|
Name |
Accession |
Description |
Interval |
E-value |
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
12-910 |
0e+00 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 1950.31 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 12 VAQLAGVSQHYGKTVALNNITLDIPARCMVGLIGPDGVGKSSLLSLISGARVIEQGNVMVLGGDMRDPKHRRDVCPRIAW 91
Cdd:NF033858 1 VARLEGVSHRYGKTVALDDVSLDIPAGCMVGLIGPDGVGKSSLLSLIAGARKIQQGRVEVLGGDMADARHRRAVCPRIAY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 92 MPQGLGKNLYHTLSVYENVDFFARLFGHDKAEREVRINELLTSTGLAPFRDRPAGKLSGGMKQKLGLCCALIHDPELLIL 171
Cdd:NF033858 81 MPQGLGKNLYPTLSVFENLDFFGRLFGQDAAERRRRIDELLRATGLAPFADRPAGKLSGGMKQKLGLCCALIHDPDLLIL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 172 DEPTTGVDPLSRSQFWDLIDSIRQRQSNMSVLVATAYMEEAERFDWLVAMNAGEVLATGSAEELRQQTQSATLEEAFINL 251
Cdd:NF033858 161 DEPTTGVDPLSRRQFWELIDRIRAERPGMSVLVATAYMEEAERFDWLVAMDAGRVLATGTPAELLARTGADTLEAAFIAL 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 252 LPQAQRQAHQAVVIPPYQPENAE-IAIEARDLTMRFGSFVAVDHVNFRIPRGEIFGFLGSNGCGKSTTMKMLTGLLPASE 330
Cdd:NF033858 241 LPEEKRRGHQPVVIPPRPADDDDePAIEARGLTMRFGDFTAVDHVSFRIRRGEIFGFLGSNGCGKSTTMKMLTGLLPASE 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 331 GEAWLFGQPVDPKDIDTRRRVGYMSQAFSLYNELTVRQNLELHARLFHIPEAEIPARVAEMSERFKLNDVEDILPESLPL 410
Cdd:NF033858 321 GEAWLFGQPVDAGDIATRRRVGYMSQAFSLYGELTVRQNLELHARLFHLPAAEIAARVAEMLERFDLADVADALPDSLPL 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 411 GIRQRLSLAVAVIHRPEMLILDEPTSGVDPVARDMFWQLMVDLSRQDKVTIFISTHFMNEAERCDRISLMHAGKVLASGT 490
Cdd:NF033858 401 GIRQRLSLAVAVIHKPELLILDEPTSGVDPVARDMFWRLLIELSREDGVTIFISTHFMNEAERCDRISLMHAGRVLASDT 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 491 PQELVEKRGAASLEEAFIAYLQEAAGQSNEAEAPPVV-------HDTTHAPRQGFSLRRLFSYSRREALELRRDPVRSTL 563
Cdd:NF033858 481 PAALVAARGAATLEEAFIAYLEEAAGAAAAPAAAAAPaaaaaapAAPAPAPRRRFSLRRLLAYARREALELLRDPIRLTF 560
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 564 ALMGTVILMLIMGYGISMDVENLRFAVLDRDQTVSSQAWTLNLSGSRYFIEQPPLTSYDELDRRMRAGDITVAIEIPPNF 643
Cdd:NF033858 561 ALLGSVILMFVMGYGISLDVENLTFAVLDRDQTPESRAYLLNFAGSRYFIEQPPIADYAELDRRMRSGELSLAIEIPPGF 640
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 644 GRDIARGTPVELGVWIDGAMPSRAETVKGYVQAMHQSWLQDVAsRQSTPASQSGLMNIETRYRYNPDVKSLPAIVPAVIP 723
Cdd:NF033858 641 GRDLLRGRPPEVGAWIDGAMPFRAETIRGYVQGMHQQWLADLA-RERGGAAAASPATIETRYRYNPDFKSLPAMVPAVIP 719
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 724 LLLMMIPSMLSALSVVREKELGSIINLYVTPTTRSEFLLGKQLPYIALGMLNFFLLCGLSVFVFGVPHKGSFLTLTLAAL 803
Cdd:NF033858 720 LLLMLIPAMLTALSVVREKELGSITNLYVTPVTRLEFLLGKQLPYVALAMLNFLLLVLLAVFVFGVPLKGSFLALALGAL 799
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 804 LYIIIATGMGLLISTFMKSQIAAIFGTAIITLIPATQFSGMIDPVASLEGPGRWIGEVYPTSHFLTIARGTFSKALDLTD 883
Cdd:NF033858 800 LYVTATTGLGLLISTFTRSQIAAIFGTAILTLIPAVQFSGLLDPVSSLEGAGRLIGRIFPATYFLTISRGTFTKGLGFAD 879
|
890 900
....*....|....*....|....*..
gi 732682709 884 LWQLFIPLLIAIPLVMGLSILLLKKQE 910
Cdd:NF033858 880 LWPSFLALAAFIPVLLGLSVLLLKKQE 906
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
277-515 |
9.65e-106 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 326.64 E-value: 9.65e-106
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 277 IEARDLTMRFGSFVAVDHVNFRIPRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGEAWLFGQPVDPKDIDTRRRVGYMSQ 356
Cdd:COG1131 1 IEVRGLTKRYGDKTALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRVLGEDVARDPAEVRRRIGYVPQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 357 AFSLYNELTVRQNLELHARLFHIPEAEIPARVAEMSERFKLNDVEDILPESLPLGIRQRLSLAVAVIHRPEMLILDEPTS 436
Cdd:COG1131 81 EPALYPDLTVRENLRFFARLYGLPRKEARERIDELLELFGLTDAADRKVGTLSGGMKQRLGLALALLHDPELLILDEPTS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 437 GVDPVARDMFWQLMVDLSRQDKvTIFISTHFMNEAER-CDRISLMHAGKVLASGTPQELVEKrgaaSLEEAFIAYLQEAA 515
Cdd:COG1131 161 GLDPEARRELWELLRELAAEGK-TVLLSTHYLEEAERlCDRVAIIDKGRIVADGTPDELKAR----LLEDVFLELTGEEA 235
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
11-494 |
1.03e-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: 297.20 E-value: 1.03e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 11 PVAQLAGVSQHY--GKTVALNNITLDIPARCMVGLIGPDGVGKSSLLSLISG-----ARVieQGNVMVLGGDMRDPKhRR 83
Cdd:COG1123 3 PLLEVRDLSVRYpgGDVPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGllphgGRI--SGEVLLDGRDLLELS-EA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 84 DVCPRIAWMPQGLGKNLyHTLSVYENVDFFARLFGHDKAEREVRINELLTSTGLAPFRDRPAGKLSGGMKQKLGLCCALI 163
Cdd:COG1123 80 LRGRRIGMVFQDPMTQL-NPVTVGDQIAEALENLGLSRAEARARVLELLEAVGLERRLDRYPHQLSGGQRQRVAIAMALA 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 164 HDPELLILDEPTTGVDPLSRSQFWDLIDSIrQRQSNMSVLVATAYMEE-AERFDWLVAMNAGEVLATGSAEELRQQTQSa 242
Cdd:COG1123 159 LDPDLLIADEPTTALDVTTQAEILDLLREL-QRERGTTVLLITHDLGVvAEIADRVVVMDDGRIVEDGPPEEILAAPQA- 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 243 tleeafinllPQAQRQAHQAVVIPPYQPENAEIAIEARDLTMRF-----GSFVAVDHVNFRIPRGEIFGFLGSNGCGKST 317
Cdd:COG1123 237 ----------LAAVPRLGAARGRAAPAAAAAEPLLEVRNLSKRYpvrgkGGVRAVDDVSLTLRRGETLGLVGESGSGKST 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 318 TMKMLTGLLPASEGEAWLFGQPVDPKDIDT----RRRVGYMSQ--AFSLYNELTVRQNLELHARLFHI-PEAEIPARVAE 390
Cdd:COG1123 307 LARLLLGLLRPTSGSILFDGKDLTKLSRRSlrelRRRVQMVFQdpYSSLNPRMTVGDIIAEPLRLHGLlSRAERRERVAE 386
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 391 MSERFKLN-DVEDILPESLPLGIRQRLSLAVAVIHRPEMLILDEPTSGVDPVARDMFWQLMVDLSRQDKVT-IFIsTHFM 468
Cdd:COG1123 387 LLERVGLPpDLADRYPHELSGGQRQRVAIARALALEPKLLILDEPTSALDVSVQAQILNLLRDLQRELGLTyLFI-SHDL 465
|
490 500
....*....|....*....|....*..
gi 732682709 469 NEAER-CDRISLMHAGKVLASGTPQEL 494
Cdd:COG1123 466 AVVRYiADRVAVMYDGRIVEDGPTEEV 492
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
17-257 |
3.54e-89 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 283.11 E-value: 3.54e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 17 GVSQHYGKTVALNNITLDIPARCMVGLIGPDGVGKSSLLSLISGARVIEQGNVMVLGGDMRdpKHRRDVCPRIAWMPQGL 96
Cdd:COG1131 5 GLTKRYGDKTALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRVLGEDVA--RDPAEVRRRIGYVPQEP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 97 gkNLYHTLSVYENVDFFARLFGHDKAEREVRINELLTSTGLAPFRDRPAGKLSGGMKQKLGLCCALIHDPELLILDEPTT 176
Cdd:COG1131 83 --ALYPDLTVRENLRFFARLYGLPRKEARERIDELLELFGLTDAADRKVGTLSGGMKQRLGLALALLHDPELLILDEPTS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 177 GVDPLSRSQFWDLIDSIRQRqsNMSVLVATAYMEEAERF-DWLVAMNAGEVLATGSAEELRQQtqsaTLEEAFINLLPQA 255
Cdd:COG1131 161 GLDPEARRELWELLRELAAE--GKTVLLSTHYLEEAERLcDRVAIIDKGRIVADGTPDELKAR----LLEDVFLELTGEE 234
|
..
gi 732682709 256 QR 257
Cdd:COG1131 235 AR 236
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
277-494 |
1.66e-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: 246.13 E-value: 1.66e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 277 IEARDLTMRFGSFVAVDHVNFRIPRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGEAWLFGQPVDPKDIDTRRRVGYMSQ 356
Cdd:cd03265 1 IEVENLVKKYGDFEAVRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATVAGHDVVREPREVRRRIGIVFQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 357 AFSLYNELTVRQNLELHARLFHIPEAEIPARVAEMSERFKLNDVEDILPESLPLGIRQRLSLAVAVIHRPEMLILDEPTS 436
Cdd:cd03265 81 DLSVDDELTGWENLYIHARLYGVPGAERRERIDELLDFVGLLEAADRLVKTYSGGMRRRLEIARSLVHRPEVLFLDEPTI 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 732682709 437 GVDPVARDMFWQLMVDLSRQDKVTIFISTHFMNEAER-CDRISLMHAGKVLASGTPQEL 494
Cdd:cd03265 161 GLDPQTRAHVWEYIEKLKEEFGMTILLTTHYMEEAEQlCDRVAIIDHGRIIAEGTPEEL 219
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
277-485 |
4.75e-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: 243.07 E-value: 4.75e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 277 IEARDLTMRFGSFVAVDHVNFRIPRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGEAWLFGQPVDPKDIDTRRRVGYMSQ 356
Cdd:cd03230 1 IEVRNLSKRYGKKTALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVLGKDIKKEPEEVKRRIGYLPE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 357 AFSLYNELTVRQNLElharlfhipeaeiparvaemserfklndvedilpesLPLGIRQRLSLAVAVIHRPEMLILDEPTS 436
Cdd:cd03230 81 EPSLYENLTVRENLK------------------------------------LSGGMKQRLALAQALLHDPELLILDEPTS 124
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 732682709 437 GVDPVARDMFWQLMVDLSRQDKvTIFISTHFMNEAER-CDRISLMHAGKV 485
Cdd:cd03230 125 GLDPESRREFWELLRELKKEGK-TILLSSHILEEAERlCDRVAILNNGRI 173
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
277-517 |
8.28e-75 |
|
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, Inorganic ion transport and metabolism];
Pssm-ID: 443618 [Multi-domain] Cd Length: 243 Bit Score: 245.15 E-value: 8.28e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 277 IEARDLTMRFGSFVAVDHVNFRIPRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGEAWLFGQPVDPKDIDTRRRVGYMSQ 356
Cdd:COG4555 2 IEVENLSKKYGKVPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIDGEDVRKEPREARRQIGVLPD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 357 AFSLYNELTVRQNLELHARLFHIPEAEIPARVAEMSERFKLNDVEDILPESLPLGIRQRLSLAVAVIHRPEMLILDEPTS 436
Cdd:COG4555 82 ERGLYDRLTVRENIRYFAELYGLFDEELKKRIEELIELLGLEEFLDRRVGELSTGMKKKVALARALVHDPKVLLLDEPTN 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 437 GVDPVARDMFWQLMVDLSRQDKvTIFISTHFMNEAER-CDRISLMHAGKVLASGTPQELVEKRGAASLEEAFIAYLQEAA 515
Cdd:COG4555 162 GLDVMARRLLREILRALKKEGK-TVLFSSHIMQEVEAlCDRVVILHKGKVVAQGSLDELREEIGEENLEDAFVALIGSEE 240
|
..
gi 732682709 516 GQ 517
Cdd:COG4555 241 GE 242
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
276-516 |
8.23e-71 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 236.16 E-value: 8.23e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 276 AIEARDLTMRFGSFVAVDHVNFRIPRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGEAWLFGQPVDPKDidtRRRVGYMS 355
Cdd:COG4152 1 MLELKGLTKRFGDKTAVDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDSGEVLWDGEPLDPED---RRRIGYLP 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 356 QAFSLYNELTVRQNLELHARLFHIPEAEIPARVAEMSERFKLNDVEDILPESLPLGIRQRLSLAVAVIHRPEMLILDEPT 435
Cdd:COG4152 78 EERGLYPKMKVGEQLVYLARLKGLSKAEAKRRADEWLERLGLGDRANKKVEELSKGNQQKVQLIAALLHDPELLILDEPF 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 436 SGVDPVARDMFWQLMVDLSRQDKVTIFiSTHFMNEAER-CDRISLMHAGKVLASGTPQELVEKRGAASLE---EAFIAYL 511
Cdd:COG4152 158 SGLDPVNVELLKDVIRELAAKGTTVIF-SSHQMELVEElCDRIVIINKGRKVLSGSVDEIRRQFGRNTLRleaDGDAGWL 236
|
....*
gi 732682709 512 QEAAG 516
Cdd:COG4152 237 RALPG 241
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
277-494 |
1.86e-70 |
|
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: 232.40 E-value: 1.86e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 277 IEARDLTMRFGS--FVAVDHVNFRIPRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGEAWLFGQPVDPKDIDTRRRVGYM 354
Cdd:cd03263 1 LQIRNLTKTYKKgtKPAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYINGYSIRTDRKAARQSLGYC 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 355 SQAFSLYNELTVRQNLELHARLFHIPEAEIPARVAEMSERFKLNDVEDILPESLPLGIRQRLSLAVAVIHRPEMLILDEP 434
Cdd:cd03263 81 PQFDALFDELTVREHLRFYARLKGLPKSEIKEEVELLLRVLGLTDKANKRARTLSGGMKRKLSLAIALIGGPSVLLLDEP 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 732682709 435 TSGVDPVARDMFWQLMVDLsRQDKvTIFISTHFMNEAER-CDRISLMHAGKVLASGTPQEL 494
Cdd:cd03263 161 TSGLDPASRRAIWDLILEV-RKGR-SIILTTHSMDEAEAlCDRIAIMSDGKLRCIGSPQEL 219
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
14-256 |
1.76e-61 |
|
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: 208.56 E-value: 1.76e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 14 QLAGVSQHYGKTVALNNITLDIPARCMVGLIGPDGVGKSSLLSLISGARVIEQGNVMVLGGDMR--DPKHRRdvcpRIAW 91
Cdd:COG4555 3 EVENLSKKYGKVPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIDGEDVRkePREARR----QIGV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 92 MPQGLGknLYHTLSVYENVDFFARLFGHDKAEREVRINELLTSTGLAPFRDRPAGKLSGGMKQKLGLCCALIHDPELLIL 171
Cdd:COG4555 79 LPDERG--LYDRLTVRENIRYFAELYGLFDEELKKRIEELIELLGLEEFLDRRVGELSTGMKKKVALARALVHDPKVLLL 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 172 DEPTTGVDPLSRSQFWDLIdsIRQRQSNMSVLVATAYMEEAER-FDWLVAMNAGEVLATGSAEELRQQTQSATLEEAFIN 250
Cdd:COG4555 157 DEPTNGLDVMARRLLREIL--RALKKEGKTVLFSSHIMQEVEAlCDRVVILHKGKVVAQGSLDELREEIGEENLEDAFVA 234
|
....*.
gi 732682709 251 LLPQAQ 256
Cdd:COG4555 235 LIGSEE 240
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
277-489 |
1.97e-59 |
|
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: 201.74 E-value: 1.97e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 277 IEARDLTMRFGSFVAVDHVNFRIPRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGEAWLFGQPVDpkdIDTRRRVGYMSQ 356
Cdd:cd03269 1 LEVENVTKRFGRVTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDGKPLD---IAARNRIGYLPE 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 357 AFSLYNELTVRQNLELHARLFHIPEAEIPARVAEMSERFKLNDVEDILPESLPLGIRQRLSLAVAVIHRPEMLILDEPTS 436
Cdd:cd03269 78 ERGLYPKMKVIDQLVYLAQLKGLKKEEARRRIDEWLERLELSEYANKRVEELSKGNQQKVQFIAAVIHDPELLILDEPFS 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 732682709 437 GVDPVARDMFWQLMVDLSRQDKvTIFISTHFMNEAER-CDRISLMHAGKVLASG 489
Cdd:cd03269 158 GLDPVNVELLKDVIRELARAGK-TVILSTHQMELVEElCDRVLLLNKGRAVLYG 210
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
14-226 |
8.45e-59 |
|
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: 198.39 E-value: 8.45e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 14 QLAGVSQHYGKTVALNNITLDIPARCMVGLIGPDGVGKSSLLSLISGARVIEQGNVMVLGGDMRdpKHRRDVCPRIAWMP 93
Cdd:cd03230 2 EVRNLSKRYGKKTALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVLGKDIK--KEPEEVKRRIGYLP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 94 QGLGknLYHTLSVYENVdffarlfghdkaerevrinelltstglapfrdrpagKLSGGMKQKLGLCCALIHDPELLILDE 173
Cdd:cd03230 80 EEPS--LYENLTVRENL------------------------------------KLSGGMKQRLALAQALLHDPELLILDE 121
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 732682709 174 PTTGVDPLSRSQFWDLIDSIRQRqsNMSVLVATAYMEEAER-FDWLVAMNAGEV 226
Cdd:cd03230 122 PTSGLDPESRREFWELLRELKKE--GKTILLSSHILEEAERlCDRVAILNNGRI 173
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
273-494 |
3.04e-58 |
|
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: 199.44 E-value: 3.04e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 273 AEIAIEARDLTMRFGSFVAVDHVNFRIPRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGEAWLFGQPVDPKDIDT----R 348
Cdd:COG1127 2 SEPMIEVRNLTKSFGDRVVLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEILVDGQDITGLSEKElyelR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 349 RRVGYMSQAFSLYNELTVRQNLEL----HARLfhiPEAEIPARVAEMSERFKLNDVEDILPESLPLGIRQRLSLAVAVIH 424
Cdd:COG1127 82 RRIGMLFQGGALFDSLTVFENVAFplreHTDL---SEAEIRELVLEKLELVGLPGAADKMPSELSGGMRKRVALARALAL 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 732682709 425 RPEMLILDEPTSGVDPVARDMFWQLMVDLSRQDKVTIFISTHFMNEAER-CDRISLMHAGKVLASGTPQEL 494
Cdd:COG1127 159 DPEILLYDEPTAGLDPITSAVIDELIRELRDELGLTSVVVTHDLDSAFAiADRVAVLADGKIIAEGTPEEL 229
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
277-498 |
1.27e-55 |
|
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: 191.78 E-value: 1.27e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 277 IEARDLTMRF-GSFVAVDHVNFRIPRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGEAWLFGQPVDPKDI-DTRRRVGYM 354
Cdd:COG1122 1 IELENLSFSYpGGTPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVDGKDITKKNLrELRRKVGLV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 355 -----SQAFslynELTVRQNLELHARLFHIPEAEIPARVAEMSERFKLNDVEDILPESLPLGIRQRLSLAVAVIHRPEML 429
Cdd:COG1122 81 fqnpdDQLF----APTVEEDVAFGPENLGLPREEIRERVEEALELVGLEHLADRPPHELSGGQKQRVAIAGVLAMEPEVL 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 430 ILDEPTSGVDPVARDMFWQLMVDLSRQDKvTIFISTHFMNEAER-CDRISLMHAGKVLASGTPQELVEKR 498
Cdd:COG1122 157 VLDEPTAGLDPRGRRELLELLKRLNKEGK-TVIIVTHDLDLVAElADRVIVLDDGRIVADGTPREVFSDY 225
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
277-489 |
9.09e-55 |
|
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: 188.58 E-value: 9.09e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 277 IEARDLTMRFGSFVAVDHVNFRIPRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGEAWLFGQPVDpKDIDTRRRVGYMSQ 356
Cdd:cd03268 1 LKTNDLTKTYGKKRVLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEITFDGKSYQ-KNIEALRRIGALIE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 357 AFSLYNELTVRQNLELHARLFHIPEaeipARVAEMSERFKLNDVEDILPESLPLGIRQRLSLAVAVIHRPEMLILDEPTS 436
Cdd:cd03268 80 APGFYPNLTARENLRLLARLLGIRK----KRIDEVLDVVGLKDSAKKKVKGFSLGMKQRLGIALALLGNPDLLILDEPTN 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 732682709 437 GVDPVARDMFWQLMVDLSRQDKvTIFISTHFMNEAER-CDRISLMHAGKVLASG 489
Cdd:cd03268 156 GLDPDGIKELRELILSLRDQGI-TVLISSHLLSEIQKvADRIGIINKGKLIEEG 208
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
14-236 |
3.09e-54 |
|
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: 187.71 E-value: 3.09e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 14 QLAGVSQHYGK--TVALNNITLDIPARCMVGLIGPDGVGKSSLLSLISGARVIEQGNVMVLGGDMRdpKHRRDVCPRIAW 91
Cdd:cd03263 2 QIRNLTKTYKKgtKPAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYINGYSIR--TDRKAARQSLGY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 92 MPQGlgKNLYHTLSVYENVDFFARLFGHDKAEREVRINELLTSTGLAPFRDRPAGKLSGGMKQKLGLCCALIHDPELLIL 171
Cdd:cd03263 80 CPQF--DALFDELTVREHLRFYARLKGLPKSEIKEEVELLLRVLGLTDKANKRARTLSGGMKRKLSLAIALIGGPSVLLL 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 732682709 172 DEPTTGVDPLSRSQFWDLIDSIRQrqsNMSVLVATAYMEEAERF-DWLVAMNAGEVLATGSAEELR 236
Cdd:cd03263 158 DEPTSGLDPASRRAIWDLILEVRK---GRSIILTTHSMDEAEALcDRIAIMSDGKLRCIGSPQELK 220
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
273-493 |
2.44e-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: 186.40 E-value: 2.44e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 273 AEIAIEARDLTMRFGSFVAVDHVNFRIPRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGEAWLFGQPVDPKDIDTRRRVG 352
Cdd:COG0411 1 SDPLLEVRGLTKRFGGLVAVDDVSLEVERGEIVGLIGPNGAGKTTLFNLITGFYRPTSGRILFDGRDITGLPPHRIARLG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 353 yMSQAF---SLYNELTVRQNLEL--HAR--------LFHIP-----EAEIPARVAEMSERFKLNDVEDILPESLPLGIRQ 414
Cdd:COG0411 81 -IARTFqnpRLFPELTVLENVLVaaHARlgrgllaaLLRLPrarreEREARERAEELLERVGLADRADEPAGNLSYGQQR 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 415 RLSLAVAVIHRPEMLILDEPTSGVDPVARDMFWQLMVDLSRQDKVTIFISTHFMNEAER-CDRISLMHAGKVLASGTPQE 493
Cdd:COG0411 160 RLEIARALATEPKLLLLDEPAAGLNPEETEELAELIRRLRDERGITILLIEHDMDLVMGlADRIVVLDFGRVIAEGTPAE 239
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
277-494 |
3.96e-53 |
|
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: 185.01 E-value: 3.96e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 277 IEARDLTMRFGSFVAVDHVNFRIPRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGEAWLFGQPVDP----KDIDTRRRVG 352
Cdd:cd03261 1 IELRGLTKSFGGRTVLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGEDISGlseaELYRLRRRMG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 353 YMSQAFSLYNELTVRQNLEL----HARLfhiPEAEIPARVAEMSERFKLNDVEDILPESLPLGIRQRLSLAVAVIHRPEM 428
Cdd:cd03261 81 MLFQSGALFDSLTVFENVAFplreHTRL---SEEEIREIVLEKLEAVGLRGAEDLYPAELSGGMKKRVALARALALDPEL 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 732682709 429 LILDEPTSGVDPVARDMFWQLMVDLSRQDKVTIFISTHFMNEAER-CDRISLMHAGKVLASGTPQEL 494
Cdd:cd03261 158 LLYDEPTAGLDPIASGVIDDLIRSLKKELGLTSIMVTHDLDTAFAiADRIAVLYDGKIVAEGTPEEL 224
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
277-489 |
3.98e-53 |
|
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: 184.49 E-value: 3.98e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 277 IEARDLTMRF----GSFVAVDHVNFRIPRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGEAWLFGQPVDPKDIDTRRRVG 352
Cdd:cd03266 2 ITADALTKRFrdvkKTVQAVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDGFDVVKEPAEARRRLG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 353 YMSQAFSLYNELTVRQNLELHARLFHIPEAEIPARVAEMSERFKLNDVEDILPESLPLGIRQRLSLAVAVIHRPEMLILD 432
Cdd:cd03266 82 FVSDSTGLYDRLTARENLEYFAGLYGLKGDELTARLEELADRLGMEELLDRRVGGFSTGMRQKVAIARALVHDPPVLLLD 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 732682709 433 EPTSGVDPVARDMFWQLMVDLSRQDKVTIFiSTHFMNEAER-CDRISLMHAGKVLASG 489
Cdd:cd03266 162 EPTTGLDVMATRALREFIRQLRALGKCILF-STHIMQEVERlCDRVVVLHRGRVVYEG 218
|
|
| drrA |
TIGR01188 |
daunorubicin resistance ABC transporter ATP-binding subunit; This model describes daunorubicin ... |
20-245 |
2.41e-51 |
|
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: 182.59 E-value: 2.41e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 20 QHYGKTVALNNITLDIPARCMVGLIGPDGVGKSSLLSLISGARVIEQGNVMVLGGDM-RDPkhrRDVCPRIAWMPQGlgK 98
Cdd:TIGR01188 1 KVYGDFKAVDGVNFKVREGEVFGFLGPNGAGKTTTIRMLTTLLRPTSGTARVAGYDVvREP---RKVRRSIGIVPQY--A 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 99 NLYHTLSVYENVDFFARLFGHDKAEREVRINELLTSTGLAPFRDRPAGKLSGGMKQKLGLCCALIHDPELLILDEPTTGV 178
Cdd:TIGR01188 76 SVDEDLTGRENLEMMGRLYGLPKDEAEERAEELLELFELGEAADRPVGTYSGGMRRRLDIAASLIHQPDVLFLDEPTTGL 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 732682709 179 DPLSRSQFWDLIDSIrqRQSNMSVLVATAYMEEAERF-DWLVAMNAGEVLATGSAEELRQQTQSATLE 245
Cdd:TIGR01188 156 DPRTRRAIWDYIRAL--KEEGVTILLTTHYMEEADKLcDRIAIIDHGRIIAEGTPEELKRRLGKDTLE 221
|
|
| PQQ_ABC_ATP |
TIGR03864 |
ABC transporter, ATP-binding subunit, PQQ-dependent alcohol dehydrogenase system; Members of ... |
276-509 |
4.74e-51 |
|
ABC transporter, ATP-binding subunit, PQQ-dependent alcohol dehydrogenase system; Members of this protein family are the ATP-binding subunit of an ABC transporter system that is associated with PQQ biosynthesis and PQQ-dependent alcohol dehydrogenases. While this family shows homology to several efflux ABC transporter subunits, the presence of a periplasmic substrate-binding protein and association with systems for catabolism of alcohols suggests a role in import rather than detoxification. [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 274822 [Multi-domain] Cd Length: 236 Bit Score: 179.41 E-value: 4.74e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 276 AIEARDLTMRFGSFVAVDHVNFRIPRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGEAWLFGQPVDPKDIDTRRRVGYMS 355
Cdd:TIGR03864 1 ALEVAGLSFRYGARRALDDVSFTVRPGRFVALLGPNGAGKSTLFSLLTRLYVAQSGQISVAGHDLRRAPRAALARLGVVF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 356 QAFSLYNELTVRQNLELHARLFHIPEAEIPARVAEMSERFKLNDVEDILPESLPLGIRQRLSLAVAVIHRPEMLILDEPT 435
Cdd:TIGR03864 81 QQPTLDLDLSVRQNLRYHAALHGLSRAEARARIAELLARLGLAERADDKVRELNGGHRRRVEIARALLHRPALLLLDEPT 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 732682709 436 SGVDPVARDMFWQLMVDLSRQDKVTIFISTHFMNEAERCDRISLMHAGKVLASGTPQELVEKRGAASLEEAFIA 509
Cdd:TIGR03864 161 VGLDPASRAAITAHVRALARDQGLSVLWATHLVDEIEASDRLVVLHRGRVLADGAAAELRGATGGADLEAAFLA 234
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
277-493 |
2.21e-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: 177.24 E-value: 2.21e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 277 IEARDLTMRFGSFVAVDHVNFRIPRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGEAWLFGQPVDPKDIDTRRRVGyMSQ 356
Cdd:cd03219 1 LEVRGLTKRFGGLVALDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFDGEDITGLPPHEIARLG-IGR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 357 AF---SLYNELTVRQNLEL--HARLFHIP--------EAEIPARVAEMSERFKLNDVEDILPESLPLGIRQRLSLAVAVI 423
Cdd:cd03219 80 TFqipRLFPELTVLENVMVaaQARTGSGLllararreEREARERAEELLERVGLADLADRPAGELSYGQQRRLEIARALA 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 732682709 424 HRPEMLILDEPTSGVDPVARDMFWQLMVDLSRQDkVTIFISTHFMNEAER-CDRISLMHAGKVLASGTPQE 493
Cdd:cd03219 160 TDPKLLLLDEPAAGLNPEETEELAELIRELRERG-ITVLLVEHDMDVVMSlADRVTVLDQGRVIAEGTPDE 229
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
276-496 |
9.43e-50 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 178.08 E-value: 9.43e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 276 AIEARDLTMRFGSFVAVDHVNFRIPRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGEAWLFGQPVDPKDIDTRRRVGYMS 355
Cdd:PRK13537 7 PIDFRNVEKRYGDKLVVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCGEPVPSRARHARQRVGVVP 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 356 QAFSLYNELTVRQNLELHARLFHIPEAEIPARVAEMSERFKLNDVEDILPESLPLGIRQRLSLAVAVIHRPEMLILDEPT 435
Cdd:PRK13537 87 QFDNLDPDFTVRENLLVFGRYFGLSAAAARALVPPLLEFAKLENKADAKVGELSGGMKRRLTLARALVNDPDVLVLDEPT 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 732682709 436 SGVDPVARDMFWQLMVDLSRQDKvTIFISTHFMNEAER-CDRISLMHAGKVLASGTPQELVE 496
Cdd:PRK13537 167 TGLDPQARHLMWERLRSLLARGK-TILLTTHFMEEAERlCDRLCVIEEGRKIAEGAPHALIE 227
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
22-236 |
1.25e-49 |
|
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein component of a bacterial exporter complex that confers resistance to the antibiotics daunorubicin and doxorubicin. In addition to DrrA, the complex includes an integral membrane protein called DrrB. DrrA belongs to the ABC family of transporters and shares sequence and functional similarities with a protein found in cancer cells called P-glycoprotein. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region in addition to the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213232 [Multi-domain] Cd Length: 220 Bit Score: 174.87 E-value: 1.25e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 22 YGKTVALNNITLDIPARCMVGLIGPDGVGKSSLLSLISGARVIEQGNVMVLGGDM-RDPkhrRDVCPRIAWMPQGLgkNL 100
Cdd:cd03265 10 YGDFEAVRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATVAGHDVvREP---REVRRRIGIVFQDL--SV 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 101 YHTLSVYENVDFFARLFGHDKAEREVRINELLTSTGLAPFRDRPAGKLSGGMKQKLGLCCALIHDPELLILDEPTTGVDP 180
Cdd:cd03265 85 DDELTGWENLYIHARLYGVPGAERRERIDELLDFVGLLEAADRLVKTYSGGMRRRLEIARSLVHRPEVLFLDEPTIGLDP 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 732682709 181 LSRSQFWDLIDSIrQRQSNMSVLVATAYMEEAERF-DWLVAMNAGEVLATGSAEELR 236
Cdd:cd03265 165 QTRAHVWEYIEKL-KEEFGMTILLTTHYMEEAEQLcDRVAIIDHGRIIAEGTPEELK 220
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
249-497 |
1.56e-49 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 178.49 E-value: 1.56e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 249 INLLPQAQRQAHQAVVIPPYQPENAEIAIEARDLTMRFGSFVAVDHVNFRIPRGEIFGFLGSNGCGKSTTMKMLTGLLPA 328
Cdd:PRK13536 14 LELSPIERKHQGISEAKASIPGSMSTVAIDLAGVSKSYGDKAVVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSP 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 329 SEGEAWLFGQPVDPKDIDTRRRVGYMSQAFSLYNELTVRQNLELHARLFHIPEAEIPARVAEMSERFKLNDVEDILPESL 408
Cdd:PRK13536 94 DAGKITVLGVPVPARARLARARIGVVPQFDNLDLEFTVRENLLVFGRYFGMSTREIEAVIPSLLEFARLESKADARVSDL 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 409 PLGIRQRLSLAVAVIHRPEMLILDEPTSGVDPVARDMFWQLMVDLSRQDKvTIFISTHFMNEAER-CDRISLMHAGKVLA 487
Cdd:PRK13536 174 SGGMKRRLTLARALINDPQLLILDEPTTGLDPHARHLIWERLRSLLARGK-TILLTTHFMEEAERlCDRLCVLEAGRKIA 252
|
250
....*....|
gi 732682709 488 SGTPQELVEK 497
Cdd:PRK13536 253 EGRPHALIDE 262
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
277-485 |
2.49e-49 |
|
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: 173.83 E-value: 2.49e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 277 IEARDLTMRFGS----FVAVDHVNFRIPRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGEAWLFGQPV---DPKDIDT-- 347
Cdd:cd03255 1 IELKNLSKTYGGggekVQALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRVDGTDIsklSEKELAAfr 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 348 RRRVGYMSQAFSLYNELTVRQNLELHARLFHIPEAEIPARVAEMSERFKLNDVEDILPESLPLGIRQRLSLAVAVIHRPE 427
Cdd:cd03255 81 RRHIGFVFQSFNLLPDLTALENVELPLLLAGVPKKERRERAEELLERVGLGDRLNHYPSELSGGQQQRVAIARALANDPK 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 732682709 428 MLILDEPTSGVDPVARDMFWQLMVDLSRQDKVTIFISTHFMNEAERCDRISLMHAGKV 485
Cdd:cd03255 161 IILADEPTGNLDSETGKEVMELLRELNKEAGTTIVVVTHDPELAEYADRIIELRDGKI 218
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
277-489 |
3.03e-49 |
|
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: 173.15 E-value: 3.03e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 277 IEARDLTMRFGSFVAVDHVNFRIPRGeIFGFLGSNGCGKSTTMKMLTGLLPASEGEAWLFGQPVDPKDIDTRRRVGYMSQ 356
Cdd:cd03264 1 LQLENLTKRYGKKRALDGVSLTLGPG-MYGLLGPNGAGKTTLMRILATLTPPSSGTIRIDGQDVLKQPQKLRRRIGYLPQ 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 357 AFSLYNELTVRQNLELHARLFHIPEAEIPARVAEMSERFKLNDVEDILPESLPLGIRQRLSLAVAVIHRPEMLILDEPTS 436
Cdd:cd03264 80 EFGVYPNFTVREFLDYIAWLKGIPSKEVKARVDEVLELVNLGDRAKKKIGSLSGGMRRRVGIAQALVGDPSILIVDEPTA 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 732682709 437 GVDPVARDMFWQLMVDLSrQDKVTIfISTHFMNEAER-CDRISLMHAGKVLASG 489
Cdd:cd03264 160 GLDPEERIRFRNLLSELG-EDRIVI-LSTHIVEDVESlCNQVAVLNKGKLVFEG 211
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
273-598 |
1.49e-48 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 176.06 E-value: 1.49e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 273 AEIAIEARDLTMRFGSFVAVDHVNFRIPRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGEAWLFGQPVDpkdiDT---RR 349
Cdd:COG3842 2 AMPALELENVSKRYGDVTALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRILLDGRDVT----GLppeKR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 350 RVGYMSQAFSLYNELTVRQNLELHARLFHIPEAEIPARVAEMSERFKLNDVEDILPESLPLGIRQRLSLAVAVIHRPEML 429
Cdd:COG3842 78 NVGMVFQDYALFPHLTVAENVAFGLRMRGVPKAEIRARVAELLELVGLEGLADRYPHQLSGGQQQRVALARALAPEPRVL 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 430 ILDEPTSGVDPVARDMFWQLMVDLSRQDKVTIFISTHFMNEAER-CDRISLMHAGKVLASGTPQELVEK---RGAASlee 505
Cdd:COG3842 158 LLDEPLSALDAKLREEMREELRRLQRELGITFIYVTHDQEEALAlADRIAVMNDGRIEQVGTPEEIYERpatRFVAD--- 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 506 aFIaylqeaaGQSN--EAEAPPVVHDTTHAPRQGFSLRRLFSYS---------RREALELRRDPVRSTL-------ALMG 567
Cdd:COG3842 235 -FI-------GEANllPGTVLGDEGGGVRTGGRTLEVPADAGLAaggpvtvaiRPEDIRLSPEGPENGLpgtvedvVFLG 306
|
330 340 350
....*....|....*....|....*....|....
gi 732682709 568 TVILMLI---MGYGISMDVENLRFAVLDRDQTVS 598
Cdd:COG3842 307 SHVRYRVrlgDGQELVVRVPNRAALPLEPGDRVG 340
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
273-483 |
2.12e-48 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 172.58 E-value: 2.12e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 273 AEIAIEARDLTMRF----GSFVAVDHVNFRIPRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGEAWLFGQPVDPKDidtr 348
Cdd:COG1116 4 AAPALELRGVSKRFptggGGVTALDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPTSGEVLVDGKPVTGPG---- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 349 RRVGYMSQAFSLYNELTVRQNLELHARLFHIPEAEIPARVAEMSERFKLNDVEDILPESLPLGIRQRLSLAVAVIHRPEM 428
Cdd:COG1116 80 PDRGVVFQEPALLPWLTVLDNVALGLELRGVPKAERRERARELLELVGLAGFEDAYPHQLSGGMRQRVAIARALANDPEV 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 732682709 429 LILDEPTSGVDPVARDMFWQLMVDLSRQDKVTIFISTHFMNEAER-CDRISLMHAG 483
Cdd:COG1116 160 LLMDEPFGALDALTRERLQDELLRLWQETGKTVLFVTHDVDEAVFlADRVVVLSAR 215
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
278-484 |
1.51e-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: 168.41 E-value: 1.51e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 278 EARDLTMRFGSF--VAVDHVNFRIPRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGEAWLFGQPVDPKDI-DTRRRVGYM 354
Cdd:cd03225 1 ELKNLSFSYPDGarPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDLTKLSLkELRRKVGLV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 355 -----SQAFslynELTVRQNLELHARLFHIPEAEIPARVAEMSERFKLNDVEDILPESLPLGIRQRLSLAVAVIHRPEML 429
Cdd:cd03225 81 fqnpdDQFF----GPTVEEEVAFGLENLGLPEEEIEERVEEALELVGLEGLRDRSPFTLSGGQKQRVAIAGVLAMDPDIL 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 732682709 430 ILDEPTSGVDPVARDMFWQLMVDLSRQDKvTIFISTHFMNEAER-CDRISLMHAGK 484
Cdd:cd03225 157 LLDEPTAGLDPAGRRELLELLKKLKAEGK-TIIIVTHDLDLLLElADRVIVLEDGK 211
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
277-489 |
2.15e-47 |
|
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: 168.08 E-value: 2.15e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 277 IEARDLTMRFGSFVAVDHVNFRIPRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGEAWLFGQPVDPKDIDtRRRVGYMSQ 356
Cdd:cd03259 1 LELKGLSKTYGSVRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDGRDVTGVPPE-RRNIGMVFQ 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 357 AFSLYNELTVRQNLELHARLFHIPEAEIPARVAEMSERFKLNDVEDILPESLPLGIRQRLSLAVAVIHRPEMLILDEPTS 436
Cdd:cd03259 80 DYALFPHLTVAENIAFGLKLRGVPKAEIRARVRELLELVGLEGLLNRYPHELSGGQQQRVALARALAREPSLLLLDEPLS 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 732682709 437 GVDPVARDMFWQLMVDLSRQDKVTIFISTHFMNEAER-CDRISLMHAGKVLASG 489
Cdd:cd03259 160 ALDAKLREELREELKELQRELGITTIYVTHDQEEALAlADRIAVMNEGRIVQVG 213
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
276-500 |
6.03e-46 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 167.96 E-value: 6.03e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 276 AIEARDLTMRF----------GSF-----------VAVDHVNFRIPRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGEAW 334
Cdd:COG4586 1 IIEVENLSKTYrvyekepglkGALkglfrreyrevEAVDDISFTIEPGEIVGFIGPNGAGKSTTIKMLTGILVPTSGEVR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 335 LFGqpVDP--KDIDTRRRVGY-MSQAFSLYNELTVRQNLELHARLFHIPEAEIPARVAEMSERFKLNDVEDILPESLPLG 411
Cdd:COG4586 81 VLG--YVPfkRRKEFARRIGVvFGQRSQLWWDLPAIDSFRLLKAIYRIPDAEYKKRLDELVELLDLGELLDTPVRQLSLG 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 412 IRQRLSLAVAVIHRPEMLILDEPTSGVDPVARDMFWQLMVDLSRQDKVTIFISTHFMNEAER-CDRISLMHAGKVLASGT 490
Cdd:COG4586 159 QRMRCELAAALLHRPKILFLDEPTIGLDVVSKEAIREFLKEYNRERGTTILLTSHDMDDIEAlCDRVIVIDHGRIIYDGS 238
|
250
....*....|
gi 732682709 491 PQELVEKRGA 500
Cdd:COG4586 239 LEELKERFGP 248
|
|
| YadH |
COG0842 |
ABC-type multidrug transport system, permease component [Defense mechanisms]; |
713-910 |
6.84e-46 |
|
ABC-type multidrug transport system, permease component [Defense mechanisms];
Pssm-ID: 440604 [Multi-domain] Cd Length: 200 Bit Score: 163.45 E-value: 6.84e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 713 SLPAIVPAVIPLLLMMIPSMLSALSVVREKELGSIINLYVTPTTRSEFLLGKQLPYIALGMLNFFLLCGLSVFVFGVPHK 792
Cdd:COG0842 1 YLAFLVPGLLAMSLLFTALMLTALSIAREREQGTLERLLVTPVSRLEILLGKVLAYLLRGLLQALLVLLVALLFFGVPLR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 793 G-SFLTLTLAALLYIIIATGMGLLISTFMKSQIAAIFGTAIItLIPATQFSGMIDPVASLEGPGRWIGEVYPTSHFLTIA 871
Cdd:COG0842 81 GlSLLLLLLVLLLFALAFSGLGLLISTLARSQEQASAISNLV-ILPLTFLSGAFFPIESLPGWLQAIAYLNPLTYFVEAL 159
|
170 180 190
....*....|....*....|....*....|....*....
gi 732682709 872 RGTFSKALDLTDLWQLFIPLLIAIPLVMGLSILLLKKQE 910
Cdd:COG0842 160 RALFLGGAGLADVWPSLLVLLAFAVVLLALALRLFRRRL 198
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
274-487 |
7.94e-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: 7.94e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 274 EIAIEARDLTMRFGS----FVAVDHVNFRIPRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGEAWLFGQPV---DPKDID 346
Cdd:COG1136 2 SPLLELRNLTKSYGTgegeVTALRGVSLSIEAGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVLIDGQDIsslSERELA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 347 T--RRRVGYMSQAFSLYNELTVRQNLELHARLFHIPEAEIPARVAEMSERFKLNDVEDILPESLPLGIRQRLSLAVAVIH 424
Cdd:COG1136 82 RlrRRHIGFVFQFFNLLPELTALENVALPLLLAGVSRKERRERARELLERVGLGDRLDHRPSQLSGGQQQRVAIARALVN 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 732682709 425 RPEMLILDEPTSGVDPVARDMFWQLMVDLSRQDKVTIFISTHFMNEAERCDRISLMHAGKVLA 487
Cdd:COG1136 162 RPKLILADEPTGNLDSKTGEEVLELLRELNRELGTTIVMVTHDPELAARADRVIRLRDGRIVS 224
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
277-487 |
1.02e-45 |
|
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ATP-binding subunits of the bacterial ABC-type nitrate and sulfonate transport systems, respectively. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213260 [Multi-domain] Cd Length: 220 Bit Score: 163.41 E-value: 1.02e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 277 IEARDLTMRFGS----FVAVDHVNFRIPRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGEAWLFGQPVDpkdiDTRRRVG 352
Cdd:cd03293 1 LEVRNVSKTYGGgggaVTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVDGEPVT----GPGPDRG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 353 YMSQAFSLYNELTVRQNLELHARLFHIPEAEIPARVAEMSERFKLNDVEDILPESLPLGIRQRLSLAVAVIHRPEMLILD 432
Cdd:cd03293 77 YVFQQDALLPWLTVLDNVALGLELQGVPKAEARERAEELLELVGLSGFENAYPHQLSGGMRQRVALARALAVDPDVLLLD 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 732682709 433 EPTSGVDPVARDMFWQLMVDLSRQDKVTIFISTHFMNEAER-CDRISLMHA--GKVLA 487
Cdd:cd03293 157 EPFSALDALTREQLQEELLDIWRETGKTVLLVTHDIDEAVFlADRVVVLSArpGRIVA 214
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
14-230 |
3.76e-45 |
|
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: 161.59 E-value: 3.76e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 14 QLAGVSQHYGKTVALNNITLDIPARcMVGLIGPDGVGKSSLLSLISGARVIEQGNVMVLGGDmrDPKHRRDVCPRIAWMP 93
Cdd:cd03264 2 QLENLTKRYGKKRALDGVSLTLGPG-MYGLLGPNGAGKTTLMRILATLTPPSSGTIRIDGQD--VLKQPQKLRRRIGYLP 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 94 QGLGknLYHTLSVYENVDFFARLFGHDKAEREVRINELLTSTGLAPFRDRPAGKLSGGMKQKLGLCCALIHDPELLILDE 173
Cdd:cd03264 79 QEFG--VYPNFTVREFLDYIAWLKGIPSKEVKARVDEVLELVNLGDRAKKKIGSLSGGMRRRVGIAQALVGDPSILIVDE 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 732682709 174 PTTGVDPLSRSQFWDLIDSIrqrQSNMSVLVATAYMEEAERF-DWLVAMNAGEVLATG 230
Cdd:cd03264 157 PTAGLDPEERIRFRNLLSEL---GEDRIVILSTHIVEDVESLcNQVAVLNKGKLVFEG 211
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
10-521 |
3.88e-45 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 170.20 E-value: 3.88e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 10 PPVAQLAGVSQHYGKTVALNNITLDIPARCMVGLIGPDGVGKSSLLSLISGARVIEQGnVMVLGG---DMRDPKHRRDVc 86
Cdd:COG1129 2 EPLLEMRGISKSFGGVKALDGVSLELRPGEVHALLGENGAGKSTLMKILSGVYQPDSG-EILLDGepvRFRSPRDAQAA- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 87 pRIAWMPQGLgkNLYHTLSVYENVdFFARLFGH----DKAEREVRINELLTSTGLA--PfrDRPAGKLSGGMKQKLGLCC 160
Cdd:COG1129 80 -GIAIIHQEL--NLVPNLSVAENI-FLGREPRRggliDWRAMRRRARELLARLGLDidP--DTPVGDLSVAQQQLVEIAR 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 161 ALIHDPELLILDEPTTgvdPLSRSQFWDLIDSIRQ-RQSNMSVLVATAYMEEAERF-DWLVAMNAGEVLATGSAEELrqq 238
Cdd:COG1129 154 ALSRDARVLILDEPTA---SLTEREVERLFRIIRRlKAQGVAIIYISHRLDEVFEIaDRVTVLRDGRLVGTGPVAEL--- 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 239 TQSA--------TLEEAFinllpqaqrqahqavviPPYQPENAEIAIEARDLTMRfgsfVAVDHVNFRIPRGEIFGFLGS 310
Cdd:COG1129 228 TEDElvrlmvgrELEDLF-----------------PKRAAAPGEVVLEVEGLSVG----GVVRDVSFSVRAGEILGIAGL 286
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 311 NGCGKSTTMKMLTGLLPASEGEAWLFGQPVDPKDIDT--RRRVGYMS---QAFSLYNELTVRQN-----LELHARLFHIP 380
Cdd:COG1129 287 VGAGRTELARALFGADPADSGEIRLDGKPVRIRSPRDaiRAGIAYVPedrKGEGLVLDLSIRENitlasLDRLSRGGLLD 366
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 381 EAEIPARVAEMSERF--KLNDVEDILpESLPLGIRQRLSLAVAVIHRPEMLILDEPTSGVDPVARDMFWQLMVDLSRQDK 458
Cdd:COG1129 367 RRRERALAEEYIKRLriKTPSPEQPV-GNLSGGNQQKVVLAKWLATDPKVLILDEPTRGIDVGAKAEIYRLIRELAAEGK 445
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 732682709 459 VTIFISTHfMNEAER-CDRISLMHAGKVLAsgtpqELveKRGAASlEEAFIAYlqeAAGQSNEA 521
Cdd:COG1129 446 AVIVISSE-LPELLGlSDRILVMREGRIVG-----EL--DREEAT-EEAIMAA---ATGGAAAA 497
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
14-235 |
4.21e-45 |
|
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and metabolism, General function prediction only];
Pssm-ID: 440739 [Multi-domain] Cd Length: 230 Bit Score: 162.12 E-value: 4.21e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 14 QLAGVSQHY-GKTVALNNITLDIPARCMVGLIGPDGVGKSSLLSLISGARVIEQGNVMVLGGDMRDpKHRRDVCPRIAWM 92
Cdd:COG1122 2 ELENLSFSYpGGTPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVDGKDITK-KNLRELRRKVGLV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 93 PQglgkN----LYHTlSVYENVDFFARLFGHDKAEREVRINELLTSTGLAPFRDRPAGKLSGGMKQKLGLCCALIHDPEL 168
Cdd:COG1122 81 FQ----NpddqLFAP-TVEEDVAFGPENLGLPREEIRERVEEALELVGLEHLADRPPHELSGGQKQRVAIAGVLAMEPEV 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 732682709 169 LILDEPTTGVDPLSRSQFWDLIDSIRQRqsNMSVLVATAYMEEAER-FDWLVAMNAGEVLATGSAEEL 235
Cdd:COG1122 156 LVLDEPTAGLDPRGRRELLELLKRLNKE--GKTVIIVTHDLDLVAElADRVIVLDDGRIVADGTPREV 221
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
14-238 |
6.01e-45 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 164.13 E-value: 6.01e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 14 QLAGVSQHYGKTVALNNITLDIPARCMVGLIGPDGVGKSSLLSLISGarVIE--QGNVMVLGGDMrDPKHRRdvcpRIAW 91
Cdd:COG4152 3 ELKGLTKRFGDKTAVDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILG--ILApdSGEVLWDGEPL-DPEDRR----RIGY 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 92 MPQGLGknLYHTLSVYENVDFFARLFGHDKAEREVRINELLTSTGLAPFRDRPAGKLSGGMKQKLGLCCALIHDPELLIL 171
Cdd:COG4152 76 LPEERG--LYPKMKVGEQLVYLARLKGLSKAEAKRRADEWLERLGLGDRANKKVEELSKGNQQKVQLIAALLHDPELLIL 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 732682709 172 DEPTTGVDPLSRSQFWDLIdsIRQRQSNMSVLVATAYMEEAERF-DWLVAMNAGEVLATGSAEELRQQ 238
Cdd:COG4152 154 DEPFSGLDPVNVELLKDVI--RELAAKGTTVIFSSHQMELVEELcDRIVIINKGRKVLSGSVDEIRRQ 219
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
276-507 |
7.92e-45 |
|
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: 162.14 E-value: 7.92e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 276 AIEARDLTMRFGSFVAVDHVNFRIPRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGEAWLFGQPV---DPKDIdtRRRVG 352
Cdd:COG1120 1 MLEAENLSVGYGGRPVLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDGRDLaslSRREL--ARRIA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 353 YMSQAFSLYNELTVRQNLEL----HARLFHIPEAEIPARVAEMSERFKLNDVEDILPESLPLGIRQRLSLAVAVIHRPEM 428
Cdd:COG1120 79 YVPQEPPAPFGLTVRELVALgrypHLGLFGRPSAEDREAVEEALERTGLEHLADRPVDELSGGERQRVLIARALAQEPPL 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 429 LILDEPTSGVDPVARDMFWQLMVDLSRQDKVTIFISTHFMNEAER-CDRISLMHAGKVLASGTPQELVEkrgAASLEEAF 507
Cdd:COG1120 159 LLLDEPTSHLDLAHQLEVLELLRRLARERGRTVVMVLHDLNLAARyADRLVLLKDGRIVAQGPPEEVLT---PELLEEVY 235
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
272-496 |
1.01e-44 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 169.05 E-value: 1.01e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 272 NAEIAIEARDLTMRFGSFVAVDHVNFRIPRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGEAWLFGQPV---DPKD-Idt 347
Cdd:COG3845 1 MMPPALELRGITKRFGGVVANDDVSLTVRPGEIHALLGENGAGKSTLMKILYGLYQPDSGEILIDGKPVrirSPRDaI-- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 348 RRRVGYMSQAFSLYNELTVRQNLEL---HARLFHIPEAEIPARVAEMSERFKLnDVE-DILPESLPLGIRQRLSLAVAVI 423
Cdd:COG3845 79 ALGIGMVHQHFMLVPNLTVAENIVLglePTKGGRLDRKAARARIRELSERYGL-DVDpDAKVEDLSVGEQQRVEILKALY 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 732682709 424 HRPEMLILDEPTSGVDPVARDMFWQLMVDLSRQDKVTIFIsTHFMNEAER-CDRISLMHAGKVLASG-----TPQELVE 496
Cdd:COG3845 158 RGARILILDEPTAVLTPQEADELFEILRRLAAEGKSIIFI-THKLREVMAiADRVTVLRRGKVVGTVdtaetSEEELAE 235
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
20-494 |
6.59e-44 |
|
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: 167.55 E-value: 6.59e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 20 QHYGKTVALNNITLDIPARCMVGLIGPDGVGKS----SLLSLISGARVIEQGNVMVLGGDMR--DPKHRRDVC-PRIAwM 92
Cdd:COG4172 18 QGGGTVEAVKGVSFDIAAGETLALVGESGSGKSvtalSILRLLPDPAAHPSGSILFDGQDLLglSERELRRIRgNRIA-M 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 93 ----------P-QGLGKNLYHTLSVYEnvdffarlfGHDKAEREVRINELLTSTGLapfrDRPAGK-------LSGGMKQ 154
Cdd:COG4172 97 ifqepmtslnPlHTIGKQIAEVLRLHR---------GLSGAAARARALELLERVGI----PDPERRldayphqLSGGQRQ 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 155 KLGLCCALIHDPELLILDEPTTGVDPLSRSQFWDLIDSIrQRQSNMSVLVATAYMEEAERF-DWLVAMNAGEVLATGSAE 233
Cdd:COG4172 164 RVMIAMALANEPDLLIADEPTTALDVTVQAQILDLLKDL-QRELGMALLLITHDLGVVRRFaDRVAVMRQGEIVEQGPTA 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 234 ELRQQTQSA-TLEeafinLLpqaqrqAHQAVVIPPYQPENAEIAIEARDLTMRF-----------GSFVAVDHVNFRIPR 301
Cdd:COG4172 243 ELFAAPQHPyTRK-----LL------AAEPRGDPRPVPPDAPPLLEARDLKVWFpikrglfrrtvGHVKAVDGVSLTLRR 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 302 GEIFGFLGSNGCGKSTTMKMLTGLLPaSEGEAWLFGQPVDPKDIDT----RRRVgymsQA-F-----SLYNELTVRQ--- 368
Cdd:COG4172 312 GETLGLVGESGSGKSTLGLALLRLIP-SEGEIRFDGQDLDGLSRRAlrplRRRM----QVvFqdpfgSLSPRMTVGQiia 386
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 369 -NLELHARlfHIPEAEIPARVAEMserfkLNDVEdiLPESLPL--------GIRQRLSLAVAVIHRPEMLILDEPTSgvd 439
Cdd:COG4172 387 eGLRVHGP--GLSAAERRARVAEA-----LEEVG--LDPAARHryphefsgGQRQRIAIARALILEPKLLVLDEPTS--- 454
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 732682709 440 pvARDMFWQ-----LMVDLSRQDKVT-IFIStH------FMneaerCDRISLMHAGKVLASGTPQEL 494
Cdd:COG4172 455 --ALDVSVQaqildLLRDLQREHGLAyLFIS-HdlavvrAL-----AHRVMVMKDGKVVEQGPTEQV 513
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
277-494 |
2.10e-43 |
|
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: 157.85 E-value: 2.10e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 277 IEARDLTMRF-GSFVAVDHVNFRIPRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGEAWLFGQPVDPKD-IDTRRRVGYM 354
Cdd:cd03295 1 IEFENVTKRYgGGKKAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGEDIREQDpVELRRKIGYV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 355 SQAFSLYNELTVRQNLELHARLFHIPEAEIPARVAEMSERFKLNDVE--DILPESLPLGIRQRLSLAVAVIHRPEMLILD 432
Cdd:cd03295 81 IQQIGLFPHMTVEENIALVPKLLKWPKEKIRERADELLALVGLDPAEfaDRYPHELSGGQQQRVGVARALAADPPLLLMD 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 732682709 433 EPTSGVDPVARDMFWQLMVDLSRQDKVTIFISTHFMNEAER-CDRISLMHAGKVLASGTPQEL 494
Cdd:cd03295 161 EPFGALDPITRDQLQEEFKRLQQELGKTIVFVTHDIDEAFRlADRIAIMKNGEIVQVGTPDEI 223
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
277-479 |
3.59e-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: 155.71 E-value: 3.59e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 277 IEARDLTMRFGSFVAVDHVNFRIPRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGEAWLFGQPVDPKDIDTRRRVGYMSQ 356
Cdd:COG4133 3 LEAENLSCRRGERLLFSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWNGEPIRDAREDYRRRLAYLGH 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 357 AFSLYNELTVRQNLELHARLFHIPEAEipARVAEMSERFKLNDVEDILPESLPLGIRQRLSLAVAVIHRPEMLILDEPTS 436
Cdd:COG4133 83 ADGLKPELTVRENLRFWAALYGLRADR--EAIDEALEAVGLAGLADLPVRQLSAGQKRRVALARLLLSPAPLWLLDEPFT 160
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 732682709 437 GVDPVARDMFWQLMVDLsRQDKVTIFISTHFMNEAERCDRISL 479
Cdd:COG4133 161 ALDAAGVALLAELIAAH-LARGGAVLLTTHQPLELAAARVLDL 202
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
277-484 |
4.32e-43 |
|
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: 154.65 E-value: 4.32e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 277 IEARDLTMRFGSFVAVDHVNFRIPRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGEAWLFGQPVDPKDIDT---RRRVGY 353
Cdd:cd03229 1 LELKNVSKRYGQKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGEDLTDLEDELpplRRRIGM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 354 MSQAFSLYNELTVRQNLelharlfhipeaeiparvaemserfklndvedilpeSLPL--GIRQRLSLAVAVIHRPEMLIL 431
Cdd:cd03229 81 VFQDFALFPHLTVLENI------------------------------------ALGLsgGQQQRVALARALAMDPDVLLL 124
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 732682709 432 DEPTSGVDPVARDMFWQLMVDLSRQDKVTIFISTHFMNEAER-CDRISLMHAGK 484
Cdd:cd03229 125 DEPTSALDPITRREVRALLKSLQAQLGITVVLVTHDLDEAARlADRVVVLRDGK 178
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
285-489 |
5.37e-43 |
|
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: 156.34 E-value: 5.37e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 285 RFGSFVAVDHVNFRIPRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGEAWLFGQPVDPKDIDTRRRVGY-MSQAFSLYNE 363
Cdd:cd03267 30 KYREVEALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRVAGLVPWKRRKKFLRRIGVvFGQKTQLWWD 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 364 LTVRQNLELHARLFHIPEAEIPARVAEMSERFKLNDVEDILPESLPLGIRQRLSLAVAVIHRPEMLILDEPTSGVDPVAR 443
Cdd:cd03267 110 LPVIDSFYLLAAIYDLPPARFKKRLDELSELLDLEELLDTPVRQLSLGQRMRAEIAAALLHEPEILFLDEPTIGLDVVAQ 189
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 732682709 444 DMFWQLMVDLSRQDKVTIFISTHFMNEAER-CDRISLMHAGKVLASG 489
Cdd:cd03267 190 ENIRNFLKEYNRERGTTVLLTSHYMKDIEAlARRVLVIDKGRLLYDG 236
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
277-496 |
5.95e-43 |
|
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: 156.16 E-value: 5.95e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 277 IEARDLTMRFGSFVAVDHVNFRIPRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGEAWLFGQPVDPKDIDTRRR--VGYM 354
Cdd:cd03218 1 LRAENLSKRYGKRKVVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDGQDITKLPMHKRARlgIGYL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 355 SQAFSLYNELTVRQNLELHARLFHIPEAEIPARVAEMSERFKLNDVEDILPESLPLGIRQRLSLAVAVIHRPEMLILDEP 434
Cdd:cd03218 81 PQEASIFRKLTVEENILAVLEIRGLSKKEREEKLEELLEEFHITHLRKSKASSLSGGERRRVEIARALATNPKFLLLDEP 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 732682709 435 TSGVDPVA-RDMfwQLMVDLSRQDKVTIFISTHFMNEA-ERCDRISLMHAGKVLASGTPQELVE 496
Cdd:cd03218 161 FAGVDPIAvQDI--QKIIKILKDRGIGVLITDHNVRETlSITDRAYIIYEGKVLAEGTPEEIAA 222
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
276-497 |
8.20e-43 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 159.47 E-value: 8.20e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 276 AIEARDLTMRFGSFVAVDHVNFRIPRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGEAWLFGQPV---DPKDidtrRRVG 352
Cdd:COG3839 3 SLELENVSKSYGGVEALKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAGLEDPTSGEILIGGRDVtdlPPKD----RNIA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 353 YMSQAFSLYNELTVRQNLELHARLFHIPEAEIPARVAEMSERFKLNDVEDILPESLPLGIRQRLSLAVAVIHRPEMLILD 432
Cdd:COG3839 79 MVFQSYALYPHMTVYENIAFPLKLRKVPKAEIDRRVREAAELLGLEDLLDRKPKQLSGGQRQRVALGRALVREPKVFLLD 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 732682709 433 EPTSGVDPVARdmfWQLMVDLS---RQDKVTIFISTHFMNEAER-CDRISLMHAGKVLASGTPQELVEK 497
Cdd:COG3839 159 EPLSNLDAKLR---VEMRAEIKrlhRRLGTTTIYVTHDQVEAMTlADRIAVMNDGRIQQVGTPEELYDR 224
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
272-507 |
1.17e-42 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 155.63 E-value: 1.17e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 272 NAEIAIEARDLTMRFGSFVAVDHVNFRIPRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGEAWLFGQPVDPKdidtRRRV 351
Cdd:COG1121 2 MMMPAIELENLTVSYGGRPVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLFGKPPRRA----RRRI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 352 GYMSQAFSLYNE--LTVRQ----NLELHARLFHIPEAEIPARVAEMSERFKLNDVEDILPESLPLGIRQRLSLAVAVIHR 425
Cdd:COG1121 78 GYVPQRAEVDWDfpITVRDvvlmGRYGRRGLFRRPSRADREAVDEALERVGLEDLADRPIGELSGGQQQRVLLARALAQD 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 426 PEMLILDEPTSGVDPVARDMFWQLMVDLSRQDKvTIFISTHFMNEAER-CDRISLMhAGKVLASGTPQELVEkrgAASLE 504
Cdd:COG1121 158 PDLLLLDEPFAGVDAATEEALYELLRELRREGK-TILVVTHDLGAVREyFDRVLLL-NRGLVAHGPPEEVLT---PENLS 232
|
...
gi 732682709 505 EAF 507
Cdd:COG1121 233 RAY 235
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
15-435 |
1.54e-42 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 163.31 E-value: 1.54e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 15 LAGVSQHYGKTVALNNITLDIPARCMVGLIGPDGVGKSSLLSLISGARVIEQGNVMVlggdmrdpkhRRDVcpRIAWMPQ 94
Cdd:COG0488 1 LENLSKSFGGRPLLDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEVSI----------PKGL--RIGYLPQ 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 95 GLgkNLYHTLSVYENV-----------------------------------DFFARLFGHDkaeREVRINELLTSTGLAP 139
Cdd:COG0488 69 EP--PLDDDLTVLDTVldgdaelraleaeleeleaklaepdedlerlaelqEEFEALGGWE---AEARAEEILSGLGFPE 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 140 F-RDRPAGKLSGGMKQKLGLCCALIHDPELLILDEPTTGVDplsrsqfwdlIDSIRQ-----RQSNMSVL---------- 203
Cdd:COG0488 144 EdLDRPVSELSGGWRRRVALARALLSEPDLLLLDEPTNHLD----------LESIEWleeflKNYPGTVLvvshdryfld 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 204 -VATAYME----EAERF-----DWLVAmnagevlatgSAEELRQQTQSATL-------EEAFINLLPQAQRQAHQA---- 262
Cdd:COG0488 214 rVATRILEldrgKLTLYpgnysAYLEQ----------RAERLEQEAAAYAKqqkkiakEEEFIRRFRAKARKAKQAqsri 283
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 263 -------VVIPPYQPENAEIA-----------IEARDLTMRFGSFVAVDHVNFRIPRGEIFGFLGSNGCGKSTTMKMLTG 324
Cdd:COG0488 284 kalekleREEPPRRDKTVEIRfppperlgkkvLELEGLSKSYGDKTLLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAG 363
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 325 LLPASEGEAWLfGQPVdpkdidtrrRVGYMSQAF-SLYNELTVRQNL--------ELHAR------LFHIPEAEipARVA 389
Cdd:COG0488 364 ELEPDSGTVKL-GETV---------KIGYFDQHQeELDPDKTVLDELrdgapggtEQEVRgylgrfLFSGDDAF--KPVG 431
|
490 500 510 520
....*....|....*....|....*....|....*....|....*...
gi 732682709 390 EMS--ERFklndvedilpeslplgirqRLSLAVAVIHRPEMLILDEPT 435
Cdd:COG0488 432 VLSggEKA-------------------RLALAKLLLSPPNVLLLDEPT 460
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
18-496 |
1.62e-42 |
|
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in methanogenesis, methyl coenzyme M reductase, contains alpha, beta, and gamma chains. In older literature, the complex of alpha, beta, and gamma chains was termed component C, while this single chain protein was termed methyl coenzyme M reductase system component A2. [Energy metabolism, Methanogenesis]
Pssm-ID: 132313 [Multi-domain] Cd Length: 520 Bit Score: 163.05 E-value: 1.62e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 18 VSQHYGKTVALNNITLDIPARCMVGLIGPDGVGKSSLLSLISGARVIE--QGNVM-----------------------VL 72
Cdd:TIGR03269 6 LTKKFDGKEVLKNISFTIEEGEVLGILGRSGAGKSVLMHVLRGMDQYEptSGRIIyhvalcekcgyverpskvgepcpVC 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 73 GGDMR---------DPKHRRDVCPRIAWMPQGLGKnLYHTLSVYENVDFFARLFGHDKAEREVRINELLTSTGLAPFRDR 143
Cdd:TIGR03269 86 GGTLEpeevdfwnlSDKLRRRIRKRIAIMLQRTFA-LYGDDTVLDNVLEALEEIGYEGKEAVGRAVDLIEMVQLSHRITH 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 144 PAGKLSGGMKQKLGLCCALIHDPELLILDEPTTGVDPlsrsQFWDLI-DSIRQ--RQSNMSVLVATAYMEEAERF-DWLV 219
Cdd:TIGR03269 165 IARDLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDP----QTAKLVhNALEEavKASGISMVLTSHWPEVIEDLsDKAI 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 220 AMNAGEVLATGSAEELrqqtqsatlEEAFINLLPQAQRQAhqavvippyQPENAEIAIEARDLTMRF-----GSFVAVDH 294
Cdd:TIGR03269 241 WLENGEIKEEGTPDEV---------VAVFMEGVSEVEKEC---------EVEVGEPIIKVRNVSKRYisvdrGVVKAVDN 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 295 VNFRIPRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGEAW-LFGQP-VD--PKDIDTRRRV----GYMSQAFSLYNELTV 366
Cdd:TIGR03269 303 VSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGEVNvRVGDEwVDmtKPGPDGRGRAkryiGILHQEYDLYPHRTV 382
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 367 RQNLELHARL-----FHIPEAEIPARVAEMSERfKLNDVEDILPESLPLGIRQRLSLAVAVIHRPEMLILDEPTSGVDPV 441
Cdd:TIGR03269 383 LDNLTEAIGLelpdeLARMKAVITLKMVGFDEE-KAEEILDKYPDELSEGERHRVALAQVLIKEPRIVILDEPTGTMDPI 461
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*.
gi 732682709 442 ARDMFWQLMVDLSRQDKVTIFISTHFMNEA-ERCDRISLMHAGKVLASGTPQELVE 496
Cdd:TIGR03269 462 TKVDVTHSILKAREEMEQTFIIVSHDMDFVlDVCDRAALMRDGKIVKIGDPEEIVE 517
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
277-496 |
7.41e-42 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 156.85 E-value: 7.41e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 277 IEARDLTMRFGSFVAVDHVNFRIPRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGEAWLFGQpvdpkDIDT-----RRRV 351
Cdd:COG1118 3 IEVRNISKRFGSFTLLDDVSLEIASGELVALLGPSGSGKTTLLRIIAGLETPDSGRIVLNGR-----DLFTnlpprERRV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 352 GYMSQAFSLYNELTVRQNLELHARLFHIPEAEIPARVAEMSERFKLNDVEDILPESLPLGIRQRLSLAVAVIHRPEMLIL 431
Cdd:COG1118 78 GFVFQHYALFPHMTVAENIAFGLRVRPPSKAEIRARVEELLELVQLEGLADRYPSQLSGGQRQRVALARALAVEPEVLLL 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 732682709 432 DEPTSGVDP-VARDMfWQLMVDLSRQDKVTIFISTHFMNEA-ERCDRISLMHAGKVLASGTPQELVE 496
Cdd:COG1118 158 DEPFGALDAkVRKEL-RRWLRRLHDELGGTTVFVTHDQEEAlELADRVVVMNQGRIEQVGTPDEVYD 223
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
277-494 |
2.58e-41 |
|
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: 151.58 E-value: 2.58e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 277 IEARDLTMRFGS----FVAVDHVNFRIPRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGEAWLFGQPV---DPKDI-DTR 348
Cdd:cd03258 2 IELKNVSKVFGDtggkVTALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGSVLVDGTDLtllSGKELrKAR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 349 RRVGYMSQAFSLYNELTVRQNLELHARLFHIPEAEIPARVAEMSERFKLNDVEDILPESLPLGIRQRLSLAVAVIHRPEM 428
Cdd:cd03258 82 RRIGMIFQHFNLLSSRTVFENVALPLEIAGVPKAEIEERVLELLELVGLEDKADAYPAQLSGGQKQRVGIARALANNPKV 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 732682709 429 LILDEPTSGVDPVARDMFWQLMVDLSRQDKVTIFISTHFMNEAER-CDRISLMHAGKVLASGTPQEL 494
Cdd:cd03258 162 LLCDEATSALDPETTQSILALLRDINRELGLTIVLITHEMEVVKRiCDRVAVMEKGEVVEEGTVEEV 228
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
10-248 |
4.75e-41 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 151.01 E-value: 4.75e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 10 PPVAQLAGVSQHYGKTVALNNITLDIPARCMVGLIGPDGVGKSSLLSLISGARVIEQGNVMVLGgdmRDPKHRRdvcPRI 89
Cdd:COG1121 4 MPAIELENLTVSYGGRPVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLFG---KPPRRAR---RRI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 90 AWMPQGLGKNLYHTLSVYENVD--------FFARLfghDKAEREvRINELLTSTGLAPFRDRPAGKLSGGMKQKLGLCCA 161
Cdd:COG1121 78 GYVPQRAEVDWDFPITVRDVVLmgrygrrgLFRRP---SRADRE-AVDEALERVGLEDLADRPIGELSGGQQQRVLLARA 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 162 LIHDPELLILDEPTTGVDPLSRSQFWDLIDSIRQRqsNMSVLVATAYMEEAER-FDWLVAMNaGEVLATGSAEELRqqtQ 240
Cdd:COG1121 154 LAQDPDLLLLDEPFAGVDAATEEALYELLRELRRE--GKTILVVTHDLGAVREyFDRVLLLN-RGLVAHGPPEEVL---T 227
|
....*...
gi 732682709 241 SATLEEAF 248
Cdd:COG1121 228 PENLSRAY 235
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
14-225 |
7.87e-41 |
|
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ABC component of a cobalt transport family found in bacteria, archaea, and eukaryota. The transition metal cobalt is an essential component of many enzymes and must be transported into cells in appropriate amounts when needed. This ABC transport system of the CbiMNQO family is involved in cobalt transport in association with the cobalamin (vitamin B12) biosynthetic pathways. Most of cobalt (Cbi) transport systems possess a separate CbiN component, the cobalt-binding periplasmic protein, and they are encoded by the conserved gene cluster cbiMNQO. Both the CbiM and CbiQ proteins are integral cytoplasmic membrane proteins, and the CbiO protein has the linker peptide and the Walker A and B motifs commonly found in the ATPase components of the ABC-type transport systems.
Pssm-ID: 213192 [Multi-domain] Cd Length: 211 Bit Score: 149.15 E-value: 7.87e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 14 QLAGVSQHY--GKTVALNNITLDIPARCMVGLIGPDGVGKSSLLSLISGARVIEQGNVMVLGGDMRDpKHRRDVCPRIAW 91
Cdd:cd03225 1 ELKNLSFSYpdGARPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDLTK-LSLKELRRKVGL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 92 MPQglgkNLYH---TLSVYENVDFFARLFGHDKAEREVRINELLTSTGLAPFRDRPAGKLSGGMKQKLGLCCALIHDPEL 168
Cdd:cd03225 80 VFQ----NPDDqffGPTVEEEVAFGLENLGLPEEEIEERVEEALELVGLEGLRDRSPFTLSGGQKQRVAIAGVLAMDPDI 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 732682709 169 LILDEPTTGVDPLSRSQFWDLIDSIRQRqsNMSVLVATAYMEEAERF-DWLVAMNAGE 225
Cdd:cd03225 156 LLLDEPTAGLDPAGRRELLELLKKLKAE--GKTIIIVTHDLDLLLELaDRVIVLEDGK 211
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
277-497 |
8.72e-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: 8.72e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 277 IEARDLTMRFGSFVAVDHVNFRIPRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGEAWLFGQPVDPKDIDtRRRVGYMSQ 356
Cdd:cd03300 1 IELENVSKFYGGFVALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGKDITNLPPH-KRPVNTVFQ 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 357 AFSLYNELTVRQNLELHARLFHIPEAEIPARVAEMSERFKLNDVEDILPESLPLGIRQRLSLAVAVIHRPEMLILDEPTS 436
Cdd:cd03300 80 NYALFPHLTVFENIAFGLRLKKLPKAEIKERVAEALDLVQLEGYANRKPSQLSGGQQQRVAIARALVNEPKVLLLDEPLG 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 732682709 437 GVDPVAR-DMFWQLMvDLSRQDKVTIFISTHFMNEA-ERCDRISLMHAGKVLASGTPQELVEK 497
Cdd:cd03300 160 ALDLKLRkDMQLELK-RLQKELGITFVFVTHDQEEAlTMSDRIAVMNKGKIQQIGTPEEIYEE 221
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
276-497 |
1.03e-40 |
|
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: 149.80 E-value: 1.03e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 276 AIEARDLTMRFGSFVAVDHVNFRIPRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGEAWLFGQPVDPKDIDtRRRVGYMS 355
Cdd:cd03296 2 SIEVRNVSKRFGDFVALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGGEDATDVPVQ-ERNVGFVF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 356 QAFSLYNELTVRQN----LELHARLFHIPEAEIPARVAEMSERFKLNDVEDILPESLPLGIRQRLSLAVAVIHRPEMLIL 431
Cdd:cd03296 81 QHYALFRHMTVFDNvafgLRVKPRSERPPEAEIRAKVHELLKLVQLDWLADRYPAQLSGGQRQRVALARALAVEPKVLLL 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 732682709 432 DEPTSGVDPVARDMFWQLMVDLSRQDKVTIFISTHFMNEA-ERCDRISLMHAGKVLASGTPQELVEK 497
Cdd:cd03296 161 DEPFGALDAKVRKELRRWLRRLHDELHVTTVFVTHDQEEAlEVADRVVVMNKGRIEQVGTPDEVYDH 227
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
278-489 |
1.16e-40 |
|
ATP-binding cassette domain of the metal-type transporters; This family includes transporters involved in the uptake of various metallic cations such as iron, manganese, and zinc. The ATPases of this group of transporters are very similar to members of iron-siderophore uptake family suggesting that they share a common ancestor. The best characterized metal-type ABC transporters are the YfeABCD system of Y. pestis, the SitABCD system of Salmonella enterica serovar Typhimurium, and the SitABCD transporter of Shigella flexneri. Moreover other uncharacterized homologs of these metal-type transporters are mainly found in pathogens like Haemophilus or enteroinvasive E. coli isolates.
Pssm-ID: 213202 [Multi-domain] Cd Length: 213 Bit Score: 148.84 E-value: 1.16e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 278 EARDLTMRFGSFVAVDHVNFRIPRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGEAWLFGQPVDpkdiDTRRRVGYMSQA 357
Cdd:cd03235 1 EVEDLTVSYGGHPVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFGKPLE----KERKRIGYVPQR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 358 FSLYNE--LTVRQ----NLELHARLFHIPEAEIPARVAEMSERFKLNDVEDILPESLPLGIRQRLSLAVAVIHRPEMLIL 431
Cdd:cd03235 77 RSIDRDfpISVRDvvlmGLYGHKGLFRRLSKADKAKVDEALERVGLSELADRQIGELSGGQQQRVLLARALVQDPDLLLL 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 732682709 432 DEPTSGVDPVARDMFWQLMVDLSRQDKvTIFISTHFMNEAER-CDRISLMhAGKVLASG 489
Cdd:cd03235 157 DEPFAGVDPKTQEDIYELLRELRREGM-TILVVTHDLGLVLEyFDRVLLL-NRTVVASG 213
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
273-497 |
2.11e-40 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 156.33 E-value: 2.11e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 273 AEIAIEARDLTMRFGSFVAVDHVNFRIPRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGEAWLFGQPVDPKDI-DTRRR- 350
Cdd:COG1129 1 AEPLLEMRGISKSFGGVKALDGVSLELRPGEVHALLGENGAGKSTLMKILSGVYQPDSGEILLDGEPVRFRSPrDAQAAg 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 351 VGYMSQAFSLYNELTVRQNL----ELHARLFhIPEAEIPARVAEMSERFKLN-DVEDILpESLPLGIRQRLSLAVAVIHR 425
Cdd:COG1129 81 IAIIHQELNLVPNLSVAENIflgrEPRRGGL-IDWRAMRRRARELLARLGLDiDPDTPV-GDLSVAQQQLVEIARALSRD 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 732682709 426 PEMLILDEPTSGVDPVARDMFWQLMVDLSRQDKVTIFIStHFMNEAER-CDRISLMHAGKVLASG-----TPQELVEK 497
Cdd:COG1129 159 ARVLILDEPTASLTEREVERLFRIIRRLKAQGVAIIYIS-HRLDEVFEiADRVTVLRDGRLVGTGpvaelTEDELVRL 235
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
277-466 |
3.80e-40 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 147.89 E-value: 3.80e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 277 IEARDLTMRF-GSFVAVDHVNFRIPRGEiFGFL-GSNGCGKSTTMKMLTGLLPASEGEAWLFGQPV---DPKDI-DTRRR 350
Cdd:COG2884 2 IRFENVSKRYpGGREALSDVSLEIEKGE-FVFLtGPSGAGKSTLLKLLYGEERPTSGQVLVNGQDLsrlKRREIpYLRRR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 351 VGYMSQAFSLYNELTVRQNLELHARLFHIPEAEIPARVAEMSERFKLNDVEDILPESLPLGIRQRLSLAVAVIHRPEMLI 430
Cdd:COG2884 81 IGVVFQDFRLLPDRTVYENVALPLRVTGKSRKEIRRRVREVLDLVGLSDKAKALPHELSGGEQQRVAIARALVNRPELLL 160
|
170 180 190
....*....|....*....|....*....|....*.
gi 732682709 431 LDEPTSGVDPVARDMFWQLMVDLSRQdKVTIFISTH 466
Cdd:COG2884 161 ADEPTGNLDPETSWEIMELLEEINRR-GTTVLIATH 195
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
277-494 |
6.16e-40 |
|
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: 147.33 E-value: 6.16e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 277 IEARDLTMRFGSFVAVDHVNFRIPRGEIFGFLGSNGCGKSTTMKMLTGLLPA-----SEGEAWLFGQPVDPKDIDT---R 348
Cdd:cd03260 1 IELRDLNVYYGDKHALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRLNDLipgapDEGEVLLDGKDIYDLDVDVlelR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 349 RRVGYMSQAFSLYNeLTVRQNLELHARLFHI-PEAEIPARVAEMSERFKLND-VEDIL-PESLPLGIRQRLSLAVAVIHR 425
Cdd:cd03260 81 RRVGMVFQKPNPFP-GSIYDNVAYGLRLHGIkLKEELDERVEEALRKAALWDeVKDRLhALGLSGGQQQRLCLARALANE 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 426 PEMLILDEPTSGVDPVARDMFWQLMVDLSRQdkVTIFISTHFMNEAERC-DRISLMHAGKVLASGTPQEL 494
Cdd:cd03260 160 PEVLLLDEPTSALDPISTAKIEELIAELKKE--YTIVIVTHNMQQAARVaDRTAFLLNGRLVEFGPTEQI 227
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
277-496 |
1.18e-39 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 147.10 E-value: 1.18e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 277 IEARDLTMRFGSFVAVDHVNFRIPRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGEAWLFGQPVDPKDIDTRRR--VGYM 354
Cdd:COG1137 4 LEAENLVKSYGKRTVVKDVSLEVNQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGRIFLDGEDITHLPMHKRARlgIGYL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 355 SQAFSLYNELTVRQNLELHARLFHIPEAEIPARVAEMSERFKLNDVEDILPESLPLGIRQRLSLAVAVIHRPEMLILDEP 434
Cdd:COG1137 84 PQEASIFRKLTVEDNILAVLELRKLSKKEREERLEELLEEFGITHLRKSKAYSLSGGERRRVEIARALATNPKFILLDEP 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 732682709 435 TSGVDPVA----RDMFWQLmvdlsRQDKVTIFISTHFMNEAER-CDRISLMHAGKVLASGTPQELVE 496
Cdd:COG1137 164 FAGVDPIAvadiQKIIRHL-----KERGIGVLITDHNVRETLGiCDRAYIISEGKVLAEGTPEEILN 225
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
276-517 |
1.63e-39 |
|
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid transport and metabolism, Inorganic ion transport and metabolism];
Pssm-ID: 440741 [Multi-domain] Cd Length: 248 Bit Score: 146.87 E-value: 1.63e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 276 AIEARDLTMRFGS----FVAVDHVNFRIPRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGEAWLFGQPVDPKDI-DTRRR 350
Cdd:COG1124 1 MLEVRNLSVSYGQggrrVPVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVTFDGRPVTRRRRkAFRRR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 351 VGYMSQ--AFSLYNELTVRQNLELHARLFHIPEAEipARVAEMSERFKLN-DVEDILPESLPLGIRQRLSLAVAVIHRPE 427
Cdd:COG1124 81 VQMVFQdpYASLHPRHTVDRILAEPLRIHGLPDRE--ERIAELLEQVGLPpSFLDRYPHQLSGGQRQRVAIARALILEPE 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 428 MLILDEPTSGVDPVARDMFWQLMVDLSRQDKVTIFISTHFMNEAER-CDRISLMHAGKVLASGTPQELvekrgAASLEEA 506
Cdd:COG1124 159 LLLLDEPTSALDVSVQAEILNLLKDLREERGLTYLFVSHDLAVVAHlCDRVAVMQNGRIVEELTVADL-----LAGPKHP 233
|
250
....*....|.
gi 732682709 507 FIAYLQEAAGQ 517
Cdd:COG1124 234 YTRELLAASLA 244
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
14-230 |
1.75e-39 |
|
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: 145.50 E-value: 1.75e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 14 QLAGVSQHYGKTVALNNITLDIPARCMVGLIGPDGVGKSSLLSLISGARVIEQGNVMVLGGDMrDPKHRRdvcpRIAWMP 93
Cdd:cd03269 2 EVENVTKRFGRVTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDGKPL-DIAARN----RIGYLP 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 94 QGLGknLYHTLSVYENVDFFARLFGHDKAEREVRINELLTSTGLAPFRDRPAGKLSGGMKQKLGLCCALIHDPELLILDE 173
Cdd:cd03269 77 EERG--LYPKMKVIDQLVYLAQLKGLKKEEARRRIDEWLERLELSEYANKRVEELSKGNQQKVQFIAAVIHDPELLILDE 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 732682709 174 PTTGVDPLSRSQFWDLIDSirQRQSNMSVLVATAYMEEAERF-DWLVAMNAGEVLATG 230
Cdd:cd03269 155 PFSGLDPVNVELLKDVIRE--LARAGKTVILSTHQMELVEELcDRVLLLNKGRAVLYG 210
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
14-206 |
1.94e-39 |
|
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: 144.93 E-value: 1.94e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 14 QLAGVSQHYGKTVALNNITLDIPARCMVGLIGPDGVGKSSLLSLISGARVIEQGNVMVLGGDMRDpkHRRDVCPRIAWMP 93
Cdd:COG4133 4 EAENLSCRRGERLLFSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWNGEPIRD--AREDYRRRLAYLG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 94 QGLGknLYHTLSVYENVDFFARLFGHDKAERevRINELLTSTGLAPFRDRPAGKLSGGMKQKLGLCCALIHDPELLILDE 173
Cdd:COG4133 82 HADG--LKPELTVRENLRFWAALYGLRADRE--AIDEALEAVGLAGLADLPVRQLSAGQKRRVALARLLLSPAPLWLLDE 157
|
170 180 190
....*....|....*....|....*....|...
gi 732682709 174 PTTGVDPLSRSQFWDLIDsiRQRQSNMSVLVAT 206
Cdd:COG4133 158 PFTALDAAGVALLAELIA--AHLARGGAVLLTT 188
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
14-248 |
6.63e-39 |
|
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: 145.19 E-value: 6.63e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 14 QLAGVSQHYGKTVALNNITLDIPARCMVGLIGPDGVGKSSLLSLISGARVIEQGNVMVLGGDMRDPKhRRDVCPRIAWMP 93
Cdd:COG1120 3 EAENLSVGYGGRPVLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDGRDLASLS-RRELARRIAYVP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 94 QGLGKNLYhtLSVYENVDF----FARLFGHDKAEREVRINELLTSTGLAPFRDRPAGKLSGGMKQKLGLCCALIHDPELL 169
Cdd:COG1120 82 QEPPAPFG--LTVRELVALgrypHLGLFGRPSAEDREAVEEALERTGLEHLADRPVDELSGGERQRVLIARALAQEPPLL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 170 ILDEPTTGVDPlsRSQFwDLIDSIRQ--RQSNMSVLVATAYMEEAERF-DWLVAMNAGEVLATGSAEELrqqTQSATLEE 246
Cdd:COG1120 160 LLDEPTSHLDL--AHQL-EVLELLRRlaRERGRTVVMVLHDLNLAARYaDRLVLLKDGRIVAQGPPEEV---LTPELLEE 233
|
..
gi 732682709 247 AF 248
Cdd:COG1120 234 VY 235
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
15-230 |
6.89e-39 |
|
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is comprised of proteins involved in the transport of apparently unrelated solutes and proteins specific for di- and oligosaccharides and polyols. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213226 [Multi-domain] Cd Length: 213 Bit Score: 143.81 E-value: 6.89e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 15 LAGVSQHYGKTVALNNITLDIPARCMVGLIGPDGVGKSSLLSLISGARVIEQGNVMVLGGDMRD-PKHRRDvcprIAWMP 93
Cdd:cd03259 3 LKGLSKTYGSVRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDGRDVTGvPPERRN----IGMVF 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 94 QGLgkNLYHTLSVYENVDFFARLFGHDKAEREVRINELLTSTGLAPFRDRPAGKLSGGMKQKLGLCCALIHDPELLILDE 173
Cdd:cd03259 79 QDY--ALFPHLTVAENIAFGLKLRGVPKAEIRARVRELLELVGLEGLLNRYPHELSGGQQQRVALARALAREPSLLLLDE 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 732682709 174 PTTGVDPLSRSQFWDLIDSIrQRQSNMSVLVATAYMEEAERF-DWLVAMNAGEVLATG 230
Cdd:cd03259 157 PLSALDAKLREELREELKEL-QRELGITTIYVTHDQEEALALaDRIAVMNEGRIVQVG 213
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
23-230 |
2.11e-38 |
|
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: 142.51 E-value: 2.11e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 23 GKTVALNNITLDIPARCMVGLIGPDGVGKSSLLSLISGARVIEQGNVMVLGGDM-RDPkhrRDVCPRIAWMPQGLGknLY 101
Cdd:cd03266 16 KTVQAVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDGFDVvKEP---AEARRRLGFVSDSTG--LY 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 102 HTLSVYENVDFFARLFGHDKAEREVRINELLTSTGLAPFRDRPAGKLSGGMKQKLGLCCALIHDPELLILDEPTTGVDPL 181
Cdd:cd03266 91 DRLTARENLEYFAGLYGLKGDELTARLEELADRLGMEELLDRRVGGFSTGMRQKVAIARALVHDPPVLLLDEPTTGLDVM 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 732682709 182 SRSQFWDLIDsiRQRQSNMSVLVATAYMEEAERF-DWLVAMNAGEVLATG 230
Cdd:cd03266 171 ATRALREFIR--QLRALGKCILFSTHIMQEVERLcDRVVVLHRGRVVYEG 218
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
14-226 |
4.23e-38 |
|
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: 141.86 E-value: 4.23e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 14 QLAGVSQHYG----KTVALNNITLDIPARCMVGLIGPDGVGKSSLLSLISGARVIEQGNVMVLGGDMRDPKH------RR 83
Cdd:cd03255 2 ELKNLSKTYGgggeKVQALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRVDGTDISKLSEkelaafRR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 84 DvcpRIAWMPQGLgkNLYHTLSVYENVDFFARLFGHDKAEREVRINELLTSTGLAPFRDRPAGKLSGGMKQKLGLCCALI 163
Cdd:cd03255 82 R---HIGFVFQSF--NLLPDLTALENVELPLLLAGVPKKERRERAEELLERVGLGDRLNHYPSELSGGQQQRVAIARALA 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 732682709 164 HDPELLILDEPTTGVDPLSRSQFWDLIDSIrQRQSNMSVLVATAYMEEAERFDWLVAMNAGEV 226
Cdd:cd03255 157 NDPKIILADEPTGNLDSETGKEVMELLREL-NKEAGTTIVVVTHDPELAEYADRIIELRDGKI 218
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
14-230 |
8.91e-38 |
|
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: 140.75 E-value: 8.91e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 14 QLAGVSQHYGKTVALNNITLDIPARCMVGLIGPDGVGKSSLLSLISGARVIEQGNVMVLGgdmrdpKHRRDVCPRIAWMP 93
Cdd:cd03235 1 EVEDLTVSYGGHPVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFG------KPLEKERKRIGYVP 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 94 QGLGKNLYHTLSVYENV----DFFARLFGHDKAEREVRINELLTSTGLAPFRDRPAGKLSGGMKQKLGLCCALIHDPELL 169
Cdd:cd03235 75 QRRSIDRDFPISVRDVVlmglYGHKGLFRRLSKADKAKVDEALERVGLSELADRQIGELSGGQQQRVLLARALVQDPDLL 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 732682709 170 ILDEPTTGVDPLSRSQFWDLIDSIRQRqsNMSVLVATAYMEEAER-FDWLVAMNaGEVLATG 230
Cdd:cd03235 155 LLDEPFAGVDPKTQEDIYELLRELRRE--GMTILVVTHDLGLVLEyFDRVLLLN-RTVVASG 213
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
264-496 |
9.75e-38 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 145.75 E-value: 9.75e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 264 VIPPYQPENAEIA---IEARDLTMRFGSFVAVDHVNFRIPRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGEAWLFGQP- 339
Cdd:PRK11607 4 AIPRPQAKTRKALtplLEIRNLTKSFDGQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVDl 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 340 --VDPkdidTRRRVGYMSQAFSLYNELTVRQNLELHARLFHIPEAEIPARVAEMSERFKLNDVEDILPESLPLGIRQRLS 417
Cdd:PRK11607 84 shVPP----YQRPINMMFQSYALFPHMTVEQNIAFGLKQDKLPKAEIASRVNEMLGLVHMQEFAKRKPHQLSGGQRQRVA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 418 LAVAVIHRPEMLILDEPTSGVDPVARDMFWQLMVDLSRQDKVTIFISTHFMNEA-ERCDRISLMHAGKVLASGTPQELVE 496
Cdd:PRK11607 160 LARSLAKRPKLLLLDEPMGALDKKLRDRMQLEVVDILERVGVTCVMVTHDQEEAmTMAGRIAIMNRGKFVQIGEPEEIYE 239
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
268-497 |
1.43e-37 |
|
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This family comprises the glycine betaine/L-proline ATP binding subunit in bacteria and its equivalents in archaea. This transport system belong to the larger ATP-Binding Cassette (ABC) transporter superfamily. The characteristic feature of these transporters is the obligatory coupling of ATP hydrolysis to substrate translocation. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213261 [Multi-domain] Cd Length: 269 Bit Score: 142.01 E-value: 1.43e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 268 YQPENAEIAIE----ARDLTMRFGSFVAVDHVNFRIPRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGEAWLFGQPV--- 340
Cdd:cd03294 12 KNPQKAFKLLAkgksKEEILKKTGQTVGVNDVSLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGKVLIDGQDIaam 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 341 DPKDIDT--RRRVGYMSQAFSLYNELTVRQNLELHARLFHIPEAEIPARVAEMSERFKLNDVEDILPESLPLGIRQRLSL 418
Cdd:cd03294 92 SRKELRElrRKKISMVFQSFALLPHRTVLENVAFGLEVQGVPRAEREERAAEALELVGLEGWEHKYPDELSGGMQQRVGL 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 419 AVAVIHRPEMLILDEPTSGVDPVAR-DMFWQLMvDLSRQDKVTIFISTHFMNEAERC-DRISLMHAGKVLASGTPQELVE 496
Cdd:cd03294 172 ARALAVDPDILLMDEAFSALDPLIRrEMQDELL-RLQAELQKTIVFITHDLDEALRLgDRIAIMKDGRLVQVGTPEEILT 250
|
.
gi 732682709 497 K 497
Cdd:cd03294 251 N 251
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
292-436 |
1.55e-37 |
|
ABC transporter; ABC transporters for a large family of proteins responsible for translocation of a variety of compounds across biological membranes. ABC transporters are the largest family of proteins in many completely sequenced bacteria. ABC transporters are composed of two copies of this domain and two copies of a transmembrane domain pfam00664. These four domains may belong to a single polypeptide or belong in different polypeptide chains.
Pssm-ID: 394964 [Multi-domain] Cd Length: 150 Bit Score: 137.78 E-value: 1.55e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 292 VDHVNFRIPRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGEAWLFGQPVDPKDI-DTRRRVGYMSQAFSLYNELTVRQNL 370
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDLTDDERkSLRKEIGYVFQDPQLFPRLTVRENL 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 371 ELHARLFHIPEAEIPARVAEMSERFKLNDVED----ILPESLPLGIRQRLSLAVAVIHRPEMLILDEPTS 436
Cdd:pfam00005 81 RLGLLLKGLSKREKDARAEEALEKLGLGDLADrpvgERPGTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
278-484 |
1.60e-37 |
|
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213179 [Multi-domain] Cd Length: 157 Bit Score: 137.76 E-value: 1.60e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 278 EARDLTMRFGSFVAVDHVNFRIPRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGEAWLFGQPVDPKDIDT-RRRVGYMSQ 356
Cdd:cd00267 1 EIENLSFRYGGRTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGKDIAKLPLEElRRRIGYVPQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 357 afslyneltvrqnlelharlfhipeaeiparvaemserfklndvedilpesLPLGIRQRLSLAVAVIHRPEMLILDEPTS 436
Cdd:cd00267 81 ---------------------------------------------------LSGGQRQRVALARALLLNPDLLLLDEPTS 109
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 732682709 437 GVDPVARDMFWQLMVDLSRQDKvTIFISTHFMNEAER-CDRISLMHAGK 484
Cdd:cd00267 110 GLDPASRERLLELLRELAEEGR-TVIIVTHDPELAELaADRVIVLKDGK 157
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
10-237 |
1.70e-37 |
|
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: 140.89 E-value: 1.70e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 10 PPVAQLAGVSQHYGKTVALNNITLDIPARCMVGLIGPDGVGKSSLLSLISGARVIEQGNVMVLGGDMR--DPKHRRDVCP 87
Cdd:COG1127 3 EPMIEVRNLTKSFGDRVVLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEILVDGQDITglSEKELYELRR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 88 RIAWMPQGLGknLYHTLSVYENVDFFARLFGH-DKAEREVRINELLTSTGLAPFRDRPAGKLSGGMKQKLGLCCALIHDP 166
Cdd:COG1127 83 RIGMLFQGGA--LFDSLTVFENVAFPLREHTDlSEAEIRELVLEKLELVGLPGAADKMPSELSGGMRKRVALARALALDP 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 732682709 167 ELLILDEPTTGVDPLSRSQFWDLIDSIRqRQSNMSVLVATAYMEEAERF-DWLVAMNAGEVLATGSAEELRQ 237
Cdd:COG1127 161 EILLYDEPTAGLDPITSAVIDELIRELR-DELGLTSVVVTHDLDSAFAIaDRVAVLADGKIIAEGTPEELLA 231
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
10-494 |
2.55e-37 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 147.10 E-value: 2.55e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 10 PPVAQLAGVSQHYGKTVALNNITLDIPARCMVGLIGPDGVGKSSLLSLISGARVIEQGNVMVLGG--DMRDPKHRRDvcp 87
Cdd:COG3845 3 PPALELRGITKRFGGVVANDDVSLTVRPGEIHALLGENGAGKSTLMKILYGLYQPDSGEILIDGKpvRIRSPRDAIA--- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 88 riawmpQGLGK-----NLYHTLSVYENV-----DFFARLFGHDKAEREVRinELLTSTGLA--PfrDRPAGKLSGGMKQK 155
Cdd:COG3845 80 ------LGIGMvhqhfMLVPNLTVAENIvlglePTKGGRLDRKAARARIR--ELSERYGLDvdP--DAKVEDLSVGEQQR 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 156 LGLCCALIHDPELLILDEPTTG-----VDplsrsqfwDLIDSIRQ-RQSNMSVLVATAYMEEAERF-DWLVAMNAGEVLA 228
Cdd:COG3845 150 VEILKALYRGARILILDEPTAVltpqeAD--------ELFEILRRlAAEGKSIIFITHKLREVMAIaDRVTVLRRGKVVG 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 229 TGSAEElrqqTQSATLEEAFInllpqaQRQAHQAVVIPPYQPenAEIAIEARDLTMR-FGSFVAVDHVNFRIPRGEIFGF 307
Cdd:COG3845 222 TVDTAE----TSEEELAELMV------GREVLLRVEKAPAEP--GEVVLEVENLSVRdDRGVPALKDVSLEVRAGEILGI 289
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 308 LGSNGCGKSTTMKMLTGLLPASEGEAWLFGQPVDPKDIDTRRR--VGYMS---QAFSLYNELTVRQN--LELH-----AR 375
Cdd:COG3845 290 AGVAGNGQSELAEALAGLRPPASGSIRLDGEDITGLSPRERRRlgVAYIPedrLGRGLVPDMSVAENliLGRYrrppfSR 369
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 376 LFHIPEAEIPARVAEMSERFklndveDILPESLPLGIR-------QRLSLAVAVIHRPEMLILDEPTSGVDPVARDMFWQ 448
Cdd:COG3845 370 GGFLDRKAIRAFAEELIEEF------DVRTPGPDTPARslsggnqQKVILARELSRDPKLLIAAQPTRGLDVGAIEFIHQ 443
|
490 500 510 520
....*....|....*....|....*....|....*....|....*..
gi 732682709 449 LMVDLSRQDKVTIFISTHfMNEA-ERCDRISLMHAGKVLASGTPQEL 494
Cdd:COG3845 444 RLLELRDAGAAVLLISED-LDEIlALSDRIAVMYEGRIVGEVPAAEA 489
|
|
| proV |
TIGR01186 |
glycine betaine/L-proline transport ATP binding subunit; This model describes the glycine ... |
287-563 |
2.60e-37 |
|
glycine betaine/L-proline transport ATP binding subunit; This model describes the glycine betaine/L-proline ATP binding subunit in bacteria and its equivalents in archaea. This transport system belong to the larger ATP-Binding Cassette (ABC) transporter superfamily. The characteristic feature of these transporter is the obligatory coupling of ATP hydrolysis to substrate translocation. The minimal configuration of bacterial ABC transport system: an ATPase or ATP binding subunit; An integral membrane protein; a hydrophilic polypetpide, which likely functions as substrate binding protein. Functionally, this transport system is involved in osmoregulation. Under conditions of stress, the organism recruits these transport system to accumulate glycine betaine and other solutes which offer osmo-protection. It has been demonstrated that glycine betaine uptake is accompanied by symport with sodium ions. The locus has been named variously as proU or opuA. A gene library from L.lactis functionally complements an E.coli proU mutant. The comlementing locus is similar to a opuA locus in B.sutlis. This clarifies the differences in nomenclature. [Transport and binding proteins, Amino acids, peptides and amines]
Pssm-ID: 130254 [Multi-domain] Cd Length: 363 Bit Score: 144.22 E-value: 2.60e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 287 GSFVAVDHVNFRIPRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGEAWLFGQPVDPKDID-----TRRRVGYMSQAFSLY 361
Cdd:TIGR01186 4 GGKKGVNDADLAIAKGEIFVIMGLSGSGKSTTVRMLNRLIEPTAGQIFIDGENIMKQSPVelrevRRKKIGMVFQQFALF 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 362 NELTVRQNLELHARLFHIPEAEIPARVAEMSERFKLNDVEDILPESLPLGIRQRLSLAVAVIHRPEMLILDEPTSGVDPV 441
Cdd:TIGR01186 84 PHMTILQNTSLGPELLGWPEQERKEKALELLKLVGLEEYEHRYPDELSGGMQQRVGLARALAAEPDILLMDEAFSALDPL 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 442 ARDMFWQLMVDLSRQDKVTIFISTHFMNEAERC-DRISLMHAGKVLASGTPQELVeKRGAASLEEAFIAylQEAAGQSNE 520
Cdd:TIGR01186 164 IRDSMQDELKKLQATLQKTIVFITHDLDEAIRIgDRIVIMKAGEIVQVGTPDEIL-RNPANEYVEEFIG--KVDLSQVFD 240
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 732682709 521 AEappvvHDTTHAPRQgfSLRRLFSYSRREALELRRDPVRSTL 563
Cdd:TIGR01186 241 AE-----RIAQRMNTG--PITKTADKGPRSALQLMRDERVDSL 276
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
10-237 |
3.04e-37 |
|
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid transport and metabolism];
Pssm-ID: 440180 [Multi-domain] Cd Length: 257 Bit Score: 140.56 E-value: 3.04e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 10 PPVAQLAGVSQHYGKTVALNNITLDIPARCMVGLIGPDGVGKSSLLSLISGARVIEQGNVMVLGGDMRD-PKHrrdvcpR 88
Cdd:COG0411 2 DPLLEVRGLTKRFGGLVAVDDVSLEVERGEIVGLIGPNGAGKTTLFNLITGFYRPTSGRILFDGRDITGlPPH------R 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 89 IAWMpqGLGK-----NLYHTLSVYENV-------------DFFARLFGHDKAEREVR--INELLTSTGLAPFRDRPAGKL 148
Cdd:COG0411 76 IARL--GIARtfqnpRLFPELTVLENVlvaaharlgrgllAALLRLPRARREEREARerAEELLERVGLADRADEPAGNL 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 149 SGGMKQKLGLCCALIHDPELLILDEPTTGVDPLSRSQFWDLIDSIRQRQS--------NMSVLVATAymeeaerfDWLVA 220
Cdd:COG0411 154 SYGQQRRLEIARALATEPKLLLLDEPAAGLNPEETEELAELIRRLRDERGitilliehDMDLVMGLA--------DRIVV 225
|
250
....*....|....*..
gi 732682709 221 MNAGEVLATGSAEELRQ 237
Cdd:COG0411 226 LDFGRVIAEGTPAEVRA 242
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
17-236 |
3.40e-37 |
|
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ABC transporter subfamily is involved in the transport of the hydrophobic amino acids leucine, isoleucine and valine. MJ1267 is a branched-chain amino acid transporter with 29% similarity to both the LivF and LivG components of the E. coli branched-chain amino acid transporter. MJ1267 contains an insertion from residues 114 to 123 characteristic of LivG (Leucine-Isoleucine-Valine) homologs. The branched-chain amino acid transporter from E. coli comprises a heterodimer of ABCs (LivF and LivG), a heterodimer of six-helix TM domains (LivM and LivH), and one of two alternative soluble periplasmic substrate binding proteins (LivK or LivJ).
Pssm-ID: 213186 [Multi-domain] Cd Length: 236 Bit Score: 139.88 E-value: 3.40e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 17 GVSQHYGKTVALNNITLDIPARCMVGLIGPDGVGKSSLLSLISGARVIEQGNVMVLGGDM-RDPKHRRDVcpriawmpQG 95
Cdd:cd03219 5 GLTKRFGGLVALDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFDGEDItGLPPHEIAR--------LG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 96 LGK-----NLYHTLSVYENV-----------DFFARLFGHDKAEREvRINELLTSTGLAPFRDRPAGKLSGGMKQKLGLC 159
Cdd:cd03219 77 IGRtfqipRLFPELTVLENVmvaaqartgsgLLLARARREEREARE-RAEELLERVGLADLADRPAGELSYGQQRRLEIA 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 160 CALIHDPELLILDEPTTGVDPLSRSQFWDLIDSIRQRqsNMSVLVA----TAYMEEAERfdwLVAMNAGEVLATGSAEEL 235
Cdd:cd03219 156 RALATDPKLLLLDEPAAGLNPEETEELAELIRELRER--GITVLLVehdmDVVMSLADR---VTVLDQGRVIAEGTPDEV 230
|
.
gi 732682709 236 R 236
Cdd:cd03219 231 R 231
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
277-485 |
3.75e-37 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 138.80 E-value: 3.75e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 277 IEARDLTMRFGSFVAVDHVNFRIPRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGEAWLFGQPVDPKDIDT-RRRVGYMS 355
Cdd:COG4619 1 LELEGLSFRVGGKPILSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIYLDGKPLSAMPPPEwRRQVAYVP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 356 QAFSLYNElTVRQNLELHARLFHIPEAeiPARVAEMSERFKLNdvEDIL---PESLPLGIRQRLSLAVAVIHRPEMLILD 432
Cdd:COG4619 81 QEPALWGG-TVRDNLPFPFQLRERKFD--RERALELLERLGLP--PDILdkpVERLSGGERQRLALIRALLLQPDVLLLD 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 732682709 433 EPTSGVDPVARDMFWQLMVDLSRQDKVTIFISTHFMNEAER-CDRISLMHAGKV 485
Cdd:COG4619 156 EPTSALDPENTRRVEELLREYLAEEGRAVLWVSHDPEQIERvADRVLTLEAGRL 209
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
9-235 |
6.49e-37 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 142.28 E-value: 6.49e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 9 VPPVA-QLAGVSQHYGKTVALNNITLDIPARCMVGLIGPDGVGKSSLLSLISGARVIEQGNVMVLGGDMrdPKHRRDVCP 87
Cdd:PRK13536 37 MSTVAiDLAGVSKSYGDKAVVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKITVLGVPV--PARARLARA 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 88 RIAWMPQGlgKNLYHTLSVYENVDFFARLFGHDKAEREVRINELLTSTGLAPFRDRPAGKLSGGMKQKLGLCCALIHDPE 167
Cdd:PRK13536 115 RIGVVPQF--DNLDLEFTVRENLLVFGRYFGMSTREIEAVIPSLLEFARLESKADARVSDLSGGMKRRLTLARALINDPQ 192
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 732682709 168 LLILDEPTTGVDPLSRSQFWDLIDSIRQRqsNMSVLVATAYMEEAERF-DWLVAMNAGEVLATGSAEEL 235
Cdd:PRK13536 193 LLILDEPTTGLDPHARHLIWERLRSLLAR--GKTILLTTHFMEEAERLcDRLCVLEAGRKIAEGRPHAL 259
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
277-489 |
9.26e-37 |
|
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter subfamily specific for the transport of dipeptides, oligopeptides (OppD), and nickel (NikDE). The NikABCDE system of E. coli belongs to this family and is composed of the periplasmic binding protein NikA, two integral membrane components (NikB and NikC), and two ATPase (NikD and NikE). The NikABCDE transporter is synthesized under anaerobic conditions to meet the increased demand for nickel resulting from hydrogenase synthesis. The molecular mechanism of nickel uptake in many bacteria and most archaea is not known. Many other members of this ABC family are also involved in the uptake of dipeptides and oligopeptides. The oligopeptide transport system (Opp) is a five-component ABC transport composed of a membrane-anchored substrate binding proteins (SRP), OppA, two transmembrane proteins, OppB and OppC, and two ATP-binding domains, OppD and OppF.
Pssm-ID: 213224 [Multi-domain] Cd Length: 228 Bit Score: 138.02 E-value: 9.26e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 277 IEARDLTMRF----GSFVAVDHVNFRIPRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGEAWLFGQPVDPKDI----DTR 348
Cdd:cd03257 2 LEVKNLSVSFptggGSVKALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGKDLLKLSRrlrkIRR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 349 RRVGYMSQ--AFSLYNELTVRQNLE--LHARLFHIPEAEIPARVAEMSERFKLN-DVEDILPESLPLGIRQRLSLAVAVI 423
Cdd:cd03257 82 KEIQMVFQdpMSSLNPRMTIGEQIAepLRIHGKLSKKEARKEAVLLLLVGVGLPeEVLNRYPHELSGGQRQRVAIARALA 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 732682709 424 HRPEMLILDEPTSGVDPVARDMFWQLMVDLSRQDKVTIFISTHFMNEAER-CDRISLMHAGKVLASG 489
Cdd:cd03257 162 LNPKLLIADEPTSALDVSVQAQILDLLKKLQEELGLTLLFITHDLGVVAKiADRVAVMYAGKIVEEG 228
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
277-485 |
1.25e-36 |
|
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) proteins function from bacteria to human, mediating the translocation of substances into and out of cells or organelles. ABC transporters contain two transmembrane-spanning domains (TMDs) or subunits and two nucleotide binding domains (NBDs) or subunits that couple transport to the hydrolysis of ATP. In the maltose transport system, the periplasmic maltose binding protein (MBP) stimulates the ATPase activity of the membrane-associated transporter, which consists of two transmembrane subunits, MalF and MalG, and two copies of the ATP binding subunit, MalK, and becomes tightly bound to the transporter in the catalytic transition state, ensuring that maltose is passed to the transporter as ATP is hydrolyzed.
Pssm-ID: 213268 [Multi-domain] Cd Length: 213 Bit Score: 137.39 E-value: 1.25e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 277 IEARDLTMRFGSFVAVDHVNFRIPRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGEAWLFGQPV---DPKDidtrRRVGY 353
Cdd:cd03301 1 VELENVTKRFGNVTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGRDVtdlPPKD----RDIAM 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 354 MSQAFSLYNELTVRQNLELHARLFHIPEAEIPARVAEMSERFKLNDVEDILPESLPLGIRQRLSLAVAVIHRPEMLILDE 433
Cdd:cd03301 77 VFQNYALYPHMTVYDNIAFGLKLRKVPKDEIDERVREVAELLQIEHLLDRKPKQLSGGQRQRVALGRAIVREPKVFLMDE 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 732682709 434 PTSGVDPVARDMFWQLMVDLSRQDKVTIFISTHFMNEAER-CDRISLMHAGKV 485
Cdd:cd03301 157 PLSNLDAKLRVQMRAELKRLQQRLGTTTIYVTHDQVEAMTmADRIAVMNDGQI 209
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
8-212 |
1.28e-36 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 138.68 E-value: 1.28e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 8 PVPPVAQLAGVSQHY----GKTVALNNITLDIPARCMVGLIGPDGVGKSSLLSLISGARVIEQGNVMVLGGDMRDPKhrr 83
Cdd:COG1116 3 AAAPALELRGVSKRFptggGGVTALDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPTSGEVLVDGKPVTGPG--- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 84 dvcPRIAWMPQGlgknlyHTL----SVYENVDFFARLFGHDKAEREVRINELLTSTGLAPFRDRPAGKLSGGMKQKLGLC 159
Cdd:COG1116 80 ---PDRGVVFQE------PALlpwlTVLDNVALGLELRGVPKAERRERARELLELVGLAGFEDAYPHQLSGGMRQRVAIA 150
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 732682709 160 CALIHDPELLILDEPTTGVDPLSRSQFWDLIDSIRQRQsNMSVLVATAYMEEA 212
Cdd:COG1116 151 RALANDPEVLLMDEPFGALDALTRERLQDELLRLWQET-GKTVLFVTHDVDEA 202
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
218-500 |
1.40e-36 |
|
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: 146.06 E-value: 1.40e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 218 LVAMNAGEVLA--TGSAEELRQQTQSATLEEAFINLLPQAQRQAHQAvvippyqPENAEIAIEARDLTMRF--GSFVAVD 293
Cdd:COG4987 280 LAALALFEALAplPAAAQHLGRVRAAARRLNELLDAPPAVTEPAEPA-------PAPGGPSLELEDVSFRYpgAGRPVLD 352
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 294 HVNFRIPRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGEAWLFGQPVDPKDIDT-RRRVGYMSQAFSLYNElTVRQNLEL 372
Cdd:COG4987 353 GLSLTLPPGERVAIVGPSGSGKSTLLALLLRFLDPQSGSITLGGVDLRDLDEDDlRRRIAVVPQRPHLFDT-TLRENLRL 431
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 373 hARlfhiPEAEiPARVAEMSERFKLNDVEDILPESL--PLGI---------RQRLSLAVAVIHRPEMLILDEPTSGVDPV 441
Cdd:COG4987 432 -AR----PDAT-DEELWAALERVGLGDWLAALPDGLdtWLGEggrrlsggeRRRLALARALLRDAPILLLDEPTEGLDAA 505
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 732682709 442 ARDMFWQLMVDLSrQDKVTIFIsTHFMNEAERCDRISLMHAGKVLASGTPQELVEKRGA 500
Cdd:COG4987 506 TEQALLADLLEAL-AGRTVLLI-THRLAGLERMDRILVLEDGRIVEQGTHEELLAQNGR 562
|
|
| LPS_export_lptB |
TIGR04406 |
LPS export ABC transporter ATP-binding protein; Members of this fmaily are LptB, the ... |
279-496 |
1.43e-36 |
|
LPS export ABC transporter ATP-binding protein; Members of this fmaily are LptB, the ATP-binding cassette protein of an ABC transporter involved in lipopolysaccharide export. [Cell envelope, Biosynthesis and degradation of surface polysaccharides and lipopolysaccharides, Transport and binding proteins, Other]
Pssm-ID: 275199 [Multi-domain] Cd Length: 239 Bit Score: 138.18 E-value: 1.43e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 279 ARDLTMRFGSFVAVDHVNFRIPRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGEAWLFGQPVDPKDIDTRRR--VGYMSQ 356
Cdd:TIGR04406 4 AENLIKSYKKRKVVNDVSLSVKSGEIVGLLGPNGAGKTTSFYMIVGLVRPDAGKILIDGQDITHLPMHERARlgIGYLPQ 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 357 AFSLYNELTVRQN----LELHARLfhiPEAEIPARVAEMSERFKLNDVEDILPESLPLGIRQRLSLAVAVIHRPEMLILD 432
Cdd:TIGR04406 84 EASIFRKLTVEENimavLEIRKDL---DRAEREERLEALLEEFQISHLRDNKAMSLSGGERRRVEIARALATNPKFILLD 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 732682709 433 EPTSGVDPVARDMFWQLMVDLsRQDKVTIFISTHFMNEA-ERCDRISLMHAGKVLASGTPQELVE 496
Cdd:TIGR04406 161 EPFAGVDPIAVGDIKKIIKHL-KERGIGVLITDHNVRETlDICDRAYIISDGKVLAEGTPAEIVA 224
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
277-488 |
1.52e-36 |
|
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: 135.25 E-value: 1.52e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 277 IEARDLTMRFGSFVAVDHVNFRIPRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGEAWLFGQPVDPKDIDTRRRVG-YMs 355
Cdd:cd03216 1 LELRGITKRFGGVKALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVDGKEVSFASPRDARRAGiAM- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 356 qafslyneltVRQnlelharlfhipeaeiparvaemserfklndvedilpesLPLGIRQRLSLAVAVIHRPEMLILDEPT 435
Cdd:cd03216 80 ----------VYQ---------------------------------------LSVGERQMVEIARALARNARLLILDEPT 110
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 732682709 436 SGVDPVARDMFWQLMVDLSRQDKVTIFIStHFMNEAER-CDRISLMHAGKVLAS 488
Cdd:cd03216 111 AALTPAEVERLFKVIRRLRAQGVAVIFIS-HRLDEVFEiADRVTVLRDGRVVGT 163
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
14-230 |
3.43e-36 |
|
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: 135.81 E-value: 3.43e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 14 QLAGVSQHYGKTVALNNITLDIPARCMVGLIGPDGVGKSSLLSLISGARVIEQGNVMVLGGDMRDPKhrrDVCPRIAWMP 93
Cdd:cd03268 2 KTNDLTKTYGKKRVLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEITFDGKSYQKNI---EALRRIGALI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 94 QGLGknLYHTLSVYENVDFFARLFGHDKAerevRINELLTSTGLAPFRDRPAGKLSGGMKQKLGLCCALIHDPELLILDE 173
Cdd:cd03268 79 EAPG--FYPNLTARENLRLLARLLGIRKK----RIDEVLDVVGLKDSAKKKVKGFSLGMKQRLGIALALLGNPDLLILDE 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 732682709 174 PTTGVDPLSRSQFWDLIdsIRQRQSNMSVLVATAYMEEAERF-DWLVAMNAGEVLATG 230
Cdd:cd03268 153 PTNGLDPDGIKELRELI--LSLRDQGITVLISSHLLSEIQKVaDRIGIINKGKLIEEG 208
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
278-489 |
5.51e-36 |
|
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related proteins; ABC transporters, involved in the uptake of siderophores, heme, and vitamin B12, are widely conserved in bacteria and archaea. Only very few species lack representatives of the siderophore family transporters. The E. coli BtuCD protein is an ABC transporter mediating vitamin B12 uptake. The two ATP-binding cassettes (BtuD) are in close contact with each other, as are the two membrane-spanning subunits (BtuC); this arrangement is distinct from that observed for the E. coli lipid flippase MsbA. The BtuC subunits provide 20 transmembrane helices grouped around a translocation pathway that is closed to the cytoplasm by a gate region, whereas the dimer arrangement of the BtuD subunits resembles the ATP-bound form of the Rad50 DNA repair enzyme. A prominent cytoplasmic loop of BtuC forms the contact region with the ATP-binding cassette and represent a conserved motif among the ABC transporters.
Pssm-ID: 213181 [Multi-domain] Cd Length: 180 Bit Score: 134.10 E-value: 5.51e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 278 EARDLTMRFGSFVAVDHVNFRIPRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGEAWLFGQPV---DPKDIdtRRRVGYM 354
Cdd:cd03214 1 EVENLSVGYGGRTVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDGKDLaslSPKEL--ARKIAYV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 355 SQAfslyneltvrqnLELharlfhipeaeipARVAEMSERFkLNdvedilpeSLPLGIRQRLSLAVAVIHRPEMLILDEP 434
Cdd:cd03214 79 PQA------------LEL-------------LGLAHLADRP-FN--------ELSGGERQRVLLARALAQEPPILLLDEP 124
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 732682709 435 TSGVDPVARDMFWQLMVDLSRQDKVTIFISTHFMNEAER-CDRISLMHAGKVLASG 489
Cdd:cd03214 125 TSHLDIAHQIELLELLRRLARERGKTVVMVLHDLNLAARyADRVILLKDGRIVAQG 180
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
277-516 |
4.08e-35 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 136.75 E-value: 4.08e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 277 IEARDLTMRF----GSFVAVDHVNFRIPRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGEAWLFGQPV---DPKDI-DTR 348
Cdd:COG1135 2 IELENLSKTFptkgGPVTALDDVSLTIEKGEIFGIIGYSGAGKSTLIRCINLLERPTSGSVLVDGVDLtalSERELrAAR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 349 RRVGYMSQAFSLYNELTVRQNLELHARLFHIPEAEIPARVAEMSERFKLNDVEDILPESLPLGIRQRLSLAVAVIHRPEM 428
Cdd:COG1135 82 RKIGMIFQHFNLLSSRTVAENVALPLEIAGVPKAEIRKRVAELLELVGLSDKADAYPSQLSGGQKQRVGIARALANNPKV 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 429 LILDEPTSGVDPVARDMFWQLMVDLSRQDKVTIFISTHFMNEAER-CDRISLMHAGKVLASGT-------PQ-----ELV 495
Cdd:COG1135 162 LLCDEATSALDPETTRSILDLLKDINRELGLTIVLITHEMDVVRRiCDRVAVLENGRIVEQGPvldvfanPQseltrRFL 241
|
250 260
....*....|....*....|.
gi 732682709 496 EKRGAASLEEAFIAYLQEAAG 516
Cdd:COG1135 242 PTVLNDELPEELLARLREAAG 262
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
252-500 |
4.16e-35 |
|
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: 143.44 E-value: 4.16e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 252 LPQAQRQAHQAVVIPPYQPEnaeiaIEARDLTMRFG--SFVAVDHVNFRIPRGEIFGFLGSNGCGKSTTMKMLTGLLPAS 329
Cdd:COG2274 454 LPPEREEGRSKLSLPRLKGD-----IELENVSFRYPgdSPPVLDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEPT 528
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 330 EGEAWLFGQPVdpKDIDT---RRRVGYMSQAFSLYNElTVRQNLELHARlfHIPEAEIpARVAEMSErfkLNDVEDILPE 406
Cdd:COG2274 529 SGRILIDGIDL--RQIDPaslRRQIGVVLQDVFLFSG-TIRENITLGDP--DATDEEI-IEAARLAG---LHDFIEALPM 599
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 407 -----------SLPLGIRQRLSLAVAVIHRPEMLILDEPTSGVDPVARDMFWQLMVDLSRqdKVTIFISTHFMNEAERCD 475
Cdd:COG2274 600 gydtvvgeggsNLSGGQRQRLAIARALLRNPRILILDEATSALDAETEAIILENLRRLLK--GRTVIIIAHRLSTIRLAD 677
|
250 260
....*....|....*....|....*
gi 732682709 476 RISLMHAGKVLASGTPQELVEKRGA 500
Cdd:COG2274 678 RIIVLDKGRIVEDGTHEELLARKGL 702
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
277-494 |
1.07e-34 |
|
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of the LIV-I bacterial ABC-type two-component transport system that imports neutral, branched-chain amino acids. The E. coli branched-chain amino acid transporter comprises a heterodimer of ABC transporters (LivF and LivG), a heterodimer of six-helix TM domains (LivM and LivH), and one of two alternative soluble periplasmic substrate binding proteins (LivK or LivJ). ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules.
Pssm-ID: 213191 [Multi-domain] Cd Length: 222 Bit Score: 132.17 E-value: 1.07e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 277 IEARDLTMRFGSFVAVDHVNFRIPRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGEAWLFGQPVDPKDIDTRRR--VGYM 354
Cdd:cd03224 1 LEVENLNAGYGKSQILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDGRDITGLPPHERARagIGYV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 355 SQAFSLYNELTVRQNLELHARLFhiPEAEIPARVAEMSERF-KLNDVEDILPESLPLGIRQRLSLAVAVIHRPEMLILDE 433
Cdd:cd03224 81 PEGRRIFPELTVEENLLLGAYAR--RRAKRKARLERVYELFpRLKERRKQLAGTLSGGEQQMLAIARALMSRPKLLLLDE 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 732682709 434 PTSGVDPVARDMFWQLMVDLsRQDKVTIFISTHFMNEA-ERCDRISLMHAGKVLASGTPQEL 494
Cdd:cd03224 159 PSEGLAPKIVEEIFEAIREL-RDEGVTILLVEQNARFAlEIADRAYVLERGRVVLEGTAAEL 219
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
10-228 |
1.79e-34 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 131.70 E-value: 1.79e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 10 PPVAQLAGVSQHYG----KTVALNNITLDIPARCMVGLIGPDGVGKSSLLSLISGARVIEQGNVMVLG---GDMRDP--- 79
Cdd:COG1136 2 SPLLELRNLTKSYGtgegEVTALRGVSLSIEAGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVLIDGqdiSSLSERela 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 80 KHRRDvcpRIAWMPQGLgkNLYHTLSVYENVDFFARLFGHDKAEREVRINELLTSTGLAPFRDRPAGKLSGGMKQKLGLC 159
Cdd:COG1136 82 RLRRR---HIGFVFQFF--NLLPELTALENVALPLLLAGVSRKERRERARELLERVGLGDRLDHRPSQLSGGQQQRVAIA 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 732682709 160 CALIHDPELLILDEPTTGVDPLSRSQFWDLIDSIRqRQSNMSVLVATAYMEEAERFDWLVAMNAGEVLA 228
Cdd:COG1136 157 RALVNRPKLILADEPTGNLDSKTGEEVLELLRELN-RELGTTIVMVTHDPELAARADRVIRLRDGRIVS 224
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
9-514 |
3.07e-34 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 138.38 E-value: 3.07e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 9 VPPVAQLAGVSQHYGKTVALNNITLDIPARCMVGLIGPDGVGKSSLLSLISGARVIEQGNVMVLGGDMRDPKHRRDVCPR 88
Cdd:PRK09700 2 ATPYISMAGIGKSFGPVHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNINYNKLDHKLAAQLG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 89 IAWMPQGLgkNLYHTLSVYENVdFFARL-----FGH---DKAEREVRINELLTSTGLAPFRDRPAGKLSGGMKQKLGLCC 160
Cdd:PRK09700 82 IGIIYQEL--SVIDELTVLENL-YIGRHltkkvCGVniiDWREMRVRAAMMLLRVGLKVDLDEKVANLSISHKQMLEIAK 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 161 ALIHDPELLILDEPTTGvdpLSRSQFWDLIDSIRQ-RQSNMSVLVATAYMEEAERF-DWLVAMNAGEVLATG-----SAE 233
Cdd:PRK09700 159 TLMLDAKVIIMDEPTSS---LTNKEVDYLFLIMNQlRKEGTAIVYISHKLAEIRRIcDRYTVMKDGSSVCSGmvsdvSND 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 234 ELRQQTQSATLEEAFINLLPQAQRQAHQAVvippyqpenaeiaIEARDLTMRfgSFVAVDHVNFRIPRGEIFGFLGSNGC 313
Cdd:PRK09700 236 DIVRLMVGRELQNRFNAMKENVSNLAHETV-------------FEVRNVTSR--DRKKVRDISFSVCRGEILGFAGLVGS 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 314 GKSTTMKMLTGLLPASEGEAWLFGQPVDPKD------------IDTRRRVGYMSQaFSLYNELTVRQNLELHAR-----L 376
Cdd:PRK09700 301 GRTELMNCLFGVDKRAGGEIRLNGKDISPRSpldavkkgmayiTESRRDNGFFPN-FSIAQNMAISRSLKDGGYkgamgL 379
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 377 FHIPEAEIPARVAEMSERFKLNDVEDILPEsLPLGIRQRLSLAVAVIHRPEMLILDEPTSGVDPVARDMFWQLMVDLSRQ 456
Cdd:PRK09700 380 FHEVDEQRTAENQRELLALKCHSVNQNITE-LSGGNQQKVLISKWLCCCPEVIIFDEPTRGIDVGAKAEIYKVMRQLADD 458
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*...
gi 732682709 457 DKVTIFISTHFMNEAERCDRISLMHAGKVlasgtpQELVEKRGAASLEEAFIAYLQEA 514
Cdd:PRK09700 459 GKVILMVSSELPEIITVCDRIAVFCEGRL------TQILTNRDDMSEEEIMAWALPQE 510
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
8-235 |
3.29e-34 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 133.39 E-value: 3.29e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 8 PVPPVaQLAGVSQHYGKTVALNNITLDI-PARCMvGLIGPDGVGKSSLLSLISGARVIEQGNVMVLGGDMrdPKHRRDVC 86
Cdd:PRK13537 4 SVAPI-DFRNVEKRYGDKLVVDGLSFHVqRGECF-GLLGPNGAGKTTTLRMLLGLTHPDAGSISLCGEPV--PSRARHAR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 87 PRIAWMPQGlgKNLYHTLSVYENVDFFARLFGHDKAEREVRINELLTSTGLAPFRDRPAGKLSGGMKQKLGLCCALIHDP 166
Cdd:PRK13537 80 QRVGVVPQF--DNLDPDFTVRENLLVFGRYFGLSAAAARALVPPLLEFAKLENKADAKVGELSGGMKRRLTLARALVNDP 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 167 ELLILDEPTTGVDPLSRSQFWDLIDSIRQRqsNMSVLVATAYMEEAERF-DWLVAMNAGEVLATGSAEEL 235
Cdd:PRK13537 158 DVLVLDEPTTGLDPQARHLMWERLRSLLAR--GKTILLTTHFMEEAERLcDRLCVIEEGRKIAEGAPHAL 225
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
14-237 |
4.32e-34 |
|
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of the LIV-I bacterial ABC-type two-component transport system that imports neutral, branched-chain amino acids. The E. coli branched-chain amino acid transporter comprises a heterodimer of ABC transporters (LivF and LivG), a heterodimer of six-helix TM domains (LivM and LivH), and one of two alternative soluble periplasmic substrate binding proteins (LivK or LivJ). ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules.
Pssm-ID: 213191 [Multi-domain] Cd Length: 222 Bit Score: 130.25 E-value: 4.32e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 14 QLAGVSQHYGKTVALNNITLDIPARCMVGLIGPDGVGKSSLLSLISGARVIEQGNVMVLGGDMRD-PKHRRdvcPR--IA 90
Cdd:cd03224 2 EVENLNAGYGKSQILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDGRDITGlPPHER---ARagIG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 91 WMPQGlgKNLYHTLSVYENVDFFARLFGHDKAEREV-RINELLTStgLAPFRDRPAGKLSGGMKQKLGLCCALIHDPELL 169
Cdd:cd03224 79 YVPEG--RRIFPELTVEENLLLGAYARRRAKRKARLeRVYELFPR--LKERRKQLAGTLSGGEQQMLAIARALMSRPKLL 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 732682709 170 ILDEPTTGVDPLSRSQFWDLIDSIRQRQsnMSVLV----ATAYMEEAERFdwlVAMNAGEVLATGSAEELRQ 237
Cdd:cd03224 155 LLDEPSEGLAPKIVEEIFEAIRELRDEG--VTILLveqnARFALEIADRA---YVLERGRVVLEGTAAELLA 221
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
14-240 |
5.12e-34 |
|
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: 130.70 E-value: 5.12e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 14 QLAGVSQHYGKTVALNNITLDIPARCMVGLIGPDGVGKSSLLSLISGARVIEQGNVMVLGGDMRD--PKHRRDVCPRIAW 91
Cdd:cd03261 2 ELRGLTKSFGGRTVLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGEDISGlsEAELYRLRRRMGM 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 92 MPQGLGknLYHTLSVYENVDFFARLFGhDKAEREVR--INELLTSTGLAPFRDRPAGKLSGGMKQKLGLCCALIHDPELL 169
Cdd:cd03261 82 LFQSGA--LFDSLTVFENVAFPLREHT-RLSEEEIReiVLEKLEAVGLRGAEDLYPAELSGGMKKRVALARALALDPELL 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 732682709 170 ILDEPTTGVDPLSRSQFWDLIDSIrQRQSNMSVLVATAYMEEAERF-DWLVAMNAGEVLATGSAEELRQQTQ 240
Cdd:cd03261 159 LYDEPTAGLDPIASGVIDDLIRSL-KKELGLTSIMVTHDLDTAFAIaDRIAVLYDGKIVAEGTPEELRASDD 229
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
19-235 |
8.50e-34 |
|
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ABC-type transporter encoded by metN of the metNPQ operon in Bacillus subtilis that is involved in methionine transport. Other members of this system include the MetP permease and the MetQ substrate binding protein. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213225 [Multi-domain] Cd Length: 233 Bit Score: 130.01 E-value: 8.50e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 19 SQHYGKTVALNNITLDIPARCMVGLIGPDGVGKSSLLSLISGARVIEQGNVMVLGGDM--RDPKHRRDVCPRIAWMPQGL 96
Cdd:cd03258 12 GDTGGKVTALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGSVLVDGTDLtlLSGKELRKARRRIGMIFQHF 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 97 gkNLYHTLSVYENVDFFARLFGHDKAEREVRINELLTSTGLAPFRDRPAGKLSGGMKQKLGLCCALIHDPELLILDEPTT 176
Cdd:cd03258 92 --NLLSSRTVFENVALPLEIAGVPKAEIEERVLELLELVGLEDKADAYPAQLSGGQKQRVGIARALANNPKVLLCDEATS 169
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 177 GVDPLSRSQFWDLIDSIrQRQSNMSVLVATAYMEEAERFDWLVA-MNAGEVLATGSAEEL 235
Cdd:cd03258 170 ALDPETTQSILALLRDI-NRELGLTIVLITHEMEVVKRICDRVAvMEKGEVVEEGTVEEV 228
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
10-242 |
8.56e-34 |
|
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: 136.96 E-value: 8.56e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 10 PPVAQLAGVSQHY-----GKTVALNNITLDIPARCMVGLIGPDGVGKSSLLSLISGARVIEQGNVMVLGGDMRDPKHR-- 82
Cdd:COG1123 258 EPLLEVRNLSKRYpvrgkGGVRAVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRPTSGSILFDGKDLTKLSRRsl 337
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 83 RDVCPRIAWMPQglgkNLYHTL----SVYENVDFFARLFGH-DKAEREVRINELLTSTGLAP-FRDRPAGKLSGGMKQKL 156
Cdd:COG1123 338 RELRRRVQMVFQ----DPYSSLnprmTVGDIIAEPLRLHGLlSRAERRERVAELLERVGLPPdLADRYPHELSGGQRQRV 413
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 157 GLCCALIHDPELLILDEPTTGVDPLSRSQFWDLIDSIrQRQSNMSVLVATAYMEEAERF-DWLVAMNAGEVLATGSAEEL 235
Cdd:COG1123 414 AIARALALEPKLLILDEPTSALDVSVQAQILNLLRDL-QRELGLTYLFISHDLAVVRYIaDRVAVMYDGRIVEDGPTEEV 492
|
....*..
gi 732682709 236 RQQTQSA 242
Cdd:COG1123 493 FANPQHP 499
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
14-212 |
1.12e-33 |
|
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: 129.13 E-value: 1.12e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 14 QLAGVSQHYG----KTVALNNITLDIPARCMVGLIGPDGVGKSSLLSLISGARVIEQGNVMVLGGDMRDPKhrrdvcPRI 89
Cdd:cd03293 2 EVRNVSKTYGggggAVTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVDGEPVTGPG------PDR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 90 AWMPQGlgKNLYHTLSVYENVDFFARLFGHDKAEREVRINELLTSTGLAPFRDRPAGKLSGGMKQKLGLCCALIHDPELL 169
Cdd:cd03293 76 GYVFQQ--DALLPWLTVLDNVALGLELQGVPKAEARERAEELLELVGLSGFENAYPHQLSGGMRQRVALARALAVDPDVL 153
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 732682709 170 ILDEPTTGVDPLSRSQFWDLIDSIRQRQSNMSVLVaTAYMEEA 212
Cdd:cd03293 154 LLDEPFSALDALTREQLQEELLDIWRETGKTVLLV-THDIDEA 195
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
14-235 |
1.79e-33 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 132.53 E-value: 1.79e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 14 QLAGVSQHYGKTVALNNITLDIPARCMVGLIGPDGVGKSSLLSLISGARVIEQGNVMVLGGDMRD-PKHRRDvcprIAWM 92
Cdd:COG3842 7 ELENVSKRYGDVTALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRILLDGRDVTGlPPEKRN----VGMV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 93 PQGlgknlY----HtLSVYENVDFFARLFGHDKAEREVRINELLTSTGLAPFRDRPAGKLSGGMKQKLGLCCALIHDPEL 168
Cdd:COG3842 83 FQD-----YalfpH-LTVAENVAFGLRMRGVPKAEIRARVAELLELVGLEGLADRYPHQLSGGQQQRVALARALAPEPRV 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 732682709 169 LILDEPTTGVDPLSRSQFWDLIDSIrQRQSNMSVLVATAYMEEAERF-DWLVAMNAGEVLATGSAEEL 235
Cdd:COG3842 157 LLLDEPLSALDAKLREEMREELRRL-QRELGITFIYVTHDQEEALALaDRIAVMNDGRIEQVGTPEEI 223
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
14-206 |
1.96e-33 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 128.63 E-value: 1.96e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 14 QLAGVSQHY-GKTVALNNITLDIPARCMVGLIGPDGVGKSSLLSLISGARVIEQGNVMVLGGDMRD------PKHRRDvc 86
Cdd:COG2884 3 RFENVSKRYpGGREALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLVNGQDLSRlkrreiPYLRRR-- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 87 priawmpqgLG------KNLYHtLSVYENVDFFARLFGHDKAEREVRINELLTSTGLAPFRDRPAGKLSGGMKQKLGLCC 160
Cdd:COG2884 81 ---------IGvvfqdfRLLPD-RTVYENVALPLRVTGKSRKEIRRRVREVLDLVGLSDKAKALPHELSGGEQQRVAIAR 150
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 732682709 161 ALIHDPELLILDEPTTGVDPLSRSQFWDLIDSIRQRqsNMSVLVAT 206
Cdd:COG2884 151 ALVNRPELLLADEPTGNLDPETSWEIMELLEEINRR--GTTVLIAT 194
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
277-485 |
2.71e-33 |
|
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ATP-binding components of the bacterial periplasmic histidine and glutamine permeases, respectively. Histidine permease is a multi-subunit complex containing the HisQ and HisM integral membrane subunits and two copies of HisP. HisP has properties intermediate between those of integral and peripheral membrane proteins and is accessible from both sides of the membrane, presumably by its interaction with HisQ and HisM. The two HisP subunits form a homodimer within the complex. The domain structure of the amino acid uptake systems is typical for prokaryotic extracellular solute binding protein-dependent uptake systems. All of the amino acid uptake systems also have at least one, and in a few cases, two extracellular solute binding proteins located in the periplasm of Gram-negative bacteria, or attached to the cell membrane of Gram-positive bacteria. The best-studied member of the PAAT (polar amino acid transport) family is the HisJQMP system of S. typhimurium, where HisJ is the extracellular solute binding proteins and HisP is the ABC protein.
Pssm-ID: 213229 [Multi-domain] Cd Length: 213 Bit Score: 127.65 E-value: 2.71e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 277 IEARDLTMRFGSFVAVDHVNFRIPRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGEAWLFGQPV--DPKDIDT-RRRVGY 353
Cdd:cd03262 1 IEIKNLHKSFGDFHVLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIDGLKLtdDKKNINElRQKVGM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 354 MSQAFSLYNELTVRQNLELHAR-LFHIPEAEIPARVAEMSERFKLNDVEDILPESLPLGIRQRLSLAVAVIHRPEMLILD 432
Cdd:cd03262 81 VFQQFNLFPHLTVLENITLAPIkVKGMSKAEAEERALELLEKVGLADKADAYPAQLSGGQQQRVAIARALAMNPKVMLFD 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 732682709 433 EPTSGVDPVARDMFWQLMVDLSrQDKVTIFISTHFMNEA-ERCDRISLMHAGKV 485
Cdd:cd03262 161 EPTSALDPELVGEVLDVMKDLA-EEGMTMVVVTHEMGFArEVADRVIFMDDGRI 213
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
228-499 |
3.37e-33 |
|
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: 135.66 E-value: 3.37e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 228 ATGSAEELrqqtqsatleEAFINLLPQAQRQAHQAVvippyqPENAEIAIEARDLTMRF-GSFVAVDHVNFRIPRGEIFG 306
Cdd:COG4988 304 GIAAAEKI----------FALLDAPEPAAPAGTAPL------PAAGPPSIELEDVSFSYpGGRPALDGLSLTIPPGERVA 367
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 307 FLGSNGCGKSTTMKMLTGLLPASEGEAWLFGQPVDPKDIDT-RRRVGYMSQAFSLYNElTVRQNLELHARlfHIPEAEIp 385
Cdd:COG4988 368 LVGPSGAGKSTLLNLLLGFLPPYSGSILINGVDLSDLDPASwRRQIAWVPQNPYLFAG-TIRENLRLGRP--DASDEEL- 443
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 386 ARVAEMSerfklnDVEDILpESLPLGI---------------RQRLSLAVAVIHRPEMLILDEPTSGVDPVARDMFWQLM 450
Cdd:COG4988 444 EAALEAA------GLDEFV-AALPDGLdtplgeggrglsggqAQRLALARALLRDAPLLLLDEPTAHLDAETEAEILQAL 516
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 732682709 451 VDLSRQdkVTIFISTHFMNEAERCDRISLMHAGKVLASGTPQELVEKRG 499
Cdd:COG4988 517 RRLAKG--RTVILITHRLALLAQADRILVLDDGRIVEQGTHEELLAKNG 563
|
|
| GldA_ABC_ATP |
TIGR03522 |
gliding motility-associated ABC transporter ATP-binding subunit GldA; Members of this protein ... |
18-248 |
4.00e-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: 129.89 E-value: 4.00e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 18 VSQHYGKTVALNNITLDIPARCMVGLIGPDGVGKSSLLSLISGARVIEQGNVMVLGGD-MRDPKhrrDVCPRIAWMPQGl 96
Cdd:TIGR03522 8 LTKLYGTQNALDEVSFEAQKGRIVGFLGPNGAGKSTTMKIITGYLPPDSGSVQVCGEDvLQNPK---EVQRNIGYLPEH- 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 97 gKNLYHTLSVYENVDFFARLFGHDKAEREVRINELLTSTGLAPFRDRPAGKLSGGMKQKLGLCCALIHDPELLILDEPTT 176
Cdd:TIGR03522 84 -NPLYLDMYVREYLQFIAGIYGMKGQLLKQRVEEMIELVGLRPEQHKKIGQLSKGYRQRVGLAQALIHDPKVLILDEPTT 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 732682709 177 GVDPLSRSQFWDLIDSIRQRQsnmSVLVATAYMEEAERF-DWLVAMNAGEVLATGSAEELRQQTQSATLEEAF 248
Cdd:TIGR03522 163 GLDPNQLVEIRNVIKNIGKDK---TIILSTHIMQEVEAIcDRVIIINKGKIVADKKLDELSAANKKQVIEVEF 232
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
28-176 |
5.04e-33 |
|
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: 124.68 E-value: 5.04e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 28 LNNITLDIPARCMVGLIGPDGVGKSSLLSLISGARVIEQGNVMVLGGDMRDP--KHRRDvcpRIAWMPQGLgkNLYHTLS 105
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDLTDDerKSLRK---EIGYVFQDP--QLFPRLT 75
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 732682709 106 VYENVDFFARLFGHDKAEREVRINELLTSTGLAPFRDRPAGK----LSGGMKQKLGLCCALIHDPELLILDEPTT 176
Cdd:pfam00005 76 VRENLRLGLLLKGLSKREKDARAEEALEKLGLGDLADRPVGErpgtLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
|
|
| ABC2_membrane_3 |
pfam12698 |
ABC-2 family transporter protein; This family is related to the ABC-2 membrane transporter ... |
569-904 |
9.96e-33 |
|
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: 130.20 E-value: 9.96e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 569 VILMLIMGYGISMDVENLRFAVLDRDQTVSSQAWTLNLSGSRYFIEQPPLTSYDELDRRMRAGDITVAIEIPPNFGRDIA 648
Cdd:pfam12698 15 ILLLGLIFSNAVNDPEELPVAVVDEDNSSLSRQLVRALEASPTVNLVQYVDSEEEAKEALKNGKIDGLLVIPKGFSKDLL 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 649 RGTPVELGVWIDGAMPSRAETVKGYVQAMHQSWLQDVASRQSTPASQSGLMNIETRYRYNPDVKSLPAIVPaVIPLLLMM 728
Cdd:pfam12698 95 KGESATVTVYINSSNLLVSKLILNALQSLLQQLNASALVLLLEALSTSAPIPVESTPLFNPQSGYAYYLVG-LILMIIIL 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 729 IPSMLSALSVVREKELGSIINLYVTPTTRSEFLLGKQLPYIALGMLnFFLLCGLSVFVFGVPHKGSFlTLTLAALLYIII 808
Cdd:pfam12698 174 IGAAIIAVSIVEEKESRIKERLLVSGVSPLQYWLGKILGDFLVGLL-QLLIILLLLFGIGIPFGNLG-LLLLLFLLYGLA 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 809 ATGMGLLISTFMKSQIAAIFGTAIITLIPATqFSGMIDPVASLEGPGRWIGEVYPTSH----FLTIARGTFskaldLTDL 884
Cdd:pfam12698 252 YIALGYLLGSLFKNSEDAQSIIGIVILLLSG-FFGGLFPLEDPPSFLQWIFSIIPFFSpidgLLRLIYGDS-----LWEI 325
|
330 340
....*....|....*....|
gi 732682709 885 WQLFIPLLIAIPLVMGLSIL 904
Cdd:pfam12698 326 APSLIILLLFAVVLLLLALL 345
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
277-484 |
1.05e-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: 124.42 E-value: 1.05e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 277 IEARDLTMRFGSF--VAVDHVNFRIPRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGEAWLFGQPVdpKDIDT---RRRV 351
Cdd:cd03228 1 IEFKNVSFSYPGRpkPVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGVDL--RDLDLeslRKNI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 352 GYMSQAFSLYNElTVRQNLelharlfhipeaeiparvaemserfklndvedilpesLPLGIRQRLSLAVAVIHRPEMLIL 431
Cdd:cd03228 79 AYVPQDPFLFSG-TIRENI-------------------------------------LSGGQRQRIAIARALLRDPPILIL 120
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 732682709 432 DEPTSGVDPVARDMFWQLMVDLSRqdKVTIFISTHFMNEAERCDRISLMHAGK 484
Cdd:cd03228 121 DEATSALDPETEALILEALRALAK--GKTVIVIAHRLSTIRDADRIIVLDDGR 171
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
277-496 |
1.42e-32 |
|
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: 129.02 E-value: 1.42e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 277 IEARDLTMRF----GSFVAVDHVNFRIPRGEIFGFLGSNGCGKSTTMKMLTGLLPA---SEGEAWLFGQPV---DPKDID 346
Cdd:COG0444 2 LEVRNLKVYFptrrGVVKAVDGVSFDVRRGETLGLVGESGSGKSTLARAILGLLPPpgiTSGEILFDGEDLlklSEKELR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 347 TRR--RVGYMSQ-AFSLYNE-LTVRQ----NLELHARLfhiPEAEIPARVAEMSERFKLNDVEDIL---PESLPLGIRQR 415
Cdd:COG0444 82 KIRgrEIQMIFQdPMTSLNPvMTVGDqiaePLRIHGGL---SKAEARERAIELLERVGLPDPERRLdryPHELSGGMRQR 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 416 LSLAVAVIHRPEMLILDEPTSGVDPVARDMFWQLMVDLSRQDKVT-IFIsTHFMNE-AERCDRISLMHAGKVLASGTPQE 493
Cdd:COG0444 159 VMIARALALEPKLLIADEPTTALDVTIQAQILNLLKDLQRELGLAiLFI-THDLGVvAEIADRVAVMYAGRIVEEGPVEE 237
|
...
gi 732682709 494 LVE 496
Cdd:COG0444 238 LFE 240
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
274-507 |
1.61e-32 |
|
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA [Inorganic ion transport and metabolism];
Pssm-ID: 440736 [Multi-domain] Cd Length: 250 Bit Score: 126.74 E-value: 1.61e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 274 EIAIEARDLTMRFGSFVAVDHVNFRIPRGEIFGFLGSNGCGKSTTMKMLTGLLPASEG-EAWLFGQP---VDPKDIdtRR 349
Cdd:COG1119 1 DPLLELRNVTVRRGGKTILDDISWTVKPGEHWAILGPNGAGKSTLLSLITGDLPPTYGnDVRLFGERrggEDVWEL--RK 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 350 RVGYMSQAFSLY--NELTVRQ--------NLELHARlfhiPEAEIPARVAEMSERFKLNDVEDILPESLPLGIRQRLSLA 419
Cdd:COG1119 79 RIGLVSPALQLRfpRDETVLDvvlsgffdSIGLYRE----PTDEQRERARELLELLGLAHLADRPFGTLSQGEQRRVLIA 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 420 VAVIHRPEMLILDEPTSGVDPVARDMFWQLMVDLSRQDKVTIFISTHFMNEAERC-DRISLMHAGKVLASGTPQELVekr 498
Cdd:COG1119 155 RALVKDPELLILDEPTAGLDLGARELLLALLDKLAAEGAPTLVLVTHHVEEIPPGiTHVLLLKDGRVVAAGPKEEVL--- 231
|
....*....
gi 732682709 499 GAASLEEAF 507
Cdd:COG1119 232 TSENLSEAF 240
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
14-235 |
1.87e-32 |
|
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of fundamental importance in the cell physiology of bacteria because phosphate is required as a nutrient. The Pst system of E. coli comprises four distinct subunits encoded by the pstS, pstA, pstB, and pstC genes. The PstS protein is a phosphate-binding protein located in the periplasmic space. PstA and PstC are hydrophobic and they form the transmembrane portion of the Pst system. PstB is the catalytic subunit, which couples the energy of ATP hydrolysis to the import of phosphate across cellular membranes through the Pst system, often referred as ABC-protein. PstB belongs to one of the largest superfamilies of proteins characterized by a highly conserved adenosine triphosphate (ATP) binding cassette (ABC), which is also a nucleotide binding domain (NBD).
Pssm-ID: 213227 [Multi-domain] Cd Length: 227 Bit Score: 125.76 E-value: 1.87e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 14 QLAGVSQHYGKTVALNNITLDIPARCMVGLIGPDGVGKSSLL-------SLISGARVieQGNVMVLGGDMRDPKHRRDVC 86
Cdd:cd03260 2 ELRDLNVYYGDKHALKDISLDIPKGEITALIGPSGCGKSTLLrllnrlnDLIPGAPD--EGEVLLDGKDIYDLDVDVLEL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 87 PRIAWM----PqglgkNLYHtLSVYENVDFFARLFG-HDKAEREVRINELLTSTGLAP-FRDRP-AGKLSGGMKQKLGLC 159
Cdd:cd03260 80 RRRVGMvfqkP-----NPFP-GSIYDNVAYGLRLHGiKLKEELDERVEEALRKAALWDeVKDRLhALGLSGGQQQRLCLA 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 732682709 160 CALIHDPELLILDEPTTGVDPLSRSQFWDLIDSIRQRqsnMSVLVATAYMEEAERF-DWLVAMNAGEVLATGSAEEL 235
Cdd:cd03260 154 RALANEPEVLLLDEPTSALDPISTAKIEELIAELKKE---YTIVIVTHNMQQAARVaDRTAFLLNGRLVEFGPTEQI 227
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
277-497 |
2.08e-32 |
|
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely related to ModC. ModC is an ABC-type transporter and the ATPase component of a molybdate transport system that also includes the periplasmic binding protein ModA and the membrane protein ModB. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213266 [Multi-domain] Cd Length: 235 Bit Score: 125.91 E-value: 2.08e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 277 IEARDLTMRFGSFVaVDHVNFRIPRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGEAWLFGqpvdpKDIDT----RRRVG 352
Cdd:cd03299 1 LKVENLSKDWKEFK-LKNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNG-----KDITNlppeKRDIS 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 353 YMSQAFSLYNELTVRQNLELHARLFHIPEAEIPARVAEMSERFKLNDVEDILPESLPLGIRQRLSLAVAVIHRPEMLILD 432
Cdd:cd03299 75 YVPQNYALFPHMTVYKNIAYGLKKRKVDKKEIERKVLEIAEMLGIDHLLNRKPETLSGGEQQRVAIARALVVNPKILLLD 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 732682709 433 EPTSGVDPVARDMFWQLMVDLSRQDKVTIFISTHFMNEAER-CDRISLMHAGKVLASGTPQELVEK 497
Cdd:cd03299 155 EPFSALDVRTKEKLREELKKIRKEFGVTVLHVTHDFEEAWAlADKVAIMLNGKLIQVGKPEEVFKK 220
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
14-230 |
2.29e-32 |
|
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: 123.70 E-value: 2.29e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 14 QLAGVSQHYGKTVALNNITLDIPARCMVGLIGPDGVGKSSLLSLISGARVIEQGNVMVLGGDMRDPKhRRDVCPRIAWMP 93
Cdd:cd03214 1 EVENLSVGYGGRTVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDGKDLASLS-PKELARKIAYVP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 94 QglgknlyhtlsvyenvdffarlfghdkaerevrineLLTSTGLAPFRDRPAGKLSGGMKQKLGLCCALIHDPELLILDE 173
Cdd:cd03214 80 Q------------------------------------ALELLGLAHLADRPFNELSGGERQRVLLARALAQEPPILLLDE 123
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 174 PTTGVDPlsRSQFwDLIDSIRQ--RQSNMSVLVATAYMEEAERF-DWLVAMNAGEVLATG 230
Cdd:cd03214 124 PTSHLDI--AHQI-ELLELLRRlaRERGKTVVMVLHDLNLAARYaDRVILLKDGRIVAQG 180
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
272-496 |
3.03e-32 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 126.67 E-value: 3.03e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 272 NAEIAIEARDLTMRF--GSFVAVDHVNFRIPRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGEAWLFGQPVDPKDI-DTR 348
Cdd:PRK13635 1 MKEEIIRVEHISFRYpdAATYALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGGMVLSEETVwDVR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 349 RRVGYMSQ---------------AFSLYNEltvrqnlelharlfHIPEAEIPARVAEMSERFKLNDVEDILPESLPLGIR 413
Cdd:PRK13635 81 RQVGMVFQnpdnqfvgatvqddvAFGLENI--------------GVPREEMVERVDQALRQVGMEDFLNREPHRLSGGQK 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 414 QRLSLAVAVIHRPEMLILDEPTSGVDPVARDMFWQLMVDLSRQDKVTIFISTHFMNEAERCDRISLMHAGKVLASGTPQE 493
Cdd:PRK13635 147 QRVAIAGVLALQPDIIILDEATSMLDPRGRREVLETVRQLKEQKGITVLSITHDLDEAAQADRVIVMNKGEILEEGTPEE 226
|
...
gi 732682709 494 LVE 496
Cdd:PRK13635 227 IFK 229
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
277-498 |
4.62e-32 |
|
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; Phosphonates are a class of organophosphorus compounds characterized by a chemically stable carbon-to-phosphorus (C-P) bond. Phosphonates are widespread among naturally occurring compounds in all kingdoms of wildlife, but only prokaryotic microorganisms are able to cleave this bond. Certain bacteria such as E. coli can use alkylphosphonates as a phosphorus source. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213223 [Multi-domain] Cd Length: 241 Bit Score: 124.99 E-value: 4.62e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 277 IEARDLTMRFGS-FVAVDHVNFRIPRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGEAWLFGQPV---DPKDI-DTRRRV 351
Cdd:cd03256 1 IEVENLSKTYPNgKKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGTDInklKGKALrQLRRQI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 352 GYMSQAFSLYNELTVRQNLeLHARLFHI----------PEAEIPaRVAEMSERFKLNDVEDILPESLPLGIRQRLSLAVA 421
Cdd:cd03256 81 GMIFQQFNLIERLSVLENV-LSGRLGRRstwrslfglfPKEEKQ-RALAALERVGLLDKAYQRADQLSGGQQQRVAIARA 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 732682709 422 VIHRPEMLILDEPTSGVDPVARDMFWQLMVDLSRQDKVTIFISTHFMNEAER-CDRISLMHAGKVLASGTPQELVEKR 498
Cdd:cd03256 159 LMQQPKLILADEPVASLDPASSRQVMDLLKRINREEGITVIVSLHQVDLAREyADRIVGLKDGRIVFDGPPAELTDEV 236
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
272-496 |
6.06e-32 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 125.87 E-value: 6.06e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 272 NAEIAIEARDLTMRFGSFV--AVDHVNFRIPRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGEAWLFGQPVDPKDID-TR 348
Cdd:PRK13632 3 NKSVMIKVENVSFSYPNSEnnALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIDGITISKENLKeIR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 349 RRVGYMSQ---------------AFSLYNELtvrqnlelharlfhIPEAEIPARVAEMSERFKLNDVEDILPESLPLGIR 413
Cdd:PRK13632 83 KKIGIIFQnpdnqfigatveddiAFGLENKK--------------VPPKKMKDIIDDLAKKVGMEDYLDKEPQNLSGGQK 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 414 QRLSLAVAVIHRPEMLILDEPTSGVDPVARDMFWQLMVDLSRQDKVTIFISTHFMNEAERCDRISLMHAGKVLASGTPQE 493
Cdd:PRK13632 149 QRVAIASVLALNPEIIIFDESTSMLDPKGKREIKKIMVDLRKTRKKTLISITHDMDEAILADKVIVFSEGKLIAQGKPKE 228
|
...
gi 732682709 494 LVE 496
Cdd:PRK13632 229 ILN 231
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
292-485 |
7.44e-32 |
|
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of the ABC component of a cobalt transport family found in bacteria, archaea, and eukaryota. The transition metal cobalt is an essential component of many enzymes and must be transported into cells in appropriate amounts when needed. The CbiMNQO family ABC transport system is involved in cobalt transport in association with the cobalamin (vitamin B12) biosynthetic pathways. Most cobalt (Cbi) transport systems possess a separate CbiN component, the cobalt-binding periplasmic protein, and they are encoded by the conserved gene cluster cbiMNQO. Both the CbiM and CbiQ proteins are integral cytoplasmic membrane proteins, and the CbiO protein has the linker peptide and the Walker A and B motifs commonly found in the ATPase components of the ABC-type transport systems.
Pssm-ID: 213193 [Multi-domain] Cd Length: 205 Bit Score: 123.14 E-value: 7.44e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 292 VDHVNFRIPRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGEAWLFGQPVDPKDidTRRRVGYMSQ--AFSLYNElTVRQN 369
Cdd:cd03226 16 LDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLNGKPIKAKE--RRKSIGYVMQdvDYQLFTD-SVREE 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 370 LELHARLFHipeaEIPARVAEMSERFKLNDVEDILPESLPLGIRQRLSLAVAVIHRPEMLILDEPTSGVDPVARDMFWQL 449
Cdd:cd03226 93 LLLGLKELD----AGNEQAETVLKDLDLYALKERHPLSLSGGQKQRLAIAAALLSGKDLLIFDEPTSGLDYKNMERVGEL 168
|
170 180 190
....*....|....*....|....*....|....*....
gi 732682709 450 MVDLSRQDKvTIFISTH---FMneAERCDRISLMHAGKV 485
Cdd:cd03226 169 IRELAAQGK-AVIVITHdyeFL--AKVCDRVLLLANGAI 204
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
14-235 |
9.31e-32 |
|
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; Phosphonates are a class of organophosphorus compounds characterized by a chemically stable carbon-to-phosphorus (C-P) bond. Phosphonates are widespread among naturally occurring compounds in all kingdoms of wildlife, but only prokaryotic microorganisms are able to cleave this bond. Certain bacteria such as E. coli can use alkylphosphonates as a phosphorus source. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213223 [Multi-domain] Cd Length: 241 Bit Score: 124.22 E-value: 9.31e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 14 QLAGVSQHYG-KTVALNNITLDIPARCMVGLIGPDGVGKSSLLSLISGARVIEQGNVMVLGGDMRDPKHR--RDVCPRIA 90
Cdd:cd03256 2 EVENLSKTYPnGKKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGTDINKLKGKalRQLRRQIG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 91 WMPQGLgkNLYHTLSVYENV--------DFFARLFGH-DKAEREVRInELLTSTGLAPFRDRPAGKLSGGMKQKLGLCCA 161
Cdd:cd03256 82 MIFQQF--NLIERLSVLENVlsgrlgrrSTWRSLFGLfPKEEKQRAL-AALERVGLLDKAYQRADQLSGGQQQRVAIARA 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 732682709 162 LIHDPELLILDEPTTGVDPLSRSQFWDLIDSIRqRQSNMSVLVATAYMEEAERF-DWLVAMNAGEVLATGSAEEL 235
Cdd:cd03256 159 LMQQPKLILADEPVASLDPASSRQVMDLLKRIN-REEGITVIVSLHQVDLAREYaDRIVGLKDGRIVFDGPPAEL 232
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
290-494 |
1.26e-31 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 125.20 E-value: 1.26e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 290 VAVDHVNFRIPRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGEAWLFGqpVDPKDI----DTRRRVGYMSQafSLYNELT 365
Cdd:PRK13633 24 LALDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVYVDG--LDTSDEenlwDIRNKAGMVFQ--NPDNQIV 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 366 ---VRQNLELHARLFHIPEAEIPARVAEMSERFKLNDVEDILPESLPLGIRQRLSLAVAVIHRPEMLILDEPTSGVDPVA 442
Cdd:PRK13633 100 atiVEEDVAFGPENLGIPPEEIRERVDESLKKVGMYEYRRHAPHLLSGGQKQRVAIAGILAMRPECIIFDEPTAMLDPSG 179
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 732682709 443 RDMFWQLMVDLSRQDKVTIFISTHFMNEAERCDRISLMHAGKVLASGTPQEL 494
Cdd:PRK13633 180 RREVVNTIKELNKKYGITIILITHYMEEAVEADRIIVMDSGKVVMEGTPKEI 231
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
269-497 |
1.41e-31 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 124.38 E-value: 1.41e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 269 QPENAEIAIEARDLTMRFGSFVAVDHVNFRIPRGEIFGFLGSNGCGKSTTMKML---TGLLPAS--EGEAWLFGQPVDPK 343
Cdd:COG1117 4 PASTLEPKIEVRNLNVYYGDKQALKDINLDIPENKVTALIGPSGCGKSTLLRCLnrmNDLIPGArvEGEILLDGEDIYDP 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 344 DIDT---RRRVGYMSQ-----AFSLYNeltvrqNLELHARLFHI-PEAEIPARVaEMSerfkL------NDVEDILPES- 407
Cdd:COG1117 84 DVDVvelRRRVGMVFQkpnpfPKSIYD------NVAYGLRLHGIkSKSELDEIV-EES----LrkaalwDEVKDRLKKSa 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 408 --LPLGIRQRLSLAVAVIHRPEMLILDEPTSGVDPVARDMFWQLMVDLSrqDKVTIFISTHFMNEAERC-DRISLMHAGK 484
Cdd:COG1117 153 lgLSGGQQQRLCIARALAVEPEVLLMDEPTSALDPISTAKIEELILELK--KDYTIVIVTHNMQQAARVsDYTAFFYLGE 230
|
250
....*....|...
gi 732682709 485 VLASGTPQELVEK 497
Cdd:COG1117 231 LVEFGPTEQIFTN 243
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
10-248 |
1.44e-31 |
|
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: 124.04 E-value: 1.44e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 10 PPVAQLAGVSQHYGKTVALNNITLDIPARCMVGLIGPDGVGKSSLLSLISG-ARVIEQGNVMVLGgdmrdpkHRR----- 83
Cdd:COG1119 1 DPLLELRNVTVRRGGKTILDDISWTVKPGEHWAILGPNGAGKSTLLSLITGdLPPTYGNDVRLFG-------ERRggedv 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 84 -DVCPRIAWMPQGLGKNLYHTLSVYENV--DFFA--RLFGHDKAEREVRINELLTSTGLAPFRDRPAGKLSGGMKQKLGL 158
Cdd:COG1119 74 wELRKRIGLVSPALQLRFPRDETVLDVVlsGFFDsiGLYREPTDEQRERARELLELLGLAHLADRPFGTLSQGEQRRVLI 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 159 CCALIHDPELLILDEPTTGVDPLSRSQFWDLIDSIRQRQSNMSVLVaTAYMEEA-ERFDWLVAMNAGEVLATGSAEELRq 237
Cdd:COG1119 154 ARALVKDPELLILDEPTAGLDLGARELLLALLDKLAAEGAPTLVLV-THHVEEIpPGITHVLLLKDGRVVAAGPKEEVL- 231
|
250
....*....|.
gi 732682709 238 qtQSATLEEAF 248
Cdd:COG1119 232 --TSENLSEAF 240
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
276-497 |
1.65e-31 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 123.65 E-value: 1.65e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 276 AIEARDLTMRF----------------------GSFVAVDHVNFRIPRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGE- 332
Cdd:COG1134 4 MIEVENVSKSYrlyhepsrslkelllrrrrtrrEEFWALKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTSGRv 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 333 ------AWLFGqpvdpkdidtrrrvgyMSQAFSlyNELTVRQNLELHARLFHIPEAEIPAR---VAEMSErfkLNDVEDi 403
Cdd:COG1134 84 evngrvSALLE----------------LGAGFH--PELTGRENIYLNGRLLGLSRKEIDEKfdeIVEFAE---LGDFID- 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 404 lpesLPL-----GIRQRLSLAVAVIHRPEMLILDEPTSGVDPVARDMFWQLMVDLSRQDKvTIFISTHFMNEAER-CDRI 477
Cdd:COG1134 142 ----QPVktyssGMRARLAFAVATAVDPDILLVDEVLAVGDAAFQKKCLARIRELRESGR-TVIFVSHSMGAVRRlCDRA 216
|
250 260
....*....|....*....|
gi 732682709 478 SLMHAGKVLASGTPQELVEK 497
Cdd:COG1134 217 IWLEKGRLVMDGDPEEVIAA 236
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
14-498 |
3.57e-31 |
|
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose isomerase and xylulokinase enzymes for xylose utilization. Members of this protein family are the ATP-binding cassette (ABC) subunit of the known or predicted high-affinity xylose ABC transporter for xylose import. These genes, which closely resemble other sugar transport ABC transporter genes, typically are encoded near xylose utilization enzymes and regulatory proteins. Note that this form of the transporter contains two copies of the ABC transporter domain (pfam00005). [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 131681 [Multi-domain] Cd Length: 500 Bit Score: 128.79 E-value: 3.57e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 14 QLAGVSQHYGKTVALNNITLDIPARCMVGLIGPDGVGKSSLLSLISGARV--IEQGNVMVLGGDMRDPKHRRDVCPRIAW 91
Cdd:TIGR02633 3 EMKGIVKTFGGVKALDGIDLEVRPGECVGLCGENGAGKSTLMKILSGVYPhgTWDGEIYWSGSPLKASNIRDTERAGIVI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 92 MPQGLgkNLYHTLSVYENVdFFARLFGH-----DKAEREVRINELLTSTGLAPFRD-RPAGKLSGGMKQKLGLCCALIHD 165
Cdd:TIGR02633 83 IHQEL--TLVPELSVAENI-FLGNEITLpggrmAYNAMYLRAKNLLRELQLDADNVtRPVGDYGGGQQQLVEIAKALNKQ 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 166 PELLILDEPTTGvdpLSRSQFWDLIDSIRQ-RQSNMSVLVATAYMEEAERF-DWLVAMNAGEVLATGSAEELRqqtqsat 243
Cdd:TIGR02633 160 ARLLILDEPSSS---LTEKETEILLDIIRDlKAHGVACVYISHKLNEVKAVcDTICVIRDGQHVATKDMSTMS------- 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 244 lEEAFInllpqAQRQAHQAVVIPPYQP-ENAEIAIEARDLTMRF---GSFVAVDHVNFRIPRGEIFGFLGSNGCGKSTTM 319
Cdd:TIGR02633 230 -EDDII-----TMMVGREITSLYPHEPhEIGDVILEARNLTCWDvinPHRKRVDDVSFSLRRGEILGVAGLVGAGRTELV 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 320 KMLTGLLP-ASEGEAWLFGQPVD---------------PKDidtRRRVGYMSQafslyneLTVRQNLEL-----HARLFH 378
Cdd:TIGR02633 304 QALFGAYPgKFEGNVFINGKPVDirnpaqairagiamvPED---RKRHGIVPI-------LGVGKNITLsvlksFCFKMR 373
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 379 IPEAEIPARVAEMSERFKLNDVEDILP-ESLPLGIRQRLSLAVAVIHRPEMLILDEPTSGVDPVARDMFWQLMVDLSRQD 457
Cdd:TIGR02633 374 IDAAAELQIIGSAIQRLKVKTASPFLPiGRLSGGNQQKAVLAKMLLTNPRVLILDEPTRGVDVGAKYEIYKLINQLAQEG 453
|
490 500 510 520
....*....|....*....|....*....|....*....|.
gi 732682709 458 KVTIFISTHFMNEAERCDRISLMHAGKVLASGTPQELVEKR 498
Cdd:TIGR02633 454 VAIIVVSSELAEVLGLSDRVLVIGEGKLKGDFVNHALTQEQ 494
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
14-236 |
3.80e-31 |
|
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid transport and metabolism];
Pssm-ID: 440179 [Multi-domain] Cd Length: 236 Bit Score: 122.40 E-value: 3.80e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 14 QLAGVSQHYGKTVALNNITLDIPARCMVGLIGPDGVGKSSLLSLISGARVIEQGNVMVLGGDM-RDPKHRRdvcPR--IA 90
Cdd:COG0410 5 EVENLHAGYGGIHVLHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRSGSIRFDGEDItGLPPHRI---ARlgIG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 91 WMPQGlgKNLYHTLSVYENVDFFARLFGHDKAEREV--RINELLTStgLAPFRDRPAGKLSGGMKQKLGLCCALIHDPEL 168
Cdd:COG0410 82 YVPEG--RRIFPSLTVEENLLLGAYARRDRAEVRADleRVYELFPR--LKERRRQRAGTLSGGEQQMLAIGRALMSRPKL 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 732682709 169 LILDEPTTGVDPLSRSQFWDLIDSIRQRqsNMSVLV----ATAYMEEAERFdwlVAMNAGEVLATGSAEELR 236
Cdd:COG0410 158 LLLDEPSLGLAPLIVEEIFEIIRRLNRE--GVTILLveqnARFALEIADRA---YVLERGRIVLEGTAAELL 224
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
291-499 |
4.19e-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: 132.44 E-value: 4.19e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 291 AVDHVNFRIPRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGEAWLFGQPVDPKDIDTRRRVGYMSQAFSLYNELTVRQNL 370
Cdd:TIGR01257 1954 AVDRLCVGVRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAGKSILTNISDVHQNMGYCPQFDAIDDLLTGREHL 2033
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 371 ELHARLFHIPEAEIpARVAEMS-ERFKLNDVEDILPESLPLGIRQRLSLAVAVIHRPEMLILDEPTSGVDPVARDMFWQL 449
Cdd:TIGR01257 2034 YLYARLRGVPAEEI-EKVANWSiQSLGLSLYADRLAGTYSGGNKRKLSTAIALIGCPPLVLLDEPTTGMDPQARRMLWNT 2112
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 732682709 450 MVDLSRQDKVTIfISTHFMNEAER-CDRISLMHAGKVLASGTPQELVEKRG 499
Cdd:TIGR01257 2113 IVSIIREGRAVV-LTSHSMEECEAlCTRLAIMVKGAFQCLGTIQHLKSKFG 2162
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
15-235 |
4.37e-31 |
|
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: 122.41 E-value: 4.37e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 15 LAGVSQHYGK-TVALNNITLDIPARCMVGLIGPDGVGKSSLLSLISgaRVIE--QGNVMVLGGDMR--DP-KHRRdvcpR 88
Cdd:cd03295 3 FENVTKRYGGgKKAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMIN--RLIEptSGEIFIDGEDIReqDPvELRR----K 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 89 IAWMPQGLGknLYHTLSVYENVDFFARLFGHDKAEREVRINELLTSTGLAP--FRDRPAGKLSGGMKQKLGLCCALIHDP 166
Cdd:cd03295 77 IGYVIQQIG--LFPHMTVEENIALVPKLLKWPKEKIRERADELLALVGLDPaeFADRYPHELSGGQQQRVGVARALAADP 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 167 ELLILDEPTTGVDPLSRSQFWDLIDSIrQRQSNMSVLVATAYMEEAERF-DWLVAMNAGEVLATGSAEEL 235
Cdd:cd03295 155 PLLLMDEPFGALDPITRDQLQEEFKRL-QQELGKTIVFVTHDIDEAFRLaDRIAIMKNGEIVQVGTPDEI 223
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
290-493 |
8.89e-31 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 122.85 E-value: 8.89e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 290 VAVDHVNFRIPRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGEAWLFGQPVDPKDI---DTRRRVGYMSQ--AFSLYNEl 364
Cdd:PRK13637 21 KALDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDGVDITDKKVklsDIRKKVGLVFQypEYQLFEE- 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 365 TVRQNLELHARLFHIPEAEIPARVAEMSERFKL--NDVEDILPESLPLGIRQRLSLAVAVIHRPEMLILDEPTSGVDPVA 442
Cdd:PRK13637 100 TIEKDIAFGPINLGLSEEEIENRVKRAMNIVGLdyEDYKDKSPFELSGGQKRRVAIAGVVAMEPKILILDEPTAGLDPKG 179
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 732682709 443 RDMFWQLMVDLSRQDKVTIFISTHFMNE-AERCDRISLMHAGKVLASGTPQE 493
Cdd:PRK13637 180 RDEILNKIKELHKEYNMTIILVSHSMEDvAKLADRIIVMNKGKCELQGTPRE 231
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
14-225 |
1.23e-30 |
|
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: 118.12 E-value: 1.23e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 14 QLAGVSQHYGKTVALNNITLDIPARCMVGLIGPDGVGKSSLLSLISGARVIEQGNVMVLGGDM--RDPKHRRDvcpRIAW 91
Cdd:cd00267 1 EIENLSFRYGGRTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGKDIakLPLEELRR---RIGY 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 92 MPQglgknlyhtlsvyenvdffarlfghdkaerevrinelltstglapfrdrpagkLSGGMKQKLGLCCALIHDPELLIL 171
Cdd:cd00267 78 VPQ-----------------------------------------------------LSGGQRQRVALARALLLNPDLLLL 104
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 732682709 172 DEPTTGVDPLSRSQFWDLIDSIRQRqsNMSVLVATAYMEEAERF-DWLVAMNAGE 225
Cdd:cd00267 105 DEPTSGLDPASRERLLELLRELAEE--GRTVIIVTHDPELAELAaDRVIVLKDGK 157
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
14-225 |
1.33e-30 |
|
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: 118.83 E-value: 1.33e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 14 QLAGVSQHYGKTVALNNITLDIPARCMVGLIGPDGVGKSSLLSLISGARVIEQGNVMVLG-----GDMRDPKHRRdvcpR 88
Cdd:cd03229 2 ELKNVSKRYGQKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGedltdLEDELPPLRR----R 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 89 IAWMPQGLgkNLYHTLSVYENVDFfarlfghdkaerevrinelltstglapfrdrpagKLSGGMKQKLGLCCALIHDPEL 168
Cdd:cd03229 78 IGMVFQDF--ALFPHLTVLENIAL----------------------------------GLSGGQQQRVALARALAMDPDV 121
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 732682709 169 LILDEPTTGVDPLSRSQFWDLIDSIRQrQSNMSVLVATAYMEEAERF-DWLVAMNAGE 225
Cdd:cd03229 122 LLLDEPTSALDPITRREVRALLKSLQA-QLGITVVLVTHDLDEAARLaDRVVVLRDGK 178
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
1-485 |
2.43e-30 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 126.32 E-value: 2.43e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 1 MTHLELVPvPPVAQLAGVSQHYGKTVALNNITLDIPARCMVGLIGPDGVGKSSLLSLISGARVIEQGNVMVLGgdmrdpK 80
Cdd:PRK15439 1 MQTSDTTA-PPLLCARSISKQYSGVEVLKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIGG------N 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 81 HRRDVCPRIAwmpQGLG-------KNLYHTLSVYENVDFfaRLFGHDKAERevRINELLTSTGLAPFRDRPAGKLSGGMK 153
Cdd:PRK15439 74 PCARLTPAKA---HQLGiylvpqePLLFPNLSVKENILF--GLPKRQASMQ--KMKQLLAALGCQLDLDSSAGSLEVADR 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 154 QKLGLCCALIHDPELLILDEPTTGVDPLSRSQFWDLIDSIRQRQSNMsVLVATAYMEEAERFDWLVAMNAGEVLATGSAE 233
Cdd:PRK15439 147 QIVEILRGLMRDSRILILDEPTASLTPAETERLFSRIRELLAQGVGI-VFISHKLPEIRQLADRISVMRDGTIALSGKTA 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 234 EL-----------RQQTQSATLEEAFINLLPQAQRQAHQAvvippyQPenaeiAIEARDLTMRfgSFVavdHVNFRIPRG 302
Cdd:PRK15439 226 DLstddiiqaitpAAREKSLSASQKLWLELPGNRRQQAAG------AP-----VLTVEDLTGE--GFR---NISLEVRAG 289
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 303 EIFGFLGSNGCGKSTTMKMLTGLLPASEGEAWLFGQPVDPKDIDTRRRVG--YMS---QAFSLYNELTVRQN---LELHA 374
Cdd:PRK15439 290 EILGLAGVVGAGRTELAETLYGLRPARGGRIMLNGKEINALSTAQRLARGlvYLPedrQSSGLYLDAPLAWNvcaLTHNR 369
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 375 RLFHIPeaeiPARVAEMSERF------KLNDVEDILpESLPLGIRQRLSLAVAVIHRPEMLILDEPTSGVDPVARDMFWQ 448
Cdd:PRK15439 370 RGFWIK----PARENAVLERYrralniKFNHAEQAA-RTLSGGNQQKVLIAKCLEASPQLLIVDEPTRGVDVSARNDIYQ 444
|
490 500 510
....*....|....*....|....*....|....*...
gi 732682709 449 LMVDLSRQDKVTIFISTHFmNEAER-CDRISLMHAGKV 485
Cdd:PRK15439 445 LIRSIAAQNVAVLFISSDL-EEIEQmADRVLVMHQGEI 481
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
17-235 |
2.50e-30 |
|
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the YhbG family are similar to members of the Mj1267_LivG family, which is involved in the transport of branched-chain amino acids. The genes yhbG and yhbN are located in a single operon and may function together in cell envelope during biogenesis. YhbG is the putative ATP-binding cassette component and YhbN is the putative periplasmic-binding protein. Depletion of each gene product leads to growth arrest, irreversible cell damage and loss of viability in E. coli. The YhbG homolog (NtrA) is essential in Rhizobium meliloti, a symbiotic nitrogen-fixing bacterium.
Pssm-ID: 213185 [Multi-domain] Cd Length: 232 Bit Score: 119.96 E-value: 2.50e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 17 GVSQHYGKTVALNNITLDIPARCMVGLIGPDGVGKSSLLSLISGARVIEQGNVMVLGGDM-RDPKHRRdvcPR--IAWMP 93
Cdd:cd03218 5 NLSKRYGKRKVVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDGQDItKLPMHKR---ARlgIGYLP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 94 QGlgKNLYHTLSVYENVDFFARLFGHDKAEREVRINELLTSTGLAPFRDRPAGKLSGGMKQKLGLCCALIHDPELLILDE 173
Cdd:cd03218 82 QE--ASIFRKLTVEENILAVLEIRGLSKKEREEKLEELLEEFHITHLRKSKASSLSGGERRRVEIARALATNPKFLLLDE 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 732682709 174 PTTGVDPLSRSQFWDLIDSIRQRqsNMSVL------------VATAYMeeaerfdwlvaMNAGEVLATGSAEEL 235
Cdd:cd03218 160 PFAGVDPIAVQDIQKIIKILKDR--GIGVLitdhnvretlsiTDRAYI-----------IYEGKVLAEGTPEEI 220
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
277-514 |
3.21e-30 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 120.09 E-value: 3.21e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 277 IEARDLTMRFGSFVAVDHVNFRIPRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGEAWLFGQPVD--PKDIDTRRRVGYM 354
Cdd:PRK11300 6 LSVSGLMMRFGGLLAVNNVNLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTILLRGQHIEglPGHQIARMGVVRT 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 355 SQAFSLYNELTVRQNL----------ELHARLFHIP-----EAEIPARVAEMSERFKLNDVEDILPESLPLGIRQRLSLA 419
Cdd:PRK11300 86 FQHVRLFREMTVIENLlvaqhqqlktGLFSGLLKTPafrraESEALDRAATWLERVGLLEHANRQAGNLAYGQQRRLEIA 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 420 VAVIHRPEMLILDEPTSGVDPVARDMFWQLMVDLSRQDKVTIFISTHFMNEA-ERCDRISLMHAGKVLASGTPQELvekr 498
Cdd:PRK11300 166 RCMVTQPEILMLDEPAAGLNPKETKELDELIAELRNEHNVTVLLIEHDMKLVmGISDRIYVVNQGTPLANGTPEEI---- 241
|
250
....*....|....*.
gi 732682709 499 gaASLEEAFIAYLQEA 514
Cdd:PRK11300 242 --RNNPDVIKAYLGEA 255
|
|
| galliderm_ABC |
TIGR03740 |
gallidermin-class lantibiotic protection ABC transporter, ATP-binding subunit; Model TIGR03731 ... |
14-213 |
3.60e-30 |
|
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: 119.04 E-value: 3.60e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 14 QLAGVSQHYGKTVALNNITLDIPARCMVGLIGPDGVGKSSLLSLISGARVIEQGNVMVLGGDMRDpKHRRDVCPRIAWMP 93
Cdd:TIGR03740 2 ETKNLSKRFGKQTAVNNISLTVPKNSVYGLLGPNGAGKSTLLKMITGILRPTSGEIIFDGHPWTR-KDLHKIGSLIESPP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 94 qglgknLYHTLSVYENVDFFARLFGHDKAerevRINELLTSTGLAPFRDRPAGKLSGGMKQKLGLCCALIHDPELLILDE 173
Cdd:TIGR03740 81 ------LYENLTARENLKVHTTLLGLPDS----RIDEVLNIVDLTNTGKKKAKQFSLGMKQRLGIAIALLNHPKLLILDE 150
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 732682709 174 PTTGVDPLSRSQFWDLIDSIRQRqsNMSVLVATAYMEEAE 213
Cdd:TIGR03740 151 PTNGLDPIGIQELRELIRSFPEQ--GITVILSSHILSEVQ 188
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
277-514 |
1.53e-29 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 119.03 E-value: 1.53e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 277 IEARDLTMRF-GSFVAVDHVNFRIPRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGEAWLFGQPV--DPKD-IDTRRRVG 352
Cdd:PRK13639 2 LETRDLKYSYpDGTEALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIKGEPIkyDKKSlLEVRKTVG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 353 YM-----SQAFSLynelTVRQNLELHARLFHIPEAEIPARVAEMSERFKLNDVEDILPESLPLGIRQRLSLAVAVIHRPE 427
Cdd:PRK13639 82 IVfqnpdDQLFAP----TVEEDVAFGPLNLGLSKEEVEKRVKEALKAVGMEGFENKPPHHLSGGQKKRVAIAGILAMKPE 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 428 MLILDEPTSGVDPVARDMFWQLMVDLSRQDkVTIFISTHFMNEAER-CDRISLMHAGKVLASGTPQEL---VEKRGAASL 503
Cdd:PRK13639 158 IIVLDEPTSGLDPMGASQIMKLLYDLNKEG-ITIIISTHDVDLVPVyADKVYVMSDGKIIKEGTPKEVfsdIETIRKANL 236
|
250
....*....|.
gi 732682709 504 EEAFIAYLQEA 514
Cdd:PRK13639 237 RLPRVAHLIEI 247
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
291-499 |
2.72e-29 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 124.12 E-value: 2.72e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 291 AVDHVNFRIPRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGEAWLFGQPVdpKDIDT---RRRVGYMSQAFSLYNElTVR 367
Cdd:COG1132 355 VLKDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYDPTSGRILIDGVDI--RDLTLeslRRQIGVVPQDTFLFSG-TIR 431
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 368 QNLELhARLfHIPEAEIpARVAEMSErfklndVEDILpESLPLGI---------------RQRLSLAVAVIHRPEMLILD 432
Cdd:COG1132 432 ENIRY-GRP-DATDEEV-EEAAKAAQ------AHEFI-EALPDGYdtvvgergvnlsggqRQRIAIARALLKDPPILILD 501
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 732682709 433 EPTSGVDPVA----RDMFWQLMvdlsrQDKVTIFIStHFMNEAERCDRISLMHAGKVLASGTPQELVEKRG 499
Cdd:COG1132 502 EATSALDTETealiQEALERLM-----KGRTTIVIA-HRLSTIRNADRILVLDDGRIVEQGTHEELLARGG 566
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
14-235 |
2.82e-29 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 120.18 E-value: 2.82e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 14 QLAGVSQHYGKTVALNNITLDIPARCMVGLIGPDGVGKSSLLSLISGARVIEQGNVMVLGGDM--RDPKHRRdvcprIAW 91
Cdd:COG3839 5 ELENVSKSYGGVEALKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAGLEDPTSGEILIGGRDVtdLPPKDRN-----IAM 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 92 MPQGLGknLYHTLSVYENVDFFARLFGHDKAEREVRINELLTSTGLAPFRDRPAGKLSGGMKQKLGLCCALIHDPELLIL 171
Cdd:COG3839 80 VFQSYA--LYPHMTVYENIAFPLKLRKVPKAEIDRRVREAAELLGLEDLLDRKPKQLSGGQRQRVALGRALVREPKVFLL 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 732682709 172 DEPTTGVDPLSRsqfWDLIDSIR--QRQSNMSVLVATAYMEEAERF-DWLVAMNAGEVLATGSAEEL 235
Cdd:COG3839 158 DEPLSNLDAKLR---VEMRAEIKrlHRRLGTTTIYVTHDQVEAMTLaDRIAVMNDGRIQQVGTPEEL 221
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
291-491 |
3.02e-29 |
|
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: 126.67 E-value: 3.02e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 291 AVDHVNFRIPRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGEAWLFGQPVDPKDIDTRRRVGYMSQAFSLYNELTVRQNL 370
Cdd:TIGR01257 945 AVDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGKDIETNLDAVRQSLGMCPQHNILFHHLTVAEHI 1024
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 371 ELHARLFHIPEAEIPARVAEMSERFKLNDVEDILPESLPLGIRQRLSLAVAVIHRPEMLILDEPTSGVDPVARDMFWQLM 450
Cdd:TIGR01257 1025 LFYAQLKGRSWEEAQLEMEAMLEDTGLHHKRNEEAQDLSGGMQRKLSVAIAFVGDAKVVVLDEPTSGVDPYSRRSIWDLL 1104
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 732682709 451 vdLSRQDKVTIFISTHFMNEAERC-DRISLMHAGKVLASGTP 491
Cdd:TIGR01257 1105 --LKYRSGRTIIMSTHHMDEADLLgDRIAIISQGRLYCSGTP 1144
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
302-489 |
3.35e-29 |
|
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type transporter and the ATPase component of a molybdate transport system that also includes the periplasmic binding protein ModA and the membrane protein ModB. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213264 [Multi-domain] Cd Length: 214 Bit Score: 115.86 E-value: 3.35e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 302 GEIFGFLGSNGCGKSTTMKMLTGLLPASEGEAWLFGQPVDP--KDID---TRRRVGYMSQAFSLYNELTVRQNLELHARl 376
Cdd:cd03297 23 EEVTGIFGASGAGKSTLLRCIAGLEKPDGGTIVLNGTVLFDsrKKINlppQQRKIGLVFQQYALFPHLNVRENLAFGLK- 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 377 FHIPeAEIPARVAEMSERFKLNDVEDILPESLPLGIRQRLSLAVAVIHRPEMLILDEPTSGVDPVARDMFWQLMVDLSRQ 456
Cdd:cd03297 102 RKRN-REDRISVDELLDLLGLDHLLNRYPAQLSGGEKQRVALARALAAQPELLLLDEPFSALDRALRLQLLPELKQIKKN 180
|
170 180 190
....*....|....*....|....*....|....
gi 732682709 457 DKVTIFISTHFMNEAER-CDRISLMHAGKVLASG 489
Cdd:cd03297 181 LNIPVIFVTHDLSEAEYlADRIVVMEDGRLQYIG 214
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
10-240 |
4.68e-29 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 117.06 E-value: 4.68e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 10 PPVAQLAGVSQHYGKTVALNNITLDIPARCMVGLIGPDGVGKSSLLS-------LISGARVieQGNVMVLGGDMRDPK-- 80
Cdd:COG1117 9 EPKIEVRNLNVYYGDKQALKDINLDIPENKVTALIGPSGCGKSTLLRclnrmndLIPGARV--EGEILLDGEDIYDPDvd 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 81 ---HRRdvcpRIAWMPQglgK-NLYhTLSVYENVDFFARLFG-HDKAEREVRINELLTSTGLAP-FRDR---PAGKLSGG 151
Cdd:COG1117 87 vveLRR----RVGMVFQ---KpNPF-PKSIYDNVAYGLRLHGiKSKSELDEIVEESLRKAALWDeVKDRlkkSALGLSGG 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 152 MKQKLglcC---ALIHDPELLILDEPTTGVDPLSRSQFWDLIDSIRQrqsNMSVLVATAYMEEAERF-DWLVAMNAGEVL 227
Cdd:COG1117 159 QQQRL---CiarALAVEPEVLLMDEPTSALDPISTAKIEELILELKK---DYTIVIVTHNMQQAARVsDYTAFFYLGELV 232
|
250
....*....|....*...
gi 732682709 228 ATGSAEEL-----RQQTQ 240
Cdd:COG1117 233 EFGPTEQIftnpkDKRTE 250
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
15-241 |
7.81e-29 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 118.67 E-value: 7.81e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 15 LAGVSQHYGKTVALNNITLDIPARCMVGLIGPDGVGKSSLLSLISGARVIEQGNVMVLGGDMRDPK-HRRDVCprIAWMP 93
Cdd:PRK11432 9 LKNITKRFGSNTVIDNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIFIDGEDVTHRSiQQRDIC--MVFQS 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 94 QGLgknlYHTLSVYENVDFFARLFGHDKAEREVRINELLTSTGLAPFRDRPAGKLSGGMKQKLGLCCALIHDPELLILDE 173
Cdd:PRK11432 87 YAL----FPHMSLGENVGYGLKMLGVPKEERKQRVKEALELVDLAGFEDRYVDQISGGQQQRVALARALILKPKVLLFDE 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 732682709 174 PTTGVDP-LSRSqfwdLIDSIR--QRQSNMSVLVATayMEEAERF---DWLVAMNAGEVLATGSAEELRQQTQS 241
Cdd:PRK11432 163 PLSNLDAnLRRS----MREKIRelQQQFNITSLYVT--HDQSEAFavsDTVIVMNKGKIMQIGSPQELYRQPAS 230
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
277-498 |
7.96e-29 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 116.87 E-value: 7.96e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 277 IEARDLTMRFGSFV-AVDHVNFRIPRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGEAWLFGQPVDPKD---IDTRRRVG 352
Cdd:PRK13636 6 LKVEELNYNYSDGThALKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGKPIDYSRkglMKLRESVG 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 353 YMSQafSLYNEL---TVRQNLELHARLFHIPEAEIPARVAEMSERFKLNDVEDILPESLPLGIRQRLSLAVAVIHRPEML 429
Cdd:PRK13636 86 MVFQ--DPDNQLfsaSVYQDVSFGAVNLKLPEDEVRKRVDNALKRTGIEHLKDKPTHCLSFGQKKRVAIAGVLVMEPKVL 163
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 430 ILDEPTSGVDPVARDMFWQLMVDLSRQDKVTIFISTHFMNE-AERCDRISLMHAGKVLASGTPQELVEKR 498
Cdd:PRK13636 164 VLDEPTAGLDPMGVSEIMKLLVEMQKELGLTIIIATHDIDIvPLYCDNVFVMKEGRVILQGNPKEVFAEK 233
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
277-511 |
9.75e-29 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 115.24 E-value: 9.75e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 277 IEARDLTMRFGSFVAvdHVNFRIPRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGEAWLFGQPVDPKDIDtRRRVGYMSQ 356
Cdd:COG3840 2 LRLDDLTYRYGDFPL--RFDLTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILWNGQDLTALPPA-ERPVSMLFQ 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 357 AFSLYNELTVRQN--LELHARLfHIPEAEIpARVAEMSERFKLNDVEDILPESLPLGIRQRLSLAVAVI-HRPeMLILDE 433
Cdd:COG3840 79 ENNLFPHLTVAQNigLGLRPGL-KLTAEQR-AQVEQALERVGLAGLLDRLPGQLSGGQRQRVALARCLVrKRP-ILLLDE 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 732682709 434 PTSGVDPVARDMFWQLMVDLSRQDKVTIFISTHFMNEAER-CDRISLMHAGKVLASGTPQELVEKRGAasleEAFIAYL 511
Cdd:COG3840 156 PFSALDPALRQEMLDLVDELCRERGLTVLMVTHDPEDAARiADRVLLVADGRIAADGPTAALLDGEPP----PALAAYL 230
|
|
| potA |
TIGR01187 |
spermidine/putrescine ABC transporter ATP-binding subunit; This model describes spermidine ... |
308-496 |
1.41e-28 |
|
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: 117.59 E-value: 1.41e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 308 LGSNGCGKSTTMKMLTGLLPASEGEAWLFGQPVD--PKDidtRRRVGYMSQAFSLYNELTVRQNLELHARLFHIPEAEIP 385
Cdd:TIGR01187 2 LGPSGCGKTTLLRLLAGFEQPDSGSIMLDGEDVTnvPPH---LRHINMVFQSYALFPHMTVEENVAFGLKMRKVPRAEIK 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 386 ARVAEMSERFKLNDVEDILPESLPLGIRQRLSLAVAVIHRPEMLILDEPTSGVDPVARDMFWQLMVDLSRQDKVTIFIST 465
Cdd:TIGR01187 79 PRVLEALRLVQLEEFADRKPHQLSGGQQQRVALARALVFKPKILLLDEPLSALDKKLRDQMQLELKTIQEQLGITFVFVT 158
|
170 180 190
....*....|....*....|....*....|..
gi 732682709 466 HFMNEA-ERCDRISLMHAGKVLASGTPQELVE 496
Cdd:TIGR01187 159 HDQEEAmTMSDRIAIMRKGKIAQIGTPEEIYE 190
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
277-496 |
1.43e-28 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 118.51 E-value: 1.43e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 277 IEARDLTMRFGSFVAVDHVNFRIPRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGEAWLFGQPVD--PKDidtRRRVGYM 354
Cdd:PRK09452 15 VELRGISKSFDGKEVISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLDGQDIThvPAE---NRHVNTV 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 355 SQAFSLYNELTVRQNLELHARLFHIPEAEIPARVAEMSERFKLNDVEDILPESLPLGIRQRLSLAVAVIHRPEMLILDEP 434
Cdd:PRK09452 92 FQSYALFPHMTVFENVAFGLRMQKTPAAEITPRVMEALRMVQLEEFAQRKPHQLSGGQQQRVAIARAVVNKPKVLLLDES 171
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 732682709 435 TSGVDPVARDMFWQLMVDLSRQDKVT-IFIsTHFMNEA-ERCDRISLMHAGKVLASGTPQELVE 496
Cdd:PRK09452 172 LSALDYKLRKQMQNELKALQRKLGITfVFV-THDQEEAlTMSDRIVVMRDGRIEQDGTPREIYE 234
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
10-238 |
2.04e-28 |
|
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease components [Energy production and conversion, Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 444012 [Multi-domain] Cd Length: 563 Bit Score: 121.02 E-value: 2.04e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 10 PPVAQLAGVS-QHYGKTVALNNITLDIPARCMVGLIGPDGVGKSSLLSLISGARVIEQGNVMVLGGDMR--DPKHRRDvc 86
Cdd:COG4988 334 PPSIELEDVSfSYPGGRPALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPPYSGSILINGVDLSdlDPASWRR-- 411
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 87 pRIAWMPQglgkN--LYHTlSVYENVdffarLFGHDKAEREvRINELLTSTGLAPF-RDRPAG----------KLSGGMK 153
Cdd:COG4988 412 -QIAWVPQ----NpyLFAG-TIRENL-----RLGRPDASDE-ELEAALEAAGLDEFvAALPDGldtplgeggrGLSGGQA 479
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 154 QKLGLCCALIHDPELLILDEPTTGVDPLSRSQFWDLIDSIRQRQsnmSVLVATAYMEEAERFDWLVAMNAGEVLATGSAE 233
Cdd:COG4988 480 QRLALARALLRDAPLLLLDEPTAHLDAETEAEILQALRRLAKGR---TVILITHRLALLAQADRILVLDDGRIVEQGTHE 556
|
....*
gi 732682709 234 ELRQQ 238
Cdd:COG4988 557 ELLAK 561
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
15-235 |
2.25e-28 |
|
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and the ATPase component of the spermidine/putrescine-preferential uptake system consisting of PotA, -B, -C, and -D. PotA has two domains with the N-terminal domain containing the ATPase activity and the residues required for homodimerization with PotA and heterdimerization with PotB. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213267 [Multi-domain] Cd Length: 232 Bit Score: 114.26 E-value: 2.25e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 15 LAGVSQHYGKTVALNNITLDIPARCMVGLIGPDGVGKSSLLSLISGARVIEQGNVMVLGGDMRD-PKHRRdvcpRIAWMP 93
Cdd:cd03300 3 LENVSKFYGGFVALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGKDITNlPPHKR----PVNTVF 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 94 QGLGknLYHTLSVYENVDFFARLFGHDKAEREVRINELLTSTGLAPFRDRPAGKLSGGMKQKLGLCCALIHDPELLILDE 173
Cdd:cd03300 79 QNYA--LFPHLTVFENIAFGLRLKKLPKAEIKERVAEALDLVQLEGYANRKPSQLSGGQQQRVAIARALVNEPKVLLLDE 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 732682709 174 PTTGVDPLSRSQFWDLIDSIrQRQSNMSVLVATAYMEEAERF-DWLVAMNAGEVLATGSAEEL 235
Cdd:cd03300 157 PLGALDLKLRKDMQLELKRL-QKELGITFVFVTHDQEEALTMsDRIAVMNKGKIQQIGTPEEI 218
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
277-466 |
2.45e-28 |
|
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where FtsE is the ATPase and the membrane subunit FtsX resembles a permease subunit. But rather than transporting any substrate, the complex acts in cell division by undergoing conformational changes that alter the activity of cell wall hydrolases located outside the plasma membrane. The complex is widely conserved in bacteria, but also extremely divergent in sequence between different lineages
Pssm-ID: 213259 [Multi-domain] Cd Length: 214 Bit Score: 113.66 E-value: 2.45e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 277 IEARDLTMRF-GSFVAVDHVNFRIPRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGEAWLFGQPV-DPKDIDT---RRRV 351
Cdd:cd03292 1 IEFINVTKTYpNGTAALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQDVsDLRGRAIpylRRKI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 352 GYMSQAFSLYNELTVRQNLELHARLFHIPEAEIPARVAEMSERFKLNDVEDILPESLPLGIRQRLSLAVAVIHRPEMLIL 431
Cdd:cd03292 81 GVVFQDFRLLPDRNVYENVAFALEVTGVPPREIRKRVPAALELVGLSHKHRALPAELSGGEQQRVAIARAIVNSPTILIA 160
|
170 180 190
....*....|....*....|....*....|....*..
gi 732682709 432 DEPTSGVDPvarDMFWQLMVDLSRQDK--VTIFISTH 466
Cdd:cd03292 161 DEPTGNLDP---DTTWEIMNLLKKINKagTTVVVATH 194
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
21-230 |
2.83e-28 |
|
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter subfamily specific for the transport of dipeptides, oligopeptides (OppD), and nickel (NikDE). The NikABCDE system of E. coli belongs to this family and is composed of the periplasmic binding protein NikA, two integral membrane components (NikB and NikC), and two ATPase (NikD and NikE). The NikABCDE transporter is synthesized under anaerobic conditions to meet the increased demand for nickel resulting from hydrogenase synthesis. The molecular mechanism of nickel uptake in many bacteria and most archaea is not known. Many other members of this ABC family are also involved in the uptake of dipeptides and oligopeptides. The oligopeptide transport system (Opp) is a five-component ABC transport composed of a membrane-anchored substrate binding proteins (SRP), OppA, two transmembrane proteins, OppB and OppC, and two ATP-binding domains, OppD and OppF.
Pssm-ID: 213224 [Multi-domain] Cd Length: 228 Bit Score: 113.75 E-value: 2.83e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 21 HYGKTVALNNITLDIPARCMVGLIGPDGVGKSSLLSLISGARVIEQGNVMVLGGDM--RDPKHRRDVCPRIAWMPQGLGK 98
Cdd:cd03257 14 GGGSVKALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGKDLlkLSRRLRKIRRKEIQMVFQDPMS 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 99 NLYHTLSVYENVD--FFARLFGHDKAEREVRINELLTSTGLAP-FRDRPAGKLSGGMKQKLGLCCALIHDPELLILDEPT 175
Cdd:cd03257 94 SLNPRMTIGEQIAepLRIHGKLSKKEARKEAVLLLLVGVGLPEeVLNRYPHELSGGQRQRVAIARALALNPKLLIADEPT 173
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 732682709 176 TGVDPLSRSQFWDLIDSIrQRQSNMSVLVAT------AYMeeAERfdwLVAMNAGEVLATG 230
Cdd:cd03257 174 SALDVSVQAQILDLLKKL-QEELGLTLLFIThdlgvvAKI--ADR---VAVMYAGKIVEEG 228
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
14-256 |
3.15e-28 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 116.72 E-value: 3.15e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 14 QLAGVSQHY----GKTVALNNITLDIPARCMVGLIGPDGVGKSSLLSLISGarvIEQ---GNVMVLGGDM--RDPKHRRD 84
Cdd:COG1135 3 ELENLSKTFptkgGPVTALDDVSLTIEKGEIFGIIGYSGAGKSTLIRCINL---LERptsGSVLVDGVDLtaLSERELRA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 85 VCPRIAWMPQGLgkNLYHTLSVYENVDFFARLFGHDKAEREVRINELLTSTGLAPFRDR-PAgKLSGGMKQKLGLCCALI 163
Cdd:COG1135 80 ARRKIGMIFQHF--NLLSSRTVAENVALPLEIAGVPKAEIRKRVAELLELVGLSDKADAyPS-QLSGGQKQRVGIARALA 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 164 HDPELLILDEPTTGVDPLSRSQFWDLIDSIRQRQsNMSVLVATAYMEE----AERfdwlVA-MNAGEVLATGSAEELRQQ 238
Cdd:COG1135 157 NNPKVLLCDEATSALDPETTRSILDLLKDINREL-GLTIVLITHEMDVvrriCDR----VAvLENGRIVEQGPVLDVFAN 231
|
250
....*....|....*...
gi 732682709 239 TQSATLEEaFINLLPQAQ 256
Cdd:COG1135 232 PQSELTRR-FLPTVLNDE 248
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
277-494 |
4.34e-28 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 114.90 E-value: 4.34e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 277 IEARDLTMRF-GSFVAVDHVNFRIPRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGEAWLFGQPVDPKDI-DTRRRVGYM 354
Cdd:PRK13652 4 IETRDLCYSYsGSKEALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIRGEPITKENIrEVRKFVGLV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 355 -----SQAFSLynelTVRQNLELHARLFHIPEAEIPARVAEMSERFKLNDVEDILPESLPLGIRQRLSLAVAVIHRPEML 429
Cdd:PRK13652 84 fqnpdDQIFSP----TVEQDIAFGPINLGLDEETVAHRVSSALHMLGLEELRDRVPHHLSGGEKKRVAIAGVIAMEPQVL 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 732682709 430 ILDEPTSGVDPVARDMFWQLMVDLSRQDKVTIFISTHFMN-EAERCDRISLMHAGKVLASGTPQEL 494
Cdd:PRK13652 160 VLDEPTAGLDPQGVKELIDFLNDLPETYGMTVIFSTHQLDlVPEMADYIYVMDKGRIVAYGTVEEI 225
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
275-493 |
6.63e-28 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 113.71 E-value: 6.63e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 275 IAIEARDLTMRFGSFVAVDHVNFRIPRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGEAWLFGQPVD---PKDIDTRRRV 351
Cdd:PRK13548 1 AMLEARNLSVRLGGRTLLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLNGRPLAdwsPAELARRRAV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 352 gyMSQAFSLYNELTVRQNLELHARLFHIPEAEIPARVAEMSERFKLNDVEDILPESLPLGIRQRLSLA-V-----AVIHR 425
Cdd:PRK13548 81 --LPQHSSLSFPFTVEEVVAMGRAPHGLSRAEDDALVAAALAQVDLAHLAGRDYPQLSGGEQQRVQLArVlaqlwEPDGP 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 732682709 426 PEMLILDEPTSgvdpvARDMFWQLMV-----DLSRQDKVTIFISTHFMNEAER-CDRISLMHAGKVLASGTPQE 493
Cdd:PRK13548 159 PRWLLLDEPTS-----ALDLAHQHHVlrlarQLAHERGLAVIVVLHDLNLAARyADRIVLLHQGRLVADGTPAE 227
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
277-490 |
7.50e-28 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 115.67 E-value: 7.50e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 277 IEARDLTMRF----GSFVAVDHVNFRIPRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGEAWLFGQPV---DPKD-IDTR 348
Cdd:PRK11153 2 IELKNISKVFpqggRTIHALNNVSLHIPAGEIFGVIGASGAGKSTLIRCINLLERPTSGRVLVDGQDLtalSEKElRKAR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 349 RRVGYMSQAFSLYNELTVRQNLELHARLFHIPEAEIPARVAEMSERFKLNDVEDILPESLPLGIRQRLSLAVAVIHRPEM 428
Cdd:PRK11153 82 RQIGMIFQHFNLLSSRTVFDNVALPLELAGTPKAEIKARVTELLELVGLSDKADRYPAQLSGGQKQRVAIARALASNPKV 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 732682709 429 LILDEPTSGVDPVARDMFWQLMVDLSRQDKVTIFISTHFMNEAER-CDRISLMHAGKVLASGT 490
Cdd:PRK11153 162 LLCDEATSALDPATTRSILELLKDINRELGLTIVLITHEMDVVKRiCDRVAVIDAGRLVEQGT 224
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
277-494 |
1.06e-27 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 115.59 E-value: 1.06e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 277 IEARDLTMRFGSFVAVDHVNFRIPRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGEAWLFGQPVDPKDIDtRRRVGYMSQ 356
Cdd:PRK11432 7 VVLKNITKRFGSNTVIDNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIFIDGEDVTHRSIQ-QRDICMVFQ 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 357 AFSLYNELTVRQNLELHARLFHIPEAEIPARVAEMSERFKLNDVEDILPESLPLGIRQRLSLAVAVIHRPEMLILDEPTS 436
Cdd:PRK11432 86 SYALFPHMSLGENVGYGLKMLGVPKEERKQRVKEALELVDLAGFEDRYVDQISGGQQQRVALARALILKPKVLLFDEPLS 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 732682709 437 GVDPVARDMFWQLMVDLSRQDKVTIFISTHFMNEA-ERCDRISLMHAGKVLASGTPQEL 494
Cdd:PRK11432 166 NLDANLRRSMREKIRELQQQFNITSLYVTHDQSEAfAVSDTVIVMNKGKIMQIGSPQEL 224
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
274-496 |
1.07e-27 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 113.01 E-value: 1.07e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 274 EIAIEARDLTMRFGSFVAVDHVNFRIPRGEIFGFLGSNGCGKSTTMKMLTGLLPAS-----EGEAWLFGQPVDPKDID-- 346
Cdd:PRK14267 2 KFAIETVNLRVYYGSNHVIKGVDLKIPQNGVFALMGPSGCGKSTLLRTFNRLLELNeearvEGEVRLFGRNIYSPDVDpi 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 347 -TRRRVGYMSQAFSLYNELTVRQNLELHARLFHI--PEAEIPARVAEMSERFKL-NDVEDIL---PESLPLGIRQRLSLA 419
Cdd:PRK14267 82 eVRREVGMVFQYPNPFPHLTIYDNVAIGVKLNGLvkSKKELDERVEWALKKAALwDEVKDRLndyPSNLSGGQRQRLVIA 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 732682709 420 VAVIHRPEMLILDEPTSGVDPVARDMFWQLMVDLsrQDKVTIFISTHFMNEAER-CDRISLMHAGKVLASGTPQELVE 496
Cdd:PRK14267 162 RALAMKPKILLMDEPTANIDPVGTAKIEELLFEL--KKEYTIVLVTHSPAQAARvSDYVAFLYLGKLIEVGPTRKVFE 237
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
14-242 |
1.47e-27 |
|
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: 112.05 E-value: 1.47e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 14 QLAGVSQHYGKTVALNNITLDIPARCMVGLIGPDGVGKSSLLSLISGARVIEQGNVMVLGGDM--RDPKHRrdvcpRIAW 91
Cdd:cd03296 4 EVRNVSKRFGDFVALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGGEDAtdVPVQER-----NVGF 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 92 MPQGLGknLYHTLSVYENVDFFARL----FGHDKAEREVRINELLTSTGLAPFRDRPAGKLSGGMKQKLGLCCALIHDPE 167
Cdd:cd03296 79 VFQHYA--LFRHMTVFDNVAFGLRVkprsERPPEAEIRAKVHELLKLVQLDWLADRYPAQLSGGQRQRVALARALAVEPK 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 732682709 168 LLILDEPTTGVDPLSRSQFWDLIDSIRQRQSNMSVLVATAYMEEAERFDWLVAMNAGEVLATGSAEELRQQTQSA 242
Cdd:cd03296 157 VLLLDEPFGALDAKVRKELRRWLRRLHDELHVTTVFVTHDQEEALEVADRVVVMNKGRIEQVGTPDEVYDHPASP 231
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
289-489 |
1.68e-27 |
|
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: 111.47 E-value: 1.68e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 289 FVAVDHVNFRIPRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGEAWLFGQPVDPKDIDTrrrvgymsqafSLYNELTVRQ 368
Cdd:cd03220 35 FWALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVTVRGRVSSLLGLGG-----------GFNPELTGRE 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 369 NLELHARLFHIPEAEIPARVAEMSERFKLNDVEDilpesLPL-----GIRQRLSLAVAVIHRPEMLILDEPTSGVDPVAR 443
Cdd:cd03220 104 NIYLNGRLLGLSRKEIDEKIDEIIEFSELGDFID-----LPVktyssGMKARLAFAIATALEPDILLIDEVLAVGDAAFQ 178
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 732682709 444 DMFWQLMVDLSRQDKvTIFISTHFMNEAER-CDRISLMHAGKVLASG 489
Cdd:cd03220 179 EKCQRRLRELLKQGK-TVILVSHDPSSIKRlCDRALVLEKGKIRFDG 224
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
29-494 |
1.91e-27 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 117.88 E-value: 1.91e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 29 NNITLDIPARCMVGLIGPDGVGKS----SLLSLI-SGARVIEQGNVMVLGGDM---RDPKHRRDVCPRIAWMPQ------ 94
Cdd:PRK15134 26 NDVSLQIEAGETLALVGESGSGKSvtalSILRLLpSPPVVYPSGDIRFHGESLlhaSEQTLRGVRGNKIAMIFQepmvsl 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 95 ----GLGKNLYHTLSVYenvdffaRLFGHDKAEREvrINELLTSTGL--APFR--DRPAgKLSGGMKQKLGLCCALIHDP 166
Cdd:PRK15134 106 nplhTLEKQLYEVLSLH-------RGMRREAARGE--ILNCLDRVGIrqAAKRltDYPH-QLSGGERQRVMIAMALLTRP 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 167 ELLILDEPTTGVDPLSRSQFWDLIDSIRQrQSNMSVLVATAYMEEAERF-DWLVAMNAGEVLATGSAEELRQQTQSAtLE 245
Cdd:PRK15134 176 ELLIADEPTTALDVSVQAQILQLLRELQQ-ELNMGLLFITHNLSIVRKLaDRVAVMQNGRCVEQNRAATLFSAPTHP-YT 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 246 EAFINLLPQAQRQAHQAVVIPPYQPENAEIAIEARDLTMR--FGSFVAVDHVNFRIPRGEIFGFLGSNGCGKSTTMKMLT 323
Cdd:PRK15134 254 QKLLNSEPSGDPVPLPEPASPLLDVEQLQVAFPIRKGILKrtVDHNVVVKNISFTLRPGETLGLVGESGSGKSTTGLALL 333
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 324 GLLpASEGEAWLFGQPVDPKD----IDTRRRVGYMSQ--AFSLYNELTVRQ----NLELHARlfHIPEAEIPARVAEMSE 393
Cdd:PRK15134 334 RLI-NSQGEIWFDGQPLHNLNrrqlLPVRHRIQVVFQdpNSSLNPRLNVLQiieeGLRVHQP--TLSAAQREQQVIAVME 410
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 394 RFKLN-DVEDILPESLPLGIRQRLSLAVAVIHRPEMLILDEPTSGVDPVARDMFWQLMVDLSRQDKVT-IFISTHFMNEA 471
Cdd:PRK15134 411 EVGLDpETRHRYPAEFSGGQRQRIAIARALILKPSLIILDEPTSSLDKTVQAQILALLKSLQQKHQLAyLFISHDLHVVR 490
|
490 500
....*....|....*....|...
gi 732682709 472 ERCDRISLMHAGKVLASGTPQEL 494
Cdd:PRK15134 491 ALCHQVIVLRQGEVVEQGDCERV 513
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
271-497 |
2.91e-27 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 112.15 E-value: 2.91e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 271 ENAEIAIEARDLTMRFGS--FVAVDHVNFRIPRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGEAWLFGQPVDPKDI-DT 347
Cdd:PRK13648 2 EDKNSIIVFKNVSFQYQSdaSFTLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIFYNNQAITDDNFeKL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 348 RRRVGYMSQ---------------AFSLYNELtvrqnlelharlfhIPEAEIPARVAEMSERFKLNDVEDILPESLPLGI 412
Cdd:PRK13648 82 RKHIGIVFQnpdnqfvgsivkydvAFGLENHA--------------VPYDEMHRRVSEALKQVDMLERADYEPNALSGGQ 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 413 RQRLSLAVAVIHRPEMLILDEPTSGVDPVARDMFWQLMVDLSRQDKVTIFISTHFMNEAERCDRISLMHAGKVLASGTPQ 492
Cdd:PRK13648 148 KQRVAIAGVLALNPSVIILDEATSMLDPDARQNLLDLVRKVKSEHNITIISITHDLSEAMEADHVIVMNKGTVYKEGTPT 227
|
....*
gi 732682709 493 ELVEK 497
Cdd:PRK13648 228 EIFDH 232
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
30-230 |
4.68e-27 |
|
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: 109.69 E-value: 4.68e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 30 NITLDIPARcMVGLIGPDGVGKSSLLSLISGARVIEQGNVMVLGGDMRD-------PKHRRdvcpRIAWMPQGLGknLYH 102
Cdd:cd03297 16 KIDFDLNEE-VTGIFGASGAGKSTLLRCIAGLEKPDGGTIVLNGTVLFDsrkkinlPPQQR----KIGLVFQQYA--LFP 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 103 TLSVYENVDFFARlfGHDKAEREVRINELLTSTGLAPFRDRPAGKLSGGMKQKLGLCCALIHDPELLILDEPTTGVDPLS 182
Cdd:cd03297 89 HLNVRENLAFGLK--RKRNREDRISVDELLDLLGLDHLLNRYPAQLSGGEKQRVALARALAAQPELLLLDEPFSALDRAL 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 732682709 183 RSQfwdLIDSIRQRQS--NMSVLVATAYMEEAERF-DWLVAMNAGEVLATG 230
Cdd:cd03297 167 RLQ---LLPELKQIKKnlNIPVIFVTHDLSEAEYLaDRIVVMEDGRLQYIG 214
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
15-242 |
6.69e-27 |
|
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: 110.28 E-value: 6.69e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 15 LAGVSQHYGK----TVALNNITLDIPARCMVGLIGPDGVGKSSLLSLISGARVIEQGNVMVLGGDMRdPKHRRDVCPRIA 90
Cdd:COG1124 4 VRNLSVSYGQggrrVPVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVTFDGRPVT-RRRRKAFRRRVQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 91 WMPQglgkNLYHTL----SVYENVDFFARLFGHDkaEREVRINELLTSTGLAP-FRDRPAGKLSGGMKQKLGLCCALIHD 165
Cdd:COG1124 83 MVFQ----DPYASLhprhTVDRILAEPLRIHGLP--DREERIAELLEQVGLPPsFLDRYPHQLSGGQRQRVAIARALILE 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 732682709 166 PELLILDEPTTGVDPLSRSQFWDLIDSIRqRQSNMSVLVATAYMEEAERF-DWLVAMNAGEVLATGSAEELRQQTQSA 242
Cdd:COG1124 157 PELLLLDEPTSALDVSVQAEILNLLKDLR-EERGLTYLFVSHDLAVVAHLcDRVAVMQNGRIVEELTVADLLAGPKHP 233
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
277-494 |
7.36e-27 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 110.39 E-value: 7.36e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 277 IEARDLTMRFGSFVAVDHVNFRIPRGEIFGFLGSNGCGKSTTMKMLTGLL-----PASEGEAWLFGQPVDPKD-IDTRRR 350
Cdd:PRK14247 4 IEIRDLKVSFGQVEVLDGVNLEIPDNTITALMGPSGSGKSTLLRVFNRLIelypeARVSGEVYLDGQDIFKMDvIELRRR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 351 VGYMSQAFSLYNELTVRQNLELHARLFHI--PEAEIPARVAEMSERFKL-NDVEDIL---PESLPLGIRQRLSLAVAVIH 424
Cdd:PRK14247 84 VQMVFQIPNPIPNLSIFENVALGLKLNRLvkSKKELQERVRWALEKAQLwDEVKDRLdapAGKLSGGQQQRLCIARALAF 163
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 732682709 425 RPEMLILDEPTSGVDPVARDMFWQLMVDLSRQdkVTIFISTHFMNEAERC-DRISLMHAGKVLASGTPQEL 494
Cdd:PRK14247 164 QPEVLLADEPTANLDPENTAKIESLFLELKKD--MTIVLVTHFPQQAARIsDYVAFLYKGQIVEWGPTREV 232
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
291-489 |
9.04e-27 |
|
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic bacteriocins of lactic acid bacteria are produced as precursors which have N-terminal leader peptides that share similarities in amino acid sequence and contain a conserved processing site of two glycine residues in positions -1 and -2. A dedicated ATP-binding cassette (ABC) transporter is responsible for the proteolytic cleavage of the leader peptides and subsequent translocation of the bacteriocins across the cytoplasmic membrane.
Pssm-ID: 213212 [Multi-domain] Cd Length: 220 Bit Score: 109.22 E-value: 9.04e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 291 AVDHVNFRIPRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGEAWLFG---QPVDPKDIdtRRRVGYMSQAFSLYNElTVR 367
Cdd:cd03245 19 ALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGtdiRQLDPADL--RRNIGYVPQDVTLFYG-TLR 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 368 QNLELHArlfhiPEAEiPARVAEMSERFKLNDVEDILPESLPL-----------GIRQRLSLAVAVIHRPEMLILDEPTS 436
Cdd:cd03245 96 DNITLGA-----PLAD-DERILRAAELAGVTDFVNKHPNGLDLqigergrglsgGQRQAVALARALLNDPPILLLDEPTS 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 732682709 437 GVDPVARDMFWQLMVDLSRQDkvTIFISTHFMNEAERCDRISLMHAGKVLASG 489
Cdd:cd03245 170 AMDMNSEERLKERLRQLLGDK--TLIIITHRPSLLDLVDRIIVMDSGRIVADG 220
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
291-499 |
1.06e-26 |
|
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: 109.24 E-value: 1.06e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 291 AVDHVNFRIPRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGEAWLFGQPVdpKDIDT---RRRVGYMSQAFSLYNElTVR 367
Cdd:cd03254 18 VLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGIDI--RDISRkslRSMIGVVLQDTFLFSG-TIM 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 368 QNLelhaRLFHiPEAEiPARVAEMSERFKLNDVEDILPE-----------SLPLGIRQRLSLAVAVIHRPEMLILDEPTS 436
Cdd:cd03254 95 ENI----RLGR-PNAT-DEEVIEAAKEAGAHDFIMKLPNgydtvlgenggNLSQGERQLLAIARAMLRDPKILILDEATS 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 732682709 437 GVDPVARDMFWQLMVDLsRQDKVTIFIStHFMNEAERCDRISLMHAGKVLASGTPQELVEKRG 499
Cdd:cd03254 169 NIDTETEKLIQEALEKL-MKGRTSIIIA-HRLSTIKNADKILVLDDGKIIEEGTHDELLAKKG 229
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
18-246 |
1.51e-26 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 109.03 E-value: 1.51e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 18 VSQHYGKTVALNNITLDIPARCMVGLIGPDGVGKSSLLSLISGARVIEQGNVMVLGGDMRDPKHRRDVCPRIAWMP-QGL 96
Cdd:PRK09493 7 VSKHFGPTQVLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGLKVNDPKVDERLIRQEAGMVfQQF 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 97 gkNLYHTLSVYENVDFFA-RLFGHDKAEREVRINELLTSTGLAPFRDRPAGKLSGGMKQKLGLCCALIHDPELLILDEPT 175
Cdd:PRK09493 87 --YLFPHLTALENVMFGPlRVRGASKEEAEKQARELLAKVGLAERAHHYPSELSGGQQQRVAIARALAVKPKLMLFDEPT 164
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 732682709 176 TGVDPLSRSQFWDLIDSIrqRQSNMSVLVATAYMEEAERF-DWLVAMNAGEVLATGSAEELRQQTQSATLEE 246
Cdd:PRK09493 165 SALDPELRHEVLKVMQDL--AEEGMTMVIVTHEIGFAEKVaSRLIFIDKGRIAEDGDPQVLIKNPPSQRLQE 234
|
|
| COG4559 |
COG4559 |
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism]; |
277-507 |
1.91e-26 |
|
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443620 [Multi-domain] Cd Length: 258 Bit Score: 109.43 E-value: 1.91e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 277 IEARDLTMRFGSFVAVDHVNFRIPRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGEAWLFGQPVD---PKDIDTRRRVgy 353
Cdd:COG4559 2 LEAENLSVRLGGRTLLDDVSLTLRPGELTAIIGPNGAGKSTLLKLLTGELTPSSGEVRLNGRPLAawsPWELARRRAV-- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 354 MSQAFSLYNELTVRQNLELhARLFHI-PEAEIPARVAEMSERFKLNDVEDILPESLPLGIRQRLSLA--VAVIHRPEM-- 428
Cdd:COG4559 80 LPQHSSLAFPFTVEEVVAL-GRAPHGsSAAQDRQIVREALALVGLAHLAGRSYQTLSGGEQQRVQLArvLAQLWEPVDgg 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 429 ---LILDEPTSGVDPvardmFWQLMV-----DLSRQdKVTIFISTHFMNEAER-CDRISLMHAGKVLASGTPQELVEkrg 499
Cdd:COG4559 159 prwLFLDEPTSALDL-----AHQHAVlrlarQLARR-GGGVVAVLHDLNLAAQyADRILLLHQGRLVAQGTPEEVLT--- 229
|
....*...
gi 732682709 500 AASLEEAF 507
Cdd:COG4559 230 DELLERVY 237
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
14-226 |
2.52e-26 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 107.59 E-value: 2.52e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 14 QLAGVSQHYGKTVALNNITLDIPARCMVGLIGPDGVGKSSLLSLISGARVIEQGNVMVLGGDMRD---PKHRRdvcpRIA 90
Cdd:COG4619 2 ELEGLSFRVGGKPILSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIYLDGKPLSAmppPEWRR----QVA 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 91 WMPQ--GLGKNlyhtlSVYENVDFfARLFGHDKAEREvRINELLTSTGLAP-FRDRPAGKLSGGMKQKLGLCCALIHDPE 167
Cdd:COG4619 78 YVPQepALWGG-----TVRDNLPF-PFQLRERKFDRE-RALELLERLGLPPdILDKPVERLSGGERQRLALIRALLLQPD 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 168 LLILDEPTTGVDPLSRSQFWDLIDSIRQRQsNMSVLVATAYMEEAERF-DWLVAMNAGEV 226
Cdd:COG4619 151 VLLLDEPTSALDPENTRRVEELLREYLAEE-GRAVLWVSHDPEQIERVaDRVLTLEAGRL 209
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
27-238 |
2.66e-26 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 110.56 E-value: 2.66e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 27 ALNNITLDIPARCMVGLIGPDGVGKSSLLSLISGARVIEQGNVMVLGgdmRDP-KHRRDVCPRIAW-MPQglgKN-LYHT 103
Cdd:COG4586 37 AVDDISFTIEPGEIVGFIGPNGAGKSTTIKMLTGILVPTSGEVRVLG---YVPfKRRKEFARRIGVvFGQ---RSqLWWD 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 104 LSVYENVDFFARLFGHDKAEREVRINELLTSTGLAPFRDRPAGKLSGGMKQKLGLCCALIHDPELLILDEPTTGVDPLSR 183
Cdd:COG4586 111 LPAIDSFRLLKAIYRIPDAEYKKRLDELVELLDLGELLDTPVRQLSLGQRMRCELAAALLHRPKILFLDEPTIGLDVVSK 190
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 732682709 184 SQFWDLIDSIRQRQsNMSVLVATAYMEEAERF-DWLVAMNAGEVLATGSAEELRQQ 238
Cdd:COG4586 191 EAIREFLKEYNRER-GTTILLTSHDMDDIEALcDRVIVIDHGRIIYDGSLEELKER 245
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
30-244 |
2.73e-26 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 108.30 E-value: 2.73e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 30 NITLDIPARCMVGLIGPDGVGKSSLLSLISGARVIEQGNVMVLGGDMRD-PKHRRDVcpriAWMPQGlgKNLYHTLSVYE 108
Cdd:COG3840 17 RFDLTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILWNGQDLTAlPPAERPV----SMLFQE--NNLFPHLTVAQ 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 109 NVDF----FARLfghDKAEREvRINELLTSTGLAPFRDRPAGKLSGGMKQKLGLCCALIHDPELLILDEPTTGVDPLSRS 184
Cdd:COG3840 91 NIGLglrpGLKL---TAEQRA-QVEQALERVGLAGLLDRLPGQLSGGQRQRVALARCLVRKRPILLLDEPFSALDPALRQ 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 732682709 185 QFWDLIDSIRQRQsNMSVLVATAYMEEAERF-DWLVAMNAGEVLATGSAEELRQQTQSATL 244
Cdd:COG3840 167 EMLDLVDELCRER-GLTVLMVTHDPEDAARIaDRVLLVADGRIAADGPTAALLDGEPPPAL 226
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
291-539 |
3.57e-26 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 109.34 E-value: 3.57e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 291 AVDHVNFRIPRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGEAWLfGQPV-----DPKDIDT-RRRVGYM-----SQAFs 359
Cdd:PRK13634 22 ALYDVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVTI-GERVitagkKNKKLKPlRKKVGIVfqfpeHQLF- 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 360 lynELTVRQNLELHARLFHIPEAEIPARVAEMSERFKLNdvEDILPES---LPLGIRQRLSLAVAVIHRPEMLILDEPTS 436
Cdd:PRK13634 100 ---EETVEKDICFGPMNFGVSEEDAKQKAREMIELVGLP--EELLARSpfeLSGGQMRRVAIAGVLAMEPEVLVLDEPTA 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 437 GVDPVAR----DMFWQlmvdLSRQDKVTIFISTHFMNEAER-CDRISLMHAGKVLASGTPQELVEKrgAASLEE------ 505
Cdd:PRK13634 175 GLDPKGRkemmEMFYK----LHKEKGLTTVLVTHSMEDAARyADQIVVMHKGTVFLQGTPREIFAD--PDELEAigldlp 248
|
250 260 270
....*....|....*....|....*....|....*..
gi 732682709 506 ---AFIAYLQEAAGQSNEaEAPPVVHDTTHAPRQGFS 539
Cdd:PRK13634 249 etvKFKRALEEKFGISFP-KPCLTLEELAHEVVQLLR 284
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
8-238 |
3.64e-26 |
|
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: 114.09 E-value: 3.64e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 8 PVPPVAQLAGVSQHY--GKTVALNNITLDIPARCMVGLIGPDGVGKSSLLSLISGARVIEQGNVMVLGGDMR--DPKHRR 83
Cdd:COG4987 329 PGGPSLELEDVSFRYpgAGRPVLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFLDPQSGSITLGGVDLRdlDEDDLR 408
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 84 DvcpRIAWMPQglgKN-LYHTlSVYENVdffaRLFGHDKAEREVRinELLTSTGLAPF-RDRPAG----------KLSGG 151
Cdd:COG4987 409 R---RIAVVPQ---RPhLFDT-TLRENL----RLARPDATDEELW--AALERVGLGDWlAALPDGldtwlgeggrRLSGG 475
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 152 MKQKLGLCCALIHDPELLILDEPTTGVDPLSRSQFWDLIDSIRQrqsNMSVLVATAYMEEAERFDWLVAMNAGEVLATGS 231
Cdd:COG4987 476 ERRRLALARALLRDAPILLLDEPTEGLDAATEQALLADLLEALA---GRTVLLITHRLAGLERMDRILVLEDGRIVEQGT 552
|
....*..
gi 732682709 232 AEELRQQ 238
Cdd:COG4987 553 HEELLAQ 559
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
14-230 |
5.39e-26 |
|
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) proteins function from bacteria to human, mediating the translocation of substances into and out of cells or organelles. ABC transporters contain two transmembrane-spanning domains (TMDs) or subunits and two nucleotide binding domains (NBDs) or subunits that couple transport to the hydrolysis of ATP. In the maltose transport system, the periplasmic maltose binding protein (MBP) stimulates the ATPase activity of the membrane-associated transporter, which consists of two transmembrane subunits, MalF and MalG, and two copies of the ATP binding subunit, MalK, and becomes tightly bound to the transporter in the catalytic transition state, ensuring that maltose is passed to the transporter as ATP is hydrolyzed.
Pssm-ID: 213268 [Multi-domain] Cd Length: 213 Bit Score: 106.57 E-value: 5.39e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 14 QLAGVSQHYGKTVALNNITLDIPARCMVGLIGPDGVGKSSLLSLISGARVIEQGNVMVLGGDMRD--PKHRrdvcpRIAW 91
Cdd:cd03301 2 ELENVTKRFGNVTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGRDVTDlpPKDR-----DIAM 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 92 MPQGLGknLYHTLSVYENVDFFARLFGHDKAEREVRINELLTSTGLAPFRDRPAGKLSGGMKQKLGLCCALIHDPELLIL 171
Cdd:cd03301 77 VFQNYA--LYPHMTVYDNIAFGLKLRKVPKDEIDERVREVAELLQIEHLLDRKPKQLSGGQRQRVALGRAIVREPKVFLM 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 732682709 172 DEPTTGVDPLSRSQFWDLIDSIRQRQSNMSVLVATAYMEEAERFDWLVAMNAGEVLATG 230
Cdd:cd03301 155 DEPLSNLDAKLRVQMRAELKRLQQRLGTTTIYVTHDQVEAMTMADRIAVMNDGQIQQIG 213
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
20-206 |
5.90e-26 |
|
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: 106.19 E-value: 5.90e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 20 QHYGKTVALNNITLDIPARCMVGLIGPDGVGKSSLLSLISGARVIEQGNVmVLGGDMRDPKHRRDvcpRIAWMPQGLGKN 99
Cdd:cd03226 8 SYKKGTEILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSI-LLNGKPIKAKERRK---SIGYVMQDVDYQ 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 100 LYhTLSVYENVDFFARlfghDKAEREVRINELLTSTGLAPFRDRPAGKLSGGMKQKLGLCCALIHDPELLILDEPTTGVD 179
Cdd:cd03226 84 LF-TDSVREELLLGLK----ELDAGNEQAETVLKDLDLYALKERHPLSLSGGQKQRLAIAAALLSGKDLLIFDEPTSGLD 158
|
170 180
....*....|....*....|....*..
gi 732682709 180 PLSRSQFWDLIDSIrQRQSNmSVLVAT 206
Cdd:cd03226 159 YKNMERVGELIREL-AAQGK-AVIVIT 183
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
277-499 |
5.99e-26 |
|
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: 107.19 E-value: 5.99e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 277 IEARDLTMRFG--SFVAVDHVNFRIPRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGEAWlfgqpVDPKDIDT------R 348
Cdd:cd03252 1 ITFEHVRFRYKpdGPVILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVL-----VDGHDLALadpawlR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 349 RRVGYMSQAFSLYNElTVRQNLELHARLFHIPEAEIPARVA-------EMSERFklndvEDILPE---SLPLGIRQRLSL 418
Cdd:cd03252 76 RQVGVVLQENVLFNR-SIRDNIALADPGMSMERVIEAAKLAgahdfisELPEGY-----DTIVGEqgaGLSGGQRQRIAI 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 419 AVAVIHRPEMLILDEPTSGVDPVARDMFWQLMVDLSrqDKVTIFISTHFMNEAERCDRISLMHAGKVLASGTPQELVEKR 498
Cdd:cd03252 150 ARALIHNPRILIFDEATSALDYESEHAIMRNMHDIC--AGRTVIIIAHRLSTVKNADRIIVMEKGRIVEQGSHDELLAEN 227
|
.
gi 732682709 499 G 499
Cdd:cd03252 228 G 228
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
22-230 |
1.06e-25 |
|
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: 106.65 E-value: 1.06e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 22 YGKTVALNNITLDIPARCMVGLIGPDGVGKSSLLSLISGARVIEQGNVMVLGGD--MRDPKHRRdvcpRIAWMpQGLGKN 99
Cdd:cd03267 31 YREVEALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRVAGLVpwKRRKKFLR----RIGVV-FGQKTQ 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 100 LYHTLSVYENVDFFARLFGHDKAEREVRINELLTSTGLAPFRDRPAGKLSGGMKQKLGLCCALIHDPELLILDEPTTGVD 179
Cdd:cd03267 106 LWWDLPVIDSFYLLAAIYDLPPARFKKRLDELSELLDLEELLDTPVRQLSLGQRMRAEIAAALLHEPEILFLDEPTIGLD 185
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 732682709 180 PLSRSQFWDLIDsIRQRQSNMSVLVATAYMEEAERF-DWLVAMNAGEVLATG 230
Cdd:cd03267 186 VVAQENIRNFLK-EYNRERGTTVLLTSHYMKDIEALaRRVLVIDKGRLLYDG 236
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
20-496 |
1.46e-25 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 112.64 E-value: 1.46e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 20 QHYGKTVALNNITLDIPARCMVGLIGPDGVGKS----SLLSLISGARVIEQGNVMVLG---------GDMRDPKHRRDVC 86
Cdd:PRK10261 24 QEQQKIAAVRNLSFSLQRGETLAIVGESGSGKSvtalALMRLLEQAGGLVQCDKMLLRrrsrqvielSEQSAAQMRHVRG 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 87 PRIAWMPQGLGKNLYHTLSVYENVDFFARL---FGHDKAERE-------VRINELLTSTGLAPFrdrpagKLSGGMKQKL 156
Cdd:PRK10261 104 ADMAMIFQEPMTSLNPVFTVGEQIAESIRLhqgASREEAMVEakrmldqVRIPEAQTILSRYPH------QLSGGMRQRV 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 157 GLCCALIHDPELLILDEPTTGVDPLSRSQFWDLIDSIRQRQSnMSVLVATAYME-EAERFDWLVAMNAGEVLATGSAEEL 235
Cdd:PRK10261 178 MIAMALSCRPAVLIADEPTTALDVTIQAQILQLIKVLQKEMS-MGVIFITHDMGvVAEIADRVLVMYQGEAVETGSVEQI 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 236 RQQTQ---SATLEEAFINL----------------LPQAQR---QAHQAVVIPpyqpenAEIAIEARDLTMRF----GSF 289
Cdd:PRK10261 257 FHAPQhpyTRALLAAVPQLgamkgldyprrfplisLEHPAKqepPIEQDTVVD------GEPILQVRNLVTRFplrsGLL 330
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 290 V-------AVDHVNFRIPRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGEAWLFGQPVDP----KDIDTRRRVGYMSQaf 358
Cdd:PRK10261 331 NrvtrevhAVEKVSFDLWPGETLSLVGESGSGKSTTGRALLRLVESQGGEIIFNGQRIDTlspgKLQALRRDIQFIFQ-- 408
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 359 SLYNELTVRQN--------LELHaRLFHIPEAEipARVAEMSERFKLNDVEDI-LPESLPLGIRQRLSLAVAVIHRPEML 429
Cdd:PRK10261 409 DPYASLDPRQTvgdsimepLRVH-GLLPGKAAA--ARVAWLLERVGLLPEHAWrYPHEFSGGQRQRICIARALALNPKVI 485
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 732682709 430 ILDEPTSGVDPVARDMFWQLMVDLSRQDKVTIFISTHFMNEAERCD-RISLMHAGKVLASGTPQELVE 496
Cdd:PRK10261 486 IADEAVSALDVSIRGQIINLLLDLQRDFGIAYLFISHDMAVVERIShRVAVMYLGQIVEIGPRRAVFE 553
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
15-225 |
1.71e-25 |
|
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: 104.00 E-value: 1.71e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 15 LAGVSQHYG--KTVALNNITLDIPARCMVGLIGPDGVGKSSLLSLISGARVIEQGNVMVLGGDMRDPKhRRDVCPRIAWM 92
Cdd:cd03228 3 FKNVSFSYPgrPKPVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGVDLRDLD-LESLRKNIAYV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 93 PQGLgkNLYHTlSVYENVdffarlfghdkaerevrinelltstglapfrdrpagkLSGGMKQKLGLCCALIHDPELLILD 172
Cdd:cd03228 82 PQDP--FLFSG-TIRENI-------------------------------------LSGGQRQRIAIARALLRDPPILILD 121
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 732682709 173 EPTTGVDPLSRSQFWDLIDSIRQrqsNMSVLVATAYMEEAERFDWLVAMNAGE 225
Cdd:cd03228 122 EATSALDPETEALILEALRALAK---GKTVIVIAHRLSTIRDADRIIVLDDGR 171
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
6-231 |
1.82e-25 |
|
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim protein) in eukaryotes. It is the member of ABC transporter superfamily. Rim protein is a membrane glycoprotein which is localized in the photoreceptor outer segment discs. Mutation/s in its genetic loci is implicated in the recessive Stargardt's disease. [Transport and binding proteins, Other]
Pssm-ID: 130324 [Multi-domain] Cd Length: 2272 Bit Score: 114.34 E-value: 1.82e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 6 LVPVPPVAQLAGVSQHYGKTvALNNITLDIPARCMVGLIGPDGVGKSSLLSLISGARVIEQGNVMVLGGDMRDP----KH 81
Cdd:TIGR01257 925 LVPGVCVKNLVKIFEPSGRP-AVDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGKDIETNldavRQ 1003
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 82 RRDVCPRiawmpqglGKNLYHTLSVYENVDFFARLFGHDKAEREVRINELLTSTGLAPFRDRPAGKLSGGMKQKLGLCCA 161
Cdd:TIGR01257 1004 SLGMCPQ--------HNILFHHLTVAEHILFYAQLKGRSWEEAQLEMEAMLEDTGLHHKRNEEAQDLSGGMQRKLSVAIA 1075
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 732682709 162 LIHDPELLILDEPTTGVDPLSRSQFWDLIDSIRqrqSNMSVLVATAYMEEAERF-DWLVAMNAGEVLATGS 231
Cdd:TIGR01257 1076 FVGDAKVVVLDEPTSGVDPYSRRSIWDLLLKYR---SGRTIIMSTHHMDEADLLgDRIAIISQGRLYCSGT 1143
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
14-238 |
1.93e-25 |
|
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: 113.01 E-value: 1.93e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 14 QLAGVSQHYG--KTVALNNITLDIPARCMVGLIGPDGVGKSSLLSLISGARVIEQGNVMVLGGDMR--DPKHRRDvcpRI 89
Cdd:COG2274 475 ELENVSFRYPgdSPPVLDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEPTSGRILIDGIDLRqiDPASLRR---QI 551
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 90 AWMPQGLgkNLYHTlSVYENVdffarLFGHDKAEREvRINELLTSTGLAPF-RDRPAG----------KLSGGMKQKLGL 158
Cdd:COG2274 552 GVVLQDV--FLFSG-TIRENI-----TLGDPDATDE-EIIEAARLAGLHDFiEALPMGydtvvgeggsNLSGGQRQRLAI 622
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 159 CCALIHDPELLILDEPTTGVDPLSRSQFwdlIDSIRQRQSNMSVLVATAYMEEAERFDWLVAMNAGEVLATGSAEELRQQ 238
Cdd:COG2274 623 ARALLRNPRILILDEATSALDAETEAII---LENLRRLLKGRTVIIIAHRLSTIRLADRIIVLDKGRIVEDGTHEELLAR 699
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
295-489 |
2.12e-25 |
|
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: 105.43 E-value: 2.12e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 295 VNFRIPRGEIFGFLGSNGCGKSTTMKMLTGLLP---ASEGEAWLFGQPVDPKDidTRRRVGYMSQAFSLYNELTVRQNLE 371
Cdd:cd03234 26 VSLHVESGQVMAILGSSGSGKTTLLDAISGRVEgggTTSGQILFNGQPRKPDQ--FQKCVAYVRQDDILLPGLTVRETLT 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 372 LHARL---FHIPEAEIPARVAEMSER-FKLNDVEDILPESLPLGIRQRLSLAVAVIHRPEMLILDEPTSGVDPVARDMFW 447
Cdd:cd03234 104 YTAILrlpRKSSDAIRKKRVEDVLLRdLALTRIGGNLVKGISGGERRRVSIAVQLLWDPKVLILDEPTSGLDSFTALNLV 183
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 732682709 448 QLMVDLSRQDKvTIFISTH------FmneaERCDRISLMHAGKVLASG 489
Cdd:cd03234 184 STLSQLARRNR-IVILTIHqprsdlF----RLFDRILLLSSGEIVYSG 226
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
23-235 |
2.52e-25 |
|
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: 106.57 E-value: 2.52e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 23 GKTVALNNITLDIPARCMVGLIGPDGVGKSSLLSLISgaRVIE--QGNVMVLGGDMRDPKH------RRDvcpRIAWMPQ 94
Cdd:cd03294 35 GQTVGVNDVSLDVREGEIFVIMGLSGSGKSTLLRCIN--RLIEptSGKVLIDGQDIAAMSRkelrelRRK---KISMVFQ 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 95 GLGknLYHTLSVYENVDFFARLFGHDKAEREVRINELLTSTGLAPFRDRPAGKLSGGMKQKLGLCCALIHDPELLILDEP 174
Cdd:cd03294 110 SFA--LLPHRTVLENVAFGLEVQGVPRAEREERAAEALELVGLEGWEHKYPDELSGGMQQRVGLARALAVDPDILLMDEA 187
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 732682709 175 TTGVDPLSRSQFWDLIDSIrQRQSNMSVLVATAYMEEAERF-DWLVAMNAGEVLATGSAEEL 235
Cdd:cd03294 188 FSALDPLIRREMQDELLRL-QAELQKTIVFITHDLDEALRLgDRIAIMKDGRLVQVGTPEEI 248
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
14-212 |
2.91e-25 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 106.10 E-value: 2.91e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 14 QLAGVSQHYGK----TVALNNITLDIPARCMVGLIGPDGVGKSSLLSLISGARVIEQGNVMVLGGDMRDPKHRRDVC-PR 88
Cdd:COG4525 5 TVRHVSVRYPGggqpQPALQDVSLTIESGEFVVALGASGCGKTTLLNLIAGFLAPSSGEITLDGVPVTGPGADRGVVfQK 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 89 IAWMPQglgknlyhtLSVYENVDFFARLFGHDKAEREVRINELLTSTGLAPFRDRPAGKLSGGMKQKLGLCCALIHDPEL 168
Cdd:COG4525 85 DALLPW---------LNVLDNVAFGLRLRGVPKAERRARAEELLALVGLADFARRRIWQLSGGMRQRVGIARALAADPRF 155
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 732682709 169 LILDEPTTGVDPLSRSQFWDLIDSIRQRqSNMSVLVATAYMEEA 212
Cdd:COG4525 156 LLMDEPFGALDALTREQMQELLLDVWQR-TGKGVFLITHSVEEA 198
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
277-494 |
3.43e-25 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 106.35 E-value: 3.43e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 277 IEARDLTMRFGS---FVAVDHVNFRIPRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGEAWLFGQPVDPKDI-DTRRRVG 352
Cdd:PRK13650 5 IEVKNLTFKYKEdqeKYTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIIDGDLLTEENVwDIRHKIG 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 353 YMSQ---------------AFSLYNEltvrqnlelharlfHIPEAEIPARVAEMSERFKLNDVEDILPESLPLGIRQRLS 417
Cdd:PRK13650 85 MVFQnpdnqfvgatveddvAFGLENK--------------GIPHEEMKERVNEALELVGMQDFKEREPARLSGGQKQRVA 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 732682709 418 LAVAVIHRPEMLILDEPTSGVDPVARDMFWQLMVDLSRQDKVTIFISTHFMNEAERCDRISLMHAGKVLASGTPQEL 494
Cdd:PRK13650 151 IAGAVAMRPKIIILDEATSMLDPEGRLELIKTIKGIRDDYQMTVISITHDLDEVALSDRVLVMKNGQVESTSTPREL 227
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
281-494 |
3.93e-25 |
|
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: 107.88 E-value: 3.93e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 281 DLTMRFGSFvAVDhVNFRIPRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGEAWLFGQPV--DPKDIDT---RRRVGYMS 355
Cdd:COG4148 6 DFRLRRGGF-TLD-VDFTLPGRGVTALFGPSGSGKTTLLRAIAGLERPDSGRIRLGGEVLqdSARGIFLpphRRRIGYVF 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 356 QAFSLYNELTVRQNLELHARlfHIPEAEIPARVAEMSERFKLNDVEDILPESLPLGIRQRLSLAVAVIHRPEMLILDEPT 435
Cdd:COG4148 84 QEARLFPHLSVRGNLLYGRK--RAPRAERRISFDEVVELLGIGHLLDRRPATLSGGERQRVAIGRALLSSPRLLLMDEPL 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 732682709 436 SGVDPVARDmfwQLM---VDLSRQDKVTIFISTHFMNEAER-CDRISLMHAGKVLASGTPQEL 494
Cdd:COG4148 162 AALDLARKA---EILpylERLRDELDIPILYVSHSLDEVARlADHVVLLEQGRVVASGPLAEV 221
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
14-235 |
5.81e-25 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 107.15 E-value: 5.81e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 14 QLAGVSQHYGKTVALNNITLDIPARCMVGLIGPDGVGKSSLLSLISGarvIEQ---GNVMVLGGDM---RDPKHRRdvcp 87
Cdd:COG1118 4 EVRNISKRFGSFTLLDDVSLEIASGELVALLGPSGSGKTTLLRIIAG---LETpdsGRIVLNGRDLftnLPPRERR---- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 88 rIAWMPQglgkN--LYHTLSVYENVDFFARLFGHDKAEREVRINELLTSTGLAPFRDRPAGKLSGGMKQKLGLCCALIHD 165
Cdd:COG1118 77 -VGFVFQ----HyaLFPHMTVAENIAFGLRVRPPSKAEIRARVEELLELVQLEGLADRYPSQLSGGQRQRVALARALAVE 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 732682709 166 PELLILDEPTTGVDPLSRSQFWDLIDSIRQRQSNMSVLVaTAYMEEAERF-DWLVAMNAGEVLATGSAEEL 235
Cdd:COG1118 152 PEVLLLDEPFGALDAKVRKELRRWLRRLHDELGGTTVFV-THDQEEALELaDRVVVMNQGRIEQVGTPDEV 221
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
10-498 |
6.13e-25 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 109.63 E-value: 6.13e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 10 PPVAQLAGVSQHYGKTVALNNITLDIPARCMVGLIGPDGVGKSSLLSLISGarVIEQGNV---MVLGGDMRDPKHRRDVC 86
Cdd:PRK13549 3 EYLLEMKNITKTFGGVKALDNVSLKVRAGEIVSLCGENGAGKSTLMKVLSG--VYPHGTYegeIIFEGEELQASNIRDTE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 87 PR-IAWMPQGLGknLYHTLSVYENVdFFARLFGH----DKAEREVRINELLTSTGLAPFRDRPAGKLSGGMKQKLGLCCA 161
Cdd:PRK13549 81 RAgIAIIHQELA--LVKELSVLENI-FLGNEITPggimDYDAMYLRAQKLLAQLKLDINPATPVGNLGLGQQQLVEIAKA 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 162 LIHDPELLILDEPTTgvdPLSRSQFWDLIDSIRQRQSNMsvlVATAYM-----EEAERFDWLVAMNAGEVLATGSAEELR 236
Cdd:PRK13549 158 LNKQARLLILDEPTA---SLTESETAVLLDIIRDLKAHG---IACIYIshklnEVKAISDTICVIRDGRHIGTRPAAGMT 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 237 qqtqsatlEEAFI---------NLLPQAQRQAHQAVV----IPPYQPENAEIAIeardltmrfgsfvaVDHVNFRIPRGE 303
Cdd:PRK13549 232 --------EDDIItmmvgreltALYPREPHTIGEVILevrnLTAWDPVNPHIKR--------------VDDVSFSLRRGE 289
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 304 IFGFLGSNGCGKSTTMKMLTGLLP-ASEGEAWLFGQPVD---------------PKDidtRRRVGYMSQAFSLYN-ELTV 366
Cdd:PRK13549 290 ILGIAGLVGAGRTELVQCLFGAYPgRWEGEIFIDGKPVKirnpqqaiaqgiamvPED---RKRDGIVPVMGVGKNiTLAA 366
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 367 RQNLELHARLFHipEAEIPARVAEMSeRFKLNDVEDILP-ESLPLGIRQRLSLAVAVIHRPEMLILDEPTSGVDPVARDM 445
Cdd:PRK13549 367 LDRFTGGSRIDD--AAELKTILESIQ-RLKVKTASPELAiARLSGGNQQKAVLAKCLLLNPKILILDEPTRGIDVGAKYE 443
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|...
gi 732682709 446 FWQLMVDLSRQDKVTIFISTHFMNEAERCDRISLMHAGKVLASGTPQELVEKR 498
Cdd:PRK13549 444 IYKLINQLVQQGVAIIVISSELPEVLGLSDRVLVMHEGKLKGDLINHNLTQEQ 496
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
14-212 |
6.63e-25 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 104.78 E-value: 6.63e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 14 QLAGVSQHYGKTVALNNITLDIPARCMVGLIGPDGVGKSSLLSLISGARVIEQGNVMVLGGDMRDPKHRRDVcpriawMP 93
Cdd:PRK11248 3 QISHLYADYGGKPALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDGKPVEGPGAERGV------VF 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 94 QGLGknLYHTLSVYENVDFFARLFGHDKAEREVRINELLTSTGLAPFRDRPAGKLSGGMKQKLGLCCALIHDPELLILDE 173
Cdd:PRK11248 77 QNEG--LLPWRNVQDNVAFGLQLAGVEKMQRLEIAHQMLKKVGLEGAEKRYIWQLSGGQRQRVGIARALAANPQLLLLDE 154
|
170 180 190
....*....|....*....|....*....|....*....
gi 732682709 174 PTTGVDPLSRSQFWDLIDSIRQRQSNmSVLVATAYMEEA 212
Cdd:PRK11248 155 PFGALDAFTREQMQTLLLKLWQETGK-QVLLITHDIEEA 192
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
281-516 |
6.86e-25 |
|
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: 107.12 E-value: 6.86e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 281 DLTMRFGSFvAVDhVNFRIPRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGEAWLFGQPVDP--KDIDT---RRRVGYMS 355
Cdd:TIGR02142 4 RFSKRLGDF-SLD-ADFTLPGQGVTAIFGRSGSGKTTLIRLIAGLTRPDEGEIVLNGRTLFDsrKGIFLppeKRRIGYVF 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 356 QAFSLYNELTVRQNLELHARLFHIPEAEI-PARVAEMserFKLNDVEDILPESLPLGIRQRLSLAVAVIHRPEMLILDEP 434
Cdd:TIGR02142 82 QEARLFPHLSVRGNLRYGMKRARPSERRIsFERVIEL---LGIGHLLGRLPGRLSGGEKQRVAIGRALLSSPRLLLMDEP 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 435 TSGVDPVARDMFWQLMVDLSRQDKVTIFISTHFMNEAER-CDRISLMHAGKVLASGTPQEL--------VEKRGAASLEE 505
Cdd:TIGR02142 159 LAALDDPRKYEILPYLERLHAEFGIPILYVSHSLQEVLRlADRVVVLEDGRVAAAGPIAEVwaspdlpwLAREDQGSLIE 238
|
250
....*....|.
gi 732682709 506 AFIAYLQEAAG 516
Cdd:TIGR02142 239 GVVAEHDQHYG 249
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
279-495 |
7.04e-25 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 104.21 E-value: 7.04e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 279 ARDLTMRFGSFVAVDHVNFRIPRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGEAwlfgqPVDPKDID-------TRRRV 351
Cdd:PRK10895 6 AKNLAKAYKGRRVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNI-----IIDDEDISllplharARRGI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 352 GYMSQAFSLYNELTVRQNLELHARLFH-IPEAEIPARVAEMSERFKLNDVEDILPESLPLGIRQRLSLAVAVIHRPEMLI 430
Cdd:PRK10895 81 GYLPQEASIFRRLSVYDNLMAVLQIRDdLSAEQREDRANELMEEFHIEHLRDSMGQSLSGGERRRVEIARALAANPKFIL 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 732682709 431 LDEPTSGVDPVARDMFWQLMVDLsRQDKVTIFISTHFMNEA-ERCDRISLMHAGKVLASGTPQELV 495
Cdd:PRK10895 161 LDEPFAGVDPISVIDIKRIIEHL-RDSGLGVLITDHNVRETlAVCERAYIVSQGHLIAHGTPTEIL 225
|
|
| LPS_export_lptB |
TIGR04406 |
LPS export ABC transporter ATP-binding protein; Members of this fmaily are LptB, the ... |
17-235 |
7.51e-25 |
|
LPS export ABC transporter ATP-binding protein; Members of this fmaily are LptB, the ATP-binding cassette protein of an ABC transporter involved in lipopolysaccharide export. [Cell envelope, Biosynthesis and degradation of surface polysaccharides and lipopolysaccharides, Transport and binding proteins, Other]
Pssm-ID: 275199 [Multi-domain] Cd Length: 239 Bit Score: 104.28 E-value: 7.51e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 17 GVSQHYGKTVALNNITLDIPARCMVGLIGPDGVGKSSLLSLISGARVIEQGNVMVLGGDMRD-PKHRRdvcPR--IAWMP 93
Cdd:TIGR04406 6 NLIKSYKKRKVVNDVSLSVKSGEIVGLLGPNGAGKTTSFYMIVGLVRPDAGKILIDGQDITHlPMHER---ARlgIGYLP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 94 QGlgKNLYHTLSVYENVDFFARLFGH-DKAEREVRINELLTSTGLAPFRDRPAGKLSGGMKQKLGLCCALIHDPELLILD 172
Cdd:TIGR04406 83 QE--ASIFRKLTVEENIMAVLEIRKDlDRAEREERLEALLEEFQISHLRDNKAMSLSGGERRRVEIARALATNPKFILLD 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 732682709 173 EPTTGVDPLSRSQFWDLIDSIRQRqsNMSVLVA------------TAYMeeaerfdwlvaMNAGEVLATGSAEEL 235
Cdd:TIGR04406 161 EPFAGVDPIAVGDIKKIIKHLKER--GIGVLITdhnvretldicdRAYI-----------ISDGKVLAEGTPAEI 222
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
291-497 |
8.98e-25 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 105.27 E-value: 8.98e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 291 AVDHVNFRIPRGEIFGFLGSNGCGKSTTMKMLTGLL---PASEGEAWLFGQPVDPKDI-DTRRRVGYMSQ---------- 356
Cdd:PRK13640 22 ALNDISFSIPRGSWTALIGHNGSGKSTISKLINGLLlpdDNPNSKITVDGITLTAKTVwDIREKVGIVFQnpdnqfvgat 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 357 -----AFSLYNeltvRQnlelharlfhIPEAEIPARVAEMSERFKLNDVEDILPESLPLGIRQRLSLAVAVIHRPEMLIL 431
Cdd:PRK13640 102 vgddvAFGLEN----RA----------VPRPEMIKIVRDVLADVGMLDYIDSEPANLSGGQKQRVAIAGILAVEPKIIIL 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 732682709 432 DEPTSGVDPVARDMFWQLMVDLSRQDKVTIFISTHFMNEAERCDRISLMHAGKVLASGTPQELVEK 497
Cdd:PRK13640 168 DESTSMLDPAGKEQILKLIRKLKKKNNLTVISITHDIDEANMADQVLVLDDGKLLAQGSPVEIFSK 233
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
17-235 |
1.41e-24 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 103.57 E-value: 1.41e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 17 GVSQHYGKTVALNNITLDIPARCMVGLIGPDGVGKSSLLSLISGARVIEQGNVMVLGGDM-RDPKHRRdvcpriAWMpqG 95
Cdd:COG1137 8 NLVKSYGKRTVVKDVSLEVNQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGRIFLDGEDItHLPMHKR------ARL--G 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 96 LGknlY--------HTLSVYENVDFFARLFGHDKAEREVRINELLTSTGLAPFRDRPAGKLSGGMKQKLGLCCALIHDPE 167
Cdd:COG1137 80 IG---YlpqeasifRKLTVEDNILAVLELRKLSKKEREERLEELLEEFGITHLRKSKAYSLSGGERRRVEIARALATNPK 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 168 LLILDEPTTGVDPLSRSQFWDLIDSIRQRqsNMSVLVA------------TAYMeeaerfdwlvaMNAGEVLATGSAEEL 235
Cdd:COG1137 157 FILLDEPFAGVDPIAVADIQKIIRHLKER--GIGVLITdhnvretlgicdRAYI-----------ISEGKVLAEGTPEEI 223
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
277-505 |
2.22e-24 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 102.86 E-value: 2.22e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 277 IEARDLTMRFGSFVAVDHVNFRIPRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGEAWLFGQPV-DPK--DIDTRRRVGY 353
Cdd:PRK09493 2 IEFKNVSKHFGPTQVLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGLKVnDPKvdERLIRQEAGM 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 354 MSQAFSLYNELTVRQNL---ELHARLFHIPEAEIPARvaEMSERFKLNDVEDILPESLPLGIRQRLSLAVAVIHRPEMLI 430
Cdd:PRK09493 82 VFQQFYLFPHLTALENVmfgPLRVRGASKEEAEKQAR--ELLAKVGLAERAHHYPSELSGGQQQRVAIARALAVKPKLML 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 732682709 431 LDEPTSGVDPVARDMFWQLMVDLSrQDKVTIFISTHFMNEAERC-DRISLMHAGKVLASGTPQELVEKRGAASLEE 505
Cdd:PRK09493 160 FDEPTSALDPELRHEVLKVMQDLA-EEGMTMVIVTHEIGFAEKVaSRLIFIDKGRIAEDGDPQVLIKNPPSQRLQE 234
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
11-485 |
2.77e-24 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 107.78 E-value: 2.77e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 11 PVAQLAGVSQHYGKTVALNNITLDI-PARCMvGLIGPDGVGKSSLLSLISGARVIEQGNVMVLGGDMR--DPKHRRDVcp 87
Cdd:PRK10762 3 ALLQLKGIDKAFPGVKALSGAALNVyPGRVM-ALVGENGAGKSTMMKVLTGIYTRDAGSILYLGKEVTfnGPKSSQEA-- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 88 RIAWMPQGLgkNLYHTLSVYENVdFFARLFGH-------DKAEREVriNELLTSTGLAPFRDRPAGKLSGGMKQKLGLCC 160
Cdd:PRK10762 80 GIGIIHQEL--NLIPQLTIAENI-FLGREFVNrfgridwKKMYAEA--DKLLARLNLRFSSDKLVGELSIGEQQMVEIAK 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 161 ALIHDPELLILDEPTtgvDPLSRSQFWDLIDSIRQ-RQSNMSVLVATAYMEEA-ERFDWLVAMNAGEVLAtgsaeelrQQ 238
Cdd:PRK10762 155 VLSFESKVIIMDEPT---DALTDTETESLFRVIRElKSQGRGIVYISHRLKEIfEICDDVTVFRDGQFIA--------ER 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 239 TQSATLEEAFINLLpQAQRQAHQavvIPPYQPENAEIAIEARDLTmrfGSfvAVDHVNFRIPRGEIFGFLGSNGCGKSTT 318
Cdd:PRK10762 224 EVADLTEDSLIEMM-VGRKLEDQ---YPRLDKAPGEVRLKVDNLS---GP--GVNDVSFTLRKGEILGVSGLMGAGRTEL 294
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 319 MKMLTGLLPASEGEAWLFGQPVDPKDIDTRRRVG--YMSQ---AFSLYNELTVRQNLELHA------RLFHIPEAEIPAR 387
Cdd:PRK10762 295 MKVLYGALPRTSGYVTLDGHEVVTRSPQDGLANGivYISEdrkRDGLVLGMSVKENMSLTAlryfsrAGGSLKHADEQQA 374
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 388 VAEMSERF--KLNDVEDILPEsLPLGIRQRLSLAVAVIHRPEMLILDEPTSGVDPVARDMFWQLmVDLSRQDKVTIFIST 465
Cdd:PRK10762 375 VSDFIRLFniKTPSMEQAIGL-LSGGNQQKVAIARGLMTRPKVLILDEPTRGVDVGAKKEIYQL-INQFKAEGLSIILVS 452
|
490 500
....*....|....*....|.
gi 732682709 466 HFMNEA-ERCDRISLMHAGKV 485
Cdd:PRK10762 453 SEMPEVlGMSDRILVMHEGRI 473
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
270-497 |
3.06e-24 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 104.81 E-value: 3.06e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 270 PENAEIAIEARDLTMRF---GSFV--------AVDHVNFRIPRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGEAWLFGQ 338
Cdd:COG4608 1 AAMAEPLLEVRDLKKHFpvrGGLFgrtvgvvkAVDGVSFDIRRGETLGLVGESGCGKSTLGRLLLRLEEPTSGEILFDGQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 339 PV---DPKDI-DTRRRVGYMSQ---AfSLYNELTVRQNLELHARLFHI-PEAEIPARVAEMSERFKLN-DVEDILPESLP 409
Cdd:COG4608 81 DItglSGRELrPLRRRMQMVFQdpyA-SLNPRMTVGDIIAEPLRIHGLaSKAERRERVAELLELVGLRpEHADRYPHEFS 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 410 LGIRQRLSLAVAVIHRPEMLILDEPTSgvdpvARDMFWQ-----LMVDLSRQDKVT-IFIStHFMNEAER-CDRISLMHA 482
Cdd:COG4608 160 GGQRQRIGIARALALNPKLIVCDEPVS-----ALDVSIQaqvlnLLEDLQDELGLTyLFIS-HDLSVVRHiSDRVAVMYL 233
|
250
....*....|....*
gi 732682709 483 GKVLASGTPQELVEK 497
Cdd:COG4608 234 GKIVEIAPRDELYAR 248
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
28-234 |
3.39e-24 |
|
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: 102.03 E-value: 3.39e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 28 LNNITLDIPARCMVGLIGPDGVGKSSLLSLISGARVIEQGNVMVLGGDMRD-PKHRRDvcprIAWMPQGlgKNLYHTLSV 106
Cdd:cd03299 15 LKNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNGKDITNlPPEKRD----ISYVPQN--YALFPHMTV 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 107 YENVDFFARLFGHDKAEREVRINELLTSTGLAPFRDRPAGKLSGGMKQKLGLCCALIHDPELLILDEPTTGVDPLSRSQF 186
Cdd:cd03299 89 YKNIAYGLKKRKVDKKEIERKVLEIAEMLGIDHLLNRKPETLSGGEQQRVAIARALVVNPKILLLDEPFSALDVRTKEKL 168
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 732682709 187 WDLIDSIRqRQSNMSVLVATAYMEEAERF-DWLVAMNAGEVLATGSAEE 234
Cdd:cd03299 169 REELKKIR-KEFGVTVLHVTHDFEEAWALaDKVAIMLNGKLIQVGKPEE 216
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
277-494 |
4.20e-24 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 103.25 E-value: 4.20e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 277 IEARDLTMRFGSFVAVDHVN---FRIPRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGEAWLFGQPVDPKDI-DTRRRVG 352
Cdd:PRK13642 5 LEVENLVFKYEKESDVNQLNgvsFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDGELLTAENVwNLRRKIG 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 353 YMSQ-AFSLYNELTVRQNLELHARLFHIPEAEIPARVAEMSERFKLNDVEDILPESLPLGIRQRLSLAVAVIHRPEMLIL 431
Cdd:PRK13642 85 MVFQnPDNQFVGATVEDDVAFGMENQGIPREEMIKRVDEALLAVNMLDFKTREPARLSGGQKQRVAVAGIIALRPEIIIL 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 732682709 432 DEPTSGVDPVARDMFWQLMVDLSRQDKVTIFISTHFMNEAERCDRISLMHAGKVLASGTPQEL 494
Cdd:PRK13642 165 DESTSMLDPTGRQEIMRVIHEIKEKYQLTVLSITHDLDEAASSDRILVMKAGEIIKEAAPSEL 227
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
273-504 |
4.54e-24 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 104.82 E-value: 4.54e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 273 AEIAIEARDLTMRFGSFVAVDHVNFRIPRGEIFGFLGSNGCGKSTtmkmltGLLPA------SEGEAWLFGQPVDPKDId 346
Cdd:NF000106 10 ARNAVEVRGLVKHFGEVKAVDGVDLDVREGTVLGVLGP*GAA**R------GALPAhv*gpdAGRRPWRF*TWCANRRA- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 347 TRRRVGYMSQAFSLYNE-LTVRQNLELHARLFHIPEAEIPARVAEMSERFKLNDVEDILPESLPLGIRQRLSLAVAVIHR 425
Cdd:NF000106 83 LRRTIG*HRPVR*GRREsFSGRENLYMIGR*LDLSRKDARARADELLERFSLTEAAGRAAAKYSGGMRRRLDLAASMIGR 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 426 PEMLILDEPTSGVDPVARDMFWQLMVDLSRqDKVTIFISTHFMNEAER-CDRISLMHAGKVLASGTPQELVEKRGAASLE 504
Cdd:NF000106 163 PAVLYLDEPTTGLDPRTRNEVWDEVRSMVR-DGATVLLTTQYMEEAEQlAHELTVIDRGRVIADGKVDELKTKVGGRTLQ 241
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
285-480 |
5.53e-24 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 100.39 E-value: 5.53e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 285 RFGSFVAVDHVNFRIPRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGEAwlfgqpvdpkDIDTRRRVGYMSQAFSLYNEL 364
Cdd:NF040873 1 GYGGRPVLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTV----------RRAGGARVAYVPQRSEVPDSL 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 365 --TVRQNLEL----HARLFHIPEAEIPARVAEMSERFKLNDVEDILPESLPLGIRQRLSLAVAVIHRPEMLILDEPTSGV 438
Cdd:NF040873 71 plTVRDLVAMgrwaRRGLWRRLTRDDRAAVDDALERVGLADLAGRQLGELSGGQRQRALLAQGLAQEADLLLLDEPTTGL 150
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 732682709 439 DPVARDMFWQLMVDLSRqDKVTIFISTHFMNEAERCDRISLM 480
Cdd:NF040873 151 DAESRERIIALLAEEHA-RGATVVVVTHDLELVRRADPCVLL 191
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
272-494 |
6.47e-24 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 106.79 E-value: 6.47e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 272 NAEIAIEARDLTMRFGSFVAVDHVNFRIPRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGEAWLFGQP---VDPKdIDTR 348
Cdd:PRK09700 1 MATPYISMAGIGKSFGPVHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNINynkLDHK-LAAQ 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 349 RRVGYMSQAFSLYNELTVRQNL----ELHARLFHIP---EAEIPARVAEMSERFKLNDVEDILPESLPLGIRQRLSLAVA 421
Cdd:PRK09700 80 LGIGIIYQELSVIDELTVLENLyigrHLTKKVCGVNiidWREMRVRAAMMLLRVGLKVDLDEKVANLSISHKQMLEIAKT 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 732682709 422 VIHRPEMLILDEPTSGVDPVARDMFWQLMVDLSRQDKVTIFIStHFMNEAER-CDRISLMHAGKVLASGTPQEL 494
Cdd:PRK09700 160 LMLDAKVIIMDEPTSSLTNKEVDYLFLIMNQLRKEGTAIVYIS-HKLAEIRRiCDRYTVMKDGSSVCSGMVSDV 232
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
276-471 |
8.53e-24 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 101.86 E-value: 8.53e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 276 AIEARDLTMRFGSFV----AVDHVNFRIPRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGEAWLFGQPVDPKDIDtrRRV 351
Cdd:COG4525 3 MLTVRHVSVRYPGGGqpqpALQDVSLTIESGEFVVALGASGCGKTTLLNLIAGFLAPSSGEITLDGVPVTGPGAD--RGV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 352 GYmsQAFSLYNELTVRQNLELHARLFHIPEAEIPARVAEMSERFKLNDVEDILPESLPLGIRQRLSLAVAVIHRPEMLIL 431
Cdd:COG4525 81 VF--QKDALLPWLNVLDNVAFGLRLRGVPKAERRARAEELLALVGLADFARRRIWQLSGGMRQRVGIARALAADPRFLLM 158
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 732682709 432 DEPTSGVDPVARDMFWQLMVDLSRQDKVTIFISTHFMNEA 471
Cdd:COG4525 159 DEPFGALDALTREQMQELLLDVWQRTGKGVFLITHSVEEA 198
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
276-536 |
1.00e-23 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 101.74 E-value: 1.00e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 276 AIEARDLTMRFGSFV-AVDHVNFRIPRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGEAWLFGQPVDPKDI-DTRRRVGY 353
Cdd:PRK13647 4 IIEVEDLHFRYKDGTkALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGREVNAENEkWVRSKVGL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 354 M-----SQAFSLYNELTVR---QNLELHArlfhipeAEIPARVAEMSERFKLNDVEDILPESLPLGIRQRLSLAVAVIHR 425
Cdd:PRK13647 84 VfqdpdDQVFSSTVWDDVAfgpVNMGLDK-------DEVERRVEEALKAVRMWDFRDKPPYHLSYGQKKRVAIAGVLAMD 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 426 PEMLILDEPTSGVDPVARDMFWQLMVDLSRQDKvTIFISTHFMN-EAERCDRISLMHAGKVLASGTPQELVEKR--GAAS 502
Cdd:PRK13647 157 PDVIVLDEPMAYLDPRGQETLMEILDRLHNQGK-TVIVATHDVDlAAEWADQVIVLKEGRVLAEGDKSLLTDEDivEQAG 235
|
250 260 270
....*....|....*....|....*....|....
gi 732682709 503 LEEAFIAYLQEAAGQSNEAEAPPVVHDTTHAPRQ 536
Cdd:PRK13647 236 LRLPLVAQIFEDLPELGQSKLPLTVKEAVQIIRK 269
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
14-245 |
1.35e-23 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 103.28 E-value: 1.35e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 14 QLAGVSQHYGKTVALNNITLDIPARCMVGLIGPDGVgkssllSLISGARvieqgNVMVLGGDM-RDPKHRRDVCPRIAWM 92
Cdd:NF000106 15 EVRGLVKHFGEVKAVDGVDLDVREGTVLGVLGP*GA------A**RGAL-----PAHV*GPDAgRRPWRF*TWCANRRAL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 93 PQGLGKNL------YHTLSVYENVDFFARLFGHDKAEREVRINELLTSTGLAPFRDRPAGKLSGGMKQKLGLCCALIHDP 166
Cdd:NF000106 84 RRTIG*HRpvr*grRESFSGRENLYMIGR*LDLSRKDARARADELLERFSLTEAAGRAAAKYSGGMRRRLDLAASMIGRP 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 167 ELLILDEPTTGVDPLSRSQFWDLIDSIrqRQSNMSVLVATAYMEEAERF-DWLVAMNAGEVLATGSAEELRQQTQSATLE 245
Cdd:NF000106 164 AVLYLDEPTTGLDPRTRNEVWDEVRSM--VRDGATVLLTTQYMEEAEQLaHELTVIDRGRVIADGKVDELKTKVGGRTLQ 241
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
295-489 |
1.63e-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: 98.78 E-value: 1.63e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 295 VNFRIPRGEIFGFLGSNGCGKSTTMKMLTGLL--PASEGEAWLFGQPVDPKDIdtRRRVGYMSQAFSLYNELTVRQNLEL 372
Cdd:cd03213 28 VSGKAKPGELTAIMGPSGAGKSTLLNALAGRRtgLGVSGEVLINGRPLDKRSF--RKIIGYVPQDDILHPTLTVRETLMF 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 373 HARLfhipeaeiparvaemserfklndvedilpESLPLGIRQRLSLAVAVIHRPEMLILDEPTSGVDPVardMFWQLMVD 452
Cdd:cd03213 106 AAKL-----------------------------RGLSGGERKRVSIALELVSNPSLLFLDEPTSGLDSS---SALQVMSL 153
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 732682709 453 LSR--QDKVTIFISTH------FmneaERCDRISLMHAGKVLASG 489
Cdd:cd03213 154 LRRlaDTGRTIICSIHqpsseiF----ELFDKLLLLSQGRVIYFG 194
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
273-485 |
1.63e-23 |
|
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: 98.66 E-value: 1.63e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 273 AEIAIEARDLTMRfgsfVAVDHVNFRIPRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGEAWLFGQPVDPKDIDTRRRVG 352
Cdd:cd03215 1 GEPVLEVRGLSVK----GAVRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITLDGKPVTRRSPRDAIRAG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 353 ymsqafslyneltvrqnlelharLFHIPEAeipaR-----VAEMSERFKLndvedILPESLPLGIRQRLSLAVAVIHRPE 427
Cdd:cd03215 77 -----------------------IAYVPED----RkreglVLDLSVAENI-----ALSSLLSGGNQQKVVLARWLARDPR 124
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 732682709 428 MLILDEPTSGVDPVARDMFWQLMVDLSRQDKVTIFISTHfMNEAER-CDRISLMHAGKV 485
Cdd:cd03215 125 VLILDEPTRGVDVGAKAEIYRLIRELADAGKAVLLISSE-LDELLGlCDRILVMYEGRI 182
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
8-221 |
2.78e-23 |
|
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family transporter in which each gene contains an N-terminal membrane-spanning domain (pfam00664) and a C-terminal ATP-binding domain (pfam00005). In E. coli these genes were discovered as mutants which caused the terminal heme-copper oxidase complex cytochrome bd to fail to assemble. Recent work has shown that the transporter is involved in export of redox-active thiol compounds such as cysteine and glutathione. The linkage to assembly of the cytochrome bd complex is further supported by the conserved operon structure found outside the gammaproteobacteria (cydABCD) containing both the transporter and oxidase genes components. The genes used as the seed members for this model are all either found in the gammproteobacterial context or the CydABCD context. All members of this family scoring above trusted at the time of its creation were from genomes which encode a cytochrome bd complex. Unfortunately, the gene symbol nomenclature adopted based on this operon in B. subtilis assigns cydC to the third gene in the operon where this gene is actually homologous to the E. coli cydD gene. We have chosen to name all homologs in this family in accordance with the precedence of publication of the E. coli name, CydD
Pssm-ID: 274323 [Multi-domain] Cd Length: 529 Bit Score: 105.06 E-value: 2.78e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 8 PVPPVAQLAGVSQHY-GKTVALNNITLDIPARCMVGLIGPDGVGKSSLLSLISGARVIEQGNVMVLGGDMR--DPKHRRD 84
Cdd:TIGR02857 317 APASSLEFSGVSVAYpGRRPALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSIAVNGVPLAdaDADSWRD 396
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 85 vcpRIAWMPQGLGknLYHTlSVYENVdffaRLFGHDKAEREVRinELLTSTGLAPF-RDRPAG----------KLSGGMK 153
Cdd:TIGR02857 397 ---QIAWVPQHPF--LFAG-TIAENI----RLARPDASDAEIR--EALERAGLDEFvAALPQGldtpigeggaGLSGGQA 464
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 732682709 154 QKLGLCCALIHDPELLILDEPTTGVDPLSRSQfwdLIDSIRQRQSNMSVLVATAYMEEAERFDWLVAM 221
Cdd:TIGR02857 465 QRLALARAFLRDAPLLLLDEPTAHLDAETEAE---VLEALRALAQGRTVLLVTHRLALAALADRIVVL 529
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
18-206 |
3.20e-23 |
|
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: 98.63 E-value: 3.20e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 18 VSQHY-GKTVALNNITLDIPARCMVGLIGPDGVGKSSLLSLISGARVIEQGNVMVLGGDMRDPKHRRdvcprIAWMPQGL 96
Cdd:cd03292 6 VTKTYpNGTAALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQDVSDLRGRA-----IPYLRRKI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 97 G------KNLYHtLSVYENVDFFARLFGHDKAEREVRINELLTSTGLAPFRDRPAGKLSGGMKQKLGLCCALIHDPELLI 170
Cdd:cd03292 81 GvvfqdfRLLPD-RNVYENVAFALEVTGVPPREIRKRVPAALELVGLSHKHRALPAELSGGEQQRVAIARAIVNSPTILI 159
|
170 180 190
....*....|....*....|....*....|....*.
gi 732682709 171 LDEPTTGVDPLSRSQFWDLIDSIRQRqsNMSVLVAT 206
Cdd:cd03292 160 ADEPTGNLDPDTTWEIMNLLKKINKA--GTTVVVAT 193
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
25-238 |
5.52e-23 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 99.78 E-value: 5.52e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 25 TVALNNITLDIPARCMVGLIGPDGVGKSSLLSLISGARVIEQGNVMVLGGDMRDPKHRRDVCPRIAWMPQGLGKNLYHTL 104
Cdd:PRK13633 23 KLALDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVYVDGLDTSDEENLWDIRNKAGMVFQNPDNQIVATI 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 105 sVYENVDFFARLFGHDKAEREVRINELLTSTGLAPFRDRPAGKLSGGMKQKLGLCCALIHDPELLILDEPTTGVDPLSRS 184
Cdd:PRK13633 103 -VEEDVAFGPENLGIPPEEIRERVDESLKKVGMYEYRRHAPHLLSGGQKQRVAIAGILAMRPECIIFDEPTAMLDPSGRR 181
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 732682709 185 QFWDLIDSIrQRQSNMSVLVATAYMEEAERFDWLVAMNAGEVLATGSAEELRQQ 238
Cdd:PRK13633 182 EVVNTIKEL-NKKYGITIILITHYMEEAVEADRIIVMDSGKVVMEGTPKEIFKE 234
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
277-500 |
7.88e-23 |
|
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: 98.07 E-value: 7.88e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 277 IEARDLTMRFGS--FVAVDHVNFRIPRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGEAWLFGqpVDPKDI---DTRRRV 351
Cdd:cd03251 1 VEFKNVTFRYPGdgPPVLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDG--HDVRDYtlaSLRRQI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 352 GYMSQAFSLYNElTVRQNLelharLFHIPEAEiPARVAEMSERFKLNDVEDILPE-----------SLPLGIRQRLSLAV 420
Cdd:cd03251 79 GLVSQDVFLFND-TVAENI-----AYGRPGAT-REEVEEAARAANAHEFIMELPEgydtvigergvKLSGGQRQRIAIAR 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 421 AVIHRPEMLILDEPTSGVDPVARDMFWQLMVDLSrQDKVTIFIStHFMNEAERCDRISLMHAGKVLASGTPQELVEKRGA 500
Cdd:cd03251 152 ALLKDPPILILDEATSALDTESERLVQAALERLM-KNRTTFVIA-HRLSTIENADRIVVLEDGKIVERGTHEELLAQGGV 229
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
22-235 |
8.05e-23 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 98.83 E-value: 8.05e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 22 YGKTVALNNITLDIPARCMVGLIGPDGVGKSSLLSLISgaRVIE-------QGNVMVLGGD---MRDPKHRRDVcPRIAW 91
Cdd:PRK14247 13 FGQVEVLDGVNLEIPDNTITALMGPSGSGKSTLLRVFN--RLIElypearvSGEVYLDGQDifkMDVIELRRRV-QMVFQ 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 92 MPqglgkNLYHTLSVYENVDFFARL--FGHDKAEREVRINELLTSTGL-APFRDR---PAGKLSGGMKQKLGLCCALIHD 165
Cdd:PRK14247 90 IP-----NPIPNLSIFENVALGLKLnrLVKSKKELQERVRWALEKAQLwDEVKDRldaPAGKLSGGQQQRLCIARALAFQ 164
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 732682709 166 PELLILDEPTTGVDPLSRSQFWDLIDSIRQrqsNMSVLVATAYMEEAERF-DWLVAMNAGEVLATGSAEEL 235
Cdd:PRK14247 165 PEVLLADEPTANLDPENTAKIESLFLELKK---DMTIVLVTHFPQQAARIsDYVAFLYKGQIVEWGPTREV 232
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
120-443 |
9.95e-23 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 102.79 E-value: 9.95e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 120 DKAEREVRINELLTSTGLAPFRDRPAGKLSGGMKQKLGLCCALIHDPELLILDEPTTGVDPLSRSQFWDLIDSIRQRQSN 199
Cdd:PRK10938 108 DEVKDPARCEQLAQQFGITALLDRRFKYLSTGETRKTLLCQALMSEPDLLILDEPFDGLDVASRQQLAELLASLHQSGIT 187
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 200 MsVLVATaymeeaeRFDWL--VAMNAGeVLA------TGSAEELRQQTQSATL--EEAFINL-LPQAQR-QAHQAvvIPP 267
Cdd:PRK10938 188 L-VLVLN-------RFDEIpdFVQFAG-VLAdctlaeTGEREEILQQALVAQLahSEQLEGVqLPEPDEpSARHA--LPA 256
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 268 YQPEnaeiaIEARDLTMRFGSFVAVDHVNFRIPRGEIFGFLGSNGCGKSTTMKMLTGLLPAS-EGEAWLFGQPVDPKDI- 345
Cdd:PRK10938 257 NEPR-----IVLNNGVVSYNDRPILHNLSWQVNPGEHWQIVGPNGAGKSTLLSLITGDHPQGySNDLTLFGRRRGSGETi 331
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 346 -DTRRRVGYMSQAFSL----------------------YNELTVRQNL---ELHARLfhipeaEIPARVAEMSERfklnd 399
Cdd:PRK10938 332 wDIKKHIGYVSSSLHLdyrvstsvrnvilsgffdsigiYQAVSDRQQKlaqQWLDIL------GIDKRTADAPFH----- 400
|
330 340 350 360
....*....|....*....|....*....|....*....|....*
gi 732682709 400 vedilpeSLPLGiRQRLSLAV-AVIHRPEMLILDEPTSGVDPVAR 443
Cdd:PRK10938 401 -------SLSWG-QQRLALIVrALVKHPTLLILDEPLQGLDPLNR 437
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
276-490 |
1.59e-22 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 97.39 E-value: 1.59e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 276 AIEARDLTMRFGSFVAVDHVNFRIPRGEIFGFLGSNGCGKSTTMKMLTGL-LPAS-----EGEAWLFGQPVDPKDI-DTR 348
Cdd:PRK11124 2 SIQLNGINCFYGAHQALFDITLDCPQGETLVLLGPSGAGKSSLLRVLNLLeMPRSgtlniAGNHFDFSKTPSDKAIrELR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 349 RRVGYMSQAFSLYNELTVRQNL-ELHARLFHIPEAEIPARVAEMSERFKLNDVEDILPESLPLGIRQRLSLAVAVIHRPE 427
Cdd:PRK11124 82 RNVGMVFQQYNLWPHLTVQQNLiEAPCRVLGLSKDQALARAEKLLERLRLKPYADRFPLHLSGGQQQRVAIARALMMEPQ 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 732682709 428 MLILDEPTSGVDPVARDMFWQLMVDLSrQDKVTIFISTHFMNEAER-CDRISLMHAGKVLASGT 490
Cdd:PRK11124 162 VLLFDEPTAALDPEITAQIVSIIRELA-ETGITQVIVTHEVEVARKtASRVVYMENGHIVEQGD 224
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
33-230 |
1.93e-22 |
|
ATP-binding cassette domain of the thiamine transport system; Part of the binding-protein-dependent transport system tbpA-thiPQ for thiamine and TPP. Probably responsible for the translocation of thiamine across the membrane. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213265 [Multi-domain] Cd Length: 211 Bit Score: 96.41 E-value: 1.93e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 33 LDIPARCMVGLIGPDGVGKSSLLSLISGARVIEQGNVMVLGGDMRD-PKHRRDVcpriAWMPQGlgKNLYHTLSVYENVD 111
Cdd:cd03298 19 LTFAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLINGVDVTAaPPADRPV----SMLFQE--NNLFAHLTVEQNVG 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 112 FFARLFGHDKAEREVRINELLTSTGLAPFRDRPAGKLSGGMKQKLGLCCALIHDPELLILDEPTTGVDPLSRSQFWDLID 191
Cdd:cd03298 93 LGLSPGLKLTAEDRQAIEVALARVGLAGLEKRLPGELSGGERQRVALARVLVRDKPVLLLDEPFAALDPALRAEMLDLVL 172
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 732682709 192 SIRqRQSNMSVLVATAYMEEAER-FDWLVAMNAGEVLATG 230
Cdd:cd03298 173 DLH-AETKMTVLMVTHQPEDAKRlAQRVVFLDNGRIAAQG 211
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
280-494 |
3.01e-22 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 99.72 E-value: 3.01e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 280 RDLTMRFGSFVAVDHVNFRIPRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGEAWLFGQ---PVDPKDidtrRRVGYMSQ 356
Cdd:PRK11000 7 RNVTKAYGDVVISKDINLDIHEGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLFIGEKrmnDVPPAE----RGVGMVFQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 357 AFSLYNELTVRQNLELHARLFHIPEAEIPARVAEMSERFKLNDVEDILPESLPLGIRQRLSLAVAVIHRPEMLILDEPTS 436
Cdd:PRK11000 83 SYALYPHLSVAENMSFGLKLAGAKKEEINQRVNQVAEVLQLAHLLDRKPKALSGGQRQRVAIGRTLVAEPSVFLLDEPLS 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 732682709 437 GVDPVARdmfWQLMVDLSRQDK---VTIFISTHFMNEA-ERCDRISLMHAGKVLASGTPQEL 494
Cdd:PRK11000 163 NLDAALR---VQMRIEISRLHKrlgRTMIYVTHDQVEAmTLADKIVVLDAGRVAQVGKPLEL 221
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
25-245 |
3.03e-22 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 97.50 E-value: 3.03e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 25 TVALNNITLDIPARCMVGLIGPDGVGKSSLLSLISGARVIEQGNVMVLGGDMrDPKHRRDVCPRIAWMPQGLGKNLYhTL 104
Cdd:PRK13647 18 TKALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGREV-NAENEKWVRSKVGLVFQDPDDQVF-SS 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 105 SVYENVDFFARLFGHDKAEREVRINELLTSTGLAPFRDRPAGKLSGGMKQKLGLCCALIHDPELLILDEPTTGVDPLSRS 184
Cdd:PRK13647 96 TVWDDVAFGPVNMGLDKDEVERRVEEALKAVRMWDFRDKPPYHLSYGQKKRVAIAGVLAMDPDVIVLDEPMAYLDPRGQE 175
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 732682709 185 QFWDLIDSIRQRQSnmSVLVATAYME-EAERFDWLVAMNAGEVLATGSAEEL--RQQTQSATLE 245
Cdd:PRK13647 176 TLMEILDRLHNQGK--TVIVATHDVDlAAEWADQVIVLKEGRVLAEGDKSLLtdEDIVEQAGLR 237
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
275-480 |
3.46e-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: 101.59 E-value: 3.46e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 275 IAIEARDLTMRF-GSFVAVDHVNFRIPRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGEAWLFGQPVDPKDIDT-RRRVG 352
Cdd:TIGR02857 320 SSLEFSGVSVAYpGRRPALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSIAVNGVPLADADADSwRDQIA 399
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 353 YMSQAFSLYNElTVRQNLeLHARlfhiPEAEiPARVAEMSERFKLNDVEDILPESLPL-----------GIRQRLSLAVA 421
Cdd:TIGR02857 400 WVPQHPFLFAG-TIAENI-RLAR----PDAS-DAEIREALERAGLDEFVAALPQGLDTpigeggaglsgGQAQRLALARA 472
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 732682709 422 VIHRPEMLILDEPTSGVDPVARDMFWQLMVDLSRqdKVTIFISTHFMNEAERCDRISLM 480
Cdd:TIGR02857 473 FLRDAPLLLLDEPTAHLDAETEAEVLEALRALAQ--GRTVLLVTHRLALAALADRIVVL 529
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
277-510 |
4.79e-22 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 99.53 E-value: 4.79e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 277 IEARDLTMRFGSFVAVDHVNFRIPRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGEAWLFGQPVDPKDIDT-RRRVGYMS 355
Cdd:PRK09536 4 IDVSDLSVEFGDTTVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGDDVEALSARAaSRRVASVP 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 356 QAFSLYNELTVRQNLEL----HARLFHIPEAEIPARVAEMSERFKLNDVEDILPESLPLGIRQRLSLAVAVIHRPEMLIL 431
Cdd:PRK09536 84 QDTSLSFEFDVRQVVEMgrtpHRSRFDTWTETDRAAVERAMERTGVAQFADRPVTSLSGGERQRVLLARALAQATPVLLL 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 432 DEPTSGVDPVARDMFWQLMVDLSRQDKvTIFISTHFMNEAER-CDRISLMHAGKVLASGTPQELVEkrgAASLEEAFIAY 510
Cdd:PRK09536 164 DEPTASLDINHQVRTLELVRRLVDDGK-TAVAAIHDLDLAARyCDELVLLADGRVRAAGPPADVLT---ADTLRAAFDAR 239
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
22-238 |
4.90e-22 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 96.62 E-value: 4.90e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 22 YGKTVALNNITLDIPARCMVGLIGPDGVGKSSLLSLISGARVIEQGNVMVLGGDMRDPKHRRdVCPRIAWMPQglgknlY 101
Cdd:PRK11231 12 YGTKRILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDKPISMLSSRQ-LARRLALLPQ------H 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 102 HT----LSVYENV--------DFFARLFGHDKAerevRINELLTSTGLAPFRDRPAGKLSGGMKQKLGLCCALIHDPELL 169
Cdd:PRK11231 85 HLtpegITVRELVaygrspwlSLWGRLSAEDNA----RVNQAMEQTRINHLADRRLTDLSGGQRQRAFLAMVLAQDTPVV 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 732682709 170 ILDEPTTGVDpLSRSQfwDLIDSIRQRQSNMSVLVATAY-MEEAERF-DWLVAMNAGEVLATGSAEELRQQ 238
Cdd:PRK11231 161 LLDEPTTYLD-INHQV--ELMRLMRELNTQGKTVVTVLHdLNQASRYcDHLVVLANGHVMAQGTPEEVMTP 228
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
277-500 |
5.51e-22 |
|
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: 95.76 E-value: 5.51e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 277 IEARDLTMRFG-SFVAVDHVNFRIPRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGEAWLFGQPVDPKDIDT-RRRVGYM 354
Cdd:cd03253 1 IEFENVTFAYDpGRPVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDGQDIREVTLDSlRRAIGVV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 355 SQAFSLYNElTVRQNLE---LHARLFHIPEAEIPARVAEMSERFKlNDVEDILPE---SLPLGIRQRLSLAVAVIHRPEM 428
Cdd:cd03253 81 PQDTVLFND-TIGYNIRygrPDATDEEVIEAAKAAQIHDKIMRFP-DGYDTIVGErglKLSGGEKQRVAIARAILKNPPI 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 732682709 429 LILDEPTSGVDPVARDMFWQLMVDLSRqDKVTIFIsTHFMNEAERCDRISLMHAGKVLASGTPQELVEKRGA 500
Cdd:cd03253 159 LLLDEATSALDTHTEREIQAALRDVSK-GRTTIVI-AHRLSTIVNADKIIVLKDGRIVERGTHEELLAKGGL 228
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
282-495 |
6.63e-22 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 96.21 E-value: 6.63e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 282 LTMRFGSFVAVDHVNFRIPRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGEAWLFGQPVDP-KDIDTRRRVGYMSQAFSL 360
Cdd:PRK10253 13 LTLGYGKYTVAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIQHyASKEVARRIGLLAQNATT 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 361 YNELTVrQNLELHARLFHIP-----EAEIPARVAEMSERFKLNDVEDILPESLPLGIRQRLSLAVAVIHRPEMLILDEPT 435
Cdd:PRK10253 93 PGDITV-QELVARGRYPHQPlftrwRKEDEEAVTKAMQATGITHLADQSVDTLSGGQRQRAWIAMVLAQETAIMLLDEPT 171
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 732682709 436 SGVDPVARDMFWQLMVDLSRQDKVTIFISTHFMNEAER-CDRISLMHAGKVLASGTPQELV 495
Cdd:PRK10253 172 TWLDISHQIDLLELLSELNREKGYTLAAVLHDLNQACRyASHLIALREGKIVAQGAPKEIV 232
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
295-476 |
6.71e-22 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 95.23 E-value: 6.71e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 295 VNFRIPRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGEAWLFGQPVDPKDIDTR-----RRVGYMSQAFSLYNELTVRQN 369
Cdd:PRK10584 29 VELVVKRGETIALIGESGSGKSTLLAILAGLDDGSSGEVSLVGQPLHQMDEEARaklraKHVGFVFQSFMLIPTLNALEN 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 370 LELHARLFHIPEAEIPARVAEMSERFKLNDVEDILPESLPLGIRQRLSLAVAVIHRPEMLILDEPTSGVDPVARDMFWQL 449
Cdd:PRK10584 109 VELPALLRGESSRQSRNGAKALLEQLGLGKRLDHLPAQLSGGEQQRVALARAFNGRPDVLFADEPTGNLDRQTGDKIADL 188
|
170 180
....*....|....*....|....*..
gi 732682709 450 MVDLSRQDKVTIFISTHFMNEAERCDR 476
Cdd:PRK10584 189 LFSLNREHGTTLILVTHDLQLAARCDR 215
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
272-496 |
6.80e-22 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 96.39 E-value: 6.80e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 272 NAEIAIEARDLTMRFGSFVAVDHVNFRIPRGEIFGFLGSNGCGKSTTMK---MLTGLLPA--SEGEAWLFGQPVDPKDID 346
Cdd:PRK14243 6 GTETVLRTENLNVYYGSFLAVKNVWLDIPKNQITAFIGPSGCGKSTILRcfnRLNDLIPGfrVEGKVTFHGKNLYAPDVD 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 347 ---TRRRVGYMSQAFSLYNElTVRQNLELHARL--FHIPEAEIPARvaEMSERFKLNDVEDILPES---LPLGIRQRLSL 418
Cdd:PRK14243 86 pveVRRRIGMVFQKPNPFPK-SIYDNIAYGARIngYKGDMDELVER--SLRQAALWDEVKDKLKQSglsLSGGQQQRLCI 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 732682709 419 AVAVIHRPEMLILDEPTSGVDPVARDMFWQLMVDLSRQdkVTIFISTHFMNEAERCDRISLMHAGKVLASGTPQ-ELVE 496
Cdd:PRK14243 163 ARAIAVQPEVILMDEPCSALDPISTLRIEELMHELKEQ--YTIIIVTHNMQQAARVSDMTAFFNVELTEGGGRYgYLVE 239
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
22-230 |
7.10e-22 |
|
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC transporter subfamily is involved in extracellular polysaccharide export. Among the variety of membrane-linked or extracellular polysaccharides excreted by bacteria, only capsular polysaccharides, lipopolysaccharides, and teichoic acids have been shown to be exported by ABC transporters. A typical system is made of a conserved integral membrane and an ABC. In addition to these proteins, capsular polysaccharide exporter systems require two 'accessory' proteins to perform their function: a periplasmic (E.coli) or a lipid-anchored outer membrane protein called OMA (Neisseria meningitidis and Haemophilus influenza) and a cytoplasmic membrane protein MPA2.
Pssm-ID: 213187 [Multi-domain] Cd Length: 224 Bit Score: 95.29 E-value: 7.10e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 22 YGKTVALNNITLDIPARCMVGLIGPDGVGKSSLLSLISGARVIEQGNVMVLGgdmrdpkhrrdvcpRIAWMPqGLGKNLY 101
Cdd:cd03220 32 VGEFWALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVTVRG--------------RVSSLL-GLGGGFN 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 102 HTLSVYENVDFFARLFGHDKAEREVRINELLTSTGLAPFRDRPAGKLSGGMKQKLGLCCALIHDPELLILDEPTTGVDPL 181
Cdd:cd03220 97 PELTGRENIYLNGRLLGLSRKEIDEKIDEIIEFSELGDFIDLPVKTYSSGMKARLAFAIATALEPDILLIDEVLAVGDAA 176
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 732682709 182 SRSQFWDLIDSIRQRQSnmSVLVATAYMEEAERF-DWLVAMNAGEVLATG 230
Cdd:cd03220 177 FQEKCQRRLRELLKQGK--TVILVSHDPSSIKRLcDRALVLEKGKIRFDG 224
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
11-195 |
1.03e-21 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 94.95 E-value: 1.03e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 11 PVAQLAGVSQHYGKTVALNNITLDIPARCMVGLIGPDGVGKSSLLSLISGARVIEQGNVMVLGGDMRDPKHRRDVCPRIA 90
Cdd:PRK11614 4 VMLSFDKVSAHYGKIQALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDGKDITDWQTAKIMREAVA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 91 WMPQglGKNLYHTLSVYENV---DFFARlfGHDKAEREVRINELLTStgLAPFRDRPAGKLSGGMKQKLGLCCALIHDPE 167
Cdd:PRK11614 84 IVPE--GRRVFSRMTVEENLamgGFFAE--RDQFQERIKWVYELFPR--LHERRIQRAGTMSGGEQQMLAIGRALMSQPR 157
|
170 180
....*....|....*....|....*...
gi 732682709 168 LLILDEPTTGVDPLSRSQFWDLIDSIRQ 195
Cdd:PRK11614 158 LLLLDEPSLGLAPIIIQQIFDTIEQLRE 185
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
292-483 |
1.03e-21 |
|
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: 94.84 E-value: 1.03e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 292 VDHVNFRIPRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGEAWLFGQPVDPKDIDtrRRVGYmsQAFSLYNELTVRQNLE 371
Cdd:TIGR01184 1 LKGVNLTIQQGEFISLIGHSGCGKSTLLNLISGLAQPTSGGVILEGKQITEPGPD--RMVVF--QNYSLLPWLTVRENIA 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 372 L--HARLFHIPEAEIPARVAEMSERFKLNDVEDILPESLPLGIRQRLSLAVAVIHRPEMLILDEPTSGVDPVARDMFWQL 449
Cdd:TIGR01184 77 LavDRVLPDLSKSERRAIVEEHIALVGLTEAADKRPGQLSGGMKQRVAIARALSIRPKVLLLDEPFGALDALTRGNLQEE 156
|
170 180 190
....*....|....*....|....*....|....*
gi 732682709 450 MVDLSRQDKVTIFISTHFMNEAE-RCDRISLMHAG 483
Cdd:TIGR01184 157 LMQIWEEHRVTVLMVTHDVDEALlLSDRVVMLTNG 191
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
12-439 |
1.06e-21 |
|
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: 100.01 E-value: 1.06e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 12 VAQLAGVSQHY-GKTVALNNITLDIPARCMVGLIGPDGVGKSSLLSLISGARVIEQGNVMVLGGdmrdpkhrrdvcPRIA 90
Cdd:TIGR03719 4 IYTMNRVSKVVpPKKEILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKDFNGEARPQPG------------IKVG 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 91 WMPQGlgKNLYHTLSVYENV--------DFFARL------FG-----HDK-AEREVRINELLTSTGL------------- 137
Cdd:TIGR03719 72 YLPQE--PQLDPTKTVRENVeegvaeikDALDRFneisakYAepdadFDKlAAEQAELQEIIDAADAwdldsqleiamda 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 138 --APFRDRPAGKLSGGMKQKLGLCCALIHDPELLILDEPTTGVDplSRSQFWdlIDSIRQRQSNMSVLV---------AT 206
Cdd:TIGR03719 150 lrCPPWDADVTKLSGGERRRVALCRLLLSKPDMLLLDEPTNHLD--AESVAW--LERHLQEYPGTVVAVthdryfldnVA 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 207 AYMEEAER----------FDWLVAMNagEVLAT-GSAEELRQQTQSATLE-----------------EAFINLLPQA--Q 256
Cdd:TIGR03719 226 GWILELDRgrgipwegnySSWLEQKQ--KRLEQeEKEESARQKTLKRELEwvrqspkgrqakskarlARYEELLSQEfqK 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 257 RQAHQAVVIPPyQPENAEIAIEARDLTMRFGSFVAVDHVNFRIPRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGEAwLF 336
Cdd:TIGR03719 304 RNETAEIYIPP-GPRLGDKVIEAENLTKAFGDKLLIDDLSFKLPPGGIVGVIGPNGAGKSTLFRMITGQEQPDSGTI-EI 381
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 337 GQPVdpkdidtrrRVGYMSQAF-SLYNELTVRQNLELHARLFHIPEAEIPARVAEMSERFKLNDVEDILPEsLPLGIRQR 415
Cdd:TIGR03719 382 GETV---------KLAYVDQSRdALDPNKTVWEEISGGLDIIKLGKREIPSRAYVGRFNFKGSDQQKKVGQ-LSGGERNR 451
|
490 500
....*....|....*....|....
gi 732682709 416 LSLAVAVIHRPEMLILDEPTSGVD 439
Cdd:TIGR03719 452 VHLAKTLKSGGNVLLLDEPTNDLD 475
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
287-495 |
1.13e-21 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 98.57 E-value: 1.13e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 287 GSFVAVDHVNFRIPRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGEAWLFGqpVDPKDIDT-------RRRVGYMSQAFS 359
Cdd:PRK10070 39 GLSLGVKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDG--VDIAKISDaelrevrRKKIAMVFQSFA 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 360 LYNELTVRQNLELHARLFHIPEAEIPARVAEMSERFKLNDVEDILPESLPLGIRQRLSLAVAVIHRPEMLILDEPTSGVD 439
Cdd:PRK10070 117 LMPHMTVLDNTAFGMELAGINAEERREKALDALRQVGLENYAHSYPDELSGGMRQRVGLARALAINPDILLMDEAFSALD 196
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 732682709 440 PVARDMFWQLMVDLSRQDKVTIFISTHFMNEAERC-DRISLMHAGKVLASGTPQELV 495
Cdd:PRK10070 197 PLIRTEMQDELVKLQAKHQRTIVFISHDLDEAMRIgDRIAIMQNGEVVQVGTPDEIL 253
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
280-477 |
1.16e-21 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 94.09 E-value: 1.16e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 280 RDLTMRFGSFVAVDHVNFRIPRGEIFGFLGSNGCGKSTTMKMLTGLLPA---SEGEAWLFGQPVDPKDIDtRRRVGYMSQ 356
Cdd:COG4136 5 ENLTITLGGRPLLAPLSLTVAPGEILTLMGPSGSGKSTLLAAIAGTLSPafsASGEVLLNGRRLTALPAE-QRRIGILFQ 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 357 AFSLYNELTVRQNLelharLFHIPE----AEIPARVAEMSERFKLNDVEDILPESLPLGIRQRLSLAVAVIHRPEMLILD 432
Cdd:COG4136 84 DDLLFPHLSVGENL-----AFALPPtigrAQRRARVEQALEEAGLAGFADRDPATLSGGQRARVALLRALLAEPRALLLD 158
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 732682709 433 EPTSGVDPVARDMFWQLMVDLSRQDKVTIFISTHFMNEAERCDRI 477
Cdd:COG4136 159 EPFSKLDAALRAQFREFVFEQIRQRGIPALLVTHDEEDAPAAGRV 203
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
268-496 |
1.23e-21 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 95.62 E-value: 1.23e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 268 YQPENAEIAIEARDLTMRFGSFVAVDHVNFRIPRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGEAWLFGQPVDPKDIDT 347
Cdd:PRK10575 3 EYTNHSDTTFALRNVSFRVPGRTLLHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPLESWSSKA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 348 -RRRVGYMSQAFSLYNELTVRQNLEL-----HARLFHIpEAEIPARVAEMSERFKLNDVEDILPESLPLGIRQRLSLAVA 421
Cdd:PRK10575 83 fARKVAYLPQQLPAAEGMTVRELVAIgrypwHGALGRF-GAADREKVEEAISLVGLKPLAHRLVDSLSGGERQRAWIAML 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 732682709 422 VIHRPEMLILDEPTSGVDPVARDMFWQLMVDLSRQDKVTIFISTHFMNEAER-CDRISLMHAGKVLASGTPQELVE 496
Cdd:PRK10575 162 VAQDSRCLLLDEPTSALDIAHQVDVLALVHRLSQERGLTVIAVLHDINMAARyCDYLVALRGGEMIAQGTPAELMR 237
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
14-242 |
1.24e-21 |
|
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440743 [Multi-domain] Cd Length: 239 Bit Score: 94.68 E-value: 1.24e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 14 QLAGVSQHYGKTVALNNITLDIPARCMVGLIGPDGVGKSSLLSLISGARVIEQGNVMVLGGDMRDP-KHRRDVCPRIAWM 92
Cdd:COG1126 3 EIENLHKSFGDLEVLKGISLDVEKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTITVDGEDLTDSkKDINKLRRKVGMV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 93 PQGLgkNLYHTLSVYENVdFFA--RLFGHDKAEREVRINELLTSTGLAPFRDRPAGKLSGGMKQKLGLCCALIHDPELLI 170
Cdd:COG1126 83 FQQF--NLFPHLTVLENV-TLApiKVKKMSKAEAEERAMELLERVGLADKADAYPAQLSGGQQQRVAIARALAMEPKVML 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 732682709 171 LDEPTTGVDP-LSRsqfwDLIDSIRQ-RQSNMSVLVATAYMEEAER-FDWLVAMNAGEVLATGSAEELRQQTQSA 242
Cdd:COG1126 160 FDEPTSALDPeLVG----EVLDVMRDlAKEGMTMVVVTHEMGFAREvADRVVFMDGGRIVEEGPPEEFFENPQHE 230
|
|
| LolD_lipo_ex |
TIGR02211 |
lipoprotein releasing system, ATP-binding protein; This model represents LolD, a member of the ... |
277-485 |
1.40e-21 |
|
lipoprotein releasing system, ATP-binding protein; This model represents LolD, a member of the ABC transporter family (pfam00005). LolD is involved in localization of lipoproteins in some bacteria. It works with a transmembrane protein LolC, which in some species is a paralogous pair LolC and LolE. Depending on whether the residue immediately following the new, modified N-terminal Cys residue, the nascent lipoprotein may be carried further by LolA and LolB to the outer membrane, or remain at the inner membrane. The top scoring proteins excluded by this model include homologs from the archaeal genus Methanosarcina. [Protein fate, Protein and peptide secretion and trafficking]
Pssm-ID: 131266 [Multi-domain] Cd Length: 221 Bit Score: 94.34 E-value: 1.40e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 277 IEARDLTMRF--GSF--VAVDHVNFRIPRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGEAWLFGQPV----DPKDIDTR 348
Cdd:TIGR02211 2 LKCENLGKRYqeGKLdtRVLKGVSLSIGKGEIVAIVGSSGSGKSTLLHLLGGLDNPTSGEVLFNGQSLsklsSNERAKLR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 349 -RRVGYMSQAFSLYNELTVRQNLELHARLFHIPEAEIPARVAEMSERFKLNDVEDILPESLPLGIRQRLSLAVAVIHRPE 427
Cdd:TIGR02211 82 nKKLGFIYQFHHLLPDFTALENVAMPLLIGKKSVKEAKERAYEMLEKVGLEHRINHRPSELSGGERQRVAIARALVNQPS 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 732682709 428 MLILDEPTSGVDPVARDMFWQLMVDLSRQDKVTIFISTHFMNEAERCDRISLMHAGKV 485
Cdd:TIGR02211 162 LVLADEPTGNLDNNNAKIIFDLMLELNRELNTSFLVVTHDLELAKKLDRVLEMKDGQL 219
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
282-502 |
1.61e-21 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 94.26 E-value: 1.61e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 282 LTMRFgsfvavdhvNFRIPRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGEAWLFGQP---VDPkdidTRRRVGYMSQAF 358
Cdd:PRK10771 14 LPMRF---------DLTVERGERVAILGPSGAGKSTLLNLIAGFLTPASGSLTLNGQDhttTPP----SRRPVSMLFQEN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 359 SLYNELTVRQN--LELHA--RLfhipEAEIPARVAEMSERFKLNDVEDILPESLPLGIRQRLSLAVAVIHRPEMLILDEP 434
Cdd:PRK10771 81 NLFSHLTVAQNigLGLNPglKL----NAAQREKLHAIARQMGIEDLLARLPGQLSGGQRQRVALARCLVREQPILLLDEP 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 732682709 435 TSGVDPVARDMFWQLMVDLSRQDKVTIFISTHFMNEAER-CDRISLMHAGKVLASGTPQELVEKRGAAS 502
Cdd:PRK10771 157 FSALDPALRQEMLTLVSQVCQERQLTLLMVSHSLEDAARiAPRSLVVADGRIAWDGPTDELLSGKASAS 225
|
|
| anch_rpt_ABC |
TIGR03771 |
anchored repeat-type ABC transporter, ATP-binding subunit; This protein family is the ... |
297-494 |
1.76e-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: 94.15 E-value: 1.76e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 297 FRIPRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGEAWLFGQPVDPKdidtRRRVGYMSQ--AFSLYNELTVRQNLeLHA 374
Cdd:TIGR03771 1 LSADKGELLGLLGPNGAGKTTLLRAILGLIPPAKGTVKVAGASPGKG----WRHIGYVPQrhEFAWDFPISVAHTV-MSG 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 375 RLFHI-----PEAEIPARVAEMSERFKLNDVEDILPESLPLGIRQRLSLAVAVIHRPEMLILDEPTSGVDPVARDMFWQL 449
Cdd:TIGR03771 76 RTGHIgwlrrPCVADFAAVRDALRRVGLTELADRPVGELSGGQRQRVLVARALATRPSVLLLDEPFTGLDMPTQELLTEL 155
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 732682709 450 MVDLSrQDKVTIFISTHFMNEA-ERCDRISLMHaGKVLASGTPQEL 494
Cdd:TIGR03771 156 FIELA-GAGTAILMTTHDLAQAmATCDRVVLLN-GRVIADGTPQQL 199
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
31-235 |
1.76e-21 |
|
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding cassette (ABC) protein of the three subunit molybdate ABC transporter. The three proteins of this complex are homologous to proteins of the sulfate ABC transporter. Molybdenum may be used in nitrogenases of nitrogen-fixing bacteria and in molybdopterin cofactors. In some cases, molybdate may be transported by a sulfate transporter rather than by a specific molybdate transporter. [Transport and binding proteins, Anions]
Pssm-ID: 131197 [Multi-domain] Cd Length: 354 Bit Score: 97.10 E-value: 1.76e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 31 ITLDIPARCMVGLIGPDGVGKSSLLSLISGARVIEQGNVMVLGGDMRD-------PKHRRdvcpRIAWMPQGlgKNLYHT 103
Cdd:TIGR02142 16 ADFTLPGQGVTAIFGRSGSGKTTLIRLIAGLTRPDEGEIVLNGRTLFDsrkgiflPPEKR----RIGYVFQE--ARLFPH 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 104 LSVYENVDF-FARLFGHDKAEREVRINELLtstGLAPFRDRPAGKLSGGMKQKLGLCCALIHDPELLILDEPTTGVDPLS 182
Cdd:TIGR02142 90 LSVRGNLRYgMKRARPSERRISFERVIELL---GIGHLLGRLPGRLSGGEKQRVAIGRALLSSPRLLLMDEPLAALDDPR 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 732682709 183 RSQFWDLIDSIRQrQSNMSVLVATAYMEEAERF-DWLVAMNAGEVLATGSAEEL 235
Cdd:TIGR02142 167 KYEILPYLERLHA-EFGIPILYVSHSLQEVLRLaDRVVVLEDGRVAAAGPIAEV 219
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
25-254 |
1.82e-21 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 95.50 E-value: 1.82e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 25 TVALNNITLDIPARCMVGLIGPDGVGKSSLLSLISGARVIEQGNVMVLGGDMRDPKHR-RDVCPRIAWMPQGLGKNLYHT 103
Cdd:PRK13637 20 KKALDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDGVDITDKKVKlSDIRKKVGLVFQYPEYQLFEE 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 104 lSVYENVDFFARLFGHDKAEREVRINELLTSTGLA--PFRDRPAGKLSGGMKQKLGLCCALIHDPELLILDEPTTGVDPL 181
Cdd:PRK13637 100 -TIEKDIAFGPINLGLSEEEIENRVKRAMNIVGLDyeDYKDKSPFELSGGQKRRVAIAGVVAMEPKILILDEPTAGLDPK 178
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 732682709 182 SRSQFWDLIDSIrQRQSNMSVLVATAYMEEAERF-DWLVAMNAGEVLATGSAEELRQQTQsaTLEEafINL-LPQ 254
Cdd:PRK13637 179 GRDEILNKIKEL-HKEYNMTIILVSHSMEDVAKLaDRIIVMNKGKCELQGTPREVFKEVE--TLES--IGLaVPQ 248
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
10-234 |
1.94e-21 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 97.33 E-value: 1.94e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 10 PPVAQLAGVSQHYGKTVALNNITLDIPARCMVGLIGPDGVGKSSLLSLISGARVIEQGNVMVLGGDMRD-PKHRRDVcpr 88
Cdd:PRK09452 12 SPLVELRGISKSFDGKEVISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLDGQDITHvPAENRHV--- 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 89 iawmpqglgkN-------LYHTLSVYENVDFFARLFGHDKAEREVRINELLTSTGLAPFRDRPAGKLSGGMKQKLGLCCA 161
Cdd:PRK09452 89 ----------NtvfqsyaLFPHMTVFENVAFGLRMQKTPAAEITPRVMEALRMVQLEEFAQRKPHQLSGGQQQRVAIARA 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 732682709 162 LIHDPELLILDEPTTGVDPLSRSQFWDLIDSIrQRQSNMSVLVATAYMEEAERF-DWLVAMNAGEVLATGSAEE 234
Cdd:PRK09452 159 VVNKPKVLLLDESLSALDYKLRKQMQNELKAL-QRKLGITFVFVTHDQEEALTMsDRIVVMRDGRIEQDGTPRE 231
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
14-226 |
1.94e-21 |
|
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: 93.36 E-value: 1.94e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 14 QLAGVSQHYGKTVALNNITLDIPARCMVGLIGPDGVGKSSLLSLISGARVIEQGNVMVLGGDMRDPKhrrdvcPRIAWMP 93
Cdd:cd03262 2 EIKNLHKSFGDFHVLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIDGLKLTDDK------KNINELR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 94 QGLGK-----NLYHTLSVYENVDFFAR-LFGHDKAEREVRINELLTSTGLAPFRDRPAGKLSGGMKQKLGLCCALIHDPE 167
Cdd:cd03262 76 QKVGMvfqqfNLFPHLTVLENITLAPIkVKGMSKAEAEERALELLEKVGLADKADAYPAQLSGGQQQRVAIARALAMNPK 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 732682709 168 LLILDEPTTGVDP-LSRsqfwDLIDSIRQ-RQSNMSVLVATAYMEEA-ERFDWLVAMNAGEV 226
Cdd:cd03262 156 VMLFDEPTSALDPeLVG----EVLDVMKDlAEEGMTMVVVTHEMGFArEVADRVIFMDDGRI 213
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
15-235 |
1.97e-21 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 97.02 E-value: 1.97e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 15 LAGVSQHYGKTVALNNITLDIPARCMVGLIGPDGVGKSSLLSLISGARVIEQGNVMVLGGDMRD--PKHRrdvcpriawm 92
Cdd:PRK11000 6 LRNVTKAYGDVVISKDINLDIHEGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLFIGEKRMNDvpPAER---------- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 93 pqGLGK-----NLYHTLSVYENVDFFARLFGHDKAEREVRINELLTSTGLAPFRDRPAGKLSGGMKQKLGLCCALIHDPE 167
Cdd:PRK11000 76 --GVGMvfqsyALYPHLSVAENMSFGLKLAGAKKEEINQRVNQVAEVLQLAHLLDRKPKALSGGQRQRVAIGRTLVAEPS 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 732682709 168 LLILDEPTTGVDPLSRSQFWDLIDSIRQR-QSNMsVLVATAYMEEAERFDWLVAMNAGEVLATGSAEEL 235
Cdd:PRK11000 154 VFLLDEPLSNLDAALRVQMRIEISRLHKRlGRTM-IYVTHDQVEAMTLADKIVVLDAGRVAQVGKPLEL 221
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
277-493 |
2.37e-21 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 94.31 E-value: 2.37e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 277 IEARDLTMRFGSFVAVDHVNFRIPRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGEAWLFGQP----------------- 339
Cdd:PRK11231 3 LRTENLTVGYGTKRILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDKPismlssrqlarrlallp 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 340 ---VDPKDIDTRRRVGY-MSQAFSLYNELTVRQNlelharlfhipeaeipARVAEMSERFKLNDVEDILPESLPLGIRQR 415
Cdd:PRK11231 83 qhhLTPEGITVRELVAYgRSPWLSLWGRLSAEDN----------------ARVNQAMEQTRINHLADRRLTDLSGGQRQR 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 732682709 416 LSLAVAVIHRPEMLILDEPTSGVDPVARDMFWQLMVDLSRQDKvTIFISTHFMNEAER-CDRISLMHAGKVLASGTPQE 493
Cdd:PRK11231 147 AFLAMVLAQDTPVVLLDEPTTYLDINHQVELMRLMRELNTQGK-TVVTVLHDLNQASRyCDHLVVLANGHVMAQGTPEE 224
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
30-235 |
2.53e-21 |
|
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: 96.71 E-value: 2.53e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 30 NITLDIPARCMVGLIGPDGVGKSSLLSLISGARVIEQGNVMVLGGDMRD-------PKHRRdvcpRIAWMPQGlgKNLYH 102
Cdd:COG4148 17 DVDFTLPGRGVTALFGPSGSGKTTLLRAIAGLERPDSGRIRLGGEVLQDsargiflPPHRR----RIGYVFQE--ARLFP 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 103 TLSVYENVdffarLFGH---DKAEREVRINELLTSTGLAPFRDRPAGKLSGGMKQKLGLCCALIHDPELLILDEPTTGVD 179
Cdd:COG4148 91 HLSVRGNL-----LYGRkraPRAERRISFDEVVELLGIGHLLDRRPATLSGGERQRVAIGRALLSSPRLLLMDEPLAALD 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 732682709 180 PLSRSQFWDLIDSIRqRQSNMSVLVATAYMEEAERF-DWLVAMNAGEVLATGSAEEL 235
Cdd:COG4148 166 LARKAEILPYLERLR-DELDIPILYVSHSLDEVARLaDHVVLLEQGRVVASGPLAEV 221
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
22-216 |
2.66e-21 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 92.30 E-value: 2.66e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 22 YGKTVALNNITLDIPARCMVGLIGPDGVGKSSLLSLISGARVIEQGNVMVLGGDmrdpkhrrdvcpRIAWMPQGLGKNLY 101
Cdd:NF040873 2 YGGRPVLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTVRRAGGA------------RVAYVPQRSEVPDS 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 102 HTLSVYENVD--FFAR--LFGHDKAEREVRINELLTSTGLAPFRDRPAGKLSGGMKQKLGLCCALIHDPELLILDEPTTG 177
Cdd:NF040873 70 LPLTVRDLVAmgRWARrgLWRRLTRDDRAAVDDALERVGLADLAGRQLGELSGGQRQRALLAQGLAQEADLLLLDEPTTG 149
|
170 180 190
....*....|....*....|....*....|....*....
gi 732682709 178 VDPLSRSQFWDLIDSIRQRQSnmSVLVATAYMEEAERFD 216
Cdd:NF040873 150 LDAESRERIIALLAEEHARGA--TVVVVTHDLELVRRAD 186
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
277-488 |
3.10e-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: 98.36 E-value: 3.10e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 277 IEARDLTMRFGSFVAVDHVNFRIPRGEIFGFLGSNGCGKSTTMKMLTGLLPAS--EGEAWLFGQPVDPKDI-DTRRR-VG 352
Cdd:TIGR02633 2 LEMKGIVKTFGGVKALDGIDLEVRPGECVGLCGENGAGKSTLMKILSGVYPHGtwDGEIYWSGSPLKASNIrDTERAgIV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 353 YMSQAFSLYNELTVRQNLELHARLFH----IPEAEIPARVAEMSERFKLNDVEDILPES-LPLGIRQRLSLAVAVIHRPE 427
Cdd:TIGR02633 82 IIHQELTLVPELSVAENIFLGNEITLpggrMAYNAMYLRAKNLLRELQLDADNVTRPVGdYGGGQQQLVEIAKALNKQAR 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 732682709 428 MLILDEPTSGVDPVARDMFWQLMVDLSRQDKVTIFIStHFMNEAER-CDRISLMHAGKVLAS 488
Cdd:TIGR02633 162 LLILDEPSSSLTEKETEILLDIIRDLKAHGVACVYIS-HKLNEVKAvCDTICVIRDGQHVAT 222
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
294-489 |
3.45e-21 |
|
ATP-binding cassette domain of the thiamine transport system; Part of the binding-protein-dependent transport system tbpA-thiPQ for thiamine and TPP. Probably responsible for the translocation of thiamine across the membrane. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213265 [Multi-domain] Cd Length: 211 Bit Score: 92.94 E-value: 3.45e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 294 HVNFRIPRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGEAWLFGQPVDPKDIdTRRRVGYMSQAFSLYNELTVRQN--LE 371
Cdd:cd03298 16 HFDLTFAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLINGVDVTAAPP-ADRPVSMLFQENNLFAHLTVEQNvgLG 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 372 LHARLFHIPEAEipARVAEMSERFKLNDVEDILPESLPLGIRQRLSLAVAVIHRPEMLILDEPTSGVDPVARDMFWQLMV 451
Cdd:cd03298 95 LSPGLKLTAEDR--QAIEVALARVGLAGLEKRLPGELSGGERQRVALARVLVRDKPVLLLDEPFAALDPALRAEMLDLVL 172
|
170 180 190
....*....|....*....|....*....|....*....
gi 732682709 452 DLSRQDKVTIFISTHFMNEAERC-DRISLMHAGKVLASG 489
Cdd:cd03298 173 DLHAETKMTVLMVTHQPEDAKRLaQRVVFLDNGRIAAQG 211
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
270-499 |
4.02e-21 |
|
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: 98.64 E-value: 4.02e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 270 PENAEIAIEARDLTMRFG--SFVAVDHVNFRIPRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGEAWLFGQPV-DPKDID 346
Cdd:TIGR02203 324 IERARGDVEFRNVTFRYPgrDRPALDSISLVIEPGETVALVGRSGSGKSTLVNLIPRFYEPDSGQILLDGHDLaDYTLAS 403
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 347 TRRRVGYMSQAFSLYNElTVRQNLElHARLFHIPEAEIpARVAEMSerfKLNDVEDILPESL--PLGI---------RQR 415
Cdd:TIGR02203 404 LRRQVALVSQDVVLFND-TIANNIA-YGRTEQADRAEI-ERALAAA---YAQDFVDKLPLGLdtPIGEngvllsggqRQR 477
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 416 LSLAVAVIHRPEMLILDEPTSGVDPVARDMFwQLMVDLSRQDKVTIFIStHFMNEAERCDRISLMHAGKVLASGTPQELV 495
Cdd:TIGR02203 478 LAIARALLKDAPILILDEATSALDNESERLV-QAALERLMQGRTTLVIA-HRLSTIEKADRIVVMDDGRIVERGTHNELL 555
|
....
gi 732682709 496 EKRG 499
Cdd:TIGR02203 556 ARNG 559
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
14-234 |
5.62e-21 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 95.25 E-value: 5.62e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 14 QLAGVSQHY----GKTVALNNITLDIPARCMVGLIGPDGVGKSSLLSLI------SGARVIEQG-NVMVLG-GDMRdpKH 81
Cdd:PRK11153 3 ELKNISKVFpqggRTIHALNNVSLHIPAGEIFGVIGASGAGKSTLIRCInllerpTSGRVLVDGqDLTALSeKELR--KA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 82 RRdvcpRIAWMPQGLgkNLYHTLSVYENVDFFARLFGHDKAEREVRINELLTSTGLAPFRDR-PAgKLSGGMKQKLGLCC 160
Cdd:PRK11153 81 RR----QIGMIFQHF--NLLSSRTVFDNVALPLELAGTPKAEIKARVTELLELVGLSDKADRyPA-QLSGGQKQRVAIAR 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 732682709 161 ALIHDPELLILDEPTTGVDPLSRSQFWDLIDSIrQRQSNMSVLVATAYMEEAERF-DWLVAMNAGEVLATGSAEE 234
Cdd:PRK11153 154 ALASNPKVLLCDEATSALDPATTRSILELLKDI-NRELGLTIVLITHEMDVVKRIcDRVAVIDAGRLVEQGTVSE 227
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
295-497 |
6.07e-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: 97.90 E-value: 6.07e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 295 VNFRIPRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGEAWLFGQPVDPKDIDTR-RRVGYMSQAFSLYnELTVRQNLelh 373
Cdd:COG4618 351 VSFSLEPGEVLGVIGPSGSGKSTLARLLVGVWPPTAGSVRLDGADLSQWDREELgRHIGYLPQDVELF-DGTIAENI--- 426
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 374 ARLfhiPEAEiPARVAEMSerfKLNDVED-ILpeSLPLG----I-----------RQRLSLAVAVIHRPEMLILDEPTSG 437
Cdd:COG4618 427 ARF---GDAD-PEKVVAAA---KLAGVHEmIL--RLPDGydtrIgeggarlsggqRQRIGLARALYGDPRLVVLDEPNSN 497
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 438 VDPVARDMFWQLMVDLsRQDKVTIFISTHFMNEAERCDRISLMHAGKVLASGTPQELVEK 497
Cdd:COG4618 498 LDDEGEAALAAAIRAL-KARGATVVVITHRPSLLAAVDKLLVLRDGRVQAFGPRDEVLAR 556
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
218-466 |
6.82e-21 |
|
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family transporter in which each gene contains an N-terminal membrane-spanning domain (pfam00664) and a C-terminal ATP-binding domain (pfam00005). In E. coli these genes were discovered as mutants which caused the terminal heme-copper oxidase complex cytochrome bd to fail to assemble. Recent work has shown that the transporter is involved in export of redox-active thiol compounds such as cysteine and glutathione. The linkage to assembly of the cytochrome bd complex is further supported by the conserved operon structure found outside the gammaproteobacteria (cydABCD) containing both the transporter and oxidase genes components. The genes used as the seed members for this model are all either found in the gammproteobacterial context or the CydABCD context. All members of this family scoring above trusted at the time of its creation were from genomes which encode a cytochrome bd complex.
Pssm-ID: 274331 [Multi-domain] Cd Length: 530 Bit Score: 97.43 E-value: 6.82e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 218 LVAMNAGEVLA--TGSAEELRQQTQSAT-LEEAFINLLPQAQRQAHQAVVIPPYQPEnaeiaIEARDLTMRF-GSFVAVD 293
Cdd:TIGR02868 278 LLPLAAFEAFAalPAAAQQLTRVRAAAErIVEVLDAAGPVAEGSAPAAGAVGLGKPT-----LELRDLSAGYpGAPPVLD 352
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 294 HVNFRIPRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGEAWLFGQPVDPKDID-TRRRVGYMSQAFSLYNElTVRQNLEL 372
Cdd:TIGR02868 353 GVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPLQGEVTLDGVPVSSLDQDeVRRRVSVCAQDAHLFDT-TVRENLRL 431
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 373 hARlfhiPEAEiPARVAEMSERFKLNDVEDILPE-----------SLPLGIRQRLSLAVAVIHRPEMLILDEPTSGVDPV 441
Cdd:TIGR02868 432 -AR----PDAT-DEELWAALERVGLADWLRALPDgldtvlgeggaRLSGGERQRLALARALLADAPILLLDEPTEHLDAE 505
|
250 260
....*....|....*....|....*..
gi 732682709 442 ARDmfwQLMVDLSRQD--KVTIFISTH 466
Cdd:TIGR02868 506 TAD---ELLEDLLAALsgRTVVLITHH 529
|
|
| PvdE |
COG4615 |
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ... |
242-485 |
7.46e-21 |
|
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: 97.56 E-value: 7.46e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 242 ATLEEAfinlLPQAQRQAHQAVVIPPYQPENAeiaIEARDLTMRF------GSFvAVDHVNFRIPRGEIFGFLGSNGCGK 315
Cdd:COG4615 300 EELELA----LAAAEPAAADAAAPPAPADFQT---LELRGVTYRYpgedgdEGF-TLGPIDLTIRRGELVFIVGGNGSGK 371
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 316 STTMKMLTGLLPASEGEAWLFGQPVDPKDIDTRRrvgymsQAFSlynelTVRQNLELHARLFHIPEAEIPARVAEMSERF 395
Cdd:COG4615 372 STLAKLLTGLYRPESGEILLDGQPVTADNREAYR------QLFS-----AVFSDFHLFDRLLGLDGEADPARARELLERL 440
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 396 KLND---VED--ILPESLPLGIRQRLSLAVAVI-HRPeMLILDEPTSGVDPVARDMFW-QLMVDLSRQDKvTIFISTH-- 466
Cdd:COG4615 441 ELDHkvsVEDgrFSTTDLSQGQRKRLALLVALLeDRP-ILVFDEWAADQDPEFRRVFYtELLPELKARGK-TVIAISHdd 518
|
250 260
....*....|....*....|.
gi 732682709 467 --FmneaERCDRISLMHAGKV 485
Cdd:COG4615 519 ryF----DLADRVLKMDYGKL 535
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
14-235 |
8.17e-21 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 95.15 E-value: 8.17e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 14 QLAGVSQHYGKTVALNNITLDIPARCMVGLIGPDGVGKSSLLSLISGARVIEQGNVMVLGGDMRDpKHRRDvcPRIAWMP 93
Cdd:PRK10851 4 EIANIKKSFGRTQVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFHGTDVSR-LHARD--RKVGFVF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 94 QGLGknLYHTLSVYENVDFFARLFGH----DKAEREVRINELLTSTGLAPFRDRPAGKLSGGMKQKLGLCCALIHDPELL 169
Cdd:PRK10851 81 QHYA--LFRHMTVFDNIAFGLTVLPRrerpNAAAIKAKVTQLLEMVQLAHLADRYPAQLSGGQKQRVALARALAVEPQIL 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 732682709 170 ILDEPTTGVDPLSRSQF--WdlidsIRQRQSNM---SVLVaTAYMEEA-ERFDWLVAMNAGEVLATGSAEEL 235
Cdd:PRK10851 159 LLDEPFGALDAQVRKELrrW-----LRQLHEELkftSVFV-THDQEEAmEVADRVVVMSQGNIEQAGTPDQV 224
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
14-248 |
9.01e-21 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 92.84 E-value: 9.01e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 14 QLAGVSQHYGKTVALNNITLDIPARCMVGLIGPDGVGKSSLLSLISGARVIEQGNVMVLGGDMRDPKhRRDVCPRIAWMP 93
Cdd:COG4604 3 EIKNVSKRYGGKVVLDDVSLTIPKGGITALIGPNGAGKSTLLSMISRLLPPDSGEVLVDGLDVATTP-SRELAKRLAILR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 94 QGLGKNLyhTLSVYENVdFFARlFGHDK----AEREVRINELLTSTGLAPFRDRPAGKLSGGMKQKlglccALI-----H 164
Cdd:COG4604 82 QENHINS--RLTVRELV-AFGR-FPYSKgrltAEDREIIDEAIAYLDLEDLADRYLDELSGGQRQR-----AFIamvlaQ 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 165 DPELLILDEPTTGVDPL-SRsqfwDLIDSIRQ--RQSNMSVLV-------ATAYMeeaerfDWLVAMNAGEVLATGSAEE 234
Cdd:COG4604 153 DTDYVLLDEPLNNLDMKhSV----QMMKLLRRlaDELGKTVVIvlhdinfASCYA------DHIVAMKDGRVVAQGTPEE 222
|
250
....*....|....
gi 732682709 235 LrqqTQSATLEEAF 248
Cdd:COG4604 223 I---ITPEVLSDIY 233
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
18-214 |
1.05e-20 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 92.92 E-value: 1.05e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 18 VSQHYGKTVALNNITLDIPARCMVGLIGPDGVGKSSLL-------SLISGARVieQGNVMVLGGDMRDPkhrrDVCP--- 87
Cdd:PRK14243 16 LNVYYGSFLAVKNVWLDIPKNQITAFIGPSGCGKSTILrcfnrlnDLIPGFRV--EGKVTFHGKNLYAP----DVDPvev 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 88 --RIAWM---PQGLGKnlyhtlSVYENVDFFARLFGH-----DKAEREVR-------INELLTSTGLApfrdrpagkLSG 150
Cdd:PRK14243 90 rrRIGMVfqkPNPFPK------SIYDNIAYGARINGYkgdmdELVERSLRqaalwdeVKDKLKQSGLS---------LSG 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 732682709 151 GMKQKLGLCCALIHDPELLILDEPTTGVDPLSRSQFWDLIDSIRQRqsnMSVLVATAYMEEAER 214
Cdd:PRK14243 155 GQQQRLCIARAIAVQPEVILMDEPCSALDPISTLRIEELMHELKEQ---YTIIIVTHNMQQAAR 215
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
14-230 |
1.19e-20 |
|
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: 91.50 E-value: 1.19e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 14 QLAGVSQHY--GKTVALNNITLDIPARCMVGLIGPDGVGKSSLLSLISGARVIEQGNVMVLGGDMR--DPkhrRDVCPRI 89
Cdd:cd03245 4 EFRNVSFSYpnQEIPALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGTDIRqlDP---ADLRRNI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 90 AWMPQGLgknlyhTL---SVYENVDFFARLfgHDkaerEVRINELLTSTGLAPF-RDRPAG----------KLSGGMKQK 155
Cdd:cd03245 81 GYVPQDV------TLfygTLRDNITLGAPL--AD----DERILRAAELAGVTDFvNKHPNGldlqigergrGLSGGQRQA 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 732682709 156 LGLCCALIHDPELLILDEPTTGVDPLSRSQFwdlIDSIRQRQSNMSVLVATAYMEEAERFDWLVAMNAGEVLATG 230
Cdd:cd03245 149 VALARALLNDPPILLLDEPTSAMDMNSEERL---KERLRQLLGDKTLIIITHRPSLLDLVDRIIVMDSGRIVADG 220
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
293-500 |
1.33e-20 |
|
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: 91.83 E-value: 1.33e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 293 DHVNFRIPRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGEAWLFGQpvDPKDI---DTRRRVGYMSQAFSLYNeLTVRQN 369
Cdd:cd03249 20 KGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEILLDGV--DIRDLnlrWLRSQIGLVSQEPVLFD-GTIAEN 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 370 LELHARLFHIPEAEIPARVAEMSErFKLNdvediLPE-----------SLPLGIRQRLSLAVAVIHRPEMLILDEPTSGV 438
Cdd:cd03249 97 IRYGKPDATDEEVEEAAKKANIHD-FIMS-----LPDgydtlvgergsQLSGGQKQRIAIARALLRNPKILLLDEATSAL 170
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 732682709 439 DpVARDMFWQLMVDLSRQDKVTIFIStHFMNEAERCDRISLMHAGKVLASGTPQELVEKRGA 500
Cdd:cd03249 171 D-AESEKLVQEALDRAMKGRTTIVIA-HRLSTIRNADLIAVLQNGQVVEQGTHDELMAQKGV 230
|
|
| thiQ |
TIGR01277 |
thiamine ABC transporter, ATP-binding protein; This model describes the energy-transducing ... |
296-485 |
1.53e-20 |
|
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: 91.08 E-value: 1.53e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 296 NFRIPRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGEAWLFGQPVdPKDIDTRRRVGYMSQAFSLYNELTVRQNLELHAR 375
Cdd:TIGR01277 18 DLNVADGEIVAIMGPSGAGKSTLLNLIAGFIEPASGSIKVNDQSH-TGLAPYQRPVSMLFQENNLFAHLTVRQNIGLGLH 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 376 LFHIPEAEIPARVAEMSERFKLNDVEDILPESLPLGIRQRLSLAVAVIHRPEMLILDEPTSGVDPVARDMFWQLMVDLSR 455
Cdd:TIGR01277 97 PGLKLNAEQQEKVVDAAQQVGIADYLDRLPEQLSGGQRQRVALARCLVRPNPILLLDEPFSALDPLLREEMLALVKQLCS 176
|
170 180 190
....*....|....*....|....*....|.
gi 732682709 456 QDKVTIFISTHFMNEAER-CDRISLMHAGKV 485
Cdd:TIGR01277 177 ERQRTLLMVTHHLSDARAiASQIAVVSQGKI 207
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
277-485 |
2.07e-20 |
|
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of the protease secretion system PrtD, a 60-kDa integral membrane protein sharing 37% identity with HlyB, the ABC component of the alpha-hemolysin secretion pathway, in the C-terminal domain. They export degradative enzymes by using a type I protein secretion system and lack an N-terminal signal peptide, but contain a C-terminal secretion signal. The Type I secretion apparatus is made up of three components, an ABC transporter, a membrane fusion protein (MFP), and an outer membrane protein (OMP). For the HlyA transporter complex, HlyB (ABC transporter) and HlyD (MFP) reside in the inner membrane of E. coli. The OMP component is TolC, which is thought to interact with the MFP to form a continuous channel across the periplasm from the cytoplasm to the exterior. HlyB belongs to the family of ABC transporters, which are ubiquitous, ATP-dependent transmembrane pumps or channels. The spectrum of transport substrates ranges from inorganic ions, nutrients such as amino acids, sugars, or peptides, hydrophobic drugs, to large polypeptides, such as HlyA.
Pssm-ID: 213213 [Multi-domain] Cd Length: 173 Bit Score: 89.20 E-value: 2.07e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 277 IEARDLTMRFG--SFVAVDHVNFRIPRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGEAWLFGQPVDPKDIDT-RRRVGY 353
Cdd:cd03246 1 LEVENVSFRYPgaEPPVLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDGADISQWDPNElGDHVGY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 354 MSQAFSLYnELTVRQNLelharlfhipeaeiparvaemserfklndvedilpesLPLGIRQRLSLAVAVIHRPEMLILDE 433
Cdd:cd03246 81 LPQDDELF-SGSIAENI-------------------------------------LSGGQRQRLGLARALYGNPRILVLDE 122
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 732682709 434 PTSGVDPVARDMFWQLMVDLSRQDKVTIFIsTHFMNEAERCDRISLMHAGKV 485
Cdd:cd03246 123 PNSHLDVEGERALNQAIAALKAAGATRIVI-AHRPETLASADRILVLEDGRV 173
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
277-489 |
2.28e-20 |
|
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome bd biogenesis. The CydC and CydD proteins are important for the formation of cytochrome bd terminal oxidase of E. coli and it has been proposed that they were necessary for biosynthesis of the cytochrome bd quinol oxidase and for periplasmic c-type cytochromes. CydCD were proposed to determine a heterooligomeric complex important for heme export into the periplasm or to be involved in the maintenance of the proper redox state of the periplasmic space. In Bacillus subtilis, the absence of CydCD does not affect the presence of halo-cytochrome c in the membrane and this observation suggests that CydCD proteins are not involved in the export of heme in this organism.
Pssm-ID: 213214 [Multi-domain] Cd Length: 178 Bit Score: 89.29 E-value: 2.28e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 277 IEARDLTMRFG--SFVAVDHVNFRIPRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGEAWLFGQPVDPKDIDTRRRVGYM 354
Cdd:cd03247 1 LSINNVSFSYPeqEQQVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDGVPVSDLEKALSSLISVL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 355 SQAFSLYNElTVRQNLelharlfhipeaeiparvaemSERFKlndvedilpeslpLGIRQRLSLAVAVIHRPEMLILDEP 434
Cdd:cd03247 81 NQRPYLFDT-TLRNNL---------------------GRRFS-------------GGERQRLALARILLQDAPIVLLDEP 125
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 732682709 435 TSGVDPVARDMFWQLMVDLSRqDKVTIFIsTHFMNEAERCDRISLMHAGKVLASG 489
Cdd:cd03247 126 TVGLDPITERQLLSLIFEVLK-DKTLIWI-THHLTGIEHMDKILFLENGKIIMQG 178
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
275-494 |
2.62e-20 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 93.61 E-value: 2.62e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 275 IAIEARDLTMRFGSFVAVDHVNFRIPRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGEAWLFGQPVD---PKDidtrRRV 351
Cdd:PRK10851 1 MSIEIANIKKSFGRTQVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFHGTDVSrlhARD----RKV 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 352 GYMSQAFSLYNELTVRQNLELHARLFHIPE----AEIPARVAEMSERFKLNDVEDILPESLPLGIRQRLSLAVAVIHRPE 427
Cdd:PRK10851 77 GFVFQHYALFRHMTVFDNIAFGLTVLPRRErpnaAAIKAKVTQLLEMVQLAHLADRYPAQLSGGQKQRVALARALAVEPQ 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 732682709 428 MLILDEPTSGVDPVARDMFWQLMVDLSRQDKVTIFISTHFMNEA-ERCDRISLMHAGKVLASGTPQEL 494
Cdd:PRK10851 157 ILLLDEPFGALDAQVRKELRRWLRQLHEELKFTSVFVTHDQEEAmEVADRVVVMSQGNIEQAGTPDQV 224
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
271-494 |
2.80e-20 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 91.75 E-value: 2.80e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 271 ENAEIAIEARDLTMRFGSFVAVDHVNFRIPRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGEAWLFGQPVDP----KDID 346
Cdd:PRK11831 2 QSVANLVDMRGVSFTRGNRCIFDNISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEILFDGENIPAmsrsRLYT 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 347 TRRRVGYMSQAFSLYNELTVRQN----LELHARLfhiPEAEIPARVAEMSERFKLNDVEDILPESLPLGIRQRLSLAVAV 422
Cdd:PRK11831 82 VRKRMSMLFQSGALFTDMNVFDNvaypLREHTQL---PAPLLHSTVMMKLEAVGLRGAAKLMPSELSGGMARRAALARAI 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 732682709 423 IHRPEMLILDEPTSGVDPVARDMFWQLMVDLSRQDKVTIFISTHFMNEA-ERCDRISLMHAGKVLASGTPQEL 494
Cdd:PRK11831 159 ALEPDLIMFDEPFVGQDPITMGVLVKLISELNSALGVTCVVVSHDVPEVlSIADHAYIVADKKIVAHGSAQAL 231
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
20-276 |
3.87e-20 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 91.40 E-value: 3.87e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 20 QHYGKTVALNNITLDIPARCMVGLIGPDGVGKSSLLSLISGARVIEQGNVMVLGGDMRDpKHRRDVCPRIAWMPQGLGKN 99
Cdd:PRK13652 12 SYSGSKEALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIRGEPITK-ENIREVRKFVGLVFQNPDDQ 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 100 LYHTlSVYENVDFFARLFGHDKAEREVRINELLTSTGLAPFRDRPAGKLSGGMKQKLGLCCALIHDPELLILDEPTTGVD 179
Cdd:PRK13652 91 IFSP-TVEQDIAFGPINLGLDEETVAHRVSSALHMLGLEELRDRVPHHLSGGEKKRVAIAGVIAMEPQVLVLDEPTAGLD 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 180 PLSRSQFWDLIDSIRQRQSnMSVLVATAYME-EAERFDWLVAMNAGEVLATGSAEELRQQTQSATLEEAFINLLPQAQR- 257
Cdd:PRK13652 170 PQGVKELIDFLNDLPETYG-MTVIFSTHQLDlVPEMADYIYVMDKGRIVAYGTVEEIFLQPDLLARVHLDLPSLPKLIRs 248
|
250 260
....*....|....*....|
gi 732682709 258 -QAHQAVVIPPYQPENAEIA 276
Cdd:PRK13652 249 lQAQGIAIDMAYTYQEAEDA 268
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
277-484 |
4.97e-20 |
|
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This subfamily is also known as MRP (multidrug resistance-associated protein). Some of the MRP members have five additional transmembrane segments in their N-terminus, but the function of these additional membrane-spanning domains is not clear. The MRP was found in the multidrug-resisting lung cancer cell in which p-glycoprotein was not overexpressed. MRP exports glutathione by drug stimulation, as well as, certain substrates in conjugated forms with anions, such as glutathione, glucuronate, and sulfate.
Pssm-ID: 213217 [Multi-domain] Cd Length: 204 Bit Score: 89.07 E-value: 4.97e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 277 IEARDLTMRFGS-----FVAVDHVNFRIPRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGEAWLFGqpvdpkdidtrrRV 351
Cdd:cd03250 1 ISVEDASFTWDSgeqetSFTLKDINLEVPKGELVAIVGPVGSGKSSLLSALLGELEKLSGSVSVPG------------SI 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 352 GYMSQAFSLYNElTVRQNLelharLFHIPEAEiparvaemsERFK--------LNDVEdILPE-----------SLPLGI 412
Cdd:cd03250 69 AYVSQEPWIQNG-TIRENI-----LFGKPFDE---------ERYEkvikacalEPDLE-ILPDgdlteigekgiNLSGGQ 132
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 732682709 413 RQRLSLAVAVIHRPEMLILDEPTSGVDP-VARDMFWQLMVDLSRQDKvTIFISTHFMNEAERCDRISLMHAGK 484
Cdd:cd03250 133 KQRISLARAVYSDADIYLLDDPLSAVDAhVGRHIFENCILGLLLNNK-TRILVTHQLQLLPHADQIVVLDNGR 204
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
10-485 |
7.06e-20 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 94.21 E-value: 7.06e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 10 PPVAQLAGVSQHYGKTVALNNITLDIPARCMVGLIGPDGVGKSSLLSLISGARVIEQGNVMVLGGDMRDPKHRRDVCPRI 89
Cdd:PRK11288 2 SPYLSFDGIGKTFPGVKALDDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSILIDGQEMRFASTTAALAAGV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 90 AWMPQGLgkNLYHTLSVYENVdFFARL---FGH-DKAEREVRINELLTSTGLAPFRDRPAGKLSGGMKQKLGLCCALIHD 165
Cdd:PRK11288 82 AIIYQEL--HLVPEMTVAENL-YLGQLphkGGIvNRRLLNYEAREQLEHLGVDIDPDTPLKYLSIGQRQMVEIAKALARN 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 166 PELLILDEPTTGvdpLSRSQFWDLIDSIRQ-RQSNMSVLVATAYMEEAERFdwlvaMNAGEVLATGSaeelrqqtqsatl 244
Cdd:PRK11288 159 ARVIAFDEPTSS---LSAREIEQLFRVIRElRAEGRVILYVSHRMEEIFAL-----CDAITVFKDGR------------- 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 245 eeaFINLLPQAQRQAHQAVV----------IPPYQP-ENAEIAIEARDLTmrfGSFVAVDhVNFRIPRGEIFGFLGSNGC 313
Cdd:PRK11288 218 ---YVATFDDMAQVDRDQLVqamvgreigdIYGYRPrPLGEVRLRLDGLK---GPGLREP-ISFSVRAGEIVGLFGLVGA 290
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 314 GKSTTMKMLTGLLPASEGEAWLFGQPVDPKDIDTRRRVGYM-----SQAFSLYNELTVRQNLELHARLFHIPEAEI--PA 386
Cdd:PRK11288 291 GRSELMKLLYGATRRTAGQVYLDGKPIDIRSPRDAIRAGIMlcpedRKAEGIIPVHSVADNINISARRHHLRAGCLinNR 370
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 387 RVAEMSERF--KLN-----DVEDILpeSLPLGIRQRLSLAVAVIHRPEMLILDEPTSGVDPVARDMFWQLMVDLSRQDKV 459
Cdd:PRK11288 371 WEAENADRFirSLNiktpsREQLIM--NLSGGNQQKAILGRWLSEDMKVILLDEPTRGIDVGAKHEIYNVIYELAAQGVA 448
|
490 500
....*....|....*....|....*.
gi 732682709 460 TIFISTHFMNEAERCDRISLMHAGKV 485
Cdd:PRK11288 449 VLFVSSDLPEVLGVADRIVVMREGRI 474
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
272-485 |
7.33e-20 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 90.12 E-value: 7.33e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 272 NAEIAIEARDLTMRFGSFVAVDHVNFRIPRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGEAWLFGQPVDPKDIDTRrrv 351
Cdd:PRK11247 8 NQGTPLLLNAVSKRYGERTVLNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAGELLAGTAPLAEAREDTR--- 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 352 gYMSQAFSLYNELTVRQNLELHARLFHIPEAEIPARVAEMSERfkLNDvediLPESLPLGIRQRLSLAVAVIHRPEMLIL 431
Cdd:PRK11247 85 -LMFQDARLLPWKKVIDNVGLGLKGQWRDAALQALAAVGLADR--ANE----WPAALSGGQKQRVALARALIHRPGLLLL 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 732682709 432 DEPTSGVDPVARDMFWQLMVDLSRQDKVTIFISTHFMNEA-ERCDRISLMHAGKV 485
Cdd:PRK11247 158 DEPLGALDALTRIEMQDLIESLWQQHGFTVLLVTHDVSEAvAMADRVLLIEEGKI 212
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
277-466 |
7.96e-20 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 88.78 E-value: 7.96e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 277 IEARDLTMRFGSFVAVDHVNFRIPRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGEAWLFGQPVDpkDIDTRRRVGYMSQ 356
Cdd:PRK13539 3 LEGEDLACVRGGRVLFSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDGGDID--DPDVAEACHYLGH 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 357 AFSLYNELTVRQNLELHARLFHIPEAEIPARVaemsERFKLNDVEDILPESLPLGIRQRLSLA-VAVIHRPeMLILDEPT 435
Cdd:PRK13539 81 RNAMKPALTVAENLEFWAAFLGGEELDIAAAL----EAVGLAPLAHLPFGYLSAGQKRRVALArLLVSNRP-IWILDEPT 155
|
170 180 190
....*....|....*....|....*....|.
gi 732682709 436 SGVDPVARDMFWQLMVDLSRQDKvTIFISTH 466
Cdd:PRK13539 156 AALDAAAVALFAELIRAHLAQGG-IVIAATH 185
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
36-238 |
9.33e-20 |
|
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: 95.47 E-value: 9.33e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 36 PARCMvGLIGPDGVGKSSLLSLISGARVIEQGNVMVLGGDMRdpKHRRDVCPRIAWMPQGlgKNLYHTLSVYENVDFFAR 115
Cdd:TIGR01257 1964 PGECF-GLLGVNGAGKTTTFKMLTGDTTVTSGDATVAGKSIL--TNISDVHQNMGYCPQF--DAIDDLLTGREHLYLYAR 2038
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 116 LFGHDKAEREVRINELLTSTGLAPFRDRPAGKLSGGMKQKLGLCCALIHDPELLILDEPTTGVDPLSRSQFWDLIDSIRQ 195
Cdd:TIGR01257 2039 LRGVPAEEIEKVANWSIQSLGLSLYADRLAGTYSGGNKRKLSTAIALIGCPPLVLLDEPTTGMDPQARRMLWNTIVSIIR 2118
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 732682709 196 RQSnmSVLVATAYMEEAERF-DWLVAMNAGEVLATGSAEELRQQ 238
Cdd:TIGR01257 2119 EGR--AVVLTSHSMEECEALcTRLAIMVKGAFQCLGTIQHLKSK 2160
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
277-504 |
9.99e-20 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 93.88 E-value: 9.99e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 277 IEARDLTMRFG--SFvAVDHVNFRIPRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGEAWLFGQPVDPKDIDTRRRVgyM 354
Cdd:PRK10522 323 LELRNVTFAYQdnGF-SVGPINLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKPVTAEQPEDYRKL--F 399
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 355 SQAFS---LYNELTVRQNlelharlfhipEAEIPARVAEMSERFKLND---VED--ILPESLPLGIRQRLSLAVAVIHRP 426
Cdd:PRK10522 400 SAVFTdfhLFDQLLGPEG-----------KPANPALVEKWLERLKMAHkleLEDgrISNLKLSKGQKKRLALLLALAEER 468
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 732682709 427 EMLILDEPTSGVDPVARDMFWQLMVDLSRQDKVTIFISTHFMNEAERCDRISLMHAGKVlasgtpQELV-EKRGAASLE 504
Cdd:PRK10522 469 DILLLDEWAADQDPHFRREFYQVLLPLLQEMGKTIFAISHDDHYFIHADRLLEMRNGQL------SELTgEERDAASRD 541
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
277-497 |
1.16e-19 |
|
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: 93.71 E-value: 1.16e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 277 IEARDLTMRFGSFVAVDHVNFRIPRGEIFGFLGSNGCGKSTTMKMLTGL--LPASEGE-----------AWL-------- 335
Cdd:TIGR03269 1 IEVKNLTKKFDGKEVLKNISFTIEEGEVLGILGRSGAGKSVLMHVLRGMdqYEPTSGRiiyhvalcekcGYVerpskvge 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 336 ---------------FGQPVDPKDIDTRRRVGYMSQ-AFSLYNELTVRQNLelharLFHIPEAEIPA-----RVAEMSER 394
Cdd:TIGR03269 81 pcpvcggtlepeevdFWNLSDKLRRRIRKRIAIMLQrTFALYGDDTVLDNV-----LEALEEIGYEGkeavgRAVDLIEM 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 395 FKLNDVEDILPESLPLGIRQRLSLAVAVIHRPEMLILDEPTSGVDPVARDMFWQLMVDLSRQDKVTIFISTHFMNEAER- 473
Cdd:TIGR03269 156 VQLSHRITHIARDLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALEEAVKASGISMVLTSHWPEVIEDl 235
|
250 260
....*....|....*....|....
gi 732682709 474 CDRISLMHAGKVLASGTPQELVEK 497
Cdd:TIGR03269 236 SDKAIWLENGEIKEEGTPDEVVAV 259
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
43-206 |
1.40e-19 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 88.01 E-value: 1.40e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 43 LIGPDGVGKSSLLSLISGARVIEQGNVMVLGGDMRDPKHRrdvcPRIAWmpqgLG-KN-LYHTLSVYENVDFFARLFGhd 120
Cdd:PRK13539 33 LTGPNGSGKTTLLRLIAGLLPPAAGTIKLDGGDIDDPDVA----EACHY----LGhRNaMKPALTVAENLEFWAAFLG-- 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 121 kaEREVRINELLTSTGLAPFRDRPAGKLSGGMKQKLGLCCALIHDPELLILDEPTTGVDPLSRSQFWDLIdSIRQRQSNM 200
Cdd:PRK13539 103 --GEELDIAAALEAVGLAPLAHLPFGYLSAGQKRRVALARLLVSNRPIWILDEPTAALDAAAVALFAELI-RAHLAQGGI 179
|
....*.
gi 732682709 201 sVLVAT 206
Cdd:PRK13539 180 -VIAAT 184
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
20-173 |
1.57e-19 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 88.99 E-value: 1.57e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 20 QHYGKTVALNNITLDIPARCMVGLIGPDGVGKSSLLSLISGarVIE--QGNVMVLGgdmrdpkhrrdvcpRIAWmPQGLG 97
Cdd:COG1134 34 TRREEFWALKDVSFEVERGESVGIIGRNGAGKSTLLKLIAG--ILEptSGRVEVNG--------------RVSA-LLELG 96
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 732682709 98 KNLYHTLSVYENVDFFARLFGHDKAEREVRINELLTSTGLAPFRDRPAGKLSGGMKQKLGLCCALIHDPELLILDE 173
Cdd:COG1134 97 AGFHPELTGRENIYLNGRLLGLSRKEIDEKFDEIVEFAELGDFIDQPVKTYSSGMRARLAFAVATAVDPDILLVDE 172
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
18-235 |
2.51e-19 |
|
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; MsbA is an essential ABC transporter, closely related to eukaryotic MDR proteins. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213218 [Multi-domain] Cd Length: 234 Bit Score: 88.06 E-value: 2.51e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 18 VSQHYGKTV--ALNNITLDIPARCMVGLIGPDGVGKSSLLSLISGARVIEQGNVMVLGGDMRD---PKHRRdvcpRIAWM 92
Cdd:cd03251 6 VTFRYPGDGppVLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDGHDVRDytlASLRR----QIGLV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 93 PQGLgkNLYHTlSVYENVdffarLFGHDKAEREvRINELLTSTGLAPFRDR-PAG----------KLSGGMKQKLGLCCA 161
Cdd:cd03251 82 SQDV--FLFND-TVAENI-----AYGRPGATRE-EVEEAARAANAHEFIMElPEGydtvigergvKLSGGQRQRIAIARA 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 732682709 162 LIHDPELLILDEPTTGVDplSRSQfwDLI-DSIRQRQSNMSVLVATAYMEEAERFDWLVAMNAGEVLATGSAEEL 235
Cdd:cd03251 153 LLKDPPILILDEATSALD--TESE--RLVqAALERLMKNRTTFVIAHRLSTIENADRIVVLEDGKIVERGTHEEL 223
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
277-450 |
2.54e-19 |
|
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein encoded by ccmA in bacteria. An exception is, an arabidopsis protein. Quite likely this is encoded by an organelle. Bacterial c-type cytocromes are located on the periplasmic side of the cytoplasmic membrane. Several gene products encoded in a locus designated as 'ccm' are implicated in the transport and assembly of the functional cytochrome C. This cluster includes genes: ccmA;B;C;D;E;F;G and H. The posttranslational pathway includes the transport of heme moiety, the secretion of the apoprotein and the covalent attachment of the heme with the apoprotein. The proteins ccmA and B represent an ABC transporter; ccmC and D participate in heme transfer to ccmE, which function as a periplasmic heme chaperone. The presence of ccmF, G and H is suggested to be obligatory for the final functional assembly of cytochrome c. [Protein fate, Protein and peptide secretion and trafficking, Transport and binding proteins, Other]
Pssm-ID: 273491 [Multi-domain] Cd Length: 198 Bit Score: 87.03 E-value: 2.54e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 277 IEARDLTMRFGSFVAVDHVNFRIPRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGEAWLFGQPVDPKDIDTRRRVGYMSQ 356
Cdd:TIGR01189 1 LAARNLACSRGERMLFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRWNGTPLAEQRDEPHENILYLGH 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 357 AFSLYNELTVRQNLELHARLFHIPEAEIPARVAEMSerfkLNDVEDILPESLPLGIRQRLSLAVAVIHRPEMLILDEPTS 436
Cdd:TIGR01189 81 LPGLKPELSALENLHFWAAIHGGAQRTIEDALAAVG----LTGFEDLPAAQLSAGQQRRLALARLWLSRRPLWILDEPTT 156
|
170
....*....|....
gi 732682709 437 GVDPVARDMFWQLM 450
Cdd:TIGR01189 157 ALDKAGVALLAGLL 170
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
23-235 |
3.24e-19 |
|
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid transport and metabolism, Inorganic ion transport and metabolism];
Pssm-ID: 440213 [Multi-domain] Cd Length: 320 Bit Score: 89.73 E-value: 3.24e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 23 GKTVALNNITLDIPARCMVGLIGPDGVGKSSLLSLISG---ARVIEQGNVMVLGGDMR--DPKHRRDVCPR-IAWMPQGL 96
Cdd:COG0444 16 GVVKAVDGVSFDVRRGETLGLVGESGSGKSTLARAILGllpPPGITSGEILFDGEDLLklSEKELRKIRGReIQMIFQDP 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 97 GKNLYHTLSVYENVDFFARLFGH-DKAEREVRINELLTSTGLAPFRDRpAGK----LSGGMKQKLGLCCALIHDPELLIL 171
Cdd:COG0444 96 MTSLNPVMTVGDQIAEPLRIHGGlSKAEARERAIELLERVGLPDPERR-LDRypheLSGGMRQRVMIARALALEPKLLIA 174
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 732682709 172 DEPTTGVDPLSRSQFWDLIDSIrQRQSNMSVLVAT------AYMeeAERfdwlVA-MNAGEVLATGSAEEL 235
Cdd:COG0444 175 DEPTTALDVTIQAQILNLLKDL-QRELGLAILFIThdlgvvAEI--ADR----VAvMYAGRIVEEGPVEEL 238
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
28-258 |
3.41e-19 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 88.64 E-value: 3.41e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 28 LNNITLDIPARCMVGLIGPDGVGKSSLLSLISGARVIEQGNVMVLGgDMRDPKHRRDVCPRIAWMPQGlGKNLYHTLSVY 107
Cdd:PRK13650 23 LNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIIDG-DLLTEENVWDIRHKIGMVFQN-PDNQFVGATVE 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 108 ENVDFFARLFGHDKAEREVRINELLTSTGLAPFRDRPAGKLSGGMKQKLGLCCALIHDPELLILDEPTTGVDPLSRSQFW 187
Cdd:PRK13650 101 DDVAFGLENKGIPHEEMKERVNEALELVGMQDFKEREPARLSGGQKQRVAIAGAVAMRPKIIILDEATSMLDPEGRLELI 180
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 732682709 188 DLIDSIRQrQSNMSVLVATAYMEEAERFDWLVAMNAGEVLATGSAEEL---RQQTQSATLEEAFINLLPQAQRQ 258
Cdd:PRK13650 181 KTIKGIRD-DYQMTVISITHDLDEVALSDRVLVMKNGQVESTSTPRELfsrGNDLLQLGLDIPFTTSLVQSLRQ 253
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
11-227 |
3.92e-19 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 88.20 E-value: 3.92e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 11 PVAqLAGVSQHYGKTVALNNITLDIPARCMVGLIGPDGVGKSSLLSLISGARVIEQGNVmvLGGDMRDPKHRRDvcprIA 90
Cdd:PRK11247 12 PLL-LNAVSKRYGERTVLNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAGEL--LAGTAPLAEARED----TR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 91 WMPQGlgKNLYHTLSVYENVDFfaRLFGHDKAEREvrinELLTSTGLApfrDR----PAGkLSGGMKQKLGLCCALIHDP 166
Cdd:PRK11247 85 LMFQD--ARLLPWKKVIDNVGL--GLKGQWRDAAL----QALAAVGLA---DRanewPAA-LSGGQKQRVALARALIHRP 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 732682709 167 ELLILDEPTTGVDPLSRSQFWDLIDSIRQrQSNMSVLVATAYMEEAerfdwlVAMnAGEVL 227
Cdd:PRK11247 153 GLLLLDEPLGALDALTRIEMQDLIESLWQ-QHGFTVLLVTHDVSEA------VAM-ADRVL 205
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
11-237 |
4.15e-19 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 87.74 E-value: 4.15e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 11 PVAQLAGVSQHYGKTVALNNITLDIPARCMVGLIGPDGVGKSSLLSLISGARVIEQGNVMVLGGDMRD-PKHrrdvcpRI 89
Cdd:PRK11300 4 PLLSVSGLMMRFGGLLAVNNVNLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTILLRGQHIEGlPGH------QI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 90 AWMpqGLGKN-----LYHTLSVYENV----------DFFARLF---GHDKAEREV--RINELLTSTGLAPFRDRPAGKLS 149
Cdd:PRK11300 78 ARM--GVVRTfqhvrLFREMTVIENLlvaqhqqlktGLFSGLLktpAFRRAESEAldRAATWLERVGLLEHANRQAGNLA 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 150 GGMKQKLGLCCALIHDPELLILDEPTTGVDPLSRSQFWDLIDSIRqRQSNMSVLV----ATAYMEEAERfdwLVAMNAGE 225
Cdd:PRK11300 156 YGQQRRLEIARCMVTQPEILMLDEPAAGLNPKETKELDELIAELR-NEHNVTVLLiehdMKLVMGISDR---IYVVNQGT 231
|
250
....*....|..
gi 732682709 226 VLATGSAEELRQ 237
Cdd:PRK11300 232 PLANGTPEEIRN 243
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
295-497 |
4.15e-19 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 88.65 E-value: 4.15e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 295 VNFRIPRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGEAWLFGQPVDP----KDIDT-RRRVGYM-----SQAFslynEL 364
Cdd:PRK13649 26 VNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDDTLITStsknKDIKQiRKKVGLVfqfpeSQLF----EE 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 365 TVRQNLELHARLFHIPEAEiparvAEMSERFKLNDV---EDIL---PESLPLGIRQRLSLAVAVIHRPEMLILDEPTSGV 438
Cdd:PRK13649 102 TVLKDVAFGPQNFGVSQEE-----AEALAREKLALVgisESLFeknPFELSGGQMRRVAIAGILAMEPKILVLDEPTAGL 176
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 439 DPVARDMFWQLMVDLsRQDKVTIFISTHFMNE-AERCDRISLMHAGKVLASGTPQELVEK 497
Cdd:PRK13649 177 DPKGRKELMTLFKKL-HQSGMTIVLVTHLMDDvANYADFVYVLEKGKLVLSGKPKDIFQD 235
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
277-494 |
4.40e-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: 91.67 E-value: 4.40e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 277 IEARDLTMRFGS----FVAVDHVNFRIPRGEIFGFLGSNGCGKSTTMKMLTGLLPAS----EGEAWLFGQPVDPKDIDTR 348
Cdd:COG4172 7 LSVEDLSVAFGQgggtVEAVKGVSFDIAAGETLALVGESGSGKSVTALSILRLLPDPaahpSGSILFDGQDLLGLSEREL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 349 RRV--GYMSQAF-----SLyNEL-TV-RQ---NLELHARLfhiPEAEIPARVAEMSERFKLNDVEDIL---PESLPLGIR 413
Cdd:COG4172 87 RRIrgNRIAMIFqepmtSL-NPLhTIgKQiaeVLRLHRGL---SGAAARARALELLERVGIPDPERRLdayPHQLSGGQR 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 414 QRLSLAVAVIHRPEMLILDEPTSGVDPVARDMFWQLMVDLSRQDKVTI-FIsTHFMNEAER-CDRISLMHAGKVLASGTP 491
Cdd:COG4172 163 QRVMIAMALANEPDLLIADEPTTALDVTVQAQILDLLKDLQRELGMALlLI-THDLGVVRRfADRVAVMRQGEIVEQGPT 241
|
...
gi 732682709 492 QEL 494
Cdd:COG4172 242 AEL 244
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
291-495 |
4.91e-19 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 88.12 E-value: 4.91e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 291 AVDHVNFRIPRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGEAWLFGQPV-DPKDI-DTRRRVGYMSQ-AFSLYNELTVR 367
Cdd:PRK13644 17 ALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLVSGIDTgDFSKLqGIRKLVGIVFQnPETQFVGRTVE 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 368 QNLELHARLFHIPEAEIPARVAEMSERFKLNDVEDILPESLPLGIRQRLSLAVAVIHRPEMLILDEPTSGVDPVARDMFW 447
Cdd:PRK13644 97 EDLAFGPENLCLPPIEIRKRVDRALAEIGLEKYRHRSPKTLSGGQGQCVALAGILTMEPECLIFDEVTSMLDPDSGIAVL 176
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 732682709 448 QLMVDLSRQDKVTIFIsTHFMNEAERCDRISLMHAGKVLASGTPQELV 495
Cdd:PRK13644 177 ERIKKLHEKGKTIVYI-THNLEELHDADRIIVMDRGKIVLEGEPENVL 223
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
265-494 |
5.48e-19 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 89.14 E-value: 5.48e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 265 IPPYQPENAEIAIEARDLTMRFGS-----FVAVDHVNFRIPRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGEAWL---- 335
Cdd:PRK13631 10 LKVPNPLSDDIILRVKNLYCVFDEkqeneLVALNNISYTFEKNKIYFIIGNSGSGKSTLVTHFNGLIKSKYGTIQVgdiy 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 336 FGQPVD---------PKDIDT----RRRVGYMSQ--AFSLYNElTVRQNLELHARLFHIPEAEIPARVAEMSERFKLND- 399
Cdd:PRK13631 90 IGDKKNnhelitnpySKKIKNfkelRRRVSMVFQfpEYQLFKD-TIEKDIMFGPVALGVKKSEAKKLAKFYLNKMGLDDs 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 400 VEDILPESLPLGIRQRLSLAVAVIHRPEMLILDEPTSGVDPVARDMFWQLMVDLSRQDKvTIFISTHFM-NEAERCDRIS 478
Cdd:PRK13631 169 YLERSPFGLSGGQKRRVAIAGILAIQPEILIFDEPTAGLDPKGEHEMMQLILDAKANNK-TVFVITHTMeHVLEVADEVI 247
|
250
....*....|....*.
gi 732682709 479 LMHAGKVLASGTPQEL 494
Cdd:PRK13631 248 VMDKGKILKTGTPYEI 263
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
12-235 |
5.71e-19 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 88.37 E-value: 5.71e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 12 VAQLAGVSQHYGK-TVALNNITLDIPARCMVGLIGPDGVGKSSLLSLISGARVIEQGNVMvLGGDMRD--PKHRRDVCPR 88
Cdd:PRK13636 5 ILKVEELNYNYSDgTHALKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRIL-FDGKPIDysRKGLMKLRES 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 89 IAWMPQGLGKNLYhTLSVYENVDFFARLFGHDKAEREVRINELLTSTGLAPFRDRPAGKLSGGMKQKLGLCCALIHDPEL 168
Cdd:PRK13636 84 VGMVFQDPDNQLF-SASVYQDVSFGAVNLKLPEDEVRKRVDNALKRTGIEHLKDKPTHCLSFGQKKRVAIAGVLVMEPKV 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 732682709 169 LILDEPTTGVDPLSRSQFWDLIDSIrQRQSNMSVLVATAYMEEAERF-DWLVAMNAGEVLATGSAEEL 235
Cdd:PRK13636 163 LVLDEPTAGLDPMGVSEIMKLLVEM-QKELGLTIIIATHDIDIVPLYcDNVFVMKEGRVILQGNPKEV 229
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
289-494 |
5.83e-19 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 88.14 E-value: 5.83e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 289 FVAVDHVNFRIPRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGEAWL--FGQPVDPKDI----DTRRRVGYMSQ--AFSL 360
Cdd:PRK13645 24 FKALNNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGLIISETGQTIVgdYAIPANLKKIkevkRLRKEIGLVFQfpEYQL 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 361 YNElTVRQNLELHARLFHIPEAEIPARVAEMSERFKL-NDVEDILPESLPLGIRQRLSLAVAVIHRPEMLILDEPTSGVD 439
Cdd:PRK13645 104 FQE-TIEKDIAFGPVNLGENKQEAYKKVPELLKLVQLpEDYVKRSPFELSGGQKRRVALAGIIAMDGNTLVLDEPTGGLD 182
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 732682709 440 PVARDMFWQLMVDLSRQDKVTIFISTHFMNEAER-CDRISLMHAGKVLASGTPQEL 494
Cdd:PRK13645 183 PKGEEDFINLFERLNKEYKKRIIMVTHNMDQVLRiADEVIVMHEGKVISIGSPFEI 238
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
292-498 |
6.26e-19 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 88.35 E-value: 6.26e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 292 VDHVNFRIPRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGEAWLFGQPVDP-------KDIdtRRRVGYM-----SQAFs 359
Cdd:PRK13641 23 LDNISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITIAGYHITPetgnknlKKL--RKKVSLVfqfpeAQLF- 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 360 lynELTVRQNLELHARLFHIPEAEIPARVAEMSERFKLN-DVEDILPESLPLGIRQRLSLAVAVIHRPEMLILDEPTSGV 438
Cdd:PRK13641 100 ---ENTVLKDVEFGPKNFGFSEDEAKEKALKWLKKVGLSeDLISKSPFELSGGQMRRVAIAGVMAYEPEILCLDEPAAGL 176
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 732682709 439 DPVARDMFWQLMVDLSRQDKVTIFIsTHFMNE-AERCDRISLMHAGKVLASGTPQELVEKR 498
Cdd:PRK13641 177 DPEGRKEMMQLFKDYQKAGHTVILV-THNMDDvAEYADDVLVLEHGKLIKHASPKEIFSDK 236
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
22-247 |
6.81e-19 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 87.76 E-value: 6.81e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 22 YGKTVALNNITLDIPARCMVGLIGPDGVGKSSLLSLISGARVIEQGNVMVLGGDMrDPKHRRDVCPR--IAWMPQGLGKN 99
Cdd:PRK13638 11 YQDEPVLKGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLRPQKGAVLWQGKPL-DYSKRGLLALRqqVATVFQDPEQQ 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 100 LYHTlSVYENVDFFARLFGHDKAEREVRINELLTSTGLAPFRDRPAGKLSGGMKQKLGLCCALIHDPELLILDEPTTGVD 179
Cdd:PRK13638 90 IFYT-DIDSDIAFSLRNLGVPEAEITRRVDEALTLVDAQHFRHQPIQCLSHGQKKRVAIAGALVLQARYLLLDEPTAGLD 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 732682709 180 PLSRSQFWDLIDSIRQrQSNMSVLVATAYMEEAERFDWLVAMNAGEVLATGSAEELRQQTQsaTLEEA 247
Cdd:PRK13638 169 PAGRTQMIAIIRRIVA-QGNHVIISSHDIDLIYEISDAVYVLRQGQILTHGAPGEVFACTE--AMEQA 233
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
23-206 |
6.89e-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: 85.87 E-value: 6.89e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 23 GKTVALNNITLDIPARCMVGLIGPDGVGKSSLLSLISGARVIEQGNVMVLGGDMrdPKHRRDVCPRIAWMpqGLGKNLYH 102
Cdd:TIGR01189 11 GERMLFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRWNGTPL--AEQRDEPHENILYL--GHLPGLKP 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 103 TLSVYENVDFFARLfgHDKAEREvrINELLTSTGLAPFRDRPAGKLSGGMKQKLGLCCALIHDPELLILDEPTTGVDPLS 182
Cdd:TIGR01189 87 ELSALENLHFWAAI--HGGAQRT--IEDALAAVGLTGFEDLPAAQLSAGQQRRLALARLWLSRRPLWILDEPTTALDKAG 162
|
170 180
....*....|....*....|....
gi 732682709 183 RSQFWDLIDSIRQRQSnmSVLVAT 206
Cdd:TIGR01189 163 VALLAGLLRAHLARGG--IVLLTT 184
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
17-239 |
6.93e-19 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 87.13 E-value: 6.93e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 17 GVSQHYGKTVALNNITLDIPARCMVGLIGPDGVGKSSLLSLISGARVIEQGNVMVLGGDMRDPKhRRDVCPRIAWMPQgl 96
Cdd:PRK13548 7 NLSVRLGGRTLLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLNGRPLADWS-PAELARRRAVLPQ-- 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 97 gknlYHTLS----VYENVDFFARLFGHDKAEREVRINELLTSTGLAPFRDRPAGKLSGGMKQKLGLCCALI------HDP 166
Cdd:PRK13548 84 ----HSSLSfpftVEEVVAMGRAPHGLSRAEDDALVAAALAQVDLAHLAGRDYPQLSGGEQQRVQLARVLAqlwepdGPP 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 167 ELLILDEPTTGVDPlsRSQFwDLIDSIRQ--RQSNMSVLV-------ATAYmeeAERfdwLVAMNAGEVLATGSAEE-LR 236
Cdd:PRK13548 160 RWLLLDEPTSALDL--AHQH-HVLRLARQlaHERGLAVIVvlhdlnlAARY---ADR---IVLLHQGRLVADGTPAEvLT 230
|
...
gi 732682709 237 QQT 239
Cdd:PRK13548 231 PET 233
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
277-498 |
8.38e-19 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 87.38 E-value: 8.38e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 277 IEARDLTMRFGSFVAVDHVNFRIPRGEIFGFLGSNGCGKSTTMKMLTGLL---PASEGEAWLFGQPVD-----PKDI-DT 347
Cdd:PRK09984 5 IRVEKLAKTFNQHQALHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGLItgdKSAGSHIELLGRTVQregrlARDIrKS 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 348 RRRVGYMSQAFSLYNELTVRQNLELHA-----------RLFHIPEAEipaRVAEMSERFKLNDVEDILPESLPLGIRQRL 416
Cdd:PRK09984 85 RANTGYIFQQFNLVNRLSVLENVLIGAlgstpfwrtcfSWFTREQKQ---RALQALTRVGMVHFAHQRVSTLSGGQQQRV 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 417 SLAVAVIHRPEMLILDEPTSGVDPVARDMFWQLMVDLSRQDKVTIFISTHFMNEAER-CDRISLMHAGKVLASGTPQELV 495
Cdd:PRK09984 162 AIARALMQQAKVILADEPIASLDPESARIVMDTLRDINQNDGITVVVTLHQVDYALRyCERIVALRQGHVFYDGSSQQFD 241
|
...
gi 732682709 496 EKR 498
Cdd:PRK09984 242 NER 244
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
27-235 |
9.46e-19 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 87.38 E-value: 9.46e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 27 ALNNITLDIPARCMVGLIGPDGVGKSSLLSLISGARVIEQGNVMVlGGDMRDPKHRRDVCPRIAWMPQGlGKNLYHTLSV 106
Cdd:PRK13635 22 ALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITV-GGMVLSEETVWDVRRQVGMVFQN-PDNQFVGATV 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 107 YENVDFFARLFGHDKAEREVRINELLTSTGLAPFRDRPAGKLSGGMKQKLGLCCALIHDPELLILDEPTTGVDPLSRSQf 186
Cdd:PRK13635 100 QDDVAFGLENIGVPREEMVERVDQALRQVGMEDFLNREPHRLSGGQKQRVAIAGVLALQPDIIILDEATSMLDPRGRRE- 178
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 732682709 187 wdLIDSIRQ--RQSNMSVLVATAYMEEAERFDWLVAMNAGEVLATGSAEEL 235
Cdd:PRK13635 179 --VLETVRQlkEQKGITVLSITHDLDEAAQADRVIVMNKGEILEEGTPEEI 227
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
277-450 |
1.75e-18 |
|
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the bacterial CcmAB transporter. The CCM family is involved in bacterial cytochrome c biogenesis. Cytochrome c maturation in E. coli requires the ccm operon, which encodes eight membrane proteins (CcmABCDEFGH). CcmE is a periplasmic heme chaperon that binds heme covalently and transfers it onto apocytochrome c in the presence of CcmF, CcmG, and CcmH. The CcmAB proteins represent an ABC transporter and the CcmCD proteins participate in heme transfer to CcmE.
Pssm-ID: 213198 [Multi-domain] Cd Length: 201 Bit Score: 84.85 E-value: 1.75e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 277 IEARDLTMRFGSFVAVDHVNFRIPRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGEAWLFGQPVDPKDIDTRRRVGYMSQ 356
Cdd:cd03231 1 LEADELTCERDGRALFSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNGGPLDFQRDSIARGLLYLGH 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 357 AFSLYNELTVRQNLELHARlFHIPEAeiparVAEMSERFKLNDVEDILPESLPLGIRQRLSLAVAVIHRPEMLILDEPTS 436
Cdd:cd03231 81 APGIKTTLSVLENLRFWHA-DHSDEQ-----VEEALARVGLNGFEDRPVAQLSAGQQRRVALARLLLSGRPLWILDEPTT 154
|
170
....*....|....
gi 732682709 437 GVDPVARDMFWQLM 450
Cdd:cd03231 155 ALDKAGVARFAEAM 168
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
6-206 |
2.31e-18 |
|
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: 89.73 E-value: 2.31e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 6 LVPVPPVAQLAGVSQHY-GKTVALNNITLDIPARCMVGLIGPDGVGKSSLLSLISGARVIEQGNVMVLGGDMRDPKHRrD 84
Cdd:TIGR02868 328 VGLGKPTLELRDLSAGYpGAPPVLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPLQGEVTLDGVPVSSLDQD-E 406
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 85 VCPRIAWMPQGlgKNLYHTlSVYENVdffaRLFGHDKAEREVRinELLTSTGLAPF-RDRPAG----------KLSGGMK 153
Cdd:TIGR02868 407 VRRRVSVCAQD--AHLFDT-TVRENL----RLARPDATDEELW--AALERVGLADWlRALPDGldtvlgeggaRLSGGER 477
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 732682709 154 QKLGLCCALIHDPELLILDEPTTGVDPLSRSQfwdLIDSIRQRQSNMSVLVAT 206
Cdd:TIGR02868 478 QRLALARALLADAPILLLDEPTEHLDAETADE---LLEDLLAALSGRTVVLIT 527
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
27-261 |
2.49e-18 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 86.33 E-value: 2.49e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 27 ALNNITLDIPARCMVGLIGPDGVGKSSLLSLISGARVIEQGNVMVlgGDM-----RDPKHRRDVCPRIAWMPQGLGKNLY 101
Cdd:PRK13643 21 ALFDIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVTV--GDIvvsstSKQKEIKPVRKKVGVVFQFPESQLF 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 102 HTlSVYENVDFFARLFGHDKAEREVRINELLTSTGLAP-FRDRPAGKLSGGMKQKLGLCCALIHDPELLILDEPTTGVDP 180
Cdd:PRK13643 99 EE-TVLKDVAFGPQNFGIPKEKAEKIAAEKLEMVGLADeFWEKSPFELSGGQMRRVAIAGILAMEPEVLVLDEPTAGLDP 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 181 LSRSQFWDLIDSIrqRQSNMSVLVATAYMEE-AERFDWLVAMNAGEVLATGSAEELRQQTQSATLEEAFInllPQAQRQA 259
Cdd:PRK13643 178 KARIEMMQLFESI--HQSGQTVVLVTHLMDDvADYADYVYLLEKGHIISCGTPSDVFQEVDFLKAHELGV---PKATHFA 252
|
..
gi 732682709 260 HQ 261
Cdd:PRK13643 253 DQ 254
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
290-507 |
2.97e-18 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 85.37 E-value: 2.97e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 290 VAVDH----VNFRIPRGEIFGFLGSNGCGKSTTMKMLTGLLPaSEGEAWLFGQPVDPKDIDT--RRRvGYMSQAFSLYNE 363
Cdd:PRK03695 6 VAVSTrlgpLSAEVRAGEILHLVGPNGAGKSTLLARMAGLLP-GSGSIQFAGQPLEAWSAAElaRHR-AYLSQQQTPPFA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 364 LTVRQNLELHaRLFHIPEAEIPARVAEMSERFKLndvEDILPES---LPLGIRQRLSLAVAV--IHR---PE--MLILDE 433
Cdd:PRK03695 84 MPVFQYLTLH-QPDKTRTEAVASALNEVAEALGL---DDKLGRSvnqLSGGEWQRVRLAAVVlqVWPdinPAgqLLLLDE 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 732682709 434 PTSGVDPVARDMFWQLMVDLSRQDkVTIFISTHFMNE-AERCDRISLMHAGKVLASGTPQELVEKRGaasLEEAF 507
Cdd:PRK03695 160 PMNSLDVAQQAALDRLLSELCQQG-IAVVMSSHDLNHtLRHADRVWLLKQGKLLASGRRDEVLTPEN---LAQVF 230
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
14-266 |
3.41e-18 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 85.81 E-value: 3.41e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 14 QLAGVSQHYGK-TVALNNITLDIPARCMVGLIGPDGVGKSSLLSLISGARVIEQGNVMVLGGDMRDPKHRRDVCPRIAWM 92
Cdd:PRK13644 3 RLENVSYSYPDgTPALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLVSGIDTGDFSKLQGIRKLVGIV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 93 PQGlGKNLYHTLSVYENVDFFARLFGHDKAEREVRINELLTSTGLAPFRDRPAGKLSGGMKQKLGLCCALIHDPELLILD 172
Cdd:PRK13644 83 FQN-PETQFVGRTVEEDLAFGPENLCLPPIEIRKRVDRALAEIGLEKYRHRSPKTLSGGQGQCVALAGILTMEPECLIFD 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 173 EPTTGVDPLSRSQFWDLIDSIRQRqsNMSVLVATAYMEEAERFDWLVAMNAGEVLATGSAEELRQQTQSATLEEAFINLL 252
Cdd:PRK13644 162 EVTSMLDPDSGIAVLERIKKLHEK--GKTIVYITHNLEELHDADRIIVMDRGKIVLEGEPENVLSDVSLQTLGLTPPSLI 239
|
250
....*....|....
gi 732682709 253 PQAQRQAHQAVVIP 266
Cdd:PRK13644 240 ELAENLKMHGVVIP 253
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
295-490 |
3.62e-18 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 84.48 E-value: 3.62e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 295 VNFRIPRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGEAWLFGQPVDPKDIDTR-----RRVGYMSQAFSLYNELTVRQN 369
Cdd:PRK11629 28 VSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPMSKLSSAAKaelrnQKLGFIYQFHHLLPDFTALEN 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 370 LELHARLFHIPEAEIPARVAEMSERFKLNDVEDILPESLPLGIRQRLSLAVAVIHRPEMLILDEPTSGVDPVARDMFWQL 449
Cdd:PRK11629 108 VAMPLLIGKKKPAEINSRALEMLAAVGLEHRANHRPSELSGGERQRVAIARALVNNPRLVLADEPTGNLDARNADSIFQL 187
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 732682709 450 MVDLSRQDKVTIFISTHFMNEAERCDRISLMHAGKVLASGT 490
Cdd:PRK11629 188 LGELNRLQGTAFLVVTHDLQLAKRMSRQLEMRDGRLTAELS 228
|
|
| type_I_sec_PrtD |
TIGR01842 |
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in ... |
295-497 |
3.70e-18 |
|
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: 88.94 E-value: 3.70e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 295 VNFRIPRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGEAWLFGQPVDPKDIDT-RRRVGYMSQAFSLYnELTVRQNLELH 373
Cdd:TIGR01842 337 ISFSLQAGEALAIIGPSGSGKSTLARLIVGIWPPTSGSVRLDGADLKQWDRETfGKHIGYLPQDVELF-PGTVAENIARF 415
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 374 ARLF---HIPEAEIPARVAEMSERFKLNDVEDILPESLPL--GIRQRLSLAVAVIHRPEMLILDEPTSGVDPVARDMFWQ 448
Cdd:TIGR01842 416 GENAdpeKIIEAAKLAGVHELILRLPDGYDTVIGPGGATLsgGQRQRIALARALYGDPKLVVLDEPNSNLDEEGEQALAN 495
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 732682709 449 LMVDLSRQDKVTIFIsTHFMNEAERCDRISLMHAGKVLASGTPQELVEK 497
Cdd:TIGR01842 496 AIKALKARGITVVVI-THRPSLLGCVDKILVLQDGRIARFGERDEVLAK 543
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
281-494 |
4.35e-18 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 85.44 E-value: 4.35e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 281 DLTMRFGSFVAVDHVNFRIPRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGEAWLFGQPVdpkDIDTRRRVGYMSQAFSL 360
Cdd:PRK13638 6 DLWFRYQDEPVLKGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLRPQKGAVLWQGKPL---DYSKRGLLALRQQVATV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 361 YNE-------LTVRQNLELHARLFHIPEAEIPARVAEM-----SERFKLNDVedilpESLPLGIRQRLSLAVAVIHRPEM 428
Cdd:PRK13638 83 FQDpeqqifyTDIDSDIAFSLRNLGVPEAEITRRVDEAltlvdAQHFRHQPI-----QCLSHGQKKRVAIAGALVLQARY 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 732682709 429 LILDEPTSGVDPVARDMFWQLMVDLSRQDKvTIFISTHFMNEA-ERCDRISLMHAGKVLASGTPQEL 494
Cdd:PRK13638 158 LLLDEPTAGLDPAGRTQMIAIIRRIVAQGN-HVIISSHDIDLIyEISDAVYVLRQGQILTHGAPGEV 223
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
28-249 |
5.67e-18 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 84.71 E-value: 5.67e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 28 LNNITLDIPARCMVGLIGPDGVGKSSLLSLISgaRVIE--------QGNVMVLGGDMR--DPKHRRDVCPRIAWMPqglg 97
Cdd:PRK14246 26 LKDITIKIPNNSIFGIMGPSGSGKSTLLKVLN--RLIEiydskikvDGKVLYFGKDIFqiDAIKLRKEVGMVFQQP---- 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 98 kNLYHTLSVYENVDFFARLFG-HDKAEREVRINELLTSTGL-APFRDR---PAGKLSGGMKQKLGLCCALIHDPELLILD 172
Cdd:PRK14246 100 -NPFPHLSIYDNIAYPLKSHGiKEKREIKKIVEECLRKVGLwKEVYDRlnsPASQLSGGQQQRLTIARALALKPKVLLMD 178
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 732682709 173 EPTTGVDPLSRSQFWDLIDSIRQRqsnMSVLVATAYMEEAERF-DWLVAMNAGEVLATGSAEELRQQTQSATLEEAFI 249
Cdd:PRK14246 179 EPTSMIDIVNSQAIEKLITELKNE---IAIVIVSHNPQQVARVaDYVAFLYNGELVEWGSSNEIFTSPKNELTEKYVI 253
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
25-260 |
6.02e-18 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 85.13 E-value: 6.02e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 25 TVALNNITLDIPARCMVGLIGPDGVGKSSLLSLISGARVIEQGNVMVLGGDMR-DPKHRRDVCPRIAWMPQGLGKNLYHT 103
Cdd:PRK13639 15 TEALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIKGEPIKyDKKSLLEVRKTVGIVFQNPDDQLFAP 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 104 lSVYENVDFFARLFGHDKAEREVRINELLTSTGLAPFRDRPAGKLSGGMKQKLGLCCALIHDPELLILDEPTTGVDPLSR 183
Cdd:PRK13639 95 -TVEEDVAFGPLNLGLSKEEVEKRVKEALKAVGMEGFENKPPHHLSGGQKKRVAIAGILAMKPEIIVLDEPTSGLDPMGA 173
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 732682709 184 SQFWDLIDSIRQRqsNMSVLVATAYMEEAERF-DWLVAMNAGEVLATGSAEELRqqTQSATLEEAfiNL-LPqaqRQAH 260
Cdd:PRK13639 174 SQIMKLLYDLNKE--GITIIISTHDVDLVPVYaDKVYVMSDGKIIKEGTPKEVF--SDIETIRKA--NLrLP---RVAH 243
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
27-240 |
6.38e-18 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 85.07 E-value: 6.38e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 27 ALNNITLDIPARCMVGLIGPDGVGKSSLLSLISGARVIEQGNVMvLGGDM----RDPKHRRDVCPRIAWMPQGLGKNLYH 102
Cdd:PRK13634 22 ALYDVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVT-IGERVitagKKNKKLKPLRKKVGIVFQFPEHQLFE 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 103 TlSVYENVDFFARLFGHDKAEREVRINELLTSTGLAP-FRDRPAGKLSGGMKQKLGLCCALIHDPELLILDEPTTGVDPL 181
Cdd:PRK13634 101 E-TVEKDICFGPMNFGVSEEDAKQKAREMIELVGLPEeLLARSPFELSGGQMRRVAIAGVLAMEPEVLVLDEPTAGLDPK 179
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 182 SRSQFWDLIDSIRQRQsNMSVLVATAYMEEAERF-DWLVAMNAGEVLATGSAEELRQQTQ 240
Cdd:PRK13634 180 GRKEMMEMFYKLHKEK-GLTTVLVTHSMEDAARYaDQIVVMHKGTVFLQGTPREIFADPD 238
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
10-226 |
6.44e-18 |
|
Second domain of the ATP-binding cassette component of monosaccharide transport system; This family represents domain II of the carbohydrate uptake proteins that transport only monosaccharides (Monos). The Carb_Monos family is involved in the uptake of monosaccharides, such as pentoses (such as xylose, arabinose, and ribose) and hexoses (such as xylose, arabinose, and ribose), that cannot be broken down to simple sugars by hydrolysis. In members of Carb_Monos family the single hydrophobic gene product forms a homodimer, while the ABC protein represents a fusion of two nucleotide-binding domains. However, it is assumed that two copies of the ABC domains are present in the assembled transporter.
Pssm-ID: 213182 [Multi-domain] Cd Length: 182 Bit Score: 82.48 E-value: 6.44e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 10 PPVAQLAGVSQHYgktvALNNITLDIPARCMVGLIGPDGVGKSSLLSLISGARVIEQGNVMVLGGDMRDPKHRRDVCPRI 89
Cdd:cd03215 2 EPVLEVRGLSVKG----AVRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITLDGKPVTRRSPRDAIRAGI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 90 AWMP---QGLGknLYHTLSVYENVdFFARLfghdkaerevrinelltstglapfrdrpagkLSGGMKQKLGLCCALIHDP 166
Cdd:cd03215 78 AYVPedrKREG--LVLDLSVAENI-ALSSL-------------------------------LSGGNQQKVVLARWLARDP 123
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 732682709 167 ELLILDEPTTGVDPLSRSQFWDLIDSIRQRqsNMSVLVATAYMEEAERF-DWLVAMNAGEV 226
Cdd:cd03215 124 RVLILDEPTRGVDVGAKAEIYRLIRELADA--GKAVLLISSELDELLGLcDRILVMYEGRI 182
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
269-499 |
7.47e-18 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 88.34 E-value: 7.47e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 269 QPENAEIAIEARDLTMRF--GSFVAVDHVNFRIPRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGEAWLFGQPVDPKDID 346
Cdd:PRK11160 331 TAAADQVSLTLNNVSFTYpdQPQPVLKGLSLQIKAGEKVALLGRTGCGKSTLLQLLTRAWDPQQGEILLNGQPIADYSEA 410
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 347 T-RRRVGYMSQAFSLYNElTVRQNLELharlfhipeAEIPARVAEMSErfKLNDV--EDILPESLPL------GIRQ--- 414
Cdd:PRK11160 411 AlRQAISVVSQRVHLFSA-TLRDNLLL---------AAPNASDEALIE--VLQQVglEKLLEDDKGLnawlgeGGRQlsg 478
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 415 ----RLSLAVAVIHRPEMLILDEPTSGVDPVARDMFWQLMVDLSrQDKVTIFIsTHFMNEAERCDRISLMHAGKVLASGT 490
Cdd:PRK11160 479 geqrRLGIARALLHDAPLLLLDEPTEGLDAETERQILELLAEHA-QNKTVLMI-THRLTGLEQFDRICVMDNGQIIEQGT 556
|
....*....
gi 732682709 491 PQELVEKRG 499
Cdd:PRK11160 557 HQELLAQQG 565
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
14-252 |
8.31e-18 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 83.91 E-value: 8.31e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 14 QLAGVSQHYGKTVALNNITLDIPARCMVGLIGPDGVGKSSLLSLISGARVIEQGNVMVLGG--DMR---DPKH----RRD 84
Cdd:PRK11124 4 QLNGINCFYGAHQALFDITLDCPQGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLNIAGNhfDFSktpSDKAirelRRN 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 85 VcpriawmpqGL---GKNLYHTLSVYEN-VDFFARLFGHDKAEREVRINELLTSTGLAPFRDRPAGKLSGGMKQKLGLCC 160
Cdd:PRK11124 84 V---------GMvfqQYNLWPHLTVQQNlIEAPCRVLGLSKDQALARAEKLLERLRLKPYADRFPLHLSGGQQQRVAIAR 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 161 ALIHDPELLILDEPTTGVDPLSRSQFWDLIDSIrqRQSNMSVLVATAYMEEAERF-DWLVAMNAGEVLATGSAEELRQ-Q 238
Cdd:PRK11124 155 ALMMEPQVLLFDEPTAALDPEITAQIVSIIREL--AETGITQVIVTHEVEVARKTaSRVVYMENGHIVEQGDASCFTQpQ 232
|
250
....*....|....
gi 732682709 239 TqsatleEAFINLL 252
Cdd:PRK11124 233 T------EAFKNYL 240
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
15-235 |
9.87e-18 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 84.67 E-value: 9.87e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 15 LAGVSQHYGKTV-----ALNNITLDIPARCMVGLIGPDGVGKSSLLSLISGARVIEQGNVMVlgGDMRDP------KHRR 83
Cdd:PRK13645 9 LDNVSYTYAKKTpfefkALNNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGLIISETGQTIV--GDYAIPanlkkiKEVK 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 84 DVCPRIAWMPQGLGKNLYHTlSVYENVDFFARLFGHDKAEREVRINELLTSTGLA-PFRDRPAGKLSGGMKQKLGLCCAL 162
Cdd:PRK13645 87 RLRKEIGLVFQFPEYQLFQE-TIEKDIAFGPVNLGENKQEAYKKVPELLKLVQLPeDYVKRSPFELSGGQKRRVALAGII 165
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 732682709 163 IHDPELLILDEPTTGVDPLSRSQFWDLIDSIRQRQSNMSVLVaTAYMEEAERF-DWLVAMNAGEVLATGSAEEL 235
Cdd:PRK13645 166 AMDGNTLVLDEPTGGLDPKGEEDFINLFERLNKEYKKRIIMV-THNMDQVLRIaDEVIVMHEGKVISIGSPFEI 238
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
277-494 |
1.07e-17 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 87.41 E-value: 1.07e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 277 IEARDLTMRFGSFVAVDHVNFRIPRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGEAWLFGQPVDPKDIDTRRRVG-YM- 354
Cdd:PRK15439 12 LCARSISKQYSGVEVLKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIGGNPCARLTPAKAHQLGiYLv 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 355 SQAFSLYNELTVRQNLelharLFHIP-----EAEIPARVAEMSERFKLndveDILPESLPLGIRQRLSLAVAVIHRPEML 429
Cdd:PRK15439 92 PQEPLLFPNLSVKENI-----LFGLPkrqasMQKMKQLLAALGCQLDL----DSSAGSLEVADRQIVEILRGLMRDSRIL 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 732682709 430 ILDEPTSGVDPVARDMFWQLMVDLSRQDKVTIFIStHFMNEA-ERCDRISLMHAGKVLASGTPQEL 494
Cdd:PRK15439 163 ILDEPTASLTPAETERLFSRIRELLAQGVGIVFIS-HKLPEIrQLADRISVMRDGTIALSGKTADL 227
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
27-238 |
1.20e-17 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 84.03 E-value: 1.20e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 27 ALNNITLDIPARCMVGLIGPDGVGKSSLLSLISGARVIEQGNVMVLGGDMRDPKHRRDVCP---RIAWMPQGLGKNLYHT 103
Cdd:PRK13649 22 ALFDVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDDTLITSTSKNKDIKQirkKVGLVFQFPESQLFEE 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 104 lSVYENVDFFARLFGHDKAEREVRINELLTSTGLAP-FRDRPAGKLSGGMKQKLGLCCALIHDPELLILDEPTTGVDPLS 182
Cdd:PRK13649 102 -TVLKDVAFGPQNFGVSQEEAEALAREKLALVGISEsLFEKNPFELSGGQMRRVAIAGILAMEPKILVLDEPTAGLDPKG 180
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 732682709 183 RSQFWDLIDSIrqRQSNMSVLVATAYMEE-AERFDWLVAMNAGEVLATGSAEELRQQ 238
Cdd:PRK13649 181 RKELMTLFKKL--HQSGMTIVLVTHLMDDvANYADFVYVLEKGKLVLSGKPKDIFQD 235
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
292-494 |
1.36e-17 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 83.60 E-value: 1.36e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 292 VDHVNFRIPRGEIFGFLGSNGCGKSTTMKMLTGLLPA----SEGEAWLFGQPVDPKDIDTRRRVGYMSQAFSLYNELtvr 367
Cdd:PRK10418 19 VHGVSLTLQRGRVLALVGGSGSGKSLTCAAALGILPAgvrqTAGRVLLDGKPVAPCALRGRKIATIMQNPRSAFNPL--- 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 368 QNLELHAR--LFHIPEAEIPARVAEMSERFKLNDVEDIL---PESLPLGIRQRLSLAVAVIHRPEMLILDEPTSGVDPVA 442
Cdd:PRK10418 96 HTMHTHARetCLALGKPADDATLTAALEAVGLENAARVLklyPFEMSGGMLQRMMIALALLCEAPFIIADEPTTDLDVVA 175
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 732682709 443 RDMFWQLMVDLSRQDKVTIFISTHFMNEAERC-DRISLMHAGKVLASGTPQEL 494
Cdd:PRK10418 176 QARILDLLESIVQKRALGMLLVTHDMGVVARLaDDVAVMSHGRIVEQGDVETL 228
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
272-505 |
1.37e-17 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 83.48 E-value: 1.37e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 272 NAEIAIEARDLTMRFGSFVAVDHVNFRIPRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGEAWLFGQPV----------- 340
Cdd:PRK10619 1 MSENKLNVIDLHKRYGEHEVLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNGQTInlvrdkdgqlk 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 341 --DPKDIDT-RRRVGYMSQAFSLYNELTVRQN-LELHARLFHIPEAEIPARVAEMSERFKLND-VEDILPESLPLGIRQR 415
Cdd:PRK10619 81 vaDKNQLRLlRTRLTMVFQHFNLWSHMTVLENvMEAPIQVLGLSKQEARERAVKYLAKVGIDErAQGKYPVHLSGGQQQR 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 416 LSLAVAVIHRPEMLILDEPTSGVDPVARDMFWQLMVDLSRQDKvTIFISTHFMNEAERC-DRISLMHAGKVLASGTPQEL 494
Cdd:PRK10619 161 VSIARALAMEPEVLLFDEPTSALDPELVGEVLRIMQQLAEEGK-TMVVVTHEMGFARHVsSHVIFLHQGKIEEEGAPEQL 239
|
250
....*....|.
gi 732682709 495 VEKRGAASLEE 505
Cdd:PRK10619 240 FGNPQSPRLQQ 250
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
14-195 |
1.50e-17 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 83.14 E-value: 1.50e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 14 QLAGVSQHYGKTVALNNITLDIPARCMVGLIGPDGVGKSSLLSLISGARVIEQGNVMVLGGDM---RDPKHRRdvcprIA 90
Cdd:COG4161 4 QLKNINCFYGSHQALFDINLECPSGETLVLLGPSGAGKSSLLRVLNLLETPDSGQLNIAGHQFdfsQKPSEKA-----IR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 91 WMPQGLGK-----NLYHTLSVYEN-VDFFARLFGHDKAEREVRINELLTSTGLAPFRDRPAGKLSGGMKQKLGLCCALIH 164
Cdd:COG4161 79 LLRQKVGMvfqqyNLWPHLTVMENlIEAPCKVLGLSKEQAREKAMKLLARLRLTDKADRFPLHLSGGQQQRVAIARALMM 158
|
170 180 190
....*....|....*....|....*....|.
gi 732682709 165 DPELLILDEPTTGVDPLSRSQFWDLIDSIRQ 195
Cdd:COG4161 159 EPQVLLFDEPTAALDPEITAQVVEIIRELSQ 189
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
277-505 |
1.67e-17 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 83.21 E-value: 1.67e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 277 IEARDLTMRFGS-----FVAVDHVNFRIPRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGEAWLFGQPVdpkdidTR--- 348
Cdd:COG1101 2 LELKNLSKTFNPgtvneKRALDGLNLTIEEGDFVTVIGSNGAGKSTLLNAIAGSLPPDSGSILIDGKDV------TKlpe 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 349 -RRVGYMSQAFSlyN-------ELTVRQNLEL-----HARLFHIpeAEIPARVAEMSERFKL--NDVEDILP---ESLPL 410
Cdd:COG1101 76 yKRAKYIGRVFQ--DpmmgtapSMTIEENLALayrrgKRRGLRR--GLTKKRRELFRELLATlgLGLENRLDtkvGLLSG 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 411 GIRQRLSLAVAVIHRPEMLILDEPTSGVDPVARDMFWQLMVDLSRQDKVTIFISTHFMNEAERC-DRISLMHAGKVL--A 487
Cdd:COG1101 152 GQRQALSLLMATLTKPKLLLLDEHTAALDPKTAALVLELTEKIVEENNLTTLMVTHNMEQALDYgNRLIMMHEGRIIldV 231
|
250 260
....*....|....*....|....
gi 732682709 488 SG------TPQELVEKRGAASLEE 505
Cdd:COG1101 232 SGeekkklTVEDLLELFEEIRGEE 255
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
289-494 |
1.76e-17 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 83.68 E-value: 1.76e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 289 FVAVDHVNFRIPRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGEAWLFGQPVDPKDID-----TRRRVGYM-----SQAF 358
Cdd:PRK13646 20 HQAIHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVDDITITHKTKDkyirpVRKRIGMVfqfpeSQLF 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 359 slynELTVRQNLELHARLFHIPEAEIPARVAEMSERFKLN-DVEDILPESLPLGIRQRLSLAVAVIHRPEMLILDEPTSG 437
Cdd:PRK13646 100 ----EDTVEREIIFGPKNFKMNLDEVKNYAHRLLMDLGFSrDVMSQSPFQMSGGQMRKIAIVSILAMNPDIIVLDEPTAG 175
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 732682709 438 VDPVARDMFWQLMVDLSRQDKVTIFISTHFMNE-AERCDRISLMHAGKVLASGTPQEL 494
Cdd:PRK13646 176 LDPQSKRQVMRLLKSLQTDENKTIILVSHDMNEvARYADEVIVMKEGSIVSQTSPKEL 233
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
11-235 |
1.92e-17 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 85.27 E-value: 1.92e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 11 PVAQLAGVSQHYGKTVALNNITLDIPARCMVGLIGPDGVGKSSLLSLISGARVIEQGNVMVLGGDMRD-PKHRRDvcprI 89
Cdd:PRK11607 18 PLLEIRNLTKSFDGQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVDLSHvPPYQRP----I 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 90 AWMPQGLGknLYHTLSVYENVDFFARLFGHDKAEREVRINELLTSTGLAPFRDRPAGKLSGGMKQKLGLCCALIHDPELL 169
Cdd:PRK11607 94 NMMFQSYA--LFPHMTVEQNIAFGLKQDKLPKAEIASRVNEMLGLVHMQEFAKRKPHQLSGGQRQRVALARSLAKRPKLL 171
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 732682709 170 ILDEPTTGVDPLSRSQFWDLIDSIRQRQSNMSVLVaTAYMEEAERFDWLVA-MNAGEVLATGSAEEL 235
Cdd:PRK11607 172 LLDEPMGALDKKLRDRMQLEVVDILERVGVTCVMV-THDQEEAMTMAGRIAiMNRGKFVQIGEPEEI 237
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
277-491 |
2.14e-17 |
|
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C is also known as MRP (multidrug resistance-associated protein). Some of the MRP members have five additional transmembrane segments in their N-terminus, but the function of these additional membrane-spanning domains is not clear. The MRP was found in the multidrug-resistance lung cancer cell in which p-glycoprotein was not overexpressed. MRP exports glutathione by drug stimulation, as well as, certain substrates in conjugated forms with anions, such as glutathione, glucuronate, and sulfate.
Pssm-ID: 213211 [Multi-domain] Cd Length: 221 Bit Score: 82.16 E-value: 2.14e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 277 IEARDLTMRF--GSFVAVDHVNFRIPRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGEAWLFGQP---VDPKDIdtRRRV 351
Cdd:cd03244 3 IEFKNVSLRYrpNLPPVLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSILIDGVDiskIGLHDL--RSRI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 352 GYMSQ---AFSLynelTVRQNLELH-----ARLFHIPE-AEIPARVAEMSErfKLNDVEDILPESLPLGIRQRLSLAVAV 422
Cdd:cd03244 81 SIIPQdpvLFSG----TIRSNLDPFgeysdEELWQALErVGLKEFVESLPG--GLDTVVEEGGENLSVGQRQLLCLARAL 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 732682709 423 IHRPEMLILDEPTSGVDP--------VARDMFwqlmvdlsrqDKVTIFISTHFMNEAERCDRISLMHAGKVLASGTP 491
Cdd:cd03244 155 LRKSKILVLDEATASVDPetdaliqkTIREAF----------KDCTVLTIAHRLDTIIDSDRILVLDKGRVVEFDSP 221
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
302-496 |
2.54e-17 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 86.64 E-value: 2.54e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 302 GEIFGFLGSNGCGKSTTMKMLTGLLPAS---EGEAWLFGQPVDPKDIdtRRRVGYMSQAFSLYNELTVRQNLELHARLF- 377
Cdd:TIGR00955 51 GELLAVMGSSGAGKTTLMNALAFRSPKGvkgSGSVLLNGMPIDAKEM--RAISAYVQQDDLFIPTLTVREHLMFQAHLRm 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 378 --HIPEAEIPARVAEMSERFKLNDVEDIL------PESLPLGIRQRLSLAVAVIHRPEMLILDEPTSGVDPVARDMFWQL 449
Cdd:TIGR00955 129 prRVTKKEKRERVDEVLQALGLRKCANTRigvpgrVKGLSGGERKRLAFASELLTDPPLLFCDEPTSGLDSFMAYSVVQV 208
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 732682709 450 MVDLSRQDKvTIFISTH------FmneaERCDRISLMHAGKVLASGTPQELVE 496
Cdd:TIGR00955 209 LKGLAQKGK-TIICTIHqpsselF----ELFDKIILMAEGRVAYLGSPDQAVP 256
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
272-484 |
2.82e-17 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 81.68 E-value: 2.82e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 272 NAEIAIEARDLTMRFGSFVAVDHVNFRIPRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGEAWLFGQPVDPKDIDT-RRR 350
Cdd:PRK10247 3 ENSPLLQLQNVGYLAGDAKILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFEGEDISTLKPEIyRQQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 351 VGYMSQAFSLYNElTVRQNLELHARLFHI-PEaeiPARVAEMSERFKLNdvEDILPES---LPLGIRQRLSLAVAVIHRP 426
Cdd:PRK10247 83 VSYCAQTPTLFGD-TVYDNLIFPWQIRNQqPD---PAIFLDDLERFALP--DTILTKNiaeLSGGEKQRISLIRNLQFMP 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 427 EMLILDEPTSGVDPVARDMFWQLMVDLSRQDKVTIFISTHFMNEAERCDR-ISLM-HAGK 484
Cdd:PRK10247 157 KVLLLDEITSALDESNKHNVNEIIHRYVREQNIAVLWVTHDKDEINHADKvITLQpHAGE 216
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
27-252 |
2.85e-17 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 83.01 E-value: 2.85e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 27 ALNNITLDIPARCMVGLIGPDGVGKSSLLSLISGARVIEQGNVMVLGGDMRDPKHRRdvcpRIAWMPQGLGKNLYHTLSV 106
Cdd:PRK15056 22 ALRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKISILGQPTRQALQKN----LVAYVPQSEEVDWSFPVLV 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 107 yENVDFFARlFGH------DKAEREVRINELLTSTGLAPFRDRPAGKLSGGMKQKLGLCCALIHDPELLILDEPTTGVDP 180
Cdd:PRK15056 98 -EDVVMMGR-YGHmgwlrrAKKRDRQIVTAALARVDMVEFRHRQIGELSGGQKKRVFLARAIAQQGQVILLDEPFTGVDV 175
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 732682709 181 LSRSQFWDLIDSIRQRQSNMsvLVATAYMEEAERFDWLVAMNAGEVLATGSAEelrQQTQSATLEEAFINLL 252
Cdd:PRK15056 176 KTEARIISLLRELRDEGKTM--LVSTHNLGSVTEFCDYTVMVKGTVLASGPTE---TTFTAENLELAFSGVL 242
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
28-212 |
3.46e-17 |
|
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: 81.74 E-value: 3.46e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 28 LNNITLDIPARCMVGLIGPDGVGKSSLLSLISGARVIEQGNVMVLGGDMRDPKHRRDVCPRiawmpqglGKNLYHTLSVY 107
Cdd:TIGR01184 1 LKGVNLTIQQGEFISLIGHSGCGKSTLLNLISGLAQPTSGGVILEGKQITEPGPDRMVVFQ--------NYSLLPWLTVR 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 108 ENVDFFARLFGHD--KAEREVRINELLTSTGLAPFRDRPAGKLSGGMKQKLGLCCALIHDPELLILDEPTTGVDPLSRSQ 185
Cdd:TIGR01184 73 ENIALAVDRVLPDlsKSERRAIVEEHIALVGLTEAADKRPGQLSGGMKQRVAIARALSIRPKVLLLDEPFGALDALTRGN 152
|
170 180
....*....|....*....|....*..
gi 732682709 186 FWDLIDSIRQrQSNMSVLVATAYMEEA 212
Cdd:TIGR01184 153 LQEELMQIWE-EHRVTVLMVTHDVDEA 178
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
270-491 |
3.78e-17 |
|
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type transporter 1). NFT1 belongs to the MRP (multidrug resistance-associated protein) family of ABC transporters. Some of the MRP members have five additional transmembrane segments in their N-terminus, but the function of these additional membrane-spanning domains is not clear. The MRP was found in the multidrug-resisting lung cancer cell in which p-glycoprotein was not overexpressed. MRP exports glutathione by drug stimulation, as well as, certain substrates in conjugated forms with anions such as glutathione, glucuronate, and sulfate.
Pssm-ID: 213269 [Multi-domain] Cd Length: 207 Bit Score: 80.92 E-value: 3.78e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 270 PENAEIAIEarDLTMRFGSFV--AVDHVNFRIPRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGEAwlfgqPVDPKDI-- 345
Cdd:cd03369 2 PEHGEIEVE--NLSVRYAPDLppVLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKI-----EIDGIDIst 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 346 ----DTRRRVGYMSQAFSLYNElTVRQNLElhaRLFHIPEAEIPA--RVAEMSerfklndvedilpESLPLGIRQRLSLA 419
Cdd:cd03369 75 ipleDLRSSLTIIPQDPTLFSG-TIRSNLD---PFDEYSDEEIYGalRVSEGG-------------LNLSQGQRQLLCLA 137
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 732682709 420 VAVIHRPEMLILDEPTSGVDpVARDMFWQLMVDLSRQDkVTIFISTHFMNEAERCDRISLMHAGKVLASGTP 491
Cdd:cd03369 138 RALLKRPRVLVLDEATASID-YATDALIQKTIREEFTN-STILTIAHRLRTIIDYDKILVMDAGEVKEYDHP 207
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
287-497 |
4.29e-17 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 83.74 E-value: 4.29e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 287 GSFVAVDHVNFRIPRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGEAWLFGQPV---DPKDidtrRRVGYMSQAFSLYNE 363
Cdd:PRK11650 15 GKTQVIKGIDLDVADGEFIVLVGPSGCGKSTLLRMVAGLERITSGEIWIGGRVVnelEPAD----RDIAMVFQNYALYPH 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 364 LTVRQNLELHARLFHIPEAEIPARVAEMSERFKLNDVEDILPESLPLGIRQRLSLAVAVIHRPEMLILDEPTSGVDPVAR 443
Cdd:PRK11650 91 MSVRENMAYGLKIRGMPKAEIEERVAEAARILELEPLLDRKPRELSGGQRQRVAMGRAIVREPAVFLFDEPLSNLDAKLR 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 732682709 444 -DMFWQLMvDLSRQDKVTIFISTHFMNEA-ERCDRISLMHAGKVLASGTPQELVEK 497
Cdd:PRK11650 171 vQMRLEIQ-RLHRRLKTTSLYVTHDQVEAmTLADRVVVMNGGVAEQIGTPVEVYEK 225
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
28-182 |
4.72e-17 |
|
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: 81.16 E-value: 4.72e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 28 LNNITLDIPARCMVGLIGPDGVGKSSLLSLISGaRVIEQGN---VMVLGGDMRDPKHRRDvcpRIAWMPQGlgKNLYHTL 104
Cdd:cd03234 23 LNDVSLHVESGQVMAILGSSGSGKTTLLDAISG-RVEGGGTtsgQILFNGQPRKPDQFQK---CVAYVRQD--DILLPGL 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 105 SVYENVDFFARLFGH---DKAEREVRI-NELLTSTGLAPFRDRPAGKLSGGMKQKLGLCCALIHDPELLILDEPTTGVDP 180
Cdd:cd03234 97 TVRETLTYTAILRLPrksSDAIRKKRVeDVLLRDLALTRIGGNLVKGISGGERRRVSIAVQLLWDPKVLILDEPTSGLDS 176
|
..
gi 732682709 181 LS 182
Cdd:cd03234 177 FT 178
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
28-235 |
5.46e-17 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 82.06 E-value: 5.46e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 28 LNNITLDIPARCMVGLIGPDGVGKSSLLSLISGARVIEQGnVMVLGGDMRDPKHRRDVCPRIAWMPQGlGKNLYHTLSVY 107
Cdd:PRK13642 23 LNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEG-KVKIDGELLTAENVWNLRRKIGMVFQN-PDNQFVGATVE 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 108 ENVDFFARLFGHDKAEREVRINELLTSTGLAPFRDRPAGKLSGGMKQKLGLCCALIHDPELLILDEPTTGVDPLSRSQFW 187
Cdd:PRK13642 101 DDVAFGMENQGIPREEMIKRVDEALLAVNMLDFKTREPARLSGGQKQRVAVAGIIALRPEIIILDESTSMLDPTGRQEIM 180
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 732682709 188 DLIDSIRQRQsNMSVLVATAYMEEAERFDWLVAMNAGEVLATGSAEEL 235
Cdd:PRK13642 181 RVIHEIKEKY-QLTVLSITHDLDEAASSDRILVMKAGEIIKEAAPSEL 227
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
24-266 |
6.37e-17 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 82.16 E-value: 6.37e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 24 KTVALNNITLDIPARCMVGLIGPDGVGKSSLLSLISGARVIEQGN---VMVLGGDMRDpKHRRDVCPRIAWMPQGlGKNL 100
Cdd:PRK13640 19 KKPALNDISFSIPRGSWTALIGHNGSGKSTISKLINGLLLPDDNPnskITVDGITLTA-KTVWDIREKVGIVFQN-PDNQ 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 101 YHTLSVYENVDFFARLFGHDKAEREVRINELLTSTGLAPFRDRPAGKLSGGMKQKLGLCCALIHDPELLILDEPTTGVDP 180
Cdd:PRK13640 97 FVGATVGDDVAFGLENRAVPRPEMIKIVRDVLADVGMLDYIDSEPANLSGGQKQRVAIAGILAVEPKIIILDESTSMLDP 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 181 LSRSQFWDLIDSIrQRQSNMSVLVATAYMEEAERFDWLVAMNAGEVLATGSAEELRQQT---QSATLEEAFINLLPQAQR 257
Cdd:PRK13640 177 AGKEQILKLIRKL-KKKNNLTVISITHDIDEANMADQVLVLDDGKLLAQGSPVEIFSKVemlKEIGLDIPFVYKLKNKLK 255
|
....*....
gi 732682709 258 QahQAVVIP 266
Cdd:PRK13640 256 E--KGISVP 262
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
269-494 |
6.53e-17 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 82.83 E-value: 6.53e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 269 QPENAEIAIEARDLTMRFG-------------SFVAVDHVNFRIPRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGE-AW 334
Cdd:PRK15079 1 VTEGKKVLLEVADLKVHFDikdgkqwfwqppkTLKAVDGVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGEvAW 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 335 LfGQPV---DPKDI-DTRRRVGYMSQ--AFSLYNELTVRQNLELHARLFH--IPEAEIPARVAEMSERFKL-NDVEDILP 405
Cdd:PRK15079 81 L-GKDLlgmKDDEWrAVRSDIQMIFQdpLASLNPRMTIGEIIAEPLRTYHpkLSRQEVKDRVKAMMLKVGLlPNLINRYP 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 406 ESLPLGIRQRLSLAVAVIHRPEMLILDEPTSGVDPVARDMFWQLMVDLSRQDKVT-IFISTHFMNEAERCDRISLMHAGK 484
Cdd:PRK15079 160 HEFSGGQCQRIGIARALILEPKLIICDEPVSALDVSIQAQVVNLLQQLQREMGLSlIFIAHDLAVVKHISDRVLVMYLGH 239
|
250
....*....|
gi 732682709 485 VLASGTPQEL 494
Cdd:PRK15079 240 AVELGTYDEV 249
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
277-496 |
6.55e-17 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 82.44 E-value: 6.55e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 277 IEARDLTMRFGS-----FVAVDHVNFRIPRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGEA-WLFGQPVDPKDIDT--- 347
Cdd:PRK13651 3 IKVKNIVKIFNKklpteLKALDNVSVEINQGEFIAIIGQTGSGKTTFIEHLNALLLPDTGTIeWIFKDEKNKKKTKEkek 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 348 ---------------------RRRVGYMSQaFSLYN--ELTVRQNLELHARLFHIPEAEIPARVAEMSERFKLNdvEDIL 404
Cdd:PRK13651 83 vleklviqktrfkkikkikeiRRRVGVVFQ-FAEYQlfEQTIEKDIIFGPVSMGVSKEEAKKRAAKYIELVGLD--ESYL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 405 PES---LPLGIRQRLSLAVAVIHRPEMLILDEPTSGVDPVARDMFWQLMVDLSRQDKvTIFISTHFMNEA-ERCDRISLM 480
Cdd:PRK13651 160 QRSpfeLSGGQKRRVALAGILAMEPDFLVFDEPTAGLDPQGVKEILEIFDNLNKQGK-TIILVTHDLDNVlEWTKRTIFF 238
|
250
....*....|....*.
gi 732682709 481 HAGKVLASGTPQELVE 496
Cdd:PRK13651 239 KDGKIIKDGDTYDILS 254
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
20-248 |
6.59e-17 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 81.76 E-value: 6.59e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 20 QHYGKTVALNNITLDIPARCMV-------------GLIGPDGVGKSSLLSLISGARVIEQGNVMvLGGDMRDPKHRRDVC 86
Cdd:PRK10575 6 NHSDTTFALRNVSFRVPGRTLLhplsltfpagkvtGLIGHNGSGKSTLLKMLGRHQPPSEGEIL-LDAQPLESWSSKAFA 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 87 PRIAWMPQGLGKNlyHTLSVYENVDF----FARLFGHDKAEREVRINELLTSTGLAPFRDRPAGKLSGGMKQKLGLCCAL 162
Cdd:PRK10575 85 RKVAYLPQQLPAA--EGMTVRELVAIgrypWHGALGRFGAADREKVEEAISLVGLKPLAHRLVDSLSGGERQRAWIAMLV 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 163 IHDPELLILDEPTTGVDPLSRSQFWDLIDSIRQrQSNMSVLVATAYMEEAERF-DWLVAMNAGEVLATGSAEELrqqTQS 241
Cdd:PRK10575 163 AQDSRCLLLDEPTSALDIAHQVDVLALVHRLSQ-ERGLTVIAVLHDINMAARYcDYLVALRGGEMIAQGTPAEL---MRG 238
|
....*..
gi 732682709 242 ATLEEAF 248
Cdd:PRK10575 239 ETLEQIY 245
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
11-240 |
7.00e-17 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 81.36 E-value: 7.00e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 11 PVAQLAGVSQHYGKTVALNNITLDIPARCMVGLIGPDGVGKSSLLSLIS-----GARVIEQGNVMVLGGDMRDPKHRR-D 84
Cdd:PRK14239 4 PILQVSDLSVYYNKKKALNSVSLDFYPNEITALIGPSGSGKSTLLRSINrmndlNPEVTITGSIVYNGHNIYSPRTDTvD 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 85 VCPRIAWMPQGlgKNLYhTLSVYENVDFFARLFG-HDKAEREVRINELLTSTGL-APFRDR---PAGKLSGGMKQKLGLC 159
Cdd:PRK14239 84 LRKEIGMVFQQ--PNPF-PMSIYENVVYGLRLKGiKDKQVLDEAVEKSLKGASIwDEVKDRlhdSALGLSGGQQQRVCIA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 160 CALIHDPELLILDEPTTGVDPLSRSQFWDLIDSIRQRqsnMSVLVATAYMEEAERF-DWLVAMNAGEVLATGSAEEL--- 235
Cdd:PRK14239 161 RVLATSPKIILLDEPTSALDPISAGKIEETLLGLKDD---YTMLLVTRSMQQASRIsDRTGFFLDGDLIEYNDTKQMfmn 237
|
....*..
gi 732682709 236 --RQQTQ 240
Cdd:PRK14239 238 pkHKETE 244
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
278-484 |
8.22e-17 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 84.46 E-value: 8.22e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 278 EARDLTMRFGSFVAVDHVNFRIPRGEIFGFLGSNGCGKSTTMKMLTGLLPAS--EGEAWLFGQPVDPKDIDTRRRVG--Y 353
Cdd:NF040905 3 EMRGITKTFPGVKALDDVNLSVREGEIHALCGENGAGKSTLMKVLSGVYPHGsyEGEILFDGEVCRFKDIRDSEALGivI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 354 MSQAFSLYNELTVRQNLEL---HARLFHIPEAEIPARVAEMSERFKLNDVEDILPESLPLGIRQRLSLAVAVIHRPEMLI 430
Cdd:NF040905 83 IHQELALIPYLSIAENIFLgneRAKRGVIDWNETNRRARELLAKVGLDESPDTLVTDIGVGKQQLVEIAKALSKDVKLLI 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 732682709 431 LDEPTSGVDPVARDMFWQLMVDLSRQDKVTIFIStHFMNEAER-CDRISLMHAGK 484
Cdd:NF040905 163 LDEPTAALNEEDSAALLDLLLELKAQGITSIIIS-HKLNEIRRvADSITVLRDGR 216
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
11-248 |
1.06e-16 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 83.35 E-value: 1.06e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 11 PVAQLAGVSQHYGKTVALNNITLDIPARCMVGLIGPDGVGKSSLLSLISGARVIEQGNVMVlGGDMRDPKHRRDVCPRIA 90
Cdd:PRK09536 2 PMIDVSDLSVEFGDTTVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLV-AGDDVEALSARAASRRVA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 91 WMPQGlgKNLYHTLSVYENVDF-----FARLFGHDKAEREVrINELLTSTGLAPFRDRPAGKLSGGMKQKLGLCCALIHD 165
Cdd:PRK09536 81 SVPQD--TSLSFEFDVRQVVEMgrtphRSRFDTWTETDRAA-VERAMERTGVAQFADRPVTSLSGGERQRVLLARALAQA 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 166 PELLILDEPTTGVDPLSRSQFWDLIDsiRQRQSNMSVLVATAYMEEAERF-DWLVAMNAGEVLATGSAEELrqqTQSATL 244
Cdd:PRK09536 158 TPVLLLDEPTASLDINHQVRTLELVR--RLVDDGKTAVAAIHDLDLAARYcDELVLLADGRVRAAGPPADV---LTADTL 232
|
....
gi 732682709 245 EEAF 248
Cdd:PRK09536 233 RAAF 236
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
28-197 |
1.13e-16 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 79.83 E-value: 1.13e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 28 LNNITLDIPARCMVG-------------LIGPDGVGKSSLLSLISGA---RVIEQGNVMVLGGDMRD-PKHRRdvcpRIA 90
Cdd:COG4136 4 LENLTITLGGRPLLAplsltvapgeiltLMGPSGSGKSTLLAAIAGTlspAFSASGEVLLNGRRLTAlPAEQR----RIG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 91 WMPQ-GLgknLYHTLSVYENVdffarLFG----HDKAEREVRINELLTSTGLAPFRDRPAGKLSGGMKQKLGLCCALIHD 165
Cdd:COG4136 80 ILFQdDL---LFPHLSVGENL-----AFAlpptIGRAQRRARVEQALEEAGLAGFADRDPATLSGGQRARVALLRALLAE 151
|
170 180 190
....*....|....*....|....*....|...
gi 732682709 166 PELLILDEPTTGVDPLSRSQFWDLI-DSIRQRQ 197
Cdd:COG4136 152 PRALLLDEPFSKLDAALRAQFREFVfEQIRQRG 184
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
273-522 |
1.13e-16 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 81.08 E-value: 1.13e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 273 AEIAIEARDLTMRFGSfVAVDHVNFRIPRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGEAWLFGQPVdpKDIDTRRRVG 352
Cdd:PRK15056 5 AGIVVNDVTVTWRNGH-TALRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKISILGQPT--RQALQKNLVA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 353 YMSQ------AFSLYNELTVRQNLELHARLFHIPEAEIPARVAEMSERFKLNDVEDILPESLPLGIRQRLSLAVAVIHRP 426
Cdd:PRK15056 82 YVPQseevdwSFPVLVEDVVMMGRYGHMGWLRRAKKRDRQIVTAALARVDMVEFRHRQIGELSGGQKKRVFLARAIAQQG 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 427 EMLILDEPTSGVDPVARDMFWQLMVDLsRQDKVTIFISTHFMNE-AERCDrISLMHAGKVLASGtPQELVEKrgAASLEE 505
Cdd:PRK15056 162 QVILLDEPFTGVDVKTEARIISLLREL-RDEGKTMLVSTHNLGSvTEFCD-YTVMVKGTVLASG-PTETTFT--AENLEL 236
|
250
....*....|....*..
gi 732682709 506 AFIAYLQEAAGQSNEAE 522
Cdd:PRK15056 237 AFSGVLRHVALNGSEES 253
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
277-499 |
1.53e-16 |
|
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: 84.41 E-value: 1.53e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 277 IEARDLTMRFG-SFVAVDHVNFRIPRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGEAWLFGQPVDPKDIDT-RRRVGYM 354
Cdd:TIGR01193 474 IVINDVSYSYGyGSNILSDISLTIKMNSKTTIVGMSGSGKSTLAKLLVGFFQARSGEILLNGFSLKDIDRHTlRQFINYL 553
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 355 SQAFSLYNElTVRQNLELHAR--------LFHIPEAEIPARVAEMSERFKLNDVEDilPESLPLGIRQRLSLAVAVIHRP 426
Cdd:TIGR01193 554 PQEPYIFSG-SILENLLLGAKenvsqdeiWAACEIAEIKDDIENMPLGYQTELSEE--GSSISGGQKQRIALARALLTDS 630
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 732682709 427 EMLILDEPTSGVDPVARDMFWQLMVDLsrQDKVTIFIStHFMNEAERCDRISLMHAGKVLASGTPQELVEKRG 499
Cdd:TIGR01193 631 KVLILDESTSNLDTITEKKIVNNLLNL--QDKTIIFVA-HRLSVAKQSDKIIVLDHGKIIEQGSHDELLDRNG 700
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
291-497 |
1.54e-16 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 81.32 E-value: 1.54e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 291 AVDHVNFRIPRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGEA----WLFGQPVDPKDID-TRRRVGYMSQ--AFSLYNE 363
Cdd:PRK13643 21 ALFDIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVtvgdIVVSSTSKQKEIKpVRKKVGVVFQfpESQLFEE 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 364 lTVRQNLELHARLFHIPEAEIPARVAEMSERFKLN-DVEDILPESLPLGIRQRLSLAVAVIHRPEMLILDEPTSGVDPVA 442
Cdd:PRK13643 101 -TVLKDVAFGPQNFGIPKEKAEKIAAEKLEMVGLAdEFWEKSPFELSGGQMRRVAIAGILAMEPEVLVLDEPTAGLDPKA 179
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 732682709 443 RDMFWQLMVDLsRQDKVTIFISTHFMNE-AERCDRISLMHAGKVLASGTPQELVEK 497
Cdd:PRK13643 180 RIEMMQLFESI-HQSGQTVVLVTHLMDDvADYADYVYLLEKGHIISCGTPSDVFQE 234
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
26-235 |
1.84e-16 |
|
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a central component of the secretion machinery that translocates the toxin, hemolysin A, in a Sec-independent fashion across both membranes of E. coli. The hemolysin A (HlyA) transport machinery is composed of the ATP-binding cassette (ABC) transporter HlyB located in the inner membrane, hemolysin D (HlyD), also anchored in the inner membrane, and TolC, which resides in the outer membrane. HlyD apparently forms a continuous channel that bridges the entire periplasm, interacting with TolC and HlyB. This arrangement prevents the appearance of periplasmic intermediates of HlyA during substrate transport. Little is known about the molecular details of HlyA transport, but it is evident that ATP-hydrolysis by the ABC-transporter HlyB is a necessary source of energy.
Pssm-ID: 213219 [Multi-domain] Cd Length: 237 Bit Score: 79.84 E-value: 1.84e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 26 VALNNITLDIPARCMVGLIGPDGVGKSSLLSLISGARVIEQGNVMVLGGDMR--DPkhrrdvcpriAWMPQGLG----KN 99
Cdd:cd03252 16 VILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGHDLAlaDP----------AWLRRQVGvvlqEN 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 100 LYHTLSVYENVDFfarlfGHDKAEREvRINELLTSTGLAPF-RDRPAG----------KLSGGMKQKLGLCCALIHDPEL 168
Cdd:cd03252 86 VLFNRSIRDNIAL-----ADPGMSME-RVIEAAKLAGAHDFiSELPEGydtivgeqgaGLSGGQRQRIAIARALIHNPRI 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 732682709 169 LILDEPTTGVDPLSRSqfwDLIDSIRQRQSNMSVLVATAYMEEAERFDWLVAMNAGEVLATGSAEEL 235
Cdd:cd03252 160 LIFDEATSALDYESEH---AIMRNMHDICAGRTVIIIAHRLSTVKNADRIIVMEKGRIVEQGSHDEL 223
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
23-248 |
1.88e-16 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 79.94 E-value: 1.88e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 23 GKTVaLNNITLDIPARCMVGLIGPDGVGKSSLLSLISGARVIEQGNVMVLGGDMRD-PKHRRdVCPRIAWMPQGlgKNLY 101
Cdd:PRK10895 15 GRRV-VEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEDISLlPLHAR-ARRGIGYLPQE--ASIF 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 102 HTLSVYENVDFFARLFGHDKAE-REVRINELLTSTGLAPFRDRPAGKLSGGMKQKLGLCCALIHDPELLILDEPTTGVDP 180
Cdd:PRK10895 91 RRLSVYDNLMAVLQIRDDLSAEqREDRANELMEEFHIEHLRDSMGQSLSGGERRRVEIARALAANPKFILLDEPFAGVDP 170
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 732682709 181 LSRSQFWDLIDSIrqRQSNMSVLVATAYMEEA----ERfDWLVAMnaGEVLATGSAEEL--RQQTQSATLEEAF 248
Cdd:PRK10895 171 ISVIDIKRIIEHL--RDSGLGVLITDHNVRETlavcER-AYIVSQ--GHLIAHGTPTEIlqDEHVKRVYLGEDF 239
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
292-485 |
1.99e-16 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 80.50 E-value: 1.99e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 292 VDHVNFRIPRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGEAWLFGQPVDPKD----IDTRRRVGYMSQ-AFSLYN-ELT 365
Cdd:PRK10419 28 LNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWRGEPLAKLNraqrKAFRRDIQMVFQdSISAVNpRKT 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 366 VRQNLELHAR-LFHIPEAEIPARVAEMSERFKLND-VEDILPESLPLGIRQRLSLAVAVIHRPEMLILDEPTSGVDPVAR 443
Cdd:PRK10419 108 VREIIREPLRhLLSLDKAERLARASEMLRAVDLDDsVLDKRPPQLSGGQLQRVCLARALAVEPKLLILDEAVSNLDLVLQ 187
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 732682709 444 DMFWQLMVDLSRQ-DKVTIFIsTHFMNEAER-CDRISLMHAGKV 485
Cdd:PRK10419 188 AGVIRLLKKLQQQfGTACLFI-THDLRLVERfCQRVMVMDNGQI 230
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
12-235 |
2.28e-16 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 80.06 E-value: 2.28e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 12 VAQLAGVSQHYGKTVALNNITLDIPARCMVGLIGPDGVGKSSLL----SLISGARVIEQgNVMVLGGDM-RDPKHRRDVC 86
Cdd:PRK09984 4 IIRVEKLAKTFNQHQALHAVDLNIHHGEMVALLGPSGSGKSTLLrhlsGLITGDKSAGS-HIELLGRTVqREGRLARDIR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 87 PRIA---WMPQGLgkNLYHTLSVYENV--------DFFARLFGHDKAEREVRINELLTSTGLAPFRDRPAGKLSGGMKQK 155
Cdd:PRK09984 83 KSRAntgYIFQQF--NLVNRLSVLENVligalgstPFWRTCFSWFTREQKQRALQALTRVGMVHFAHQRVSTLSGGQQQR 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 156 LGLCCALIHDPELLILDEPTTGVDPLSRSQFWDLIDSIRQrQSNMSVLVATAYMEEAERF-DWLVAMNAGEVLATGSAEE 234
Cdd:PRK09984 161 VAIARALMQQAKVILADEPIASLDPESARIVMDTLRDINQ-NDGITVVVTLHQVDYALRYcERIVALRQGHVFYDGSSQQ 239
|
.
gi 732682709 235 L 235
Cdd:PRK09984 240 F 240
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
7-234 |
2.48e-16 |
|
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: 79.40 E-value: 2.48e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 7 VPVPPVAQLAGVSQHY----GKTVALNNITLDIPARCMVGLIGPDGVGKSSLLSLISGARVIEQGNVMVLGGDM----RD 78
Cdd:COG4181 3 SSSAPIIELRGLTKTVgtgaGELTILKGISLEVEAGESVAIVGASGSGKSTLLGLLAGLDRPTSGTVRLAGQDLfaldED 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 79 P--KHRRDvcpRIAWMPQGLgkNLYHTLSVYENVDFFARLFGHDKAEREVRinELLTSTGLApfrDR----PAGkLSGGM 152
Cdd:COG4181 83 AraRLRAR---HVGFVFQSF--QLLPTLTALENVMLPLELAGRRDARARAR--ALLERVGLG---HRldhyPAQ-LSGGE 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 153 KQKLGLCCALIHDPELLILDEPTTGVDPLSRSQFWDLIDSIRQRQSNMSVLVaTAYMEEAERFDWLVAMNAGEVLATGSA 232
Cdd:COG4181 152 QQRVALARAFATEPAILFADEPTGNLDAATGEQIIDLLFELNRERGTTLVLV-THDPALAARCDRVLRLRAGRLVEDTAA 230
|
..
gi 732682709 233 EE 234
Cdd:COG4181 231 TA 232
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
27-255 |
2.80e-16 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 80.03 E-value: 2.80e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 27 ALNNITLDIPARCMVGLIGPDGVGKSSLLSLISGARVIEQGNVMVLGGDMRDP--KHRRDVCPRIAWMPQglgkNLYHTL 104
Cdd:PRK13632 24 ALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIDGITISKEnlKEIRKKIGIIFQNPD----NQFIGA 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 105 SVYENVDFFARLFGHDKAEREVRINELLTSTGLAPFRDRPAGKLSGGMKQKLGLCCALIHDPELLILDEPTTGVDPLSRS 184
Cdd:PRK13632 100 TVEDDIAFGLENKKVPPKKMKDIIDDLAKKVGMEDYLDKEPQNLSGGQKQRVAIASVLALNPEIIIFDESTSMLDPKGKR 179
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 732682709 185 QFWDLIDSIRQrQSNMSVLVATAYMEEAERFDWLVAMNAGEVLATGSAEEL---RQQTQSATLEEAFINLLPQA 255
Cdd:PRK13632 180 EIKKIMVDLRK-TRKKTLISITHDMDEAILADKVIVFSEGKLIAQGKPKEIlnnKEILEKAKIDSPFIYKLSKK 252
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
7-238 |
2.83e-16 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 83.29 E-value: 2.83e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 7 VPVPPVA---QLAGVSQHY-GKTVALNNITLDIPARCMVGLIGPDGVGKSSLLSLISGARVIEQGNVMVLGGDMRD--PK 80
Cdd:COG1132 331 VPLPPVRgeiEFENVSFSYpGDRPVLKDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYDPTSGRILIDGVDIRDltLE 410
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 81 HRRDvcpRIAWMPQglgKN-LYHTlSVYENVdffarLFGHDKAEREvRINELLTSTGLAPF-RDRPAG----------KL 148
Cdd:COG1132 411 SLRR---QIGVVPQ---DTfLFSG-TIRENI-----RYGRPDATDE-EVEEAAKAAQAHEFiEALPDGydtvvgergvNL 477
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 149 SGGMKQKLGLCCALIHDPELLILDEPTTGVDPLSRSQfwdLIDSIRQRQSNMSVLV-----ATaymeeAERFDWLVAMNA 223
Cdd:COG1132 478 SGGQRQRIAIARALLKDPPILILDEATSALDTETEAL---IQEALERLMKGRTTIViahrlST-----IRNADRILVLDD 549
|
250
....*....|....*
gi 732682709 224 GEVLATGSAEELRQQ 238
Cdd:COG1132 550 GRIVEQGTHEELLAR 564
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
15-485 |
2.84e-16 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 82.85 E-value: 2.84e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 15 LAGVSQHYGKTVALNNITLDIPARCMVGLIGPDGVGKSSLLSLISGARVIEQGNVMVLGGDMRDPKHRRDVCPRIAWMPQ 94
Cdd:PRK10982 1 MSNISKSFPGVKALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEIDFKSSKEALENGISMVHQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 95 GLgkNLYHTLSVYENV--------DFFArlfGHDKAEREVR--INELltSTGLAPfRDRPAgKLSGGMKQKLGLCCALIH 164
Cdd:PRK10982 81 EL--NLVLQRSVMDNMwlgryptkGMFV---DQDKMYRDTKaiFDEL--DIDIDP-RAKVA-TLSVSQMQMIEIAKAFSY 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 165 DPELLILDEPTTGVDPLSRSQFWDLIDSIRQRqsNMSVLVATAYMEEAERF-DWLVAMNAGEVLATGSAEELrqqtqsaT 243
Cdd:PRK10982 152 NAKIVIMDEPTSSLTEKEVNHLFTIIRKLKER--GCGIVYISHKMEEIFQLcDEITILRDGQWIATQPLAGL-------T 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 244 LEEAFINLLPQAQRQAhqavvIPPYQPENAEIAIEARDLT-MRFGSfvaVDHVNFRIPRGEIFGFLGSNGCGKSTTMKML 322
Cdd:PRK10982 223 MDKIIAMMVGRSLTQR-----FPDKENKPGEVILEVRNLTsLRQPS---IRDVSFDLHKGEILGIAGLVGAKRTDIVETL 294
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 323 TGLLPASEGEAWLFGqpvdpKDIDTRRRVGYMSQAFSLYNEltVRQNLELHARLfHIPEAEIPARVAEMSERFKLNDVED 402
Cdd:PRK10982 295 FGIREKSAGTITLHG-----KKINNHNANEAINHGFALVTE--ERRSTGIYAYL-DIGFNSLISNIRNYKNKVGLLDNSR 366
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 403 ILPE--------------------SLPLGIRQRLSLAVAVIHRPEMLILDEPTSGVDPVARDMFWQLMVDLSRQDKVTIF 462
Cdd:PRK10982 367 MKSDtqwvidsmrvktpghrtqigSLSGGNQQKVIIGRWLLTQPEILMLDEPTRGIDVGAKFEIYQLIAELAKKDKGIII 446
|
490 500
....*....|....*....|...
gi 732682709 463 ISTHFMNEAERCDRISLMHAGKV 485
Cdd:PRK10982 447 ISSEMPELLGITDRILVMSNGLV 469
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
25-230 |
2.95e-16 |
|
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome bd biogenesis. The CydC and CydD proteins are important for the formation of cytochrome bd terminal oxidase of E. coli and it has been proposed that they were necessary for biosynthesis of the cytochrome bd quinol oxidase and for periplasmic c-type cytochromes. CydCD were proposed to determine a heterooligomeric complex important for heme export into the periplasm or to be involved in the maintenance of the proper redox state of the periplasmic space. In Bacillus subtilis, the absence of CydCD does not affect the presence of halo-cytochrome c in the membrane and this observation suggests that CydCD proteins are not involved in the export of heme in this organism.
Pssm-ID: 213214 [Multi-domain] Cd Length: 178 Bit Score: 77.35 E-value: 2.95e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 25 TVALNNITLDIPARCMVGLIGPDGVGKSSLLSLISGARVIEQGNVMVLGGDmrdpkhrrdvcpriawmPQGLGKNLYHTL 104
Cdd:cd03247 15 QQVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDGVP-----------------VSDLEKALSSLI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 105 SVyenVDFFARLFghdkaerevrinelltSTGLapfRDRPAGKLSGGMKQKLGLCCALIHDPELLILDEPTTGVDPLSRS 184
Cdd:cd03247 78 SV---LNQRPYLF----------------DTTL---RNNLGRRFSGGERQRLALARILLQDAPIVLLDEPTVGLDPITER 135
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 732682709 185 QfwdLIDSIRQRQSNMSVLVATAYMEEAERFDWLVAMNAGEVLATG 230
Cdd:cd03247 136 Q---LLSLIFEVLKDKTLIWITHHLTGIEHMDKILFLENGKIIMQG 178
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
28-227 |
3.67e-16 |
|
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette superfamily; ABCG transporters are involved in eye pigment (EP) precursor transport, regulation of lipid-trafficking mechanisms, and pleiotropic drug resistance (DR). DR is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. Compared to other members of the ABC transporter subfamilies, the ABCG transporter family is composed of proteins that have an ATP-binding cassette domain at the N-terminus and a TM (transmembrane) domain at the C-terminus.
Pssm-ID: 213180 [Multi-domain] Cd Length: 194 Bit Score: 77.59 E-value: 3.67e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 28 LNNITLDIPARCMVGLIGPDGVGKSSLLSLISGARVIEQ--GNVMVLGgdmrDPKHRRDVCPRIAWMPQGLgkNLYHTLS 105
Cdd:cd03213 25 LKNVSGKAKPGELTAIMGPSGAGKSTLLNALAGRRTGLGvsGEVLING----RPLDKRSFRKIIGYVPQDD--ILHPTLT 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 106 VYENVDFFARLFGhdkaerevrinelltstglapfrdrpagkLSGGMKQKLGLCCALIHDPELLILDEPTTGVDPLSRSQ 185
Cdd:cd03213 99 VRETLMFAAKLRG-----------------------------LSGGERKRVSIALELVSNPSLLFLDEPTSGLDSSSALQ 149
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 732682709 186 FWDLIDSIRQRQSNMSVLVATAYMEEAERFDWLVAMNAGEVL 227
Cdd:cd03213 150 VMSLLRRLADTGRTIICSIHQPSSEIFELFDKLLLLSQGRVI 191
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
27-243 |
4.47e-16 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 79.41 E-value: 4.47e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 27 ALNNITLDIPARCMVGLIGPDGVGKSSLLSLISGARVIEQGNVMvLGGDMRDPKHRRDVCPRIAWMPQGlGKNLYHTLSV 106
Cdd:PRK13648 24 TLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIF-YNNQAITDDNFEKLRKHIGIVFQN-PDNQFVGSIV 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 107 YENVDFFAR--LFGHDKAEREVriNELLTSTGLAPFRDRPAGKLSGGMKQKLGLCCALIHDPELLILDEPTTGVDPLSRS 184
Cdd:PRK13648 102 KYDVAFGLEnhAVPYDEMHRRV--SEALKQVDMLERADYEPNALSGGQKQRVAIAGVLALNPSVIILDEATSMLDPDARQ 179
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 732682709 185 QFWDLIDSIRQrQSNMSVLVATAYMEEAERFDWLVAMNAGEVLATGSAEELRQQTQSAT 243
Cdd:PRK13648 180 NLLDLVRKVKS-EHNITIISITHDLSEAMEADHVIVMNKGTVYKEGTPTEIFDHAEELT 237
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
274-495 |
4.63e-16 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 79.06 E-value: 4.63e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 274 EIAIEARDLTMRF----GSF-----VAVDHVNFRIPRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGEAWLFGQPVDPKD 344
Cdd:PRK15112 2 ETLLEVRNLSKTFryrtGWFrrqtvEAVKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDHPLHFGD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 345 IDTRR---RVGYMSQAFSLYNELTVRQNLELHARLFhiPEAEIPARVAEMSERFK----LNDVEDILPESLPLGIRQRLS 417
Cdd:PRK15112 82 YSYRSqriRMIFQDPSTSLNPRQRISQILDFPLRLN--TDLEPEQREKQIIETLRqvglLPDHASYYPHMLAPGQKQRLG 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 732682709 418 LAVAVIHRPEMLILDEPTSGVDPVARDMFWQLMVDLSRQDKVT-IFISTHFMNEAERCDRISLMHAGKVLASGTPQELV 495
Cdd:PRK15112 160 LARALILRPKVIIADEALASLDMSMRSQLINLMLELQEKQGISyIYVTQHLGMMKHISDQVLVMHQGEVVERGSTADVL 238
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
23-238 |
4.86e-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: 78.42 E-value: 4.86e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 23 GKTVALNNITLDIPARCMVGLIGPDGVGKSSLLSLISGARVIEQGNVMVLGGDMRDPKH---RRdvcpRIAWMPQGLGkn 99
Cdd:cd03254 14 EKKPVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGIDIRDISRkslRS----MIGVVLQDTF-- 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 100 LYHTlSVYENVDFfarlfGHDKAEREVrINELLTSTGLAPFRDR----------PAGK-LSGGMKQKLGLCCALIHDPEL 168
Cdd:cd03254 88 LFSG-TIMENIRL-----GRPNATDEE-VIEAAKEAGAHDFIMKlpngydtvlgENGGnLSQGERQLLAIARAMLRDPKI 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 169 LILDEPTTGVDPLSRSQFWDLIDSIRQrqsNMSVLVATAYMEEAERFDWLVAMNAGEVLATGSAEELRQQ 238
Cdd:cd03254 161 LILDEATSNIDTETEKLIQEALEKLMK---GRTSIIIAHRLSTIKNADKILVLDDGKIIEEGTHDELLAK 227
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
40-186 |
5.10e-16 |
|
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the bacterial CcmAB transporter. The CCM family is involved in bacterial cytochrome c biogenesis. Cytochrome c maturation in E. coli requires the ccm operon, which encodes eight membrane proteins (CcmABCDEFGH). CcmE is a periplasmic heme chaperon that binds heme covalently and transfers it onto apocytochrome c in the presence of CcmF, CcmG, and CcmH. The CcmAB proteins represent an ABC transporter and the CcmCD proteins participate in heme transfer to CcmE.
Pssm-ID: 213198 [Multi-domain] Cd Length: 201 Bit Score: 77.53 E-value: 5.10e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 40 MVGLIGPDGVGKSSLLSLISGARVIEQGNVMVLGGDmrDPKHRRDVCPRIAWMPQGLGknLYHTLSVYENVDFFARLFGH 119
Cdd:cd03231 28 ALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNGGP--LDFQRDSIARGLLYLGHAPG--IKTTLSVLENLRFWHADHSD 103
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 732682709 120 DKAErevrinELLTSTGLAPFRDRPAGKLSGGMKQKLGLCCALIHDPELLILDEPTTGVDPLSRSQF 186
Cdd:cd03231 104 EQVE------EALARVGLNGFEDRPVAQLSAGQQRRVALARLLLSGRPLWILDEPTTALDKAGVARF 164
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
287-521 |
5.14e-16 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 82.46 E-value: 5.14e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 287 GSFVAVDHVNFRIPRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGEAWLFGQPVDPKDIDT-----RRRVGYMSQAFSLY 361
Cdd:PRK10535 19 EQVEVLKGISLDIYAGEMVAIVGASGSGKSTLMNILGCLDKPTSGTYRVAGQDVATLDADAlaqlrREHFGFIFQRYHLL 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 362 NELTVRQNLELHARLFHIPEAEIPARVAEMSERFKLNDVEDILPESLPLGIRQRLSLAVAVIHRPEMLILDEPTSGVDPV 441
Cdd:PRK10535 99 SHLTAAQNVEVPAVYAGLERKQRLLRAQELLQRLGLEDRVEYQPSQLSGGQQQRVSIARALMNGGQVILADEPTGALDSH 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 442 ARDMFWQLMVDLsRQDKVTIFISTHFMNEAERCDRISLMHAGKVLASGTPQELVEKRGAASLEEAFIAYLQEAAGQSNEA 521
Cdd:PRK10535 179 SGEEVMAILHQL-RDRGHTVIIVTHDPQVAAQAERVIEIRDGEIVRNPPAQEKVNVAGGTEPVVNTASGWRQFVSGFREA 257
|
|
| nickel_nikE |
TIGR02769 |
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a ... |
15-257 |
5.14e-16 |
|
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a multisubunit nickel import ABC transporter complex. Nickel, once imported, may be used in urease and in certain classes of hydrogenase and superoxide dismutase. [Transport and binding proteins, Cations and iron carrying compounds]
Pssm-ID: 131816 [Multi-domain] Cd Length: 265 Bit Score: 79.08 E-value: 5.14e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 15 LAGVSQHygKTVaLNNITLDIPARCMVGLIGPDGVGKSSLLSLISGARVIEQGNVMVLGGDMR--DPKHRR--------- 83
Cdd:TIGR02769 17 LFGAKQR--APV-LTNVSLSIEEGETVGLLGRSGCGKSTLARLLLGLEKPAQGTVSFRGQDLYqlDRKQRRafrrdvqlv 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 84 ------DVCPRIAwMPQGLGKNLYHTLSVyenvdffarlfghDKAEREVRINELLTSTGLAP--FRDRPAgKLSGGMKQK 155
Cdd:TIGR02769 94 fqdspsAVNPRMT-VRQIIGEPLRHLTSL-------------DESEQKARIAELLDMVGLRSedADKLPR-QLSGGQLQR 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 156 LGLCCALIHDPELLILDEPTTGVDPLSRSQFWDLIDSIRQrQSNMSVLVATAYMEEAERF-DWLVAMNAGEVLATGSAEE 234
Cdd:TIGR02769 159 INIARALAVKPKLIVLDEAVSNLDMVLQAVILELLRKLQQ-AFGTAYLFITHDLRLVQSFcQRVAVMDKGQIVEECDVAQ 237
|
250 260
....*....|....*....|....*
gi 732682709 235 LRQQTQSAT--LEEAFINLLPQAQR 257
Cdd:TIGR02769 238 LLSFKHPAGrnLQSAVLPEHPVRRS 262
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
271-494 |
5.75e-16 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 80.15 E-value: 5.75e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 271 ENAEIAIEARDLTMRF----GSFVAVDHVNFRIPRGEIFGFLGSNGCGKSTTMKMLTGLLPAS---EGEAWLFGQPVD-- 341
Cdd:PRK09473 7 QQADALLDVKDLRVTFstpdGDVTAVNDLNFSLRAGETLGIVGESGSGKSQTAFALMGLLAANgriGGSATFNGREILnl 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 342 PKDIDTRRRVGYMSQAF-----SLYNELTVRQNL----ELHARLFHIPEAEIPARVAE---MSE-RFKLNdvedILPESL 408
Cdd:PRK09473 87 PEKELNKLRAEQISMIFqdpmtSLNPYMRVGEQLmevlMLHKGMSKAEAFEESVRMLDavkMPEaRKRMK----MYPHEF 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 409 PLGIRQRLSLAVAVIHRPEMLILDEPTSGVDPVARDMFWQLMVDLSRQDKVTIFISTHFMN-EAERCDRISLMHAGKVLA 487
Cdd:PRK09473 163 SGGMRQRVMIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKREFNTAIIMITHDLGvVAGICDKVLVMYAGRTME 242
|
....*..
gi 732682709 488 SGTPQEL 494
Cdd:PRK09473 243 YGNARDV 249
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
11-175 |
6.14e-16 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 81.65 E-value: 6.14e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 11 PVAQLAGVSQHYGKTVALNNITLDIPARCMVGLIGPDGVGKSSLLSLISGARVIEQGNVmvlggdmrdpKHRRDVcpRIA 90
Cdd:COG0488 314 KVLELEGLSKSYGDKTLLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPDSGTV----------KLGETV--KIG 381
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 91 WMPQGLgKNLYHTLSVYENVdffaRLFGHDKAEREVRinELLTSTGLAPFR-DRPAGKLSGGMKQKLGLCCALIHDPELL 169
Cdd:COG0488 382 YFDQHQ-EELDPDKTVLDEL----RDGAPGGTEQEVR--GYLGRFLFSGDDaFKPVGVLSGGEKARLALAKLLLSPPNVL 454
|
....*.
gi 732682709 170 ILDEPT 175
Cdd:COG0488 455 LLDEPT 460
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
239-525 |
6.63e-16 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 81.93 E-value: 6.63e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 239 TQSATLEEaFINLLPQAQRQAHQAVVIPPyqpENAEIAIEARDLTMRF-GSFVAVDHVNFRIPRGEIFGFLGSNGCGKST 317
Cdd:PRK13657 301 MAAPKLEE-FFEVEDAVPDVRDPPGAIDL---GRVKGAVEFDDVSFSYdNSRQGVEDVSFEAKPGQTVAIVGPTGAGKST 376
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 318 TMKMLTGLLPASEGEAwlfgqPVDPKDIDT------RRRVGYMSQAFSLYNElTVRQNLEL---HARLFHIPEAEIPARV 388
Cdd:PRK13657 377 LINLLQRVFDPQSGRI-----LIDGTDIRTvtraslRRNIAVVFQDAGLFNR-SIEDNIRVgrpDATDEEMRAAAERAQA 450
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 389 AEMSERfKLNDVEDILPE---SLPLGIRQRLSLAVAVIHRPEMLILDEPTSGVDpVARDMFWQLMVDLSRQDKVTiFIST 465
Cdd:PRK13657 451 HDFIER-KPDGYDTVVGErgrQLSGGERQRLAIARALLKDPPILILDEATSALD-VETEAKVKAALDELMKGRTT-FIIA 527
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 732682709 466 HFMNEAERCDRISLMHAGKVLASGTPQELVEKRG--AASLEEAFIAyLQEAAGQSNEAEAPP 525
Cdd:PRK13657 528 HRLSTVRNADRILVFDNGRVVESGSFDELVARGGrfAALLRAQGML-QEDERRKQPAAEGAN 588
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
295-494 |
6.80e-16 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 78.55 E-value: 6.80e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 295 VNFRIPRGEIFGFLGSNGCGKSTTMKMLTGLLP------ASEGEAWLFGQPVDPKD-IDTRRRVGYMSQAFSLYNELTVR 367
Cdd:PRK14246 29 ITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLIEiydskiKVDGKVLYFGKDIFQIDaIKLRKEVGMVFQQPNPFPHLSIY 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 368 QNLELHARLFHIPEA-EIPARVAEMSERFKL-NDVEDIL--PES-LPLGIRQRLSLAVAVIHRPEMLILDEPTSGVDPVA 442
Cdd:PRK14246 109 DNIAYPLKSHGIKEKrEIKKIVEECLRKVGLwKEVYDRLnsPASqLSGGQQQRLTIARALALKPKVLLMDEPTSMIDIVN 188
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 732682709 443 RDMFWQLMVDLSRQdkVTIFISTHFMNEAER-CDRISLMHAGKVLASGTPQEL 494
Cdd:PRK14246 189 SQAIEKLITELKNE--IAIVIVSHNPQQVARvADYVAFLYNGELVEWGSSNEI 239
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
14-229 |
8.09e-16 |
|
First domain of the ATP-binding cassette component of monosaccharide transport system; This family represents the domain I of the carbohydrate uptake proteins that transport only monosaccharides (Monos). The Carb_Monos family is involved in the uptake of monosaccharides, such as pentoses (such as xylose, arabinose, and ribose) and hexoses (such as xylose, arabinose, and ribose), that cannot be broken down to simple sugars by hydrolysis. Pentoses include xylose, arabinose, and ribose. Important hexoses include glucose, galactose, and fructose. In members of the Carb_monos family, the single hydrophobic gene product forms a homodimer while the ABC protein represents a fusion of two nucleotide-binding domains. However, it is assumed that two copies of the ABC domains are present in the assembled transporter.
Pssm-ID: 213183 [Multi-domain] Cd Length: 163 Bit Score: 75.93 E-value: 8.09e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 14 QLAGVSQHYGKTVALNNITLDIPARCMVGLIGPDGVGKSSLLSLISGARVIEQGNVMVLGgdmrdpkhrrdvcpriawmp 93
Cdd:cd03216 2 ELRGITKRFGGVKALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVDG-------------------- 61
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 94 qglgknlyhtlsvyenvdffarlfghdkaeREVRINelltstglAPFRDRPAG-----KLSGGMKQKLGLCCALIHDPEL 168
Cdd:cd03216 62 ------------------------------KEVSFA--------SPRDARRAGiamvyQLSVGERQMVEIARALARNARL 103
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 732682709 169 LILDEPTTGVDPLSRSQFWDLIDsiRQRQSNMSVLVATAYMEEAERF-DWLVAMNAGEVLAT 229
Cdd:cd03216 104 LILDEPTAALTPAEVERLFKVIR--RLRAQGVAVIFISHRLDEVFEIaDRVTVLRDGRVVGT 163
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
15-204 |
9.22e-16 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 77.85 E-value: 9.22e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 15 LAGVSQHYGKTVALNNITLDIPARCMVGLIGPDGVGKSSLLSLISGARVIEQGNVmvlggdmrdpkhRRDVCPRIAWMPQ 94
Cdd:PRK09544 7 LENVSVSFGQRRVLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVI------------KRNGKLRIGYVPQ 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 95 GLgkNLYHTLSVyeNVDFFARLfghDKAEREVRINELLTSTGLAPFRDRPAGKLSGGMKQKLGLCCALIHDPELLILDEP 174
Cdd:PRK09544 75 KL--YLDTTLPL--TVNRFLRL---RPGTKKEDILPALKRVQAGHLIDAPMQKLSGGETQRVLLARALLNRPQLLVLDEP 147
|
170 180 190
....*....|....*....|....*....|
gi 732682709 175 TTGVDPLSRSQFWDLIDSIRqRQSNMSVLV 204
Cdd:PRK09544 148 TQGVDVNGQVALYDLIDQLR-RELDCAVLM 176
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
278-488 |
9.47e-16 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 81.11 E-value: 9.47e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 278 EARDLTMRFGSFVAVDHVNFRIPRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGEAWLFGQPVdpKDIDTRRR----VGY 353
Cdd:PRK11288 6 SFDGIGKTFPGVKALDDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSILIDGQEM--RFASTTAAlaagVAI 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 354 MSQAFSLYNELTVRQNL---ELHARLFHIPEAEIPARVAEMSERFKlndvEDILPE----SLPLGIRQRLSLAVAVIHRP 426
Cdd:PRK11288 84 IYQELHLVPEMTVAENLylgQLPHKGGIVNRRLLNYEAREQLEHLG----VDIDPDtplkYLSIGQRQMVEIAKALARNA 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 732682709 427 EMLILDEPTSGVDPVARDMFWQLMVDLSRQDKVTIFIStHFMNEAER-CDRISLMHAGKVLAS 488
Cdd:PRK11288 160 RVIAFDEPTSSLSAREIEQLFRVIRELRAEGRVILYVS-HRMEEIFAlCDAITVFKDGRYVAT 221
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
5-238 |
1.00e-15 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 81.41 E-value: 1.00e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 5 ELVPVPPVAQLAGVSQHY--GKTVALNNITLDIPARCMVGLIGPDGVGKSSLLSLISGARVIEQGNVMVLGgdmrdpkhr 82
Cdd:PRK11160 331 TAAADQVSLTLNNVSFTYpdQPQPVLKGLSLQIKAGEKVALLGRTGCGKSTLLQLLTRAWDPQQGEILLNG--------- 401
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 83 rdvCPRIAWMPQglgkNLYHTLSVY-ENVDFFA---R---LFGHDKAEREvRINELLTSTGLAPFRDRPAG--------- 146
Cdd:PRK11160 402 ---QPIADYSEA----ALRQAISVVsQRVHLFSatlRdnlLLAAPNASDE-ALIEVLQQVGLEKLLEDDKGlnawlgegg 473
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 147 -KLSGGMKQKLGLCCALIHDPELLILDEPTTGVDPLSRSQFWDLidsIRQRQSNMSVLVATAYMEEAERFDWLVAMNAGE 225
Cdd:PRK11160 474 rQLSGGEQRRLGIARALLHDAPLLLLDEPTEGLDAETERQILEL---LAEHAQNKTVLMITHRLTGLEQFDRICVMDNGQ 550
|
250
....*....|...
gi 732682709 226 VLATGSAEELRQQ 238
Cdd:PRK11160 551 IIEQGTHQELLAQ 563
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
21-235 |
1.58e-15 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 77.19 E-value: 1.58e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 21 HYGKTVALNNITLDIPARCMVGLIGPDGVGKSSLL-------SLISGARVieQGNVMVLGGDMRDPKH-----RRDVCPR 88
Cdd:PRK14267 13 YYGSNHVIKGVDLKIPQNGVFALMGPSGCGKSTLLrtfnrllELNEEARV--EGEVRLFGRNIYSPDVdpievRREVGMV 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 89 IAWmpqglgKNLYHTLSVYENVDFFARLFGHDKAEREV--RINELLTSTGL-APFRDR---PAGKLSGGMKQKLGLCCAL 162
Cdd:PRK14267 91 FQY------PNPFPHLTIYDNVAIGVKLNGLVKSKKELdeRVEWALKKAALwDEVKDRlndYPSNLSGGQRQRLVIARAL 164
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 732682709 163 IHDPELLILDEPTTGVDPLSRSQFWDLIDSIRQRQSnmSVLVATAYMEEAERFDWLVAMNAGEVLATGSAEEL 235
Cdd:PRK14267 165 AMKPKILLMDEPTANIDPVGTAKIEELLFELKKEYT--IVLVTHSPAQAARVSDYVAFLYLGKLIEVGPTRKV 235
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
276-494 |
1.68e-15 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 77.10 E-value: 1.68e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 276 AIEARDLTMRFGSFVAVDHVNFRIPRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGEAwlfgqPVDPKDIDT-------- 347
Cdd:PRK11264 3 AIEVKNLVKKFHGQTVLHGIDLEVKPGEVVAIIGPSGSGKTTLLRCINLLEQPEAGTI-----RVGDITIDTarslsqqk 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 348 ------RRRVGYMSQAFSLYNELTVRQN-LELHARLFHIPEAEIPARVAEMSERFKLNDVEDILPESLPLGIRQRLSLAV 420
Cdd:PRK11264 78 glirqlRQHVGFVFQNFNLFPHRTVLENiIEGPVIVKGEPKEEATARARELLAKVGLAGKETSYPRRLSGGQQQRVAIAR 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 732682709 421 AVIHRPEMLILDEPTSGVDPVARDMFWQLMVDLSrQDKVTIFISTHFMNEA-ERCDRISLMHAGKVLASGTPQEL 494
Cdd:PRK11264 158 ALAMRPEVILFDEPTSALDPELVGEVLNTIRQLA-QEKRTMVIVTHEMSFArDVADRAIFMDQGRIVEQGPAKAL 231
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
18-259 |
1.98e-15 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 80.66 E-value: 1.98e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 18 VSQHYGKtVALNNITLDIPARCMVGLIGPDGVGKSSLLSLISGArVIEQGNVMVLGGDMR--DPKHRRDvcpRIAWmpqg 95
Cdd:PRK11174 357 ILSPDGK-TLAGPLNFTLPAGQRIALVGPSGAGKTSLLNALLGF-LPYQGSLKINGIELRelDPESWRK---HLSW---- 427
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 96 LGKN--LYHTlSVYENVdffarLFGHDKAEREvRINELLTSTGLAPFRDRP-----------AGKLSGGMKQKLGLCCAL 162
Cdd:PRK11174 428 VGQNpqLPHG-TLRDNV-----LLGNPDASDE-QLQQALENAWVSEFLPLLpqgldtpigdqAAGLSVGQAQRLALARAL 500
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 163 IHDPELLILDEPTTGVDPLSRSQFWDLIDSIRQRQsnmSVLVATAYMEEAERFDWLVAMNAGEVLATGSAEELRQQtqsa 242
Cdd:PRK11174 501 LQPCQLLLLDEPTASLDAHSEQLVMQALNAASRRQ---TTLMVTHQLEDLAQWDQIWVMQDGQIVQQGDYAELSQA---- 573
|
250
....*....|....*..
gi 732682709 243 tlEEAFINLLpqAQRQA 259
Cdd:PRK11174 574 --GGLFATLL--AHRQE 586
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
26-239 |
2.09e-15 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 77.05 E-value: 2.09e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 26 VALNNITLDIPARCMVGLIGPDGVGKSSLLSLISGARVIEQGNVMVLGGDM-RDPKHRR---------D----VCPRiaw 91
Cdd:COG1101 20 RALDGLNLTIEEGDFVTVIGSNGAGKSTLLNAIAGSLPPDSGSILIDGKDVtKLPEYKRakyigrvfqDpmmgTAPS--- 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 92 mpqglgknlyhtLSVYENVDFFAR-------LFGHDKAEREvRINELLTSTGLApFRDR---PAGKLSGGMKQKLGLCCA 161
Cdd:COG1101 97 ------------MTIEENLALAYRrgkrrglRRGLTKKRRE-LFRELLATLGLG-LENRldtKVGLLSGGQRQALSLLMA 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 162 LIHDPELLILDEPTTGVDPlSRSQF-WDLIDSIRQRQsNMSVLVATAYMEEAERF-DWLVAMNAGEVLATGSAEELRQQT 239
Cdd:COG1101 163 TLTKPKLLLLDEHTAALDP-KTAALvLELTEKIVEEN-NLTTLMVTHNMEQALDYgNRLIMMHEGRIILDVSGEEKKKLT 240
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
277-497 |
2.93e-15 |
|
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of iron-sulfur clusters (Fe-S) depends on multi-protein systems. The SUF system of E. coli and Erwinia chrysanthemi is important for Fe-S biogenesis under stressful conditions. The SUF system is made of six proteins: SufC is an atypical cytoplasmic ABC-ATPase, which forms a complex with SufB and SufD; SufA plays the role of a scaffold protein for assembly of iron-sulfur clusters and delivery to target proteins; SufS is a cysteine desulfurase which mobilizes the sulfur atom from cysteine and provides it to the cluster; SufE has no associated function yet.
Pssm-ID: 213184 [Multi-domain] Cd Length: 200 Bit Score: 75.26 E-value: 2.93e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 277 IEARDLTMRFGSFVAVDHVNFRIPRGEIFGFLGSNGCGKSTTMKMLTGLlPASE---GEAWLFGQPVDPKDIDTRRRVG- 352
Cdd:cd03217 1 LEIKDLHVSVGGKEILKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMGH-PKYEvteGEILFKGEDITDLPPEERARLGi 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 353 YMSqafslyneltvrqnlelharlFHIPeAEIPA-RVAEMserfkLNDVEdilpESLPLGIRQRLSLAVAVIHRPEMLIL 431
Cdd:cd03217 80 FLA---------------------FQYP-PEIPGvKNADF-----LRYVN----EGFSGGEKKRNEILQLLLLEPDLAIL 128
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 732682709 432 DEPTSGVDPVARDMFWQLMVDLsRQDKVTIFISTHFMNEAE--RCDRISLMHAGKVLASGtPQELVEK 497
Cdd:cd03217 129 DEPDSGLDIDALRLVAEVINKL-REEGKSVLIITHYQRLLDyiKPDRVHVLYDGRIVKSG-DKELALE 194
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
12-439 |
3.73e-15 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 79.39 E-value: 3.73e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 12 VAQLAGVSQHYG-KTVALNNITLD-IP-ARcmVGLIGPDGVGKSSLLSLISGARVIEQGNVMVLGGdmrdpkhrrdvcPR 88
Cdd:PRK11819 6 IYTMNRVSKVVPpKKQILKDISLSfFPgAK--IGVLGLNGAGKSTLLRIMAGVDKEFEGEARPAPG------------IK 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 89 IAWMPQGlgKNLYHTLSVYENV--------DFFARL------FGHDKA------EREVRINELLTSTGLA---------- 138
Cdd:PRK11819 72 VGYLPQE--PQLDPEKTVRENVeegvaevkAALDRFneiyaaYAEPDAdfdalaAEQGELQEIIDAADAWdldsqleiam 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 139 -----PFRDRPAGKLSGGMKQKLGLCCALIHDPELLILDEPTTGVDPLSRS---QF-----------------------W 187
Cdd:PRK11819 150 dalrcPPWDAKVTKLSGGERRRVALCRLLLEKPDMLLLDEPTNHLDAESVAwleQFlhdypgtvvavthdryfldnvagW 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 188 DL-IDsiRQR----QSNMSvlvatAYMEE-AERfdwlvamnagevLAT-GSAEELRQQTQSATLE--------------- 245
Cdd:PRK11819 230 ILeLD--RGRgipwEGNYS-----SWLEQkAKR------------LAQeEKQEAARQKALKRELEwvrqspkarqakska 290
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 246 --EAFINLLPQA--QRQAHQAVVIPPyQPENAEIAIEARDLTMRFGSFVAVDHVNFRIPRGEIFGFLGSNGCGKSTTMKM 321
Cdd:PRK11819 291 rlARYEELLSEEyqKRNETNEIFIPP-GPRLGDKVIEAENLSKSFGDRLLIDDLSFSLPPGGIVGIIGPNGAGKSTLFKM 369
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 322 LTGLLPASEGEAWLfGQPVdpkdidtrrRVGYMSQAF-SLYNELTVRQNLELHARLFHIPEAEIPAR--VAEMSerFKLN 398
Cdd:PRK11819 370 ITGQEQPDSGTIKI-GETV---------KLAYVDQSRdALDPNKTVWEEISGGLDIIKVGNREIPSRayVGRFN--FKGG 437
|
490 500 510 520
....*....|....*....|....*....|....*....|.
gi 732682709 399 DVEDILPEsLPLGIRQRLSLAVAVIHRPEMLILDEPTSGVD 439
Cdd:PRK11819 438 DQQKKVGV-LSGGERNRLHLAKTLKQGGNVLLLDEPTNDLD 477
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
270-501 |
4.47e-15 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 80.02 E-value: 4.47e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 270 PENAEIAIEARDLTMRFGSFVAVDHVNFRIPRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGEAWlfgqpVDPKDI---- 345
Cdd:PLN03232 1230 PSRGSIKFEDVHLRYRPGLPPVLHGLSFFVSPSEKVGVVGRTGAGKSSMLNALFRIVELEKGRIM-----IDDCDVakfg 1304
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 346 --DTRRRVGYMSQAFSLYNElTVRQNLElharlfhiPEAEI-PARVAEMSERFKLNDVEDILP-----------ESLPLG 411
Cdd:PLN03232 1305 ltDLRRVLSIIPQSPVLFSG-TVRFNID--------PFSEHnDADLWEALERAHIKDVIDRNPfgldaevseggENFSVG 1375
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 412 IRQRLSLAVAVIHRPEMLILDEPTSGVDpVARDMFWQLMVdlsRQD--KVTIFISTHFMNEAERCDRISLMHAGKVLASG 489
Cdd:PLN03232 1376 QRQLLSLARALLRRSKILVLDEATASVD-VRTDSLIQRTI---REEfkSCTMLVIAHRLNTIIDCDKILVLSSGQVLEYD 1451
|
250
....*....|..
gi 732682709 490 TPQELVEKRGAA 501
Cdd:PLN03232 1452 SPQELLSRDTSA 1463
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
13-439 |
4.57e-15 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 79.61 E-value: 4.57e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 13 AQLAgvsqhYGKTVALNNITLDIPARCMVGLIGPDGVGKSSLLSLISG------ARVIEQGNVMV--LGGDmrDPKHRRD 84
Cdd:PRK11147 9 AWLS-----FSDAPLLDNAELHIEDNERVCLVGRNGAGKSTLMKILNGevllddGRIIYEQDLIVarLQQD--PPRNVEG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 85 -VCPRIAWMPQGLGKNL--YHTLSvyenvdffaRLFGHDKAER--------------------EVRINELLTSTGLAPfr 141
Cdd:PRK11147 82 tVYDFVAEGIEEQAEYLkrYHDIS---------HLVETDPSEKnlnelaklqeqldhhnlwqlENRINEVLAQLGLDP-- 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 142 DRPAGKLSGGMKQKLGLCCALIHDPELLILDEPTTGVDplsrsqfwdlIDSI--------------------RQRQSNMS 201
Cdd:PRK11147 151 DAALSSLSGGWLRKAALGRALVSNPDVLLLDEPTNHLD----------IETIewlegflktfqgsiifishdRSFIRNMA 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 202 ---------VLVA-----TAYMEEAErfDWLvamnagEVLATGSAEELRQQTQsatlEEAFI------------------ 249
Cdd:PRK11147 221 trivdldrgKLVSypgnyDQYLLEKE--EAL------RVEELQNAEFDRKLAQ----EEVWIrqgikarrtrnegrvral 288
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 250 NLLPQAQRQAHQAVVIPPYQPENAE----IAIEARDLTMRFGSFVAVDHVNFRIPRGEIFGFLGSNGCGKSTTMKMLTGL 325
Cdd:PRK11147 289 KALRRERSERREVMGTAKMQVEEASrsgkIVFEMENVNYQIDGKQLVKDFSAQVQRGDKIALIGPNGCGKTTLLKLMLGQ 368
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 326 LPASEGEAwlfgqpvdpkDIDTRRRVGYMSQ-AFSLYNELTVRQNLE------------------LHARLFHIPEAEIPA 386
Cdd:PRK11147 369 LQADSGRI----------HCGTKLEVAYFDQhRAELDPEKTVMDNLAegkqevmvngrprhvlgyLQDFLFHPKRAMTPV 438
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|...
gi 732682709 387 RvaemserfklndvedilpeSLPLGIRQRLSLAVAVIHRPEMLILDEPTSGVD 439
Cdd:PRK11147 439 K-------------------ALSGGERNRLLLARLFLKPSNLLILDEPTNDLD 472
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
268-500 |
4.58e-15 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 79.77 E-value: 4.58e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 268 YQPENAEIAIEARDLTMRFGSFVAV---DHVNFRIPRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGEAWLFGQPVdpKD 344
Cdd:TIGR00958 470 LAPLNLEGLIEFQDVSFSYPNRPDVpvlKGLTFTLHPGEVVALVGPSGSGKSTVAALLQNLYQPTGGQVLLDGVPL--VQ 547
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 345 ID---TRRRVGYMSQAFSLYNElTVRQNLELHarLFHIPEAEIPArVAEMS--ERFKLNDVEDILPE------SLPLGIR 413
Cdd:TIGR00958 548 YDhhyLHRQVALVGQEPVLFSG-SVRENIAYG--LTDTPDEEIMA-AAKAAnaHDFIMEFPNGYDTEvgekgsQLSGGQK 623
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 414 QRLSLAVAVIHRPEMLILDEPTSGVDPVARDMFWQLMvdlSRQDKVTIFIsTHFMNEAERCDRISLMHAGKVLASGTPQE 493
Cdd:TIGR00958 624 QRIAIARALVRKPRVLILDEATSALDAECEQLLQESR---SRASRTVLLI-AHRLSTVERADQILVLKKGSVVEMGTHKQ 699
|
....*..
gi 732682709 494 LVEKRGA 500
Cdd:TIGR00958 700 LMEDQGC 706
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
28-235 |
5.36e-15 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 79.32 E-value: 5.36e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 28 LNNITLDIPARCMVGLIGPDGVGKSSLLSLISGAR---VIEQGNVMvLGGDMRDPKHRRDVCPRIawMPQGLgknLYHTL 104
Cdd:TIGR00955 41 LKNVSGVAKPGELLAVMGSSGAGKTTLMNALAFRSpkgVKGSGSVL-LNGMPIDAKEMRAISAYV--QQDDL---FIPTL 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 105 SVYENVDFFARLFGHD---KAEREVRINELLTSTGLAPFRDRPAGK------LSGGMKQKLGLCCALIHDPELLILDEPT 175
Cdd:TIGR00955 115 TVREHLMFQAHLRMPRrvtKKEKRERVDEVLQALGLRKCANTRIGVpgrvkgLSGGERKRLAFASELLTDPPLLFCDEPT 194
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 176 TGVDPLSRSQFWDLIDSIRQRQSNMSVLVATAYMEEAERFDWLVAMNAGEVLATGSAEEL 235
Cdd:TIGR00955 195 SGLDSFMAYSVVQVLKGLAQKGKTIICTIHQPSSELFELFDKIILMAEGRVAYLGSPDQA 254
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
277-484 |
5.65e-15 |
|
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is a cytosolic protein required by fungal ribosomes for in vitro protein synthesis and for in vivo growth. EF-3 stimulates the binding of the EF-1: GTP: aa-tRNA ternary complex to the ribosomal A site by facilitated release of the deacylated tRNA from the E site. The reaction requires ATP hydrolysis. EF-3 contains two ATP nucleotide binding sequence (NBS) motifs. NBSI is sufficient for the intrinsic ATPase activity. NBSII is essential for the ribosome-stimulated functions.
Pssm-ID: 213188 [Multi-domain] Cd Length: 144 Bit Score: 72.87 E-value: 5.65e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 277 IEARDLTMRFGSFVAVDHVNFRIPRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGEaWLFGQPVdpkdidtrrRVGYMSQ 356
Cdd:cd03221 1 IELENLSKTYGGKLLLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGI-VTWGSTV---------KIGYFEQ 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 357 afslyneltvrqnlelharlfhipeaeiparvaemserfklndvedilpesLPLGIRQRLSLAVAVIHRPEMLILDEPTS 436
Cdd:cd03221 71 ---------------------------------------------------LSGGEKMRLALAKLLLENPNLLLLDEPTN 99
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 732682709 437 GVDPVARDmfwQLMVDLSRQDKVTIFIS--THFMNEAerCDRISLMHAGK 484
Cdd:cd03221 100 HLDLESIE---ALEEALKEYPGTVILVShdRYFLDQV--ATKIIELEDGK 144
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
282-497 |
6.67e-15 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 75.51 E-value: 6.67e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 282 LTMRFGSFVAVDHVNFRIPRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGEAWLFGQPVDPKDIDTrrrvGYMSQAFSLY 361
Cdd:PRK11248 7 LYADYGGKPALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDGKPVEGPGAER----GVVFQNEGLL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 362 NELTVRQNLELHARLFHIPEAEIPARVAEMSERFKLNDVEDILPESLPLGIRQRLSLAVAVIHRPEMLILDEPTSGVDPV 441
Cdd:PRK11248 83 PWRNVQDNVAFGLQLAGVEKMQRLEIAHQMLKKVGLEGAEKRYIWQLSGGQRQRVGIARALAANPQLLLLDEPFGALDAF 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 732682709 442 ARDMFWQLMVDLSRQDKVTIFISTHFMNEAercdriSLMHAGKVLASGTPQELVEK 497
Cdd:PRK11248 163 TREQMQTLLLKLWQETGKQVLLITHDIEEA------VFMATELVLLSPGPGRVVER 212
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
266-501 |
6.83e-15 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 79.78 E-value: 6.83e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 266 PPYQPENAeiAIEARDLTMRFGSFV--AVDHVNFRIPRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGEAWlfgqpVDPK 343
Cdd:PLN03130 1229 PPGWPSSG--SIKFEDVVLRYRPELppVLHGLSFEISPSEKVGIVGRTGAGKSSMLNALFRIVELERGRIL-----IDGC 1301
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 344 DI------DTRRRVGYMSQAFSLYNElTVRQNLElharlfhiPEAE-IPARVAEMSERFKLNDVEDILP----------- 405
Cdd:PLN03130 1302 DIskfglmDLRKVLGIIPQAPVLFSG-TVRFNLD--------PFNEhNDADLWESLERAHLKDVIRRNSlgldaevseag 1372
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 406 ESLPLGIRQRLSLAVAVIHRPEMLILDEPTSGVDpVARDMFWQLMVdlsRQD--KVTIFISTHFMNEAERCDRISLMHAG 483
Cdd:PLN03130 1373 ENFSVGQRQLLSLARALLRRSKILVLDEATAAVD-VRTDALIQKTI---REEfkSCTMLIIAHRLNTIIDCDRILVLDAG 1448
|
250
....*....|....*...
gi 732682709 484 KVLASGTPQELVEKRGAA 501
Cdd:PLN03130 1449 RVVEFDTPENLLSNEGSA 1466
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
277-464 |
7.88e-15 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 76.54 E-value: 7.88e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 277 IEARDLT----MRFGSFV------AVDHVNFRIPRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGEAWLFGQPVDPKDID 346
Cdd:PRK11308 6 LQAIDLKkhypVKRGLFKperlvkALDGVSFTLERGKTLAVVGESGCGKSTLARLLTMIETPTGGELYYQGQDLLKADPE 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 347 T----RRRVGYMSQafSLYNELTVRQN--------LELHARLfhiPEAEIPARVAEMSERFKLN-DVEDILPESLPLGIR 413
Cdd:PRK11308 86 AqkllRQKIQIVFQ--NPYGSLNPRKKvgqileepLLINTSL---SAAERREKALAMMAKVGLRpEHYDRYPHMFSGGQR 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 732682709 414 QRLSLAVAVIHRPEMLILDEPTSGVDPVARDMFWQLMVDLSRQDKVT-IFIS 464
Cdd:PRK11308 161 QRIAIARALMLDPDVVVADEPVSALDVSVQAQVLNLMMDLQQELGLSyVFIS 212
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
26-240 |
9.09e-15 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 75.97 E-value: 9.09e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 26 VALNNITLDIPARCMVGLIGPDGVGKSSLLSLISGARVIEQGNVMVlgGDM------RDpKHRRDVCPRIAWMPQGLGKN 99
Cdd:PRK13646 21 QAIHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTV--DDItithktKD-KYIRPVRKRIGMVFQFPESQ 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 100 LYHTlSVYENVDFFARLFGHDKAEREVRINELLTSTG-------LAPFrdrpagKLSGGMKQKLGLCCALIHDPELLILD 172
Cdd:PRK13646 98 LFED-TVEREIIFGPKNFKMNLDEVKNYAHRLLMDLGfsrdvmsQSPF------QMSGGQMRKIAIVSILAMNPDIIVLD 170
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 732682709 173 EPTTGVDPLSRSQFWDLIDSIrQRQSNMSVLVATAYMEEAERF-DWLVAMNAGEVLATGSAEELRQQTQ 240
Cdd:PRK13646 171 EPTAGLDPQSKRQVMRLLKSL-QTDENKTIILVSHDMNEVARYaDEVIVMKEGSIVSQTSPKELFKDKK 238
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
273-494 |
9.51e-15 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 75.52 E-value: 9.51e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 273 AEIAIEARDLTMRFGSFVAVDHVNFRIPRGEIFGFLGSNGCGKSTTMKMLTGLLPASEG-----EAWLFGQPV-DPKDI- 345
Cdd:PRK14271 18 AAPAMAAVNLTLGFAGKTVLDQVSMGFPARAVTSLMGPTGSGKTTFLRTLNRMNDKVSGyrysgDVLLGGRSIfNYRDVl 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 346 DTRRRVGYMSQAFSLYnELTVRQNLELHARLFH-IPEAEI----PARVAEMSERFKLNDVEDILPESLPLGIRQRLSLAV 420
Cdd:PRK14271 98 EFRRRVGMLFQRPNPF-PMSIMDNVLAGVRAHKlVPRKEFrgvaQARLTEVGLWDAVKDRLSDSPFRLSGGQQQLLCLAR 176
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 732682709 421 AVIHRPEMLILDEPTSGVDPVARDMFWQLMVDLSrqDKVTIFISTHFMNEAER-CDRISLMHAGKVLASGTPQEL 494
Cdd:PRK14271 177 TLAVNPEVLLLDEPTSALDPTTTEKIEEFIRSLA--DRLTVIIVTHNLAQAARiSDRAALFFDGRLVEEGPTEQL 249
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
23-235 |
1.00e-14 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 77.38 E-value: 1.00e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 23 GKTVALNNITLDIPARCMVGLIGPDGVGKSSLLSLISgaRVIE--QGNVMVLGGDM---RDPKHRRDVCPRIAWMPQGLG 97
Cdd:PRK10070 39 GLSLGVKDASLAIEEGEIFVIMGLSGSGKSTMVRLLN--RLIEptRGQVLIDGVDIakiSDAELREVRRKKIAMVFQSFA 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 98 knLYHTLSVYENVDFFARLFGHDKAEREVRINELLTSTGLAPFRDRPAGKLSGGMKQKLGLCCALIHDPELLILDEPTTG 177
Cdd:PRK10070 117 --LMPHMTVLDNTAFGMELAGINAEERREKALDALRQVGLENYAHSYPDELSGGMRQRVGLARALAINPDILLMDEAFSA 194
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 732682709 178 VDPLSRSQFWDLIDSIRQRQSNMSVLVATAyMEEAERF-DWLVAMNAGEVLATGSAEEL 235
Cdd:PRK10070 195 LDPLIRTEMQDELVKLQAKHQRTIVFISHD-LDEAMRIgDRIAIMQNGEVVQVGTPDEI 252
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
14-226 |
1.02e-14 |
|
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: 73.02 E-value: 1.02e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 14 QLAGVSQHYG--KTVALNNITLDIPARCMVGLIGPDGVGKSSLLSLISGARVIEQGNVMVLGGDMR--DPKHRRDvcpRI 89
Cdd:cd03246 2 EVENVSFRYPgaEPPVLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDGADISqwDPNELGD---HV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 90 AWMPQGLgkNLYhTLSVYENVdffarlfghdkaerevrinelltstglapfrdrpagkLSGGMKQKLGLCCALIHDPELL 169
Cdd:cd03246 79 GYLPQDD--ELF-SGSIAENI-------------------------------------LSGGQRQRLGLARALYGNPRIL 118
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 732682709 170 ILDEPTTGVDPLSRSQFWDLIDSIRQRQSnmSVLVATAYMEEAERFDWLVAMNAGEV 226
Cdd:cd03246 119 VLDEPNSHLDVEGERALNQAIAALKAAGA--TRIVIAHRPETLASADRILVLEDGRV 173
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
276-473 |
1.14e-14 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 75.07 E-value: 1.14e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 276 AIEARDLTMRFGSFVAVDHVNFRIPRGEIFGFLGSNGCGKSTTMKMLTGLLPAS-----EGEAWLFGQPVDPKDIDTRRR 350
Cdd:PRK14258 7 AIKVNNLSFYYDTQKILEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLNRMNELEsevrvEGRVEFFNQNIYERRVNLNRL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 351 VGYMSQAFSLYN--ELTVRQNLELHARL--FHiPEAEIPARVAEMSERFKL-NDVEDILPES---LPLGIRQRLSLAVAV 422
Cdd:PRK14258 87 RRQVSMVHPKPNlfPMSVYDNVAYGVKIvgWR-PKLEIDDIVESALKDADLwDEIKHKIHKSaldLSGGQQQRLCIARAL 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 732682709 423 IHRPEMLILDEPTSGVDPVARDMFWQLMVDLSRQDKVTIFISTHFMNEAER 473
Cdd:PRK14258 166 AVKPKVLLMDEPCFGLDPIASMKVESLIQSLRLRSELTMVIVSHNLHQVSR 216
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
268-500 |
1.27e-14 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 77.75 E-value: 1.27e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 268 YQPENAEIAIEARDLTMRFGS--FVAVDHVNFRIPRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGEAWLFGqpVDPKDI 345
Cdd:PRK11176 333 RVIERAKGDIEFRNVTFTYPGkeVPALRNINFKIPAGKTVALVGRSGSGKSTIANLLTRFYDIDEGEILLDG--HDLRDY 410
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 346 ---DTRRRVGYMSQAFSLYNElTVRQNLElHARLFHIPEAEI--PARVAEMSErF--KLNDVED-ILPE---SLPLGIRQ 414
Cdd:PRK11176 411 tlaSLRNQVALVSQNVHLFND-TIANNIA-YARTEQYSREQIeeAARMAYAMD-FinKMDNGLDtVIGEngvLLSGGQRQ 487
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 415 RLSLAVAVIHRPEMLILDEPTSGVDpVARDMFWQLMVDLSRQDKVTIFIStHFMNEAERCDRISLMHAGKVLASGTPQEL 494
Cdd:PRK11176 488 RIAIARALLRDSPILILDEATSALD-TESERAIQAALDELQKNRTSLVIA-HRLSTIEKADEILVVEDGEIVERGTHAEL 565
|
....*.
gi 732682709 495 VEKRGA 500
Cdd:PRK11176 566 LAQNGV 571
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
26-235 |
1.99e-14 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 75.27 E-value: 1.99e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 26 VALNNITLDIPARCMVGLIGPDGVGKSSLLSLISGARVIEQGNVMVlgGDMRDPKHRRDVCPRIAWMPQGLG--KNLYHT 103
Cdd:PRK13631 40 VALNNISYTFEKNKIYFIIGNSGSGKSTLVTHFNGLIKSKYGTIQV--GDIYIGDKKNNHELITNPYSKKIKnfKELRRR 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 104 LS--------------VYENVDFFARLFGHDKAEREVRINELLTSTGL-APFRDRPAGKLSGGMKQKLGLCCALIHDPEL 168
Cdd:PRK13631 118 VSmvfqfpeyqlfkdtIEKDIMFGPVALGVKKSEAKKLAKFYLNKMGLdDSYLERSPFGLSGGQKRRVAIAGILAIQPEI 197
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 732682709 169 LILDEPTTGVDPLSRSQFWDLIdsIRQRQSNMSVLVATAYMEEA-ERFDWLVAMNAGEVLATGSAEEL 235
Cdd:PRK13631 198 LIFDEPTAGLDPKGEHEMMQLI--LDAKANNKTVFVITHTMEHVlEVADEVIVMDKGKILKTGTPYEI 263
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
41-439 |
2.04e-14 |
|
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: 77.13 E-value: 2.04e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 41 VGLIGPDGVGKSSLLSLISGarvIEQGNVmvlgGDMRDPKHRRDVCPRIAwmpqglGKNLY-HTLSVYEN---------- 109
Cdd:COG1245 102 TGILGPNGIGKSTALKILSG---ELKPNL----GDYDEEPSWDEVLKRFR------GTELQdYFKKLANGeikvahkpqy 168
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 110 VDFFARLF-GH-----DKA-EREVrINELLTSTGLAPFRDRPAGKLSGGMKQKLGLCCALIHDPELLILDEPTTGVDpls 182
Cdd:COG1245 169 VDLIPKVFkGTvrellEKVdERGK-LDELAEKLGLENILDRDISELSGGELQRVAIAAALLRDADFYFFDEPSSYLD--- 244
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 183 rsqfwdlidsIRQRqsnmsVLVATAYMEEAER-------------FDWL---VAMNAGEVLATGSAEELRQqTQSAtlee 246
Cdd:COG1245 245 ----------IYQR-----LNVARLIRELAEEgkyvlvvehdlaiLDYLadyVHILYGEPGVYGVVSKPKS-VRVG---- 304
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 247 afIN-----LLP----QAQRQAHQAVVIPPYQPENAEIAIEARDLTMRFGSF-VAVDHVNFRipRGEIFGFLGSNGCGKS 316
Cdd:COG1245 305 --INqyldgYLPeenvRIRDEPIEFEVHAPRREKEEETLVEYPDLTKSYGGFsLEVEGGEIR--EGEVLGIVGPNGIGKT 380
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 317 TTMKMLTGLLPASEGEawlfgqpvdpkdIDTRRRVGYMSQAFSLYNELTVRQNLelharlfhipEAEIPARV------AE 390
Cdd:COG1245 381 TFAKILAGVLKPDEGE------------VDEDLKISYKPQYISPDYDGTVEEFL----------RSANTDDFgssyykTE 438
|
410 420 430 440
....*....|....*....|....*....|....*....|....*....
gi 732682709 391 MSERFKLNDVEDILPESLPLGIRQRLSLAVAVIHRPEMLILDEPTSGVD 439
Cdd:COG1245 439 IIKPLGLEKLLDKNVKDLSGGELQRVAIAACLSRDADLYLLDEPSAHLD 487
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
33-439 |
2.19e-14 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 77.16 E-value: 2.19e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 33 LDIPARCMV-GLIGPDGVGKSSLLSLISGArvieqgnvMV--LGGDMRDP------KHRRdvcpriawmpqglGKNLYHT 103
Cdd:PRK13409 93 LPIPKEGKVtGILGPNGIGKTTAVKILSGE--------LIpnLGDYEEEPswdevlKRFR-------------GTELQNY 151
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 104 LS-VYEN----------VDFFARLF-GH-----DKAEREVRINELLTSTGLAPFRDRPAGKLSGGMKQKLGLCCALIHDP 166
Cdd:PRK13409 152 FKkLYNGeikvvhkpqyVDLIPKVFkGKvrellKKVDERGKLDEVVERLGLENILDRDISELSGGELQRVAIAAALLRDA 231
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 167 ELLILDEPTTGVDplsrsqfwdlidsIRQRqsnmsVLVATAYMEEAER------------FDWL---VAMNAGEVLATG- 230
Cdd:PRK13409 232 DFYFFDEPTSYLD-------------IRQR-----LNVARLIRELAEGkyvlvvehdlavLDYLadnVHIAYGEPGAYGv 293
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 231 -------------------SAEELRQQTQSATLEEAfinllpqaqrqahqavviPPYQPENAEIAIEARDLTMRFGSF-V 290
Cdd:PRK13409 294 vskpkgvrvgineylkgylPEENMRIRPEPIEFEER------------------PPRDESERETLVEYPDLTKKLGDFsL 355
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 291 AVDHVNFRipRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGEawlfgqpvdpkdIDTRRRVGYMSQAFSLYNELTVRQNL 370
Cdd:PRK13409 356 EVEGGEIY--EGEVIGIVGPNGIGKTTFAKLLAGVLKPDEGE------------VDPELKISYKPQYIKPDYDGTVEDLL 421
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 732682709 371 ELHARLFHIP--EAEIparvaemSERFKLNDVEDILPESLPLGIRQRLSLAVAVIHRPEMLILDEPTSGVD 439
Cdd:PRK13409 422 RSITDDLGSSyyKSEI-------IKPLQLERLLDKNVKDLSGGELQRVAIAACLSRDADLYLLDEPSAHLD 485
|
|
| CP_lyasePhnK |
TIGR02323 |
phosphonate C-P lyase system protein PhnK; Members of this family are the PhnK protein of C-P ... |
10-230 |
2.41e-14 |
|
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: 73.71 E-value: 2.41e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 10 PPVAQLAGVSQHYGKTVALNNITLDIPARCMVGLIGPDGVGKSSLLSLISGARVIEQGNVmvlGGDMRD---------PK 80
Cdd:TIGR02323 1 KPLLQVSGLSKSYGGGKGCRDVSFDLYPGEVLGIVGESGSGKSTLLGCLAGRLAPDHGTA---TYIMRSgaelelyqlSE 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 81 HRRDVCPRIAW--MPQGLGKNLYHTLSVYENV-----DFFARLFGHDKAE-----REVRINelltstgLAPFRDRPAgKL 148
Cdd:TIGR02323 78 AERRRLMRTEWgfVHQNPRDGLRMRVSAGANIgerlmAIGARHYGNIRATaqdwlEEVEID-------PTRIDDLPR-AF 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 149 SGGMKQKLGLCCALIHDPELLILDEPTTGVDPLSRSQFWDLIDSIrQRQSNMSVLVATAYMEEAERF-DWLVAMNAGEVL 227
Cdd:TIGR02323 150 SGGMQQRLQIARNLVTRPRLVFMDEPTGGLDVSVQARLLDLLRGL-VRDLGLAVIIVTHDLGVARLLaQRLLVMQQGRVV 228
|
...
gi 732682709 228 ATG 230
Cdd:TIGR02323 229 ESG 231
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
17-239 |
5.36e-14 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 73.26 E-value: 5.36e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 17 GVSQHYGKTVALNNITLDIPARCMVGLIGPDGVGKSSLLSLISGARVIEQGNVMVLGGDMRDPKHRR--DVCPRIAWMPQ 94
Cdd:PRK11831 12 GVSFTRGNRCIFDNISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEILFDGENIPAMSRSRlyTVRKRMSMLFQ 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 95 GlgKNLYHTLSVYENVDFFARlfghdkaEREVRINELLTST--------GLAPFRDRPAGKLSGGMKQKLGLCCALIHDP 166
Cdd:PRK11831 92 S--GALFTDMNVFDNVAYPLR-------EHTQLPAPLLHSTvmmkleavGLRGAAKLMPSELSGGMARRAALARAIALEP 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 732682709 167 ELLILDEPTTGVDPLSRSQFWDLIDSIRQRQSNMSVLVATAYMEEAERFDWLVAMNAGEVLATGSAEELRQQT 239
Cdd:PRK11831 163 DLIMFDEPFVGQDPITMGVLVKLISELNSALGVTCVVVSHDVPEVLSIADHAYIVADKKIVAHGSAQALQANP 235
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
12-235 |
5.63e-14 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 73.10 E-value: 5.63e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 12 VAQLAG--VSQHYGKTVALNNITLDIPARCMVGLIGPDGVGKSSLLSLISGARVIEQGNVMvLGGDMRDPKHRRDVCPRI 89
Cdd:PRK10253 5 VARLRGeqLTLGYGKYTVAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVW-LDGEHIQHYASKEVARRI 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 90 AWMPQGlgKNLYHTLSVYENVdffAR-------LFGHDKAEREVRINELLTSTGLAPFRDRPAGKLSGGMKQKLGLCCAL 162
Cdd:PRK10253 84 GLLAQN--ATTPGDITVQELV---ARgryphqpLFTRWRKEDEEAVTKAMQATGITHLADQSVDTLSGGQRQRAWIAMVL 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 732682709 163 IHDPELLILDEPTTGVDPLSRSQFWDLIDSIrQRQSNMSVLVATAYMEEAERF-DWLVAMNAGEVLATGSAEEL 235
Cdd:PRK10253 159 AQETAIMLLDEPTTWLDISHQIDLLELLSEL-NREKGYTLAAVLHDLNQACRYaSHLIALREGKIVAQGAPKEI 231
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
15-229 |
6.47e-14 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 72.80 E-value: 6.47e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 15 LAGVSQHygKTVaLNNITLDIPARCMVGLIGPDGVGKSSLLSLISGARVIEQGNVMVLGGDMRDPKH------RRD---- 84
Cdd:PRK10419 18 LSGKHQH--QTV-LNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWRGEPLAKLNRaqrkafRRDiqmv 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 85 -------VCPR--IAWMpqgLGKNLYHTLSVyenvdffarlfghDKAEREVRINELLTSTGLAP-FRDRPAGKLSGGMKQ 154
Cdd:PRK10419 95 fqdsisaVNPRktVREI---IREPLRHLLSL-------------DKAERLARASEMLRAVDLDDsVLDKRPPQLSGGQLQ 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 732682709 155 KLGLCCALIHDPELLILDEPTTGVDPLSRSQFWDLIDSIRQrQSNMSVLVATAYMEEAERFDWLVA-MNAGEVLAT 229
Cdd:PRK10419 159 RVCLARALAVEPKLLILDEAVSNLDLVLQAGVIRLLKKLQQ-QFGTACLFITHDLRLVERFCQRVMvMDNGQIVET 233
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
186-500 |
1.24e-13 |
|
multi drug resistance-associated protein (MRP); This model describes multi drug resistance-associated protein (MRP) in eukaryotes. The multidrug resistance-associated protein is an integral membrane protein that causes multidrug resistance when overexpressed in mammalian cells. It belongs to ABC transporter superfamily. The protein topology and function was experimentally demonstrated by epitope tagging and immunofluorescence. Insertion of tags in the critical regions associated with drug efflux, abrogated its function. The C-terminal domain seem to highly conserved. [Transport and binding proteins, Other]
Pssm-ID: 188098 [Multi-domain] Cd Length: 1522 Bit Score: 75.37 E-value: 1.24e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 186 FWDLIDSIRQRQsnMSVLVATAYMEEAERFDW-----LVAMNAGEVLATGSAEELRQQTQSATLEEAF------INLLPQ 254
Cdd:TIGR00957 518 FLDKVEGIRQEE--LKVLKKSAYLHAVGTFTWvctpfLVALITFAVYVTVDENNILDAEKAFVSLALFnilrfpLNILPM 595
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 255 AQRQAHQAVV------IPPYQPENAEIAIEAR--------DLTMRFGSFV-------AVDHVNFRIPRGEIFGFLGSNGC 313
Cdd:TIGR00957 596 VISSIVQASVslkrlrIFLSHEELEPDSIERRtikpgegnSITVHNATFTwardlppTLNGITFSIPEGALVAVVGQVGC 675
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 314 GKSTTMKMLTGLLPASEGEAWLFGQpvdpkdidtrrrVGYMSQAFSLYNElTVRQNLelharLFHIPEAEiPARVAEMSE 393
Cdd:TIGR00957 676 GKSSLLSALLAEMDKVEGHVHMKGS------------VAYVPQQAWIQND-SLRENI-----LFGKALNE-KYYQQVLEA 736
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 394 RFKLNDVEdILPE-----------SLPLGIRQRLSLAVAVIHRPEMLILDEPTSGVDP-VARDMFWQLMVDLSRQDKVTI 461
Cdd:TIGR00957 737 CALLPDLE-ILPSgdrteigekgvNLSGGQKQRVSLARAVYSNADIYLFDDPLSAVDAhVGKHIFEHVIGPEGVLKNKTR 815
|
330 340 350
....*....|....*....|....*....|....*....
gi 732682709 462 FISTHFMNEAERCDRISLMHAGKVLASGTPQELVEKRGA 500
Cdd:TIGR00957 816 ILVTHGISYLPQVDVIIVMSGGKISEMGSYQELLQRDGA 854
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
14-195 |
1.29e-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: 69.01 E-value: 1.29e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 14 QLAGVSQHYGKTVALNNITLDIPARCMVGLIGPDGVGKSSLLSLISGARVIEQGNVmvlggdmrdpkhRRDVCPRIAWMP 93
Cdd:cd03221 2 ELENLSKTYGGKLLLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIV------------TWGSTVKIGYFE 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 94 QglgknlyhtlsvyenvdffarlfghdkaerevrinelltstglapfrdrpagkLSGGMKQKLGLCCALIHDPELLILDE 173
Cdd:cd03221 70 Q-----------------------------------------------------LSGGEKMRLALAKLLLENPNLLLLDE 96
|
170 180
....*....|....*....|..
gi 732682709 174 PTTGVDPLSRSQfwdLIDSIRQ 195
Cdd:cd03221 97 PTNHLDLESIEA---LEEALKE 115
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
291-473 |
1.63e-13 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 70.67 E-value: 1.63e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 291 AVDHVNFRIPRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGEAWLFGQPVDP-KDIDT---RRRVGYMSQAFSLYNELTV 366
Cdd:PRK10908 17 ALQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDITRlKNREVpflRRQIGMIFQDHHLLMDRTV 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 367 RQNLELHARLFHIPEAEIPARVAEMSERFKLNDVEDILPESLPLGIRQRLSLAVAVIHRPEMLILDEPTSGVDPVARDMF 446
Cdd:PRK10908 97 YDNVAIPLIIAGASGDDIRRRVSAALDKVGLLDKAKNFPIQLSGGEQQRVGIARAVVNKPAVLLADEPTGNLDDALSEGI 176
|
170 180
....*....|....*....|....*..
gi 732682709 447 WQLMVDLSRQDkVTIFISTHFMNEAER 473
Cdd:PRK10908 177 LRLFEEFNRVG-VTVLMATHDIGLISR 202
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
27-235 |
1.85e-13 |
|
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: 73.98 E-value: 1.85e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 27 ALNNITLDIPARCMVGLIGPDGVGKSSLLSLISGARVIEQGNVMVLGGDMRDPKhRRDVCPRIAWMPQGLgkNLYHTlSV 106
Cdd:TIGR02203 347 ALDSISLVIEPGETVALVGRSGSGKSTLVNLIPRFYEPDSGQILLDGHDLADYT-LASLRRQVALVSQDV--VLFND-TI 422
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 107 YENVDFFARlfghDKAEREvRINELLTSTGLAPFRDR-PAG----------KLSGGMKQKLGLCCALIHDPELLILDEPT 175
Cdd:TIGR02203 423 ANNIAYGRT----EQADRA-EIERALAAAYAQDFVDKlPLGldtpigengvLLSGGQRQRLAIARALLKDAPILILDEAT 497
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 176 TGVDPLSRSQFWDLIDSIRQrqsNMSVLVATAYMEEAERFDWLVAMNAGEVLATGSAEEL 235
Cdd:TIGR02203 498 SALDNESERLVQAALERLMQ---GRTTLVIAHRLSTIEKADRIVVMDDGRIVERGTHNEL 554
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
20-246 |
1.88e-13 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 71.15 E-value: 1.88e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 20 QHYGKTVALNNITLDIPARCMVGLIGPDGVGKSSLLSLISGARVIEQGNVMVLGGDMR------------DPKHRRDVCP 87
Cdd:PRK10619 13 KRYGEHEVLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNGQTINlvrdkdgqlkvaDKNQLRLLRT 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 88 RIAWMPQGLgkNLYHTLSVYENV-DFFARLFGHDKAEREVRINELLTSTGLApfrDRPAGK----LSGGMKQKLGLCCAL 162
Cdd:PRK10619 93 RLTMVFQHF--NLWSHMTVLENVmEAPIQVLGLSKQEARERAVKYLAKVGID---ERAQGKypvhLSGGQQQRVSIARAL 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 163 IHDPELLILDEPTTGVDPLSRSQFWDLIDSIRQRQSNMsvLVATAYMEEAERF-DWLVAMNAGEVLATGSAEELRQQTQS 241
Cdd:PRK10619 168 AMEPEVLLFDEPTSALDPELVGEVLRIMQQLAEEGKTM--VVVTHEMGFARHVsSHVIFLHQGKIEEEGAPEQLFGNPQS 245
|
....*
gi 732682709 242 ATLEE 246
Cdd:PRK10619 246 PRLQQ 250
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
41-204 |
1.92e-13 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 70.58 E-value: 1.92e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 41 VGLIGPDGVGKSSLLSLISGARVIEQGNVMVLGgdmrDPKHRRDVCPRIAWMPQGLGK-----NLYHTLSVYENVDFFAR 115
Cdd:PRK10584 39 IALIGESGSGKSTLLAILAGLDDGSSGEVSLVG----QPLHQMDEEARAKLRAKHVGFvfqsfMLIPTLNALENVELPAL 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 116 LFGHDKAEREVRINELLTSTGLAPFRDRPAGKLSGGMKQKLGLCCALIHDPELLILDEPTTGVDPLSRSQFWDLIDSIRQ 195
Cdd:PRK10584 115 LRGESSRQSRNGAKALLEQLGLGKRLDHLPAQLSGGEQQRVALARAFNGRPDVLFADEPTGNLDRQTGDKIADLLFSLNR 194
|
....*....
gi 732682709 196 RQSNMSVLV 204
Cdd:PRK10584 195 EHGTTLILV 203
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
32-214 |
2.19e-13 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 70.77 E-value: 2.19e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 32 TLDIPARCMVGLIGPDGVGKSSLLSLISGARVIEQGNVMVLGGDMRD-PKHRRDVcpriAWMPQGlgKNLYHTLSVYENV 110
Cdd:PRK10771 19 DLTVERGERVAILGPSGAGKSTLLNLIAGFLTPASGSLTLNGQDHTTtPPSRRPV----SMLFQE--NNLFSHLTVAQNI 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 111 ----DFFARLFGHDKAEREvrinELLTSTGLAPFRDRPAGKLSGGMKQKLGLCCALIHDPELLILDEPTTGVDPLSRSQF 186
Cdd:PRK10771 93 glglNPGLKLNAAQREKLH----AIARQMGIEDLLARLPGQLSGGQRQRVALARCLVREQPILLLDEPFSALDPALRQEM 168
|
170 180
....*....|....*....|....*....
gi 732682709 187 WDLIDSI-RQRQsnMSVLVATAYMEEAER 214
Cdd:PRK10771 169 LTLVSQVcQERQ--LTLLMVSHSLEDAAR 195
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
228-500 |
2.93e-13 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 73.73 E-value: 2.93e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 228 ATGSAEELrqqtqsatleEAFINLLPQAQRQAHQAVvippyqPENAEIAIEARDLTMRF--GSfVAVDHVNFRIPRGEIF 305
Cdd:PRK11174 317 AVGAAESL----------VTFLETPLAHPQQGEKEL------ASNDPVTIEAEDLEILSpdGK-TLAGPLNFTLPAGQRI 379
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 306 GFLGSNGCGKSTTMKMLTGLLPaSEGEAWLFGQPVDPKDIDT-RRRVGYMSQAFSLYnELTVRQNLELHArlfhiPEAEi 384
Cdd:PRK11174 380 ALVGPSGAGKTSLLNALLGFLP-YQGSLKINGIELRELDPESwRKHLSWVGQNPQLP-HGTLRDNVLLGN-----PDAS- 451
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 385 PARVAEMSERFKLNDVEDILPESL--PLGIR---------QRLSLAVAVIHRPEMLILDEPTSGVDPVARDMFWQLMVDL 453
Cdd:PRK11174 452 DEQLQQALENAWVSEFLPLLPQGLdtPIGDQaaglsvgqaQRLALARALLQPCQLLLLDEPTASLDAHSEQLVMQALNAA 531
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 732682709 454 SRQdKVTIFIsTHFMNEAERCDRISLMHAGKVLASGTPQELVEKRGA 500
Cdd:PRK11174 532 SRR-QTTLMV-THQLEDLAQWDQIWVMQDGQIVQQGDYAELSQAGGL 576
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
277-494 |
3.12e-13 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 70.57 E-value: 3.12e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 277 IEARDLTMRFGSFVAVDHVNFRIPRGEIFGFLGSNGCGKSTTMKMLT---GLLP--ASEGEAWLFGQPVDPKDIDT---R 348
Cdd:PRK14239 6 LQVSDLSVYYNKKKALNSVSLDFYPNEITALIGPSGSGKSTLLRSINrmnDLNPevTITGSIVYNGHNIYSPRTDTvdlR 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 349 RRVGYMSQA-----FSLYneltvrQNLELHARLFHIPEAEIPARVAEMSERFK--LNDVEDILPES---LPLGIRQRLSL 418
Cdd:PRK14239 86 KEIGMVFQQpnpfpMSIY------ENVVYGLRLKGIKDKQVLDEAVEKSLKGAsiWDEVKDRLHDSalgLSGGQQQRVCI 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 732682709 419 AVAVIHRPEMLILDEPTSGVDPVARDMFWQLMVDLsrQDKVTIFISTHFMNEAER-CDRISLMHAGKVLASGTPQEL 494
Cdd:PRK14239 160 ARVLATSPKIILLDEPTSALDPISAGKIEETLLGL--KDDYTMLLVTRSMQQASRiSDRTGFFLDGDLIEYNDTKQM 234
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
11-214 |
4.06e-13 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 70.45 E-value: 4.06e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 11 PVAQLAGVSQHYGKTVALNNITLDIPARCMVGLIGPDGVGKSSLLSLISGARVIE-----QGNVMVLGGDMRDPKHRRDV 85
Cdd:PRK14258 6 PAIKVNNLSFYYDTQKILEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLNRMNELEsevrvEGRVEFFNQNIYERRVNLNR 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 86 CPRIAWM--PQglgKNLYhTLSVYENVDFFARLFG-HDKAEREVRINELLTSTGL----APFRDRPAGKLSGGMKQKLGL 158
Cdd:PRK14258 86 LRRQVSMvhPK---PNLF-PMSVYDNVAYGVKIVGwRPKLEIDDIVESALKDADLwdeiKHKIHKSALDLSGGQQQRLCI 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 732682709 159 CCALIHDPELLILDEPTTGVDPLSRSQFWDLIDSIRQRqSNMSVLVATAYMEEAER 214
Cdd:PRK14258 162 ARALAVKPKVLLMDEPCFGLDPIASMKVESLIQSLRLR-SELTMVIVSHNLHQVSR 216
|
|
| PRK15093 |
PRK15093 |
peptide ABC transporter ATP-binding protein SapD; |
277-495 |
4.74e-13 |
|
peptide ABC transporter ATP-binding protein SapD;
Pssm-ID: 185049 [Multi-domain] Cd Length: 330 Bit Score: 71.37 E-value: 4.74e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 277 IEARDLTMRF----GSFVAVDHVNFRIPRGEIFGFLGSNGCGKSTTMKMLTGLlpasEGEAW-LFGQPVDPKDID----- 346
Cdd:PRK15093 4 LDIRNLTIEFktsdGWVKAVDRVSMTLTEGEIRGLVGESGSGKSLIAKAICGV----TKDNWrVTADRMRFDDIDllrls 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 347 ---TRRRVGY-MSQAFSlynelTVRQNLELHARLFHIPEAEIPA----------------RVAEMSERFKLNDVEDIL-- 404
Cdd:PRK15093 80 preRRKLVGHnVSMIFQ-----EPQSCLDPSERVGRQLMQNIPGwtykgrwwqrfgwrkrRAIELLHRVGIKDHKDAMrs 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 405 -PESLPLGIRQRLSLAVAVIHRPEMLILDEPTSGVDPVARDMFWQLMVDLSRQDKVTIFISTHFMNEAER-CDRISLMHA 482
Cdd:PRK15093 155 fPYELTEGECQKVMIAIALANQPRLLIADEPTNAMEPTTQAQIFRLLTRLNQNNNTTILLISHDLQMLSQwADKINVLYC 234
|
250
....*....|...
gi 732682709 483 GKVLASGTPQELV 495
Cdd:PRK15093 235 GQTVETAPSKELV 247
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
23-242 |
8.08e-13 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 69.74 E-value: 8.08e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 23 GKTVaLNNITLDIPARCMVGLIGPDGVGKSSLLSL-------ISGARVieQGNVMvLGGdmRDPKHRRDVCP---RIAWM 92
Cdd:PRK14271 33 GKTV-LDQVSMGFPARAVTSLMGPTGSGKTTFLRTlnrmndkVSGYRY--SGDVL-LGG--RSIFNYRDVLEfrrRVGML 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 93 PQglgKNLYHTLSVYENVdfFARLFGHDKAER-EVR--INELLTSTGL-APFRDRPAG---KLSGGMKQKLGLCCALIHD 165
Cdd:PRK14271 107 FQ---RPNPFPMSIMDNV--LAGVRAHKLVPRkEFRgvAQARLTEVGLwDAVKDRLSDspfRLSGGQQQLLCLARTLAVN 181
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 732682709 166 PELLILDEPTTGVDPLSRSQFWDLIDSIRQRqsnMSVLVATAYMEEAERF-DWLVAMNAGEVLATGSAEELRQQTQSA 242
Cdd:PRK14271 182 PEVLLLDEPTSALDPTTTEKIEEFIRSLADR---LTVIIVTHNLAQAARIsDRAALFFDGRLVEEGPTEQLFSSPKHA 256
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
282-527 |
8.29e-13 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 70.54 E-value: 8.29e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 282 LTMRFGS----FVAVDHVNFRIPRGEIFGFLGSNGCGKSTTMKMLTGLL--PAS-EGEAWLFGQpVDPKDIDTRRR---V 351
Cdd:PRK11022 9 LSVHFGDesapFRAVDRISYSVKQGEVVGIVGESGSGKSVSSLAIMGLIdyPGRvMAEKLEFNG-QDLQRISEKERrnlV 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 352 GY-MSQAF-----SLYNELTVRqnlelharlFHIPEA----------EIPARVAEMSERFKLNDVE---DILPESLPLGI 412
Cdd:PRK11022 88 GAeVAMIFqdpmtSLNPCYTVG---------FQIMEAikvhqggnkkTRRQRAIDLLNQVGIPDPAsrlDVYPHQLSGGM 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 413 RQRLSLAVAVIHRPEMLILDEPTSGVDPVARDMFWQLMVDLSRQDKVTIFISTHFMN-EAERCDRISLMHAGKVLASGTP 491
Cdd:PRK11022 159 SQRVMIAMAIACRPKLLIADEPTTALDVTIQAQIIELLLELQQKENMALVLITHDLAlVAEAAHKIIVMYAGQVVETGKA 238
|
250 260 270
....*....|....*....|....*....|....*..
gi 732682709 492 QELVeKRGAASLEEAFIAYLQE-AAGQSNEAEAPPVV 527
Cdd:PRK11022 239 HDIF-RAPRHPYTQALLRALPEfAQDKARLASLPGVV 274
|
|
| ABC2_membrane |
pfam01061 |
ABC-2 type transporter; |
724-874 |
1.35e-12 |
|
ABC-2 type transporter;
Pssm-ID: 426023 [Multi-domain] Cd Length: 204 Bit Score: 67.68 E-value: 1.35e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 724 LLLMMIPSMLSALSVVREKELGSIINLYVTPT-TRSEFLLGKQLPYIALGMLNFFLLCGLSVFVFGVP-HKGSFLTLTLA 801
Cdd:pfam01061 53 SILFNAFSALSGISPVFEKERGVLYRELASPLySPSAYVLAKILSELPLSLLQSLIFLLIVYFMVGLPpSAGRFFLFLLV 132
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 732682709 802 ALLYIIIATGMGLLISTFMKSQIAAIFGTAIITLiPATQFSGMIDPVASLEGPGRWIGEVYPTSHFLTIARGT 874
Cdd:pfam01061 133 LLLTALAASSLGLFISALAPSFEDASQLGPLVLL-PLLLLSGFFIPIDSMPVWWQWIYYLNPLTYAIEALRAN 204
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
18-235 |
1.74e-12 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 68.24 E-value: 1.74e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 18 VSQHYGKTVaLNNITLDIPARCMVGLIGPDGVGKSSLLSLISGARVIEQGNVMVlgGDMRDPKHR---------RDVCPR 88
Cdd:PRK11264 10 VKKFHGQTV-LHGIDLEVKPGEVVAIIGPSGSGKTTLLRCINLLEQPEAGTIRV--GDITIDTARslsqqkgliRQLRQH 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 89 IAWMPQGLgkNLYHTLSVYENV-DFFARLFGHDKAEREVRINELLTSTGLAPFRDRPAGKLSGGMKQKLGLCCALIHDPE 167
Cdd:PRK11264 87 VGFVFQNF--NLFPHRTVLENIiEGPVIVKGEPKEEATARARELLAKVGLAGKETSYPRRLSGGQQQRVAIARALAMRPE 164
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 168 LLILDEPTTGVDPlsrSQFWDLIDSIRQ-RQSNMSVLVATAYMEEA-ERFDWLVAMNAGEVLATGSAEEL 235
Cdd:PRK11264 165 VILFDEPTSALDP---ELVGEVLNTIRQlAQEKRTMVIVTHEMSFArDVADRAIFMDQGRIVEQGPAKAL 231
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
14-253 |
2.06e-12 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 69.49 E-value: 2.06e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 14 QLAGVSQHY-GKTVALNNITLDIPARCMVGLIGPDGVGKSSLLSLISGARVIEQGNVMVlgGDMR----DPKHRRdvcpr 88
Cdd:PRK11650 5 KLQAVRKSYdGKTQVIKGIDLDVADGEFIVLVGPSGCGKSTLLRMVAGLERITSGEIWI--GGRVvnelEPADRD----- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 89 IAWMPQglgkN--LYHTLSVYENVDFFARLFGHDKAEREVRINELLTSTGLAPFRDRPAGKLSGGMKQKLGLCCALIHDP 166
Cdd:PRK11650 78 IAMVFQ----NyaLYPHMSVRENMAYGLKIRGMPKAEIEERVAEAARILELEPLLDRKPRELSGGQRQRVAMGRAIVREP 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 167 ELLILDEPTTGVDPLSRSQFWDLIDSIRQRQSNMSVLVATAYMEEAERFDWLVAMNAGEVLATGSAEELRQQTQSaTLEE 246
Cdd:PRK11650 154 AVFLFDEPLSNLDAKLRVQMRLEIQRLHRRLKTTSLYVTHDQVEAMTLADRVVVMNGGVAEQIGTPVEVYEKPAS-TFVA 232
|
250
....*....|..
gi 732682709 247 AFI-----NLLP 253
Cdd:PRK11650 233 SFIgspamNLLD 244
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
277-511 |
2.43e-12 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 67.60 E-value: 2.43e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 277 IEARDLTMRFGSFVAVDHVNFRIPRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGEAWLFGQPVD--PKDIDTRRRVGYM 354
Cdd:PRK11614 6 LSFDKVSAHYGKIQALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDGKDITdwQTAKIMREAVAIV 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 355 SQAFSLYNELTVRQNLELHArlFHIPEAEIPARVAEMSERF-KLNDVEDILPESLPLGIRQRLSLAVAVIHRPEMLILDE 433
Cdd:PRK11614 86 PEGRRVFSRMTVEENLAMGG--FFAERDQFQERIKWVYELFpRLHERRIQRAGTMSGGEQQMLAIGRALMSQPRLLLLDE 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 434 PTSGVDPVARDMFWQLMVDLsRQDKVTIFISTHFMNEAercdrISLMHAGKVLASGtpQELVEKRGAASLEEAFI--AYL 511
Cdd:PRK11614 164 PSLGLAPIIIQQIFDTIEQL-REQGMTIFLVEQNANQA-----LKLADRGYVLENG--HVVLEDTGDALLANEAVrsAYL 235
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
277-434 |
3.11e-12 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 66.37 E-value: 3.11e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 277 IEARDLTMRFGSFVAVDHVNFRIPRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGEAWLFGQPVDPKDIDTRRRVGYMSQ 356
Cdd:PRK13538 2 LEARNLACERDERILFSGLSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVLWQGEPIRRQRDEYHQDLLYLGH 81
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 732682709 357 AFSLYNELTVRQNLELHARLFHIPEAEipaRVAEMSERFKLNDVEDILPESLPLGIRQRLSLAVAVIHRPEMLILDEP 434
Cdd:PRK13538 82 QPGIKTELTALENLRFYQRLHGPGDDE---ALWEALAQVGLAGFEDVPVRQLSAGQQRRVALARLWLTRAPLWILDEP 156
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
11-235 |
5.98e-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: 69.06 E-value: 5.98e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 11 PVAQLAGVSQHY-----GKTVALNNITLDIPARCMVGLIGPDGVGKSSLLSLISGARVIEQGNVMVLGG----DMRDPK- 80
Cdd:TIGR03269 278 PIIKVRNVSKRYisvdrGVVKAVDNVSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGEVNVRVGdewvDMTKPGp 357
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 81 -HRRDVCPRIAWMPQGLGknLYHTLSVYENV---------DFFARL----------FGHDKAErevrinELLtstglapf 140
Cdd:TIGR03269 358 dGRGRAKRYIGILHQEYD--LYPHRTVLDNLteaiglelpDELARMkavitlkmvgFDEEKAE------EIL-------- 421
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 141 rDRPAGKLSGGMKQKLGLCCALIHDPELLILDEPTTGVDPLSRSQFWDLIDSIRQRQSNMSVLVATAYMEEAERFDWLVA 220
Cdd:TIGR03269 422 -DKYPDELSEGERHRVALAQVLIKEPRIVILDEPTGTMDPITKVDVTHSILKAREEMEQTFIIVSHDMDFVLDVCDRAAL 500
|
250
....*....|....*
gi 732682709 221 MNAGEVLATGSAEEL 235
Cdd:TIGR03269 501 MRDGKIVKIGDPEEI 515
|
|
| BtuD |
COG4138 |
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ... |
28-248 |
6.18e-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: 6.18e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 28 LNNITLDIPARCMVGLIGPDGVGKSSLLSLISGArVIEQGNVMVLGGDMRDPK-----HRRdvcpriAWMPQglgknlyH 102
Cdd:COG4138 12 LGPISAQVNAGELIHLIGPNGAGKSTLLARMAGL-LPGQGEILLNGRPLSDWSaaelaRHR------AYLSQ-------Q 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 103 TLS-----VYENVDFFARLfGHDKAEREVRINELLTSTGLAPFRDRPAGKLSGGMKQKLGLCCAL--IH---DPE--LLI 170
Cdd:COG4138 78 QSPpfampVFQYLALHQPA-GASSEAVEQLLAQLAEALGLEDKLSRPLTQLSGGEWQRVRLAAVLlqVWptiNPEgqLLL 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 171 LDEPTTGVDPLSRSQFWDLIDSIRQRQsnMSVLVATAYMEEAERF-D--WLvaMNAGEVLATGSAEELRQQtqsATLEEA 247
Cdd:COG4138 157 LDEPMNSLDVAQQAALDRLLRELCQQG--ITVVMSSHDLNHTLRHaDrvWL--LKQGKLVASGETAEVMTP---ENLSEV 229
|
.
gi 732682709 248 F 248
Cdd:COG4138 230 F 230
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
308-483 |
6.29e-12 |
|
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding cassette transporters; The pleiotropic drug resistance (PDR) is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. This PDR subfamily represents domain I of its (ABC-IM)2 organization. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds including sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213199 [Multi-domain] Cd Length: 192 Bit Score: 65.34 E-value: 6.29e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 308 LGSNGCGKSTTMKMLTGLLPAS--EGEAWLFGQPvdpKDIDTRRRVGYMSQAFSLYNELTVRQNLELHARLfhipeaeip 385
Cdd:cd03232 39 MGESGAGKTTLLDVLAGRKTAGviTGEILINGRP---LDKNFQRSTGYVEQQDVHSPNLTVREALRFSALL--------- 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 386 arvaemserfklndvedilpESLPLGIRQRLSLAVAVIHRPEMLILDEPTSGVDPVARDMFWQLMVDLSRQDKvTIFIST 465
Cdd:cd03232 107 --------------------RGLSVEQRKRLTIGVELAAKPSILFLDEPTSGLDSQAAYNIVRFLKKLADSGQ-AILCTI 165
|
170 180
....*....|....*....|
gi 732682709 466 HFMNEA--ERCDRISLMHAG 483
Cdd:cd03232 166 HQPSASifEKFDRLLLLKRG 185
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
14-237 |
8.45e-12 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 68.98 E-value: 8.45e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 14 QLAGVSQHY----GKTVALNNITLDIPARCMVGLIGPDGVGKSSLLSLI-------SGARVIEQGNVMVLGGDMRDPKHR 82
Cdd:PRK10535 6 ELKDIRRSYpsgeEQVEVLKGISLDIYAGEMVAIVGASGSGKSTLMNILgcldkptSGTYRVAGQDVATLDADALAQLRR 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 83 RDVcpriawmpqGLGKNLYHTLS---VYENVDFFARLFGHDKAEREVRINELLTSTGLAPFRDRPAGKLSGGMKQKLGLC 159
Cdd:PRK10535 86 EHF---------GFIFQRYHLLShltAAQNVEVPAVYAGLERKQRLLRAQELLQRLGLEDRVEYQPSQLSGGQQQRVSIA 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 732682709 160 CALIHDPELLILDEPTTGVDPLSRSQFWDLIDSIRQRqsNMSVLVATAYMEEAERFDWLVAMNAGEVLATGSAEELRQ 237
Cdd:PRK10535 157 RALMNGGQVILADEPTGALDSHSGEEVMAILHQLRDR--GHTVIIVTHDPQVAAQAERVIEIRDGEIVRNPPAQEKVN 232
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
266-466 |
1.06e-11 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 65.36 E-value: 1.06e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 266 PPYQPENAEIAIEARDLTMRFGSFVAVDHVNFRIPRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGEAWlfgqpVDPKDI 345
Cdd:COG2401 20 VLDLSERVAIVLEAFGVELRVVERYVLRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGALKGTPVAGC-----VDVPDN 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 346 DtrrrvgymsqafsLYNELTVRQNLelhARLFHIPEA-EIPARVaemserfKLNDVEDIL--PESLPLGIRQRLSLAVAV 422
Cdd:COG2401 95 Q-------------FGREASLIDAI---GRKGDFKDAvELLNAV-------GLSDAVLWLrrFKELSTGQKFRFRLALLL 151
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 732682709 423 IHRPEMLILDEPTSGVDP-----VARDmfwqlMVDLSRQDKVTIFISTH 466
Cdd:COG2401 152 AERPKLLVIDEFCSHLDRqtakrVARN-----LQKLARRAGITLVVATH 195
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
23-564 |
1.19e-11 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 68.66 E-value: 1.19e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 23 GKTVALNNITLDIPARCMVGLIGPDGVGKSSLLSLISGARVIEQGNVMVLGGdmrdpkhrrdvcPRIAWMPQGL------ 96
Cdd:PRK10636 12 GVRVLLDNATATINPGQKVGLVGKNGCGKSTLLALLKNEISADGGSYTFPGN------------WQLAWVNQETpalpqp 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 97 -------GKNLYHTLS-----VYENVDFFARLFGHDKAER------EVRINELLTSTGLA-PFRDRPAGKLSGGMKQKLG 157
Cdd:PRK10636 80 aleyvidGDREYRQLEaqlhdANERNDGHAIATIHGKLDAidawtiRSRAASLLHGLGFSnEQLERPVSDFSGGWRMRLN 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 158 LCCALIHDPELLILDEPTTGVDP-----LSR------------SQFWDLIDSIRQRqsnmsvlvaTAYMEEAERFDWLVA 220
Cdd:PRK10636 160 LAQALICRSDLLLLDEPTNHLDLdaviwLEKwlksyqgtliliSHDRDFLDPIVDK---------IIHIEQQSLFEYTGN 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 221 MNAGEV-----LATGSAEELRQQTQSATLEeAFINLLPQAQRQAHQA-----------VVIP-----PY-----QPE--- 271
Cdd:PRK10636 231 YSSFEVqratrLAQQQAMYESQQERVAHLQ-SYIDRFRAKATKAKQAqsrikmlermeLIAPahvdnPFhfsfrAPEslp 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 272 NAEIAIEarDLTMRFGSFVAVDHVNFRIPRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGEAWLfgqpvdPKDIdtrrRV 351
Cdd:PRK10636 310 NPLLKME--KVSAGYGDRIILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELAPVSGEIGL------AKGI----KL 377
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 352 GYMSQafslyneltvrQNLEL----HARLFHIpeAEIPARVAEMSER-------FKLNDVEDIlPESLPLGIRQRLSLAV 420
Cdd:PRK10636 378 GYFAQ-----------HQLEFlradESPLQHL--ARLAPQELEQKLRdylggfgFQGDKVTEE-TRRFSGGEKARLVLAL 443
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 421 AVIHRPEMLILDEPTSGVDPVARDMFWQLMVDLsrqDKVTIFIS--THFMNEAerCDRISLMHAGKVlasgtpqelveKR 498
Cdd:PRK10636 444 IVWQRPNLLLLDEPTNHLDLDMRQALTEALIDF---EGALVVVShdRHLLRST--TDDLYLVHDGKV-----------EP 507
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 732682709 499 GAASLEEaFIAYLQEAAGQSNEAEAPPvvhdtthAPRQGFSLRRLFSYSRREAlELRR--DPVRSTLA 564
Cdd:PRK10636 508 FDGDLED-YQQWLSDVQKQENQTDEAP-------KENNANSAQARKDQKRREA-ELRTqtQPLRKEIA 566
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
11-179 |
1.53e-11 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 66.68 E-value: 1.53e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 11 PVAQLAGVSQHY-------GKTV----ALNNITLDIPARCMVGLIGPDGVGKSSL----LSLI---SGARVIEQGNVMVL 72
Cdd:COG4608 6 PLLEVRDLKKHFpvrgglfGRTVgvvkAVDGVSFDIRRGETLGLVGESGCGKSTLgrllLRLEeptSGEILFDGQDITGL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 73 GG-DMRdpKHRRDV-----------CPRiawmpqglgknlyhtLSVYENVDFFARLFG-HDKAEREVRINELLTSTGLAP 139
Cdd:COG4608 86 SGrELR--PLRRRMqmvfqdpyaslNPR---------------MTVGDIIAEPLRIHGlASKAERRERVAELLELVGLRP 148
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 732682709 140 -FRDRPAGKLSGGMKQKLGLCCALIHDPELLILDEPTTGVD 179
Cdd:COG4608 149 eHADRYPHEFSGGQRQRIGIARALALNPKLIVCDEPVSALD 189
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
41-239 |
1.59e-11 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 67.72 E-value: 1.59e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 41 VGLIGPDGVGKSSLLSLISGARVIEQGNVMVLGgdmrdpkhrRDVCPRiawMPQ-GL------------GKNLYHTLSVY 107
Cdd:PRK10762 281 LGVSGLMGAGRTELMKVLYGALPRTSGYVTLDG---------HEVVTR---SPQdGLangivyisedrkRDGLVLGMSVK 348
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 108 EN-----VDFFARLFGHDKAERE-------VRINELLTstglaPFRDRPAGKLSGGMKQKLGLCCALIHDPELLILDEPT 175
Cdd:PRK10762 349 ENmsltaLRYFSRAGGSLKHADEqqavsdfIRLFNIKT-----PSMEQAIGLLSGGNQQKVAIARGLMTRPKVLILDEPT 423
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 732682709 176 TGVDPLSRSQFWDLIDsiRQRQSNMSVLVATAYMEEAERF-DWLVAMNAGEVLATGSAEELRQQT 239
Cdd:PRK10762 424 RGVDVGAKKEIYQLIN--QFKAEGLSIILVSSEMPEVLGMsDRILVMHEGRISGEFTREQATQEK 486
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
118-235 |
1.62e-11 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 66.69 E-value: 1.62e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 118 GHDKAEREVRINELLTSTGLAPFRDR----PAgKLSGGMKQKLGLCCALIHDPELLILDEPTTGVDPLSRSQFWDLIDSI 193
Cdd:PRK11022 121 GGNKKTRRQRAIDLLNQVGIPDPASRldvyPH-QLSGGMSQRVMIAMAIACRPKLLIADEPTTALDVTIQAQIIELLLEL 199
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 732682709 194 rQRQSNMSVLVATAYME-EAERFDWLVAMNAGEVLATGSAEEL 235
Cdd:PRK11022 200 -QQKENMALVLITHDLAlVAEAAHKIIVMYAGQVVETGKAHDI 241
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
27-225 |
2.05e-11 |
|
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: 64.03 E-value: 2.05e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 27 ALNNITLDIPARCMVGLIGPDGVGKSSLLSLISGARVIEQGNVMVLGgdmrdpkhRRDVCPRIAWMPQGlgknlyhtlSV 106
Cdd:cd03250 20 TLKDINLEVPKGELVAIVGPVGSGKSSLLSALLGELEKLSGSVSVPG--------SIAYVSQEPWIQNG---------TI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 107 YENVdffarLFGHDkaEREVRINELLTSTGLAP-FRDRPAG----------KLSGGMKQKLGLCCALIHDPELLILDEPT 175
Cdd:cd03250 83 RENI-----LFGKP--FDEERYEKVIKACALEPdLEILPDGdlteigekgiNLSGGQKQRISLARAVYSDADIYLLDDPL 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 732682709 176 TGVDPLSRSQFWDliDSIRQRQSNMS-VLVATAYMEEAERFDWLVAMNAGE 225
Cdd:cd03250 156 SAVDAHVGRHIFE--NCILGLLLNNKtRILVTHQLQLLPHADQIVVLDNGR 204
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
292-483 |
2.12e-11 |
|
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: 64.66 E-value: 2.12e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 292 VDHVNFRIPRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGEA-WLFGQPVDPKDIDTRRR----VGYMSQAFSLYNElTV 366
Cdd:cd03290 17 LSNINIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVhWSNKNESEPSFEATRSRnrysVAYAAQKPWLLNA-TV 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 367 RQNLelharLFHIPEAEipARVAEMSERFKLNDVEDILPE-----------SLPLGIRQRLSLAVAVIHRPEMLILDEPT 435
Cdd:cd03290 96 EENI-----TFGSPFNK--QRYKAVTDACSLQPDIDLLPFgdqteigergiNLSGGQRQRICVARALYQNTNIVFLDDPF 168
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 732682709 436 SGVDPVARDMFWQL-MVDLSRQDKVTIFISTHFMNEAERCDRISLMHAG 483
Cdd:cd03290 169 SALDIHLSDHLMQEgILKFLQDDKRTLVLVTHKLQYLPHADWIIAMKDG 217
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
302-466 |
2.39e-11 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 67.60 E-value: 2.39e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 302 GEIFGFLGSNGCGKSTTMKMLTGLLPASEGEAWLF---GQPVDPkdidTRRRVGYMSQAFSLYNELTVRQNLeLHARLFH 378
Cdd:PLN03211 94 GEILAVLGPSGSGKSTLLNALAGRIQGNNFTGTILannRKPTKQ----ILKRTGFVTQDDILYPHLTVRETL-VFCSLLR 168
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 379 IPEA---EIPARVAE--MSErFKLNDVED-ILPESLPLGI----RQRLSLAVAVIHRPEMLILDEPTSGVDPVARDMFWQ 448
Cdd:PLN03211 169 LPKSltkQEKILVAEsvISE-LGLTKCENtIIGNSFIRGIsggeRKRVSIAHEMLINPSLLILDEPTSGLDATAAYRLVL 247
|
170
....*....|....*...
gi 732682709 449 LMVDLSRQDKvTIFISTH 466
Cdd:PLN03211 248 TLGSLAQKGK-TIVTSMH 264
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
279-494 |
2.52e-11 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 64.95 E-value: 2.52e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 279 ARDLTMRFGSFVAVDHVNFRIPRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGEAWLFGQPVDPKDIDT-----RRRVGY 353
Cdd:PRK11701 9 VRGLTKLYGPRKGCRDVSFDLYPGEVLGIVGESGSGKTTLLNALSARLAPDAGEVHYRMRDGQLRDLYAlseaeRRRLLR 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 354 MSQAFslyneltVRQNLELHARLFHIPEAEIPARVAEMSER----------FKLNDVE------DILPESLPLGIRQRLS 417
Cdd:PRK11701 89 TEWGF-------VHQHPRDGLRMQVSAGGNIGERLMAVGARhygdiratagDWLERVEidaariDDLPTTFSGGMQQRLQ 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 418 LAVAVIHRPEMLILDEPTSGVDpV---AR--DMFWQLMVDLSrqdkVTIFISTHFMNEAeR--CDRISLMHAGKVLASG- 489
Cdd:PRK11701 162 IARNLVTHPRLVFMDEPTGGLD-VsvqARllDLLRGLVRELG----LAVVIVTHDLAVA-RllAHRLLVMKQGRVVESGl 235
|
....*
gi 732682709 490 TPQEL 494
Cdd:PRK11701 236 TDQVL 240
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
25-224 |
2.63e-11 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 64.45 E-value: 2.63e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 25 TVALNNITLDIPARCMVGLIGPDGVGKSSLLSLISGARVIEQGNVMVLGgdmrDPKHRRDVCPRIAWMPQGLG--KNLYH 102
Cdd:PRK11629 22 TDVLHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNG----QPMSKLSSAAKAELRNQKLGfiYQFHH 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 103 TL---SVYENVDFFARLFGHDKAEREVRINELLTSTGLAPFRDRPAGKLSGGMKQKLGLCCALIHDPELLILDEPTTGVD 179
Cdd:PRK11629 98 LLpdfTALENVAMPLLIGKKKPAEINSRALEMLAAVGLEHRANHRPSELSGGERQRVAIARALVNNPRLVLADEPTGNLD 177
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 732682709 180 PLSRSQFWDLIDSIRQRQSNmSVLVATAYMEEAERFDWLVAMNAG 224
Cdd:PRK11629 178 ARNADSIFQLLGELNRLQGT-AFLVVTHDLQLAKRMSRQLEMRDG 221
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
292-442 |
3.25e-11 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 63.43 E-value: 3.25e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 292 VDHVNFRIPRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGEAWLFGQPVDPKDIDTRRRVGYMSQAFSLYNELTVRQNLe 371
Cdd:PRK13540 17 LQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEILFERQSIKKDLCTYQKQLCFVGHRSGINPYLTLRENC- 95
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 732682709 372 lharLFHIPEAEIPARVAEMSERFKLNDVEDILPESLPLGIRQRLSLAVAVIHRPEMLILDEPTSGVDPVA 442
Cdd:PRK13540 96 ----LYDIHFSPGAVGITELCRLFSLEHLIDYPCGLLSSGQKRQVALLRLWMSKAKLWLLDEPLVALDELS 162
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
295-485 |
4.02e-11 |
|
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; TAP (Transporter Associated with Antigen Processing) is essential for peptide delivery from the cytosol into the lumen of the endoplasmic reticulum (ER), where these peptides are loaded on major histocompatibility complex (MHC) I molecules. Loaded MHC I leave the ER and display their antigenic cargo on the cell surface to cytotoxic T cells. Subsequently, virus-infected or malignantly transformed cells can be eliminated. TAP belongs to the large family of ATP-binding cassette (ABC) transporters, which translocate a vast variety of solutes across membranes.
Pssm-ID: 213215 [Multi-domain] Cd Length: 226 Bit Score: 63.64 E-value: 4.02e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 295 VNFRIPRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGEAWLFGQPVDPKDID-TRRRVGYMSQAFSLYNElTVRQNLEL- 372
Cdd:cd03248 33 VSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDGKPISQYEHKyLHSKVSLVGQEPVLFAR-SLQDNIAYg 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 373 --HARLFHIPEAEIPARVAEMSERFKLNDVEDILPES--LPLGIRQRLSLAVAVIHRPEMLILDEPTSGVDPVARDMFWQ 448
Cdd:cd03248 112 lqSCSFECVKEAAQKAHAHSFISELASGYDTEVGEKGsqLSGGQKQRVAIARALIRNPQVLILDEATSALDAESEQQVQQ 191
|
170 180 190
....*....|....*....|....*....|....*...
gi 732682709 449 LMVD-LSRQdkvTIFISTHFMNEAERCDRISLMHAGKV 485
Cdd:cd03248 192 ALYDwPERR---TVLVIAHRLSTVERADQILVLDGGRI 226
|
|
| PRK13546 |
PRK13546 |
teichoic acids export ABC transporter ATP-binding subunit TagH; |
288-497 |
4.18e-11 |
|
teichoic acids export ABC transporter ATP-binding subunit TagH;
Pssm-ID: 184131 [Multi-domain] Cd Length: 264 Bit Score: 64.45 E-value: 4.18e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 288 SFVAVDHVNFRIPRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGeawlfgqpvdpkDIDTRRRVGYMSQAFSLYNELTVR 367
Cdd:PRK13546 36 TFFALDDISLKAYEGDVIGLVGINGSGKSTLSNIIGGSLSPTVG------------KVDRNGEVSVIAISAGLSGQLTGI 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 368 QNLELHARLFHIPEAEIPARVAEMSERFKLNDVEDILPESLPLGIRQRLSLAVAVIHRPEMLILDEPTSGVDPVARDMFW 447
Cdd:PRK13546 104 ENIEFKMLCMGFKRKEIKAMTPKIIEFSELGEFIYQPVKKYSSGMRAKLGFSINITVNPDILVIDEALSVGDQTFAQKCL 183
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 732682709 448 QLMVDLSRQDKVTIFISTHFMNEAERCDRISLMHAGKVLASGTPQELVEK 497
Cdd:PRK13546 184 DKIYEFKEQNKTIFFVSHNLGQVRQFCTKIAWIEGGKLKDYGELDDVLPK 233
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
244-499 |
4.48e-11 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 66.67 E-value: 4.48e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 244 LEEAFINLLPQaQRQAHQAVVI------------PPYQPENAEIA---IEARDLTMRFGSFVAV-DHVNFRIPRGEIFGF 307
Cdd:PRK10790 294 LNEPLIELTTQ-QSMLQQAVVAgervfelmdgprQQYGNDDRPLQsgrIDIDNVSFAYRDDNLVlQNINLSVPSRGFVAL 372
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 308 LGSNGCGKSTTMKMLTGLLPASEGEAWLFGQPVDPKDIDTRRRVGYMSQAFSLYNELTVRQNLELhARlfHIPEaeipAR 387
Cdd:PRK10790 373 VGHTGSGKSTLASLLMGYYPLTEGEIRLDGRPLSSLSHSVLRQGVAMVQQDPVVLADTFLANVTL-GR--DISE----EQ 445
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 388 VAEMSERFKLNDVEDILPE-----------SLPLGIRQRLSLAVAVIHRPEMLILDEPTSGVDPVARDMFWQLMVDLSRQ 456
Cdd:PRK10790 446 VWQALETVQLAELARSLPDglytplgeqgnNLSVGQKQLLALARVLVQTPQILILDEATANIDSGTEQAIQQALAAVREH 525
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 732682709 457 dkVTIFISTHFMNEAERCDRISLMHAGKVLASGTPQELVEKRG 499
Cdd:PRK10790 526 --TTLVVIAHRLSTIVEADTILVLHRGQAVEQGTHQQLLAAQG 566
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
30-245 |
5.02e-11 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 65.28 E-value: 5.02e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 30 NITLDIPARCMVGLIGPDGVGKSSLLSLISGARVIEQGNVmVLGG----DMRD----PKHRRdvcpRIAWMPQGlgknly 101
Cdd:PRK11144 16 TVNLTLPAQGITAIFGRSGAGKTSLINAISGLTRPQKGRI-VLNGrvlfDAEKgiclPPEKR----RIGYVFQD------ 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 102 htlsvyenvdffARLFGH--------------DKAEREvRINELLtstGLAPFRDRPAGKLSGGMKQKLGLCCALIHDPE 167
Cdd:PRK11144 85 ------------ARLFPHykvrgnlrygmaksMVAQFD-KIVALL---GIEPLLDRYPGSLSGGEKQRVAIGRALLTAPE 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 168 LLILDEPTTGVDpLSRSQfwDLIDSIRQ--RQSNMSVLVATAYMEEAERF-DWLVAMNAGEVLATGSAEE---------- 234
Cdd:PRK11144 149 LLLMDEPLASLD-LPRKR--ELLPYLERlaREINIPILYVSHSLDEILRLaDRVVVLEQGKVKAFGPLEEvwassamrpw 225
|
250
....*....|.
gi 732682709 235 LRQQTQSATLE 245
Cdd:PRK11144 226 LPKEEQSSILK 236
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
28-238 |
5.04e-11 |
|
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: 66.89 E-value: 5.04e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 28 LNNITLDIPARCMVGLIGPDGVGKSSLLSLISGARVIEQGNVMVLGGdmrdpkhrrdvcprIAWMPQglgKNLYHTLSVY 107
Cdd:TIGR00957 654 LNGITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVHMKGS--------------VAYVPQ---QAWIQNDSLR 716
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 108 ENVdffarLFGHdkAEREVRINELLTSTGLAP-FRDRPAG----------KLSGGMKQKLGLCCALIHDPELLILDEPTT 176
Cdd:TIGR00957 717 ENI-----LFGK--ALNEKYYQQVLEACALLPdLEILPSGdrteigekgvNLSGGQKQRVSLARAVYSNADIYLFDDPLS 789
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 732682709 177 GVDPLSRSQFWDLIDSIRQRQSNMSVLVATAYMEEAERFDWLVAMNAGEVLATGSAEELRQQ 238
Cdd:TIGR00957 790 AVDAHVGKHIFEHVIGPEGVLKNKTRILVTHGISYLPQVDVIIVMSGGKISEMGSYQELLQR 851
|
|
| tagH |
PRK13545 |
teichoic acids export protein ATP-binding subunit; Provisional |
291-500 |
5.11e-11 |
|
teichoic acids export protein ATP-binding subunit; Provisional
Pssm-ID: 184130 [Multi-domain] Cd Length: 549 Bit Score: 66.45 E-value: 5.11e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 291 AVDHVNFRIPRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGEawlfgqpvdpkdIDTRRRVGYMSQAFSLYNELTVRQNL 370
Cdd:PRK13545 39 ALNNISFEVPEGEIVGIIGLNGSGKSTLSNLIAGVTMPNKGT------------VDIKGSAALIAISSGLNGQLTGIENI 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 371 ELHARLFHIPEAEIPARVAEMSERFKLNDVEDILPESLPLGIRQRLSLAVAVIHRPEMLILDEPTSGVDPVARDMFWQLM 450
Cdd:PRK13545 107 ELKGLMMGLTKEKIKEIIPEIIEFADIGKFIYQPVKTYSSGMKSRLGFAISVHINPDILVIDEALSVGDQTFTKKCLDKM 186
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 732682709 451 VDLSRQDKvTIFISTHFMNEAER-CDRISLMHAGKVLASGTPQELVEKRGA 500
Cdd:PRK13545 187 NEFKEQGK-TIFFISHSLSQVKSfCTKALWLHYGQVKEYGDIKEVVDHYDE 236
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
291-498 |
5.17e-11 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 66.18 E-value: 5.17e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 291 AVDHVNFRIPRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGEAWLFGQPVD---PKDiDTRRRVGYMSQAFSLYNELTVR 367
Cdd:PRK10762 19 ALSGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSILYLGKEVTfngPKS-SQEAGIGIIHQELNLIPQLTIA 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 368 QNL----ELHARLFHIPEAEIPARVAEMSERFKLNDVEDILPESLPLGIRQRLSLAVAVIHRPEMLILDEPTSGVDPVAR 443
Cdd:PRK10762 98 ENIflgrEFVNRFGRIDWKKMYAEADKLLARLNLRFSSDKLVGELSIGEQQMVEIAKVLSFESKVIIMDEPTDALTDTET 177
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 732682709 444 DMFWQLMVDLSRQDKVTIFIStHFMNEA-ERCDRISLMHAGKVLASGTPQELVEKR 498
Cdd:PRK10762 178 ESLFRVIRELKSQGRGIVYIS-HRLKEIfEICDDVTVFRDGQFIAEREVADLTEDS 232
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
22-182 |
5.90e-11 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 62.66 E-value: 5.90e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 22 YGKTVALNNITLDIPARCMVGLIGPDGVGKSSLLSLISGARVIEQGNVMVLGGDMRdpkhrRDVCP---RIAWMPQGLGK 98
Cdd:PRK13540 11 YHDQPLLQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEILFERQSIK-----KDLCTyqkQLCFVGHRSGI 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 99 NLYHTLSvyENVdffarLFGHDKAEREVRINELLTSTGLAPFRDRPAGKLSGGMKQKLGLCCALIHDPELLILDEPTTGV 178
Cdd:PRK13540 86 NPYLTLR--ENC-----LYDIHFSPGAVGITELCRLFSLEHLIDYPCGLLSSGQKRQVALLRLWMSKAKLWLLDEPLVAL 158
|
....
gi 732682709 179 DPLS 182
Cdd:PRK13540 159 DELS 162
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
30-179 |
6.52e-11 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 62.51 E-value: 6.52e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 30 NITLDIPARCMVGLIGPDGVGKSSLLSLISGARVIEQGNVMVLGGDMR--DPKHRRDVCpriaWmpqgLG-----KNLyh 102
Cdd:PRK13538 19 GLSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVLWQGEPIRrqRDEYHQDLL----Y----LGhqpgiKTE-- 88
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 732682709 103 tLSVYENVDFFARLfgHDKAEREvRINELLTSTGLAPFRDRPAGKLSGGMKQKLGLCCALIHDPELLILDEPTTGVD 179
Cdd:PRK13538 89 -LTALENLRFYQRL--HGPGDDE-ALWEALAQVGLAGFEDVPVRQLSAGQQRRVALARLWLTRAPLWILDEPFTAID 161
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
25-226 |
7.61e-11 |
|
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; TAP (Transporter Associated with Antigen Processing) is essential for peptide delivery from the cytosol into the lumen of the endoplasmic reticulum (ER), where these peptides are loaded on major histocompatibility complex (MHC) I molecules. Loaded MHC I leave the ER and display their antigenic cargo on the cell surface to cytotoxic T cells. Subsequently, virus-infected or malignantly transformed cells can be eliminated. TAP belongs to the large family of ATP-binding cassette (ABC) transporters, which translocate a vast variety of solutes across membranes.
Pssm-ID: 213215 [Multi-domain] Cd Length: 226 Bit Score: 62.87 E-value: 7.61e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 25 TVALNNITLDIPARCMVGLIGPDGVGKSSLLSLISGARVIEQGNVMVLGGDMRDPKHR--RDVCPRIAWMPQGLGKNLYH 102
Cdd:cd03248 27 TLVLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDGKPISQYEHKylHSKVSLVGQEPVLFARSLQD 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 103 TLSV-YENVDFFARLFGHDKAEREVRINELltSTGLAPFRDRPAGKLSGGMKQKLGLCCALIHDPELLILDEPTTGVDPL 181
Cdd:cd03248 107 NIAYgLQSCSFECVKEAAQKAHAHSFISEL--ASGYDTEVGEKGSQLSGGQKQRVAIARALIRNPQVLILDEATSALDAE 184
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 732682709 182 SRSQFWDLidsIRQRQSNMSVLVATAYMEEAERFDWLVAMNAGEV 226
Cdd:cd03248 185 SEQQVQQA---LYDWPERRTVLVIAHRLSTVERADQILVLDGGRI 226
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
291-499 |
8.51e-11 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 65.50 E-value: 8.51e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 291 AVDHVNFRIPRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGEAWLFGQPVDPKDIDT-RRRVGYMSQAFSLYNElTVRQN 369
Cdd:PRK10789 330 ALENVNFTLKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGDIRFHDIPLTKLQLDSwRSRLAVVSQTPFLFSD-TVANN 408
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 370 LELHArlfhiPEAEiparVAEMSERFKLNDV-EDI--LPES-----------LPLGIRQRLSLAVAVIHRPEMLILDEPT 435
Cdd:PRK10789 409 IALGR-----PDAT----QQEIEHVARLASVhDDIlrLPQGydtevgergvmLSGGQKQRISIARALLLNAEILILDDAL 479
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 732682709 436 SGVDPVARdmfWQLMVDLSR-QDKVTIFISTHFMNEAERCDRISLMHAGKVLASGTPQELVEKRG 499
Cdd:PRK10789 480 SAVDGRTE---HQILHNLRQwGEGRTVIISAHRLSALTEASEILVMQHGHIAQRGNHDQLAQQSG 541
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
241-464 |
9.49e-11 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 65.60 E-value: 9.49e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 241 SATLE--EAFINLLPQAQRQAHQAVVIPPyqPENAEIAIEARDLTMRFGSFVaVDHVNFRIPRGEifGFL--GSNGCGKS 316
Cdd:COG4178 329 RATVDrlAGFEEALEAADALPEAASRIET--SEDGALALEDLTLRTPDGRPL-LEDLSLSLKPGE--RLLitGPSGSGKS 403
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 317 TTMKMLTGLLPASEGEAWLfgqpvdPKDidtrRRVGYMSQafSLY-NELTVRQNLELHARLFHIPEAEIPA-----RVAE 390
Cdd:COG4178 404 TLLRAIAGLWPYGSGRIAR------PAG----ARVLFLPQ--RPYlPLGTLREALLYPATAEAFSDAELREaleavGLGH 471
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 732682709 391 MSERFklnDVEDILPESLPLGIRQRLSLAVAVIHRPEMLILDEPTSGVDPVARDMFWQLmvdLSRQDKVTIFIS 464
Cdd:COG4178 472 LAERL---DEEADWDQVLSLGEQQRLAFARLLLHKPDWLFLDEATSALDEENEAALYQL---LREELPGTTVIS 539
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
24-235 |
1.04e-10 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 63.69 E-value: 1.04e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 24 KTVALNNITLDIPARCMVGLIGPDGVGKSSLLSLISGARVIEQGNVMVLGGDMR---DPKHRRDVCPRIAWMPQGLGKNL 100
Cdd:PRK13641 19 EKKGLDNISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITIAGYHITpetGNKNLKKLRKKVSLVFQFPEAQL 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 101 YHTlSVYENVDFFARLFGHDKAEREVRINELLTSTGL-------APFrdrpagKLSGGMKQKLGLCCALIHDPELLILDE 173
Cdd:PRK13641 99 FEN-TVLKDVEFGPKNFGFSEDEAKEKALKWLKKVGLsedliskSPF------ELSGGQMRRVAIAGVMAYEPEILCLDE 171
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 732682709 174 PTTGVDPLSRSQFWDLIDSIrQRQSNMSVLVATAYMEEAERFDWLVAMNAGEVLATGSAEEL 235
Cdd:PRK13641 172 PAAGLDPEGRKEMMQLFKDY-QKAGHTVILVTHNMDDVAEYADDVLVLEHGKLIKHASPKEI 232
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
18-196 |
1.06e-10 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 65.11 E-value: 1.06e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 18 VSQHYgktvALNNITLDIPARCMVGLIGPDGVGKSS----LLSLISgarviEQGNVMVLGgdmrDPKH---RRDVCP--- 87
Cdd:PRK15134 296 VDHNV----VVKNISFTLRPGETLGLVGESGSGKSTtglaLLRLIN-----SQGEIWFDG----QPLHnlnRRQLLPvrh 362
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 88 RIAWMPQGLGKNLYHTLSVYENVDFFARLfgHDK----AEREVRINELLTSTGLAP-FRDRPAGKLSGGMKQKLGLCCAL 162
Cdd:PRK15134 363 RIQVVFQDPNSSLNPRLNVLQIIEEGLRV--HQPtlsaAQREQQVIAVMEEVGLDPeTRHRYPAEFSGGQRQRIAIARAL 440
|
170 180 190
....*....|....*....|....*....|....
gi 732682709 163 IHDPELLILDEPTTGVDPLSRSQFWDLIDSIRQR 196
Cdd:PRK15134 441 ILKPSLIILDEPTSSLDKTVQAQILALLKSLQQK 474
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
23-243 |
1.22e-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: 65.15 E-value: 1.22e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 23 GKTVALNNITLDIPARCMVGLIGPDGVGKSSLLSLISGARVIEQGNVMVLGGDMRDpKHRRDVCPRIAWMPQGLGknlyh 102
Cdd:COG4618 343 SKRPILRGVSFSLEPGEVLGVIGPSGSGKSTLARLLVGVWPPTAGSVRLDGADLSQ-WDREELGRHIGYLPQDVE----- 416
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 103 tL---SVYENVdffARLFGHD-----KAEREVRINEL-----------LTSTGLApfrdrpagkLSGGMKQKLGLCCALI 163
Cdd:COG4618 417 -LfdgTIAENI---ARFGDADpekvvAAAKLAGVHEMilrlpdgydtrIGEGGAR---------LSGGQRQRIGLARALY 483
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 164 HDPELLILDEPTTGVDPLSRSQfwdLIDSIRQ-RQSNMSVLVAT---AYMEEAerfDWLVAMNAGEVLATGSAEE-LRQQ 238
Cdd:COG4618 484 GDPRLVVLDEPNSNLDDEGEAA---LAAAIRAlKARGATVVVIThrpSLLAAV---DKLLVLRDGRVQAFGPRDEvLARL 557
|
....*
gi 732682709 239 TQSAT 243
Cdd:COG4618 558 ARPAA 562
|
|
| nickel_nikD |
TIGR02770 |
nickel import ATP-binding protein NikD; This family represents the NikD subunit of a ... |
30-243 |
1.23e-10 |
|
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: 62.39 E-value: 1.23e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 30 NITLDIPARCMVGLIGPDGVGKS----SLLSLISGARVIEQGNVMVLGGDMRDPKHR-RDVC-----PRIAWMP-QGLGK 98
Cdd:TIGR02770 4 DLNLSLKRGEVLALVGESGSGKSltclAILGLLPPGLTQTSGEILLDGRPLLPLSIRgRHIAtimqnPRTAFNPlFTMGN 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 99 NLYHTLsvyenvdffaRLFGHDKAEREVRINELLTSTGLA---------PFrdrpagKLSGGMKQKLGLCCALIHDPELL 169
Cdd:TIGR02770 84 HAIETL----------RSLGKLSKQARALILEALEAVGLPdpeevlkkyPF------QLSGGMLQRVMIALALLLEPPFL 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 732682709 170 ILDEPTTGVDPLSRSQFWDLIDSIRQRQSNMSVLVATAYMEEAERFDWLVAMNAGEVLATGSAEELRQQTQSAT 243
Cdd:TIGR02770 148 IADEPTTDLDVVNQARVLKLLRELRQLFGTGILLITHDLGVVARIADEVAVMDDGRIVERGTVKEIFYNPKHET 221
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
292-494 |
1.27e-10 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 65.11 E-value: 1.27e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 292 VDHVNFRIPRGEIFGFLGSNGCGKSTTMKMLTGLLPAS-----EGEAWLFGQPVDPKDIDTRRRV--GYMSQAFS----- 359
Cdd:PRK15134 25 VNDVSLQIEAGETLALVGESGSGKSVTALSILRLLPSPpvvypSGDIRFHGESLLHASEQTLRGVrgNKIAMIFQepmvs 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 360 ---LYN-ELTVRQNLELHARLFHIP-EAEIPA---RVAEMSERFKLNDvediLPESLPLGIRQRLSLAVAVIHRPEMLIL 431
Cdd:PRK15134 105 lnpLHTlEKQLYEVLSLHRGMRREAaRGEILNcldRVGIRQAAKRLTD----YPHQLSGGERQRVMIAMALLTRPELLIA 180
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 732682709 432 DEPTSGVDPVARDMFWQLMVDLSRQDKVTIFISTHFMNEAER-CDRISLMHAGKVLASGTPQEL 494
Cdd:PRK15134 181 DEPTTALDVSVQAQILQLLRELQQELNMGLLFITHNLSIVRKlADRVAVMQNGRCVEQNRAATL 244
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
266-494 |
1.31e-10 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 65.53 E-value: 1.31e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 266 PPYQPENAEIAIeardltmRFGSFV--------AVDHVNFRIPRGEIFGFLGSNGCGKSTTMKMLTGLLPasegeawlfg 337
Cdd:PLN03130 606 PPLEPGLPAISI-------KNGYFSwdskaerpTLSNINLDVPVGSLVAIVGSTGEGKTSLISAMLGELP---------- 668
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 338 qPVDPKDIDTRRRVGYMSQAFSLYNElTVRQNLeLHARLFHIPEAEIPARVAEMSERFKL---NDVEDILPESLPL--GI 412
Cdd:PLN03130 669 -PRSDASVVIRGTVAYVPQVSWIFNA-TVRDNI-LFGSPFDPERYERAIDVTALQHDLDLlpgGDLTEIGERGVNIsgGQ 745
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 413 RQRLSLAVAVIHRPEMLILDEPTSGVDP-VARDMFWQLMVD-LSRQDKVTIFISTHFMNeaeRCDRISLMHAGKVLASGT 490
Cdd:PLN03130 746 KQRVSMARAVYSNSDVYIFDDPLSALDAhVGRQVFDKCIKDeLRGKTRVLVTNQLHFLS---QVDRIILVHEGMIKEEGT 822
|
....
gi 732682709 491 PQEL 494
Cdd:PLN03130 823 YEEL 826
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
25-235 |
1.73e-10 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 64.65 E-value: 1.73e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 25 TVALNNITLDIPARCMVGLIGPDGVGKSSLLSLISGARVIEQGNVMVLGGDMRDPKHR--RDVCpriAWMPQGLgkNLYH 102
Cdd:PRK11176 356 VPALRNINFKIPAGKTVALVGRSGSGKSTIANLLTRFYDIDEGEILLDGHDLRDYTLAslRNQV---ALVSQNV--HLFN 430
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 103 -TLS---VYENVDFFARlfghDKAEREVR-------INELltSTGLapfrDRPAGK----LSGGMKQKLGLCCALIHDPE 167
Cdd:PRK11176 431 dTIAnniAYARTEQYSR----EQIEEAARmayamdfINKM--DNGL----DTVIGEngvlLSGGQRQRIAIARALLRDSP 500
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 732682709 168 LLILDEPTTGVDPLSRSQFWDLIDSIrqrQSNMSVLVATAYMEEAERFDWLVAMNAGEVLATGSAEEL 235
Cdd:PRK11176 501 ILILDEATSALDTESERAIQAALDEL---QKNRTSLVIAHRLSTIEKADEILVVEDGEIVERGTHAEL 565
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
26-196 |
2.22e-10 |
|
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: 61.68 E-value: 2.22e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 26 VALNNITLDIPA-RCmVGLIGPDGVGKSSLLSLISGARVIEQGNVMVL-GGDMRD----PKH-----RRD---------- 84
Cdd:COG4778 25 PVLDGVSFSVAAgEC-VALTGPSGAGKSTLLKCIYGNYLPDSGSILVRhDGGWVDlaqaSPReilalRRRtigyvsqflr 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 85 VCPRIAwmpqglgknlyhTLSVYENVdffARLFGHDKAEREVRINELLTSTGLaPFR--DRPAGKLSGGMKQKLGLCCAL 162
Cdd:COG4778 104 VIPRVS------------ALDVVAEP---LLERGVDREEARARARELLARLNL-PERlwDLPPATFSGGEQQRVNIARGF 167
|
170 180 190
....*....|....*....|....*....|....
gi 732682709 163 IHDPELLILDEPTTGVDPLSRSQFWDLIDSIRQR 196
Cdd:COG4778 168 IADPPLLLLDEPTASLDAANRAVVVELIEEAKAR 201
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
28-238 |
2.76e-10 |
|
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: 61.40 E-value: 2.76e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 28 LNNITLDIPARCMVGLIGPDGVGKSSLLSLISGARVIEQGNVMVLGGDMRD--PKHRRDvcpRIAWMPQGlgKNLYHTlS 105
Cdd:cd03249 19 LKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEILLDGVDIRDlnLRWLRS---QIGLVSQE--PVLFDG-T 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 106 VYENVdffarLFGHDKAEREVRInELLTSTGLAPF-RDRPAG----------KLSGGMKQKLGLCCALIHDPELLILDEP 174
Cdd:cd03249 93 IAENI-----RYGKPDATDEEVE-EAAKKANIHDFiMSLPDGydtlvgergsQLSGGQKQRIAIARALLRNPKILLLDEA 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 732682709 175 TTGVDPLSRSQFWDLIDSIRQrqsNMSVLVATAYMEEAERFDWLVAMNAGEVLATGSAEELRQQ 238
Cdd:cd03249 167 TSALDAESEKLVQEALDRAMK---GRTTIVIAHRLSTIRNADLIAVLQNGQVVEQGTHDELMAQ 227
|
|
| NosY |
COG1277 |
ABC-type transport system involved in multi-copper enzyme maturation, permease component ... |
721-836 |
3.63e-10 |
|
ABC-type transport system involved in multi-copper enzyme maturation, permease component [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440888 [Multi-domain] Cd Length: 201 Bit Score: 60.60 E-value: 3.63e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 721 VIPLLLMMIPSMLSALSVVREKELGSIINLYVTPTTRSEFLLGKqlpYIALGMLNFFLLC-------GLSVFVFGVPHK- 792
Cdd:COG1277 56 LLSLLLPLLAPALGMDAISGERESGTLELLLTLPISRWEIVLGK---FLGALLVLLLALLitfllalLLGLLLFGSPPPd 132
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 732682709 793 -GSFLTLTLAALLYIIIATGMGLLISTFMKSQIAAIFGTAIITLI 836
Cdd:COG1277 133 lGAILGFYLGLLLLGLAFLAIGLFISALTRNQIVAAILAIALWLL 177
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
277-439 |
4.38e-10 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 61.28 E-value: 4.38e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 277 IEARDLTMRFGSFVAVDHVNFRIPRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGEAwlfgqpvdpkDIDTRRRVGYMSQ 356
Cdd:PRK09544 5 VSLENVSVSFGQRRVLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVI----------KRNGKLRIGYVPQ 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 357 AFSLYNE--LTVRQNLELHArlfHIPEAEI-PARvaemsERFKLNDVEDILPESLPLGIRQRLSLAVAVIHRPEMLILDE 433
Cdd:PRK09544 75 KLYLDTTlpLTVNRFLRLRP---GTKKEDIlPAL-----KRVQAGHLIDAPMQKLSGGETQRVLLARALLNRPQLLVLDE 146
|
....*.
gi 732682709 434 PTSGVD 439
Cdd:PRK09544 147 PTQGVD 152
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
277-499 |
4.46e-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: 63.81 E-value: 4.46e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 277 IEARDLTMRF--GSFVAVDHVNFRIPRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGEAWLFGqpVDPKDI---DTRRRV 351
Cdd:TIGR00957 1285 VEFRNYCLRYreDLDLVLRHINVTIHGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDG--LNIAKIglhDLRFKI 1362
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 352 GYMSQ--------------AFSLYNELTVRQNLEL-HARLFhipEAEIPARVA-EMSERfklndvedilPESLPLGIRQR 415
Cdd:TIGR00957 1363 TIIPQdpvlfsgslrmnldPFSQYSDEEVWWALELaHLKTF---VSALPDKLDhECAEG----------GENLSVGQRQL 1429
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 416 LSLAVAVIHRPEMLILDEPTSGVDpVARDMFWQLMVDlSRQDKVTIFISTHFMNEAERCDRISLMHAGKVLASGTPQELV 495
Cdd:TIGR00957 1430 VCLARALLRKTKILVLDEATAAVD-LETDNLIQSTIR-TQFEDCTVLTIAHRLNTIMDYTRVIVLDKGEVAEFGAPSNLL 1507
|
....
gi 732682709 496 EKRG 499
Cdd:TIGR00957 1508 QQRG 1511
|
|
| ABC2_membrane_2 |
pfam12679 |
ABC-2 family transporter protein; This family is related to the ABC-2 membrane transporter ... |
724-910 |
5.49e-10 |
|
ABC-2 family transporter protein; This family is related to the ABC-2 membrane transporter family.
Pssm-ID: 403774 [Multi-domain] Cd Length: 281 Bit Score: 61.26 E-value: 5.49e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 724 LLLMMIPSMLSALSVVREKELGSIINLYVTPTTRSEFLLGKQLPYIALGMLNFFLLCGLSVFVFGVPHKGSFLTLTLAAL 803
Cdd:pfam12679 76 FLIPVIAALLGADAIAGERERGTIELLLSLPVSRSEILLGKFIGRLAIGLILAVALLAGVLLALAITLALGDPLDLGDLL 155
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 804 LYII---------IATGMGLLISTFMKSQIAAIFGTAIITLIPATQFSGMIDPVASLEGPGRWIGEVYPTSHFLT----- 869
Cdd:pfam12679 156 LLVAasvllalalVFLSIGLLLSSVARSTRTAAAIALGLFFVLAILWPIVLYGLAELLAGPAPPQELLDFLLFLNptspy 235
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 732682709 870 -IARGTFSKALDLTDL---WQLFIPLLIAIPLVMGLSILLLKKQE 910
Cdd:pfam12679 236 nTLLSTILAGSDLSLYgstATNLLILLAWIAVPLALAYVLFKRKD 280
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
61-247 |
5.63e-10 |
|
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: 62.92 E-value: 5.63e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 61 ARVIEQGNVMVlggdmrdPKHRRdvcpRIAWMPQ-GLGKNLyhTLSVYENVDFFARLfghDKAEREVRINELLTSTGLAP 139
Cdd:TIGR02633 331 AQAIRAGIAMV-------PEDRK----RHGIVPIlGVGKNI--TLSVLKSFCFKMRI---DAAAELQIIGSAIQRLKVKT 394
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 140 FR-DRPAGKLSGGMKQKLGLCCALIHDPELLILDEPTTGVDPLSRSQFWDLIDSIRQRqsNMSVLVATAYMEEAERF-DW 217
Cdd:TIGR02633 395 ASpFLPIGRLSGGNQQKAVLAKMLLTNPRVLILDEPTRGVDVGAKYEIYKLINQLAQE--GVAIIVVSSELAEVLGLsDR 472
|
170 180 190
....*....|....*....|....*....|
gi 732682709 218 LVAMNAGEVLATGSAEELrqqTQSATLEEA 247
Cdd:TIGR02633 473 VLVIGEGKLKGDFVNHAL---TQEQVLAAA 499
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
31-255 |
5.94e-10 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 62.62 E-value: 5.94e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 31 ITLDIPARCMVGLIGPDGVGKSSLLSLISGARVIEQGNVMVLGG--DMRDPKH--RRDV--CP--RIAwmpQGLgknlYH 102
Cdd:PRK11288 272 ISFSVRAGEIVGLFGLVGAGRSELMKLLYGATRRTAGQVYLDGKpiDIRSPRDaiRAGImlCPedRKA---EGI----IP 344
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 103 TLSVYENVDFFAR-------LFGHDKAERE---VRINELLTSTglaPFRDRPAGKLSGGMKQKLGLCCALIHDPELLILD 172
Cdd:PRK11288 345 VHSVADNINISARrhhlragCLINNRWEAEnadRFIRSLNIKT---PSREQLIMNLSGGNQQKAILGRWLSEDMKVILLD 421
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 173 EPTTGVDPLSRSQFWDLIDSIRQRqsNMSVLVATAYMEE----AERfdwLVAMNAGEVlatgSAEELRQQtqsATlEEAF 248
Cdd:PRK11288 422 EPTRGIDVGAKHEIYNVIYELAAQ--GVAVLFVSSDLPEvlgvADR---IVVMREGRI----AGELAREQ---AT-ERQA 488
|
....*...
gi 732682709 249 INL-LPQA 255
Cdd:PRK11288 489 LSLaLPRT 496
|
|
| tagH |
PRK13545 |
teichoic acids export protein ATP-binding subunit; Provisional |
21-173 |
7.61e-10 |
|
teichoic acids export protein ATP-binding subunit; Provisional
Pssm-ID: 184130 [Multi-domain] Cd Length: 549 Bit Score: 62.60 E-value: 7.61e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 21 HYgktvALNNITLDIPARCMVGLIGPDGVGKSSLLSLISGARVIEQGNVMVLGGdmrdpkhrrdvCPRIAwmpqgLGKNL 100
Cdd:PRK13545 37 HY----ALNNISFEVPEGEIVGIIGLNGSGKSTLSNLIAGVTMPNKGTVDIKGS-----------AALIA-----ISSGL 96
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 732682709 101 YHTLSVYENVDFFARLFGHDKAEREVRINELLTSTGLAPFRDRPAGKLSGGMKQKLGLCCALIHDPELLILDE 173
Cdd:PRK13545 97 NGQLTGIENIELKGLMMGLTKEKIKEIIPEIIEFADIGKFIYQPVKTYSSGMKSRLGFAISVHINPDILVIDE 169
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
18-235 |
1.04e-09 |
|
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: 62.45 E-value: 1.04e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 18 VSQHYG-KTVALNNITLDIPARCMVGLIGPDGVGKSSLLSLISGARVIEQGNVMVLGGDMRD-PKH--RRdvcpRIAWMP 93
Cdd:TIGR01193 479 VSYSYGyGSNILSDISLTIKMNSKTTIVGMSGSGKSTLAKLLVGFFQARSGEILLNGFSLKDiDRHtlRQ----FINYLP 554
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 94 QglgKNLYHTLSVYENVdffarLFGhdkAEREVRINELLTSTGLAPFRD--------------RPAGKLSGGMKQKLGLC 159
Cdd:TIGR01193 555 Q---EPYIFSGSILENL-----LLG---AKENVSQDEIWAACEIAEIKDdienmplgyqtelsEEGSSISGGQKQRIALA 623
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 732682709 160 CALIHDPELLILDEPTTGVDPLSRSQfwdLIDSIRQRQSNMSVLVATAyMEEAERFDWLVAMNAGEVLATGSAEEL 235
Cdd:TIGR01193 624 RALLTDSKVLILDESTSNLDTITEKK---IVNNLLNLQDKTIIFVAHR-LSVAKQSDKIIVLDHGKIIEQGSHDEL 695
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
28-238 |
1.58e-09 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 61.66 E-value: 1.58e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 28 LNNITLDIPARCMVGLIGPDGVGKSSLLSLISGARVIEQGNVMVLGGDMRDPKHR--RDVCPRIAWMPQGLGKnlyhtlS 105
Cdd:PRK10790 357 LQNINLSVPSRGFVALVGHTGSGKSTLASLLMGYYPLTEGEIRLDGRPLSSLSHSvlRQGVAMVQQDPVVLAD------T 430
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 106 VYENVDffarlFGHDKAEREVRinELLTSTGLAPF-RDRPAG----------KLSGGMKQKLGLCCALIHDPELLILDEP 174
Cdd:PRK10790 431 FLANVT-----LGRDISEEQVW--QALETVQLAELaRSLPDGlytplgeqgnNLSVGQKQLLALARVLVQTPQILILDEA 503
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 732682709 175 TTGVDPLSRSQFWDLIDSIRQRqsnmSVLVATAY----MEEAerfDWLVAMNAGEVLATGSAEELRQQ 238
Cdd:PRK10790 504 TANIDSGTEQAIQQALAAVREH----TTLVVIAHrlstIVEA---DTILVLHRGQAVEQGTHQQLLAA 564
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
28-235 |
1.89e-09 |
|
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: 59.17 E-value: 1.89e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 28 LNNITLDIPARCMVGLIGPDGVGKSSLLSLISGARVIEQGNVMVLGGDMRD---PKHRRdvcpRIAWMPQGLgkNLYHTl 104
Cdd:cd03253 17 LKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDGQDIREvtlDSLRR----AIGVVPQDT--VLFND- 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 105 SVYENVDFfARLFGHD----KAEREVRINELLTSTglaPFR-DRPAG----KLSGGMKQKLGLCCALIHDPELLILDEPT 175
Cdd:cd03253 90 TIGYNIRY-GRPDATDeeviEAAKAAQIHDKIMRF---PDGyDTIVGerglKLSGGEKQRVAIARAILKNPPILLLDEAT 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 176 TGVDPLSRSQfwdLIDSIRQRQSNMSVLVATAYMEEAERFDWLVAMNAGEVLATGSAEEL 235
Cdd:cd03253 166 SALDTHTERE---IQAALRDVSKGRTTIVIAHRLSTIVNADKIIVLKDGRIVERGTHEEL 222
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
291-488 |
2.02e-09 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 60.90 E-value: 2.02e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 291 AVDHVNFRIPRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGEAWLFGQPVDPKDIDT--RRRVGYMSQAFSLYNELTVRQ 368
Cdd:PRK10982 13 ALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEIDFKSSKEalENGISMVHQELNLVLQRSVMD 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 369 NLELharlfhipeAEIPARVAEMSERFKLNDVEDILPE------------SLPLGIRQRLSLAVAVIHRPEMLILDEPTS 436
Cdd:PRK10982 93 NMWL---------GRYPTKGMFVDQDKMYRDTKAIFDEldididprakvaTLSVSQMQMIEIAKAFSYNAKIVIMDEPTS 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 732682709 437 GVDPVARDMFWQLMVDLSRQDKVTIFIStHFMNEA-ERCDRISLMHAGKVLAS 488
Cdd:PRK10982 164 SLTEKEVNHLFTIIRKLKERGCGIVYIS-HKMEEIfQLCDEITILRDGQWIAT 215
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
23-237 |
4.11e-09 |
|
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of iron-sulfur clusters (Fe-S) depends on multi-protein systems. The SUF system of E. coli and Erwinia chrysanthemi is important for Fe-S biogenesis under stressful conditions. The SUF system is made of six proteins: SufC is an atypical cytoplasmic ABC-ATPase, which forms a complex with SufB and SufD; SufA plays the role of a scaffold protein for assembly of iron-sulfur clusters and delivery to target proteins; SufS is a cysteine desulfurase which mobilizes the sulfur atom from cysteine and provides it to the cluster; SufE has no associated function yet.
Pssm-ID: 213184 [Multi-domain] Cd Length: 200 Bit Score: 57.15 E-value: 4.11e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 23 GKTVaLNNITLDIPARCMVGLIGPDGVGKSSLLSLISG---ARVIEqGNVMVLGGDMRDpkhrrdvcpriawmpqglgkn 99
Cdd:cd03217 12 GKEI-LKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMGhpkYEVTE-GEILFKGEDITD--------------------- 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 100 lyhtLSVYENvdffARL-----FGHDKAEREVRINELLtstglapfRDRPAGkLSGGMKQKLGLCCALIHDPELLILDEP 174
Cdd:cd03217 69 ----LPPEER----ARLgiflaFQYPPEIPGVKNADFL--------RYVNEG-FSGGEKKRNEILQLLLLEPDLAILDEP 131
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 732682709 175 TTGVDplsrsqfwdlIDSIRQ--------RQSNMSVLVATAYMEEAE--RFDWLVAMNAGEVLATGSAEELRQ 237
Cdd:cd03217 132 DSGLD----------IDALRLvaevinklREEGKSVLIITHYQRLLDyiKPDRVHVLYDGRIVKSGDKELALE 194
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
270-440 |
4.11e-09 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 57.55 E-value: 4.11e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 270 PENAEIAIEARDLTMRFGSFVAVDHVNFRIPRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGEAWLFGQPVdpKDIDTRR 349
Cdd:PRK13543 5 LHTAPPLLAAHALAFSRNEEPVFGPLDFHVDAGEALLVQGDNGAGKTTLLRVLAGLLHVESGQIQIDGKTA--TRGDRSR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 350 RVGYMSQAFSLYNELTVRQNLELHARLFHIPEAEIPARVAEMserFKLNDVEDILPESLPLGIRQRLSLAVAVIHRPEML 429
Cdd:PRK13543 83 FMAYLGHLPGLKADLSTLENLHFLCGLHGRRAKQMPGSALAI---VGLAGYEDTLVRQLSAGQKKRLALARLWLSPAPLW 159
|
170
....*....|.
gi 732682709 430 ILDEPTSGVDP 440
Cdd:PRK13543 160 LLDEPYANLDL 170
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
290-495 |
4.29e-09 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 58.68 E-value: 4.29e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 290 VAVDHVNFRIPRGEIFGFLGSNGCGKSTTMKMLTGLLPAS--------EGEAWLFGQP---VDPKDIDTRRRVgyMSQAF 358
Cdd:PRK13547 15 AILRDLSLRIEPGRVTALLGRNGAGKSTLLKALAGDLTGGgaprgarvTGDVTLNGEPlaaIDAPRLARLRAV--LPQAA 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 359 SLYNELTVRQNLEL----HAR---LFHIPEAEIPARVAEMSERFKLnDVEDILPESLPLGIRQRLSLAVAVIH------- 424
Cdd:PRK13547 93 QPAFAFSAREIVLLgrypHARragALTHRDGEIAWQALALAGATAL-VGRDVTTLSGGELARVQFARVLAQLWpphdaaq 171
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 732682709 425 RPEMLILDEPTSGVDPVARDMFWQLMVDLSRQDKVTIFISTHFMNEAER-CDRISLMHAGKVLASGTPQELV 495
Cdd:PRK13547 172 PPRYLLLDEPTAALDLAHQHRLLDTVRRLARDWNLGVLAIVHDPNLAARhADRIAMLADGAIVAHGAPADVL 243
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
27-206 |
4.36e-09 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 58.94 E-value: 4.36e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 27 ALNNITLDIPARCMVGLIGPDGVGKSSLLSLISGARVIEQGNVMVLGGDMRD------------------PKHRR----- 83
Cdd:PRK13651 22 ALDNVSVEINQGEFIAIIGQTGSGKTTFIEHLNALLLPDTGTIEWIFKDEKNkkktkekekvleklviqkTRFKKikkik 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 84 DVCPRIAWMPQGLGKNLYHTlSVYENVDFFARLFGHDKAEREVRINELLTSTGL-APFRDRPAGKLSGGMKQKLGLCCAL 162
Cdd:PRK13651 102 EIRRRVGVVFQFAEYQLFEQ-TIEKDIIFGPVSMGVSKEEAKKRAAKYIELVGLdESYLQRSPFELSGGQKRRVALAGIL 180
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 732682709 163 IHDPELLILDEPTTGVDPLSRSQFWDLIDSIrqRQSNMSVLVAT 206
Cdd:PRK13651 181 AMEPDFLVFDEPTAGLDPQGVKEILEIFDNL--NKQGKTIILVT 222
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
27-235 |
5.25e-09 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 58.26 E-value: 5.25e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 27 ALNNITLDIPARCMVGLIGPDGVGKSSLLSLISGARVIEQGNVMVLGGDMR--DPKHRRDvcpRIAWMPQGLGKNLYHTL 104
Cdd:PRK15112 28 AVKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDHPLHfgDYSYRSQ---RIRMIFQDPSTSLNPRQ 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 105 SVYENVDFFARL-FGHDKAEREVRINELLTSTGLAPfrDRPA---GKLSGGMKQKLGLCCALIHDPELLILDEPTTGVDP 180
Cdd:PRK15112 105 RISQILDFPLRLnTDLEPEQREKQIIETLRQVGLLP--DHASyypHMLAPGQKQRLGLARALILRPKVIIADEALASLDM 182
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 732682709 181 LSRSQFWDLIDSIRQRQSnMSVLVATAYMEEAERF-DWLVAMNAGEVLATGSAEEL 235
Cdd:PRK15112 183 SMRSQLINLMLELQEKQG-ISYIYVTQHLGMMKHIsDQVLVMHQGEVVERGSTADV 237
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
277-439 |
5.46e-09 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 59.52 E-value: 5.46e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 277 IEARDLTMRFGSFVAVDHVNFRIPRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGEAWLfgqpvDPKDidtrrRVGYMSQ 356
Cdd:PRK15064 2 LSTANITMQFGAKPLFENISVKFGGGNRYGLIGANGCGKSTFMKILGGDLEPSAGNVSL-----DPNE-----RLGKLRQ 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 357 ---AFSLYNEL-TVRQ-NLELHA------RLFHIPEA--EIPARVAEMSERFKLND-------VEDIL-----PESLPLG 411
Cdd:PRK15064 72 dqfAFEEFTVLdTVIMgHTELWEvkqerdRIYALPEMseEDGMKVADLEVKFAEMDgytaearAGELLlgvgiPEEQHYG 151
|
170 180 190
....*....|....*....|....*....|....*.
gi 732682709 412 IRQ--------RLSLAVAVIHRPEMLILDEPTSGVD 439
Cdd:PRK15064 152 LMSevapgwklRVLLAQALFSNPDILLLDEPTNNLD 187
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
290-439 |
6.23e-09 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 60.12 E-value: 6.23e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 290 VAVDHVNFRIPRGEIFGFLGSNGCGKSTTMKML-----TGLLpaSEGEAWLFGQPVDPKdidTRRRVGYMSQAFSLYNEL 364
Cdd:TIGR00956 777 VILNNVDGWVKPGTLTALMGASGAGKTTLLNVLaervtTGVI--TGGDRLVNGRPLDSS---FQRSIGYVQQQDLHLPTS 851
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 365 TVRQNLELHARLF---HIPEAEIPARVAEMSERFKLNDVEDIL----PESLPLGIRQRLSLAVAVIHRPEMLI-LDEPTS 436
Cdd:TIGR00956 852 TVRESLRFSAYLRqpkSVSKSEKMEYVEEVIKLLEMESYADAVvgvpGEGLNVEQRKRLTIGVELVAKPKLLLfLDEPTS 931
|
...
gi 732682709 437 GVD 439
Cdd:TIGR00956 932 GLD 934
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
266-494 |
6.45e-09 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 59.99 E-value: 6.45e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 266 PPYQPENAEIAIE----ARDLTMrfgSFVAVDHVNFRIPRGEIFGFLGSNGCGKSTTMKMLTGLLPasegeawlfgqPVD 341
Cdd:PLN03232 606 PPLQPGAPAISIKngyfSWDSKT---SKPTLSDINLEIPVGSLVAIVGGTGEGKTSLISAMLGELS-----------HAE 671
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 342 PKDIDTRRRVGYMSQAFSLYNElTVRQNLELHARLfhipEAEIPARVAEMS------ERFKLNDVEDILPESLPL--GIR 413
Cdd:PLN03232 672 TSSVVIRGSVAYVPQVSWIFNA-TVRENILFGSDF----ESERYWRAIDVTalqhdlDLLPGRDLTEIGERGVNIsgGQK 746
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 414 QRLSLAVAVIHRPEMLILDEPTSGVDP-VARDMFWQLMVD-LSRQDKVTIFISTHFMNEAercDRISLMHAGKVLASGTP 491
Cdd:PLN03232 747 QRVSMARAVYSNSDIYIFDDPLSALDAhVAHQVFDSCMKDeLKGKTRVLVTNQLHFLPLM---DRIILVSEGMIKEEGTF 823
|
...
gi 732682709 492 QEL 494
Cdd:PLN03232 824 AEL 826
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
10-235 |
7.79e-09 |
|
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 443332 [Multi-domain] Cd Length: 533 Bit Score: 59.31 E-value: 7.79e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 10 PPVAQLAGVSQHY-------GKTV----ALNNITLDIPARCMVGLIGPDGVGKSSL----LSLISGarvieQGNVMVLG- 73
Cdd:COG4172 273 PPLLEARDLKVWFpikrglfRRTVghvkAVDGVSLTLRRGETLGLVGESGSGKSTLglalLRLIPS-----EGEIRFDGq 347
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 74 -------GDMRdpKHRRDV-----------CPR------IAwmpQGLgknlyHTLSVyenvdffarlfGHDKAEREVRIN 129
Cdd:COG4172 348 dldglsrRALR--PLRRRMqvvfqdpfgslSPRmtvgqiIA---EGL-----RVHGP-----------GLSAAERRARVA 406
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 130 ELLTSTGLAP-FRDRPAGKLSGGMKQKLGLCCALIHDPELLILDEPTTGVDPLSRSQFWDLIDSIRQRQS--------NM 200
Cdd:COG4172 407 EALEEVGLDPaARHRYPHEFSGGQRQRIAIARALILEPKLLVLDEPTSALDVSVQAQILDLLRDLQREHGlaylfishDL 486
|
250 260 270
....*....|....*....|....*....|....*
gi 732682709 201 SVLVATAymeeaerfDWLVAMNAGEVLATGSAEEL 235
Cdd:COG4172 487 AVVRALA--------HRVMVMKDGKVVEQGPTEQV 513
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
27-231 |
9.27e-09 |
|
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C is also known as MRP (multidrug resistance-associated protein). Some of the MRP members have five additional transmembrane segments in their N-terminus, but the function of these additional membrane-spanning domains is not clear. The MRP was found in the multidrug-resistance lung cancer cell in which p-glycoprotein was not overexpressed. MRP exports glutathione by drug stimulation, as well as, certain substrates in conjugated forms with anions, such as glutathione, glucuronate, and sulfate.
Pssm-ID: 213211 [Multi-domain] Cd Length: 221 Bit Score: 56.73 E-value: 9.27e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 27 ALNNITLDIPARCMVGLIGPDGVGKSSL-LSLIsgaRVIE--QGNVMVLGGDMRD-PKH--RR--DVCPRIAWMPQGlgk 98
Cdd:cd03244 19 VLKNISFSIKPGEKVGIVGRTGSGKSSLlLALF---RLVElsSGSILIDGVDISKiGLHdlRSriSIIPQDPVLFSG--- 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 99 nlyhtlSVYENVDFFARlfgHDKAErevrINELLTSTGLAPFRDRPAGKL-----------SGGMKQKLGLCCALIHDPE 167
Cdd:cd03244 93 ------TIRSNLDPFGE---YSDEE----LWQALERVGLKEFVESLPGGLdtvveeggenlSVGQRQLLCLARALLRKSK 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 168 LLILDEPTTGVDPLSRSQfwdLIDSIRQRQSNMSVLVAtaymeeAER------FDWLVAMNAGEVLATGS 231
Cdd:cd03244 160 ILVLDEATASVDPETDAL---IQKTIREAFKDCTVLTI------AHRldtiidSDRILVLDKGRVVEFDS 220
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
295-498 |
9.31e-09 |
|
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis fibrosis transmembrane conductor regulator (CFTR) in eukaryotes. The principal role of this protein is chloride ion conductance. The protein is predicted to consist of 12 transmembrane domains. Mutations or lesions in the genetic loci have been linked to the aetiology of asthma, bronchiectasis, chronic obstructive pulmonary disease etc. Disease-causing mutations have been studied by 36Cl efflux assays in vitro cell cultures and electrophysiology, all of which point to the impairment of chloride channel stability and not the biosynthetic processing per se. [Transport and binding proteins, Anions]
Pssm-ID: 273530 [Multi-domain] Cd Length: 1490 Bit Score: 59.54 E-value: 9.31e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 295 VNFRIPRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGEawlfgqpvdpkdIDTRRRVGYMSQaFSLYNELTVRQNLelha 374
Cdd:TIGR01271 445 ISFKLEKGQLLAVAGSTGSGKSSLLMMIMGELEPSEGK------------IKHSGRISFSPQ-TSWIMPGTIKDNI---- 507
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 375 rLFHIPEAEIpaRVAEMSERFKLNDVEDILPE-----------SLPLGIRQRLSLAVAVIHRPEMLILDEPTSGVDPVA- 442
Cdd:TIGR01271 508 -IFGLSYDEY--RYTSVIKACQLEEDIALFPEkdktvlgeggiTLSGGQRARISLARAVYKDADLYLLDSPFTHLDVVTe 584
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 443 RDMF----WQLMVDLSRqdkvtiFISTHFMNEAERCDRISLMHAGKVLASGTPQELVEKR 498
Cdd:TIGR01271 585 KEIFesclCKLMSNKTR------ILVTSKLEHLKKADKILLLHEGVCYFYGTFSELQAKR 638
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
25-236 |
9.47e-09 |
|
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis fibrosis transmembrane conductor regulator (CFTR) in eukaryotes. The principal role of this protein is chloride ion conductance. The protein is predicted to consist of 12 transmembrane domains. Mutations or lesions in the genetic loci have been linked to the aetiology of asthma, bronchiectasis, chronic obstructive pulmonary disease etc. Disease-causing mutations have been studied by 36Cl efflux assays in vitro cell cultures and electrophysiology, all of which point to the impairment of chloride channel stability and not the biosynthetic processing per se. [Transport and binding proteins, Anions]
Pssm-ID: 273530 [Multi-domain] Cd Length: 1490 Bit Score: 59.54 E-value: 9.47e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 25 TVALNNITLDIPARCMVGLIGPDGVGKSSLLSLISGARVIEQGNVmvlggdmrdpKH--RRDVCPRIAW-MPQGLGKNLY 101
Cdd:TIGR01271 439 TPVLKNISFKLEKGQLLAVAGSTGSGKSSLLMMIMGELEPSEGKI----------KHsgRISFSPQTSWiMPGTIKDNII 508
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 102 HTLSVYEnvdffarlFGHDKAEREVRINELLTstgLAPFRDR-PAGK----LSGGMKQKLGLCCALIHDPELLILDEPTT 176
Cdd:TIGR01271 509 FGLSYDE--------YRYTSVIKACQLEEDIA---LFPEKDKtVLGEggitLSGGQRARISLARAVYKDADLYLLDSPFT 577
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 177 GVDPLSRSQFWDliDSIRQRQSNMSVLVATAYMEEAERFDWLVAMNAGEVLATGSAEELR 236
Cdd:TIGR01271 578 HLDVVTEKEIFE--SCLCKLMSNKTRILVTSKLEHLKKADKILLLHEGVCYFYGTFSELQ 635
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
287-466 |
1.52e-08 |
|
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: 56.65 E-value: 1.52e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 287 GSF-VAVDHVNFRipRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGEAwlfgqpvdPKDIDTrrrVGYMSQAFSLYNELT 365
Cdd:cd03237 11 GEFtLEVEGGSIS--ESEVIGILGPNGIGKTTFIKMLAGVLKPDEGDI--------EIELDT---VSYKPQYIKADYEGT 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 366 VRQNL-ELHARLFHIPEAEiparvAEMSERFKLNDVEDILPESLPLGIRQRLSLAVAVIHRPEMLILDEPTSGVDPVARD 444
Cdd:cd03237 78 VRDLLsSITKDFYTHPYFK-----TEIAKPLQIEQILDREVPELSGGELQRVAIAACLSKDADIYLLDEPSAYLDVEQRL 152
|
170 180
....*....|....*....|..
gi 732682709 445 MFWQLMVDLSRQDKVTIFISTH 466
Cdd:cd03237 153 MASKVIRRFAENNEKTAFVVEH 174
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
27-485 |
1.53e-08 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 58.26 E-value: 1.53e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 27 ALNNITLDIPARCMVGLIGPDGVGKSSLLSLISG--------ARVIEQGNVMVLGgDMRDPKHRRdvcprIAWMPQGLGk 98
Cdd:NF040905 16 ALDDVNLSVREGEIHALCGENGAGKSTLMKVLSGvyphgsyeGEILFDGEVCRFK-DIRDSEALG-----IVIIHQELA- 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 99 nLYHTLSVYENVdffarLFGHDKAEREV--------RINELLTSTGLAPFRDRPAGKLSGGMKQKLGLCCALIHDPELLI 170
Cdd:NF040905 89 -LIPYLSIAENI-----FLGNERAKRGVidwnetnrRARELLAKVGLDESPDTLVTDIGVGKQQLVEIAKALSKDVKLLI 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 171 LDEPTTGvdpLSRSQFWDLIDSIRQ-RQSNMSVLVATAYMEEAERfdwlVAmNAGEVLATG-SAEELRQQTQSATlEEAF 248
Cdd:NF040905 163 LDEPTAA---LNEEDSAALLDLLLElKAQGITSIIISHKLNEIRR----VA-DSITVLRDGrTIETLDCRADEVT-EDRI 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 249 InllpqaqrqahQAVV-------IPPYQPENAEIAIEARDLTMR---FGSFVAVDHVNFRIPRGEIFGFLGSNGCGKsTT 318
Cdd:NF040905 234 I-----------RGMVgrdledrYPERTPKIGEVVFEVKNWTVYhplHPERKVVDDVSLNVRRGEIVGIAGLMGAGR-TE 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 319 MKMltGLLPAS-----EGEAWLFGQPVDPKDIDTRRRVG--YMSQ---AFSLYNELTVRQNLELhARLFHI-------PE 381
Cdd:NF040905 302 LAM--SVFGRSygrniSGTVFKDGKEVDVSTVSDAIDAGlaYVTEdrkGYGLNLIDDIKRNITL-ANLGKVsrrgvidEN 378
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 382 AEIpaRVAEmSERFKLN----DVEDILpESLPLGIRQRLSLAVAVIHRPEMLILDEPTSGVDPVARDMFWQLMVDLSRQD 457
Cdd:NF040905 379 EEI--KVAE-EYRKKMNiktpSVFQKV-GNLSGGNQQKVVLSKWLFTDPDVLILDEPTRGIDVGAKYEIYTIINELAAEG 454
|
490 500
....*....|....*....|....*....
gi 732682709 458 KVTIFISTHfMNEA-ERCDRISLMHAGKV 485
Cdd:NF040905 455 KGVIVISSE-LPELlGMCDRIYVMNEGRI 482
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
234-498 |
1.55e-08 |
|
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The CFTR subfamily domain 1. The cystic fibrosis transmembrane regulator (CFTR), the product of the gene mutated in patients with cystic fibrosis, has adapted the ABC transporter structural motif to form a tightly regulated anion channel at the apical surface of many epithelia. Use of the term assembly of a functional ion channel implies the coming together of subunits, or at least smaller not-yet functional components of the active whole. In fact, on the basis of current knowledge only the CFTR polypeptide itself is required to form an ATP- and protein kinase A-dependent low-conductance chloride channel of the type present in the apical membrane of many epithelial cells. CFTR displays the typical organization (IM-ABC)2 and carries a characteristic hydrophilic R-domain that separates IM1-ABC1 from IM2-ABC2.
Pssm-ID: 213258 [Multi-domain] Cd Length: 282 Bit Score: 56.79 E-value: 1.55e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 234 ELRQQTQSATLEEAFINLLPQAQRqahqavvippyqpENAEIAIEARDLTMRFGSFVAV-----DHVNFRIPRGEIFGFL 308
Cdd:cd03291 3 GVIMENVTAFWDEGFGELLEKAKQ-------------ENNDRKHSSDDNNLFFSNLCLVgapvlKNINLKIEKGEMLAIT 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 309 GSNGCGKSTTMKMLTGLLPASEGEawlfgqpvdpkdIDTRRRVGYMSQaFSLYNELTVRQNLelharLFHIPEAEIpaRV 388
Cdd:cd03291 70 GSTGSGKTSLLMLILGELEPSEGK------------IKHSGRISFSSQ-FSWIMPGTIKENI-----IFGVSYDEY--RY 129
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 389 AEMSERFKLNdvEDI--LPE-----------SLPLGIRQRLSLAVAVIHRPEMLILDEPTSGVDPVARDMFWQLMVDLSR 455
Cdd:cd03291 130 KSVVKACQLE--EDItkFPEkdntvlgeggiTLSGGQRARISLARAVYKDADLYLLDSPFGYLDVFTEKEIFESCVCKLM 207
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 732682709 456 QDKVTIFIsTHFMNEAERCDRISLMHAGKVLASGTPQELVEKR 498
Cdd:cd03291 208 ANKTRILV-TSKMEHLKKADKILILHEGSSYFYGTFSELQSLR 249
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
18-179 |
1.66e-08 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 56.04 E-value: 1.66e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 18 VSQHY-GKTVALNNITLDIPARCMVGLIGPDGVGKSSLLSLISGARVIEQGNVMVLGGDMRDPKHRRdvcprIAWMPQGL 96
Cdd:PRK10908 7 VSKAYlGGRQALQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDITRLKNRE-----VPFLRRQI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 97 GKNL--YHTL---SVYENVDFFARLFGHDKAEREVRINELLTSTGLAPFRDRPAGKLSGGMKQKLGLCCALIHDPELLIL 171
Cdd:PRK10908 82 GMIFqdHHLLmdrTVYDNVAIPLIIAGASGDDIRRRVSAALDKVGLLDKAKNFPIQLSGGEQQRVGIARAVVNKPAVLLA 161
|
....*...
gi 732682709 172 DEPTTGVD 179
Cdd:PRK10908 162 DEPTGNLD 169
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
295-464 |
1.86e-08 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 58.50 E-value: 1.86e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 295 VNFRIPRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGEAwLFGQPVDPKDIDT---RRRVGYMSQ-------------AF 358
Cdd:PTZ00265 404 LNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDI-IINDSHNLKDINLkwwRSKIGVVSQdpllfsnsiknniKY 482
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 359 SLY------------NELTVRQNLELHAR----------------------LFHI-PEAEI--PARVAEMSERFKLNDVE 401
Cdd:PTZ00265 483 SLYslkdlealsnyyNEDGNDSQENKNKRnscrakcagdlndmsnttdsneLIEMrKNYQTikDSEVVDVSKKVLIHDFV 562
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 732682709 402 DILPE-----------SLPLGIRQRLSLAVAVIHRPEMLILDEPTSGVDPVARDMFWQLMVDLS-RQDKVTIFIS 464
Cdd:PTZ00265 563 SALPDkyetlvgsnasKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQKTINNLKgNENRITIIIA 637
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
295-489 |
1.90e-08 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 57.19 E-value: 1.90e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 295 VNFRIPRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGEAWLFGQP-VDP-KDID---TRRRVGYMSQAFSLYNELTVRQN 369
Cdd:PRK11144 17 VNLTLPAQGITAIFGRSGAGKTSLINAISGLTRPQKGRIVLNGRVlFDAeKGIClppEKRRIGYVFQDARLFPHYKVRGN 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 370 LELHARlfhipeaeiparvAEMSERF----KLNDVEDIL---PESLPLGIRQRLSLAVAVIHRPEMLILDEPTSGVD-PV 441
Cdd:PRK11144 97 LRYGMA-------------KSMVAQFdkivALLGIEPLLdryPGSLSGGEKQRVAIGRALLTAPELLLMDEPLASLDlPR 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 732682709 442 ARdmfwQLMV---DLSRQDKVTIFISTHFMNEAER-CDRISLMHAGKVLASG 489
Cdd:PRK11144 164 KR----ELLPyleRLAREINIPILYVSHSLDEILRlADRVVVLEQGKVKAFG 211
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
203-498 |
3.23e-08 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 57.87 E-value: 3.23e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 203 LVATAYMEEAERFDWLVAMNAGEVLATGSAEELRQQTQSATLEEA--FINLLPQAQRQAHQA------VVIPPYQPENAE 274
Cdd:PTZ00243 1221 LSLTMAMQTTATLNWLVRQVATVEADMNSVERLLYYTDEVPHEDMpeLDEEVDALERRTGMAadvtgtVVIEPASPTSAA 1300
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 275 I------AIEARDLTMRF--GSFVAVDHVNFRIPRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGEAWLFGQPVDPKDI- 345
Cdd:PTZ00243 1301 PhpvqagSLVFEGVQMRYreGLPLVLRGVSFRIAPREKVGIVGRTGSGKSTLLLTFMRMVEVCGGEIRVNGREIGAYGLr 1380
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 346 DTRRRVGYMSQAFSLYNElTVRQNLE--LHARlfhipEAEIPA---------RVAEMSERFKLNDVEDILPESLplGIRQ 414
Cdd:PTZ00243 1381 ELRRQFSMIPQDPVLFDG-TVRQNVDpfLEAS-----SAEVWAalelvglreRVASESEGIDSRVLEGGSNYSV--GQRQ 1452
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 415 RLSLAVAVIHRPEMLIL-DEPTSGVDPvARDMFWQLMVdLSRQDKVTIFISTHFMNEAERCDRISLMHAGKVLASGTPQE 493
Cdd:PTZ00243 1453 LMCMARALLKKGSGFILmDEATANIDP-ALDRQIQATV-MSAFSAYTVITIAHRLHTVAQYDKIIVMDHGAVAEMGSPRE 1530
|
....*
gi 732682709 494 LVEKR 498
Cdd:PTZ00243 1531 LVMNR 1535
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
282-439 |
3.33e-08 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 57.49 E-value: 3.33e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 282 LTMRFGSFVAVDHVNFRIPRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGE---------AWL------FGQPVDPKDID 346
Cdd:PRK10636 7 LQIRRGVRVLLDNATATINPGQKVGLVGKNGCGKSTLLALLKNEISADGGSytfpgnwqlAWVnqetpaLPQPALEYVID 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 347 TRRRVGYMSQAFSLYNELTVRQNLE-LHARLFHIPEAEIPARVAEMSERFKLNDVEDILP-ESLPLGIRQRLSLAVAVIH 424
Cdd:PRK10636 87 GDREYRQLEAQLHDANERNDGHAIAtIHGKLDAIDAWTIRSRAASLLHGLGFSNEQLERPvSDFSGGWRMRLNLAQALIC 166
|
170
....*....|....*
gi 732682709 425 RPEMLILDEPTSGVD 439
Cdd:PRK10636 167 RSDLLLLDEPTNHLD 181
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
27-203 |
3.96e-08 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 56.25 E-value: 3.96e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 27 ALNNITLDIPARCMVGLIGPDGVGKSSLLSLISGARVIEQGNVMVLGGDMR--DPKHRRDVCPRIAWMPQGLGKNLYHTL 104
Cdd:PRK15079 36 AVDGVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGEVAWLGKDLLgmKDDEWRAVRSDIQMIFQDPLASLNPRM 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 105 SVYENV-----DFFARLfghDKAEREVRINELLTSTGLAP-FRDRPAGKLSGGMKQKLGLCCALIHDPELLILDEPTTGV 178
Cdd:PRK15079 116 TIGEIIaeplrTYHPKL---SRQEVKDRVKAMMLKVGLLPnLINRYPHEFSGGQCQRIGIARALILEPKLIICDEPVSAL 192
|
170 180
....*....|....*....|....*
gi 732682709 179 DPLSRSQFWDLIDSIrQRQSNMSVL 203
Cdd:PRK15079 193 DVSIQAQVVNLLQQL-QREMGLSLI 216
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
148-262 |
4.14e-08 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 55.48 E-value: 4.14e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 148 LSGGMKQKLGLCCALIHDPELLILDEPTTGVDPLSRSQFWDLIDSIRQRQSnMSVLVATAYMEEAERF-DWLVAMNAGEV 226
Cdd:PRK10418 141 MSGGMLQRMMIALALLCEAPFIIADEPTTDLDVVAQARILDLLESIVQKRA-LGMLLVTHDMGVVARLaDDVAVMSHGRI 219
|
90 100 110
....*....|....*....|....*....|....*.
gi 732682709 227 LATGSAEELRQQTQSATLEeafiNLLpqaqrQAHQA 262
Cdd:PRK10418 220 VEQGDVETLFNAPKHAVTR----SLV-----SAHLA 246
|
|
| PRK13541 |
PRK13541 |
cytochrome c biogenesis protein CcmA; Provisional |
309-451 |
4.74e-08 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184128 [Multi-domain] Cd Length: 195 Bit Score: 54.11 E-value: 4.74e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 309 GSNGCGKSTTMKMLTGLLPASEGEAWLfgqpvdpKDIDTRR----RVGYMSQAFSLYNELTVRQNLELHARLFHIPEAeI 384
Cdd:PRK13541 33 GANGCGKSSLLRMIAGIMQPSSGNIYY-------KNCNINNiakpYCTYIGHNLGLKLEMTVFENLKFWSEIYNSAET-L 104
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 732682709 385 PARVaemsERFKLNDVEDILPESLPLGIRQRLSLAVAVIHRPEMLILDEPTSGVDPVARDMFWQLMV 451
Cdd:PRK13541 105 YAAI----HYFKLHDLLDEKCYSLSSGMQKIVAIARLIACQSDLWLLDEVETNLSKENRDLLNNLIV 167
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
28-238 |
5.48e-08 |
|
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The CFTR subfamily domain 1. The cystic fibrosis transmembrane regulator (CFTR), the product of the gene mutated in patients with cystic fibrosis, has adapted the ABC transporter structural motif to form a tightly regulated anion channel at the apical surface of many epithelia. Use of the term assembly of a functional ion channel implies the coming together of subunits, or at least smaller not-yet functional components of the active whole. In fact, on the basis of current knowledge only the CFTR polypeptide itself is required to form an ATP- and protein kinase A-dependent low-conductance chloride channel of the type present in the apical membrane of many epithelial cells. CFTR displays the typical organization (IM-ABC)2 and carries a characteristic hydrophilic R-domain that separates IM1-ABC1 from IM2-ABC2.
Pssm-ID: 213258 [Multi-domain] Cd Length: 282 Bit Score: 55.25 E-value: 5.48e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 28 LNNITLDIPARCMVGLIGPDGVGKSSLLSLISGARVIEQGNVmvlggdmrdpKH--RRDVCPRIAW-MPQGLGKNLYHTL 104
Cdd:cd03291 53 LKNINLKIEKGEMLAITGSTGSGKTSLLMLILGELEPSEGKI----------KHsgRISFSSQFSWiMPGTIKENIIFGV 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 105 SV----YENVDFFARLfGHDKAEREVRINELLTSTGLApfrdrpagkLSGGMKQKLGLCCALIHDPELLILDEPTTGVDP 180
Cdd:cd03291 123 SYdeyrYKSVVKACQL-EEDITKFPEKDNTVLGEGGIT---------LSGGQRARISLARAVYKDADLYLLDSPFGYLDV 192
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 732682709 181 LSRSQFWDliDSIRQRQSNMSVLVATAYMEEAERFDWLVAMNAGEVLATGSAEELRQQ 238
Cdd:cd03291 193 FTEKEIFE--SCVCKLMANKTRILVTSKMEHLKKADKILILHEGSSYFYGTFSELQSL 248
|
|
| PRK13546 |
PRK13546 |
teichoic acids export ABC transporter ATP-binding subunit TagH; |
18-173 |
5.51e-08 |
|
teichoic acids export ABC transporter ATP-binding subunit TagH;
Pssm-ID: 184131 [Multi-domain] Cd Length: 264 Bit Score: 55.21 E-value: 5.51e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 18 VSQHYGKTV-ALNNITLDIPARCMVGLIGPDGVGKSSLLSLISGARVIEQGNVMVLGgdmrdpkhrrDVcpRIAWMPQGL 96
Cdd:PRK13546 29 IPKHKNKTFfALDDISLKAYEGDVIGLVGINGSGKSTLSNIIGGSLSPTVGKVDRNG----------EV--SVIAISAGL 96
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 732682709 97 GKNLyhtlSVYENVDFFARLFGHDKAEREVRINELLTSTGLAPFRDRPAGKLSGGMKQKLGLCCALIHDPELLILDE 173
Cdd:PRK13546 97 SGQL----TGIENIEFKMLCMGFKRKEIKAMTPKIIEFSELGEFIYQPVKKYSSGMRAKLGFSINITVNPDILVIDE 169
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
280-498 |
5.91e-08 |
|
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis fibrosis transmembrane conductor regulator (CFTR) in eukaryotes. The principal role of this protein is chloride ion conductance. The protein is predicted to consist of 12 transmembrane domains. Mutations or lesions in the genetic loci have been linked to the aetiology of asthma, bronchiectasis, chronic obstructive pulmonary disease etc. Disease-causing mutations have been studied by 36Cl efflux assays in vitro cell cultures and electrophysiology, all of which point to the impairment of chloride channel stability and not the biosynthetic processing per se. [Transport and binding proteins, Anions]
Pssm-ID: 273530 [Multi-domain] Cd Length: 1490 Bit Score: 56.84 E-value: 5.91e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 280 RDLTMRF--GSFVAVDHVNFRIPRGEIFGFLGSNGCGKSTTMKMLTGLLpASEGEAWLFGQPVDPKDIDT-RRRVGYMSQ 356
Cdd:TIGR01271 1221 QGLTAKYteAGRAVLQDLSFSVEGGQRVGLLGRTGSGKSTLLSALLRLL-STEGEIQIDGVSWNSVTLQTwRKAFGVIPQ 1299
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 357 AFSLYNElTVRQNLELHARLfhiPEAEIpARVAE------MSERF--KLNDVEDILPESLPLGIRQRLSLAVAVIHRPEM 428
Cdd:TIGR01271 1300 KVFIFSG-TFRKNLDPYEQW---SDEEI-WKVAEevglksVIEQFpdKLDFVLVDGGYVLSNGHKQLMCLARSILSKAKI 1374
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 732682709 429 LILDEPTSGVDPVArdmfWQLMVDLSRQ--DKVTIFISTHFMNEAERCDRISLMHAGKVLASGTPQELVEKR 498
Cdd:TIGR01271 1375 LLLDEPSAHLDPVT----LQIIRKTLKQsfSNCTVILSEHRVEALLECQQFLVIEGSSVKQYDSIQKLLNET 1442
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
42-332 |
9.08e-08 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 55.67 E-value: 9.08e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 42 GLIGPDGVGKSSLLSLISGARVIEQGNVMVlggdmrDPKHRrdvcpriawmpqgLGKnL------YHTLSVYENVdffar 115
Cdd:PRK15064 31 GLIGANGCGKSTFMKILGGDLEPSAGNVSL------DPNER-------------LGK-LrqdqfaFEEFTVLDTV----- 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 116 LFGHD-----KAER--------------------------------EVRINELLTSTGLA-PFRDRPAGKLSGGMKQKLG 157
Cdd:PRK15064 86 IMGHTelwevKQERdriyalpemseedgmkvadlevkfaemdgytaEARAGELLLGVGIPeEQHYGLMSEVAPGWKLRVL 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 158 LCCALIHDPELLILDEPTTGVDplsrsqfwdlIDSIR-------QRQSNM-----------SVLVATAYMEEAE------ 213
Cdd:PRK15064 166 LAQALFSNPDILLLDEPTNNLD----------INTIRwledvlnERNSTMiiishdrhflnSVCTHMADLDYGElrvypg 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 214 RFD--WLVAMNAGEVLATGSAeelRQQTQSATLEEaFINLLPQAQRQAHQAV-------------VIP-----PYQPENA 273
Cdd:PRK15064 236 NYDeyMTAATQARERLLADNA---KKKAQIAELQS-FVSRFSANASKAKQATsrakqidkikleeVKPssrqnPFIRFEQ 311
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 732682709 274 E-----IAIEARDLTMRFGSFVAVDHVNFRIPRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGE 332
Cdd:PRK15064 312 DkklhrNALEVENLTKGFDNGPLFKNLNLLLEAGERLAIIGENGVGKTTLLRTLVGELEPDSGT 375
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
292-464 |
1.03e-07 |
|
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding cassette transporter (Pat) is involved in the import of very long-chain fatty acids (VLCFA) into the peroxisome. The peroxisomal membrane forms a permeability barrier for a wide variety of metabolites required for and formed during fatty acid beta-oxidation. To communicate with the cytoplasm and mitochondria, peroxisomes need dedicated proteins to transport such hydrophilic molecules across their membranes. X-linked adrenoleukodystrophy (X-ALD) is caused by mutations in the ALD gene, which encodes ALDP (adrenoleukodystrophy protein ), a peroxisomal integral membrane protein that is a member of the ATP-binding cassette (ABC) transporter protein family. The disease is characterized by a striking and unpredictable variation in phenotypic expression. Phenotypes include the rapidly progressive childhood cerebral form (CCALD), the milder adult form, adrenomyeloneuropathy (AMN), and variants without neurologic involvement (i.e. asymptomatic).
Pssm-ID: 213190 [Multi-domain] Cd Length: 166 Bit Score: 52.54 E-value: 1.03e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 292 VDHVNFRIPRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGEAwlfgqpvdpkDIDTRRRVGYMSQAfSLYNELTVRQNLe 371
Cdd:cd03223 17 LKDLSFEIKPGDRLLITGPSGTGKSSLFRALAGLWPWGSGRI----------GMPEGEDLLFLPQR-PYLPLGTLREQL- 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 372 lharlfhipeaeiparvaemserfklndvedILP--ESLPLGIRQRLSLAVAVIHRPEMLILDEPTSGVDPVARDMFWQL 449
Cdd:cd03223 85 -------------------------------IYPwdDVLSGGEQQRLAFARLLLHKPKFVFLDEATSALDEESEDRLYQL 133
|
170
....*....|....*
gi 732682709 450 MvdlsrQDKVTIFIS 464
Cdd:cd03223 134 L-----KELGITVIS 143
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
11-230 |
1.15e-07 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 54.16 E-value: 1.15e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 11 PVAQLAGVSQHYGKTVALNNITLDIPARCMVGLIGPDGVGKSSLLSLISGARVIEQGNVM--VLGGDMRD----PKHRRD 84
Cdd:PRK11701 5 PLLSVRGLTKLYGPRKGCRDVSFDLYPGEVLGIVGESGSGKTTLLNALSARLAPDAGEVHyrMRDGQLRDlyalSEAERR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 85 VCPRIAW--MPQGLGKNLYHTLSVYENV-----DFFARLFGHDKAE-----REVRInelltstglAPFR--DRPAgKLSG 150
Cdd:PRK11701 85 RLLRTEWgfVHQHPRDGLRMQVSAGGNIgerlmAVGARHYGDIRATagdwlERVEI---------DAARidDLPT-TFSG 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 151 GMKQKLGLCCALIHDPELLILDEPTTGVDPLSRSQFWDLIDSIrQRQSNMSVLVATAYMEEAeRF--DWLVAMNAGEVLA 228
Cdd:PRK11701 155 GMQQRLQIARNLVTHPRLVFMDEPTGGLDVSVQARLLDLLRGL-VRELGLAVVIVTHDLAVA-RLlaHRLLVMKQGRVVE 232
|
..
gi 732682709 229 TG 230
Cdd:PRK11701 233 SG 234
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
28-248 |
1.25e-07 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 53.78 E-value: 1.25e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 28 LNNITLD-----IPARCMVG----LIGPDGVGKSSLLSLISGArVIEQGNVMVLGGDMRD------PKHRRDVC----PR 88
Cdd:PRK03695 3 LNDVAVStrlgpLSAEVRAGeilhLVGPNGAGKSTLLARMAGL-LPGSGSIQFAGQPLEAwsaaelARHRAYLSqqqtPP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 89 IAwMPqglgknLYHTLSvyenvdffarLFGHDKA---EREVRINELLTSTGLAPFRDRPAGKLSGGMKQKLGLCCAL--I 163
Cdd:PRK03695 82 FA-MP------VFQYLT----------LHQPDKTrteAVASALNEVAEALGLDDKLGRSVNQLSGGEWQRVRLAAVVlqV 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 164 H---DPE--LLILDEPTTGVDPLSRSQFWDLIDSIrqRQSNMSVLVAT----AYMEEAERFdWLvaMNAGEVLATGSAEE 234
Cdd:PRK03695 145 WpdiNPAgqLLLLDEPMNSLDVAQQAALDRLLSEL--CQQGIAVVMSShdlnHTLRHADRV-WL--LKQGKLLASGRRDE 219
|
250
....*....|....*
gi 732682709 235 -LRQQtqsaTLEEAF 248
Cdd:PRK03695 220 vLTPE----NLAQVF 230
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
14-230 |
2.02e-07 |
|
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: 51.94 E-value: 2.02e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 14 QLAGVSQHygktvALNNITLDIPARCMVGLIGPDGVGKSSLLSLISGArvieqgnvmvlggdmrdpkhrrDVCPRIAWMP 93
Cdd:cd03238 2 TVSGANVH-----NLQNLDVSIPLNVLVVVTGVSGSGKSTLVNEGLYA----------------------SGKARLISFL 54
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 94 QglgknlyhtlsvyenvdffarLFGHDKAereVRINEL--LTSTGLAPFR-DRPAGKLSGGMKQKLGLCCALIHDPE--L 168
Cdd:cd03238 55 P---------------------KFSRNKL---IFIDQLqfLIDVGLGYLTlGQKLSTLSGGELQRVKLASELFSEPPgtL 110
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 169 LILDEPTTGVDPLSRSQFWDLIDSIRQrQSNMSVLV--ATAYMEEAerfDWLVAM------NAGEVLATG 230
Cdd:cd03238 111 FILDEPSTGLHQQDINQLLEVIKGLID-LGNTVILIehNLDVLSSA---DWIIDFgpgsgkSGGKVVFSG 176
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
277-498 |
2.15e-07 |
|
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator (CFTR), the product of the gene mutated in patients with cystic fibrosis, has adapted the ABC transporter structural motif to form a tightly regulated anion channel at the apical surface of many epithelia. Use of the term assembly of a functional ion channel implies the coming together of subunits or at least smaller not-yet functional components of the active whole. In fact, on the basis of current knowledge only the CFTR polypeptide itself is required to form an ATP- and protein kinase A-dependent low-conductance chloride channel of the type present in the apical membrane of many epithelial cells. CFTR displays the typical organization (IM-ABC)2 and carries a characteristic hydrophilic R-domain that separates IM1-ABC1 from IM2-ABC2.
Pssm-ID: 213256 [Multi-domain] Cd Length: 275 Bit Score: 53.32 E-value: 2.15e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 277 IEARDLTMRF--GSFVAVDHVNFRIPRGEIFGFLGSNGCGKSTTMKMLTGLLpASEGEAWLFGQPVDPKDIDT-RRRVGY 353
Cdd:cd03289 3 MTVKDLTAKYteGGNAVLENISFSISPGQRVGLLGRTGSGKSTLLSAFLRLL-NTEGDIQIDGVSWNSVPLQKwRKAFGV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 354 MSQAFSLYNElTVRQNLELHARLfhiPEAEIpARVAEmseRFKLNDVEDILPESLPL-----------GIRQRLSLAVAV 422
Cdd:cd03289 82 IPQKVFIFSG-TFRKNLDPYGKW---SDEEI-WKVAE---EVGLKSVIEQFPGQLDFvlvdggcvlshGHKQLMCLARSV 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 732682709 423 IHRPEMLILDEPTSGVDPVArdmfWQLMVDLSRQ--DKVTIFISTHFMNEAERCDRISLMHAGKVLASGTPQELVEKR 498
Cdd:cd03289 154 LSKAKILLLDEPSAHLDPIT----YQVIRKTLKQafADCTVILSEHRIEAMLECQRFLVIEENKVRQYDSIQKLLNEK 227
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
28-239 |
2.18e-07 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 54.73 E-value: 2.18e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 28 LNNITLDIPARCMVGLIGPDGVGKSSLLSLISGARVIEQGNVMVLGGDMRDPKH---RRDVCPrIAWMPQGLGKnlyhtl 104
Cdd:TIGR00958 497 LKGLTFTLHPGEVVALVGPSGSGKSTVAALLQNLYQPTGGQVLLDGVPLVQYDHhylHRQVAL-VGQEPVLFSG------ 569
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 105 SVYENVdffarLFGHDKAEREVRINELLTS------TGLAPFRDRPAGK----LSGGMKQKLGLCCALIHDPELLILDEP 174
Cdd:TIGR00958 570 SVRENI-----AYGLTDTPDEEIMAAAKAAnahdfiMEFPNGYDTEVGEkgsqLSGGQKQRIAIARALVRKPRVLILDEA 644
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 732682709 175 TTGVDPLSRSQFWDLidsiRQRQSnMSVLVATAYMEEAERFDWLVAMNAGEVLATGSAEELRQQT 239
Cdd:TIGR00958 645 TSALDAECEQLLQES----RSRAS-RTVLLIAHRLSTVERADQILVLKKGSVVEMGTHKQLMEDQ 704
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
282-528 |
4.61e-07 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 53.48 E-value: 4.61e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 282 LTMRFGSFVAVDHVNFRIPR-----GEIFGFLGSNGCGKSTTMKMLTGLLPASEGE-AWLFGQPV--------------- 340
Cdd:PRK10938 4 LQISQGTFRLSDTKTLQLPSltlnaGDSWAFVGANGSGKSALARALAGELPLLSGErQSQFSHITrlsfeqlqklvsdew 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 341 --------DPKDIDTRRRVGYMSQafslyNELTVRQNLELHARLFHIpeaeiparVAEMSERFKLndvedilpesLPLGI 412
Cdd:PRK10938 84 qrnntdmlSPGEDDTGRTTAEIIQ-----DEVKDPARCEQLAQQFGI--------TALLDRRFKY----------LSTGE 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 413 RQRLSLAVAVIHRPEMLILDEPTSGVDPVARDMFWQLMVDLSRQDKVTIFISTHFMNEAERCDRISLMHAGKVLASGTPQ 492
Cdd:PRK10938 141 TRKTLLCQALMSEPDLLILDEPFDGLDVASRQQLAELLASLHQSGITLVLVLNRFDEIPDFVQFAGVLADCTLAETGERE 220
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 732682709 493 ELvekrgaasLEEAFIAYLQEAAGQSN----EAEAPPVVH 528
Cdd:PRK10938 221 EI--------LQQALVAQLAHSEQLEGvqlpEPDEPSARH 252
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
104-235 |
5.00e-07 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 53.88 E-value: 5.00e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 104 LSVYENVDFfarlfGHDKAERE--------VRINELLTS------TGLAPFrdrpaGK-LSGGMKQKLGLCCALIHDPEL 168
Cdd:PTZ00265 1310 MSIYENIKF-----GKEDATREdvkrackfAAIDEFIESlpnkydTNVGPY-----GKsLSGGQKQRIAIARALLREPKI 1379
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 732682709 169 LILDEPTTGVDPLSRSQFWDLIDSIRQRqSNMSVLVATAYMEEAERFDWLVAMNAGE-----VLATGSAEEL 235
Cdd:PTZ00265 1380 LLLDEATSSLDSNSEKLIEKTIVDIKDK-ADKTIITIAHRIASIKRSDKIVVFNNPDrtgsfVQAHGTHEEL 1450
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
28-235 |
7.95e-07 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 53.20 E-value: 7.95e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 28 LNNITLDIPARCMVGLIGPDGVGKSSLLSLI-------SGARVIEQGNVMVLggdmrdpkhrrdvcPRIAWMpqglgknl 100
Cdd:PLN03130 633 LSNINLDVPVGSLVAIVGSTGEGKTSLISAMlgelpprSDASVVIRGTVAYV--------------PQVSWI-------- 690
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 101 yHTLSVYENVdFFARLFGHDKAEREVRINELLTSTGLAPFRDRP-----AGKLSGGMKQKLGLCCALIHDPELLILDEPT 175
Cdd:PLN03130 691 -FNATVRDNI-LFGSPFDPERYERAIDVTALQHDLDLLPGGDLTeigerGVNISGGQKQRVSMARAVYSNSDVYIFDDPL 768
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 732682709 176 TGVDPLSRSQFWD--LIDSIRQRqsnMSVLVaTAYMEEAERFDWLVAMNAGEVLATGSAEEL 235
Cdd:PLN03130 769 SALDAHVGRQVFDkcIKDELRGK---TRVLV-TNQLHFLSQVDRIILVHEGMIKEEGTYEEL 826
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
11-206 |
8.21e-07 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 50.87 E-value: 8.21e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 11 PVAQLAGVSQHYGKTVALNNITLDIPARCMVGLIGPDGVGKSSLLSLISGARVIEQGNVMVLGGDMR--DPKHRRDVCPR 88
Cdd:PRK10247 6 PLLQLQNVGYLAGDAKILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFEGEDIStlKPEIYRQQVSY 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 89 IAWMPQGLGKnlyhtlSVYENVdFFARLFGHDKAEREVRINEL----LTSTGLapfrDRPAGKLSGGMKQKLGLCCALIH 164
Cdd:PRK10247 86 CAQTPTLFGD------TVYDNL-IFPWQIRNQQPDPAIFLDDLerfaLPDTIL----TKNIAELSGGEKQRISLIRNLQF 154
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 732682709 165 DPELLILDEPTTGVDPLSRSQFWDLIDSIrQRQSNMSVLVAT 206
Cdd:PRK10247 155 MPKVLLLDEITSALDESNKHNVNEIIHRY-VREQNIAVLWVT 195
|
|
| ABC_UvrA_II |
cd03271 |
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair ... |
28-231 |
8.27e-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: 51.46 E-value: 8.27e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 28 LNNITLDIPARCMVGLIGPDGVGKSSLLSLI---SGARVIEQGNVMVLGGDM--------------RDPKHRR------- 83
Cdd:cd03271 11 LKNIDVDIPLGVLTCVTGVSGSGKSSLINDTlypALARRLHLKKEQPGNHDRieglehidkvividQSPIGRTprsnpat 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 84 -------------DVCPRIAWMPQGL-----GKNLYHTL--SVYENVDFFArlfGHDKAEREVRineLLTSTGLAPFR-D 142
Cdd:cd03271 91 ytgvfdeirelfcEVCKGKRYNRETLevrykGKSIADVLdmTVEEALEFFE---NIPKIARKLQ---TLCDVGLGYIKlG 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 143 RPAGKLSGGMKQKLGLCCALIH---DPELLILDEPTTGVDPLSRSQFWDLIDSIRQRQSnmSVLVATAYMEEAERFDWLV 219
Cdd:cd03271 165 QPATTLSGGEAQRIKLAKELSKrstGKTLYILDEPTTGLHFHDVKKLLEVLQRLVDKGN--TVVVIEHNLDVIKCADWII 242
|
250
....*....|....*...
gi 732682709 220 AM------NAGEVLATGS 231
Cdd:cd03271 243 DLgpeggdGGGQVVASGT 260
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
7-179 |
1.04e-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: 52.24 E-value: 1.04e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 7 VPVPP-----VAQLAGVSQHYGKTVALNNITLDIPARCMVGLIGPDGVGKSSLLSLISGARVIEQGNVMVlgGDMrdpkh 81
Cdd:TIGR03719 312 IPPGPrlgdkVIEAENLTKAFGDKLLIDDLSFKLPPGGIVGVIGPNGAGKSTLFRMITGQEQPDSGTIEI--GET----- 384
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 82 rrdvcPRIAWMPQGLgKNLYHTLSVYENVDffarlFGHDkaerEVRIN--ELLTSTGLAPF------RDRPAGKLSGGMK 153
Cdd:TIGR03719 385 -----VKLAYVDQSR-DALDPNKTVWEEIS-----GGLD----IIKLGkrEIPSRAYVGRFnfkgsdQQKKVGQLSGGER 449
|
170 180
....*....|....*....|....*.
gi 732682709 154 QKLGLCCALIHDPELLILDEPTTGVD 179
Cdd:TIGR03719 450 NRVHLAKTLKSGGNVLLLDEPTNDLD 475
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
27-226 |
1.11e-06 |
|
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: 50.10 E-value: 1.11e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 27 ALNNITLDIPARCMVGLIGPDGVGKSSLLSLISGARVIEQGNVMVLGGDMRDPKhRRDVCPRIAWMPQGlgknlyHTL-- 104
Cdd:cd03369 23 VLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDGIDISTIP-LEDLRSSLTIIPQD------PTLfs 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 105 -SVYENVDFFARLfghdkAEREVRINELLTSTGLapfrdrpagKLSGGMKQKLGLCCALIHDPELLILDEPTTGVDPLSR 183
Cdd:cd03369 96 gTIRSNLDPFDEY-----SDEEIYGALRVSEGGL---------NLSQGQRQLLCLARALLKRPRVLVLDEATASIDYATD 161
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 732682709 184 SQfwdLIDSIRQRQSNMSVLVATAYMEEAERFDWLVAMNAGEV 226
Cdd:cd03369 162 AL---IQKTIREEFTNSTILTIAHRLRTIIDYDKILVMDAGEV 201
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
295-523 |
1.14e-06 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 52.86 E-value: 1.14e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 295 VNFRIPRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGEAWlfgqpvdpkdidTRRRVGYMSQAFSLYNElTVRQNLelha 374
Cdd:PTZ00243 679 VSVSVPRGKLTVVLGATGSGKSTLLQSLLSQFEISEGRVW------------AERSIAYVPQQAWIMNA-TVRGNI---- 741
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 375 rLFHIPEAeiPARVAEMSERFKLN-DV-------EDILPE---SLPLGIRQRLSLAVAVIHRPEMLILDEPTSGVDP--- 440
Cdd:PTZ00243 742 -LFFDEED--AARLADAVRVSQLEaDLaqlggglETEIGEkgvNLSGGQKARVSLARAVYANRDVYLLDDPLSALDAhvg 818
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 441 --VARDMFwqlmvdLSRQDKVTIFISTHFMNEAERCDRISLMHAGKVLASGTPQELVEkrgaASLEEAFIAYLQE---AA 515
Cdd:PTZ00243 819 erVVEECF------LGALAGKTRVLATHQVHVVPRADYVVALGDGRVEFSGSSADFMR----TSLYATLAAELKEnkdSK 888
|
....*...
gi 732682709 516 GQSNEAEA 523
Cdd:PTZ00243 889 EGDADAEV 896
|
|
| SapD |
COG4170 |
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms]; |
148-269 |
1.28e-06 |
|
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms];
Pssm-ID: 443330 [Multi-domain] Cd Length: 331 Bit Score: 51.44 E-value: 1.28e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 148 LSGGMKQKLGLCCALIHDPELLILDEPTTGVDPLSRSQFWDLIDSIRQRQsNMSVLVATAYMEE-AERFDWLVAMNAGEV 226
Cdd:COG4170 159 LTEGECQKVMIAMAIANQPRLLIADEPTNAMESTTQAQIFRLLARLNQLQ-GTSILLISHDLESiSQWADTITVLYCGQT 237
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 732682709 227 LATGSAEELRQQ-----TQsatleeAFINLLPQAQRQ-AHQAV------VIPPYQ 269
Cdd:COG4170 238 VESGPTEQILKSphhpyTK------ALLRSMPDFRQPlPHKSRlntlpgSIPPLQ 286
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
28-235 |
1.37e-06 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 52.29 E-value: 1.37e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 28 LNNITLDIPARCMVGLIGPDGVGKSSLLSLISGARVIEQGNVMVLGGDMRdpkhrrdVCPRIAWMpqglgknlyHTLSVY 107
Cdd:PLN03232 633 LSDINLEIPVGSLVAIVGGTGEGKTSLISAMLGELSHAETSSVVIRGSVA-------YVPQVSWI---------FNATVR 696
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 108 ENVdFFARLFGHDKAEREVRINELLTSTGLAPFRDRP-----AGKLSGGMKQKLGLCCALIHDPELLILDEPTTGVDPLS 182
Cdd:PLN03232 697 ENI-LFGSDFESERYWRAIDVTALQHDLDLLPGRDLTeigerGVNISGGQKQRVSMARAVYSNSDIYIFDDPLSALDAHV 775
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 732682709 183 RSQFWDliDSIRQRQSNMSVLVATAYMEEAERFDWLVAMNAGEVLATGSAEEL 235
Cdd:PLN03232 776 AHQVFD--SCMKDELKGKTRVLVTNQLHFLPLMDRIILVSEGMIKEEGTFAEL 826
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
12-181 |
1.75e-06 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 49.96 E-value: 1.75e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 12 VAQLAGVSQHYGKTVALNNITLDIPARCMVGLIGPDGVGKSSLLSLISGARVIEQGNVMVlggDMRDPKHRRDvCPRIaw 91
Cdd:COG2401 30 VLEAFGVELRVVERYVLRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGALKGTPVAGCV---DVPDNQFGRE-ASLI-- 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 92 mpqglgKNLYHTLSVYENVdffarlfghdkaerevrinELLTSTGL--APFRDRPAGKLSGGMKQKLGLCCALIHDPELL 169
Cdd:COG2401 104 ------DAIGRKGDFKDAV-------------------ELLNAVGLsdAVLWLRRFKELSTGQKFRFRLALLLAERPKLL 158
|
170
....*....|..
gi 732682709 170 ILDEPTTGVDPL 181
Cdd:COG2401 159 VIDEFCSHLDRQ 170
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
28-224 |
1.89e-06 |
|
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The sulfonylurea receptor SUR is an ATP transporter of the ABCC/MRP family with tandem ATPase binding domains. Unlike other ABC proteins, it has no intrinsic transport function, neither active nor passive, but associates with the potassium channel proteins Kir6.1 or Kir6.2 to form the ATP-sensitive potassium (K(ATP)) channel. Within the channel complex, SUR serves as a regulatory subunit that fine-tunes the gating of Kir6.x in response to alterations in cellular metabolism. It constitutes a major pharmaceutical target as it binds numerous drugs, K(ATP) channel openers and blockers, capable of up- or down-regulating channel activity.
Pssm-ID: 213257 [Multi-domain] Cd Length: 218 Bit Score: 49.64 E-value: 1.89e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 28 LNNITLDIPARCMVGLIGPDGVGKSSLL-------SLISGARVIEQGNVMVLGGDMRDPKHRRDVcpriAWMPQglgKNL 100
Cdd:cd03290 17 LSNINIRIPTGQLTMIVGQVGCGKSSLLlailgemQTLEGKVHWSNKNESEPSFEATRSRNRYSV----AYAAQ---KPW 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 101 YHTLSVYENVDfFARLFGHDKAEREVRINELLTSTGLAPFRDRP-----AGKLSGGMKQKLGLCCALIHDPELLILDEPT 175
Cdd:cd03290 90 LLNATVEENIT-FGSPFNKQRYKAVTDACSLQPDIDLLPFGDQTeigerGINLSGGQRQRICVARALYQNTNIVFLDDPF 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 732682709 176 TGVD-PLSRSQFWDLIDSIRQRQSNMSVLVaTAYMEEAERFDWLVAMNAG 224
Cdd:cd03290 169 SALDiHLSDHLMQEGILKFLQDDKRTLVLV-THKLQYLPHADWIIAMKDG 217
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
149-270 |
3.12e-06 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 50.11 E-value: 3.12e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 149 SGGMKQKLGLCCALIHDPELLILDEPTTGVDPLSRSQFWDLIDSIRqRQSNMSVLVATAYME-EAERFDWLVAMNAGEVL 227
Cdd:PRK09473 163 SGGMRQRVMIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELK-REFNTAIIMITHDLGvVAGICDKVLVMYAGRTM 241
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 732682709 228 ATGSAEELRQQTqSATLEEAFINLLPQAQRQAHQAVVIP-------------PYQP 270
Cdd:PRK09473 242 EYGNARDVFYQP-SHPYSIGLLNAVPRLDAEGESLLTIPgnppnllrlpkgcPFQP 296
|
|
| ABC_Rad50 |
cd03240 |
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ... |
282-440 |
3.53e-06 |
|
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: 48.76 E-value: 3.53e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 282 LTMR-FGSFVAVDHVNFRIPrgeIFGFLGSNGCGKSTTM---KM-LTGLLPASegeawLFGQPVDPKDIDTRRRVGYMSQ 356
Cdd:cd03240 4 LSIRnIRSFHERSEIEFFSP---LTLIVGQNGAGKTTIIealKYaLTGELPPN-----SKGGAHDPKLIREGEVRAQVKL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 357 AFSLYN--ELTVRQNLELHARLFHIPEAEIPARVAEMSERfkLNDVEDILpeslpLGIRQRLSLAVAVIHRPEMLILDEP 434
Cdd:cd03240 76 AFENANgkKYTITRSLAILENVIFCHQGESNWPLLDMRGR--CSGGEKVL-----ASLIIRLALAETFGSNCGILALDEP 148
|
....*.
gi 732682709 435 TSGVDP 440
Cdd:cd03240 149 TTNLDE 154
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
28-248 |
3.64e-06 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 50.65 E-value: 3.64e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 28 LNNITLDIPARCMVGLIGPDGVGKSSLLSLISGaRVieQGNVMVLGGDMRDPKHRRDVCPRIAWMPQGlgKNLYHTLSVY 107
Cdd:PLN03211 84 LNGVTGMASPGEILAVLGPSGSGKSTLLNALAG-RI--QGNNFTGTILANNRKPTKQILKRTGFVTQD--DILYPHLTVR 158
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 108 ENVDFFARLFGHDKAEREVRI---NELLTSTGLAPFRDRPAGK-----LSGGMKQKLGLCCALIHDPELLILDEPTTGVD 179
Cdd:PLN03211 159 ETLVFCSLLRLPKSLTKQEKIlvaESVISELGLTKCENTIIGNsfirgISGGERKRVSIAHEMLINPSLLILDEPTSGLD 238
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 732682709 180 PLSRSQFWDLIDSIRQRQSNmsvlVATAYMEEAER----FDWLVAMNAGEVLATGSAEELRQQTQSATLEEAF 248
Cdd:PLN03211 239 ATAAYRLVLTLGSLAQKGKT----IVTSMHQPSSRvyqmFDSVLVLSEGRCLFFGKGSDAMAYFESVGFSPSF 307
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
277-499 |
5.77e-06 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 48.87 E-value: 5.77e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 277 IEARDLTMRFGSFVAVDHVNFRIPRGEIFGFLGSNGCGKSTTMKMLTGlLPA---SEGEAWLFGQPVDPKDIDTRRRVGy 353
Cdd:CHL00131 8 LEIKNLHASVNENEILKGLNLSINKGEIHAIMGPNGSGKSTLSKVIAG-HPAykiLEGDILFKGESILDLEPEERAHLG- 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 354 MSQAFS----------------LYNELTVRQNL-ELHA-RLFHIPEAEIParVAEMSERFKLNDVEdilpESLPLGIRQR 415
Cdd:CHL00131 86 IFLAFQypieipgvsnadflrlAYNSKRKFQGLpELDPlEFLEIINEKLK--LVGMDPSFLSRNVN----EGFSGGEKKR 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 416 LSLAVAVIHRPEMLILDEPTSGVDPVARDMFWQLMVDLSRQDKVTIFIsTHFMNEAE--RCDRISLMHAGKVLASGT--- 490
Cdd:CHL00131 160 NEILQMALLDSELAILDETDSGLDIDALKIIAEGINKLMTSENSIILI-THYQRLLDyiKPDYVHVMQNGKIIKTGDael 238
|
....*....
gi 732682709 491 PQELvEKRG 499
Cdd:CHL00131 239 AKEL-EKKG 246
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
302-490 |
6.09e-06 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 50.23 E-value: 6.09e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 302 GEIFGFLGSNGCGKSTTMKMLTGLLPAS--EGEAWLFGQPvdpKDIDTRRRV-GYMSQAFSLYNELTVRQNLELHARL-- 376
Cdd:PLN03140 906 GVLTALMGVSGAGKTTLMDVLAGRKTGGyiEGDIRISGFP---KKQETFARIsGYCEQNDIHSPQVTVRESLIYSAFLrl 982
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 377 -FHIPEAEIPARVAEMSERFKLNDVEDI---LPESLPLGI--RQRLSLAVAVIHRPEMLILDEPTSGVDPVARDMFWQLM 450
Cdd:PLN03140 983 pKEVSKEEKMMFVDEVMELVELDNLKDAivgLPGVTGLSTeqRKRLTIAVELVANPSIIFMDEPTSGLDARAAAIVMRTV 1062
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 732682709 451 ---VDLSR-------QDKVTIFisthfmneaERCDRISLM-HAGKVLASGT 490
Cdd:PLN03140 1063 rntVDTGRtvvctihQPSIDIF---------EAFDELLLMkRGGQVIYSGP 1104
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
28-226 |
6.74e-06 |
|
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette transporters; The pleiotropic drug resistance (PDR) is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. This PDR subfamily represents domain I of its (ABC-IM)2 organization. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds including sugars, ions, peptides, and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213200 [Multi-domain] Cd Length: 202 Bit Score: 48.03 E-value: 6.74e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 28 LNNITLDIPARCMVGLIGPDGVGKSSLLSLISGARVieqGNVMVlGGDMR----DPKHRRDVCPR-IAWMPQGlgKNLYH 102
Cdd:cd03233 23 LKDFSGVVKPGEMVLVLGRPGSGCSTLLKALANRTE---GNVSV-EGDIHyngiPYKEFAEKYPGeIIYVSEE--DVHFP 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 103 TLSVYENVDFFARLFGHDKaereVRinelltstglapfrdrpagKLSGGMKQKLGLCCALIHDPELLILDEPTTGVDplS 182
Cdd:cd03233 97 TLTVRETLDFALRCKGNEF----VR-------------------GISGGERKRVSIAEALVSRASVLCWDNSTRGLD--S 151
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 732682709 183 RSQFwDLIDSIRQ--RQSNMSVLVAT--AYMEEAERFDWLVAMNAGEV 226
Cdd:cd03233 152 STAL-EILKCIRTmaDVLKTTTFVSLyqASDEIYDLFDKVLVLYEGRQ 198
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
3-183 |
6.86e-06 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 49.63 E-value: 6.86e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 3 HLELVPVPPVAQLAGVSQHYGKTVALNNITLDIPARCMVGLIGPDGVGKSSLLSLISGARviEQG--NVMVLGGdmrdpk 80
Cdd:PRK10938 251 RHALPANEPRIVLNNGVVSYNDRPILHNLSWQVNPGEHWQIVGPNGAGKSTLLSLITGDH--PQGysNDLTLFG------ 322
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 81 HRR-------DVCPRIAWMPQGLGKNlYHTLSVYENV---DFF----------ARLfgHDKAEREVRINELLTSTGLAPF 140
Cdd:PRK10938 323 RRRgsgetiwDIKKHIGYVSSSLHLD-YRVSTSVRNVilsGFFdsigiyqavsDRQ--QKLAQQWLDILGIDKRTADAPF 399
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 732682709 141 RDrpagkLSGGmKQKLGLCC-ALIHDPELLILDEPTTGVDPLSR 183
Cdd:PRK10938 400 HS-----LSWG-QQRLALIVrALVKHPTLLILDEPLQGLDPLNR 437
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
406-495 |
7.34e-06 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 50.03 E-value: 7.34e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 406 ESLPLGIRQRLSLAVAVIHRPEMLILDEPTSGVDPVARDMFWQLMVDLSRQDKVTIFISTHFMNEAERCDRISLMH---- 481
Cdd:PTZ00265 1357 KSLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDIKDKADKTIITIAHRIASIKRSDKIVVFNnpdr 1436
|
90
....*....|....*
gi 732682709 482 -AGKVLASGTPQELV 495
Cdd:PTZ00265 1437 tGSFVQAHGTHEELL 1451
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
84-235 |
7.70e-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: 50.01 E-value: 7.70e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 84 DVCPRIAWMPQGL-----GKNLYHTL--SVYENVDFFArlfGHDKAEREVrinELLTSTGLAPFR-DRPAGKLSGGMKQK 155
Cdd:TIGR00630 764 EVCKGKRYNRETLevkykGKNIADVLdmTVEEAYEFFE---AVPSISRKL---QTLCDVGLGYIRlGQPATTLSGGEAQR 837
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 156 LGLCCALIHD---PELLILDEPTTGVdplsrsQFWD---LIDSIrQR---QSNmSVLVATAYMEEAERFDWLV------A 220
Cdd:TIGR00630 838 IKLAKELSKRstgRTLYILDEPTTGL------HFDDikkLLEVL-QRlvdKGN-TVVVIEHNLDVIKTADYIIdlgpegG 909
|
170
....*....|....*
gi 732682709 221 MNAGEVLATGSAEEL 235
Cdd:TIGR00630 910 DGGGTVVASGTPEEV 924
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
145-205 |
1.43e-05 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 49.26 E-value: 1.43e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 732682709 145 AGKLSGGMKQKLGLCCALIHDPELLILDEPTTGVDPLSRSQFWDLIDSIRQRQSNMSVLVA 205
Cdd:PTZ00265 577 ASKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQKTINNLKGNENRITIIIA 637
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
9-262 |
1.69e-05 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 48.42 E-value: 1.69e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 9 VPPVAQLAG------VSQHY-GKTVALNNITLDIPARCMVGLIGPDGVGKSSLLSLISGARVIEQGNVMVLGGDMRDPKH 81
Cdd:PRK13657 325 AIDLGRVKGavefddVSFSYdNSRQGVEDVSFEAKPGQTVAIVGPTGAGKSTLINLLQRVFDPQSGRILIDGTDIRTVTR 404
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 82 rrdvcpriawmpQGLGKNLYhtlSVYENVDFFAR------LFGHDKAEREvrinELLTSTGLAPFRD----RPAG----- 146
Cdd:PRK13657 405 ------------ASLRRNIA---VVFQDAGLFNRsiedniRVGRPDATDE----EMRAAAERAQAHDfierKPDGydtvv 465
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 147 -----KLSGGMKQKLGLCCALIHDPELLILDEPTTGVDPLSRSQFWDLIDSIRQRQSNMSVLVATAYMEEAERfdwLVAM 221
Cdd:PRK13657 466 gergrQLSGGERQRLAIARALLKDPPILILDEATSALDVETEAKVKAALDELMKGRTTFIIAHRLSTVRNADR---ILVF 542
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 732682709 222 NAGEVLATGSAEELRQQTQS-ATLEEAFINLLPQAQRQAHQA 262
Cdd:PRK13657 543 DNGRVVESGSFDELVARGGRfAALLRAQGMLQEDERRKQPAA 584
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
299-461 |
2.38e-05 |
|
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI), is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI s are not transport proteins and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLIs have an N-terminal Fe-S domain and two nucleotide binding domains which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213203 [Multi-domain] Cd Length: 255 Bit Score: 46.98 E-value: 2.38e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 299 IPR-GEIFGFLGSNGCGKSTTMKMLTGLLPASEGEawlFGQPVDPKDIDTRRRVGYMSQAFSLYNELTVR-----QNLEL 372
Cdd:cd03236 22 VPReGQVLGLVGPNGIGKSTALKILAGKLKPNLGK---FDDPPDWDEILDEFRGSELQNYFTKLLEGDVKvivkpQYVDL 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 373 harlfhIPEAeIPARVAEM----SERFKLNDVEDILP---------ESLPLGIRQRLSLAVAVIHRPEMLILDEPTSGVD 439
Cdd:cd03236 99 ------IPKA-VKGKVGELlkkkDERGKLDELVDQLElrhvldrniDQLSGGELQRVAIAAALARDADFYFFDEPSSYLD 171
|
170 180
....*....|....*....|..
gi 732682709 440 PVARDMFWQLMVDLSRQDKVTI 461
Cdd:cd03236 172 IKQRLNAARLIRELAEDDNYVL 193
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
292-464 |
2.43e-05 |
|
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: 46.10 E-value: 2.43e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 292 VDHVNFRIPRGEIFGFLGSNGCGKSTTMKMLTGLLPAS---EGEAWLFGQPVDPKDIDTRRRVGYMSQAFSLYNELTVRQ 368
Cdd:cd03233 23 LKDFSGVVKPGEMVLVLGRPGSGCSTLLKALANRTEGNvsvEGDIHYNGIPYKEFAEKYPGEIIYVSEEDVHFPTLTVRE 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 369 NLELHARLfhipeaeiparvaemserfKLNDVEdilpESLPLGIRQRLSLAVAVIHRPEMLILDEPTSGVDPVARDMFWQ 448
Cdd:cd03233 103 TLDFALRC-------------------KGNEFV----RGISGGERKRVSIAEALVSRASVLCWDNSTRGLDSSTALEILK 159
|
170
....*....|....*.
gi 732682709 449 LMVDLSRQDKVTIFIS 464
Cdd:cd03233 160 CIRTMADVLKTTTFVS 175
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
10-189 |
2.86e-05 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 47.27 E-value: 2.86e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 10 PPVAQLAGVSQHYG---------KTV-ALNNITLDIPARCMVGLIGPDGVGKSSLLSLISgarVIEQ---GNVMVLGGDM 76
Cdd:PRK11308 3 QPLLQAIDLKKHYPvkrglfkpeRLVkALDGVSFTLERGKTLAVVGESGCGKSTLARLLT---MIETptgGELYYQGQDL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 77 RDPKH------RRDV-----------CPRiawmpQGLGKNLYHTLSVyeNVDFfarlfghDKAEREVRINELLTSTGLAP 139
Cdd:PRK11308 80 LKADPeaqkllRQKIqivfqnpygslNPR-----KKVGQILEEPLLI--NTSL-------SAAERREKALAMMAKVGLRP 145
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 732682709 140 -FRDRPAGKLSGGMKQKLGLCCALIHDPELLILDEPTTGVDPLSRSQ----FWDL 189
Cdd:PRK11308 146 eHYDRYPHMFSGGQRQRIAIARALMLDPDVVVADEPVSALDVSVQAQvlnlMMDL 200
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
28-203 |
2.90e-05 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 47.88 E-value: 2.90e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 28 LNNITLDIPA--RCMVglIGPDGVGKSSLLSLISG------ARVI--EQGNVMVLggdmrdpkhrrdvcPRIAWMPQGlg 97
Cdd:COG4178 379 LEDLSLSLKPgeRLLI--TGPSGSGKSTLLRAIAGlwpygsGRIArpAGARVLFL--------------PQRPYLPLG-- 440
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 98 kNLYHTLSvYENvdffarlfGHDKAEREvRINELLTSTGLAPFRDRP------AGKLSGGMKQKLGLCCALIHDPELLIL 171
Cdd:COG4178 441 -TLREALL-YPA--------TAEAFSDA-ELREALEAVGLGHLAERLdeeadwDQVLSLGEQQRLAFARLLLHKPDWLFL 509
|
170 180 190
....*....|....*....|....*....|..
gi 732682709 172 DEPTTGVDPLSRSQFWDLidsIRQRQSNMSVL 203
Cdd:COG4178 510 DEATSALDEENEAALYQL---LREELPGTTVI 538
|
|
| ABCC_SUR2 |
cd03288 |
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The ... |
274-498 |
3.79e-05 |
|
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The sulfonylurea receptor SUR is an ATP binding cassette (ABC) protein of the ABCC/MRP family. Unlike other ABC proteins, it has no intrinsic transport function, neither active nor passive, but associates with the potassium channel proteins Kir6.1 or Kir6.2 to form the ATP-sensitive potassium (K(ATP)) channel. Within the channel complex, SUR serves as a regulatory subunit that fine-tunes the gating of Kir6.x in response to alterations in cellular metabolism. It constitutes a major pharmaceutical target as it binds numerous drugs, K(ATP) channel openers and blockers, capable of up- or down-regulating channel activity.
Pssm-ID: 213255 [Multi-domain] Cd Length: 257 Bit Score: 46.44 E-value: 3.79e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 274 EIAIEarDLTMRFGSFV--AVDHVNFRIPRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGEAWLFGQPVDPKDIDT-RRR 350
Cdd:cd03288 19 EIKIH--DLCVRYENNLkpVLKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVIDGIDISKLPLHTlRSR 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 351 VGYMSQAFSLYNElTVRQNLElharlfhiPEAEIP-ARVAEMSERFKLNDVEDILP-----------ESLPLGIRQRLSL 418
Cdd:cd03288 97 LSIILQDPILFSG-SIRFNLD--------PECKCTdDRLWEALEIAQLKNMVKSLPggldavvteggENFSVGQRQLFCL 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 419 AVAVIHRPEMLILDEPTSGVDpVARDMFWQLMVDLSRQDKVTIFIStHFMNEAERCDRISLMHAGKVLASGTPQELVEKR 498
Cdd:cd03288 168 ARAFVRKSSILIMDEATASID-MATENILQKVVMTAFADRTVVTIA-HRVSTILDADLVLVLSRGILVECDTPENLLAQE 245
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
45-180 |
3.85e-05 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 46.00 E-value: 3.85e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 45 GPDGVGKSSLLSLISGARVIEQGNVMVLGgdmrDPKHRRDVCPRIAWMPQGLGknLYHTLSVYENVDFFARLFGHdKAER 124
Cdd:PRK13543 44 GDNGAGKTTLLRVLAGLLHVESGQIQIDG----KTATRGDRSRFMAYLGHLPG--LKADLSTLENLHFLCGLHGR-RAKQ 116
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 732682709 125 EVriNELLTSTGLAPFRDRPAGKLSGGMKQKLGLCCALIHDPELLILDEPTTGVDP 180
Cdd:PRK13543 117 MP--GSALAIVGLAGYEDTLVRQLSAGQKKRLALARLWLSPAPLWLLDEPYANLDL 170
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
147-221 |
4.53e-05 |
|
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems involved in cellular processes other than transport. These families are characterized by the fact that the ABC subunit is made up of duplicated, fused ABC modules (ABC2). No known transmembrane proteins or domains are associated with these proteins.
Pssm-ID: 213194 [Multi-domain] Cd Length: 162 Bit Score: 44.66 E-value: 4.53e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 147 KLSGGMKQKLGLCCALIH-----DPeLLILDEPTTGVDPLSRSQFWDLIdsIRQRQSNMSVLVATAYMEEAERFDWLVAM 221
Cdd:cd03227 77 QLSGGEKELSALALILALaslkpRP-LYILDEIDRGLDPRDGQALAEAI--LEHLVKGAQVIVITHLPELAELADKLIHI 153
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
7-71 |
5.22e-05 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 47.04 E-value: 5.22e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 7 VPVPP-----VAQLAGVSQHYGKTVALNNITLDIPARCMVGLIGPDGVGKSSLLSLISGARVIEQGNVMV 71
Cdd:PRK11819 314 IPPGPrlgdkVIEAENLSKSFGDRLLIDDLSFSLPPGGIVGIIGPNGAGKSTLFKMITGQEQPDSGTIKI 383
|
|
| PRK15093 |
PRK15093 |
peptide ABC transporter ATP-binding protein SapD; |
23-235 |
5.81e-05 |
|
peptide ABC transporter ATP-binding protein SapD;
Pssm-ID: 185049 [Multi-domain] Cd Length: 330 Bit Score: 46.33 E-value: 5.81e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 23 GKTVALNNITLDIPARCMVGLIGPDGVGKSSLLSLISGarvIEQGNVMVLGGDMR---------DPKHRRDVCPRIAWM- 92
Cdd:PRK15093 18 GWVKAVDRVSMTLTEGEIRGLVGESGSGKSLIAKAICG---VTKDNWRVTADRMRfddidllrlSPRERRKLVGHNVSMi 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 93 ---PQG-------LGKNLYHTLSVYENVDFFARLFGHdkaeREVRINELLTSTGLAPFRDRPAG---KLSGGMKQKLGLC 159
Cdd:PRK15093 95 fqePQScldpserVGRQLMQNIPGWTYKGRWWQRFGW----RKRRAIELLHRVGIKDHKDAMRSfpyELTEGECQKVMIA 170
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 732682709 160 CALIHDPELLILDEPTTGVDPLSRSQFWDLIDSIRQrQSNMSVLVATAYMEEAERF-DWLVAMNAGEVLATGSAEEL 235
Cdd:PRK15093 171 IALANQPRLLIADEPTNAMEPTTQAQIFRLLTRLNQ-NNNTTILLISHDLQMLSQWaDKINVLYCGQTVETAPSKEL 246
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
27-239 |
6.24e-05 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 46.63 E-value: 6.24e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 27 ALNNITLDIPARCMVGLIGPDGVGKSSLLSLISGARVIEQGNVMVlgGDMRDPKHRRDVC-PRIAWMPQ-------GLGK 98
Cdd:PRK10789 330 ALENVNFTLKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGDIRF--HDIPLTKLQLDSWrSRLAVVSQtpflfsdTVAN 407
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 99 N--LYHTLSVYENVDFFARLFG-HDKAERevrinelltstgLAPFRDRPAGK----LSGGMKQKLGLCCALIHDPELLIL 171
Cdd:PRK10789 408 NiaLGRPDATQQEIEHVARLASvHDDILR------------LPQGYDTEVGErgvmLSGGQKQRISIARALLLNAEILIL 475
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 732682709 172 DEPTTGVDPLSRSQfwdLIDSIRQRQSNMSVLVATAYMEEAERFDWLVAMNAGEVLATGSAEELRQQT 239
Cdd:PRK10789 476 DDALSAVDGRTEHQ---ILHNLRQWGEGRTVIISAHRLSALTEASEILVMQHGHIAQRGNHDQLAQQS 540
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
26-231 |
7.11e-05 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 45.59 E-value: 7.11e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 26 VALNNITLDIPARCMVGLIGPDGVGKSSLLSLISG----------ARVieQGNVMVLGGDMRDPKHRRDVCPRiAWMPQG 95
Cdd:PRK13547 15 AILRDLSLRIEPGRVTALLGRNGAGKSTLLKALAGdltgggaprgARV--TGDVTLNGEPLAAIDAPRLARLR-AVLPQA 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 96 LGKNLyhTLSVYENVDF----FARLFGH-DKAEREVrINELLTSTGLAPFRDRPAGKLSGGMKQKLGLCCAL-------- 162
Cdd:PRK13547 92 AQPAF--AFSAREIVLLgrypHARRAGAlTHRDGEI-AWQALALAGATALVGRDVTTLSGGELARVQFARVLaqlwpphd 168
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 732682709 163 -IHDPELLILDEPTTGVDPLSRSQfwdLIDSIRQ--RQSNMSVLVATAYMEEAERFDWLVAMNA-GEVLATGS 231
Cdd:PRK13547 169 aAQPPRYLLLDEPTAALDLAHQHR---LLDTVRRlaRDWNLGVLAIVHDPNLAARHADRIAMLAdGAIVAHGA 238
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
11-179 |
8.05e-05 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 46.32 E-value: 8.05e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 11 PVAQLAGVSQHYGKTVALNNITLDIPARCMVGLIGPDGVGKSSLLSLISGARVIEQGNVMVLGGDMRD--PKH-----RR 83
Cdd:PRK10636 311 PLLKMEKVSAGYGDRIILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELAPVSGEIGLAKGIKLGyfAQHqleflRA 390
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 84 DVCP-----RIAwmPQGLGKNLYHTLSVYEnvdffarlFGHDKAErevrinelltstglapfrdRPAGKLSGGMKQKLGL 158
Cdd:PRK10636 391 DESPlqhlaRLA--PQELEQKLRDYLGGFG--------FQGDKVT-------------------EETRRFSGGEKARLVL 441
|
170 180
....*....|....*....|.
gi 732682709 159 CCALIHDPELLILDEPTTGVD 179
Cdd:PRK10636 442 ALIVWQRPNLLLLDEPTNHLD 462
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
41-179 |
1.27e-04 |
|
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: 44.71 E-value: 1.27e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 41 VGLIGPDGVGKSSLLSLISGARVIEQGNVMVLGGDmrdpkhrrdvcprIAWMPQglgknlYHTLSVYENVDFFARLFGHD 120
Cdd:cd03237 28 IGILGPNGIGKTTFIKMLAGVLKPDEGDIEIELDT-------------VSYKPQ------YIKADYEGTVRDLLSSITKD 88
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 732682709 121 KAEREVRINELLTSTGLAPFRDRPAGKLSGGMKQKLGLCCALIHDPELLILDEPTTGVD 179
Cdd:cd03237 89 FYTHPYFKTEIAKPLQIEQILDREVPELSGGELQRVAIAACLSKDADIYLLDEPSAYLD 147
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
143-317 |
1.53e-04 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 45.98 E-value: 1.53e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 143 RPAGKLSGGMKQKLGLCCALIH---DPELLILDEPTTGVDPLSRSQFWDLIDSIRQRqsNMSVLVATAYMEEAERFDWLV 219
Cdd:PRK00635 805 RPLSSLSGGEIQRLKLAYELLApskKPTLYVLDEPTTGLHTHDIKALIYVLQSLTHQ--GHTVVIIEHNMHVVKVADYVL 882
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 220 AMN------AGEVLATGSAEELRQ-QTQSATLEEAFInllpqaqrQAHQAVVIPPYQPENAEIaieARDLTMRFGSFVAV 292
Cdd:PRK00635 883 ELGpeggnlGGYLLASCSPEELIHlHTPTAKALRPYL--------SSPQELPYLPDPSPKPPV---PADITIKNAYQHNL 951
|
170 180
....*....|....*....|....*
gi 732682709 293 DHVNFRIPRGEIFGFLGSNGCGKST 317
Cdd:PRK00635 952 KHIDLSLPRNALTAVTGPSASGKHS 976
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
281-346 |
1.88e-04 |
|
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI's are not transport proteins, and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLI's have an N-terminal Fe-S domain and two nucleotide-binding domains, which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213189 [Multi-domain] Cd Length: 177 Bit Score: 43.33 E-value: 1.88e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 732682709 281 DLTMRFGSFvavdHVNFRIP---RGEIFGFLGSNGCGKSTTMKMLTG-LLPASEGEAWLFGQPV-DPKDID 346
Cdd:cd03222 5 DCVKRYGVF----FLLVELGvvkEGEVIGIVGPNGTGKTTAVKILAGqLIPNGDNDEWDGITPVyKPQYID 71
|
|
| PRK13541 |
PRK13541 |
cytochrome c biogenesis protein CcmA; Provisional |
45-190 |
3.23e-04 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184128 [Multi-domain] Cd Length: 195 Bit Score: 42.94 E-value: 3.23e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 45 GPDGVGKSSLLSLISGARVIEQGNVMVLGGDMRD-PKhrrdvcPRIAWMPQGLGKNLyhTLSVYENVDFFARLFghDKAE 123
Cdd:PRK13541 33 GANGCGKSSLLRMIAGIMQPSSGNIYYKNCNINNiAK------PYCTYIGHNLGLKL--EMTVFENLKFWSEIY--NSAE 102
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 732682709 124 revRINELLTSTGLAPFRDRPAGKLSGGMKQKLGLCCALIHDPELLILDEPTTGVDPLSRSQFWDLI 190
Cdd:PRK13541 103 ---TLYAAIHYFKLHDLLDEKCYSLSSGMQKIVAIARLIACQSDLWLLDEVETNLSKENRDLLNNLI 166
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
28-190 |
4.32e-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: 41.76 E-value: 4.32e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 28 LNNITLDIPARCMVGLIGPDGVGKSSLLSLISG------ARVI--EQGNVMVLggdmrdpkhrrdvcPRIAWMPQGlgkn 99
Cdd:cd03223 17 LKDLSFEIKPGDRLLITGPSGTGKSSLFRALAGlwpwgsGRIGmpEGEDLLFL--------------PQRPYLPLG---- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 100 lyhTLsvyenvdffarlfghdkaeREVRInelltstglAPFRDRpagkLSGGMKQKLGLCCALIHDPELLILDEPTTGVD 179
Cdd:cd03223 79 ---TL-------------------REQLI---------YPWDDV----LSGGEQQRLAFARLLLHKPKFVFLDEATSALD 123
|
170
....*....|.
gi 732682709 180 PLSRSQFWDLI 190
Cdd:cd03223 124 EESEDRLYQLL 134
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
23-224 |
1.03e-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: 1.03e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 23 GKTVALNNITLDIPARCMVGLIGPDGVGKSSLLSLISGAR---VIEQGNVMVlGGDMRDPKHRRdvcpRIAWMPQglgkN 99
Cdd:TIGR00956 774 EKRVILNNVDGWVKPGTLTALMGASGAGKTTLLNVLAERVttgVITGGDRLV-NGRPLDSSFQR----SIGYVQQ----Q 844
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 100 LYH--TLSVYENVDFFARLFGHD---KAEREVRINELLTSTGLAPFRDRPAGKLSGGM----KQKLGLCCALIHDPELLI 170
Cdd:TIGR00956 845 DLHlpTSTVRESLRFSAYLRQPKsvsKSEKMEYVEEVIKLLEMESYADAVVGVPGEGLnveqRKRLTIGVELVAKPKLLL 924
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 732682709 171 -LDEPTTGVDplSRSQfWDLIDSIRQRQSNMSVLVATAYMEEA---ERFDWLVAMNAG 224
Cdd:TIGR00956 925 fLDEPTSGLD--SQTA-WSICKLMRKLADHGQAILCTIHQPSAilfEEFDRLLLLQKG 979
|
|
| YhgE |
COG1511 |
Uncharacterized membrane protein YhgE, phage infection protein (PIP) family [Function unknown]; ... |
548-648 |
1.34e-03 |
|
Uncharacterized membrane protein YhgE, phage infection protein (PIP) family [Function unknown];
Pssm-ID: 441120 Cd Length: 225 Bit Score: 41.08 E-value: 1.34e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 548 RREALELRRDPVrSTLALMGTVILMLIMG--YGISM-----DVENLRFAVLDRDQTVSSQAWTLN--------LSGSRYF 612
Cdd:COG1511 2 KRELKRLFKNKL-ALIALIALILVPLLYAglYLWAFwdpygNLDNLPVAVVNEDKGATVDGKTVNlgdelvdeLKDNDSF 80
|
90 100 110
....*....|....*....|....*....|....*.
gi 732682709 613 IEQppLTSYDELDRRMRAGDITVAIEIPPNFGRDIA 648
Cdd:COG1511 81 DWQ--FVSEEEAEKGLKDGKYYAVIVIPEDFSANLA 114
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
297-326 |
1.92e-03 |
|
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: 41.69 E-value: 1.92e-03
10 20 30
....*....|....*....|....*....|...
gi 732682709 297 FRIP---RGEIFGFLGSNGCGKSTTMKMLTGLL 326
Cdd:COG1245 91 YGLPvpkKGKVTGILGPNGIGKSTALKILSGEL 123
|
|
| PRK15369 |
PRK15369 |
two component system response regulator; |
158-250 |
2.03e-03 |
|
two component system response regulator;
Pssm-ID: 185267 [Multi-domain] Cd Length: 211 Bit Score: 40.45 E-value: 2.03e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 158 LCCALihDPELLILDEPTTGVDPLsrsqfwDLIDSIRQRQSNMSVLVATAYMEEAERFDWLVAMNAGEVLATGSAEELRQ 237
Cdd:PRK15369 44 ACRQL--EPDIVILDLGLPGMNGL------DVIPQLHQRWPAMNILVLTARQEEHMASRTLAAGALGYVLKKSPQQILLA 115
|
90
....*....|...
gi 732682709 238 QTQSATLEEAFIN 250
Cdd:PRK15369 116 AIQTVAVGKRYID 128
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
297-439 |
2.13e-03 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 41.72 E-value: 2.13e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 297 FRIP---RGEIFGFLGSNGCGKSTTMKMLTG-LLPAsegeawlFGQPVDPKDIDT--RRRVG-----YMSQafsLYN-EL 364
Cdd:PRK13409 91 YGLPipkEGKVTGILGPNGIGKTTAVKILSGeLIPN-------LGDYEEEPSWDEvlKRFRGtelqnYFKK---LYNgEI 160
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 365 TVR---QNLELHARLFHIPEAEIPARVaemSERFKLNDVEDILP---------ESLPLGIRQRLSLAVAVIHRPEMLILD 432
Cdd:PRK13409 161 KVVhkpQYVDLIPKVFKGKVRELLKKV---DERGKLDEVVERLGlenildrdiSELSGGELQRVAIAAALLRDADFYFFD 237
|
....*..
gi 732682709 433 EPTSGVD 439
Cdd:PRK13409 238 EPTSYLD 244
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
142-317 |
4.34e-03 |
|
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of proteins of which all members for which functions are known except the UvrA proteins are involved in the transport of material through membranes. UvrA orthologs are involved in the recognition of DNA damage as a step in nucleotide excision repair. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 273184 [Multi-domain] Cd Length: 925 Bit Score: 40.77 E-value: 4.34e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 142 DRPAGKLSGGMKQKLGLC----CALIHdpELLILDEPTTGVDPLSRSQfwdLIDSIRQ-RQSNMSVLVATAYMEEAERFD 216
Cdd:TIGR00630 483 SRAAGTLSGGEAQRIRLAtqigSGLTG--VLYVLDEPSIGLHQRDNRR---LINTLKRlRDLGNTLIVVEHDEDTIRAAD 557
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 217 WLVAM------NAGEVLATGSAEELRQQTQSATLEeafinLLPQAQRQAHQAVVIPPyqpenaeiaiEARDLTMRFGSFV 290
Cdd:TIGR00630 558 YVIDIgpgageHGGEVVASGTPEEILANPDSLTGQ-----YLSGRKKIEVPAERRPG----------NGKFLTLKGAREN 622
|
170 180
....*....|....*....|....*..
gi 732682709 291 AVDHVNFRIPRGEIFGFLGSNGCGKST 317
Cdd:TIGR00630 623 NLKNITVSIPLGLFTCITGVSGSGKST 649
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
402-531 |
5.20e-03 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 40.97 E-value: 5.20e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 402 DILPESLPL-----GIRQRLSLA---VAVIHRPEMLILDEPTSGVDPVARDMFWQLMVDLSRQDKvTIFISTHFMNEAER 473
Cdd:PRK00635 799 DYLPLGRPLsslsgGEIQRLKLAyelLAPSKKPTLYVLDEPTTGLHTHDIKALIYVLQSLTHQGH-TVVIIEHNMHVVKV 877
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 732682709 474 CDRISLM------HAGKVLASGTPQELVEKRGAASLE-EAFIAYLQEAAGQSNEAEAPPVVHDTT 531
Cdd:PRK00635 878 ADYVLELgpeggnLGGYLLASCSPEELIHLHTPTAKAlRPYLSSPQELPYLPDPSPKPPVPADIT 942
|
|
| ABC_Rad50 |
cd03240 |
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ... |
43-206 |
5.44e-03 |
|
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ATP-binding cassette of ABC transporters, but are not associated with membrane-spanning domains. The conserved ATP-binding motifs common to Rad50 and the ABC transporter family include the Walker A and Walker B motifs, the Q loop, a histidine residue in the switch region, a D-loop, and a conserved LSGG sequence. This conserved sequence, LSGG, is the most specific and characteristic motif of this family and is thus known as the ABC signature sequence.
Pssm-ID: 213207 [Multi-domain] Cd Length: 204 Bit Score: 39.13 E-value: 5.44e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 43 LIGPDGVGKSSLLSLISgarvieqgnvMVLGGDM----RDPKHRRDVC---PRIA------WMPQGLGKNLYHTLSVYEN 109
Cdd:cd03240 27 IVGQNGAGKTTIIEALK----------YALTGELppnsKGGAHDPKLIregEVRAqvklafENANGKKYTITRSLAILEN 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 110 VDFFarlfghdkaeREVRINELLTstglapfrdRPAGKLSGGMKQKLGLC--CAL----IHDPELLILDEPTTGVDPLSR 183
Cdd:cd03240 97 VIFC----------HQGESNWPLL---------DMRGRCSGGEKVLASLIirLALaetfGSNCGILALDEPTTNLDEENI 157
|
170 180
....*....|....*....|....
gi 732682709 184 S-QFWDLIDSiRQRQSNMSVLVAT 206
Cdd:cd03240 158 EeSLAEIIEE-RKSQKNFQLIVIT 180
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
301-466 |
9.06e-03 |
|
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a variety of cellular activities. This profile/alignment only detects a fraction of this vast family. The poorly conserved N-terminal helix is missing from the alignment.
Pssm-ID: 214640 [Multi-domain] Cd Length: 148 Bit Score: 37.74 E-value: 9.06e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 301 RGEIFGFLGSNGCGKSTTMKMLTGLLPASEGeawlfgqpvdpkdidtrrRVGYMSqafslyneltvrqnlelharlfhip 380
Cdd:smart00382 1 PGEVILIVGPPGSGKTTLARALARELGPPGG------------------GVIYID------------------------- 37
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732682709 381 eaeiPARVAEMSERFKLNDVEDILPESLPLGIRQRLSLAVAVIHRPEMLILDEPTSGVDPVARDM-----FWQLMVDLSR 455
Cdd:smart00382 38 ----GEDILEEVLDQLLLIIVGGKKASGSGELRLRLALALARKLKPDVLILDEITSLLDAEQEALlllleELRLLLLLKS 113
|
170
....*....|.
gi 732682709 456 QDKVTIFISTH 466
Cdd:smart00382 114 EKNLTVILTTN 124
|
|
| |
