLCCALIHDPDLLILDEPTTGVD 173
Cdd:NF040905 396 PSVFQKVGNLSGGNQQKVVLSKWLFTDPDVLILDEPTRGID 436
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
7-234 |
1.23e-05 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 49.25 E-value: 1.23e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 7 VRFSDVSLRY-GK-TVALDRITLDVPAGLTTGLIGPDGVGKSSLLALASGARALQTGGVDALGGDMRSRRHrervcrria 84
Cdd:PRK11176 342 IEFRNVTFTYpGKeVPALRNINFKIPAGKTVALVGRSGSGKSTIANLLTRFYDIDEGEILLDGHDLRDYTL--------- 412
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 85 ympqglgKNLYPTLS-VEENLQFF----ARLFGHDAGER--RRRIDALTQSTGLFPFLSR-PAG----------KLSGGM 146
Cdd:PRK11176 413 -------ASLRNQVAlVSQNVHLFndtiANNIAYARTEQysREQIEEAARMAYAMDFINKmDNGldtvigengvLLSGGQ 485
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 147 KQKLGLCCALIHDPDLLILDEPTTGVDPLARAQFWDLIARIRDERptmSVIVATAYMDEAQRFDWLIAMDAGRVLATGAP 226
Cdd:PRK11176 486 RQRIAIARALLRDSPILILDEATSALDTESERAIQAALDELQKNR---TSLVIAHRLSTIEKADEILVVEDGEIVERGTH 562
|
....*...
gi 505416896 227 AELLARTG 234
Cdd:PRK11176 563 AELLAQNG 570
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
22-218 |
1.30e-05 |
|
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: 46.85 E-value: 1.30e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 22 LDRITLDVPAGLTTGLIGPDGVGKSSLLALASGARalqTGGVdaLGGDMR--SRRHRERVCRRIAYMPQglGKNLYPTLS 99
Cdd:cd03232 23 LNNISGYVKPGTLTALMGESGAGKTTLLDVLAGRK---TAGV--ITGEILinGRPLDKNFQRSTGYVEQ--QDVHSPNLT 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 100 VEENLQFFARLFGHDAGERRRridaltqstglfpflsrpagkLSGGMKqklglccaLIHDPDLLILDEPTTGVDPLARAQ 179
Cdd:cd03232 96 VREALRFSALLRGLSVEQRKR---------------------LTIGVE--------LAAKPSILFLDEPTSGLDSQAAYN 146
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 505416896 180 FWDLIARIRDERPTmsvIVATAYMDEA---QRFDWLIAMDAG 218
Cdd:cd03232 147 IVRFLKKLADSGQA---ILCTIHQPSAsifEKFDRLLLLKRG 185
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
291-434 |
1.33e-05 |
|
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440858 [Multi-domain] Cd Length: 592 Bit Score: 49.01 E-value: 1.33e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 291 SFRI------RRGEIFGFLGSNGCGKSTTMKMLTGLL----------PATE-------GTA-QLFGKEVDPKDIntrrRV 346
Cdd:COG1245 87 GFRLyglpvpKKGKVTGILGPNGIGKSTALKILSGELkpnlgdydeePSWDevlkrfrGTElQDYFKKLANGEI----KV 162
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 347 GYMSQafslYSEL-------TVRQNLvlharlfgvpaAEIDAR--VDEMARRFGLADIYGMLPDSLPLGMRQRLSLAVAM 417
Cdd:COG1245 163 AHKPQ----YVDLipkvfkgTVRELL-----------EKVDERgkLDELAEKLGLENILDRDISELSGGELQRVAIAAAL 227
|
170
....*....|....*..
gi 505416896 418 VHKPELLILDEPTSGVD 434
Cdd:COG1245 228 LRDADFYFFDEPSSYLD 244
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
1-224 |
1.39e-05 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 47.61 E-value: 1.39e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 1 MNASSVVRFSDVSLRYGKTVALDRITLDVPAGLTTGLIGPDGVGKSSLLALASGARALQTGGVDAlggDMRSRRHRERVC 80
Cdd:PRK11701 1 MMDQPLLSVRGLTKLYGPRKGCRDVSFDLYPGEVLGIVGESGSGKTTLLNALSARLAPDAGEVHY---RMRDGQLRDLYA 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 81 RRIA-----------YMPQGLGKNLYPTLSVEENLQffARLFGhdAGER---RRRIDALTqstglfpFLSR---PAGKL- 142
Cdd:PRK11701 78 LSEAerrrllrtewgFVHQHPRDGLRMQVSAGGNIG--ERLMA--VGARhygDIRATAGD-------WLERveiDAARId 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 143 ------SGGMKQKLGLCCALIHDPDLLILDEPTTGVDPLARAQFWDLIARIRDERPTMSVIV----ATAYMdEAQRfdwL 212
Cdd:PRK11701 147 dlpttfSGGMQQRLQIARNLVTHPRLVFMDEPTGGLDVSVQARLLDLLRGLVRELGLAVVIVthdlAVARL-LAHR---L 222
|
250
....*....|..
gi 505416896 213 IAMDAGRVLATG 224
Cdd:PRK11701 223 LVMKQGRVVESG 234
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
22-203 |
2.07e-05 |
|
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: 47.02 E-value: 2.07e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 22 LDRITLDVPAGLTT-----GLIGPDGVGKSSLLALASGARALQTGGVDALGGDmrsrrhrervcrrIAYMPQGLgKNLYP 96
Cdd:cd03237 10 LGEFTLEVEGGSISeseviGILGPNGIGKTTFIKMLAGVLKPDEGDIEIELDT-------------VSYKPQYI-KADYE 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 97 TlSVEENLQFFARLFGHDAGERRRRIDALtqstGLFPFLSRPAGKLSGGMKQKLGLCCALIHDPDLLILDEPTTGVDPLA 176
Cdd:cd03237 76 G-TVRDLLSSITKDFYTHPYFKTEIAKPL----QIEQILDREVPELSGGELQRVAIAACLSKDADIYLLDEPSAYLDVEQ 150
|
170 180
....*....|....*....|....*...
gi 505416896 177 RAQFWDLIAR-IRDERPTMSVIVATAYM 203
Cdd:cd03237 151 RLMASKVIRRfAENNEKTAFVVEHDIIM 178
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
20-276 |
2.07e-05 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 48.62 E-value: 2.07e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 20 VALDRITLDVPAGLTTGLIGPDGVGKSSLLALASGARALQTGGVDAlggdMRSrrhrervcrrIAYMPQglgKNLYPTLS 99
Cdd:PTZ00243 674 VLLRDVSVSVPRGKLTVVLGATGSGKSTLLQSLLSQFEISEGRVWA----ERS----------IAYVPQ---QAWIMNAT 736
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 100 VEENLQFF-----ARLfgHDAgERRRRIDA-LTQ-STGLFPFLSRPAGKLSGGMKQKLGLCCALIHDPDLLILDEPTTGV 172
Cdd:PTZ00243 737 VRGNILFFdeedaARL--ADA-VRVSQLEAdLAQlGGGLETEIGEKGVNLSGGQKARVSLARAVYANRDVYLLDDPLSAL 813
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 173 DplarAQFWDLIAR--IRDERPTMSVIVATAYMDEAQRFDWLIAMDAGRVLATGAPAElLARTgcdSLEAAFIALLPENE 250
Cdd:PTZ00243 814 D----AHVGERVVEecFLGALAGKTRVLATHQVHVVPRADYVVALGDGRVEFSGSSAD-FMRT---SLYATLAAELKENK 885
|
250 260
....*....|....*....|....*.
gi 505416896 251 RRGHKPVKIEPLRADARAGTAIEARG 276
Cdd:PTZ00243 886 DSKEGDADAEVAEVDAAPGGAVDHEP 911
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
289-480 |
2.41e-05 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 48.58 E-value: 2.41e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 289 HVSFRIRRGEIFGFLGSNGCGKSTTMKMLTGLLPATEGTAqlfgkevdpkdINTRRRVGYMSQAFSLYSElTVRQNLvlh 368
Cdd:PLN03130 635 NINLDVPVGSLVAIVGSTGEGKTSLISAMLGELPPRSDAS-----------VVIRGTVAYVPQVSWIFNA-TVRDNI--- 699
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 369 arLFGVP--AAEIDARVDEMARRFGLAdiygMLPD-----------SLPLGMRQRLSLAVAMVHKPELLILDEPTSGVDP 435
Cdd:PLN03130 700 --LFGSPfdPERYERAIDVTALQHDLD----LLPGgdlteigergvNISGGQKQRVSMARAVYSNSDVYIFDDPLSALDA 773
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 505416896 436 -VARDSFWQLMIDLAR---RDLVTifISTHFMNeaqRCDRISLMHAGRV 480
Cdd:PLN03130 774 hVGRQVFDKCIKDELRgktRVLVT--NQLHFLS---QVDRIILVHEGMI 817
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
3-234 |
4.01e-05 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 47.41 E-value: 4.01e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 3 ASSVVRFSDVSLRYGK-TVALDRITLDVPAGLTTGLIGPDGVGKSSLLALASGARALQTGGVdALGGDMRSRRHRERVCR 81
Cdd:PRK10790 337 QSGRIDIDNVSFAYRDdNLVLQNINLSVPSRGFVALVGHTGSGKSTLASLLMGYYPLTEGEI-RLDGRPLSSLSHSVLRQ 415
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 82 RIAYMPQGlgknlyPTLSVEenlQFFARL-FGHDAGERR--RRIDAL-------TQSTGLFPFLSRPAGKLSGGMKQKLG 151
Cdd:PRK10790 416 GVAMVQQD------PVVLAD---TFLANVtLGRDISEEQvwQALETVqlaelarSLPDGLYTPLGEQGNNLSVGQKQLLA 486
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 152 LCCALIHDPDLLILDEPTTGVDPLARAQFWDLIARIRdERPTMSVIvataymdeAQRFDWLIAMDA------GRVLATGA 225
Cdd:PRK10790 487 LARVLVQTPQILILDEATANIDSGTEQAIQQALAAVR-EHTTLVVI--------AHRLSTIVEADTilvlhrGQAVEQGT 557
|
....*....
gi 505416896 226 PAELLARTG 234
Cdd:PRK10790 558 HQQLLAAQG 566
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
105-434 |
4.09e-05 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 47.55 E-value: 4.09e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 105 QFFARLFGHDAGERRRRIDALTQSTGLFPFLSRPAGK-LSGGMKQKLGLCCALIHDPDLLILDEPTTGVDplARAQFWdl 183
Cdd:PLN03073 307 EIYKRLELIDAYTAEARAASILAGLSFTPEMQVKATKtFSGGWRMRIALARALFIEPDLLLLDEPTNHLD--LHAVLW-- 382
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 184 IARIRDERPTMSVIVAtaymdEAQRFDWLIAMD----AGRVLAT-GAPAELLARTGCDSLEAAFIALLPENERRGHKPVK 258
Cdd:PLN03073 383 LETYLLKWPKTFIVVS-----HAREFLNTVVTDilhlHGQKLVTyKGDYDTFERTREEQLKNQQKAFESNERSRSHMQAF 457
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 259 IEPLRADARAGTAIEARGLTM-RFGDFTAV------------------------DHVSFRIRRGEI------FGF----- 302
Cdd:PLN03073 458 IDKFRYNAKRASLVQSRIKALdRLGHVDAVvndpdykfefptpddrpgppiisfSDASFGYPGGPLlfknlnFGIdldsr 537
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 303 ---LGSNGCGKSTTMKMLTGLLPATEGT---------AQLFGKEVDPKDINTRRRVgYMSQAFSLYSEltvrQNLVLHAR 370
Cdd:PLN03073 538 iamVGPNGIGKSTILKLISGELQPSSGTvfrsakvrmAVFSQHHVDGLDLSSNPLL-YMMRCFPGVPE----QKLRAHLG 612
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 505416896 371 LFGVPAaeidarvdemarRFGLADIYgmlpdSLPLGMRQRLSLAVAMVHKPELLILDEPTSGVD 434
Cdd:PLN03073 613 SFGVTG------------NLALQPMY-----TLSGGQKSRVAFAKITFKKPHILLLDEPSNHLD 659
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
288-495 |
4.41e-05 |
|
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 444078 [Multi-domain] Cd Length: 605 Bit Score: 47.51 E-value: 4.41e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 288 DHVSFRIRRGEIFGFLGSNGCGKSTTMKMLTGLLPATEGTAQlfgkeVDPKDINT------RRRVGYMSQAFSLYSElTV 361
Cdd:COG5265 375 KGVSFEVPAGKTVAIVGPSGAGKSTLARLLFRFYDVTSGRIL-----IDGQDIRDvtqaslRAAIGIVPQDTVLFND-TI 448
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 362 RQNLvlharLFGVPAAEiDARVDEMARrfgLADIYGMLpDSLPLGM---------------RQRLSLAVAMVHKPELLIL 426
Cdd:COG5265 449 AYNI-----AYGRPDAS-EEEVEAAAR---AAQIHDFI-ESLPDGYdtrvgerglklsggeKQRVAIARTLLKNPPILIF 518
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 505416896 427 DEPTSgvdpvARDSFWQLMI----DLARRDLVTIFI----SThfmneAQRCDRISLMHAGRVLASDSPAELVRARGA 495
Cdd:COG5265 519 DEATS-----ALDSRTERAIqaalREVARGRTTLVIahrlST-----IVDADEILVLEAGRIVERGTHAELLAQGGL 585
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
295-452 |
4.75e-05 |
|
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI), is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI s are not transport proteins and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLIs have an N-terminal Fe-S domain and two nucleotide binding domains which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213203 [Multi-domain] Cd Length: 255 Bit Score: 46.21 E-value: 4.75e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 295 RRGEIFGFLGSNGCGKSTTMKMLTGLLPATEGTaqlFGKEVDPKDINTRRRVGYMSQAFSLYSELTVR-----QNLVLHA 369
Cdd:cd03236 24 REGQVLGLVGPNGIGKSTALKILAGKLKPNLGK---FDDPPDWDEILDEFRGSELQNYFTKLLEGDVKvivkpQYVDLIP 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 370 RLFGVPAAEIDARVDEMARRFGLADIYGMLP------DSLPLGMRQRLSLAVAMVHKPELLILDEPTSGVDPVARDSFWQ 443
Cdd:cd03236 101 KAVKGKVGELLKKKDERGKLDELVDQLELRHvldrniDQLSGGELQRVAIAAALARDADFYFFDEPSSYLDIKQRLNAAR 180
|
....*....
gi 505416896 444 LMIDLARRD 452
Cdd:cd03236 181 LIRELAEDD 189
|
|
| PRK13541 |
PRK13541 |
cytochrome c biogenesis protein CcmA; Provisional |
39-185 |
5.43e-05 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184128 [Multi-domain] Cd Length: 195 Bit Score: 45.25 E-value: 5.43e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 39 GPDGVGKSSLLALASGARALQTGGVDalggdMRSRRHRERVCRRIAYMPQGLGKNLypTLSVEENLQFFARLFghDAGER 118
Cdd:PRK13541 33 GANGCGKSSLLRMIAGIMQPSSGNIY-----YKNCNINNIAKPYCTYIGHNLGLKL--EMTVFENLKFWSEIY--NSAET 103
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 505416896 119 rrrIDALTQSTGLFPFLSRPAGKLSGGMKQKLGLCCALIHDPDLLILDEPTTGVDPLARAQFWDLIA 185
Cdd:PRK13541 104 ---LYAAIHYFKLHDLLDEKCYSLSSGMQKIVAIARLIACQSDLWLLDEVETNLSKENRDLLNNLIV 167
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
2-197 |
7.53e-05 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 46.73 E-value: 7.53e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 2 NASSVVRFSDVSLRYGKtvaldrITLDVPAGL-----TTGLIGPDGVGKSSLLALASGARALQTGGVDAlggDMRsrrhr 76
Cdd:PRK13409 336 ERETLVEYPDLTKKLGD------FSLEVEGGEiyegeVIGIVGPNGIGKTTFAKLLAGVLKPDEGEVDP---ELK----- 401
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 77 ervcrrIAYMPQGLGKNlyPTLSVEENLQFFARLFG-----HDagerrrridaLTQSTGLFPFLSRPAGKLSGGMKQKLG 151
Cdd:PRK13409 402 ------ISYKPQYIKPD--YDGTVEDLLRSITDDLGssyykSE----------IIKPLQLERLLDKNVKDLSGGELQRVA 463
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 505416896 152 LCCALIHDPDLLILDEPTTGVDPLARAQFWDLIARIRDER-PTMSVI 197
Cdd:PRK13409 464 IAACLSRDADLYLLDEPSAHLDVEQRLAVAKAIRRIAEEReATALVV 510
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
2-169 |
1.00e-04 |
|
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440858 [Multi-domain] Cd Length: 592 Bit Score: 46.32 E-value: 1.00e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 2 NASSVVRFSDVSLRYGKtvaldrITLDVPAGL-----TTGLIGPDGVGKSSLLALASGARALQTGGVDalgGDMRsrrhr 76
Cdd:COG1245 337 EEETLVEYPDLTKSYGG------FSLEVEGGEiregeVLGIVGPNGIGKTTFAKILAGVLKPDEGEVD---EDLK----- 402
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 77 ervcrrIAYMPQGLgKNLYPtLSVEENLqffarlfghdageRRRRIDALTQST---------GLFPFLSRPAGKLSGGMK 147
Cdd:COG1245 403 ------ISYKPQYI-SPDYD-GTVEEFL-------------RSANTDDFGSSYykteiikplGLEKLLDKNVKDLSGGEL 461
|
170 180
....*....|....*....|..
gi 505416896 148 QKLGLCCALIHDPDLLILDEPT 169
Cdd:COG1245 462 QRVAIAACLSRDADLYLLDEPS 483
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
97-312 |
1.17e-04 |
|
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of proteins of which all members for which functions are known except the UvrA proteins are involved in the transport of material through membranes. UvrA orthologs are involved in the recognition of DNA damage as a step in nucleotide excision repair. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 273184 [Multi-domain] Cd Length: 925 Bit Score: 46.16 E-value: 1.17e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 97 TLSVEENLQFFARLfghDAGERRRRI---------DALT--QSTGL-FPFLSRPAGKLSGGMKQKLGLC----CALIHdp 160
Cdd:TIGR00630 435 ELSIREAHEFFNQL---TLTPEEKKIaeevlkeirERLGflIDVGLdYLSLSRAAGTLSGGEAQRIRLAtqigSGLTG-- 509
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 161 DLLILDEPTTGVDPLARAQFWDLIARIRDERPTmsVIVATAYMDEAQRFDWLIAM------DAGRVLATGAPAELLARTg 234
Cdd:TIGR00630 510 VLYVLDEPSIGLHQRDNRRLINTLKRLRDLGNT--LIVVEHDEDTIRAADYVIDIgpgageHGGEVVASGTPEEILANP- 586
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 505416896 235 cDSLEAAFIAllpeneRRGHKPVKIEPLRADARAGTAIEARGLTMRfgdftavdHVSFRIRRGEIFGFLGSNGCGKST 312
Cdd:TIGR00630 587 -DSLTGQYLS------GRKKIEVPAERRPGNGKFLTLKGARENNLK--------NITVSIPLGLFTCITGVSGSGKST 649
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
7-184 |
1.30e-04 |
|
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: 43.68 E-value: 1.30e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 7 VRFSDVSLRY--GKTVaLDRITLDVPAGLTTGLIGPDGVGKSSLLALASGARALQTGGVDALGGDmrsrrhrervcrRIA 84
Cdd:cd03223 1 IELENLSLATpdGRVL-LKDLSFEIKPGDRLLITGPSGTGKSSLFRALAGLWPWGSGRIGMPEGE------------DLL 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 85 YMPQglgKNLYPTLSVEENLqffarlfghdagerrrridaltqstgLFPFLSRpagkLSGGMKQKLGLCCALIHDPDLLI 164
Cdd:cd03223 68 FLPQ---RPYLPLGTLREQL--------------------------IYPWDDV----LSGGEQQRLAFARLLLHKPKFVF 114
|
170 180
....*....|....*....|
gi 505416896 165 LDEPTTGVDPLARAQFWDLI 184
Cdd:cd03223 115 LDEATSALDEESEDRLYQLL 134
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
10-231 |
1.41e-04 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 45.64 E-value: 1.41e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 10 SDVSLRYGKTVALDRITLDVPAGLTTGLIGPDGVGKSSLL-ALASGARALQ-TGGVDALGGDMrsrrhRERVCRRIAYMP 87
Cdd:PLN03211 72 SDETRQIQERTILNGVTGMASPGEILAVLGPSGSGKSTLLnALAGRIQGNNfTGTILANNRKP-----TKQILKRTGFVT 146
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 88 QGlgKNLYPTLSVEENLQFFARLFGHDAGERRRRI---DALTQSTGLFPFLSRPAGK-----LSGGMKQKLGLCCALIHD 159
Cdd:PLN03211 147 QD--DILYPHLTVRETLVFCSLLRLPKSLTKQEKIlvaESVISELGLTKCENTIIGNsfirgISGGERKRVSIAHEMLIN 224
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 505416896 160 PDLLILDEPTTGVDPLARAQFWDLIARIRDERPTMSVIVATAYMDEAQRFDWLIAMDAGRVLATGAPAELLA 231
Cdd:PLN03211 225 PSLLILDEPTSGLDATAAYRLVLTLGSLAQKGKTIVTSMHQPSSRVYQMFDSVLVLSEGRCLFFGKGSDAMA 296
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
402-472 |
1.64e-04 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 45.79 E-value: 1.64e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 505416896 402 SLPLGMRQRLSLAVAMVHKPELLILDEPTSGVDPVARDSFWQLMIDLARRDLVTIFISTHFMNEAQRCDRI 472
Cdd:PTZ00265 1358 SLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDIKDKADKTIITIAHRIASIKRSDKI 1428
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
296-461 |
1.91e-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: 42.75 E-value: 1.91e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 296 RGEIFGFLGSNGCGKSTTMKMLTGLLPATEGTAqlfgKEVDPKDINtrrrvgymsqafslyseltvrqnlvlharlfgvp 375
Cdd:smart00382 1 PGEVILIVGPPGSGKTTLARALARELGPPGGGV----IYIDGEDIL---------------------------------- 42
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 376 aaeidarvdEMARRFGLADIYGMLPDSLPLGMRQRLSLAVAMVHKPELLILDEPTSGVDPVARD-----SFWQLMIDLAR 450
Cdd:smart00382 43 ---------EEVLDQLLLIIVGGKKASGSGELRLRLALALARKLKPDVLILDEITSLLDAEQEAlllllEELRLLLLLKS 113
|
170
....*....|.
gi 505416896 451 RDLVTIFISTH 461
Cdd:smart00382 114 EKNLTVILTTN 124
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
19-220 |
1.91e-04 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 44.04 E-value: 1.91e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 19 TVALDRITLDVPAGLTTGLIGPDGVGKSSLLALASGARALQTGGVDALG---GDMRSRRHRERVCRRIAYMPQGlgKNLY 95
Cdd:PRK11629 22 TDVLHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGqpmSKLSSAAKAELRNQKLGFIYQF--HHLL 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 96 PTLSVEENLQFFARLFGHDAGERRRRIDALTQSTGLFPFLSRPAGKLSGGMKQKLGLCCALIHDPDLLILDEPTTGVDPL 175
Cdd:PRK11629 100 PDFTALENVAMPLLIGKKKPAEINSRALEMLAAVGLEHRANHRPSELSGGERQRVAIARALVNNPRLVLADEPTGNLDAR 179
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 505416896 176 ARAQFWDLIARIRDERPTmSVIVATAYMDEAQRFDWLIAMDAGRV 220
Cdd:PRK11629 180 NADSIFQLLGELNRLQGT-AFLVVTHDLQLAKRMSRQLEMRDGRL 223
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
11-230 |
2.02e-04 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 44.43 E-value: 2.02e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 11 DVSLRYGktVALDRITLDVPAGLTTGLIGPDGVGKSSLL----------ALASGARAlqTGGVdALGGDMRSRRHRERVC 80
Cdd:PRK13547 8 HVARRHR--AILRDLSLRIEPGRVTALLGRNGAGKSTLLkalagdltggGAPRGARV--TGDV-TLNGEPLAAIDAPRLA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 81 RRIAYMPQGlGKNLYPtLSVEENLQF----FARLFGHDAGERRRRIDALTQSTGLFPFLSRPAGKLSGGMKQKLGLCCAL 156
Cdd:PRK13547 83 RLRAVLPQA-AQPAFA-FSAREIVLLgrypHARRAGALTHRDGEIAWQALALAGATALVGRDVTTLSGGELARVQFARVL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 157 ---------IHDPDLLILDEPTTGVDPLARAQFWDLIARI-RDERptMSVIVATAYMDEAQRFDWLIAMDA-GRVLATGA 225
Cdd:PRK13547 161 aqlwpphdaAQPPRYLLLDEPTAALDLAHQHRLLDTVRRLaRDWN--LGVLAIVHDPNLAARHADRIAMLAdGAIVAHGA 238
|
....*
gi 505416896 226 PAELL 230
Cdd:PRK13547 239 PADVL 243
|
|
| PRK15093 |
PRK15093 |
peptide ABC transporter ATP-binding protein SapD; |
118-231 |
2.21e-04 |
|
peptide ABC transporter ATP-binding protein SapD;
Pssm-ID: 185049 [Multi-domain] Cd Length: 330 Bit Score: 44.41 E-value: 2.21e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 118 RRRRIDALTQSTGL---------FPFlsrpagKLSGGMKQKLGLCCALIHDPDLLILDEPTTGVDPLARAQFWDLIARIR 188
Cdd:PRK15093 132 RKRRAIELLHRVGIkdhkdamrsFPY------ELTEGECQKVMIAIALANQPRLLIADEPTNAMEPTTQAQIFRLLTRLN 205
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 505416896 189 DERPTMSVIVATAYMDEAQRFDWLIAMDAGRVLATGAPAELLA 231
Cdd:PRK15093 206 QNNNTTILLISHDLQMLSQWADKINVLYCGQTVETAPSKELVT 248
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
294-434 |
2.84e-04 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 44.80 E-value: 2.84e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 294 IRRGEIFGFLGSNGCGKSTTMKMLTGLLPATEGTaqlFGKEVDPKDINTRRRVGYMSQAFSLYSELTVR-----QNLVLH 368
Cdd:PRK13409 96 PKEGKVTGILGPNGIGKTTAVKILSGELIPNLGD---YEEEPSWDEVLKRFRGTELQNYFKKLYNGEIKvvhkpQYVDLI 172
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 505416896 369 ARLFGVPAAEIDARVDE------MARRFGLADIYGMLPDSLPLGMRQRLSLAVAMVHKPELLILDEPTSGVD 434
Cdd:PRK13409 173 PKVFKGKVRELLKKVDErgkldeVVERLGLENILDRDISELSGGELQRVAIAAALLRDADFYFFDEPTSYLD 244
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
139-199 |
3.37e-04 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 44.63 E-value: 3.37e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 505416896 139 AGKLSGGMKQKLGLCCALIHDPDLLILDEPTTGVDPLARAQFWDLIARIRDERPTMSVIVA 199
Cdd:PTZ00265 577 ASKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQKTINNLKGNENRITIIIA 637
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
271-434 |
4.20e-04 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 44.11 E-value: 4.20e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 271 AIEARGLTMRFGDFTAVDHVSFRIRRGEIFGFLGSNGCGKSTTMKMLTGLLPATEGTAQLFGKEvdpkdintrrRVGYMS 350
Cdd:PRK15064 319 ALEVENLTKGFDNGPLFKNLNLLLEAGERLAIIGENGVGKTTLLRTLVGELEPDSGTVKWSENA----------NIGYYA 388
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 351 Q--AFSLYSELTV-------RQnlvlharlfgvpaaEIDarvDEMARR-------FGLADIyGMLPDSLPLGMRQRLSLA 414
Cdd:PRK15064 389 QdhAYDFENDLTLfdwmsqwRQ--------------EGD---DEQAVRgtlgrllFSQDDI-KKSVKVLSGGEKGRMLFG 450
|
170 180
....*....|....*....|
gi 505416896 415 VAMVHKPELLILDEPTSGVD 434
Cdd:PRK15064 451 KLMMQKPNVLVMDEPTNHMD 470
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
290-492 |
9.84e-04 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 43.43 E-value: 9.84e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 290 VSFRIRRGEIFGFLGSNGCGKSTTMKMLTGLLPATEGTAqlfgkevdpkdINTRRRVGYMSQAFSLYSElTVRQNLVL-- 367
Cdd:PLN03232 636 INLEIPVGSLVAIVGGTGEGKTSLISAMLGELSHAETSS-----------VVIRGSVAYVPQVSWIFNA-TVRENILFgs 703
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 368 ------HARLFGVPAAEIDarVDEMARRfGLADIyGMLPDSLPLGMRQRLSLAVAMVHKPELLILDEPTSGVDP-VARDS 440
Cdd:PLN03232 704 dfeserYWRAIDVTALQHD--LDLLPGR-DLTEI-GERGVNISGGQKQRVSMARAVYSNSDIYIFDDPLSALDAhVAHQV 779
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 505416896 441 FWQLMID-LARRDLVTIFISTHFMNEAqrcDRISLMHAGRVLASDSPAELVRA 492
Cdd:PLN03232 780 FDSCMKDeLKGKTRVLVTNQLHFLPLM---DRIILVSEGMIKEEGTFAELSKS 829
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
96-325 |
1.01e-03 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 43.28 E-value: 1.01e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 96 PTLSVEENLQFFarlfghdagerRRRIDALTQsTGLfPFLS--RPAGKLSGGMKQKLGLCCALihDPDLL----ILDEPT 169
Cdd:PRK00635 442 KSLSIEEVLQGL-----------KSRLSILID-LGL-PYLTpeRALATLSGGEQERTALAKHL--GAELIgityILDEPS 506
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 170 TGVDPLARAQFWDLIARIRDERPTmsvIVATAYMDEAQRF-DWLIAMD------AGRVLATGAPAELLARtgCDSLEAAF 242
Cdd:PRK00635 507 IGLHPQDTHKLINVIKKLRDQGNT---VLLVEHDEQMISLaDRIIDIGpgagifGGEVLFNGSPREFLAK--SDSLTAKY 581
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 243 IallpenerRGHKPVKIePLRADARAGTaieargLTMRFGDFTAVDHVSFRIRRGEIFGFLGSNGCGKSTTMKmlTGLLP 322
Cdd:PRK00635 582 L--------RQELTIPI-PEKRTNSLGT------LTLSKATKHNLKDLTISLPLGRLTVVTGVSGSGKSSLIN--DTLVP 644
|
...
gi 505416896 323 ATE 325
Cdd:PRK00635 645 AVE 647
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
284-479 |
1.05e-03 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 43.17 E-value: 1.05e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 284 FTAVDHVSFRIRRGEIFGFLGSNGCGKSTTMKMLTGllpATEGTAQLFGKEV-----DPKDINTRRR--VGYMSQAFSLY 356
Cdd:TIGR00956 74 FDILKPMDGLIKPGELTVVLGRPGSGCSTLLKTIAS---NTDGFHIGVEGVItydgiTPEEIKKHYRgdVVYNAETDVHF 150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 357 SELTVRQNLVLHARLFGvPAAEIDArVDEMARRFGLAD----IYGM-----------LPDSLPLGMRQRLSLAVAMVHKP 421
Cdd:TIGR00956 151 PHLTVGETLDFAARCKT-PQNRPDG-VSREEYAKHIADvymaTYGLshtrntkvgndFVRGVSGGERKRVSIAEASLGGA 228
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 505416896 422 ELLILDEPTSGVdpvarDSFWQLMIDLARRDLVTIFISTHFMNEAQrC--------DRISLMHAGR 479
Cdd:TIGR00956 229 KIQCWDNATRGL-----DSATALEFIRALKTSANILDTTPLVAIYQ-CsqdayelfDKVIVLYEGY 288
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
138-199 |
1.14e-03 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 43.09 E-value: 1.14e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 505416896 138 PAGK-LSGGMKQKLGLCCALIHDPDLLILDEPTTGVDPLARAQFWDLIARIRDERPTMSVIVA 199
Cdd:PTZ00265 1354 PYGKsLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDIKDKADKTIITIA 1416
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
121-172 |
1.35e-03 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 42.89 E-value: 1.35e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 505416896 121 RIDALTqSTGL--FPfLSRPAGKLSGGMKQKLGLCCALIH---DPDLLILDEPTTGV 172
Cdd:PRK00635 789 KIHALC-SLGLdyLP-LGRPLSSLSGGEIQRLKLAYELLApskKPTLYVLDEPTTGL 843
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
22-231 |
1.39e-03 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 42.80 E-value: 1.39e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 22 LDRITLDVPAGLTTGLIGPDGVGKSSLLALASGARALQTGGVDALGGdmrsrrhrervcrRIAYMPQglgKNLYPTLSVE 101
Cdd:PLN03130 633 LSNINLDVPVGSLVAIVGSTGEGKTSLISAMLGELPPRSDASVVIRG-------------TVAYVPQ---VSWIFNATVR 696
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 102 ENLqFFARLFGHDAGERRRRIDALTQSTGLFPF-----LSRPAGKLSGGMKQKLGLCCALIHDPDLLILDEPTTGVDPLA 176
Cdd:PLN03130 697 DNI-LFGSPFDPERYERAIDVTALQHDLDLLPGgdlteIGERGVNISGGQKQRVSMARAVYSNSDVYIFDDPLSALDAHV 775
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 505416896 177 RAQFWDLIarIRDERPTMSVIVATAYMDEAQRFDWLIAMDAGRVLATGAPAELLA 231
Cdd:PLN03130 776 GRQVFDKC--IKDELRGKTRVLVTNQLHFLSQVDRIILVHEGMIKEEGTYEELSN 828
|
|
| MFS_BCD_PucC-like |
cd06176 |
Bacteriochlorophyll delivery (BCD) family, also called PucC family, of the Major Facilitator ... |
841-927 |
1.51e-03 |
|
Bacteriochlorophyll delivery (BCD) family, also called PucC family, of the Major Facilitator Superfamily; The bacteriochlorophyll delivery (BCD) family, also called PucC family, is composed of the PucC protein and related proteins including LhaA (also called ORF477 and F1696) and bacteriochlorophyll synthase 44.5 kDa chain (also called ORF428). These proteins are found in photosynthetic organisms. Rhodobacter capsulatus LhaA and PucC are implicated in light-harvesting complex 1 and 2 (LH1 and LH2) assembly. PucC may function to shepherd or sequester LH2 alpha and beta proteins to facilitate proper assembly, as well as deliver bacteriochlorophyll a to nascent LH2 complexes. The BCD family belongs to the Major Facilitator Superfamily (MFS) of membrane transport proteins, which are thought to function through a single substrate binding site, alternating-access mechanism involving a rocker-switch type of movement.
Pssm-ID: 349950 [Multi-domain] Cd Length: 409 Bit Score: 42.10 E-value: 1.51e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 841 GKQVPYVVL-AMLNFLLMTMLARIAFDVPVKGSFMTLLLAVLIFNVVATGIGLLASTF-----------TRSQVAAIV-- 906
Cdd:cd06176 67 YRRTPYIWLgMLLLALGLALAPFAALLLAGAAFWLGLALAVLAFLLYGIGVGAAGTAFlalladltpeeRRPRAVTVVwt 146
|
90 100
....*....|....*....|.
gi 505416896 907 MTIIGTMIPTVQFAGLLTPLS 927
Cdd:cd06176 147 MLILGIIVTAIVFGRLLDPYS 167
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
11-218 |
1.54e-03 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 42.79 E-value: 1.54e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 11 DVSLRYGKTVALDRITLDVPAGLTTGLIGPDGVGKSSLLALASGARalqTGGVdALGGDMRS--RRHRERVCRRIAYMPQ 88
Cdd:TIGR00956 768 EVKIKKEKRVILNNVDGWVKPGTLTALMGASGAGKTTLLNVLAERV---TTGV-ITGGDRLVngRPLDSSFQRSIGYVQQ 843
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 89 glgKNLY-PTLSVEENLQFFARLFGHDA---GERRRRIDALTQSTGLFPF----LSRPAGKLSGGMKQKLGLCCALIHDP 160
Cdd:TIGR00956 844 ---QDLHlPTSTVRESLRFSAYLRQPKSvskSEKMEYVEEVIKLLEMESYadavVGVPGEGLNVEQRKRLTIGVELVAKP 920
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 505416896 161 DLLI-LDEPTTGVDplARAQfWDLIARIRDERPTMSVIVATAYMDEA---QRFDWLIAMDAG 218
Cdd:TIGR00956 921 KLLLfLDEPTSGLD--SQTA-WSICKLMRKLADHGQAILCTIHQPSAilfEEFDRLLLLQKG 979
|
|
| ABC_Rad50 |
cd03240 |
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ... |
277-435 |
1.91e-03 |
|
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ATP-binding cassette of ABC transporters, but are not associated with membrane-spanning domains. The conserved ATP-binding motifs common to Rad50 and the ABC transporter family include the Walker A and Walker B motifs, the Q loop, a histidine residue in the switch region, a D-loop, and a conserved LSGG sequence. This conserved sequence, LSGG, is the most specific and characteristic motif of this family and is thus known as the ABC signature sequence.
Pssm-ID: 213207 [Multi-domain] Cd Length: 204 Bit Score: 40.67 E-value: 1.91e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 277 LTMR-FGDFTAVDHVSFRirrGEIFGFLGSNGCGKSTTmkmLTGLLPATEGTAQLFGKEV--DPKDINTRRRVGYMSQAF 353
Cdd:cd03240 4 LSIRnIRSFHERSEIEFF---SPLTLIVGQNGAGKTTI---IEALKYALTGELPPNSKGGahDPKLIREGEVRAQVKLAF 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 354 SLYS--ELTVRQNL-VLHARLFgVPAAEIDARVDEMarrfgladiygmlPDSLPLGMRQRLS----LAVAMV--HKPELL 424
Cdd:cd03240 78 ENANgkKYTITRSLaILENVIF-CHQGESNWPLLDM-------------RGRCSGGEKVLASliirLALAETfgSNCGIL 143
|
170
....*....|.
gi 505416896 425 ILDEPTSGVDP 435
Cdd:cd03240 144 ALDEPTTNLDE 154
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
9-239 |
1.92e-03 |
|
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: 42.20 E-value: 1.92e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 9 FSDVSLrYGKTVaLDRITLDVPAGLTTGLIGPDGVGKSSLLALASGARALQTGGVDALGgdmrsrrhrervcrRIAYMPQ 88
Cdd:TIGR01271 431 FSNFSL-YVTPV-LKNISFKLEKGQLLAVAGSTGSGKSSLLMMIMGELEPSEGKIKHSG--------------RISFSPQ 494
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 89 glgknlYPTL---SVEENLqffarLFGHDAGERRRR--IDA--LTQSTGLFP-----FLSRPAGKLSGGMKQKLGLCCAL 156
Cdd:TIGR01271 495 ------TSWImpgTIKDNI-----IFGLSYDEYRYTsvIKAcqLEEDIALFPekdktVLGEGGITLSGGQRARISLARAV 563
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 157 IHDPDLLILDEPTTGVDPLARAQFWD------LIARIRderptmsvIVATAYMDEAQRFDWLIAMDAGRVLATGAPAELL 230
Cdd:TIGR01271 564 YKDADLYLLDSPFTHLDVVTEKEIFEsclcklMSNKTR--------ILVTSKLEHLKKADKILLLHEGVCYFYGTFSELQ 635
|
250
....*....|....*..
gi 505416896 231 ART--------GCDSLE 239
Cdd:TIGR01271 636 AKRpdfsslllGLEAFD 652
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
277-330 |
2.05e-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: 40.25 E-value: 2.05e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 505416896 277 LTMRFGDFtavdHVSFR---IRRGEIFGFLGSNGCGKSTTMKMLTGLLPATEGTAQL 330
Cdd:cd03222 6 CVKRYGVF----FLLVElgvVKEGEVIGIVGPNGTGKTTAVKILAGQLIPNGDNDEW 58
|
|
| Mtu_efflux |
TIGR00025 |
ABC transporter efflux protein, DrrB family; The seed members for this model are a paralogous ... |
812-952 |
3.02e-03 |
|
ABC transporter efflux protein, DrrB family; The seed members for this model are a paralogous family of Mycobacterium tuberculosis. Nearly all proteins scoring above the noise cutoff are from high-GC Gram-positive organisms. The members of this paralogous family of efflux proteins are all found in operons with ATP-binding chain partners. They are related to a putative daunorubicin resistance efflux protein of Streptomyces peucetius. This model represents a branch of a larger superfamily that also includes NodJ, a part of the NodIJ pair of nodulation-triggering signal efflux proteins. The members of this branch may all act in antibiotic resistance.
Pssm-ID: 272861 [Multi-domain] Cd Length: 232 Bit Score: 40.19 E-value: 3.02e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 812 TALAVVRERELGSILNLYVTPVTRTEFLIGKqVPYVVLAMLNFLLMTMLARIAFDVPVKGSFMTLLLAVLIFNVVATGIG 891
Cdd:TIGR00025 55 QAIAVARDRRYGALKRLGATPLPRLGILAGR-SLAVVARVFLQTLILLVIGFVLGFRFAGGALTALTLGAVIIALGTALF 133
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 505416896 892 LLASTFTRS--QVAAIVMTIIGTMIPTVQFAGLLTPLSSLEGTGRFIGLVYPATYMLSISRGV 952
Cdd:TIGR00025 134 AALGLVAGGtlQAEIVLAVANLVWFIFALLSAGLVPLNLIPTWIKWFVRVQPSSYATEALRQA 196
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
39-174 |
3.15e-03 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 40.22 E-value: 3.15e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 39 GPDGVGKSSLLALASGARALQTGGVDALGGDMRSRRHRERvcrrIAYMPQGLGknLYPTLSVEENLQFFARLFGHDAgeR 118
Cdd:PRK13543 44 GDNGAGKTTLLRVLAGLLHVESGQIQIDGKTATRGDRSRF----MAYLGHLPG--LKADLSTLENLHFLCGLHGRRA--K 115
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 505416896 119 RRRIDALTqSTGLFPFLSRPAGKLSGGMKQKLGLCCALIHDPDLLILDEPTTGVDP 174
Cdd:PRK13543 116 QMPGSALA-IVGLAGYEDTLVRQLSAGQKKRLALARLWLSPAPLWLLDEPYANLDL 170
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
6-54 |
3.46e-03 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 41.26 E-value: 3.46e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 505416896 6 VVRFSDVSLRYGKTVALDRITLDVPAGLTTGLIGPDGVGKSSLLALASG 54
Cdd:PRK11819 324 VIEAENLSKSFGDRLLIDDLSFSLPPGGIVGIIGPNGAGKSTLFKMITG 372
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
5-173 |
4.14e-03 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 41.00 E-value: 4.14e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 5 SVVRFSDVSLRY-GKTVALDRITLDVPAGLTTGLIGPDGVGKSSLLALASGARALQTGGVdalggdMRSrrhrerVCRRI 83
Cdd:PLN03073 507 PIISFSDASFGYpGGPLLFKNLNFGIDLDSRIAMVGPNGIGKSTILKLISGELQPSSGTV------FRS------AKVRM 574
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 84 AYMPQ----GLGKNLYPTLsveenlqFFARLFghdAGERRRRIDALTQSTGLFPFLS-RPAGKLSGGMKQKLGLCCALIH 158
Cdd:PLN03073 575 AVFSQhhvdGLDLSSNPLL-------YMMRCF---PGVPEQKLRAHLGSFGVTGNLAlQPMYTLSGGQKSRVAFAKITFK 644
|
170
....*....|....*
gi 505416896 159 DPDLLILDEPTTGVD 173
Cdd:PLN03073 645 KPHILLLDEPSNHLD 659
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
272-347 |
4.92e-03 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 40.01 E-value: 4.92e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 505416896 272 IEARGLTMRFGDFTAVDHVSFRIRRGEIFGFLGSNGCGKSTTMKMLTGlLPA---TEGTAQLFGKEVDPKDINTRRRVG 347
Cdd:CHL00131 8 LEIKNLHASVNENEILKGLNLSINKGEIHAIMGPNGSGKSTLSKVIAG-HPAykiLEGDILFKGESILDLEPEERAHLG 85
|
|
| ABC2_membrane_4 |
pfam12730 |
ABC-2 family transporter protein; This family is related to the ABC-2 membrane transporter ... |
818-913 |
6.29e-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: 38.72 E-value: 6.29e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505416896 818 RERELGSILNLYVTPVTRTEFLIGK----QVPYVVLAMLNFLLMTMLARIAFDVPVKGS------FMTLLLAVLIFNVVA 887
Cdd:pfam12730 74 REYDNDTLKNLLTIPVSRRKLLFAKlivlLLLSVLFMLVTFLITVLFGLLSGFVGFSWGlilyllKKCLEIGLLVFFAVL 153
|
90 100
....*....|....*....|....*.
gi 505416896 888 TGIGLlaSTFTRSQVAAIVMTIIGTM 913
Cdd:pfam12730 154 PIIAL--ALLFKGYVLPVILTLVYTF 177
|
|
| |
