|
Name |
Accession |
Description |
Interval |
E-value |
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
12-912 |
0e+00 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 1945.30 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 12 VAQLEGVSQHYGKTVALNNITLDIPARSMVGLIGPDGVGKSSLLSLISGARVIEQGNVIVLGGDMRDAKHRRDVCPRIAW 91
Cdd:NF033858 1 VARLEGVSHRYGKTVALDDVSLDIPAGCMVGLIGPDGVGKSSLLSLIAGARKIQQGRVEVLGGDMADARHRRAVCPRIAY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 92 MPQGLGKNLYHTLSVYENVDFFARLFGHDKAEREARITELLNSTGLAPFRDRPAGKLSGGMKQKLGLCCALIHDPELLIL 171
Cdd:NF033858 81 MPQGLGKNLYPTLSVFENLDFFGRLFGQDAAERRRRIDELLRATGLAPFADRPAGKLSGGMKQKLGLCCALIHDPDLLIL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 172 DEPTTGVDPLSRAQFWDLIDSIRQRQTNMSVLVATAYMEEAERFDWLVAMNAGEILATGSAQQLRAKTHSATLEQAFIAL 251
Cdd:NF033858 161 DEPTTGVDPLSRRQFWELIDRIRAERPGMSVLVATAYMEEAERFDWLVAMDAGRVLATGTPAELLARTGADTLEAAFIAL 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 252 LPEAQRQAHKPVVIPPYHA-EQEEIAIEAKDLTMRFGKFVAVDHVNFRIPRGEIFGFLGSNGCGKSTTMKMLTGLLPASE 330
Cdd:NF033858 241 LPEEKRRGHQPVVIPPRPAdDDDEPAIEARGLTMRFGDFTAVDHVSFRIRRGEIFGFLGSNGCGKSTTMKMLTGLLPASE 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 331 GQAWLFGQPVDPNDIDTRRRVGYMSQAFSLYNELTVRQNLELHARLFHIPPAEIPARVAQMIERFMLTEVEDTLPASLPL 410
Cdd:NF033858 321 GEAWLFGQPVDAGDIATRRRVGYMSQAFSLYGELTVRQNLELHARLFHLPAAEIAARVAEMLERFDLADVADALPDSLPL 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 411 GIRQRLSLAVAVIHRPEMLILDEPTSGVDPVARDMFWQLMVDLSRQDKVTIFISTHFMNEAERCDRMSLMHAGKVLASGT 490
Cdd:NF033858 401 GIRQRLSLAVAVIHKPELLILDEPTSGVDPVARDMFWRLLIELSREDGVTIFISTHFMNEAERCDRISLMHAGRVLASDT 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 491 PQELVQQRGAANLEAAFISWLQEAAG-----AAPETPIPPSQTPAASGKPSRQGLSFRRLFSYSRREALELRRDPVRSTL 565
Cdd:NF033858 481 PAALVAARGAATLEEAFIAYLEEAAGaaaapAAAAAPAAAAAAPAAPAPAPRRRFSLRRLLAYARREALELLRDPIRLTF 560
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 566 ALLGTVILMLIMGYGISMDVENLRFAVLDRDQTVSSQAWSLNLAGSRYFIEQPPLASYDELDRRMRSGELAVAIEIPPNF 645
Cdd:NF033858 561 ALLGSVILMFVMGYGISLDVENLTFAVLDRDQTPESRAYLLNFAGSRYFIEQPPIADYAELDRRMRSGELSLAIEIPPGF 640
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 646 GRDIARGTPAQIGVWVDGAMPSRAETVKGYVQAMHQSWLQEAASRQPNPVkQVGLLNIETRYRYNPDVKSLPAIVPAVIP 725
Cdd:NF033858 641 GRDLLRGRPPEVGAWIDGAMPFRAETIRGYVQGMHQQWLADLARERGGAA-AASPATIETRYRYNPDFKSLPAMVPAVIP 719
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 726 LLLMMIPSMLSALSVVREKELGSMINLYVTPTTRSEFLLGKQLPYIALGMLNFLLLCALSVFVFGVPLKGSFLTLTLAAL 805
Cdd:NF033858 720 LLLMLIPAMLTALSVVREKELGSITNLYVTPVTRLEFLLGKQLPYVALAMLNFLLLVLLAVFVFGVPLKGSFLALALGAL 799
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 806 LYVIIATGLGLLISTFMKSQIAAIFGTSIITLIPATQFSGMIDPVASLEGPGRWIGEIYPTSHFLTIARGTFSKALDLSD 885
Cdd:NF033858 800 LYVTATTGLGLLISTFTRSQIAAIFGTAILTLIPAVQFSGLLDPVSSLEGAGRLIGRIFPATYFLTISRGTFTKGLGFAD 879
|
890 900
....*....|....*....|....*..
gi 446125071 886 LWPLFMPLLIAVPVVMGLSILLLKKQE 912
Cdd:NF033858 880 LWPSFLALAAFIPVLLGLSVLLLKKQE 906
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
277-515 |
2.47e-104 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 323.17 E-value: 2.47e-104
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 277 IEAKDLTMRFGKFVAVDHVNFRIPRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGQAWLFGQPVDPNDIDTRRRVGYMSQ 356
Cdd:COG1131 1 IEVRGLTKRYGDKTALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRVLGEDVARDPAEVRRRIGYVPQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 357 AFSLYNELTVRQNLELHARLFHIPPAEIPARVAQMIERFMLTEVEDTLPASLPLGIRQRLSLAVAVIHRPEMLILDEPTS 436
Cdd:COG1131 81 EPALYPDLTVRENLRFFARLYGLPRKEARERIDELLELFGLTDAADRKVGTLSGGMKQRLGLALALLHDPELLILDEPTS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 437 GVDPVARDMFWQLMVDLSRQDKvTIFISTHFMNEAER-CDRMSLMHAGKVLASGTPQELVQQRgaanLEAAFISWLQEAA 515
Cdd:COG1131 161 GLDPEARRELWELLRELAAEGK-TVLLSTHYLEEAERlCDRVAIIDKGRIVADGTPDELKARL----LEDVFLELTGEEA 235
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
11-494 |
3.46e-92 |
|
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: 301.05 E-value: 3.46e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 11 PVAQLEGVSQHY--GKTVALNNITLDIPARSMVGLIGPDGVGKSSLLSLISG-----ARVieQGNVIVLGGDMRDAKhRR 83
Cdd:COG1123 3 PLLEVRDLSVRYpgGDVPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGllphgGRI--SGEVLLDGRDLLELS-EA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 84 DVCPRIAWMPQGLGKNLyHTLSVYENVDFFARLFGHDKAEREARITELLNSTGLAPFRDRPAGKLSGGMKQKLGLCCALI 163
Cdd:COG1123 80 LRGRRIGMVFQDPMTQL-NPVTVGDQIAEALENLGLSRAEARARVLELLEAVGLERRLDRYPHQLSGGQRQRVAIAMALA 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 164 HDPELLILDEPTTGVDPLSRAQFWDLIDSIrQRQTNMSVLVATAYMEE-AERFDWLVAMNAGEILATGSAQQLRAktHSA 242
Cdd:COG1123 159 LDPDLLIADEPTTALDVTTQAEILDLLREL-QRERGTTVLLITHDLGVvAEIADRVVVMDDGRIVEDGPPEEILA--APQ 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 243 TLeqafiallpEAQRQAHKPVVIPPYHAEQEEIAIEAKDLTMRF-----GKFVAVDHVNFRIPRGEIFGFLGSNGCGKST 317
Cdd:COG1123 236 AL---------AAVPRLGAARGRAAPAAAAAEPLLEVRNLSKRYpvrgkGGVRAVDDVSLTLRRGETLGLVGESGSGKST 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 318 TMKMLTGLLPASEGQAWLFGQPVDPNDIDT----RRRVGYMSQ--AFSLYNELTVRQNLELHARLFHI-PPAEIPARVAQ 390
Cdd:COG1123 307 LARLLLGLLRPTSGSILFDGKDLTKLSRRSlrelRRRVQMVFQdpYSSLNPRMTVGDIIAEPLRLHGLlSRAERRERVAE 386
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 391 MIERFML-TEVEDTLPASLPLGIRQRLSLAVAVIHRPEMLILDEPTSGVDPVARDMFWQLMVDLSRQDKVT-IFIsTHFM 468
Cdd:COG1123 387 LLERVGLpPDLADRYPHELSGGQRQRVAIARALALEPKLLILDEPTSALDVSVQAQILNLLRDLQRELGLTyLFI-SHDL 465
|
490 500
....*....|....*....|....*..
gi 446125071 469 NEAER-CDRMSLMHAGKVLASGTPQEL 494
Cdd:COG1123 466 AVVRYiADRVAVMYDGRIVEDGPTEEV 492
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
14-257 |
2.32e-90 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 286.19 E-value: 2.32e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 14 QLEGVSQHYGKTVALNNITLDIPARSMVGLIGPDGVGKSSLLSLISGARVIEQGNVIVLGGDMRdaKHRRDVCPRIAWMP 93
Cdd:COG1131 2 EVRGLTKRYGDKTALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRVLGEDVA--RDPAEVRRRIGYVP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 94 QGLgkNLYHTLSVYENVDFFARLFGHDKAEREARITELLNSTGLAPFRDRPAGKLSGGMKQKLGLCCALIHDPELLILDE 173
Cdd:COG1131 80 QEP--ALYPDLTVRENLRFFARLYGLPRKEARERIDELLELFGLTDAADRKVGTLSGGMKQRLGLALALLHDPELLILDE 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 174 PTTGVDPLSRAQFWDLIDSIRQRqtNMSVLVATAYMEEAERF-DWLVAMNAGEILATGSAQQLRAKthsaTLEQAFIALL 252
Cdd:COG1131 158 PTSGLDPEARRELWELLRELAAE--GKTVLLSTHYLEEAERLcDRVAIIDKGRIVADGTPDELKAR----LLEDVFLELT 231
|
....*
gi 446125071 253 PEAQR 257
Cdd:COG1131 232 GEEAR 236
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
277-494 |
6.21e-76 |
|
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein component of a bacterial exporter complex that confers resistance to the antibiotics daunorubicin and doxorubicin. In addition to DrrA, the complex includes an integral membrane protein called DrrB. DrrA belongs to the ABC family of transporters and shares sequence and functional similarities with a protein found in cancer cells called P-glycoprotein. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region in addition to the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213232 [Multi-domain] Cd Length: 220 Bit Score: 247.28 E-value: 6.21e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 277 IEAKDLTMRFGKFVAVDHVNFRIPRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGQAWLFGQPVDPNDIDTRRRVGYMSQ 356
Cdd:cd03265 1 IEVENLVKKYGDFEAVRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATVAGHDVVREPREVRRRIGIVFQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 357 AFSLYNELTVRQNLELHARLFHIPPAEIPARVAQMIERFMLTEVEDTLPASLPLGIRQRLSLAVAVIHRPEMLILDEPTS 436
Cdd:cd03265 81 DLSVDDELTGWENLYIHARLYGVPGAERRERIDELLDFVGLLEAADRLVKTYSGGMRRRLEIARSLVHRPEVLFLDEPTI 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 446125071 437 GVDPVARDMFWQLMVDLSRQDKVTIFISTHFMNEAER-CDRMSLMHAGKVLASGTPQEL 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 |
1.19e-74 |
|
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: 241.92 E-value: 1.19e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 277 IEAKDLTMRFGKFVAVDHVNFRIPRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGQAWLFGQPVDPNDIDTRRRVGYMSQ 356
Cdd:cd03230 1 IEVRNLSKRYGKKTALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVLGKDIKKEPEEVKRRIGYLPE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 357 AFSLYNELTVRQNLElharlfhippaeiparvaqmierfmltevedtlpasLPLGIRQRLSLAVAVIHRPEMLILDEPTS 436
Cdd:cd03230 81 EPSLYENLTVRENLK------------------------------------LSGGMKQRLALAQALLHDPELLILDEPTS 124
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 446125071 437 GVDPVARDMFWQLMVDLSRQDKvTIFISTHFMNEAER-CDRMSLMHAGKV 485
Cdd:cd03230 125 GLDPESRREFWELLRELKKEGK-TILLSSHILEEAERlCDRVAILNNGRI 173
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
277-518 |
2.65e-74 |
|
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: 243.61 E-value: 2.65e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 277 IEAKDLTMRFGKFVAVDHVNFRIPRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGQAWLFGQPVDPNDIDTRRRVGYMSQ 356
Cdd:COG4555 2 IEVENLSKKYGKVPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIDGEDVRKEPREARRQIGVLPD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 357 AFSLYNELTVRQNLELHARLFHIPPAEIPARVAQMIERFMLTEVEDTLPASLPLGIRQRLSLAVAVIHRPEMLILDEPTS 436
Cdd:COG4555 82 ERGLYDRLTVRENIRYFAELYGLFDEELKKRIEELIELLGLEEFLDRRVGELSTGMKKKVALARALVHDPKVLLLDEPTN 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 437 GVDPVARDMFWQLMVDLSRQDKvTIFISTHFMNEAER-CDRMSLMHAGKVLASGTPQELVQQRGAANLEAAFISWLQEAA 515
Cdd:COG4555 162 GLDVMARRLLREILRALKKEGK-TVLFSSHIMQEVEAlCDRVVILHKGKVVAQGSLDELREEIGEENLEDAFVALIGSEE 240
|
...
gi 446125071 516 GAA 518
Cdd:COG4555 241 GEA 243
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
277-494 |
7.69e-72 |
|
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: 236.25 E-value: 7.69e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 277 IEAKDLTMRFGK--FVAVDHVNFRIPRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGQAWLFGQPVDPNDIDTRRRVGYM 354
Cdd:cd03263 1 LQIRNLTKTYKKgtKPAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYINGYSIRTDRKAARQSLGYC 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 355 SQAFSLYNELTVRQNLELHARLFHIPPAEIPARVAQMIERFMLTEVEDTLPASLPLGIRQRLSLAVAVIHRPEMLILDEP 434
Cdd:cd03263 81 PQFDALFDELTVREHLRFYARLKGLPKSEIKEEVELLLRVLGLTDKANKRARTLSGGMKRKLSLAIALIGGPSVLLLDEP 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446125071 435 TSGVDPVARDMFWQLMVDLsRQDKvTIFISTHFMNEAER-CDRMSLMHAGKVLASGTPQEL 494
Cdd:cd03263 161 TSGLDPASRRAIWDLILEV-RKGR-SIILTTHSMDEAEAlCDRIAIMSDGKLRCIGSPQEL 219
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
276-516 |
7.01e-71 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 236.54 E-value: 7.01e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 276 AIEAKDLTMRFGKFVAVDHVNFRIPRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGQAWLFGQPVDPndiDTRRRVGYMS 355
Cdd:COG4152 1 MLELKGLTKRFGDKTAVDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDSGEVLWDGEPLDP---EDRRRIGYLP 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 356 QAFSLYNELTVRQNLELHARLFHIPPAEIPARVAQMIERFMLTEVEDTLPASLPLGIRQRLSLAVAVIHRPEMLILDEPT 435
Cdd:COG4152 78 EERGLYPKMKVGEQLVYLARLKGLSKAEAKRRADEWLERLGLGDRANKKVEELSKGNQQKVQLIAALLHDPELLILDEPF 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 436 SGVDPVARDMFWQLMVDLSRQDKVTIFiSTHFMNEAER-CDRMSLMHAGKVLASGTPQELVQQRGAANLE---AAFISWL 511
Cdd:COG4152 158 SGLDPVNVELLKDVIRELAAKGTTVIF-SSHQMELVEElCDRIVIINKGRKVLSGSVDEIRRQFGRNTLRleaDGDAGWL 236
|
....*
gi 446125071 512 QEAAG 516
Cdd:COG4152 237 RALPG 241
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
14-226 |
1.14e-60 |
|
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: 203.78 E-value: 1.14e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 14 QLEGVSQHYGKTVALNNITLDIPARSMVGLIGPDGVGKSSLLSLISGARVIEQGNVIVLGGDMRdaKHRRDVCPRIAWMP 93
Cdd:cd03230 2 EVRNLSKRYGKKTALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVLGKDIK--KEPEEVKRRIGYLP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 94 QGLGknLYHTLSVYENVdffarlfghdkaerearitellnstglapfrdrpagKLSGGMKQKLGLCCALIHDPELLILDE 173
Cdd:cd03230 80 EEPS--LYENLTVRENL------------------------------------KLSGGMKQRLALAQALLHDPELLILDE 121
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 446125071 174 PTTGVDPLSRAQFWDLIDSIRQRqtNMSVLVATAYMEEAER-FDWLVAMNAGEI 226
Cdd:cd03230 122 PTSGLDPESRREFWELLRELKKE--GKTILLSSHILEEAERlCDRVAILNNGRI 173
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
14-256 |
1.76e-60 |
|
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, Inorganic ion transport and metabolism];
Pssm-ID: 443618 [Multi-domain] Cd Length: 243 Bit Score: 205.86 E-value: 1.76e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 14 QLEGVSQHYGKTVALNNITLDIPARSMVGLIGPDGVGKSSLLSLISGARVIEQGNVIVLGGDMR--DAKHRRdvcpRIAW 91
Cdd:COG4555 3 EVENLSKKYGKVPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIDGEDVRkePREARR----QIGV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 92 MPQGLGknLYHTLSVYENVDFFARLFGHDKAEREARITELLNSTGLAPFRDRPAGKLSGGMKQKLGLCCALIHDPELLIL 171
Cdd:COG4555 79 LPDERG--LYDRLTVRENIRYFAELYGLFDEELKKRIEELIELLGLEEFLDRRVGELSTGMKKKVALARALVHDPKVLLL 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 172 DEPTTGVDPLSRAQFWDLIdsIRQRQTNMSVLVATAYMEEAER-FDWLVAMNAGEILATGSAQQLRAKTHSATLEQAFIA 250
Cdd:COG4555 157 DEPTNGLDVMARRLLREIL--RALKKEGKTVLFSSHIMQEVEAlCDRVVILHKGKVVAQGSLDELREEIGEENLEDAFVA 234
|
....*.
gi 446125071 251 LLPEAQ 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 |
1.61e-58 |
|
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the subfamily A transporters involved in drug resistance, nodulation, lipid transport, and bacteriocin and lantibiotic immunity. In eubacteria and archaea, the typical organization consists of one ABC and one or two integral membranes. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region in addition to the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213236 [Multi-domain] Cd Length: 210 Bit Score: 199.04 E-value: 1.61e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 277 IEAKDLTMRFGKFVAVDHVNFRIPRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGQAWLFGQPVDpndIDTRRRVGYMSQ 356
Cdd:cd03269 1 LEVENVTKRFGRVTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDGKPLD---IAARNRIGYLPE 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 357 AFSLYNELTVRQNLELHARLFHIPPAEIPARVAQMIERFMLTEVEDTLPASLPLGIRQRLSLAVAVIHRPEMLILDEPTS 436
Cdd:cd03269 78 ERGLYPKMKVIDQLVYLAQLKGLKKEEARRRIDEWLERLELSEYANKRVEELSKGNQQKVQFIAAVIHDPELLILDEPFS 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 446125071 437 GVDPVARDMFWQLMVDLSRQDKvTIFISTHFMNEAER-CDRMSLMHAGKVLASG 489
Cdd:cd03269 158 GLDPVNVELLKDVIRELARAGK-TVILSTHQMELVEElCDRVLLLNKGRAVLYG 210
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
272-496 |
4.08e-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: 199.05 E-value: 4.08e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 272 QEEIAIEAKDLTMRFGKFVAVDHVNFRIPRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGQAWLFGQPVDPNDIDT---- 347
Cdd:COG1127 1 MSEPMIEVRNLTKSFGDRVVLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEILVDGQDITGLSEKElyel 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 348 RRRVGYMSQAFSLYNELTVRQNLEL----HARLfhiPPAEIPARVAQMIERFMLTEVEDTLPASLPLGIRQRLSLAVAVI 423
Cdd:COG1127 81 RRRIGMLFQGGALFDSLTVFENVAFplreHTDL---SEAEIRELVLEKLELVGLPGAADKMPSELSGGMRKRVALARALA 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446125071 424 HRPEMLILDEPTSGVDPVARDMFWQLMVDLSRQDKVTIFISTHFMNEAER-CDRMSLMHAGKVLASGTPQELVQ 496
Cdd:COG1127 158 LDPEILLYDEPTAGLDPITSAVIDELIRELRDELGLTSVVVTHDLDSAFAiADRVAVLADGKIIAEGTPEELLA 231
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
277-498 |
3.09e-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: 190.62 E-value: 3.09e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 277 IEAKDLTMRF-GKFVAVDHVNFRIPRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGQAWLFGQPVDPNDI-DTRRRVGYM 354
Cdd:COG1122 1 IELENLSFSYpGGTPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVDGKDITKKNLrELRRKVGLV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 355 -----SQAFslynELTVRQNLELHARLFHIPPAEIPARVAQMIERFMLTEVEDTLPASLPLGIRQRLSLAVAVIHRPEML 429
Cdd:COG1122 81 fqnpdDQLF----APTVEEDVAFGPENLGLPREEIRERVEEALELVGLEHLADRPPHELSGGQKQRVAIAGVLAMEPEVL 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 430 ILDEPTSGVDPVARDMFWQLMVDLSRQDKvTIFISTHFMNEAER-CDRMSLMHAGKVLASGTPQELVQQR 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 |
1.48e-54 |
|
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: 188.19 E-value: 1.48e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 277 IEAKDLTMRFGKFVAVDHVNFRIPRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGQAWLFGQPVDpNDIDTRRRVGYMSQ 356
Cdd:cd03268 1 LKTNDLTKTYGKKRVLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEITFDGKSYQ-KNIEALRRIGALIE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 357 AFSLYNELTVRQNLELHARLFHIPpaeiPARVAQMIERFMLTEVEDTLPASLPLGIRQRLSLAVAVIHRPEMLILDEPTS 436
Cdd:cd03268 80 APGFYPNLTARENLRLLARLLGIR----KKRIDEVLDVVGLKDSAKKKVKGFSLGMKQRLGIALALLGNPDLLILDEPTN 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 446125071 437 GVDPVARDMFWQLMVDLSRQDKvTIFISTHFMNEAER-CDRMSLMHAGKVLASG 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 |
1.52e-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: 188.48 E-value: 1.52e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 14 QLEGVSQHYGK--TVALNNITLDIPARSMVGLIGPDGVGKSSLLSLISGARVIEQGNVIVLGGDMRdaKHRRDVCPRIAW 91
Cdd:cd03263 2 QIRNLTKTYKKgtKPAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYINGYSIR--TDRKAARQSLGY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 92 MPQGlgKNLYHTLSVYENVDFFARLFGHDKAEREARITELLNSTGLAPFRDRPAGKLSGGMKQKLGLCCALIHDPELLIL 171
Cdd:cd03263 80 CPQF--DALFDELTVREHLRFYARLKGLPKSEIKEEVELLLRVLGLTDKANKRARTLSGGMKRKLSLAIALIGGPSVLLL 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446125071 172 DEPTTGVDPLSRAQFWDLIDSIRQrqtNMSVLVATAYMEEAERF-DWLVAMNAGEILATGSAQQLR 236
Cdd:cd03263 158 DEPTSGLDPASRRAIWDLILEVRK---GRSIILTTHSMDEAEALcDRIAIMSDGKLRCIGSPQELK 220
|
|
| drrA |
TIGR01188 |
daunorubicin resistance ABC transporter ATP-binding subunit; This model describes daunorubicin ... |
20-275 |
9.73e-54 |
|
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: 189.14 E-value: 9.73e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 20 QHYGKTVALNNITLDIPARSMVGLIGPDGVGKSSLLSLISGARVIEQGNVIVLGGDMrdAKHRRDVCPRIAWMPQGlgKN 99
Cdd:TIGR01188 1 KVYGDFKAVDGVNFKVREGEVFGFLGPNGAGKTTTIRMLTTLLRPTSGTARVAGYDV--VREPRKVRRSIGIVPQY--AS 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 100 LYHTLSVYENVDFFARLFGHDKAEREARITELLNSTGLAPFRDRPAGKLSGGMKQKLGLCCALIHDPELLILDEPTTGVD 179
Cdd:TIGR01188 77 VDEDLTGRENLEMMGRLYGLPKDEAEERAEELLELFELGEAADRPVGTYSGGMRRRLDIAASLIHQPDVLFLDEPTTGLD 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 180 PLSRAQFWDLIDSIrqRQTNMSVLVATAYMEEAERF-DWLVAMNAGEILATGSAQQLRAKTHSATLEQAFIALLPEAQRQ 258
Cdd:TIGR01188 157 PRTRRAIWDYIRAL--KEEGVTILLTTHYMEEADKLcDRIAIIDHGRIIAEGTPEELKRRLGKDTLESRPRDIQSLKVEV 234
|
250
....*....|....*..
gi 446125071 259 AHKPVVIPPYHAEQEEI 275
Cdd:TIGR01188 235 SMLIAELGETGLGLLAV 251
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
277-496 |
6.05e-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: 184.63 E-value: 6.05e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 277 IEAKDLTMRFGKFVAVDHVNFRIPRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGQAWLFGQPVDPN----DIDTRRRVG 352
Cdd:cd03261 1 IELRGLTKSFGGRTVLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGEDISGLseaeLYRLRRRMG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 353 YMSQAFSLYNELTVRQNLEL----HARLfhiPPAEIPARVAQMIERFMLTEVEDTLPASLPLGIRQRLSLAVAVIHRPEM 428
Cdd:cd03261 81 MLFQSGALFDSLTVFENVAFplreHTRL---SEEEIREIVLEKLEAVGLRGAEDLYPAELSGGMKKRVALARALALDPEL 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446125071 429 LILDEPTSGVDPVARDMFWQLMVDLSRQDKVTIFISTHFMNEAER-CDRMSLMHAGKVLASGTPQELVQ 496
Cdd:cd03261 158 LLYDEPTAGLDPIASGVIDDLIRSLKKELGLTSIMVTHDLDTAFAiADRIAVLYDGKIVAEGTPEELRA 226
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
277-489 |
7.00e-53 |
|
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: 183.55 E-value: 7.00e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 277 IEAKDLTMRFGKFVAVDHVNFRIPRGeIFGFLGSNGCGKSTTMKMLTGLLPASEGQAWLFGQPVDPNDIDTRRRVGYMSQ 356
Cdd:cd03264 1 LQLENLTKRYGKKRALDGVSLTLGPG-MYGLLGPNGAGKTTLMRILATLTPPSSGTIRIDGQDVLKQPQKLRRRIGYLPQ 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 357 AFSLYNELTVRQNLELHARLFHIPPAEIPARVAQMIERFMLTEVEDTLPASLPLGIRQRLSLAVAVIHRPEMLILDEPTS 436
Cdd:cd03264 80 EFGVYPNFTVREFLDYIAWLKGIPSKEVKARVDEVLELVNLGDRAKKKIGSLSGGMRRRVGIAQALVGDPSILIVDEPTA 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 446125071 437 GVDPVARDMFWQLMVDLSrQDKVTIfISTHFMNEAER-CDRMSLMHAGKVLASG 489
Cdd:cd03264 160 GLDPEERIRFRNLLSELG-EDRIVI-LSTHIVEDVESlCNQVAVLNKGKLVFEG 211
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
277-489 |
1.82e-52 |
|
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a bacterial ABC-type Na+ transport system called NatAB, which catalyzes ATP-dependent electrogenic Na+ extrusion without mechanically coupled proton or K+ uptake. NatB possess six putative membrane spanning regions at its C-terminus. In B. subtilis, NatAB is inducible by agents such as ethanol and protonophores, which lower the proton-motive force across the membrane. The closest sequence similarity to NatA is exhibited by DrrA of the two-component daunorubicin- and doxorubicin-efflux system. Hence, the functional NatAB is presumably assembled with two copies of a single ATP-binding protein and a single integral membrane protein.
Pssm-ID: 213233 [Multi-domain] Cd Length: 218 Bit Score: 182.57 E-value: 1.82e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 277 IEAKDLTMRFGK----FVAVDHVNFRIPRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGQAWLFGQPVDPNDIDTRRRVG 352
Cdd:cd03266 2 ITADALTKRFRDvkktVQAVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDGFDVVKEPAEARRRLG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 353 YMSQAFSLYNELTVRQNLELHARLFHIPPAEIPARVAQMIERFMLTEVEDTLPASLPLGIRQRLSLAVAVIHRPEMLILD 432
Cdd:cd03266 82 FVSDSTGLYDRLTARENLEYFAGLYGLKGDELTARLEELADRLGMEELLDRRVGGFSTGMRQKVAIARALVHDPPVLLLD 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 446125071 433 EPTSGVDPVARDMFWQLMVDLSRQDKVTIFiSTHFMNEAER-CDRMSLMHAGKVLASG 489
Cdd:cd03266 162 EPTTGLDVMATRALREFIRQLRALGKCILF-STHIMQEVERlCDRVVVLHRGRVVYEG 218
|
|
| PQQ_ABC_ATP |
TIGR03864 |
ABC transporter, ATP-binding subunit, PQQ-dependent alcohol dehydrogenase system; Members of ... |
276-509 |
2.11e-52 |
|
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: 183.26 E-value: 2.11e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 276 AIEAKDLTMRFGKFVAVDHVNFRIPRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGQAWLFGQPVDPNDIDTRRRVGYMS 355
Cdd:TIGR03864 1 ALEVAGLSFRYGARRALDDVSFTVRPGRFVALLGPNGAGKSTLFSLLTRLYVAQSGQISVAGHDLRRAPRAALARLGVVF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 356 QAFSLYNELTVRQNLELHARLFHIPPAEIPARVAQMIERFMLTEVEDTLPASLPLGIRQRLSLAVAVIHRPEMLILDEPT 435
Cdd:TIGR03864 81 QQPTLDLDLSVRQNLRYHAALHGLSRAEARARIAELLARLGLAERADDKVRELNGGHRRRVEIARALLHRPALLLLDEPT 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446125071 436 SGVDPVARDMFWQLMVDLSRQDKVTIFISTHFMNEAERCDRMSLMHAGKVLASGTPQELVQQRGAANLEAAFIS 509
Cdd:TIGR03864 161 VGLDPASRAAITAHVRALARDQGLSVLWATHLVDEIEASDRLVVLHRGRVLADGAAAELRGATGGADLEAAFLA 234
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
274-493 |
3.53e-52 |
|
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid transport and metabolism];
Pssm-ID: 440180 [Multi-domain] Cd Length: 257 Bit Score: 183.32 E-value: 3.53e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 274 EIAIEAKDLTMRFGKFVAVDHVNFRIPRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGQAWLFGQPVD---PNDIdTRRR 350
Cdd:COG0411 2 DPLLEVRGLTKRFGGLVAVDDVSLEVERGEIVGLIGPNGAGKTTLFNLITGFYRPTSGRILFDGRDITglpPHRI-ARLG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 351 VGYMSQAFSLYNELTVRQNLEL--HAR--------LFHIPP-----AEIPARVAQMIERFMLTEVEDTLPASLPLGIRQR 415
Cdd:COG0411 81 IARTFQNPRLFPELTVLENVLVaaHARlgrgllaaLLRLPRarreeREARERAEELLERVGLADRADEPAGNLSYGQQRR 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446125071 416 LSLAVAVIHRPEMLILDEPTSGVDPVARDMFWQLMVDLSRQDKVTIFISTHFMNEAER-CDRMSLMHAGKVLASGTPQE 493
Cdd:COG0411 161 LEIARALATEPKLLLLDEPAAGLNPEETEELAELIRRLRDERGITILLIEHDMDLVMGlADRIVVLDFGRVIAEGTPAE 239
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
14-236 |
9.52e-51 |
|
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: 177.95 E-value: 9.52e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 14 QLEGVSQHYGKTVALNNITLDIPARSMVGLIGPDGVGKSSLLSLISGARVIEQGNVIVLGGDMRdaKHRRDVCPRIAWMP 93
Cdd:cd03265 2 EVENLVKKYGDFEAVRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATVAGHDVV--REPREVRRRIGIVF 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 94 QGLgkNLYHTLSVYENVDFFARLFGHDKAEREARITELLNSTGLAPFRDRPAGKLSGGMKQKLGLCCALIHDPELLILDE 173
Cdd:cd03265 80 QDL--SVDDELTGWENLYIHARLYGVPGAERRERIDELLDFVGLLEAADRLVKTYSGGMRRRLEIARSLVHRPEVLFLDE 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446125071 174 PTTGVDPLSRAQFWDLIDSIrQRQTNMSVLVATAYMEEAERF-DWLVAMNAGEILATGSAQQLR 236
Cdd:cd03265 158 PTIGLDPQTRAHVWEYIEKL-KEEFGMTILLTTHYMEEAEQLcDRVAIIDHGRIIAEGTPEELK 220
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
236-497 |
3.24e-50 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 180.41 E-value: 3.24e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 236 RAKTHSATLEQAfiaLLPEAQRQAHKPVVIPPYHAEQEEIAIEAKDLTMRFGKFVAVDHVNFRIPRGEIFGFLGSNGCGK 315
Cdd:PRK13536 4 RAVAEEAPRRLE---LSPIERKHQGISEAKASIPGSMSTVAIDLAGVSKSYGDKAVVNGLSFTVASGECFGLLGPNGAGK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 316 STTMKMLTGLLPASEGQAWLFGQPVDPNDIDTRRRVGYMSQAFSLYNELTVRQNLELHARLFHIPPAEIPARVAQMIERF 395
Cdd:PRK13536 81 STIARMILGMTSPDAGKITVLGVPVPARARLARARIGVVPQFDNLDLEFTVRENLLVFGRYFGMSTREIEAVIPSLLEFA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 396 MLTEVEDTLPASLPLGIRQRLSLAVAVIHRPEMLILDEPTSGVDPVARDMFWQLMVDLSRQDKvTIFISTHFMNEAER-C 474
Cdd:PRK13536 161 RLESKADARVSDLSGGMKRRLTLARALINDPQLLILDEPTTGLDPHARHLIWERLRSLLARGK-TILLTTHFMEEAERlC 239
|
250 260
....*....|....*....|...
gi 446125071 475 DRMSLMHAGKVLASGTPQELVQQ 497
Cdd:PRK13536 240 DRLCVLEAGRKIAEGRPHALIDE 262
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
277-485 |
5.67e-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: 172.67 E-value: 5.67e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 277 IEAKDLTMRFG----KFVAVDHVNFRIPRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGQAWLFGQPV---DPNDIDT-- 347
Cdd:cd03255 1 IELKNLSKTYGgggeKVQALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRVDGTDIsklSEKELAAfr 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 348 RRRVGYMSQAFSLYNELTVRQNLELHARLFHIPPAEIPARVAQMIERFMLTEVEDTLPASLPLGIRQRLSLAVAVIHRPE 427
Cdd:cd03255 81 RRHIGFVFQSFNLLPDLTALENVELPLLLAGVPKKERRERAEELLERVGLGDRLNHYPSELSGGQQQRVAIARALANDPK 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 446125071 428 MLILDEPTSGVDPVARDMFWQLMVDLSRQDKVTIFISTHFMNEAERCDRMSLMHAGKV 485
Cdd:cd03255 161 IILADEPTGNLDSETGKEVMELLRELNKEAGTTIVVVTHDPELAEYADRIIELRDGKI 218
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
277-493 |
7.38e-49 |
|
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: 173.01 E-value: 7.38e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 277 IEAKDLTMRFGKFVAVDHVNFRIPRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGQAWLFGQPV---DPNDIdTRRRVGY 353
Cdd:cd03219 1 LEVRGLTKRFGGLVALDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFDGEDItglPPHEI-ARLGIGR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 354 MSQAFSLYNELTVRQNLELHARLFHIPP----------AEIPARVAQMIERFMLTEVEDTLPASLPLGIRQRLSLAVAVI 423
Cdd:cd03219 80 TFQIPRLFPELTVLENVMVAAQARTGSGlllararreeREARERAEELLERVGLADLADRPAGELSYGQQRRLEIARALA 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446125071 424 HRPEMLILDEPTSGVDPVARDMFWQLMVDLSRQDkVTIFISTHFMNEAER-CDRMSLMHAGKVLASGTPQE 493
Cdd:cd03219 160 TDPKLLLLDEPAAGLNPEETEELAELIRELRERG-ITVLLVEHDMDVVMSlADRVTVLDQGRVIAEGTPDE 229
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
276-496 |
2.28e-48 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 174.22 E-value: 2.28e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 276 AIEAKDLTMRFGKFVAVDHVNFRIPRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGQAWLFGQPVDPNDIDTRRRVGYMS 355
Cdd:PRK13537 7 PIDFRNVEKRYGDKLVVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCGEPVPSRARHARQRVGVVP 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 356 QAFSLYNELTVRQNLELHARLFHIPPAEIPARVAQMIERFMLTEVEDTLPASLPLGIRQRLSLAVAVIHRPEMLILDEPT 435
Cdd:PRK13537 87 QFDNLDPDFTVRENLLVFGRYFGLSAAAARALVPPLLEFAKLENKADAKVGELSGGMKRRLTLARALVNDPDVLVLDEPT 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446125071 436 SGVDPVARDMFWQLMVDLSRQDKvTIFISTHFMNEAER-CDRMSLMHAGKVLASGTPQELVQ 496
Cdd:PRK13537 167 TGLDPQARHLMWERLRSLLARGK-TILLTTHFMEEAERlCDRLCVIEEGRKIAEGAPHALIE 227
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
276-494 |
3.08e-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: 175.29 E-value: 3.08e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 276 AIEAKDLTMRFGKFVAVDHVNFRIPRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGQAWLFGQPVD---PNdidtRRRVG 352
Cdd:COG3842 5 ALELENVSKRYGDVTALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRILLDGRDVTglpPE----KRNVG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 353 YMSQAFSLYNELTVRQNLELHARLFHIPPAEIPARVAQMIERFMLTEVEDTLPASLPLGIRQRLSLAVAVIHRPEMLILD 432
Cdd:COG3842 81 MVFQDYALFPHLTVAENVAFGLRMRGVPKAEIRARVAELLELVGLEGLADRYPHQLSGGQQQRVALARALAPEPRVLLLD 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446125071 433 EPTSGVDPVARDMFWQLMVDLSRQDKVTIFISTHFMNEAER-CDRMSLMHAGKVLASGTPQEL 494
Cdd:COG3842 161 EPLSALDAKLREEMREELRRLQRELGITFIYVTHDQEEALAlADRIAVMNDGRIEQVGTPEEI 223
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
272-483 |
4.20e-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: 171.81 E-value: 4.20e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 272 QEEIAIEAKDLTMRF----GKFVAVDHVNFRIPRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGQAWLFGQPVDPndidT 347
Cdd:COG1116 3 AAAPALELRGVSKRFptggGGVTALDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPTSGEVLVDGKPVTG----P 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 348 RRRVGYMSQAFSLYNELTVRQNLELHARLFHIPPAEIPARVAQMIERFMLTEVEDTLPASLPLGIRQRLSLAVAVIHRPE 427
Cdd:COG1116 79 GPDRGVVFQEPALLPWLTVLDNVALGLELRGVPKAERRERARELLELVGLAGFEDAYPHQLSGGMRQRVAIARALANDPE 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 446125071 428 MLILDEPTSGVDPVARDMFWQLMVDLSRQDKVTIFISTHFMNEAER-CDRMSLMHAG 483
Cdd:COG1116 159 VLLMDEPFGALDALTRERLQDELLRLWQETGKTVLFVTHDVDEAVFlADRVVVLSAR 215
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
20-494 |
1.09e-47 |
|
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: 178.72 E-value: 1.09e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 20 QHYGKTVALNNITLDIPARSMVGLIGPDGVGKS----SLLSLISGARVIEQGNVIVLGGDMRDA--KHRRDVC-PRIAwM 92
Cdd:COG4172 18 QGGGTVEAVKGVSFDIAAGETLALVGESGSGKSvtalSILRLLPDPAAHPSGSILFDGQDLLGLseRELRRIRgNRIA-M 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 93 ----------P-QGLGKNLYHTLSVYEnvdffarlfGHDKAEREARITELLNSTGLapfrDRPAGK-------LSGGMKQ 154
Cdd:COG4172 97 ifqepmtslnPlHTIGKQIAEVLRLHR---------GLSGAAARARALELLERVGI----PDPERRldayphqLSGGQRQ 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 155 KLGLCCALIHDPELLILDEPTTGVDPLSRAQFWDLIDSIrQRQTNMSVLVATAYMEEAERF-DWLVAMNAGEILATGSAQ 233
Cdd:COG4172 164 RVMIAMALANEPDLLIADEPTTALDVTVQAQILDLLKDL-QRELGMALLLITHDLGVVRRFaDRVAVMRQGEIVEQGPTA 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 234 QL-RAKTHSATleqafIALLpeaqrqAHKPVVIPPYHAEQEEIAIEAKDLTMRF-----------GKFVAVDHVNFRIPR 301
Cdd:COG4172 243 ELfAAPQHPYT-----RKLL------AAEPRGDPRPVPPDAPPLLEARDLKVWFpikrglfrrtvGHVKAVDGVSLTLRR 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 302 GEIFGFLGSNGCGKSTTMKMLTGLLPaSEGQAWLFGQPVDPNDIDT----RRRVgymsQA-F-----SLYNELTVRQ--- 368
Cdd:COG4172 312 GETLGLVGESGSGKSTLGLALLRLIP-SEGEIRFDGQDLDGLSRRAlrplRRRM----QVvFqdpfgSLSPRMTVGQiia 386
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 369 -NLELHARlfHIPPAEIPARVAQmierfMLTEV---EDTL---PASLPLGIRQRLSLAVAVIHRPEMLILDEPTSgvdpv 441
Cdd:COG4172 387 eGLRVHGP--GLSAAERRARVAE-----ALEEVgldPAARhryPHEFSGGQRQRIAIARALILEPKLLVLDEPTS----- 454
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446125071 442 ARDMFWQ-----LMVDLSRQDKVT-IFIStH------FMneaerCDRMSLMHAGKVLASGTPQEL 494
Cdd:COG4172 455 ALDVSVQaqildLLRDLQREHGLAyLFIS-HdlavvrAL-----AHRVMVMKDGKVVEQGPTEQV 513
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
14-230 |
1.90e-47 |
|
ABC-type multidrug transport system, ATPase component; The biological function of this family is not well characterized, but display ABC domains similar to members of ABCA subfamily. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213231 [Multi-domain] Cd Length: 211 Bit Score: 168.14 E-value: 1.90e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 14 QLEGVSQHYGKTVALNNITLDIPArSMVGLIGPDGVGKSSLLSLISGARVIEQGNVIVLGGDMRdaKHRRDVCPRIAWMP 93
Cdd:cd03264 2 QLENLTKRYGKKRALDGVSLTLGP-GMYGLLGPNGAGKTTLMRILATLTPPSSGTIRIDGQDVL--KQPQKLRRRIGYLP 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 94 QGLGknLYHTLSVYENVDFFARLFGHDKAEREARITELLNSTGLAPFRDRPAGKLSGGMKQKLGLCCALIHDPELLILDE 173
Cdd:cd03264 79 QEFG--VYPNFTVREFLDYIAWLKGIPSKEVKARVDEVLELVNLGDRAKKKIGSLSGGMRRRVGIAQALVGDPSILIVDE 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 446125071 174 PTTGVDPLSRAQFWDLIDSIrqrQTNMSVLVATAYMEEAERF-DWLVAMNAGEILATG 230
Cdd:cd03264 157 PTAGLDPEERIRFRNLLSEL---GEDRIVILSTHIVEDVESLcNQVAVLNKGKLVFEG 211
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
14-235 |
2.05e-47 |
|
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: 168.66 E-value: 2.05e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 14 QLEGVSQHY-GKTVALNNITLDIPARSMVGLIGPDGVGKSSLLSLISGARVIEQGNVIVLGGDMRDaKHRRDVCPRIAWM 92
Cdd:COG1122 2 ELENLSFSYpGGTPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVDGKDITK-KNLRELRRKVGLV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 93 PQglgkN----LYHTlSVYENVDFFARLFGHDKAEREARITELLNSTGLAPFRDRPAGKLSGGMKQKLGLCCALIHDPEL 168
Cdd:COG1122 81 FQ----NpddqLFAP-TVEEDVAFGPENLGLPREEIRERVEEALELVGLEHLADRPPHELSGGQKQRVAIAGVLAMEPEV 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446125071 169 LILDEPTTGVDPLSRAQFWDLIDSIRQRqtNMSVLVATAYMEEAER-FDWLVAMNAGEILATGSAQQL 235
Cdd:COG1122 156 LVLDEPTAGLDPRGRRELLELLKRLNKE--GKTVIIVTHDLDLVAElADRVIVLDDGRIVADGTPREV 221
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
277-489 |
7.19e-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: 166.54 E-value: 7.19e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 277 IEAKDLTMRFGKFVAVDHVNFRIPRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGQAWLFGQPVDPNDIDtRRRVGYMSQ 356
Cdd:cd03259 1 LELKGLSKTYGSVRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDGRDVTGVPPE-RRNIGMVFQ 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 357 AFSLYNELTVRQNLELHARLFHIPPAEIPARVAQMIERFMLTEVEDTLPASLPLGIRQRLSLAVAVIHRPEMLILDEPTS 436
Cdd:cd03259 80 DYALFPHLTVAENIAFGLKLRGVPKAEIRARVRELLELVGLEGLLNRYPHELSGGQQQRVALARALAREPSLLLLDEPLS 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 446125071 437 GVDPVARDMFWQLMVDLSRQDKVTIFISTHFMNEAER-CDRMSLMHAGKVLASG 489
Cdd:cd03259 160 ALDAKLREELREELKELQRELGITTIYVTHDQEEALAlADRIAVMNEGRIVQVG 213
|
|
| YadH |
COG0842 |
ABC-type multidrug transport system, permease component [Defense mechanisms]; |
715-912 |
8.27e-47 |
|
ABC-type multidrug transport system, permease component [Defense mechanisms];
Pssm-ID: 440604 [Multi-domain] Cd Length: 200 Bit Score: 165.76 E-value: 8.27e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 715 SLPAIVPAVIPLLLMMIPSMLSALSVVREKELGSMINLYVTPTTRSEFLLGKQLPYIALGMLNFLLLCALSVFVFGVPLK 794
Cdd:COG0842 1 YLAFLVPGLLAMSLLFTALMLTALSIAREREQGTLERLLVTPVSRLEILLGKVLAYLLRGLLQALLVLLVALLFFGVPLR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 795 G-SFLTLTLAALLYVIIATGLGLLISTFMKSQIAAIFGTSIItLIPATQFSGMIDPVASLEGPGRWIGEIYPTSHFLTIA 873
Cdd:COG0842 81 GlSLLLLLLVLLLFALAFSGLGLLISTLARSQEQASAISNLV-ILPLTFLSGAFFPIESLPGWLQAIAYLNPLTYFVEAL 159
|
170 180 190
....*....|....*....|....*....|....*....
gi 446125071 874 RGTFSKALDLSDLWPLFMPLLIAVPVVMGLSILLLKKQE 912
Cdd:COG0842 160 RALFLGGAGLADVWPSLLVLLAFAVVLLALALRLFRRRL 198
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
278-484 |
1.22e-46 |
|
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: 165.72 E-value: 1.22e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 278 EAKDLTMRFGKF--VAVDHVNFRIPRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGQAWLFGQPVDPNDI-DTRRRVGYM 354
Cdd:cd03225 1 ELKNLSFSYPDGarPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDLTKLSLkELRRKVGLV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 355 -----SQAFslynELTVRQNLELHARLFHIPPAEIPARVAQMIERFMLTEVEDTLPASLPLGIRQRLSLAVAVIHRPEML 429
Cdd:cd03225 81 fqnpdDQFF----GPTVEEEVAFGLENLGLPEEEIEERVEEALELVGLEGLRDRSPFTLSGGQKQRVAIAGVLAMDPDIL 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 446125071 430 ILDEPTSGVDPVARDMFWQLMVDLSRQDKvTIFISTHFMNEAER-CDRMSLMHAGK 484
Cdd:cd03225 157 LLDEPTAGLDPAGRRELLELLKKLKAEGK-TIIIVTHDLDLLLElADRVIVLEDGK 211
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
10-485 |
2.21e-46 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 174.05 E-value: 2.21e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 10 PPVAQLEGVSQHYGKTVALNNITLDIPARSMVGLIGPDGVGKSSLLSLISGARVIEQGNVIVLG-----GDMRDAKHRRd 84
Cdd:COG1129 2 EPLLEMRGISKSFGGVKALDGVSLELRPGEVHALLGENGAGKSTLMKILSGVYQPDSGEILLDGepvrfRSPRDAQAAG- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 85 vcprIAWMPQGLgkNLYHTLSVYENVdFFARLFGH----DKAEREARITELLNSTGLA--PfrDRPAGKLSGGMKQKLGL 158
Cdd:COG1129 81 ----IAIIHQEL--NLVPNLSVAENI-FLGREPRRggliDWRAMRRRARELLARLGLDidP--DTPVGDLSVAQQQLVEI 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 159 CCALIHDPELLILDEPTTgvdPLSRAQFWDLIDSIRQ-RQTNMSVLVATAYMEEAERF-DWLVAMNAGEILATGSAQQL- 235
Cdd:COG1129 152 ARALSRDARVLILDEPTA---SLTEREVERLFRIIRRlKAQGVAIIYISHRLDEVFEIaDRVTVLRDGRLVGTGPVAELt 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 236 RAKTHSA----TLEQAFiallpeaqrqahkpvviPPYHAEQEEIAIEAKDLTMRfGKFvavDHVNFRIPRGEIFGFLGSN 311
Cdd:COG1129 229 EDELVRLmvgrELEDLF-----------------PKRAAAPGEVVLEVEGLSVG-GVV---RDVSFSVRAGEILGIAGLV 287
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 312 GCGKSTTMKMLTGLLPASEGQAWLFGQPVDPNDIDT--RRRVGYMS---QAFSLYNELTVRQN-----LELHARLFHIPP 381
Cdd:COG1129 288 GAGRTELARALFGADPADSGEIRLDGKPVRIRSPRDaiRAGIAYVPedrKGEGLVLDLSIRENitlasLDRLSRGGLLDR 367
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 382 AEIPARVAQMIERFmlteveDTLPASLPLGIR-------QRLSLAVAVIHRPEMLILDEPTSGVDPVARDMFWQLMVDLS 454
Cdd:COG1129 368 RRERALAEEYIKRL------RIKTPSPEQPVGnlsggnqQKVVLAKWLATDPKVLILDEPTRGIDVGAKAEIYRLIRELA 441
|
490 500 510
....*....|....*....|....*....|..
gi 446125071 455 RQDKVTIFISTHfMNEAER-CDRMSLMHAGKV 485
Cdd:COG1129 442 AEGKAVIVISSE-LPELLGlSDRILVMREGRI 472
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
274-487 |
4.08e-46 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 164.83 E-value: 4.08e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 274 EIAIEAKDLTMRFG----KFVAVDHVNFRIPRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGQAWLFGQPV---DPNDID 346
Cdd:COG1136 2 SPLLELRNLTKSYGtgegEVTALRGVSLSIEAGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVLIDGQDIsslSERELA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 347 T--RRRVGYMSQAFSLYNELTVRQNLELHARLFHIPPAEIPARVAQMIERFMLTEVEDTLPASLPLGIRQRLSLAVAVIH 424
Cdd:COG1136 82 RlrRRHIGFVFQFFNLLPELTALENVALPLLLAGVSRKERRERARELLERVGLGDRLDHRPSQLSGGQQQRVAIARALVN 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446125071 425 RPEMLILDEPTSGVDPVARDMFWQLMVDLSRQDKVTIFISTHFMNEAERCDRMSLMHAGKVLA 487
Cdd:COG1136 162 RPKLILADEPTGNLDSKTGEEVLELLRELNRELGTTIVMVTHDPELAARADRVIRLRDGRIVS 224
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
15-435 |
5.12e-46 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 173.33 E-value: 5.12e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 15 LEGVSQHYGKTVALNNITLDIPARSMVGLIGPDGVGKSSLLSLISGARVIEQGNVIVlggdmrdakhRRDVcpRIAWMPQ 94
Cdd:COG0488 1 LENLSKSFGGRPLLDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEVSI----------PKGL--RIGYLPQ 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 95 GLgkNLYHTLSVYENV-----------------------------------DFFARLFGHDkaeREARITELLNSTGLAP 139
Cdd:COG0488 69 EP--PLDDDLTVLDTVldgdaelraleaeleeleaklaepdedlerlaelqEEFEALGGWE---AEARAEEILSGLGFPE 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 140 F-RDRPAGKLSGGMKQKLGLCCALIHDPELLILDEPTTGVDplsraqfwdlIDSIRQ-----RQTNMSVL---------- 203
Cdd:COG0488 144 EdLDRPVSELSGGWRRRVALARALLSEPDLLLLDEPTNHLD----------LESIEWleeflKNYPGTVLvvshdryfld 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 204 -VAT------------------AYMEE-AERFDWLVAMNAgeilatgSAQQLRAKthsatlEQAFIA------------- 250
Cdd:COG0488 214 rVATrileldrgkltlypgnysAYLEQrAERLEQEAAAYA-------KQQKKIAK------EEEFIRrfrakarkakqaq 280
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 251 --------LLPEAQRQAHKPVVIppyHAEQEE----IAIEAKDLTMRFGKFVAVDHVNFRIPRGEIFGFLGSNGCGKSTT 318
Cdd:COG0488 281 srikalekLEREEPPRRDKTVEI---RFPPPErlgkKVLELEGLSKSYGDKTLLDDLSLRIDRGDRIGLIGPNGAGKSTL 357
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 319 MKMLTGLLPASEGQAWLfGQPVdpndidtrrRVGYMSQAF-SLYNELTVRQNLELHArlfhipPAEIPARVAQMIERFML 397
Cdd:COG0488 358 LKLLAGELEPDSGTVKL-GETV---------KIGYFDQHQeELDPDKTVLDELRDGA------PGGTEQEVRGYLGRFLF 421
|
490 500 510
....*....|....*....|....*....|....*....
gi 446125071 398 TEVE-DTLPASLPLGIRQRLSLAVAVIHRPEMLILDEPT 435
Cdd:COG0488 422 SGDDaFKPVGVLSGGEKARLALAKLLLSPPNVLLLDEPT 460
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
276-507 |
8.28e-46 |
|
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion transport and metabolism, Coenzyme transport and metabolism];
Pssm-ID: 440737 [Multi-domain] Cd Length: 254 Bit Score: 165.22 E-value: 8.28e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 276 AIEAKDLTMRFGKFVAVDHVNFRIPRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGQAWLFGQPVDpnDIDTR---RRVG 352
Cdd:COG1120 1 MLEAENLSVGYGGRPVLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDGRDLA--SLSRRelaRRIA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 353 YMSQAFSLYNELTVRQNLEL----HARLFHIPPAEIPARVAQMIERFMLTEVEDTLPASLPLGIRQRLSLAVAVIHRPEM 428
Cdd:COG1120 79 YVPQEPPAPFGLTVRELVALgrypHLGLFGRPSAEDREAVEEALERTGLEHLADRPVDELSGGERQRVLIARALAQEPPL 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 429 LILDEPTSGVDPVARDMFWQLMVDLSRQDKVTIFISTHFMNEAER-CDRMSLMHAGKVLASGTPQELVQqrgAANLEAAF 507
Cdd:COG1120 159 LLLDEPTSHLDLAHQLEVLELLRRLARERGRTVVMVLHDLNLAARyADRLVLLKDGRIVAQGPPEEVLT---PELLEEVY 235
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
277-487 |
9.61e-46 |
|
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: 163.80 E-value: 9.61e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 277 IEAKDLTMRFG----KFVAVDHVNFRIPRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGQAWLFGQPVDpndiDTRRRVG 352
Cdd:cd03293 1 LEVRNVSKTYGggggAVTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVDGEPVT----GPGPDRG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 353 YMSQAFSLYNELTVRQNLELHARLFHIPPAEIPARVAQMIERFMLTEVEDTLPASLPLGIRQRLSLAVAVIHRPEMLILD 432
Cdd:cd03293 77 YVFQQDALLPWLTVLDNVALGLELQGVPKAEARERAEELLELVGLSGFENAYPHQLSGGMRQRVALARALAVDPDVLLLD 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 446125071 433 EPTSGVDPVARDMFWQLMVDLSRQDKVTIFISTHFMNEAER-CDRMSLMHA--GKVLA 487
Cdd:cd03293 157 EPFSALDALTREQLQEELLDIWRETGKTVLLVTHDIDEAVFlADRVVVLSArpGRIVA 214
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
14-497 |
1.19e-45 |
|
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in methanogenesis, methyl coenzyme M reductase, contains alpha, beta, and gamma chains. In older literature, the complex of alpha, beta, and gamma chains was termed component C, while this single chain protein was termed methyl coenzyme M reductase system component A2. [Energy metabolism, Methanogenesis]
Pssm-ID: 132313 [Multi-domain] Cd Length: 520 Bit Score: 172.29 E-value: 1.19e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 14 QLEGVSQHYGKTVALNNITLDIPARSMVGLIGPDGVGKSSLLSLISGARVIE--QGNVI--------------------- 70
Cdd:TIGR03269 2 EVKNLTKKFDGKEVLKNISFTIEEGEVLGILGRSGAGKSVLMHVLRGMDQYEptSGRIIyhvalcekcgyverpskvgep 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 71 --VLGGDMR---------DAKHRRDVCPRIAWMPQGLGKnLYHTLSVYENVDFFARLFGHDKAEREARITELLNSTGLAP 139
Cdd:TIGR03269 82 cpVCGGTLEpeevdfwnlSDKLRRRIRKRIAIMLQRTFA-LYGDDTVLDNVLEALEEIGYEGKEAVGRAVDLIEMVQLSH 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 140 FRDRPAGKLSGGMKQKLGLCCALIHDPELLILDEPTTGVDPlsraQFWDLI-DSIRQ--RQTNMSVLVATAYMEEAERF- 215
Cdd:TIGR03269 161 RITHIARDLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDP----QTAKLVhNALEEavKASGISMVLTSHWPEVIEDLs 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 216 DWLVAMNAGEILATGSAQQLRAKthsatleqaFIALLPEAQRQAHkpvvippyhAEQEEIAIEAKDLTMRF-----GKFV 290
Cdd:TIGR03269 237 DKAIWLENGEIKEEGTPDEVVAV---------FMEGVSEVEKECE---------VEVGEPIIKVRNVSKRYisvdrGVVK 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 291 AVDHVNFRIPRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGQAW-LFGQP-VDPND--IDTRRRV----GYMSQAFSLYN 362
Cdd:TIGR03269 299 AVDNVSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGEVNvRVGDEwVDMTKpgPDGRGRAkryiGILHQEYDLYP 378
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 363 ELTVRQNLELHARLfhippaEIPARVAQMIERFMLT----------EVEDTLPASLPLGIRQRLSLAVAVIHRPEMLILD 432
Cdd:TIGR03269 379 HRTVLDNLTEAIGL------ELPDELARMKAVITLKmvgfdeekaeEILDKYPDELSEGERHRVALAQVLIKEPRIVILD 452
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446125071 433 EPTSGVDPVARDMFWQLMVDLSRQDKVTIFISTHFMNEA-ERCDRMSLMHAGKVLASGTPQELVQQ 497
Cdd:TIGR03269 453 EPTGTMDPITKVDVTHSILKAREEMEQTFIIVSHDMDFVlDVCDRAALMRDGKIVKIGDPEEIVEE 518
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
14-238 |
6.53e-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: 6.53e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 14 QLEGVSQHYGKTVALNNITLDIPARSMVGLIGPDGVGKSSLLSLISGarVIE--QGNVIVLGGDMrDAKHRRdvcpRIAW 91
Cdd:COG4152 3 ELKGLTKRFGDKTAVDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILG--ILApdSGEVLWDGEPL-DPEDRR----RIGY 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 92 MPQGLGknLYHTLSVYENVDFFARLFGHDKAEREARITELLNSTGLAPFRDRPAGKLSGGMKQKLGLCCALIHDPELLIL 171
Cdd:COG4152 76 LPEERG--LYPKMKVGEQLVYLARLKGLSKAEAKRRADEWLERLGLGDRANKKVEELSKGNQQKVQLIAALLHDPELLIL 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446125071 172 DEPTTGVDPLSRAQFWDLIdsIRQRQTNMSVLVATAYMEEAERF-DWLVAMNAGEILATGSAQQLRAK 238
Cdd:COG4152 154 DEPFSGLDPVNVELLKDVI--RELAAKGTTVIFSSHQMELVEELcDRIVIINKGRKVLSGSVDEIRRQ 219
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
274-507 |
3.92e-44 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 159.87 E-value: 3.92e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 274 EIAIEAKDLTMRFGKFVAVDHVNFRIPRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGQAWLFGQPVDpndiDTRRRVGY 353
Cdd:COG1121 4 MPAIELENLTVSYGGRPVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLFGKPPR----RARRRIGY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 354 MSQAFSLYNE--LTVRQ----NLELHARLFHIPPAEIPARVAQMIERFMLTEVEDTLPASLPLGIRQRLSLAVAVIHRPE 427
Cdd:COG1121 80 VPQRAEVDWDfpITVRDvvlmGRYGRRGLFRRPSRADREAVDEALERVGLEDLADRPIGELSGGQQQRVLLARALAQDPD 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 428 MLILDEPTSGVDPVARDMFWQLMVDLSRQDKvTIFISTHFMNEAER-CDRMSLMhAGKVLASGTPQELVQQrgaANLEAA 506
Cdd:COG1121 160 LLLLDEPFAGVDAATEEALYELLRELRREGK-TILVVTHDLGAVREyFDRVLLL-NRGLVAHGPPEEVLTP---ENLSRA 234
|
.
gi 446125071 507 F 507
Cdd:COG1121 235 Y 235
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
277-466 |
6.21e-44 |
|
ABC-type transport system involved in cytochrome c biogenesis, ATPase component [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 443308 [Multi-domain] Cd Length: 206 Bit Score: 158.03 E-value: 6.21e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 277 IEAKDLTMRFGKFVAVDHVNFRIPRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGQAWLFGQPVDPNDIDTRRRVGYMSQ 356
Cdd:COG4133 3 LEAENLSCRRGERLLFSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWNGEPIRDAREDYRRRLAYLGH 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 357 AFSLYNELTVRQNLELHARLFHIPPAEipARVAQMIERFMLTEVEDTLPASLPLGIRQRLSLAVAVIHRPEMLILDEPTS 436
Cdd:COG4133 83 ADGLKPELTVRENLRFWAALYGLRADR--EAIDEALEAVGLAGLADLPVRQLSAGQKRRVALARLLLSPAPLWLLDEPFT 160
|
170 180 190
....*....|....*....|....*....|
gi 446125071 437 GVDPVARDMFWQLMVDLsRQDKVTIFISTH 466
Cdd:COG4133 161 ALDAAGVALLAELIAAH-LARGGAVLLTTH 189
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
277-496 |
8.26e-44 |
|
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: 158.48 E-value: 8.26e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 277 IEAKDLTMRFGKFVAVDHVNFRIPRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGQAWLFGQPVDPNDIDTRRR--VGYM 354
Cdd:cd03218 1 LRAENLSKRYGKRKVVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDGQDITKLPMHKRARlgIGYL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 355 SQAFSLYNELTVRQNLELHARLFHIPPAEIPARVAQMIERFMLTEVEDTLPASLPLGIRQRLSLAVAVIHRPEMLILDEP 434
Cdd:cd03218 81 PQEASIFRKLTVEENILAVLEIRGLSKKEREEKLEELLEEFHITHLRKSKASSLSGGERRRVEIARALATNPKFLLLDEP 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446125071 435 TSGVDPVA-RDMfwQLMVDLSRQDKVTIFISTHFMNEA-ERCDRMSLMHAGKVLASGTPQELVQ 496
Cdd:cd03218 161 FAGVDPIAvQDI--QKIIKILKDRGIGVLITDHNVRETlSITDRAYIIYEGKVLAEGTPEEIAA 222
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
291-500 |
1.14e-43 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 161.41 E-value: 1.14e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 291 AVDHVNFRIPRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGQAWLFGqpVDP--NDIDTRRRVGY-MSQAFSLYNELTVR 367
Cdd:COG4586 37 AVDDISFTIEPGEIVGFIGPNGAGKSTTIKMLTGILVPTSGEVRVLG--YVPfkRRKEFARRIGVvFGQRSQLWWDLPAI 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 368 QNLELHARLFHIPPAEIPARVAQMIERFMLTEVEDTlPA-SLPLGIRQRLSLAVAVIHRPEMLILDEPTSGVDPVARDMF 446
Cdd:COG4586 115 DSFRLLKAIYRIPDAEYKKRLDELVELLDLGELLDT-PVrQLSLGQRMRCELAAALLHRPKILFLDEPTIGLDVVSKEAI 193
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 446125071 447 WQLMVDLSRQDKVTIFISTHFMNEAER-CDRMSLMHAGKVLASGTPQELVQQRGA 500
Cdd:COG4586 194 REFLKEYNRERGTTILLTSHDMDDIEAlCDRVIVIDHGRIIYDGSLEELKERFGP 248
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
14-225 |
5.17e-43 |
|
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ABC component of a cobalt transport family found in bacteria, archaea, and eukaryota. The transition metal cobalt is an essential component of many enzymes and must be transported into cells in appropriate amounts when needed. This ABC transport system of the CbiMNQO family is involved in cobalt transport in association with the cobalamin (vitamin B12) biosynthetic pathways. Most of cobalt (Cbi) transport systems possess a separate CbiN component, the cobalt-binding periplasmic protein, and they are encoded by the conserved gene cluster cbiMNQO. Both the CbiM and CbiQ proteins are integral cytoplasmic membrane proteins, and the CbiO protein has the linker peptide and the Walker A and B motifs commonly found in the ATPase components of the ABC-type transport systems.
Pssm-ID: 213192 [Multi-domain] Cd Length: 211 Bit Score: 155.70 E-value: 5.17e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 14 QLEGVSQHY--GKTVALNNITLDIPARSMVGLIGPDGVGKSSLLSLISGARVIEQGNVIVLGGDMRDaKHRRDVCPRIAW 91
Cdd:cd03225 1 ELKNLSFSYpdGARPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDLTK-LSLKELRRKVGL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 92 MPQglgkNLYH---TLSVYENVDFFARLFGHDKAEREARITELLNSTGLAPFRDRPAGKLSGGMKQKLGLCCALIHDPEL 168
Cdd:cd03225 80 VFQ----NPDDqffGPTVEEEVAFGLENLGLPEEEIEERVEEALELVGLEGLRDRSPFTLSGGQKQRVAIAGVLAMDPDI 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 446125071 169 LILDEPTTGVDPLSRAQFWDLIDSIRQRqtNMSVLVATAYMEEAERF-DWLVAMNAGE 225
Cdd:cd03225 156 LLLDEPTAGLDPAGRRELLELLKKLKAE--GKTIIIVTHDLDLLLELaDRVIVLEDGK 211
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
277-484 |
1.03e-42 |
|
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is comprised of all BPD (Binding Protein Dependent) systems that are largely represented in archaea and eubacteria and are primarily involved in scavenging solutes from the environment. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213196 [Multi-domain] Cd Length: 178 Bit Score: 153.50 E-value: 1.03e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 277 IEAKDLTMRFGKFVAVDHVNFRIPRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGQAWLFGQPVDPNDIDT---RRRVGY 353
Cdd:cd03229 1 LELKNVSKRYGQKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGEDLTDLEDELpplRRRIGM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 354 MSQAFSLYNELTVRQNLelharlfhippaeiparvaqmierfmltevedtlpaSLPL--GIRQRLSLAVAVIHRPEMLIL 431
Cdd:cd03229 81 VFQDFALFPHLTVLENI------------------------------------ALGLsgGQQQRVALARALAMDPDVLLL 124
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 446125071 432 DEPTSGVDPVARDMFWQLMVDLSRQDKVTIFISTHFMNEAER-CDRMSLMHAGK 484
Cdd:cd03229 125 DEPTSALDPITRREVRALLKSLQAQLGITVVLVTHDLDEAARlADRVVVLRDGK 178
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
10-248 |
2.31e-42 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 154.86 E-value: 2.31e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 10 PPVAQLEGVSQHYGKTVALNNITLDIPARSMVGLIGPDGVGKSSLLSLISGARVIEQGNVIVLGGDMRDAKHRrdvcprI 89
Cdd:COG1121 4 MPAIELENLTVSYGGRPVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLFGKPPRRARRR------I 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 90 AWMPQGLGKNLYHTLSVYENV----DFFARLFGHDKAEREARITELLNSTGLAPFRDRPAGKLSGGMKQKLGLCCALIHD 165
Cdd:COG1121 78 GYVPQRAEVDWDFPITVRDVVlmgrYGRRGLFRRPSRADREAVDEALERVGLEDLADRPIGELSGGQQQRVLLARALAQD 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 166 PELLILDEPTTGVDPLSRAQFWDLIDSIRQRqtNMSVLVATAYMEEAER-FDWLVAMNaGEILATGSAQQLRAkthSATL 244
Cdd:COG1121 158 PDLLLLDEPFAGVDAATEEALYELLRELRRE--GKTILVVTHDLGAVREyFDRVLLLN-RGLVAHGPPEEVLT---PENL 231
|
....
gi 446125071 245 EQAF 248
Cdd:COG1121 232 SRAY 235
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
277-496 |
2.80e-42 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 154.42 E-value: 2.80e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 277 IEAKDLTMRFGKFVAVDHVNFRIPRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGQAWLFGQPVDPNDIDTRRR--VGYM 354
Cdd:COG1137 4 LEAENLVKSYGKRTVVKDVSLEVNQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGRIFLDGEDITHLPMHKRARlgIGYL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 355 SQAFSLYNELTVRQNLELHARLFHIPPAEIPARVAQMIERFMLTEVEDTLPASLPLGIRQRLSLAVAVIHRPEMLILDEP 434
Cdd:COG1137 84 PQEASIFRKLTVEDNILAVLELRKLSKKEREERLEELLEEFGITHLRKSKAYSLSGGERRRVEIARALATNPKFILLDEP 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446125071 435 TSGVDPVA----RDMFWQLmvdlsRQDKVTIFISTHFMNEAER-CDRMSLMHAGKVLASGTPQELVQ 496
Cdd:COG1137 164 FAGVDPIAvadiQKIIRHL-----KERGIGVLITDHNVRETLGiCDRAYIISEGKVLAEGTPEEILN 225
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
14-230 |
3.22e-42 |
|
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: 153.21 E-value: 3.22e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 14 QLEGVSQHYGKTVALNNITLDIPARSMVGLIGPDGVGKSSLLSLISGARVIEQGNVIVLGGDMRDAKHRRdvcprIAWMP 93
Cdd:cd03269 2 EVENVTKRFGRVTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDGKPLDIAARNR-----IGYLP 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 94 QGLGknLYHTLSVYENVDFFARLFGHDKAEREARITELLNSTGLAPFRDRPAGKLSGGMKQKLGLCCALIHDPELLILDE 173
Cdd:cd03269 77 EERG--LYPKMKVIDQLVYLAQLKGLKKEEARRRIDEWLERLELSEYANKRVEELSKGNQQKVQFIAAVIHDPELLILDE 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 446125071 174 PTTGVDPLSRAQFWDLIDSIRQRQTnmSVLVATAYMEEAERF-DWLVAMNAGEILATG 230
Cdd:cd03269 155 PFSGLDPVNVELLKDVIRELARAGK--TVILSTHQMELVEELcDRVLLLNKGRAVLYG 210
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
277-497 |
3.85e-42 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 157.62 E-value: 3.85e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 277 IEAKDLTMRFGKFVAVDHVNFRIPRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGQAWLFGQPVDPNdIDTR-RRVGYMS 355
Cdd:COG1118 3 IEVRNISKRFGSFTLLDDVSLEIASGELVALLGPSGSGKTTLLRIIAGLETPDSGRIVLNGRDLFTN-LPPReRRVGFVF 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 356 QAFSLYNELTVRQNLELHARLFHIPPAEIPARVAQMIERFMLTEVEDTLPASLPLGIRQRLSLAVAVIHRPEMLILDEPT 435
Cdd:COG1118 82 QHYALFPHMTVAENIAFGLRVRPPSKAEIRARVEELLELVQLEGLADRYPSQLSGGQRQRVALARALAVEPEVLLLDEPF 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446125071 436 SGVDP-VARDMfWQLMVDLSRQDKVTIFISTHFMNEA-ERCDRMSLMHAGKVLASGTPQELVQQ 497
Cdd:COG1118 162 GALDAkVRKEL-RRWLRRLHDELGGTTVFVTHDQEEAlELADRVVVMNQGRIEQVGTPDEVYDR 224
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
290-489 |
7.80e-42 |
|
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: 153.26 E-value: 7.80e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 290 VAVDHVNFRIPRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGQAWLFGQPVDPNDIDTRRRVGY-MSQAFSLYNELTVRQ 368
Cdd:cd03267 35 EALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRVAGLVPWKRRKKFLRRIGVvFGQKTQLWWDLPVID 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 369 NLELHARLFHIPPAEIPARVAQMIERFMLTEVEDTLPASLPLGIRQRLSLAVAVIHRPEMLILDEPTSGVDPVARDMFWQ 448
Cdd:cd03267 115 SFYLLAAIYDLPPARFKKRLDELSELLDLEELLDTPVRQLSLGQRMRAEIAAALLHEPEILFLDEPTIGLDVVAQENIRN 194
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 446125071 449 LMVDLSRQDKVTIFISTHFMNEAER-CDRMSLMHAGKVLASG 489
Cdd:cd03267 195 FLKEYNRERGTTVLLTSHYMKDIEAlARRVLVIDKGRLLYDG 236
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
278-489 |
9.60e-42 |
|
ATP-binding cassette domain of the metal-type transporters; This family includes transporters involved in the uptake of various metallic cations such as iron, manganese, and zinc. The ATPases of this group of transporters are very similar to members of iron-siderophore uptake family suggesting that they share a common ancestor. The best characterized metal-type ABC transporters are the YfeABCD system of Y. pestis, the SitABCD system of Salmonella enterica serovar Typhimurium, and the SitABCD transporter of Shigella flexneri. Moreover other uncharacterized homologs of these metal-type transporters are mainly found in pathogens like Haemophilus or enteroinvasive E. coli isolates.
Pssm-ID: 213202 [Multi-domain] Cd Length: 213 Bit Score: 151.92 E-value: 9.60e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 278 EAKDLTMRFGKFVAVDHVNFRIPRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGQAWLFGQPVDpndiDTRRRVGYMSQA 357
Cdd:cd03235 1 EVEDLTVSYGGHPVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFGKPLE----KERKRIGYVPQR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 358 FSLYNE--LTVRQ----NLELHARLFHIPPAEIPARVAQMIERFMLTEVEDTLPASLPLGIRQRLSLAVAVIHRPEMLIL 431
Cdd:cd03235 77 RSIDRDfpISVRDvvlmGLYGHKGLFRRLSKADKAKVDEALERVGLSELADRQIGELSGGQQQRVLLARALVQDPDLLLL 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 446125071 432 DEPTSGVDPVARDMFWQLMVDLSRQDKvTIFISTHFMNEAER-CDRMSLMhAGKVLASG 489
Cdd:cd03235 157 DEPFAGVDPKTQEDIYELLRELRREGM-TILVVTHDLGLVLEyFDRVLLL-NRTVVASG 213
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
276-508 |
1.08e-41 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 156.39 E-value: 1.08e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 276 AIEAKDLTMRFGKFVAVDHVNFRIPRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGQAWLFGQPVdpNDIDTRRR-VGYM 354
Cdd:COG3839 3 SLELENVSKSYGGVEALKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAGLEDPTSGEILIGGRDV--TDLPPKDRnIAMV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 355 SQAFSLYNELTVRQNLELHARLFHIPPAEIPARVAQMIERFMLTEVEDTLPASLPLGIRQRLSLAVAVIHRPEMLILDEP 434
Cdd:COG3839 81 FQSYALYPHMTVYENIAFPLKLRKVPKAEIDRRVREAAELLGLEDLLDRKPKQLSGGQRQRVALGRALVREPKVFLLDEP 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446125071 435 TSGVDPVARdmfWQLMVDLS---RQDKVTIFISTHFMNEAER-CDRMSLMHAGKVLASGTPQELVQQrgAANLEAA-FI 508
Cdd:COG3839 161 LSNLDAKLR---VEMRAEIKrlhRRLGTTTIYVTHDQVEAMTlADRIAVMNDGRIQQVGTPEELYDR--PANLFVAgFI 234
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
277-494 |
1.38e-41 |
|
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: 152.45 E-value: 1.38e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 277 IEAKDLTMRFGK-FVAVDHVNFRIPRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGQAWLFGQPV---DPndIDTRRRVG 352
Cdd:cd03295 1 IEFENVTKRYGGgKKAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGEDIreqDP--VELRRKIG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 353 YMSQAFSLYNELTVRQNLELHARLFHIPPAEIPARVAQMIERFMLTEVE--DTLPASLPLGIRQRLSLAVAVIHRPEMLI 430
Cdd:cd03295 79 YVIQQIGLFPHMTVEENIALVPKLLKWPKEKIRERADELLALVGLDPAEfaDRYPHELSGGQQQRVGVARALAADPPLLL 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446125071 431 LDEPTSGVDPVARDMFWQLMVDLSRQDKVTIFISTHFMNEAER-CDRMSLMHAGKVLASGTPQEL 494
Cdd:cd03295 159 MDEPFGALDPITRDQLQEEFKRLQQELGKTIVFVTHDIDEAFRlADRIAIMKNGEIVQVGTPDEI 223
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
14-226 |
2.90e-41 |
|
ATP-binding cassette domain of the transporters involved in export of lipoprotein and macrolide, and Cell division ATP-binding protein FtsE; This family is comprised of MJ0796 ATP-binding cassette, macrolide-specific ABC-type efflux carrier (MacAB), and proteins involved in cell division (FtsE), and release of lipoproteins from the cytoplasmic membrane (LolCDE). They are clustered together phylogenetically. MacAB is an exporter that confers resistance to macrolides, while the LolCDE system is not a transporter at all. The FtsEX complex resembles an ABC transporter, where FtsE is the ATPase and the membrane subunit FtsX resembles a permease subunit. But rather than transporting any substrate, the complex acts in cell division by undergoing conformational changes that alter the activity of cell wall hydrolases located outside the plasma membrane. The complex is widely conserved in bacteria, but also extremely divergent in sequence between different lineages. The LolCDE complex catalyzes the release of lipoproteins from the cytoplasmic membrane prior to their targeting to the outer membrane.
Pssm-ID: 213222 [Multi-domain] Cd Length: 218 Bit Score: 150.72 E-value: 2.90e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 14 QLEGVSQHYG----KTVALNNITLDIPARSMVGLIGPDGVGKSSLLSLISGARVIEQGNVIVLGGDMRDAKH------RR 83
Cdd:cd03255 2 ELKNLSKTYGgggeKVQALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRVDGTDISKLSEkelaafRR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 84 DvcpRIAWMPQGLgkNLYHTLSVYENVDFFARLFGHDKAEREARITELLNSTGLAPFRDRPAGKLSGGMKQKLGLCCALI 163
Cdd:cd03255 82 R---HIGFVFQSF--NLLPDLTALENVELPLLLAGVPKKERRERAEELLERVGLGDRLNHYPSELSGGQQQRVAIARALA 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446125071 164 HDPELLILDEPTTGVDPLSRAQFWDLIDSIrQRQTNMSVLVATAYMEEAERFDWLVAMNAGEI 226
Cdd:cd03255 157 NDPKIILADEPTGNLDSETGKEVMELLREL-NKEAGTTIVVVTHDPELAEYADRIIELRDGKI 218
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
277-466 |
3.24e-41 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 150.97 E-value: 3.24e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 277 IEAKDLTMRF-GKFVAVDHVNFRIPRGEiFGFL-GSNGCGKSTTMKMLTGLLPASEGQAWLFGQPV---DPNDI-DTRRR 350
Cdd:COG2884 2 IRFENVSKRYpGGREALSDVSLEIEKGE-FVFLtGPSGAGKSTLLKLLYGEERPTSGQVLVNGQDLsrlKRREIpYLRRR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 351 VGYMSQAFSLYNELTVRQNLELHARLFHIPPAEIPARVAQMIERFMLTEVEDTLPASLPLGIRQRLSLAVAVIHRPEMLI 430
Cdd:COG2884 81 IGVVFQDFRLLPDRTVYENVALPLRVTGKSRKEIRRRVREVLDLVGLSDKAKALPHELSGGEQQRVAIARALVNRPELLL 160
|
170 180 190
....*....|....*....|....*....|....*.
gi 446125071 431 LDEPTSGVDPVARDMFWQLMVDLSRQdKVTIFISTH 466
Cdd:COG2884 161 ADEPTGNLDPETSWEIMELLEEINRR-GTTVLIATH 195
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
277-494 |
3.59e-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: 151.19 E-value: 3.59e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 277 IEAKDLTMRFG----KFVAVDHVNFRIPRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGQAWLFGQpvdpnDIDT----- 347
Cdd:cd03258 2 IELKNVSKVFGdtggKVTALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGSVLVDGT-----DLTLlsgke 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 348 ----RRRVGYMSQAFSLYNELTVRQNLELHARLFHIPPAEIPARVAQMIERFMLTEVEDTLPASLPLGIRQRLSLAVAVI 423
Cdd:cd03258 77 lrkaRRRIGMIFQHFNLLSSRTVFENVALPLEIAGVPKAEIEERVLELLELVGLEDKADAYPAQLSGGQKQRVGIARALA 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446125071 424 HRPEMLILDEPTSGVDPVARDMFWQLMVDLSRQDKVTIFISTHFMNEAER-CDRMSLMHAGKVLASGTPQEL 494
Cdd:cd03258 157 NNPKVLLCDEATSALDPETTQSILALLRDINRELGLTIVLITHEMEVVKRiCDRVAVMEKGEVVEEGTVEEV 228
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
14-206 |
8.62e-41 |
|
ABC-type transport system involved in cytochrome c biogenesis, ATPase component [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 443308 [Multi-domain] Cd Length: 206 Bit Score: 149.17 E-value: 8.62e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 14 QLEGVSQHYGKTVALNNITLDIPARSMVGLIGPDGVGKSSLLSLISGARVIEQGNVIVLGGDMRDAkhRRDVCPRIAWMP 93
Cdd:COG4133 4 EAENLSCRRGERLLFSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWNGEPIRDA--REDYRRRLAYLG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 94 QGLGknLYHTLSVYENVDFFARLFGHDKAEreARITELLNSTGLAPFRDRPAGKLSGGMKQKLGLCCALIHDPELLILDE 173
Cdd:COG4133 82 HADG--LKPELTVRENLRFWAALYGLRADR--EAIDEALEAVGLAGLADLPVRQLSAGQKRRVALARLLLSPAPLWLLDE 157
|
170 180 190
....*....|....*....|....*....|...
gi 446125071 174 PTTGVDPLSRAQFWDLIDsiRQRQTNMSVLVAT 206
Cdd:COG4133 158 PFTALDAAGVALLAELIA--AHLARGGAVLLTT 188
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
14-230 |
1.53e-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: 148.45 E-value: 1.53e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 14 QLEGVSQHYGKTVALNNITLDIPARSMVGLIGPDGVGKSSLLSLISGARVIEQGNVIVLGgdmrdaKHRRDVCPRIAWMP 93
Cdd:cd03235 1 EVEDLTVSYGGHPVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFG------KPLEKERKRIGYVP 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 94 QGLGKNLYHTLSVYENV----DFFARLFGHDKAEREARITELLNSTGLAPFRDRPAGKLSGGMKQKLGLCCALIHDPELL 169
Cdd:cd03235 75 QRRSIDRDFPISVRDVVlmglYGHKGLFRRLSKADKAKVDEALERVGLSELADRQIGELSGGQQQRVLLARALVQDPDLL 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446125071 170 ILDEPTTGVDPLSRAQFWDLIDSIRQRqtNMSVLVATAYMEEAER-FDWLVAMNaGEILATG 230
Cdd:cd03235 155 LLDEPFAGVDPKTQEDIYELLRELRRE--GMTILVVTHDLGLVLEyFDRVLLLN-RTVVASG 213
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
277-494 |
2.69e-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: 148.48 E-value: 2.69e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 277 IEAKDLTMRFGKFVAVDHVNFRIPRGEIFGFLGSNGCGKSTTMKMLTGLLPA-----SEGQAWLFGQPVDPNDIDT---R 348
Cdd:cd03260 1 IELRDLNVYYGDKHALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRLNDLipgapDEGEVLLDGKDIYDLDVDVlelR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 349 RRVGYMSQAFSLYNeLTVRQNLELHARLFHI-PPAEIPARVAQMIERFMLT-EVEDTLPA-SLPLGIRQRLSLAVAVIHR 425
Cdd:cd03260 81 RRVGMVFQKPNPFP-GSIYDNVAYGLRLHGIkLKEELDERVEEALRKAALWdEVKDRLHAlGLSGGQQQRLCLARALANE 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 426 PEMLILDEPTSGVDPVARDMFWQLMVDLSRQdkVTIFISTHFMNEAERC-DRMSLMHAGKVLASGTPQEL 494
Cdd:cd03260 160 PEVLLLDEPTSALDPISTAKIEELIAELKKE--YTIVIVTHNMQQAARVaDRTAFLLNGRLVEFGPTEQI 227
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
15-230 |
3.13e-40 |
|
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: 147.67 E-value: 3.13e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 15 LEGVSQHYGKTVALNNITLDIPARSMVGLIGPDGVGKSSLLSLISGARVIEQGNVIVLGGDMRD-AKHRRDvcprIAWMP 93
Cdd:cd03259 3 LKGLSKTYGSVRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDGRDVTGvPPERRN----IGMVF 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 94 QGLgkNLYHTLSVYENVDFFARLFGHDKAEREARITELLNSTGLAPFRDRPAGKLSGGMKQKLGLCCALIHDPELLILDE 173
Cdd:cd03259 79 QDY--ALFPHLTVAENIAFGLKLRGVPKAEIRARVRELLELVGLEGLLNRYPHELSGGQQQRVALARALAREPSLLLLDE 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 446125071 174 PTTGVDPLSRAQFWDLIDSIrQRQTNMSVLVATAYMEEAERF-DWLVAMNAGEILATG 230
Cdd:cd03259 157 PLSALDAKLREELREELKEL-QRELGITTIYVTHDQEEALALaDRIAVMNEGRIVQVG 213
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
10-240 |
4.20e-40 |
|
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: 148.20 E-value: 4.20e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 10 PPVAQLEGVSQHYGKTVALNNITLDIPARSMVGLIGPDGVGKSSLLSLISGARVIEQGNVIVLGGDMR--DAKHRRDVCP 87
Cdd:COG1127 3 EPMIEVRNLTKSFGDRVVLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEILVDGQDITglSEKELYELRR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 88 RIAWMPQGLGknLYHTLSVYENVDFFARLFGH-DKAEREARITELLNSTGLAPFRDRPAGKLSGGMKQKLGLCCALIHDP 166
Cdd:COG1127 83 RIGMLFQGGA--LFDSLTVFENVAFPLREHTDlSEAEIRELVLEKLELVGLPGAADKMPSELSGGMRKRVALARALALDP 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446125071 167 ELLILDEPTTGVDPLSRAQFWDLIDSIRqRQTNMSVLVATAYMEEAERF-DWLVAMNAGEILATGSAQQLRAKTH 240
Cdd:COG1127 161 EILLYDEPTAGLDPITSAVIDELIRELR-DELGLTSVVVTHDLDSAFAIaDRVAVLADGKIIAEGTPEELLASDD 234
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
273-493 |
4.80e-40 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 155.57 E-value: 4.80e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 273 EEIAIEAKDLTMRFGKFVAVDHVNFRIPRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGQAWLFGQPVDPND-IDTRRR- 350
Cdd:COG3845 2 MPPALELRGITKRFGGVVANDDVSLTVRPGEIHALLGENGAGKSTLMKILYGLYQPDSGEILIDGKPVRIRSpRDAIALg 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 351 VGYMSQAFSLYNELTVRQNLEL---HARLFHIPPAEIPARVAQMIERFMLtEVE-DTLPASLPLGIRQRLSLAVAVIHRP 426
Cdd:COG3845 82 IGMVHQHFMLVPNLTVAENIVLglePTKGGRLDRKAARARIRELSERYGL-DVDpDAKVEDLSVGEQQRVEILKALYRGA 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446125071 427 EMLILDEPTSGVDPVARDMFWQLMVDLSRQDKVTIFIsTHFMNEAER-CDRMSLMHAGKVLASGTPQE 493
Cdd:COG3845 161 RILILDEPTAVLTPQEADELFEILRRLAAEGKSIIFI-THKLREVMAiADRVTVLRRGKVVGTVDTAE 227
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
14-266 |
5.38e-40 |
|
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion transport and metabolism, Coenzyme transport and metabolism];
Pssm-ID: 440737 [Multi-domain] Cd Length: 254 Bit Score: 148.27 E-value: 5.38e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 14 QLEGVSQHYGKTVALNNITLDIPARSMVGLIGPDGVGKSSLLSLISGARVIEQGNVIVLGGDMRDAKhRRDVCPRIAWMP 93
Cdd:COG1120 3 EAENLSVGYGGRPVLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDGRDLASLS-RRELARRIAYVP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 94 QGLGKNLYhtLSVYENVDF----FARLFGHDKAEREARITELLNSTGLAPFRDRPAGKLSGGMKQKLGLCCALIHDPELL 169
Cdd:COG1120 82 QEPPAPFG--LTVRELVALgrypHLGLFGRPSAEDREAVEEALERTGLEHLADRPVDELSGGERQRVLIARALAQEPPLL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 170 ILDEPTTGVDPLSRAQFWDLIDSIRqRQTNMSVLVATAYMEEAERF-DWLVAMNAGEILATGSAQQLrakTHSATLEQAF 248
Cdd:COG1120 160 LLDEPTSHLDLAHQLEVLELLRRLA-RERGRTVVMVLHDLNLAARYaDRLVLLKDGRIVAQGPPEEV---LTPELLEEVY 235
|
250
....*....|....*....
gi 446125071 249 -IALLPEAQRQAHKPVVIP 266
Cdd:COG1120 236 gVEARVIEDPVTGRPLVLP 254
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
274-525 |
1.38e-39 |
|
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: 154.29 E-value: 1.38e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 274 EIAIEAKDLTMRF--GKFVAVDHVNFRIPRGEIFGFLGSNGCGKSTTMKMLTGLLPAS---EGQAWLFGQPVDPNDIDTR 348
Cdd:COG1123 2 TPLLEVRDLSVRYpgGDVPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGLLPHGgriSGEVLLDGRDLLELSEALR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 349 -RRVGYMSQ-AFSLYNELTVRQNLELHARLFHIPPAEIPARVAQMIERFMLTEVEDTLPASLPLGIRQRLSLAVAVIHRP 426
Cdd:COG1123 82 gRRIGMVFQdPMTQLNPVTVGDQIAEALENLGLSRAEARARVLELLEAVGLERRLDRYPHQLSGGQRQRVAIAMALALDP 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 427 EMLILDEPTSGVDPVARDMFWQLMVDLSRQDKVTIFISTHFMNE-AERCDRMSLMHAGKVLASGTPQELVQQrgAANLEA 505
Cdd:COG1123 162 DLLIADEPTTALDVTTQAEILDLLRELQRERGTTVLLITHDLGVvAEIADRVVVMDDGRIVEDGPPEEILAA--PQALAA 239
|
250 260
....*....|....*....|
gi 446125071 506 AFISWLQEAAGAAPETPIPP 525
Cdd:COG1123 240 VPRLGAARGRAAPAAAAAEP 259
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
14-230 |
2.01e-39 |
|
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: 145.59 E-value: 2.01e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 14 QLEGVSQHYGK----TVALNNITLDIPARSMVGLIGPDGVGKSSLLSLISGARVIEQGNVIVLGGDMrdAKHRRDVCPRI 89
Cdd:cd03266 3 TADALTKRFRDvkktVQAVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDGFDV--VKEPAEARRRL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 90 AWMPQGLGknLYHTLSVYENVDFFARLFGHDKAEREARITELLNSTGLAPFRDRPAGKLSGGMKQKLGLCCALIHDPELL 169
Cdd:cd03266 81 GFVSDSTG--LYDRLTARENLEYFAGLYGLKGDELTARLEELADRLGMEELLDRRVGGFSTGMRQKVAIARALVHDPPVL 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446125071 170 ILDEPTTGVDPLSRAQFWDLIDsiRQRQTNMSVLVATAYMEEAERF-DWLVAMNAGEILATG 230
Cdd:cd03266 159 LLDEPTTGLDVMATRALREFIR--QLRALGKCILFSTHIMQEVERLcDRVVVLHRGRVVYEG 218
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
276-494 |
3.15e-39 |
|
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex cysAWTP involved in sulfate import. Responsible for energy coupling to the transport system. The complex is composed of two ATP-binding proteins (cysA), two transmembrane proteins (cysT and cysW), and a solute-binding protein (cysP). ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213263 [Multi-domain] Cd Length: 239 Bit Score: 145.56 E-value: 3.15e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 276 AIEAKDLTMRFGKFVAVDHVNFRIPRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGQAWLFGQpvDPNDIDTRRR-VGYM 354
Cdd:cd03296 2 SIEVRNVSKRFGDFVALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGGE--DATDVPVQERnVGFV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 355 SQAFSLYNELTVRQN----LELHARLFHIPPAEIPARVAQMIERFMLTEVEDTLPASLPLGIRQRLSLAVAVIHRPEMLI 430
Cdd:cd03296 80 FQHYALFRHMTVFDNvafgLRVKPRSERPPEAEIRAKVHELLKLVQLDWLADRYPAQLSGGQRQRVALARALAVEPKVLL 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446125071 431 LDEPTSGVDPVARDMFWQLMVDLSRQDKVTIFISTHFMNEA-ERCDRMSLMHAGKVLASGTPQEL 494
Cdd:cd03296 160 LDEPFGALDAKVRKELRRWLRRLHDELHVTTVFVTHDQEEAlEVADRVVVMNKGRIEQVGTPDEV 224
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
10-237 |
4.10e-39 |
|
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: 145.95 E-value: 4.10e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 10 PPVAQLEGVSQHYGKTVALNNITLDIPARSMVGLIGPDGVGKSSLLSLISGARVIEQGNVIVLGGDMRDAKHRrdvcpRI 89
Cdd:COG0411 2 DPLLEVRGLTKRFGGLVAVDDVSLEVERGEIVGLIGPNGAGKTTLFNLITGFYRPTSGRILFDGRDITGLPPH-----RI 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 90 AWMpqGLGK-----NLYHTLSVYENV-------------DFFARLFGHDKAEREAR--ITELLNSTGLAPFRDRPAGKLS 149
Cdd:COG0411 77 ARL--GIARtfqnpRLFPELTVLENVlvaaharlgrgllAALLRLPRARREEREARerAEELLERVGLADRADEPAGNLS 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 150 GGMKQKLGLCCALIHDPELLILDEPTTGVDPLSRAQFWDLIDSIRQRQT--------NMSVLVATAymeeaerfDWLVAM 221
Cdd:COG0411 155 YGQQRRLEIARALATEPKLLLLDEPAAGLNPEETEELAELIRRLRDERGitilliehDMDLVMGLA--------DRIVVL 226
|
250
....*....|....*.
gi 446125071 222 NAGEILATGSAQQLRA 237
Cdd:COG0411 227 DFGRVIAEGTPAEVRA 242
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
277-494 |
5.73e-39 |
|
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: 144.69 E-value: 5.73e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 277 IEAKDLTMRFGKFVAVDHVNFRIPRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGQAWLFGQP---VDPNdidtRRRVGY 353
Cdd:cd03300 1 IELENVSKFYGGFVALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGKDitnLPPH----KRPVNT 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 354 MSQAFSLYNELTVRQNLELHARLFHIPPAEIPARVAQMIERFMLTEVEDTLPASLPLGIRQRLSLAVAVIHRPEMLILDE 433
Cdd:cd03300 77 VFQNYALFPHLTVFENIAFGLRLKKLPKAEIKERVAEALDLVQLEGYANRKPSQLSGGQQQRVAIARALVNEPKVLLLDE 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446125071 434 PTSGVDPVAR-DMFWQLMvDLSRQDKVTIFISTHFMNEA-ERCDRMSLMHAGKVLASGTPQEL 494
Cdd:cd03300 157 PLGALDLKLRkDMQLELK-RLQKELGITFVFVTHDQEEAlTMSDRIAVMNKGKIQQIGTPEEI 218
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
8-212 |
5.84e-39 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 145.62 E-value: 5.84e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 8 PVPPVAQLEGVSQHY----GKTVALNNITLDIPARSMVGLIGPDGVGKSSLLSLISGARVIEQGNVIVLGgdmrdaKHRR 83
Cdd:COG1116 3 AAAPALELRGVSKRFptggGGVTALDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPTSGEVLVDG------KPVT 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 84 DVCPRIAWMPQGlgknlyHTL----SVYENVDFFARLFGHDKAEREARITELLNSTGLAPFRDRPAGKLSGGMKQKLGLC 159
Cdd:COG1116 77 GPGPDRGVVFQE------PALlpwlTVLDNVALGLELRGVPKAERRERARELLELVGLAGFEDAYPHQLSGGMRQRVAIA 150
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 446125071 160 CALIHDPELLILDEPTTGVDPLSRAQFWDLIDSIRQRqTNMSVLVATAYMEEA 212
Cdd:COG1116 151 RALANDPEVLLMDEPFGALDALTRERLQDELLRLWQE-TGKTVLFVTHDVDEA 202
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
276-496 |
6.44e-39 |
|
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid transport and metabolism, Inorganic ion transport and metabolism];
Pssm-ID: 440741 [Multi-domain] Cd Length: 248 Bit Score: 144.95 E-value: 6.44e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 276 AIEAKDLTMRFGK----FVAVDHVNFRIPRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGQAWLFGQPV-DPNDIDTRRR 350
Cdd:COG1124 1 MLEVRNLSVSYGQggrrVPVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVTFDGRPVtRRRRKAFRRR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 351 VGYMSQ--AFSLYNELTVRQNLELHARLFHIPpaEIPARVAQMIERFMLT-EVEDTLPASLPLGIRQRLSLAVAVIHRPE 427
Cdd:COG1124 81 VQMVFQdpYASLHPRHTVDRILAEPLRIHGLP--DREERIAELLEQVGLPpSFLDRYPHQLSGGQRQRVAIARALILEPE 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 428 MLILDEPTSGVDPVARDMFWQLMVDLSRQDKVTIFISTHFMNEAER-CDRMSLMHAGKVLASGTPQELVQ 496
Cdd:COG1124 159 LLLLDEPTSALDVSVQAEILNLLKDLREERGLTYLFVSHDLAVVAHlCDRVAVMQNGRIVEELTVADLLA 228
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
10-228 |
8.42e-39 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 144.03 E-value: 8.42e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 10 PPVAQLEGVSQHYG----KTVALNNITLDIPARSMVGLIGPDGVGKSSLLSLISGARVIEQGNVIVLGGDMRD------A 79
Cdd:COG1136 2 SPLLELRNLTKSYGtgegEVTALRGVSLSIEAGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVLIDGQDISSlserelA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 80 KHRRDvcpRIAWMPQGLgkNLYHTLSVYENVDFFARLFGHDKAEREARITELLNSTGLAPFRDRPAGKLSGGMKQKLGLC 159
Cdd:COG1136 82 RLRRR---HIGFVFQFF--NLLPELTALENVALPLLLAGVSRKERRERARELLERVGLGDRLDHRPSQLSGGQQQRVAIA 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446125071 160 CALIHDPELLILDEPTTGVDPLSRAQFWDLIDSIRqRQTNMSVLVATAYMEEAERFDWLVAMNAGEILA 228
Cdd:COG1136 157 RALVNRPKLILADEPTGNLDSKTGEEVLELLRELN-RELGTTIVMVTHDPELAARADRVIRLRDGRIVS 224
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
14-237 |
1.24e-38 |
|
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: 143.73 E-value: 1.24e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 14 QLEGVSQHYGKTVALNNITLDIPARSMVGLIGPDGVGKSSLLSLISGARVIEQGNVIVLGGDMRDAK-HRRDVcpriawm 92
Cdd:cd03219 2 EVRGLTKRFGGLVALDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFDGEDITGLPpHEIAR------- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 93 pQGLGK-----NLYHTLSVYENV----------DFFARLFGHDKAEREARITELLNSTGLAPFRDRPAGKLSGGMKQKLG 157
Cdd:cd03219 75 -LGIGRtfqipRLFPELTVLENVmvaaqartgsGLLLARARREEREARERAEELLERVGLADLADRPAGELSYGQQRRLE 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 158 LCCALIHDPELLILDEPTTGVDPLSRAQFWDLIDSIRQRqtNMSVLVA----TAYMEEAERfdwLVAMNAGEILATGSAQ 233
Cdd:cd03219 154 IARALATDPKLLLLDEPAAGLNPEETEELAELIRELRER--GITVLLVehdmDVVMSLADR---VTVLDQGRVIAEGTPD 228
|
....
gi 446125071 234 QLRA 237
Cdd:cd03219 229 EVRN 232
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
14-206 |
2.02e-38 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 142.88 E-value: 2.02e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 14 QLEGVSQHY-GKTVALNNITLDIPARSMVGLIGPDGVGKSSLLSLISGARVIEQGNVIVLGGDMRDAKHRRdvcprIAWM 92
Cdd:COG2884 3 RFENVSKRYpGGREALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLVNGQDLSRLKRRE-----IPYL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 93 PQGLG------KNLYHtLSVYENVDFFARLFGHDKAEREARITELLNSTGLAPFRDRPAGKLSGGMKQKLGLCCALIHDP 166
Cdd:COG2884 78 RRRIGvvfqdfRLLPD-RTVYENVALPLRVTGKSRKEIRRRVREVLDLVGLSDKAKALPHELSGGEQQRVAIARALVNRP 156
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 446125071 167 ELLILDEPTTGVDPLSRAQFWDLIDSIRQRQTnmSVLVAT 206
Cdd:COG2884 157 ELLLADEPTGNLDPETSWEIMELLEEINRRGT--TVLIAT 194
|
|
| LPS_export_lptB |
TIGR04406 |
LPS export ABC transporter ATP-binding protein; Members of this fmaily are LptB, the ... |
279-495 |
2.45e-38 |
|
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: 143.18 E-value: 2.45e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 279 AKDLTMRFGKFVAVDHVNFRIPRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGQAWLFGQPVD--PNDIDTRRRVGYMSQ 356
Cdd:TIGR04406 4 AENLIKSYKKRKVVNDVSLSVKSGEIVGLLGPNGAGKTTSFYMIVGLVRPDAGKILIDGQDIThlPMHERARLGIGYLPQ 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 357 AFSLYNELTVRQN----LELHARLfhiPPAEIPARVAQMIERFMLTEVEDTLPASLPLGIRQRLSLAVAVIHRPEMLILD 432
Cdd:TIGR04406 84 EASIFRKLTVEENimavLEIRKDL---DRAEREERLEALLEEFQISHLRDNKAMSLSGGERRRVEIARALATNPKFILLD 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446125071 433 EPTSGVDPVARDMFWQLMVDLsRQDKVTIFISTHFMNEA-ERCDRMSLMHAGKVLASGTPQELV 495
Cdd:TIGR04406 161 EPFAGVDPIAVGDIKKIIKHL-KERGIGVLITDHNVRETlDICDRAYIISDGKVLAEGTPAEIV 223
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
14-230 |
5.97e-38 |
|
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily represents ABC transporters involved in peptide antibiotic resistance. Bacitracin is a dodecapeptide antibiotic produced by B. licheniformis and B. subtilis. The synthesis of bacitracin is non-ribosomally catalyzed by a multi-enzyme complex BcrABC. Bacitracin has potent antibiotic activity against gram-positive bacteria. The inhibition of peptidoglycan biosynthesis is the best characterized bacterial effect of bacitracin. The bacitracin resistance of B. licheniformis is mediated by the ABC transporter Bcr which is composed of two identical BcrA ATP-binding subunits and one each of the integral membrane proteins, BcrB and BcrC. B. subtilis cells carrying bcr genes on high-copy number plasmids develop collateral detergent sensitivity, a similar phenomenon in human cells with overexpressed multi-drug resistance P-glycoprotein.
Pssm-ID: 213235 [Multi-domain] Cd Length: 208 Bit Score: 140.82 E-value: 5.97e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 14 QLEGVSQHYGKTVALNNITLDIPARSMVGLIGPDGVGKSSLLSLISGARVIEQGNVIVLGGDMRDAKhrrDVCPRIAWMP 93
Cdd:cd03268 2 KTNDLTKTYGKKRVLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEITFDGKSYQKNI---EALRRIGALI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 94 QGLGknLYHTLSVYENVDFFARLFGhdkaEREARITELLNSTGLAPFRDRPAGKLSGGMKQKLGLCCALIHDPELLILDE 173
Cdd:cd03268 79 EAPG--FYPNLTARENLRLLARLLG----IRKKRIDEVLDVVGLKDSAKKKVKGFSLGMKQRLGIALALLGNPDLLILDE 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 446125071 174 PTTGVDPLSRAQFWDLIdsIRQRQTNMSVLVATAYMEEAERF-DWLVAMNAGEILATG 230
Cdd:cd03268 153 PTNGLDPDGIKELRELI--LSLRDQGITVLISSHLLSEIQKVaDRIGIINKGKLIEEG 208
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
273-496 |
6.62e-38 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 149.01 E-value: 6.62e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 273 EEIAIEAKDLTMRFGKFVAVDHVNFRIPRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGQAWLFGQPVDPNDI-DTRRR- 350
Cdd:COG1129 1 AEPLLEMRGISKSFGGVKALDGVSLELRPGEVHALLGENGAGKSTLMKILSGVYQPDSGEILLDGEPVRFRSPrDAQAAg 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 351 VGYMSQAFSLYNELTVRQNL----ELHARLFhIPPAEIPARVAQMIERFMLTEVEDTLPASLPLGIRQRLSLAVAVIHRP 426
Cdd:COG1129 81 IAIIHQELNLVPNLSVAENIflgrEPRRGGL-IDWRAMRRRARELLARLGLDIDPDTPVGDLSVAQQQLVEIARALSRDA 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446125071 427 EMLILDEPTSGVDPVARDMFWQLMVDLSRQDKVTIFIStHFMNEAER-CDRMSLMHAGKVLASG-----TPQELVQ 496
Cdd:COG1129 160 RVLILDEPTASLTEREVERLFRIIRRLKAQGVAIIYIS-HRLDEVFEiADRVTVLRDGRLVGTGpvaelTEDELVR 234
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
292-436 |
1.43e-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: 1.43e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 292 VDHVNFRIPRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGQAWLFGQPVDPNDI-DTRRRVGYMSQAFSLYNELTVRQNL 370
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDLTDDERkSLRKEIGYVFQDPQLFPRLTVRENL 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 371 ELHARLFHIPPAEIPARVAQMIERFMLTEVEDTL----PASLPLGIRQRLSLAVAVIHRPEMLILDEPTS 436
Cdd:pfam00005 81 RLGLLLKGLSKREKDARAEEALEKLGLGDLADRPvgerPGTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
14-240 |
4.89e-37 |
|
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: 139.17 E-value: 4.89e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 14 QLEGVSQHYGKTVALNNITLDIPARSMVGLIGPDGVGKSSLLSLISGARVIEQGNVIVLGGDMRDAK------HRRdvcp 87
Cdd:cd03261 2 ELRGLTKSFGGRTVLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGEDISGLSeaelyrLRR---- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 88 RIAWMPQGLGknLYHTLSVYENVDFFARLFGH-DKAEREARITELLNSTGLAPFRDRPAGKLSGGMKQKLGLCCALIHDP 166
Cdd:cd03261 78 RMGMLFQSGA--LFDSLTVFENVAFPLREHTRlSEEEIREIVLEKLEAVGLRGAEDLYPAELSGGMKKRVALARALALDP 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446125071 167 ELLILDEPTTGVDPLSRAQFWDLIDSIrQRQTNMSVLVATAYMEEAERF-DWLVAMNAGEILATGSAQQLRAKTH 240
Cdd:cd03261 156 ELLLYDEPTAGLDPIASGVIDDLIRSL-KKELGLTSIMVTHDLDTAFAIaDRIAVLYDGKIVAEGTPEELRASDD 229
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
9-235 |
6.04e-37 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 142.28 E-value: 6.04e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 9 VPPVA-QLEGVSQHYGKTVALNNITLDIPARSMVGLIGPDGVGKSSLLSLISGARVIEQGNVIVLG----GDMRDAKHRR 83
Cdd:PRK13536 37 MSTVAiDLAGVSKSYGDKAVVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKITVLGvpvpARARLARARI 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 84 DVCPRIawmpqglgKNLYHTLSVYENVDFFARLFGHDKAEREARITELLNSTGLAPFRDRPAGKLSGGMKQKLGLCCALI 163
Cdd:PRK13536 117 GVVPQF--------DNLDLEFTVRENLLVFGRYFGMSTREIEAVIPSLLEFARLESKADARVSDLSGGMKRRLTLARALI 188
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446125071 164 HDPELLILDEPTTGVDPLSRAQFWDLIDSIRQRqtNMSVLVATAYMEEAERF-DWLVAMNAGEILATGSAQQL 235
Cdd:PRK13536 189 NDPQLLILDEPTTGLDPHARHLIWERLRSLLAR--GKTILLTTHFMEEAERLcDRLCVLEAGRKIAEGRPHAL 259
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
277-494 |
9.18e-37 |
|
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of the LIV-I bacterial ABC-type two-component transport system that imports neutral, branched-chain amino acids. The E. coli branched-chain amino acid transporter comprises a heterodimer of ABC transporters (LivF and LivG), a heterodimer of six-helix TM domains (LivM and LivH), and one of two alternative soluble periplasmic substrate binding proteins (LivK or LivJ). ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules.
Pssm-ID: 213191 [Multi-domain] Cd Length: 222 Bit Score: 137.95 E-value: 9.18e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 277 IEAKDLTMRFGKFVAVDHVNFRIPRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGQAWLFGQPVD---PNDIdTRRRVGY 353
Cdd:cd03224 1 LEVENLNAGYGKSQILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDGRDITglpPHER-ARAGIGY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 354 MSQAFSLYNELTVRQNLELHARLFhiPPAEIPARVAQMIERF-MLTEVEDTLPASLPLGIRQRLSLAVAVIHRPEMLILD 432
Cdd:cd03224 80 VPEGRRIFPELTVEENLLLGAYAR--RRAKRKARLERVYELFpRLKERRKQLAGTLSGGEQQMLAIARALMSRPKLLLLD 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446125071 433 EPTSGVDPVARDMFWQLMVDLsRQDKVTIFISTHFMNEA-ERCDRMSLMHAGKVLASGTPQEL 494
Cdd:cd03224 158 EPSEGLAPKIVEEIFEAIREL-RDEGVTILLVEQNARFAlEIADRAYVLERGRVVLEGTAAEL 219
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
278-484 |
1.00e-36 |
|
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: 135.45 E-value: 1.00e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 278 EAKDLTMRFGKFVAVDHVNFRIPRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGQAWLFGQPVDPNDIDT-RRRVGYMSQ 356
Cdd:cd00267 1 EIENLSFRYGGRTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGKDIAKLPLEElRRRIGYVPQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 357 afslyneltvrqnlelharlfhippaeiparvaqmierfmltevedtlpasLPLGIRQRLSLAVAVIHRPEMLILDEPTS 436
Cdd:cd00267 81 ---------------------------------------------------LSGGQRQRVALARALLLNPDLLLLDEPTS 109
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 446125071 437 GVDPVARDMFWQLMVDLSRQDKvTIFISTHFMNEAER-CDRMSLMHAGK 484
Cdd:cd00267 110 GLDPASRERLLELLRELAEEGR-TVIIVTHDPELAELaADRVIVLKDGK 157
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
277-519 |
1.07e-36 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 141.37 E-value: 1.07e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 277 IEAKDLTMRF----GKFVAVDHVNFRIPRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGQAWLFGQPV---DPNDI-DTR 348
Cdd:COG1135 2 IELENLSKTFptkgGPVTALDDVSLTIEKGEIFGIIGYSGAGKSTLIRCINLLERPTSGSVLVDGVDLtalSERELrAAR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 349 RRVGYMSQAFSLYNELTVRQNLELHARLFHIPPAEIPARVAQMIERFMLTEVEDTLPASLPLGIRQRLSLAVAVIHRPEM 428
Cdd:COG1135 82 RKIGMIFQHFNLLSSRTVAENVALPLEIAGVPKAEIRKRVAELLELVGLSDKADAYPSQLSGGQKQRVGIARALANNPKV 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 429 LILDEPTSGVDPVARDMFWQLMVDLSRQDKVTIFISTHFMNEAER-CDRMSLMHAGKVLASGT-------PQ-----ELV 495
Cdd:COG1135 162 LLCDEATSALDPETTRSILDLLKDINRELGLTIVLITHEMDVVRRiCDRVAVLENGRIVEQGPvldvfanPQseltrRFL 241
|
250 260
....*....|....*....|....
gi 446125071 496 QQRGAANLEAAFISWLQEAAGAAP 519
Cdd:COG1135 242 PTVLNDELPEELLARLREAAGGGR 265
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
277-485 |
1.52e-36 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 136.87 E-value: 1.52e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 277 IEAKDLTMRFGKFVAVDHVNFRIPRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGQAWLFGQPVDPNDIDT-RRRVGYMS 355
Cdd:COG4619 1 LELEGLSFRVGGKPILSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIYLDGKPLSAMPPPEwRRQVAYVP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 356 QAFSLYNElTVRQNLELHARLFHIPPAeiPARVAQMIERFMLTE-VEDTLPASLPLGIRQRLSLAVAVIHRPEMLILDEP 434
Cdd:COG4619 81 QEPALWGG-TVRDNLPFPFQLRERKFD--RERALELLERLGLPPdILDKPVERLSGGERQRLALIRALLLQPDVLLLDEP 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 446125071 435 TSGVDPVARDMFWQLMVDLSRQDKVTIFISTHFMNEAER-CDRMSLMHAGKV 485
Cdd:COG4619 158 TSALDPENTRRVEELLREYLAEEGRAVLWVSHDPEQIERvADRVLTLEAGRL 209
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
14-212 |
2.00e-36 |
|
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: 136.83 E-value: 2.00e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 14 QLEGVSQHYG----KTVALNNITLDIPARSMVGLIGPDGVGKSSLLSLISGARVIEQGNVIVLGGDMRDAKhrrdvcPRI 89
Cdd:cd03293 2 EVRNVSKTYGggggAVTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVDGEPVTGPG------PDR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 90 AWMPQGlgKNLYHTLSVYENVDFFARLFGHDKAEREARITELLNSTGLAPFRDRPAGKLSGGMKQKLGLCCALIHDPELL 169
Cdd:cd03293 76 GYVFQQ--DALLPWLTVLDNVALGLELQGVPKAEARERAEELLELVGLSGFENAYPHQLSGGMRQRVALARALAVDPDVL 153
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 446125071 170 ILDEPTTGVDPLSRAQFWDLIDSIRqRQTNMSVLVATAYMEEA 212
Cdd:cd03293 154 LLDEPFSALDALTREQLQEELLDIW-RETGKTVLLVTHDIDEA 195
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
10-494 |
2.03e-36 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 144.78 E-value: 2.03e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 10 PPVAQLEGVSQHYGKTVALNNITLDIPARSMVGLIGPDGVGKSSLLSLISGARVIEQGNVIVLG-----GDMRDAkhrrd 84
Cdd:COG3845 3 PPALELRGITKRFGGVVANDDVSLTVRPGEIHALLGENGAGKSTLMKILYGLYQPDSGEILIDGkpvriRSPRDA----- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 85 vcprIAwmpQGLGK-----NLYHTLSVYENV------DFFARLfghDKAEREARITELLNSTGLA--PfrDRPAGKLSGG 151
Cdd:COG3845 78 ----IA---LGIGMvhqhfMLVPNLTVAENIvlglepTKGGRL---DRKAARARIRELSERYGLDvdP--DAKVEDLSVG 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 152 MKQKLGLCCALIHDPELLILDEPTTGVDPLSRAQfwdLIDSIRQ-RQTNMSVLVATAYMEEAERF-DWLVAMNAGEILAT 229
Cdd:COG3845 146 EQQRVEILKALYRGARILILDEPTAVLTPQEADE---LFEILRRlAAEGKSIIFITHKLREVMAIaDRVTVLRRGKVVGT 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 230 GSAqqlrAKTHSATLEQAFI--ALLPEAQRQAHKPvvippyhaeqEEIAIEAKDLTMR-FGKFVAVDHVNFRIPRGEIFG 306
Cdd:COG3845 223 VDT----AETSEEELAELMVgrEVLLRVEKAPAEP----------GEVVLEVENLSVRdDRGVPALKDVSLEVRAGEILG 288
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 307 FLGSNGCGKSTTMKMLTGLLPASEGQAWLFGQPVDPNDIDTRRR--VGYMS---QAFSLYNELTVRQN--LELH-----A 374
Cdd:COG3845 289 IAGVAGNGQSELAEALAGLRPPASGSIRLDGEDITGLSPRERRRlgVAYIPedrLGRGLVPDMSVAENliLGRYrrppfS 368
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 375 RLFHIPPAEIPARVAQMIERF-MLTEVEDTLPASLPLGIRQRLSLAVAVIHRPEMLILDEPTSGVDPVARDMFWQLMVDL 453
Cdd:COG3845 369 RGGFLDRKAIRAFAEELIEEFdVRTPGPDTPARSLSGGNQQKVILARELSRDPKLLIAAQPTRGLDVGAIEFIHQRLLEL 448
|
490 500 510 520
....*....|....*....|....*....|....*....|..
gi 446125071 454 SRQDKVTIFISTHfMNEA-ERCDRMSLMHAGKVLASGTPQEL 494
Cdd:COG3845 449 RDAGAAVLLISED-LDEIlALSDRIAVMYEGRIVGEVPAAEA 489
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
277-485 |
5.16e-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: 135.46 E-value: 5.16e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 277 IEAKDLTMRFGKFVAVDHVNFRIPRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGQAWLFGQPV---DPNDidtrRRVGY 353
Cdd:cd03301 1 VELENVTKRFGNVTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGRDVtdlPPKD----RDIAM 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 354 MSQAFSLYNELTVRQNLELHARLFHIPPAEIPARVAQMIERFMLTEVEDTLPASLPLGIRQRLSLAVAVIHRPEMLILDE 433
Cdd:cd03301 77 VFQNYALYPHMTVYDNIAFGLKLRKVPKDEIDERVREVAELLQIEHLLDRKPKQLSGGQRQRVALGRAIVREPKVFLMDE 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 446125071 434 PTSGVDPVARDMFWQLMVDLSRQDKVTIFISTHFMNEAER-CDRMSLMHAGKV 485
Cdd:cd03301 157 PLSNLDAKLRVQMRAELKRLQQRLGTTTIYVTHDQVEAMTmADRIAVMNDGQI 209
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
14-237 |
7.88e-36 |
|
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of the LIV-I bacterial ABC-type two-component transport system that imports neutral, branched-chain amino acids. The E. coli branched-chain amino acid transporter comprises a heterodimer of ABC transporters (LivF and LivG), a heterodimer of six-helix TM domains (LivM and LivH), and one of two alternative soluble periplasmic substrate binding proteins (LivK or LivJ). ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules.
Pssm-ID: 213191 [Multi-domain] Cd Length: 222 Bit Score: 135.25 E-value: 7.88e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 14 QLEGVSQHYGKTVALNNITLDIPARSMVGLIGPDGVGKSSLLSLISGARVIEQGNVIVLGGDMRDAK-HRRdvcPR--IA 90
Cdd:cd03224 2 EVENLNAGYGKSQILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDGRDITGLPpHER---ARagIG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 91 WMPQGlgKNLYHTLSVYENVDFFARLFGHDK-AEREARITELLnsTGLAPFRDRPAGKLSGGMKQKLGLCCALIHDPELL 169
Cdd:cd03224 79 YVPEG--RRIFPELTVEENLLLGAYARRRAKrKARLERVYELF--PRLKERRKQLAGTLSGGEQQMLAIARALMSRPKLL 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446125071 170 ILDEPTTGVDPLSRAQFWDLIDSIRQRQtnMSVLV----ATAYMEEAERFdwlVAMNAGEILATGSAQQLRA 237
Cdd:cd03224 155 LLDEPSEGLAPKIVEEIFEAIRELRDEG--VTILLveqnARFALEIADRA---YVLERGRVVLEGTAAELLA 221
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
264-508 |
1.07e-35 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 139.59 E-value: 1.07e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 264 VIPPYHAEQEEIA---IEAKDLTMRFGKFVAVDHVNFRIPRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGQAWLFGQpv 340
Cdd:PRK11607 4 AIPRPQAKTRKALtplLEIRNLTKSFDGQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGV-- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 341 DPNDIDTRRR-VGYMSQAFSLYNELTVRQNLELHARLFHIPPAEIPARVAQMIERFMLTEVEDTLPASLPLGIRQRLSLA 419
Cdd:PRK11607 82 DLSHVPPYQRpINMMFQSYALFPHMTVEQNIAFGLKQDKLPKAEIASRVNEMLGLVHMQEFAKRKPHQLSGGQRQRVALA 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 420 VAVIHRPEMLILDEPTSGVDPVARDMFWQLMVDLSRQDKVTIFISTHFMNEA-ERCDRMSLMHAGKVLASGTPQElVQQR 498
Cdd:PRK11607 162 RSLAKRPKLLLLDEPMGALDKKLRDRMQLEVVDILERVGVTCVMVTHDQEEAmTMAGRIAIMNRGKFVQIGEPEE-IYEH 240
|
250
....*....|
gi 446125071 499 GAANLEAAFI 508
Cdd:PRK11607 241 PTTRYSAEFI 250
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
268-497 |
1.43e-35 |
|
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: 136.23 E-value: 1.43e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 268 YHAEQEEIAIEAKDLTM----RFGKFVAVDHVNFRIPRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGQAWLFGQPVdpN 343
Cdd:cd03294 12 KNPQKAFKLLAKGKSKEeilkKTGQTVGVNDVSLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGKVLIDGQDI--A 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 344 DIDT-------RRRVGYMSQAFSLYNELTVRQNLELHARLFHIPPAEIPARVAQMIERFMLTEVEDTLPASLPLGIRQRL 416
Cdd:cd03294 90 AMSRkelrelrRKKISMVFQSFALLPHRTVLENVAFGLEVQGVPRAEREERAAEALELVGLEGWEHKYPDELSGGMQQRV 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 417 SLAVAVIHRPEMLILDEPTSGVDPVAR-DMFWQLMvDLSRQDKVTIFISTHFMNEAERC-DRMSLMHAGKVLASGTPQEL 494
Cdd:cd03294 170 GLARALAVDPDILLMDEAFSALDPLIRrEMQDELL-RLQAELQKTIVFITHDLDEALRLgDRIAIMKDGRLVQVGTPEEI 248
|
...
gi 446125071 495 VQQ 497
Cdd:cd03294 249 LTN 251
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
277-489 |
1.91e-35 |
|
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: 134.56 E-value: 1.91e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 277 IEAKDLTMRF----GKFVAVDHVNFRIPRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGQAWLFGQPVDPNDI----DTR 348
Cdd:cd03257 2 LEVKNLSVSFptggGSVKALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGKDLLKLSRrlrkIRR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 349 RRVGYMSQ--AFSLYNELTVRQNLE--LHARLFHIPPAEIPARVAQMIERFMLTE-VEDTLPASLPLGIRQRLSLAVAVI 423
Cdd:cd03257 82 KEIQMVFQdpMSSLNPRMTIGEQIAepLRIHGKLSKKEARKEAVLLLLVGVGLPEeVLNRYPHELSGGQRQRVAIARALA 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446125071 424 HRPEMLILDEPTSGVDPVARDMFWQLMVDLSRQDKVTIFISTHFMNEAER-CDRMSLMHAGKVLASG 489
Cdd:cd03257 162 LNPKLLIADEPTSALDVSVQAQILDLLKKLQEELGLTLLFITHDLGVVAKiADRVAVMYAGKIVEEG 228
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
14-235 |
3.71e-35 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 137.54 E-value: 3.71e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 14 QLEGVSQHYGKTVALNNITLDIPARSMVGLIGPDGVGKSSLLSLISGARVIEQGNVIVLGGDMRDAK-HRRDvcprIAWM 92
Cdd:COG3842 7 ELENVSKRYGDVTALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRILLDGRDVTGLPpEKRN----VGMV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 93 PQGlgknlY----HtLSVYENVDFFARLFGHDKAEREARITELLNSTGLAPFRDRPAGKLSGGMKQKLGLCCALIHDPEL 168
Cdd:COG3842 83 FQD-----YalfpH-LTVAENVAFGLRMRGVPKAEIRARVAELLELVGLEGLADRYPHQLSGGQQQRVALARALAPEPRV 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446125071 169 LILDEPTTGVDPLSRAQFWDLIDSIrQRQTNMSVLVATAYMEEAERF-DWLVAMNAGEILATGSAQQL 235
Cdd:COG3842 157 LLLDEPLSALDAKLREEMREELRRL-QRELGITFIYVTHDQEEALALaDRIAVMNDGRIEQVGTPEEI 223
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
278-489 |
3.97e-35 |
|
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: 131.79 E-value: 3.97e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 278 EAKDLTMRFGKFVAVDHVNFRIPRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGQAWLFGQPVDPNDIDTR-RRVGYMSQ 356
Cdd:cd03214 1 EVENLSVGYGGRTVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDGKDLASLSPKELaRKIAYVPQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 357 AfslyneltvrqnLELharlfhippaeipARVAQMIERFMLTevedtlpasLPLGIRQRLSLAVAVIHRPEMLILDEPTS 436
Cdd:cd03214 81 A------------LEL-------------LGLAHLADRPFNE---------LSGGERQRVLLARALAQEPPILLLDEPTS 126
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 446125071 437 GVDPVARDMFWQLMVDLSRQDKVTIFISTHFMNEAER-CDRMSLMHAGKVLASG 489
Cdd:cd03214 127 HLDIAHQIELLELLRRLARERGKTVVMVLHDLNLAARyADRVILLKDGRIVAQG 180
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
277-488 |
5.87e-35 |
|
First domain of the ATP-binding cassette component of monosaccharide transport system; This family represents the domain I of the carbohydrate uptake proteins that transport only monosaccharides (Monos). The Carb_Monos family is involved in the uptake of monosaccharides, such as pentoses (such as xylose, arabinose, and ribose) and hexoses (such as xylose, arabinose, and ribose), that cannot be broken down to simple sugars by hydrolysis. Pentoses include xylose, arabinose, and ribose. Important hexoses include glucose, galactose, and fructose. In members of the Carb_monos family, the single hydrophobic gene product forms a homodimer while the ABC protein represents a fusion of two nucleotide-binding domains. However, it is assumed that two copies of the ABC domains are present in the assembled transporter.
Pssm-ID: 213183 [Multi-domain] Cd Length: 163 Bit Score: 130.63 E-value: 5.87e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 277 IEAKDLTMRFGKFVAVDHVNFRIPRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGQAWLFGQPVDPNDIDTRRRVGymsq 356
Cdd:cd03216 1 LELRGITKRFGGVKALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVDGKEVSFASPRDARRAG---- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 357 afslyneltvrqnlelharlfhIppaeipARVAQmierfmltevedtlpasLPLGIRQRLSLAVAVIHRPEMLILDEPTS 436
Cdd:cd03216 77 ----------------------I------AMVYQ-----------------LSVGERQMVEIARALARNARLLILDEPTA 111
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 446125071 437 GVDPVARDMFWQLMVDLSRQDKVTIFIStHFMNEAER-CDRMSLMHAGKVLAS 488
Cdd:cd03216 112 ALTPAEVERLFKVIRRLRAQGVAVIFIS-HRLDEVFEiADRVTVLRDGRVVGT 163
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
28-176 |
9.62e-35 |
|
ABC transporter; ABC transporters for a large family of proteins responsible for translocation of a variety of compounds across biological membranes. ABC transporters are the largest family of proteins in many completely sequenced bacteria. ABC transporters are composed of two copies of this domain and two copies of a transmembrane domain pfam00664. These four domains may belong to a single polypeptide or belong in different polypeptide chains.
Pssm-ID: 394964 [Multi-domain] Cd Length: 150 Bit Score: 129.69 E-value: 9.62e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 28 LNNITLDIPARSMVGLIGPDGVGKSSLLSLISGARVIEQGNVIVLGGDM--RDAKHRRDvcpRIAWMPQGLgkNLYHTLS 105
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDLtdDERKSLRK---EIGYVFQDP--QLFPRLT 75
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446125071 106 VYENVDFFARLFGHDKAEREARITELLNSTGLAPFRDRPAGK----LSGGMKQKLGLCCALIHDPELLILDEPTT 176
Cdd:pfam00005 76 VRENLRLGLLLKGLSKREKDARAEEALEKLGLGDLADRPVGErpgtLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
8-235 |
1.53e-34 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 134.55 E-value: 1.53e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 8 PVPPVaQLEGVSQHYGKTVALNNITLDIPARSMVGLIGPDGVGKSSLLSLISGARVIEQGNVIVLG----GDMRDAKHRR 83
Cdd:PRK13537 4 SVAPI-DFRNVEKRYGDKLVVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCGepvpSRARHARQRV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 84 DVCPRIawmpqglgKNLYHTLSVYENVDFFARLFGHDKAEREARITELLNSTGLAPFRDRPAGKLSGGMKQKLGLCCALI 163
Cdd:PRK13537 83 GVVPQF--------DNLDPDFTVRENLLVFGRYFGLSAAAARALVPPLLEFAKLENKADAKVGELSGGMKRRLTLARALV 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446125071 164 HDPELLILDEPTTGVDPLSRAQFWDLIDSIRQRqtNMSVLVATAYMEEAERF-DWLVAMNAGEILATGSAQQL 235
Cdd:PRK13537 155 NDPDVLVLDEPTTGLDPQARHLMWERLRSLLAR--GKTILLTTHFMEEAERLcDRLCVIEEGRKIAEGAPHAL 225
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
14-237 |
2.10e-34 |
|
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: 131.64 E-value: 2.10e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 14 QLEGVSQHYGKTVALNNITLDIPARSMVGLIGPDGVGKSSLLSLISGARVIEQGNVIVLGGDMRDAK-HRRdvcPR--IA 90
Cdd:COG0410 5 EVENLHAGYGGIHVLHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRSGSIRFDGEDITGLPpHRI---ARlgIG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 91 WMPQGlgKNLYHTLSVYEN--VDFFARLFGHDKAEREARITELLnsTGLAPFRDRPAGKLSGGMKQKLGLCCALIHDPEL 168
Cdd:COG0410 82 YVPEG--RRIFPSLTVEENllLGAYARRDRAEVRADLERVYELF--PRLKERRRQRAGTLSGGEQQMLAIGRALMSRPKL 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446125071 169 LILDEPTTGVDPLSRAQFWDLIDSIRQRqtNMSVLV----ATAYMEEAERFdwlVAMNAGEILATGSAQQLRA 237
Cdd:COG0410 158 LLLDEPSLGLAPLIVEEIFEIIRRLNRE--GVTILLveqnARFALEIADRA---YVLERGRIVLEGTAAELLA 225
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
15-235 |
3.88e-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: 130.78 E-value: 3.88e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 15 LEGVS----QHYGKTVALNNITLDIPARSMVGLIGPDGVGKSSLLSLISGARVIEQGNVIVLGGDM--RDAKHRRDVCPR 88
Cdd:cd03258 4 LKNVSkvfgDTGGKVTALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGSVLVDGTDLtlLSGKELRKARRR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 89 IAWMPQGLgkNLYHTLSVYENVDFFARLFGHDKAEREARITELLNSTGLAPFRDRPAGKLSGGMKQKLGLCCALIHDPEL 168
Cdd:cd03258 84 IGMIFQHF--NLLSSRTVFENVALPLEIAGVPKAEIEERVLELLELVGLEDKADAYPAQLSGGQKQRVGIARALANNPKV 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446125071 169 LILDEPTTGVDPLSRAQFWDLIDSIrQRQTNMSVLVATAYMEEAERFDWLVA-MNAGEILATGSAQQL 235
Cdd:cd03258 162 LLCDEATSALDPETTQSILALLRDI-NRELGLTIVLITHEMEVVKRICDRVAvMEKGEVVEEGTVEEV 228
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
218-500 |
4.00e-34 |
|
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: 138.75 E-value: 4.00e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 218 LVAMNAGEILA--TGSAQQLRAKTHSATLEQAFIALLPEAQRQAHKPVVIPPYhaeqeeiAIEAKDLTMRF--GKFVAVD 293
Cdd:COG4987 280 LAALALFEALAplPAAAQHLGRVRAAARRLNELLDAPPAVTEPAEPAPAPGGP-------SLELEDVSFRYpgAGRPVLD 352
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 294 HVNFRIPRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGQAWLFGQPVDPNDIDT-RRRVGYMSQAFSLYNElTVRQNLEL 372
Cdd:COG4987 353 GLSLTLPPGERVAIVGPSGSGKSTLLALLLRFLDPQSGSITLGGVDLRDLDEDDlRRRIAVVPQRPHLFDT-TLRENLRL 431
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 373 hARlfhipPAEIPARVAQMIERFMLTEVEDTLPASL--PLGI---------RQRLSLAVAVIHRPEMLILDEPTSGVDPV 441
Cdd:COG4987 432 -AR-----PDATDEELWAALERVGLGDWLAALPDGLdtWLGEggrrlsggeRRRLALARALLRDAPILLLDEPTEGLDAA 505
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 446125071 442 ARDMFWQLMVDLSrQDKVTIFIsTHFMNEAERCDRMSLMHAGKVLASGTPQELVQQRGA 500
Cdd:COG4987 506 TEQALLADLLEAL-AGRTVLLI-THRLAGLERMDRILVLEDGRIVEQGTHEELLAQNGR 562
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
274-507 |
4.24e-34 |
|
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: 131.36 E-value: 4.24e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 274 EIAIEAKDLTMRFGKFVAVDHVNFRIPRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGQ-AWLFGQP---VDPNDIdtRR 349
Cdd:COG1119 1 DPLLELRNVTVRRGGKTILDDISWTVKPGEHWAILGPNGAGKSTLLSLITGDLPPTYGNdVRLFGERrggEDVWEL--RK 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 350 RVGYMSQAFSLY--NELTVRQ--------NLELHARlfhiPPAEIPARVAQMIERFMLTEVEDTLPASLPLGIRQRLSLA 419
Cdd:COG1119 79 RIGLVSPALQLRfpRDETVLDvvlsgffdSIGLYRE----PTDEQRERARELLELLGLAHLADRPFGTLSQGEQRRVLIA 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 420 VAVIHRPEMLILDEPTSGVDPVARDMFWQLMVDLSRQDKVTIFISTHFMNEAERC-DRMSLMHAGKVLASGTPQELVQqr 498
Cdd:COG1119 155 RALVKDPELLILDEPTAGLDLGARELLLALLDKLAAEGAPTLVLVTHHVEEIPPGiTHVLLLKDGRVVAAGPKEEVLT-- 232
|
....*....
gi 446125071 499 gAANLEAAF 507
Cdd:COG1119 233 -SENLSEAF 240
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
14-235 |
4.40e-34 |
|
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; Phosphonates are a class of organophosphorus compounds characterized by a chemically stable carbon-to-phosphorus (C-P) bond. Phosphonates are widespread among naturally occurring compounds in all kingdoms of wildlife, but only prokaryotic microorganisms are able to cleave this bond. Certain bacteria such as E. coli can use alkylphosphonates as a phosphorus source. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213223 [Multi-domain] Cd Length: 241 Bit Score: 130.77 E-value: 4.40e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 14 QLEGVSQHYG-KTVALNNITLDIPARSMVGLIGPDGVGKSSLLSLISGARVIEQGNVIVLGGDMRDAKHR--RDVCPRIA 90
Cdd:cd03256 2 EVENLSKTYPnGKKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGTDINKLKGKalRQLRRQIG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 91 WMPQGLgkNLYHTLSVYENV--------DFFARLFGH-DKAEREARItELLNSTGLAPFRDRPAGKLSGGMKQKLGLCCA 161
Cdd:cd03256 82 MIFQQF--NLIERLSVLENVlsgrlgrrSTWRSLFGLfPKEEKQRAL-AALERVGLLDKAYQRADQLSGGQQQRVAIARA 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446125071 162 LIHDPELLILDEPTTGVDPLSRAQFWDLIDSIRQRQtNMSVLVATAYMEEAERF-DWLVAMNAGEILATGSAQQL 235
Cdd:cd03256 159 LMQQPKLILADEPVASLDPASSRQVMDLLKRINREE-GITVIVSLHQVDLAREYaDRIVGLKDGRIVFDGPPAEL 232
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
217-500 |
8.56e-34 |
|
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase domain [Defense mechanisms];
Pssm-ID: 441875 [Multi-domain] Cd Length: 711 Bit Score: 139.20 E-value: 8.56e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 217 WLV---AMNAGEILA--------TGSAQQL--------RAKTHSATLEQafIALLPEAQRQAHKPVVIPPYHAEqeeiaI 277
Cdd:COG2274 402 YLVidgQLTLGQLIAfnilsgrfLAPVAQLigllqrfqDAKIALERLDD--ILDLPPEREEGRSKLSLPRLKGD-----I 474
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 278 EAKDLTMRFGKFV--AVDHVNFRIPRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGQAWLFGQP---VDPNDIdtRRRVG 352
Cdd:COG2274 475 ELENVSFRYPGDSppVLDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEPTSGRILIDGIDlrqIDPASL--RRQIG 552
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 353 YMSQAFSLYNElTVRQNLELHARlfHIPPAEIpARVAQMIErfmLTEVEDTLP-----------ASLPLGIRQRLSLAVA 421
Cdd:COG2274 553 VVLQDVFLFSG-TIRENITLGDP--DATDEEI-IEAARLAG---LHDFIEALPmgydtvvgeggSNLSGGQRQRLAIARA 625
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446125071 422 VIHRPEMLILDEPTSGVDPVARDMFWQLMVDLSRqdKVTIFISTHFMNEAERCDRMSLMHAGKVLASGTPQELVQQRGA 500
Cdd:COG2274 626 LLRNPRILILDEATSALDAETEAIILENLRRLLK--GRTVIIIAHRLSTIRLADRIIVLDKGRIVEDGTHEELLARKGL 702
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
277-485 |
2.69e-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: 2.69e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 277 IEAKDLTMRFGKFVAVDHVNFRIPRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGQAWLFGQPV--DPNDIDT-RRRVGY 353
Cdd:cd03262 1 IEIKNLHKSFGDFHVLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIDGLKLtdDKKNINElRQKVGM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 354 MSQAFSLYNELTVRQNLELHAR-LFHIPPAEIPARVAQMIERFMLTEVEDTLPASLPLGIRQRLSLAVAVIHRPEMLILD 432
Cdd:cd03262 81 VFQQFNLFPHLTVLENITLAPIkVKGMSKAEAEERALELLEKVGLADKADAYPAQLSGGQQQRVAIARALAMNPKVMLFD 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 446125071 433 EPTSGVDPVARDMFWQLMVDLSrQDKVTIFISTHFMNEA-ERCDRMSLMHAGKV 485
Cdd:cd03262 161 EPTSALDPELVGEVLDVMKDLA-EEGMTMVVVTHEMGFArEVADRVIFMDDGRI 213
|
|
| ABC2_membrane_3 |
pfam12698 |
ABC-2 family transporter protein; This family is related to the ABC-2 membrane transporter ... |
571-906 |
2.76e-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: 131.74 E-value: 2.76e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 571 VILMLIMGYGISMDVENLRFAVLDRDQTVSSQAWSLNLAGSRYFIEQPPLASYDELDRRMRSGELAVAIEIPPNFGRDIA 650
Cdd:pfam12698 15 ILLLGLIFSNAVNDPEELPVAVVDEDNSSLSRQLVRALEASPTVNLVQYVDSEEEAKEALKNGKIDGLLVIPKGFSKDLL 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 651 RGTPAQIGVWVDGAMPSRAETVKGYVQAMHQSWLQEAASRQPNPVKQVGLLNIETRYRYNPDVKSLPAIVPaVIPLLLMM 730
Cdd:pfam12698 95 KGESATVTVYINSSNLLVSKLILNALQSLLQQLNASALVLLLEALSTSAPIPVESTPLFNPQSGYAYYLVG-LILMIIIL 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 731 IPSMLSALSVVREKELGSMINLYVTPTTRSEFLLGKQLPYIALGMLNFLLLCALsVFVFGVPLKGSFlTLTLAALLYVII 810
Cdd:pfam12698 174 IGAAIIAVSIVEEKESRIKERLLVSGVSPLQYWLGKILGDFLVGLLQLLIILLL-LFGIGIPFGNLG-LLLLLFLLYGLA 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 811 ATGLGLLISTFMKSQIAAIFGTSIITLIPATqFSGMIDPVASLEGPGRWIGEIYPTSH----FLTIARGTFskaldLSDL 886
Cdd:pfam12698 252 YIALGYLLGSLFKNSEDAQSIIGIVILLLSG-FFGGLFPLEDPPSFLQWIFSIIPFFSpidgLLRLIYGDS-----LWEI 325
|
330 340
....*....|....*....|
gi 446125071 887 WPLFMPLLIAVPVVMGLSIL 906
Cdd:pfam12698 326 APSLIILLLFAVVLLLLALL 345
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
14-235 |
2.77e-33 |
|
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: 128.07 E-value: 2.77e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 14 QLEGVSQHYGKTVALNNITLDIPARSMVGLIGPDGVGKSSLL-------SLISGARVieQGNVIVLGGDMRDAKHRRDVC 86
Cdd:cd03260 2 ELRDLNVYYGDKHALKDISLDIPKGEITALIGPSGCGKSTLLrllnrlnDLIPGAPD--EGEVLLDGKDIYDLDVDVLEL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 87 PRIAWM----PqglgkNLYHtLSVYENVDFFARLFG-HDKAEREARITELLNSTGLAP-FRDRP-AGKLSGGMKQKLGLC 159
Cdd:cd03260 80 RRRVGMvfqkP-----NPFP-GSIYDNVAYGLRLHGiKLKEELDERVEEALRKAALWDeVKDRLhALGLSGGQQQRLCLA 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446125071 160 CALIHDPELLILDEPTTGVDPLSRAQFWDLIDSIRQRQTnmsVLVATAYMEEAERF-DWLVAMNAGEILATGSAQQL 235
Cdd:cd03260 154 RALANEPEVLLLDEPTSALDPISTAKIEELIAELKKEYT---IVIVTHNMQQAARVaDRTAFLLNGRLVEFGPTEQI 227
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
14-230 |
3.20e-33 |
|
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related proteins; ABC transporters, involved in the uptake of siderophores, heme, and vitamin B12, are widely conserved in bacteria and archaea. Only very few species lack representatives of the siderophore family transporters. The E. coli BtuCD protein is an ABC transporter mediating vitamin B12 uptake. The two ATP-binding cassettes (BtuD) are in close contact with each other, as are the two membrane-spanning subunits (BtuC); this arrangement is distinct from that observed for the E. coli lipid flippase MsbA. The BtuC subunits provide 20 transmembrane helices grouped around a translocation pathway that is closed to the cytoplasm by a gate region, whereas the dimer arrangement of the BtuD subunits resembles the ATP-bound form of the Rad50 DNA repair enzyme. A prominent cytoplasmic loop of BtuC forms the contact region with the ATP-binding cassette and represent a conserved motif among the ABC transporters.
Pssm-ID: 213181 [Multi-domain] Cd Length: 180 Bit Score: 126.40 E-value: 3.20e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 14 QLEGVSQHYGKTVALNNITLDIPARSMVGLIGPDGVGKSSLLSLISGARVIEQGNVIVLGGDMRDAKhRRDVCPRIAWMP 93
Cdd:cd03214 1 EVENLSVGYGGRTVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDGKDLASLS-PKELARKIAYVP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 94 QglgknlyhtlsvyenvdffarlfghdkaereariteLLNSTGLAPFRDRPAGKLSGGMKQKLGLCCALIHDPELLILDE 173
Cdd:cd03214 80 Q------------------------------------ALELLGLAHLADRPFNELSGGERQRVLLARALAQEPPILLLDE 123
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 446125071 174 PTTGVDPLSRAQFWDLIDSIRqRQTNMSVLVATAYMEEAERF-DWLVAMNAGEILATG 230
Cdd:cd03214 124 PTSHLDIAHQIELLELLRRLA-RERGKTVVMVLHDLNLAARYaDRVILLKDGRIVAQG 180
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
9-485 |
4.80e-33 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 134.53 E-value: 4.80e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 9 VPPVAQLEGVSQHYGKTVALNNITLDIPARSMVGLIGPDGVGKSSLLSLISGARVIEQGNVIVLGGDMRDAKHRRDVCPR 88
Cdd:PRK09700 2 ATPYISMAGIGKSFGPVHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNINYNKLDHKLAAQLG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 89 IAWMPQGLgkNLYHTLSVYENVdFFARL-----FG---HDKAEREARITELLNSTGLAPFRDRPAGKLSGGMKQKLGLCC 160
Cdd:PRK09700 82 IGIIYQEL--SVIDELTVLENL-YIGRHltkkvCGvniIDWREMRVRAAMMLLRVGLKVDLDEKVANLSISHKQMLEIAK 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 161 ALIHDPELLILDEPTTGvdpLSRAQFWDLIDSIRQ-RQTNMSVLVATAYMEEAERF-DWLVAMNAGEILATG-----SAQ 233
Cdd:PRK09700 159 TLMLDAKVIIMDEPTSS---LTNKEVDYLFLIMNQlRKEGTAIVYISHKLAEIRRIcDRYTVMKDGSSVCSGmvsdvSND 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 234 QLRAKTHSATLEQAFIALLPEAQRQAHKPVvippyhaeqeeiaIEAKDLTMRfgKFVAVDHVNFRIPRGEIFGFLGSNGC 313
Cdd:PRK09700 236 DIVRLMVGRELQNRFNAMKENVSNLAHETV-------------FEVRNVTSR--DRKKVRDISFSVCRGEILGFAGLVGS 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 314 GKSTTMKMLTGLLPASEGQAWLFGQPVDPND------------IDTRRRVGYMSQaFSLYNELTVRQNLELHAR-----L 376
Cdd:PRK09700 301 GRTELMNCLFGVDKRAGGEIRLNGKDISPRSpldavkkgmayiTESRRDNGFFPN-FSIAQNMAISRSLKDGGYkgamgL 379
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 377 FHIPPAEIPARVAQMIERFMLTEVEDTLpASLPLGIRQRLSLAVAVIHRPEMLILDEPTSGVDPVARDMFWQLMVDLSRQ 456
Cdd:PRK09700 380 FHEVDEQRTAENQRELLALKCHSVNQNI-TELSGGNQQKVLISKWLCCCPEVIIFDEPTRGIDVGAKAEIYKVMRQLADD 458
|
490 500
....*....|....*....|....*....
gi 446125071 457 DKVTIFISTHFMNEAERCDRMSLMHAGKV 485
Cdd:PRK09700 459 GKVILMVSSELPEIITVCDRIAVFCEGRL 487
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
276-497 |
6.40e-33 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 127.89 E-value: 6.40e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 276 AIEAKDLTMRF----------------------GKFVAVDHVNFRIPRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGQ- 332
Cdd:COG1134 4 MIEVENVSKSYrlyhepsrslkelllrrrrtrrEEFWALKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTSGRv 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 333 ------AWLFGqpvdpndidtrrrvgyMSQAFSlyNELTVRQNLELHARLFHIPPAEIPARVAQmIERFmlTEVEDTLpa 406
Cdd:COG1134 84 evngrvSALLE----------------LGAGFH--PELTGRENIYLNGRLLGLSRKEIDEKFDE-IVEF--AELGDFI-- 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 407 SLPL-----GIRQRLSLAVAVIHRPEMLILDEPTSGVDPVARDMFWQLMVDLSRQDKvTIFISTHFMNEAER-CDRMSLM 480
Cdd:COG1134 141 DQPVktyssGMRARLAFAVATAVDPDILLVDEVLAVGDAAFQKKCLARIRELRESGR-TVIFVSHSMGAVRRlCDRAIWL 219
|
250
....*....|....*..
gi 446125071 481 HAGKVLASGTPQELVQQ 497
Cdd:COG1134 220 EKGRLVMDGDPEEVIAA 236
|
|
| GldA_ABC_ATP |
TIGR03522 |
gliding motility-associated ABC transporter ATP-binding subunit GldA; Members of this protein ... |
18-248 |
9.28e-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: 129.12 E-value: 9.28e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 18 VSQHYGKTVALNNITLDIPARSMVGLIGPDGVGKSSLLSLISGARVIEQGNVIVLGGD-MRDAKhrrDVCPRIAWMPQGl 96
Cdd:TIGR03522 8 LTKLYGTQNALDEVSFEAQKGRIVGFLGPNGAGKSTTMKIITGYLPPDSGSVQVCGEDvLQNPK---EVQRNIGYLPEH- 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 97 gKNLYHTLSVYENVDFFARLFGHDKAEREARITELLNSTGLAPFRDRPAGKLSGGMKQKLGLCCALIHDPELLILDEPTT 176
Cdd:TIGR03522 84 -NPLYLDMYVREYLQFIAGIYGMKGQLLKQRVEEMIELVGLRPEQHKKIGQLSKGYRQRVGLAQALIHDPKVLILDEPTT 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446125071 177 GVDPLSRAQFWDLIDSIRQRQTnmsVLVATAYMEEAERF-DWLVAMNAGEILATGSAQQLRAKTHSATLEQAF 248
Cdd:TIGR03522 163 GLDPNQLVEIRNVIKNIGKDKT---IILSTHIMQEVEAIcDRVIIINKGKIVADKKLDELSAANKKQVIEVEF 232
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
272-497 |
1.00e-32 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 128.21 E-value: 1.00e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 272 QEEIaIEAKDLTMRF--GKFVAVDHVNFRIPRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGQAWLFGQPVDPNDI-DTR 348
Cdd:PRK13635 2 KEEI-IRVEHISFRYpdAATYALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGGMVLSEETVwDVR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 349 RRVGYMSQ---------------AFSLYNEltvrqnlelharlfHIPPAEIPARVAQMIERFMLTEVEDTLPASLPLGIR 413
Cdd:PRK13635 81 RQVGMVFQnpdnqfvgatvqddvAFGLENI--------------GVPREEMVERVDQALRQVGMEDFLNREPHRLSGGQK 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 414 QRLSLAVAVIHRPEMLILDEPTSGVDPVARDMFWQLMVDLSRQDKVTIFISTHFMNEAERCDRMSLMHAGKVLASGTPQE 493
Cdd:PRK13635 147 QRVAIAGVLALQPDIIILDEATSMLDPRGRREVLETVRQLKEQKGITVLSITHDLDEAAQADRVIVMNKGEILEEGTPEE 226
|
....
gi 446125071 494 LVQQ 497
Cdd:PRK13635 227 IFKS 230
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
273-497 |
1.61e-32 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 127.51 E-value: 1.61e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 273 EEIAIEAKDLTMRF-----GKF-VAVDHVNFRIPRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGQAWLFGqpVDPNDI- 345
Cdd:PRK13633 1 MNEMIKCKNVSYKYesneeSTEkLALDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVYVDG--LDTSDEe 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 346 ---DTRRRVGYMSQafSLYNELT---VRQNLELHARLFHIPPAEIPARVAQMIERFMLTEVEDTLPASLPLGIRQRLSLA 419
Cdd:PRK13633 79 nlwDIRNKAGMVFQ--NPDNQIVatiVEEDVAFGPENLGIPPEEIRERVDESLKKVGMYEYRRHAPHLLSGGQKQRVAIA 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446125071 420 VAVIHRPEMLILDEPTSGVDPVARDMFWQLMVDLSRQDKVTIFISTHFMNEAERCDRMSLMHAGKVLASGTPQELVQQ 497
Cdd:PRK13633 157 GILAMRPECIIFDEPTAMLDPSGRREVVNTIKELNKKYGITIILITHYMEEAVEADRIIVMDSGKVVMEGTPKEIFKE 234
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
269-494 |
1.94e-32 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 126.69 E-value: 1.94e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 269 HAEQEEIAIEAKDLTMRFGKFVAVDHVNFRIPRGEIFGFLGSNGCGKSTTMKML---TGLLPAS--EGQAWLFGQP---- 339
Cdd:COG1117 4 PASTLEPKIEVRNLNVYYGDKQALKDINLDIPENKVTALIGPSGCGKSTLLRCLnrmNDLIPGArvEGEILLDGEDiydp 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 340 -VDPNDIdtRRRVGYMSQ-----AFSLYNeltvrqNLELHARLFHI-PPAEIPARVAQMIERFML-TEVEDTL--PA-SL 408
Cdd:COG1117 84 dVDVVEL--RRRVGMVFQkpnpfPKSIYD------NVAYGLRLHGIkSKSELDEIVEESLRKAALwDEVKDRLkkSAlGL 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 409 PLGIRQRLSLAVAVIHRPEMLILDEPTSGVDPVARDMFWQLMVDLSrqDKVTIFISTHFMNEAERC-DRMSLMHAGKVLA 487
Cdd:COG1117 156 SGGQQQRLCIARALAVEPEVLLMDEPTSALDPISTAKIEELILELK--KDYTIVIVTHNMQQAARVsDYTAFFYLGELVE 233
|
....*..
gi 446125071 488 SGTPQEL 494
Cdd:COG1117 234 FGPTEQI 240
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
291-499 |
2.81e-32 |
|
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim protein) in eukaryotes. It is the member of ABC transporter superfamily. Rim protein is a membrane glycoprotein which is localized in the photoreceptor outer segment discs. Mutation/s in its genetic loci is implicated in the recessive Stargardt's disease. [Transport and binding proteins, Other]
Pssm-ID: 130324 [Multi-domain] Cd Length: 2272 Bit Score: 136.30 E-value: 2.81e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 291 AVDHVNFRIPRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGQAWLFGQPVDPNDIDTRRRVGYMSQAFSLYNELTVRQNL 370
Cdd:TIGR01257 1954 AVDRLCVGVRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAGKSILTNISDVHQNMGYCPQFDAIDDLLTGREHL 2033
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 371 ELHARLFHIPPAEIPARVAQMIERFMLTEVEDTLPASLPLGIRQRLSLAVAVIHRPEMLILDEPTSGVDPVARDMFWQLM 450
Cdd:TIGR01257 2034 YLYARLRGVPAEEIEKVANWSIQSLGLSLYADRLAGTYSGGNKRKLSTAIALIGCPPLVLLDEPTTGMDPQARRMLWNTI 2113
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 446125071 451 VDLSRQDKVTIfISTHFMNEAER-CDRMSLMHAGKVLASGTPQELVQQRG 499
Cdd:TIGR01257 2114 VSIIREGRAVV-LTSHSMEECEAlCTRLAIMVKGAFQCLGTIQHLKSKFG 2162
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
15-246 |
4.02e-32 |
|
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: 125.49 E-value: 4.02e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 15 LEGVSQHYGK-TVALNNITLDIPARSMVGLIGPDGVGKSSLLSLISgaRVIE--QGNVIVLGGDMRD---AKHRRdvcpR 88
Cdd:cd03295 3 FENVTKRYGGgKKAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMIN--RLIEptSGEIFIDGEDIREqdpVELRR----K 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 89 IAWMPQGLGknLYHTLSVYENVDFFARLFGHDKAEREARITELLNSTGLAP--FRDRPAGKLSGGMKQKLGLCCALIHDP 166
Cdd:cd03295 77 IGYVIQQIG--LFPHMTVEENIALVPKLLKWPKEKIRERADELLALVGLDPaeFADRYPHELSGGQQQRVGVARALAADP 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 167 ELLILDEPTTGVDPLSRAQFWDLIDSIrQRQTNMSVLVATAYMEEAERF-DWLVAMNAGEILATGSAQQLRAKTHSATLE 245
Cdd:cd03295 155 PLLLMDEPFGALDPITRDQLQEEFKRL-QQELGKTIVFVTHDIDEAFRLaDRIAIMKNGEIVQVGTPDEILRSPANDFVA 233
|
.
gi 446125071 246 Q 246
Cdd:cd03295 234 E 234
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
14-498 |
5.33e-32 |
|
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: 131.10 E-value: 5.33e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 14 QLEGVSQHYGKTVALNNITLDIPARSMVGLIGPDGVGKSSLLSLISGarVIEQGNV---IVLGGDMRDAKHRRDVCPR-I 89
Cdd:TIGR02633 3 EMKGIVKTFGGVKALDGIDLEVRPGECVGLCGENGAGKSTLMKILSG--VYPHGTWdgeIYWSGSPLKASNIRDTERAgI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 90 AWMPQGLgkNLYHTLSVYENVdFFARLFGH-----DKAEREARITELLNSTGLAPFRD-RPAGKLSGGMKQKLGLCCALI 163
Cdd:TIGR02633 81 VIIHQEL--TLVPELSVAENI-FLGNEITLpggrmAYNAMYLRAKNLLRELQLDADNVtRPVGDYGGGQQQLVEIAKALN 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 164 HDPELLILDEPTTGvdpLSRAQFWDLIDSIRQ-RQTNMSVLVATAYMEEAERF-DWLVAMNAGEILATGSAQQLRakths 241
Cdd:TIGR02633 158 KQARLLILDEPSSS---LTEKETEILLDIIRDlKAHGVACVYISHKLNEVKAVcDTICVIRDGQHVATKDMSTMS----- 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 242 atlEQAFIALLPEAQRQA---HKPvvippyHAEQEEIaIEAKDLTMRF---GKFVAVDHVNFRIPRGEIFGFLGSNGCGK 315
Cdd:TIGR02633 230 ---EDDIITMMVGREITSlypHEP------HEIGDVI-LEARNLTCWDvinPHRKRVDDVSFSLRRGEILGVAGLVGAGR 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 316 STTMKMLTGLLP-ASEGQAWLFGQPVD---------------PNDidtRRRVGYMSQafslyneLTVRQNLEL-----HA 374
Cdd:TIGR02633 300 TELVQALFGAYPgKFEGNVFINGKPVDirnpaqairagiamvPED---RKRHGIVPI-------LGVGKNITLsvlksFC 369
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 375 RLFHIPPAEIPARVAQMIERFMLTEVEDTLP-ASLPLGIRQRLSLAVAVIHRPEMLILDEPTSGVDPVARDMFWQLMVDL 453
Cdd:TIGR02633 370 FKMRIDAAAELQIIGSAIQRLKVKTASPFLPiGRLSGGNQQKAVLAKMLLTNPRVLILDEPTRGVDVGAKYEIYKLINQL 449
|
490 500 510 520
....*....|....*....|....*....|....*....|....*
gi 446125071 454 SRQDKVTIFISTHFMNEAERCDRMSLMHAGKVLASGTPQELVQQR 498
Cdd:TIGR02633 450 AQEGVAIIVVSSELAEVLGLSDRVLVIGEGKLKGDFVNHALTQEQ 494
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
14-225 |
5.57e-32 |
|
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: 121.97 E-value: 5.57e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 14 QLEGVSQHYGKTVALNNITLDIPARSMVGLIGPDGVGKSSLLSLISGARVIEQGNVIVLG---GDMRDAKHRRdvcpRIA 90
Cdd:cd00267 1 EIENLSFRYGGRTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGkdiAKLPLEELRR----RIG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 91 WMPQglgknlyhtlsvyenvdffarlfghdkaerearitellnstglapfrdrpagkLSGGMKQKLGLCCALIHDPELLI 170
Cdd:cd00267 77 YVPQ-----------------------------------------------------LSGGQRQRVALARALLLNPDLLL 103
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 446125071 171 LDEPTTGVDPLSRAQFWDLIDSIRQRqtNMSVLVATAYMEEAERF-DWLVAMNAGE 225
Cdd:cd00267 104 LDEPTSGLDPASRERLLELLRELAEE--GRTVIIVTHDPELAELAaDRVIVLKDGK 157
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
14-230 |
8.01e-32 |
|
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: 124.16 E-value: 8.01e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 14 QLEGVSQHY----GKTVALNNITLDIPARSMVGLIGPDGVGKSSLLSLISGARVIEQGNVIVLGGDM--RDAKHRRDVCP 87
Cdd:cd03257 3 EVKNLSVSFptggGSVKALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGKDLlkLSRRLRKIRRK 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 88 RIAWMPQGLGKNLYHTLSVYENVD--FFARLFGHDKAEREARITELLNSTGLAP-FRDRPAGKLSGGMKQKLGLCCALIH 164
Cdd:cd03257 83 EIQMVFQDPMSSLNPRMTIGEQIAepLRIHGKLSKKEARKEAVLLLLVGVGLPEeVLNRYPHELSGGQRQRVAIARALAL 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446125071 165 DPELLILDEPTTGVDPLSRAQFWDLIDSIrQRQTNMSVLVAT------AYMeeAERfdwLVAMNAGEILATG 230
Cdd:cd03257 163 NPKLLIADEPTSALDVSVQAQILDLLKKL-QEELGLTLLFIThdlgvvAKI--ADR---VAVMYAGKIVEEG 228
|
|
| galliderm_ABC |
TIGR03740 |
gallidermin-class lantibiotic protection ABC transporter, ATP-binding subunit; Model TIGR03731 ... |
14-213 |
8.66e-32 |
|
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: 123.66 E-value: 8.66e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 14 QLEGVSQHYGKTVALNNITLDIPARSMVGLIGPDGVGKSSLLSLISGARVIEQGNVIVLGGDMrDAKHRRDVCPRIAWMP 93
Cdd:TIGR03740 2 ETKNLSKRFGKQTAVNNISLTVPKNSVYGLLGPNGAGKSTLLKMITGILRPTSGEIIFDGHPW-TRKDLHKIGSLIESPP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 94 qglgknLYHTLSVYENVDFFARLFGHDkaerEARITELLNSTGLAPFRDRPAGKLSGGMKQKLGLCCALIHDPELLILDE 173
Cdd:TIGR03740 81 ------LYENLTARENLKVHTTLLGLP----DSRIDEVLNIVDLTNTGKKKAKQFSLGMKQRLGIAIALLNHPKLLILDE 150
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 446125071 174 PTTGVDPLSRAQFWDLIDSIRQRqtNMSVLVATAYMEEAE 213
Cdd:TIGR03740 151 PTNGLDPIGIQELRELIRSFPEQ--GITVILSSHILSEVQ 188
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
14-225 |
1.43e-31 |
|
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is comprised of all BPD (Binding Protein Dependent) systems that are largely represented in archaea and eubacteria and are primarily involved in scavenging solutes from the environment. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213196 [Multi-domain] Cd Length: 178 Bit Score: 121.53 E-value: 1.43e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 14 QLEGVSQHYGKTVALNNITLDIPARSMVGLIGPDGVGKSSLLSLISGARVIEQGNVIVLGGD-MRDAKHRRDVCPRIAWM 92
Cdd:cd03229 2 ELKNVSKRYGQKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGEDlTDLEDELPPLRRRIGMV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 93 PQGLgkNLYHTLSVYENVDFfarlfghdkaerearitellnstglapfrdrpagKLSGGMKQKLGLCCALIHDPELLILD 172
Cdd:cd03229 82 FQDF--ALFPHLTVLENIAL----------------------------------GLSGGQQQRVALARALAMDPDVLLLD 125
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 446125071 173 EPTTGVDPLSRAQFWDLIDSIRQRQtNMSVLVATAYMEEAERF-DWLVAMNAGE 225
Cdd:cd03229 126 EPTSALDPITRREVRALLKSLQAQL-GITVVLVTHDLDEAARLaDRVVVLRDGK 178
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
246-499 |
1.50e-31 |
|
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease components [Energy production and conversion, Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 444012 [Multi-domain] Cd Length: 563 Bit Score: 130.65 E-value: 1.50e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 246 QAFIALLPEAQRQAHKPVVIPpyhaeqEEIAIEAKDLTMRF-GKFVAVDHVNFRIPRGEIFGFLGSNGCGKSTTMKMLTG 324
Cdd:COG4988 312 FALLDAPEPAAPAGTAPLPAA------GPPSIELEDVSFSYpGGRPALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLG 385
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 325 LLPASEGQAWLFGQPVDPNDIDT-RRRVGYMSQAFSLYNElTVRQNLELHArlfhiPPAEiPARVAQMIERFMLTEVEDT 403
Cdd:COG4988 386 FLPPYSGSILINGVDLSDLDPASwRRQIAWVPQNPYLFAG-TIRENLRLGR-----PDAS-DEELEAALEAAGLDEFVAA 458
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 404 LPASL--PL---------GIRQRLSLAVAVIHRPEMLILDEPTSGVDPVARDMFWQLMVDLSRQdkVTIFISTHFMNEAE 472
Cdd:COG4988 459 LPDGLdtPLgeggrglsgGQAQRLALARALLRDAPLLLLDEPTAHLDAETEAEILQALRRLAKG--RTVILITHRLALLA 536
|
250 260
....*....|....*....|....*..
gi 446125071 473 RCDRMSLMHAGKVLASGTPQELVQQRG 499
Cdd:COG4988 537 QADRILVLDDGRIVEQGTHEELLAKNG 563
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
278-485 |
2.37e-31 |
|
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of the ABC component of a cobalt transport family found in bacteria, archaea, and eukaryota. The transition metal cobalt is an essential component of many enzymes and must be transported into cells in appropriate amounts when needed. The CbiMNQO family ABC transport system is involved in cobalt transport in association with the cobalamin (vitamin B12) biosynthetic pathways. Most cobalt (Cbi) transport systems possess a separate CbiN component, the cobalt-binding periplasmic protein, and they are encoded by the conserved gene cluster cbiMNQO. Both the CbiM and CbiQ proteins are integral cytoplasmic membrane proteins, and the CbiO protein has the linker peptide and the Walker A and B motifs commonly found in the ATPase components of the ABC-type transport systems.
Pssm-ID: 213193 [Multi-domain] Cd Length: 205 Bit Score: 121.98 E-value: 2.37e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 278 EAKDLTMRFGKFV-AVDHVNFRIPRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGQAWLFGQPVDPNDidTRRRVGYMSQ 356
Cdd:cd03226 1 RIENISFSYKKGTeILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLNGKPIKAKE--RRKSIGYVMQ 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 357 --AFSLYNElTVRQNLELHARlfhiPPAEIPARVAQMIERFMLTEVEDTLPASLPLGIRQRLSLAVAVIHRPEMLILDEP 434
Cdd:cd03226 79 dvDYQLFTD-SVREELLLGLK----ELDAGNEQAETVLKDLDLYALKERHPLSLSGGQKQRLAIAAALLSGKDLLIFDEP 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 446125071 435 TSGVDPVARDMFWQLMVDLSRQDKvTIFISTH---FMneAERCDRMSLMHAGKV 485
Cdd:cd03226 154 TSGLDYKNMERVGELIRELAAQGK-AVIVITHdyeFL--AKVCDRVLLLANGAI 204
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
14-235 |
2.39e-31 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 126.34 E-value: 2.39e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 14 QLEGVSQHYGKTVALNNITLDIPARSMVGLIGPDGVGKSSLLSLISGARVIEQGNvIVLGGdmRDAKH----RRDvcprI 89
Cdd:COG3839 5 ELENVSKSYGGVEALKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAGLEDPTSGE-ILIGG--RDVTDlppkDRN----I 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 90 AWMPQGLGknLYHTLSVYENVDFFARLFGHDKAEREARITELLNSTGLAPFRDRPAGKLSGGMKQKLGLCCALIHDPELL 169
Cdd:COG3839 78 AMVFQSYA--LYPHMTVYENIAFPLKLRKVPKAEIDRRVREAAELLGLEDLLDRKPKQLSGGQRQRVALGRALVREPKVF 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446125071 170 ILDEPTTGVDPLSRAQfwdLIDSIR--QRQTNMSVLVATAYMEEAERF-DWLVAMNAGEILATGSAQQL 235
Cdd:COG3839 156 LLDEPLSNLDAKLRVE---MRAEIKrlHRRLGTTTIYVTHDQVEAMTLaDRIAVMNDGRIQQVGTPEEL 221
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
277-484 |
3.00e-31 |
|
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP (Multidrug Resistance Protein)-like transporters are involved in drug, peptide, and lipid export. They belong to the subfamily C of the ATP-binding cassette (ABC) superfamily of transport proteins. The ABCC subfamily contains transporters with a diverse functional spectrum that includes ion transport, cell surface receptor, and toxin secretion activities. The MRP-like family, similar to all ABC proteins, have a common four-domain core structure constituted by two membrane-spanning domains, each composed of six transmembrane (TM) helices, and two nucleotide-binding domains (NBD). ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213195 [Multi-domain] Cd Length: 171 Bit Score: 120.18 E-value: 3.00e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 277 IEAKDLTMRFG--KFVAVDHVNFRIPRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGQAWLFGQPVDPNDIDT-RRRVGY 353
Cdd:cd03228 1 IEFKNVSFSYPgrPKPVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGVDLRDLDLESlRKNIAY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 354 MSQAFSLYNElTVRQNLelharlfhippaeiparvaqmierfmltevedtlpasLPLGIRQRLSLAVAVIHRPEMLILDE 433
Cdd:cd03228 81 VPQDPFLFSG-TIRENI-------------------------------------LSGGQRQRIAIARALLRDPPILILDE 122
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 446125071 434 PTSGVDPVARDMFWQLMVDLSRqdKVTIFISTHFMNEAERCDRMSLMHAGK 484
Cdd:cd03228 123 ATSALDPETEALILEALRALAK--GKTVIVIAHRLSTIRDADRIIVLDDGR 171
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
14-256 |
4.13e-31 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 125.19 E-value: 4.13e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 14 QLEGVSQHY----GKTVALNNITLDIPARSMVGLIGPDGVGKSSLLSLISGARVIEQGNVIVLGGDM--------RDAkh 81
Cdd:COG1135 3 ELENLSKTFptkgGPVTALDDVSLTIEKGEIFGIIGYSGAGKSTLIRCINLLERPTSGSVLVDGVDLtalserelRAA-- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 82 RRdvcpRIAWMPQGLgkNLYHTLSVYENVDFFARLFGHDKAEREARITELLNSTGLAPFRDR-PAgKLSGGMKQKLGLCC 160
Cdd:COG1135 81 RR----KIGMIFQHF--NLLSSRTVAENVALPLEIAGVPKAEIRKRVAELLELVGLSDKADAyPS-QLSGGQKQRVGIAR 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 161 ALIHDPELLILDEPTTGVDPLSRAQFWDLIDSIRQRqTNMSVLVATAYMEE----AERfdwlVA-MNAGEILATGSAQQL 235
Cdd:COG1135 154 ALANNPKVLLCDEATSALDPETTRSILDLLKDINRE-LGLTIVLITHEMDVvrriCDR----VAvLENGRIVEQGPVLDV 228
|
250 260
....*....|....*....|.
gi 446125071 236 RAKTHSATLeQAFIALLPEAQ 256
Cdd:COG1135 229 FANPQSELT-RRFLPTVLNDE 248
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
10-248 |
1.42e-30 |
|
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA [Inorganic ion transport and metabolism];
Pssm-ID: 440736 [Multi-domain] Cd Length: 250 Bit Score: 120.96 E-value: 1.42e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 10 PPVAQLEGVSQHYGKTVALNNITLDIPARSMVGLIGPDGVGKSSLLSLISGARVIEQGNVIVLGG------DMRDAKhrr 83
Cdd:COG1119 1 DPLLELRNVTVRRGGKTILDDISWTVKPGEHWAILGPNGAGKSTLLSLITGDLPPTYGNDVRLFGerrggeDVWELR--- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 84 dvcPRIAWMPQGLGKNLYHTLSVYENV--DFFA--RLFGHDKAEREARITELLNSTGLAPFRDRPAGKLSGGMKQKLGLC 159
Cdd:COG1119 78 ---KRIGLVSPALQLRFPRDETVLDVVlsGFFDsiGLYREPTDEQRERARELLELLGLAHLADRPFGTLSQGEQRRVLIA 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 160 CALIHDPELLILDEPTTGVDPLSRAQFWDLIDSIRQRQTNMSVLVaTAYMEEA-ERFDWLVAMNAGEILATGSAQQLRAk 238
Cdd:COG1119 155 RALVKDPELLILDEPTAGLDLGARELLLALLDKLAAEGAPTLVLV-THHVEEIpPGITHVLLLKDGRVVAAGPKEEVLT- 232
|
250
....*....|
gi 446125071 239 thSATLEQAF 248
Cdd:COG1119 233 --SENLSEAF 240
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
302-489 |
1.68e-30 |
|
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: 119.71 E-value: 1.68e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 302 GEIFGFLGSNGCGKSTTMKMLTGLLPASEGQAWLFGQPVDP--NDID---TRRRVGYMSQAFSLYNELTVRQNLELHARL 376
Cdd:cd03297 23 EEVTGIFGASGAGKSTLLRCIAGLEKPDGGTIVLNGTVLFDsrKKINlppQQRKIGLVFQQYALFPHLNVRENLAFGLKR 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 377 fhIPPAEIPARVAQMIERFMLTEVEDTLPASLPLGIRQRLSLAVAVIHRPEMLILDEPTSGVDPVARDMFWQLMVDLSRQ 456
Cdd:cd03297 103 --KRNREDRISVDELLDLLGLDHLLNRYPAQLSGGEKQRVALARALAAQPELLLLDEPFSALDRALRLQLLPELKQIKKN 180
|
170 180 190
....*....|....*....|....*....|....
gi 446125071 457 DKVTIFISTHFMNEAER-CDRMSLMHAGKVLASG 489
Cdd:cd03297 181 LNIPVIFVTHDLSEAEYlADRIVVMEDGRLQYIG 214
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
277-498 |
1.90e-30 |
|
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: 120.37 E-value: 1.90e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 277 IEAKDLTMRFG-KFVAVDHVNFRIPRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGQAWLFGQPV---DPNDI-DTRRRV 351
Cdd:cd03256 1 IEVENLSKTYPnGKKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGTDInklKGKALrQLRRQI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 352 GYMSQAFSLYNELTVRQNLeLHARLFHI----------PPAEIPaRVAQMIERFMLTEVEDTLPASLPLGIRQRLSLAVA 421
Cdd:cd03256 81 GMIFQQFNLIERLSVLENV-LSGRLGRRstwrslfglfPKEEKQ-RALAALERVGLLDKAYQRADQLSGGQQQRVAIARA 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446125071 422 VIHRPEMLILDEPTSGVDPVARDMFWQLMVDLSRQDKVTIFISTHFMNEAER-CDRMSLMHAGKVLASGTPQELVQQR 498
Cdd:cd03256 159 LMQQPKLILADEPVASLDPASSRQVMDLLKRINREEGITVIVSLHQVDLAREyADRIVGLKDGRIVFDGPPAELTDEV 236
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
29-464 |
2.03e-30 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 126.74 E-value: 2.03e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 29 NNITLDIPARSMVGLIGPDGVGKS----SLLSLI-SGARVIEQGNVIVLGGDMRDAKHR--RDV-CPRIAWMPQ------ 94
Cdd:PRK15134 26 NDVSLQIEAGETLALVGESGSGKSvtalSILRLLpSPPVVYPSGDIRFHGESLLHASEQtlRGVrGNKIAMIFQepmvsl 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 95 ----GLGKNLYHTLSVYenvdffaRLFGHDKAEREarITELLNSTGL--APFR--DRPAgKLSGGMKQKLGLCCALIHDP 166
Cdd:PRK15134 106 nplhTLEKQLYEVLSLH-------RGMRREAARGE--ILNCLDRVGIrqAAKRltDYPH-QLSGGERQRVMIAMALLTRP 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 167 ELLILDEPTTGVDPLSRAQFWDLIDSIRQrQTNMSVLVATAYMEEAERF-DWLVAMNAGEILATGSAQQL-RAKTHSATl 244
Cdd:PRK15134 176 ELLIADEPTTALDVSVQAQILQLLRELQQ-ELNMGLLFITHNLSIVRKLaDRVAVMQNGRCVEQNRAATLfSAPTHPYT- 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 245 eQAFIALLPEAQrqahkPVVIPpyhaEQEEIAIEAKDLTMRF-----------GKFVAVDHVNFRIPRGEIFGFLGSNGC 313
Cdd:PRK15134 254 -QKLLNSEPSGD-----PVPLP----EPASPLLDVEQLQVAFpirkgilkrtvDHNVVVKNISFTLRPGETLGLVGESGS 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 314 GKSTTMKMLTGLLpASEGQAWLFGQPVDPND----IDTRRRVGYMSQ--AFSLYNELTVRQ----NLELHARlfHIPPAE 383
Cdd:PRK15134 324 GKSTTGLALLRLI-NSQGEIWFDGQPLHNLNrrqlLPVRHRIQVVFQdpNSSLNPRLNVLQiieeGLRVHQP--TLSAAQ 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 384 IPARVAQMIERFML-TEVEDTLPASLPLGIRQRLSLAVAVIHRPEMLILDEPTSGVDPVARDMFWQLMVDLSRQDKVT-I 461
Cdd:PRK15134 401 REQQVIAVMEEVGLdPETRHRYPAEFSGGQRQRIAIARALILKPSLIILDEPTSSLDKTVQAQILALLKSLQQKHQLAyL 480
|
...
gi 446125071 462 FIS 464
Cdd:PRK15134 481 FIS 483
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
9-485 |
3.04e-30 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 125.93 E-value: 3.04e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 9 VPPVAQLEGVSQHYGKTVALNNITLDIPARSMVGLIGPDGVGKSSLLSLISGARVIEQGNVIVLGgdmrdaKHRRDVCPR 88
Cdd:PRK15439 8 APPLLCARSISKQYSGVEVLKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIGG------NPCARLTPA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 89 IAwmpQGLG-------KNLYHTLSVYENVDFfaRLFGHDKAEReaRITELLNSTGLAPFRDRPAGKLSGGMKQKLGLCCA 161
Cdd:PRK15439 82 KA---HQLGiylvpqePLLFPNLSVKENILF--GLPKRQASMQ--KMKQLLAALGCQLDLDSSAGSLEVADRQIVEILRG 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 162 LIHDPELLILDEPTTGVDPLSRAQFWDLIDSIRQRQTNMsVLVATAYMEEAERFDWLVAMNAGEILATGSAQQL------ 235
Cdd:PRK15439 155 LMRDSRILILDEPTASLTPAETERLFSRIRELLAQGVGI-VFISHKLPEIRQLADRISVMRDGTIALSGKTADLstddii 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 236 -----RAKTHSATLEQAFIALLPEAQRQ--AHKPVvippyhaeqeeiaIEAKDLTmrfGK-FVavdHVNFRIPRGEIFGF 307
Cdd:PRK15439 234 qaitpAAREKSLSASQKLWLELPGNRRQqaAGAPV-------------LTVEDLT---GEgFR---NISLEVRAGEILGL 294
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 308 LGSNGCGKSTTMKMLTGLLPASEGQAWLFGQPVDPNDIDTRRRVG--YMS---QAFSLYNELTVRQNLelHARLFHIPPA 382
Cdd:PRK15439 295 AGVVGAGRTELAETLYGLRPARGGRIMLNGKEINALSTAQRLARGlvYLPedrQSSGLYLDAPLAWNV--CALTHNRRGF 372
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 383 EI-PARVAQMIERF------MLTEVEDTLpASLPLGIRQRLSLAVAVIHRPEMLILDEPTSGVDPVARDMFWQLMVDLSR 455
Cdd:PRK15439 373 WIkPARENAVLERYrralniKFNHAEQAA-RTLSGGNQQKVLIAKCLEASPQLLIVDEPTRGVDVSARNDIYQLIRSIAA 451
|
490 500 510
....*....|....*....|....*....|.
gi 446125071 456 QDKVTIFISTHFmNEAER-CDRMSLMHAGKV 485
Cdd:PRK15439 452 QNVAVLFISSDL-EEIEQmADRVLVMHQGEI 481
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
274-514 |
3.69e-30 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 120.48 E-value: 3.69e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 274 EIAIEAKDLTMRFGKFV--AVDHVNFRIPRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGQAWLFGQPVDPNDID-TRRR 350
Cdd:PRK13632 5 SVMIKVENVSFSYPNSEnnALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIDGITISKENLKeIRKK 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 351 VGYMSQ---------------AFSLYNELtvrqnlelharlfhIPPAEIPARVAQMIERFMLTEVEDTLPASLPLGIRQR 415
Cdd:PRK13632 85 IGIIFQnpdnqfigatveddiAFGLENKK--------------VPPKKMKDIIDDLAKKVGMEDYLDKEPQNLSGGQKQR 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 416 LSLAVAVIHRPEMLILDEPTSGVDPVARDMFWQLMVDLSRQDKVTIFISTHFMNEAERCDRMSLMHAGKVLASGTPQELV 495
Cdd:PRK13632 151 VAIASVLALNPEIIIFDESTSMLDPKGKREIKKIMVDLRKTRKKTLISITHDMDEAILADKVIVFSEGKLIAQGKPKEIL 230
|
250 260
....*....|....*....|..
gi 446125071 496 QQRG---AANLEAAFISWLQEA 514
Cdd:PRK13632 231 NNKEileKAKIDSPFIYKLSKK 252
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
1-235 |
6.43e-30 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 119.37 E-value: 6.43e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 1 MTSlTLVPVPPVAQLEGVSQHYGKTVALNNITLDIPARSMVGLIGPDGVGKSSLLS-------LISGARVieQGNVIVLG 73
Cdd:COG1117 1 MTA-PASTLEPKIEVRNLNVYYGDKQALKDINLDIPENKVTALIGPSGCGKSTLLRclnrmndLIPGARV--EGEILLDG 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 74 GDMRDAK-----HRRdvcpRIAWMPQglgK-NLYhTLSVYENVDFFARLFG-HDKAEREARITELLNSTGLAP-FRDR-- 143
Cdd:COG1117 78 EDIYDPDvdvveLRR----RVGMVFQ---KpNPF-PKSIYDNVAYGLRLHGiKSKSELDEIVEESLRKAALWDeVKDRlk 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 144 -PAGKLSGGMKQKLglcC---ALIHDPELLILDEPTTGVDPLSRAQFWDLIDSIRQRQTnmsVLVATAYMEEAERF-DWL 218
Cdd:COG1117 150 kSALGLSGGQQQRL---CiarALAVEPEVLLMDEPTSALDPISTAKIEELILELKKDYT---IVIVTHNMQQAARVsDYT 223
|
250
....*....|....*..
gi 446125071 219 VAMNAGEILATGSAQQL 235
Cdd:COG1117 224 AFFYLGELVEFGPTEQI 240
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
10-238 |
7.08e-30 |
|
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease components [Energy production and conversion, Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 444012 [Multi-domain] Cd Length: 563 Bit Score: 125.64 E-value: 7.08e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 10 PPVAQLEGVS-QHYGKTVALNNITLDIPARSMVGLIGPDGVGKSSLLSLISGARVIEQGNVIVLGGDMRDAKhRRDVCPR 88
Cdd:COG4988 334 PPSIELEDVSfSYPGGRPALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPPYSGSILINGVDLSDLD-PASWRRQ 412
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 89 IAWMPQglgkN--LYHTlSVYENVdffarLFGHDKAErEARITELLNSTGLAPF-RDRPAG----------KLSGGMKQK 155
Cdd:COG4988 413 IAWVPQ----NpyLFAG-TIRENL-----RLGRPDAS-DEELEAALEAAGLDEFvAALPDGldtplgeggrGLSGGQAQR 481
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 156 LGLCCALIHDPELLILDEPTTGVDPLSRAQFWDLIDSIRQRQTnmsVLVATAYMEEAERFDWLVAMNAGEILATGSAQQL 235
Cdd:COG4988 482 LALARALLRDAPLLLLDEPTAHLDAETEAEILQALRRLAKGRT---VILITHRLALLAQADRILVLDDGRIVEQGTHEEL 558
|
...
gi 446125071 236 RAK 238
Cdd:COG4988 559 LAK 561
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
277-493 |
8.90e-30 |
|
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: 118.21 E-value: 8.90e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 277 IEAKDLTMRFGKFVaVDHVNFRIPRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGQAWLFGQpvdpnDIDT----RRRVG 352
Cdd:cd03299 1 LKVENLSKDWKEFK-LKNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNGK-----DITNlppeKRDIS 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 353 YMSQAFSLYNELTVRQNLELHARLFHIPPAEIPARVAQMIERFMLTEVEDTLPASLPLGIRQRLSLAVAVIHRPEMLILD 432
Cdd:cd03299 75 YVPQNYALFPHMTVYKNIAYGLKKRKVDKKEIERKVLEIAEMLGIDHLLNRKPETLSGGEQQRVAIARALVVNPKILLLD 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446125071 433 EPTSGVDPVARDMFWQLMVDLSRQDKVTIFISTHFMNEAER-CDRMSLMHAGKVLASGTPQE 493
Cdd:cd03299 155 EPFSALDVRTKEKLREELKKIRKEFGVTVLHVTHDFEEAWAlADKVAIMLNGKLIQVGKPEE 216
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
277-494 |
8.97e-30 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 118.94 E-value: 8.97e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 277 IEAKDLTMRFGKFVAVDHVNFRIPRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGQAWLFGQPVD--PNDIDTRRRVGYM 354
Cdd:PRK11300 6 LSVSGLMMRFGGLLAVNNVNLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTILLRGQHIEglPGHQIARMGVVRT 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 355 SQAFSLYNELTVRQNL----------ELHARLFHIPP-----AEIPARVAQMIERFMLTEVEDTLPASLPLGIRQRLSLA 419
Cdd:PRK11300 86 FQHVRLFREMTVIENLlvaqhqqlktGLFSGLLKTPAfrraeSEALDRAATWLERVGLLEHANRQAGNLAYGQQRRLEIA 165
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446125071 420 VAVIHRPEMLILDEPTSGVDPVARDMFWQLMVDLSRQDKVTIFISTHFMNEA-ERCDRMSLMHAGKVLASGTPQEL 494
Cdd:PRK11300 166 RCMVTQPEILMLDEPAAGLNPKETKELDELIAELRNEHNVTVLLIEHDMKLVmGISDRIYVVNQGTPLANGTPEEI 241
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
277-490 |
9.89e-30 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 121.45 E-value: 9.89e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 277 IEAKDLTMRF----GKFVAVDHVNFRIPRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGQAWlfgqpVDPNDIDT----- 347
Cdd:PRK11153 2 IELKNISKVFpqggRTIHALNNVSLHIPAGEIFGVIGASGAGKSTLIRCINLLERPTSGRVL-----VDGQDLTAlseke 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 348 ----RRRVGYMSQAFSLYNELTVRQNLELHARLFHIPPAEIPARVAQMIERFMLTEVEDTLPASLPLGIRQRLSLAVAVI 423
Cdd:PRK11153 77 lrkaRRQIGMIFQHFNLLSSRTVFDNVALPLELAGTPKAEIKARVTELLELVGLSDKADRYPAQLSGGQKQRVAIARALA 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446125071 424 HRPEMLILDEPTSGVDPVARDMFWQLMVDLSRQDKVTIFISTHFMNEAER-CDRMSLMHAGKVLASGT 490
Cdd:PRK11153 157 SNPKVLLCDEATSALDPATTRSILELLKDINRELGLTIVLITHEMDVVKRiCDRVAVIDAGRLVEQGT 224
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
275-507 |
1.27e-29 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 118.72 E-value: 1.27e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 275 IAIEAKDLTMRFGKFVAVDHVNFRIPRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGQAWLFGQPVD---PNDIDTRRRV 351
Cdd:PRK13548 1 AMLEARNLSVRLGGRTLLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLNGRPLAdwsPAELARRRAV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 352 gyMSQAFSLYNELTVRQNLELHARLFHIPPAEIPARVAQMIERFMLTEVEDTLPASLPLGIRQRLSLA-V-----AVIHR 425
Cdd:PRK13548 81 --LPQHSSLSFPFTVEEVVAMGRAPHGLSRAEDDALVAAALAQVDLAHLAGRDYPQLSGGEQQRVQLArVlaqlwEPDGP 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 426 PEMLILDEPTSgvdpvARDMFWQLMV-----DLSRQDKVTIFISTHFMNEAER-CDRMSLMHAGKVLASGTPQELVQqrg 499
Cdd:PRK13548 159 PRWLLLDEPTS-----ALDLAHQHHVlrlarQLAHERGLAVIVVLHDLNLAARyADRIVLLHQGRLVADGTPAEVLT--- 230
|
....*...
gi 446125071 500 AANLEAAF 507
Cdd:PRK13548 231 PETLRRVY 238
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
15-235 |
2.02e-29 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 120.59 E-value: 2.02e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 15 LEGVSQHYGKTVALNNITLDIPARSMVGLIGPDGVGKSSLLSLISGARVIEQGNVIVLGGDMRD-AKHRRDVCprIAWMP 93
Cdd:PRK11432 9 LKNITKRFGSNTVIDNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIFIDGEDVTHrSIQQRDIC--MVFQS 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 94 QGLgknlYHTLSVYENVDFFARLFGHDKAEREARITELLNSTGLAPFRDRPAGKLSGGMKQKLGLCCALIHDPELLILDE 173
Cdd:PRK11432 87 YAL----FPHMSLGENVGYGLKMLGVPKEERKQRVKEALELVDLAGFEDRYVDQISGGQQQRVALARALILKPKVLLFDE 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446125071 174 PTTGVDP-LSRAqfwdLIDSIR--QRQTNMSVLVATayMEEAERF---DWLVAMNAGEILATGSAQQL 235
Cdd:PRK11432 163 PLSNLDAnLRRS----MREKIRelQQQFNITSLYVT--HDQSEAFavsDTVIVMNKGKIMQIGSPQEL 224
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
291-491 |
2.50e-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: 2.50e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 291 AVDHVNFRIPRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGQAWLFGQPVDPNDIDTRRRVGYMSQAFSLYNELTVRQNL 370
Cdd:TIGR01257 945 AVDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGKDIETNLDAVRQSLGMCPQHNILFHHLTVAEHI 1024
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 371 ELHARLFHIPPAEIPARVAQMIERFMLTEVEDTLPASLPLGIRQRLSLAVAVIHRPEMLILDEPTSGVDPVARDMFWQLM 450
Cdd:TIGR01257 1025 LFYAQLKGRSWEEAQLEMEAMLEDTGLHHKRNEEAQDLSGGMQRKLSVAIAFVGDAKVVVLDEPTSGVDPYSRRSIWDLL 1104
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 446125071 451 vdLSRQDKVTIFISTHFMNEAERC-DRMSLMHAGKVLASGTP 491
Cdd:TIGR01257 1105 --LKYRSGRTIIMSTHHMDEADLLgDRIAIISQGRLYCSGTP 1144
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
277-466 |
2.99e-29 |
|
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where FtsE is the ATPase and the membrane subunit FtsX resembles a permease subunit. But rather than transporting any substrate, the complex acts in cell division by undergoing conformational changes that alter the activity of cell wall hydrolases located outside the plasma membrane. The complex is widely conserved in bacteria, but also extremely divergent in sequence between different lineages
Pssm-ID: 213259 [Multi-domain] Cd Length: 214 Bit Score: 115.97 E-value: 2.99e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 277 IEAKDLTMRF-GKFVAVDHVNFRIPRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGQAWLFGQPVdpNDIDT------RR 349
Cdd:cd03292 1 IEFINVTKTYpNGTAALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQDV--SDLRGraipylRR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 350 RVGYMSQAFSLYNELTVRQNLELHARLFHIPPAEIPARVAQMIERFMLTEVEDTLPASLPLGIRQRLSLAVAVIHRPEML 429
Cdd:cd03292 79 KIGVVFQDFRLLPDRNVYENVAFALEVTGVPPREIRKRVPAALELVGLSHKHRALPAELSGGEQQRVAIARAIVNSPTIL 158
|
170 180 190
....*....|....*....|....*....|....*....
gi 446125071 430 ILDEPTSGVDPvarDMFWQLMVDLSRQDK--VTIFISTH 466
Cdd:cd03292 159 IADEPTGNLDP---DTTWEIMNLLKKINKagTTVVVATH 194
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
277-494 |
3.34e-29 |
|
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid transport and metabolism, Inorganic ion transport and metabolism];
Pssm-ID: 440213 [Multi-domain] Cd Length: 320 Bit Score: 119.00 E-value: 3.34e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 277 IEAKDLTMRF----GKFVAVDHVNFRIPRGEIFGFLGSNGCGKSTTMKMLTGLLPA---SEGQAWLFGQPV---DPNDID 346
Cdd:COG0444 2 LEVRNLKVYFptrrGVVKAVDGVSFDVRRGETLGLVGESGSGKSTLARAILGLLPPpgiTSGEILFDGEDLlklSEKELR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 347 TRR--RVGYMSQ-AFSLYNE-LTVRQ----NLELHARLfhiPPAEIPARVAQMIERFMLTEVEDTL---PASLPLGIRQR 415
Cdd:COG0444 82 KIRgrEIQMIFQdPMTSLNPvMTVGDqiaePLRIHGGL---SKAEARERAIELLERVGLPDPERRLdryPHELSGGMRQR 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 416 LSLAVAVIHRPEMLILDEPTSGVDPVARDMFWQLMVDLSRQDKVT-IFIsTHFMNE-AERCDRMSLMHAGKVLASGTPQE 493
Cdd:COG0444 159 VMIARALALEPKLLIADEPTTALDVTIQAQILNLLKDLQRELGLAiLFI-THDLGVvAEIADRVAVMYAGRIVEEGPVEE 237
|
.
gi 446125071 494 L 494
Cdd:COG0444 238 L 238
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
15-235 |
5.24e-29 |
|
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the YhbG family are similar to members of the Mj1267_LivG family, which is involved in the transport of branched-chain amino acids. The genes yhbG and yhbN are located in a single operon and may function together in cell envelope during biogenesis. YhbG is the putative ATP-binding cassette component and YhbN is the putative periplasmic-binding protein. Depletion of each gene product leads to growth arrest, irreversible cell damage and loss of viability in E. coli. The YhbG homolog (NtrA) is essential in Rhizobium meliloti, a symbiotic nitrogen-fixing bacterium.
Pssm-ID: 213185 [Multi-domain] Cd Length: 232 Bit Score: 116.10 E-value: 5.24e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 15 LEGVSQHYGKTVALNNITLDIPARSMVGLIGPDGVGKSSLLSLISGARVIEQGNVIVLGGDM-RDAKHRRdvcPR--IAW 91
Cdd:cd03218 3 AENLSKRYGKRKVVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDGQDItKLPMHKR---ARlgIGY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 92 MPQGlgKNLYHTLSVYENVDFFARLFGHDKAEREARITELLNSTGLAPFRDRPAGKLSGGMKQKLGLCCALIHDPELLIL 171
Cdd:cd03218 80 LPQE--ASIFRKLTVEENILAVLEIRGLSKKEREEKLEELLEEFHITHLRKSKASSLSGGERRRVEIARALATNPKFLLL 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446125071 172 DEPTTGVDPLSRAQFWDLIDSIRQRqtNMSVL------------VATAYMeeaerfdwlvaMNAGEILATGSAQQL 235
Cdd:cd03218 158 DEPFAGVDPIAVQDIQKIIKILKDR--GIGVLitdhnvretlsiTDRAYI-----------IYEGKVLAEGTPEEI 220
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
15-235 |
5.31e-29 |
|
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: 116.18 E-value: 5.31e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 15 LEGVSQHYGKTVALNNITLDIPARSMVGLIGPDGVGKSSLLSLISGARVIEQGNVIVLGGDMRD-AKHRRdvcpRIAWMP 93
Cdd:cd03300 3 LENVSKFYGGFVALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGKDITNlPPHKR----PVNTVF 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 94 QGLGknLYHTLSVYENVDFFARLFGHDKAEREARITELLNSTGLAPFRDRPAGKLSGGMKQKLGLCCALIHDPELLILDE 173
Cdd:cd03300 79 QNYA--LFPHLTVFENIAFGLRLKKLPKAEIKERVAEALDLVQLEGYANRKPSQLSGGQQQRVAIARALVNEPKVLLLDE 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446125071 174 PTTGVDPLSRAQFWDLIDSIrQRQTNMSVLVATAYMEEAERF-DWLVAMNAGEILATGSAQQL 235
Cdd:cd03300 157 PLGALDLKLRKDMQLELKRL-QKELGITFVFVTHDQEEALTMsDRIAVMNKGKIQQIGTPEEI 218
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
15-242 |
5.94e-29 |
|
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid transport and metabolism, Inorganic ion transport and metabolism];
Pssm-ID: 440741 [Multi-domain] Cd Length: 248 Bit Score: 116.44 E-value: 5.94e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 15 LEGVSQHYGK----TVALNNITLDIPARSMVGLIGPDGVGKSSLLSLISGARVIEQGNVIVLGGDMRDaKHRRDVCPRIA 90
Cdd:COG1124 4 VRNLSVSYGQggrrVPVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVTFDGRPVTR-RRRKAFRRRVQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 91 WMPQglgkNLYHTL----SVYENVDFFARLFGHDkaEREARITELLNSTGLAP-FRDRPAGKLSGGMKQKLGLCCALIHD 165
Cdd:COG1124 83 MVFQ----DPYASLhprhTVDRILAEPLRIHGLP--DREERIAELLEQVGLPPsFLDRYPHQLSGGQRQRVAIARALILE 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446125071 166 PELLILDEPTTGVDPLSRAQFWDLIDSIRqRQTNMSVLVATAYMEEAERF-DWLVAMNAGEILATGSAQQLRAKTHSA 242
Cdd:COG1124 157 PELLLLDEPTSALDVSVQAEILNLLKDLR-EERGLTYLFVSHDLAVVAHLcDRVAVMQNGRIVEELTVADLLAGPKHP 233
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
14-235 |
6.76e-29 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 119.10 E-value: 6.76e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 14 QLEGVSQHYGKTVALNNITLDIPARSMVGLIGPDGVGKSSLLSLISGarvIEQGN--VIVLGGdmRDAKHRRDVCPR-IA 90
Cdd:COG1118 4 EVRNISKRFGSFTLLDDVSLEIASGELVALLGPSGSGKTTLLRIIAG---LETPDsgRIVLNG--RDLFTNLPPRERrVG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 91 WMPQglgkN--LYHTLSVYENVDFFARLFGHDKAEREARITELLNSTGLAPFRDRPAGKLSGGMKQKLGLCCALIHDPEL 168
Cdd:COG1118 79 FVFQ----HyaLFPHMTVAENIAFGLRVRPPSKAEIRARVEELLELVQLEGLADRYPSQLSGGQRQRVALARALAVEPEV 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446125071 169 LILDEPTTGVDPLSRAQFWDLIDSIRQRQTNMSVLVaTAYMEEAERF-DWLVAMNAGEILATGSAQQL 235
Cdd:COG1118 155 LLLDEPFGALDAKVRKELRRWLRRLHDELGGTTVFV-THDQEEALELaDRVVVMNQGRIEQVGTPDEV 221
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
285-489 |
1.08e-28 |
|
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC transporter subfamily is involved in extracellular polysaccharide export. Among the variety of membrane-linked or extracellular polysaccharides excreted by bacteria, only capsular polysaccharides, lipopolysaccharides, and teichoic acids have been shown to be exported by ABC transporters. A typical system is made of a conserved integral membrane and an ABC. In addition to these proteins, capsular polysaccharide exporter systems require two 'accessory' proteins to perform their function: a periplasmic (E.coli) or a lipid-anchored outer membrane protein called OMA (Neisseria meningitidis and Haemophilus influenza) and a cytoplasmic membrane protein MPA2.
Pssm-ID: 213187 [Multi-domain] Cd Length: 224 Bit Score: 114.94 E-value: 1.08e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 285 RFGKFVAVDHVNFRIPRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGQAWLFGQPVDPNDIDTrrrvgymsqafSLYNEL 364
Cdd:cd03220 31 EVGEFWALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVTVRGRVSSLLGLGG-----------GFNPEL 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 365 TVRQNLELHARLFHIPPAEIPARVAQMIErfmLTEVEDTLpaSLPL-----GIRQRLSLAVAVIHRPEMLILDEPTSGVD 439
Cdd:cd03220 100 TGRENIYLNGRLLGLSRKEIDEKIDEIIE---FSELGDFI--DLPVktyssGMKARLAFAIATALEPDILLIDEVLAVGD 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 446125071 440 PVARDMFWQLMVDLSRQDKvTIFISTHFMNEAER-CDRMSLMHAGKVLASG 489
Cdd:cd03220 175 AAFQEKCQRRLRELLKQGK-TVILVSHDPSSIKRlCDRALVLEKGKIRFDG 224
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
277-497 |
1.36e-28 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 118.28 E-value: 1.36e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 277 IEAKDLTMRFGKFVAVDHVNFRIPRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGQAWLFGQPVDPNDIDtRRRVGYMSQ 356
Cdd:PRK11432 7 VVLKNITKRFGSNTVIDNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIFIDGEDVTHRSIQ-QRDICMVFQ 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 357 AFSLYNELTVRQNLELHARLFHIPPAEIPARVAQMIERFMLTEVEDTLPASLPLGIRQRLSLAVAVIHRPEMLILDEPTS 436
Cdd:PRK11432 86 SYALFPHMSLGENVGYGLKMLGVPKEERKQRVKEALELVDLAGFEDRYVDQISGGQQQRVALARALILKPKVLLFDEPLS 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446125071 437 GVDPVARDMFWQLMVDLSRQDKVTIFISTHFMNEA-ERCDRMSLMHAGKVLASGTPQELVQQ 497
Cdd:PRK11432 166 NLDANLRRSMREKIRELQQQFNITSLYVTHDQSEAfAVSDTVIVMNKGKIMQIGSPQELYRQ 227
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
277-505 |
1.41e-28 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 114.85 E-value: 1.41e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 277 IEAKDLTMRFGKFVAvdHVNFRIPRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGQAWLFGQPVDPNDIDtRRRVGYMSQ 356
Cdd:COG3840 2 LRLDDLTYRYGDFPL--RFDLTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILWNGQDLTALPPA-ERPVSMLFQ 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 357 AFSLYNELTVRQN--LELHARLfHIPPAEIpARVAQMIERFMLTEVEDTLPASLPLGIRQRLSLAVAVI-HRPeMLILDE 433
Cdd:COG3840 79 ENNLFPHLTVAQNigLGLRPGL-KLTAEQR-AQVEQALERVGLAGLLDRLPGQLSGGQRQRVALARCLVrKRP-ILLLDE 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446125071 434 PTSGVDPVARDMFWQLMVDLSRQDKVTIFISTHFMNEAER-CDRMSLMHAGKVLASGTPQELVQQRGAANLEA 505
Cdd:COG3840 156 PFSALDPALRQEMLDLVDELCRERGLTVLMVTHDPEDAARiADRVLLVADGRIAADGPTAALLDGEPPPALAA 228
|
|
| potA |
TIGR01187 |
spermidine/putrescine ABC transporter ATP-binding subunit; This model describes spermidine ... |
308-494 |
1.53e-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: 117.21 E-value: 1.53e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 308 LGSNGCGKSTTMKMLTGLLPASEGQAWLFGQPVDpNDIDTRRRVGYMSQAFSLYNELTVRQNLELHARLFHIPPAEIPAR 387
Cdd:TIGR01187 2 LGPSGCGKTTLLRLLAGFEQPDSGSIMLDGEDVT-NVPPHLRHINMVFQSYALFPHMTVEENVAFGLKMRKVPRAEIKPR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 388 VAQMIERFMLTEVEDTLPASLPLGIRQRLSLAVAVIHRPEMLILDEPTSGVDPVARDMFWQLMVDLSRQDKVTIFISTHF 467
Cdd:TIGR01187 81 VLEALRLVQLEEFADRKPHQLSGGQQQRVALARALVFKPKILLLDEPLSALDKKLRDQMQLELKTIQEQLGITFVFVTHD 160
|
170 180
....*....|....*....|....*...
gi 446125071 468 MNEA-ERCDRMSLMHAGKVLASGTPQEL 494
Cdd:TIGR01187 161 QEEAmTMSDRIAIMRKGKIAQIGTPEEI 188
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
273-513 |
1.63e-28 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 116.10 E-value: 1.63e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 273 EEIAIEAKDLTMRFGKFV-AVDHVNFRIPRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGQAWLFGQPVDPND---IDTR 348
Cdd:PRK13636 2 EDYILKVEELNYNYSDGThALKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGKPIDYSRkglMKLR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 349 RRVGYMSQafSLYNEL---TVRQNLELHARLFHIPPAEIPARVAQMIERFMLTEVEDTLPASLPLGIRQRLSLAVAVIHR 425
Cdd:PRK13636 82 ESVGMVFQ--DPDNQLfsaSVYQDVSFGAVNLKLPEDEVRKRVDNALKRTGIEHLKDKPTHCLSFGQKKRVAIAGVLVME 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 426 PEMLILDEPTSGVDPVARDMFWQLMVDLSRQDKVTIFISTHFMNE-AERCDRMSLMHAGKVLASGTPQELVQQRG---AA 501
Cdd:PRK13636 160 PKVLVLDEPTAGLDPMGVSEIMKLLVEMQKELGLTIIIATHDIDIvPLYCDNVFVMKEGRVILQGNPKEVFAEKEmlrKV 239
|
250
....*....|..
gi 446125071 502 NLEAAFISWLQE 513
Cdd:PRK13636 240 NLRLPRIGHLME 251
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
15-225 |
1.63e-28 |
|
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: 112.48 E-value: 1.63e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 15 LEGVSQHYG--KTVALNNITLDIPARSMVGLIGPDGVGKSSLLSLISGARVIEQGNVIVLGGDMRDAKhRRDVCPRIAWM 92
Cdd:cd03228 3 FKNVSFSYPgrPKPVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGVDLRDLD-LESLRKNIAYV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 93 PQGLgkNLYHTlSVYENVdffarlfghdkaerearitellnstglapfrdrpagkLSGGMKQKLGLCCALIHDPELLILD 172
Cdd:cd03228 82 PQDP--FLFSG-TIRENI-------------------------------------LSGGQRQRIAIARALLRDPPILILD 121
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 446125071 173 EPTTGVDPLSRAQFWDLIDSIRQRQTnmsVLVATAYMEEAERFDWLVAMNAGE 225
Cdd:cd03228 122 EATSALDPETEALILEALRALAKGKT---VIVIAHRLSTIRDADRIIVLDDGR 171
|
|
| COG4559 |
COG4559 |
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism]; |
277-524 |
2.07e-28 |
|
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443620 [Multi-domain] Cd Length: 258 Bit Score: 115.21 E-value: 2.07e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 277 IEAKDLTMRFGKFVAVDHVNFRIPRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGQAWLFGQPVD---PNDIDTRRRVgy 353
Cdd:COG4559 2 LEAENLSVRLGGRTLLDDVSLTLRPGELTAIIGPNGAGKSTLLKLLTGELTPSSGEVRLNGRPLAawsPWELARRRAV-- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 354 MSQAFSLYNELTVRQNLELHARLFHIPPAEIPARVAQMIERFMLTEVEDTLPASLPLGIRQRLSLA--VAVIHRPEM--- 428
Cdd:COG4559 80 LPQHSSLAFPFTVEEVVALGRAPHGSSAAQDRQIVREALALVGLAHLAGRSYQTLSGGEQQRVQLArvLAQLWEPVDggp 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 429 --LILDEPTSGVDPvardmFWQLMV-----DLSRQdKVTIFISTHFMNEAER-CDRMSLMHAGKVLASGTPQELVQqrgA 500
Cdd:COG4559 160 rwLFLDEPTSALDL-----AHQHAVlrlarQLARR-GGGVVAVLHDLNLAAQyADRILLLHQGRLVAQGTPEEVLT---D 230
|
250 260
....*....|....*....|....
gi 446125071 501 ANLEAAFisWLQEAAGAAPETPIP 524
Cdd:COG4559 231 ELLERVY--GADLRVLAHPEGGCP 252
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
14-235 |
2.53e-28 |
|
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex cysAWTP involved in sulfate import. Responsible for energy coupling to the transport system. The complex is composed of two ATP-binding proteins (cysA), two transmembrane proteins (cysT and cysW), and a solute-binding protein (cysP). ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213263 [Multi-domain] Cd Length: 239 Bit Score: 114.36 E-value: 2.53e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 14 QLEGVSQHYGKTVALNNITLDIPARSMVGLIGPDGVGKSSLLSLISGARVIEQGNvIVLGGdmRDAKHrRDVCPR-IAWM 92
Cdd:cd03296 4 EVRNVSKRFGDFVALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGT-ILFGG--EDATD-VPVQERnVGFV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 93 PQGLGknLYHTLSVYENVDFFARL----FGHDKAEREARITELLNSTGLAPFRDRPAGKLSGGMKQKLGLCCALIHDPEL 168
Cdd:cd03296 80 FQHYA--LFRHMTVFDNVAFGLRVkprsERPPEAEIRAKVHELLKLVQLDWLADRYPAQLSGGQRQRVALARALAVEPKV 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446125071 169 LILDEPTTGVDPLSRAQFWDLIDSIRQRQTNMSVLVATAYMEEAERFDWLVAMNAGEILATGSAQQL 235
Cdd:cd03296 158 LLLDEPFGALDAKVRKELRRWLRRLHDELHVTTVFVTHDQEEALEVADRVVVMNKGRIEQVGTPDEV 224
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
271-494 |
2.93e-28 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 114.85 E-value: 2.93e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 271 EQEEIAIEAKDLTMRF--GKFVAVDHVNFRIPRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGQAWLFGQPVDPNDI-DT 347
Cdd:PRK13648 2 EDKNSIIVFKNVSFQYqsDASFTLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIFYNNQAITDDNFeKL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 348 RRRVGYMSQ---------------AFSLYNELtvrqnlelharlfhIPPAEIPARVAQMIERFMLTEVEDTLPASLPLGI 412
Cdd:PRK13648 82 RKHIGIVFQnpdnqfvgsivkydvAFGLENHA--------------VPYDEMHRRVSEALKQVDMLERADYEPNALSGGQ 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 413 RQRLSLAVAVIHRPEMLILDEPTSGVDPVARDMFWQLMVDLSRQDKVTIFISTHFMNEAERCDRMSLMHAGKVLASGTPQ 492
Cdd:PRK13648 148 KQRVAIAGVLALNPSVIILDEATSMLDPDARQNLLDLVRKVKSEHNITIISITHDLSEAMEADHVIVMNKGTVYKEGTPT 227
|
..
gi 446125071 493 EL 494
Cdd:PRK13648 228 EI 229
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
14-230 |
4.38e-28 |
|
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) proteins function from bacteria to human, mediating the translocation of substances into and out of cells or organelles. ABC transporters contain two transmembrane-spanning domains (TMDs) or subunits and two nucleotide binding domains (NBDs) or subunits that couple transport to the hydrolysis of ATP. In the maltose transport system, the periplasmic maltose binding protein (MBP) stimulates the ATPase activity of the membrane-associated transporter, which consists of two transmembrane subunits, MalF and MalG, and two copies of the ATP binding subunit, MalK, and becomes tightly bound to the transporter in the catalytic transition state, ensuring that maltose is passed to the transporter as ATP is hydrolyzed.
Pssm-ID: 213268 [Multi-domain] Cd Length: 213 Bit Score: 112.73 E-value: 4.38e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 14 QLEGVSQHYGKTVALNNITLDIPARSMVGLIGPDGVGKSSLLSLISGARVIEQGNVIVLGGDMRD--AKHRRdvcprIAW 91
Cdd:cd03301 2 ELENVTKRFGNVTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGRDVTDlpPKDRD-----IAM 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 92 MPQGLGknLYHTLSVYENVDFFARLFGHDKAEREARITELLNSTGLAPFRDRPAGKLSGGMKQKLGLCCALIHDPELLIL 171
Cdd:cd03301 77 VFQNYA--LYPHMTVYDNIAFGLKLRKVPKDEIDERVREVAELLQIEHLLDRKPKQLSGGQRQRVALGRAIVREPKVFLM 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 446125071 172 DEPTTGVDPLSRAQFWDLIDSIRQRQTNMSVLVATAYMEEAERFDWLVAMNAGEILATG 230
Cdd:cd03301 155 DEPLSNLDAKLRVQMRAELKRLQQRLGTTTIYVTHDQVEAMTMADRIAVMNDGQIQQIG 213
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
290-493 |
5.05e-28 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 114.76 E-value: 5.05e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 290 VAVDHVNFRIPRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGQAWLFGqpVDPND-----IDTRRRVGYMSQ--AFSLYN 362
Cdd:PRK13637 21 KALDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDG--VDITDkkvklSDIRKKVGLVFQypEYQLFE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 363 ElTVRQNLELHARLFHIPPAEIPARVAQMIERFMLT--EVEDTLPASLPLGIRQRLSLAVAVIHRPEMLILDEPTSGVDP 440
Cdd:PRK13637 99 E-TIEKDIAFGPINLGLSEEEIENRVKRAMNIVGLDyeDYKDKSPFELSGGQKRRVAIAGVVAMEPKILILDEPTAGLDP 177
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 446125071 441 VARDMFWQLMVDLSRQDKVTIFISTHFMNE-AERCDRMSLMHAGKVLASGTPQE 493
Cdd:PRK13637 178 KGRDEILNKIKELHKEYNMTIILVSHSMEDvAKLADRIIVMNKGKCELQGTPRE 231
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
277-514 |
5.43e-28 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 114.40 E-value: 5.43e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 277 IEAKDLTMRFGK-FVAVDHVNFRIPRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGQAWLFGQPVDPND---IDTRRRVG 352
Cdd:PRK13639 2 LETRDLKYSYPDgTEALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIKGEPIKYDKkslLEVRKTVG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 353 YM-----SQAFSLynelTVRQNLELHARLFHIPPAEIPARVAQMIERFMLTEVEDTLPASLPLGIRQRLSLAVAVIHRPE 427
Cdd:PRK13639 82 IVfqnpdDQLFAP----TVEEDVAFGPLNLGLSKEEVEKRVKEALKAVGMEGFENKPPHHLSGGQKKRVAIAGILAMKPE 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 428 MLILDEPTSGVDPVARDMFWQLMVDLSRQDkVTIFISTHFMNEAER-CDRMSLMHAGKVLASGTPQELVQQRGA---ANL 503
Cdd:PRK13639 158 IIVLDEPTSGLDPMGASQIMKLLYDLNKEG-ITIIISTHDVDLVPVyADKVYVMSDGKIIKEGTPKEVFSDIETirkANL 236
|
250
....*....|.
gi 446125071 504 EAAFISWLQEA 514
Cdd:PRK13639 237 RLPRVAHLIEI 247
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
14-226 |
5.88e-28 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 112.22 E-value: 5.88e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 14 QLEGVSQHYGKTVALNNITLDIPARSMVGLIGPDGVGKSSLLSLISGARVIEQGNVIVLGGDMRDA---KHRRdvcpRIA 90
Cdd:COG4619 2 ELEGLSFRVGGKPILSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIYLDGKPLSAMpppEWRR----QVA 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 91 WMPQ--GLGKNlyhtlSVYENVDFfARLFGHDKAEREaRITELLNSTGLAP-FRDRPAGKLSGGMKQKLGLCCALIHDPE 167
Cdd:COG4619 78 YVPQepALWGG-----TVRDNLPF-PFQLRERKFDRE-RALELLERLGLPPdILDKPVERLSGGERQRLALIRALLLQPD 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 168 LLILDEPTTGVDPLSRAQFWDLIDSIRQRQtNMSVLVATAYMEEAERF-DWLVAMNAGEI 226
Cdd:COG4619 151 VLLLDEPTSALDPENTRRVEELLREYLAEE-GRAVLWVSHDPEQIERVaDRVLTLEAGRL 209
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
20-489 |
6.55e-28 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 120.35 E-value: 6.55e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 20 QHYGKTVALNNITLDIPARSMVGLIGPDGVGKS----SLLSLI--SGARVIEQG--------NVIVLGgDMRDAKHRRDV 85
Cdd:PRK10261 24 QEQQKIAAVRNLSFSLQRGETLAIVGESGSGKSvtalALMRLLeqAGGLVQCDKmllrrrsrQVIELS-EQSAAQMRHVR 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 86 CPRIAWMPQGLGKNLYHTLSVYENVDFFARL---FGHDKAEREA-RITELLNSTGLAPFRDRPAGKLSGGMKQKLGLCCA 161
Cdd:PRK10261 103 GADMAMIFQEPMTSLNPVFTVGEQIAESIRLhqgASREEAMVEAkRMLDQVRIPEAQTILSRYPHQLSGGMRQRVMIAMA 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 162 LIHDPELLILDEPTTGVDPLSRAQFWDLIdSIRQRQTNMSVLVATAYME-EAERFDWLVAMNAGEILATGSAQQL-RAKT 239
Cdd:PRK10261 183 LSCRPAVLIADEPTTALDVTIQAQILQLI-KVLQKEMSMGVIFITHDMGvVAEIADRVLVMYQGEAVETGSVEQIfHAPQ 261
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 240 HSATleQAFIALLPE--AQRQAHKPVVIPPYHAEQE---------------EIAIEAKDLTMRF----GKFV-------A 291
Cdd:PRK10261 262 HPYT--RALLAAVPQlgAMKGLDYPRRFPLISLEHPakqeppieqdtvvdgEPILQVRNLVTRFplrsGLLNrvtrevhA 339
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 292 VDHVNFRIPRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGQAWLFGQPVD---PNDIDT-RRRVGYMSQafSLYNELTVR 367
Cdd:PRK10261 340 VEKVSFDLWPGETLSLVGESGSGKSTTGRALLRLVESQGGEIIFNGQRIDtlsPGKLQAlRRDIQFIFQ--DPYASLDPR 417
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 368 QN--------LELHARLfhiPPAEIPARVAQMIERF-MLTEVEDTLPASLPLGIRQRLSLAVAVIHRPEMLILDEPTSGV 438
Cdd:PRK10261 418 QTvgdsimepLRVHGLL---PGKAAAARVAWLLERVgLLPEHAWRYPHEFSGGQRQRICIARALALNPKVIIADEAVSAL 494
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|..
gi 446125071 439 DPVARDMFWQLMVDLSRQDKVTIFISTHFMNEAERCD-RMSLMHAGKVLASG 489
Cdd:PRK10261 495 DVSIRGQIINLLLDLQRDFGIAYLFISHDMAVVERIShRVAVMYLGQIVEIG 546
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
8-238 |
1.31e-27 |
|
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: 118.72 E-value: 1.31e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 8 PVPPVAQLEGVSQHY--GKTVALNNITLDIPARSMVGLIGPDGVGKSSLLSLISGARVIEQGNVIVLGGDMRDAkHRRDV 85
Cdd:COG4987 329 PGGPSLELEDVSFRYpgAGRPVLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFLDPQSGSITLGGVDLRDL-DEDDL 407
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 86 CPRIAWMPQglgKN-LYHTlSVYENVdffarLFGHDKAErEARITELLNSTGLAPF-RDRPAG----------KLSGGMK 153
Cdd:COG4987 408 RRRIAVVPQ---RPhLFDT-TLRENL-----RLARPDAT-DEELWAALERVGLGDWlAALPDGldtwlgeggrRLSGGER 477
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 154 QKLGLCCALIHDPELLILDEPTTGVDPLSRAQFWDLIDSIRQRQTnmsVLVATAYMEEAERFDWLVAMNAGEILATGSAQ 233
Cdd:COG4987 478 RRLALARALLRDAPILLLDEPTEGLDAATEQALLADLLEALAGRT---VLLITHRLAGLERMDRILVLEDGRIVEQGTHE 554
|
....*
gi 446125071 234 QLRAK 238
Cdd:COG4987 555 ELLAQ 559
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
14-244 |
1.46e-27 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 111.77 E-value: 1.46e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 14 QLEGVSQHYGKTVAlnNITLDIPARSMVGLIGPDGVGKSSLLSLISGARVIEQGNVIVLGGDMRD-AKHRRDVcpriAWM 92
Cdd:COG3840 3 RLDDLTYRYGDFPL--RFDLTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILWNGQDLTAlPPAERPV----SML 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 93 PQGlgKNLYHTLSVYENVDF----FARLfghDKAEReARITELLNSTGLAPFRDRPAGKLSGGMKQKLGLCCALIHDPEL 168
Cdd:COG3840 77 FQE--NNLFPHLTVAQNIGLglrpGLKL---TAEQR-AQVEQALERVGLAGLLDRLPGQLSGGQRQRVALARCLVRKRPI 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446125071 169 LILDEPTTGVDPLSRAQFWDLIDSIrQRQTNMSVLVATAYMEEAERF-DWLVAMNAGEILATGSAQQLRAKTHSATL 244
Cdd:COG3840 151 LLLDEPFSALDPALRQEMLDLVDEL-CRERGLTVLMVTHDPEDAARIaDRVLLVADGRIAADGPTAALLDGEPPPAL 226
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
14-206 |
1.61e-27 |
|
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: 110.81 E-value: 1.61e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 14 QLEGVS-QHYGKTVALNNITLDIPARSMVGLIGPDGVGKSSLLSLISGARVIEQGNvIVLGGDMRDAKHRRDvcpRIAWM 92
Cdd:cd03226 1 RIENISfSYKKGTEILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGS-ILLNGKPIKAKERRK---SIGYV 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 93 PQGLGKNLYhTLSVYENVDFFARlfghDKAEREARITELLNSTGLAPFRDRPAGKLSGGMKQKLGLCCALIHDPELLILD 172
Cdd:cd03226 77 MQDVDYQLF-TDSVREELLLGLK----ELDAGNEQAETVLKDLDLYALKERHPLSLSGGQKQRLAIAAALLSGKDLLIFD 151
|
170 180 190
....*....|....*....|....*....|....
gi 446125071 173 EPTTGVDPLSRAQFWDLIDSIrQRQTNmSVLVAT 206
Cdd:cd03226 152 EPTSGLDYKNMERVGELIREL-AAQGK-AVIVIT 183
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
22-230 |
3.35e-27 |
|
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: 110.88 E-value: 3.35e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 22 YGKTVALNNITLDIPARSMVGLIGPDGVGKSSLLSLISGARVIEQGNVIVLGgdMRDAKHRRDVCPRIAWMpQGLGKNLY 101
Cdd:cd03267 31 YREVEALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRVAG--LVPWKRRKKFLRRIGVV-FGQKTQLW 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 102 HTLSVYENVDFFARLFGHDKAE---REARITELLNstgLAPFRDRPAGKLSGGMKQKLGLCCALIHDPELLILDEPTTGV 178
Cdd:cd03267 108 WDLPVIDSFYLLAAIYDLPPARfkkRLDELSELLD---LEELLDTPVRQLSLGQRMRAEIAAALLHEPEILFLDEPTIGL 184
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 446125071 179 DPLSRAQFWDLIDsIRQRQTNMSVLVATAYMEEAERF-DWLVAMNAGEILATG 230
Cdd:cd03267 185 DVVAQENIRNFLK-EYNRERGTTVLLTSHYMKDIEALaRRVLVIDKGRLLYDG 236
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
274-496 |
4.18e-27 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 111.09 E-value: 4.18e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 274 EIAIEAKDLTMRFGKFVAVDHVNFRIPRGEIFGFLGSNGCGKSTTMKMLTGLLPAS-----EGQAWLFGQPV---DPNDI 345
Cdd:PRK14267 2 KFAIETVNLRVYYGSNHVIKGVDLKIPQNGVFALMGPSGCGKSTLLRTFNRLLELNeearvEGEVRLFGRNIyspDVDPI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 346 DTRRRVGYMSQAFSLYNELTVRQNLELHARLFHI--PPAEIPARVAQMIERFML-TEVEDTL---PASLPLGIRQRLSLA 419
Cdd:PRK14267 82 EVRREVGMVFQYPNPFPHLTIYDNVAIGVKLNGLvkSKKELDERVEWALKKAALwDEVKDRLndyPSNLSGGQRQRLVIA 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446125071 420 VAVIHRPEMLILDEPTSGVDPVARDMFWQLMVDLsrQDKVTIFISTHFMNEAER-CDRMSLMHAGKVLASGTPQELVQ 496
Cdd:PRK14267 162 RALAMKPKILLMDEPTANIDPVGTAKIEELLFEL--KKEYTIVLVTHSPAQAARvSDYVAFLYLGKLIEVGPTRKVFE 237
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
23-235 |
9.92e-27 |
|
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This family comprises the glycine betaine/L-proline ATP binding subunit in bacteria and its equivalents in archaea. This transport system belong to the larger ATP-Binding Cassette (ABC) transporter superfamily. The characteristic feature of these transporters is the obligatory coupling of ATP hydrolysis to substrate translocation. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213261 [Multi-domain] Cd Length: 269 Bit Score: 110.43 E-value: 9.92e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 23 GKTVALNNITLDIPARSMVGLIGPDGVGKSSLLSLISgaRVIE--QGNVIVLGGDMRDAKH------RRDvcpRIAWMPQ 94
Cdd:cd03294 35 GQTVGVNDVSLDVREGEIFVIMGLSGSGKSTLLRCIN--RLIEptSGKVLIDGQDIAAMSRkelrelRRK---KISMVFQ 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 95 GLGknLYHTLSVYENVDFFARLFGHDKAEREARITELLNSTGLAPFRDRPAGKLSGGMKQKLGLCCALIHDPELLILDEP 174
Cdd:cd03294 110 SFA--LLPHRTVLENVAFGLEVQGVPRAEREERAAEALELVGLEGWEHKYPDELSGGMQQRVGLARALAVDPDILLMDEA 187
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446125071 175 TTGVDPLSRAQFWDLIDSIrQRQTNMSVLVATAYMEEAERF-DWLVAMNAGEILATGSAQQL 235
Cdd:cd03294 188 FSALDPLIRREMQDELLRL-QAELQKTIVFITHDLDEALRLgDRIAIMKDGRLVQVGTPEEI 248
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
277-494 |
1.20e-26 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 109.62 E-value: 1.20e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 277 IEAKDLTMRFGKFVAVDHVNFRIPRGEIFGFLGSNGCGKSTTMKMLTGLL-----PASEGQAWLFGQPVDPND-IDTRRR 350
Cdd:PRK14247 4 IEIRDLKVSFGQVEVLDGVNLEIPDNTITALMGPSGSGKSTLLRVFNRLIelypeARVSGEVYLDGQDIFKMDvIELRRR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 351 VGYMSQAFSLYNELTVRQNLELHARLFHI--PPAEIPARVAQMIERFML-TEVEDTLPA---SLPLGIRQRLSLAVAVIH 424
Cdd:PRK14247 84 VQMVFQIPNPIPNLSIFENVALGLKLNRLvkSKKELQERVRWALEKAQLwDEVKDRLDApagKLSGGQQQRLCIARALAF 163
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446125071 425 RPEMLILDEPTSGVDPVARDMFWQLMVDLSRQdkVTIFISTHFMNEAERC-DRMSLMHAGKVLASGTPQEL 494
Cdd:PRK14247 164 QPEVLLADEPTANLDPENTAKIESLFLELKKD--MTIVLVTHFPQQAARIsDYVAFLYKGQIVEWGPTREV 232
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
291-499 |
1.53e-26 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 115.65 E-value: 1.53e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 291 AVDHVNFRIPRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGQAWLFGQPVdpNDIDT---RRRVGYMSQAFSLYNElTVR 367
Cdd:COG1132 355 VLKDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYDPTSGRILIDGVDI--RDLTLeslRRQIGVVPQDTFLFSG-TIR 431
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 368 QNLELhARLfHIPPAEI--PARVAQmierfmLTEVEDTLP-----------ASLPLGIRQRLSLAVAVIHRPEMLILDEP 434
Cdd:COG1132 432 ENIRY-GRP-DATDEEVeeAAKAAQ------AHEFIEALPdgydtvvgergVNLSGGQRQRIAIARALLKDPPILILDEA 503
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446125071 435 TSGVDPVA----RDMFWQLMvdlsrQDKVTIFIStHFMNEAERCDRMSLMHAGKVLASGTPQELVQQRG 499
Cdd:COG1132 504 TSALDTETealiQEALERLM-----KGRTTIVIA-HRLSTIRNADRILVLDDGRIVEQGTHEELLARGG 566
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
277-494 |
1.92e-26 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 109.82 E-value: 1.92e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 277 IEAKDLTMRFGK---FVAVDHVNFRIPRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGQAWLFGQPVDPNDI-DTRRRVG 352
Cdd:PRK13650 5 IEVKNLTFKYKEdqeKYTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIIDGDLLTEENVwDIRHKIG 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 353 YMSQ---------------AFSLYNEltvrqnlelharlfHIPPAEIPARVAQMIERFMLTEVEDTLPASLPLGIRQRLS 417
Cdd:PRK13650 85 MVFQnpdnqfvgatveddvAFGLENK--------------GIPHEEMKERVNEALELVGMQDFKEREPARLSGGQKQRVA 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446125071 418 LAVAVIHRPEMLILDEPTSGVDPVARDMFWQLMVDLSRQDKVTIFISTHFMNEAERCDRMSLMHAGKVLASGTPQEL 494
Cdd:PRK13650 151 IAGAVAMRPKIIILDEATSMLDPEGRLELIKTIKGIRDDYQMTVISITHDLDEVALSDRVLVMKNGQVESTSTPREL 227
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
291-489 |
2.44e-26 |
|
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic bacteriocins of lactic acid bacteria are produced as precursors which have N-terminal leader peptides that share similarities in amino acid sequence and contain a conserved processing site of two glycine residues in positions -1 and -2. A dedicated ATP-binding cassette (ABC) transporter is responsible for the proteolytic cleavage of the leader peptides and subsequent translocation of the bacteriocins across the cytoplasmic membrane.
Pssm-ID: 213212 [Multi-domain] Cd Length: 220 Bit Score: 108.06 E-value: 2.44e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 291 AVDHVNFRIPRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGQAWLFG---QPVDPNDIdtRRRVGYMSQAFSLYNElTVR 367
Cdd:cd03245 19 ALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGtdiRQLDPADL--RRNIGYVPQDVTLFYG-TLR 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 368 QNLELHArlfhiPPAEiPARVAQMIERFMLTEVEDTLPASLPL-----------GIRQRLSLAVAVIHRPEMLILDEPTS 436
Cdd:cd03245 96 DNITLGA-----PLAD-DERILRAAELAGVTDFVNKHPNGLDLqigergrglsgGQRQAVALARALLNDPPILLLDEPTS 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 446125071 437 GVDPVARDMFWQLMVDLSRQDkvTIFISTHFMNEAERCDRMSLMHAGKVLASG 489
Cdd:cd03245 170 AMDMNSEERLKERLRQLLGDK--TLIIITHRPSLLDLVDRIIVMDSGRIVADG 220
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
14-235 |
2.68e-26 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 108.26 E-value: 2.68e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 14 QLEGVSQHYGKTVALNNITLDIPARSMVGLIGPDGVGKSSLLSLISGARVIEQGNVIVLGGDMRDAKHRRDVCPRIAWMP 93
Cdd:PRK09493 3 EFKNVSKHFGPTQVLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGLKVNDPKVDERLIRQEAGMV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 94 -QGLgkNLYHTLSVYENVDFFA-RLFGHDKAEREARITELLNSTGLAPFRDRPAGKLSGGMKQKLGLCCALIHDPELLIL 171
Cdd:PRK09493 83 fQQF--YLFPHLTALENVMFGPlRVRGASKEEAEKQARELLAKVGLAERAHHYPSELSGGQQQRVAIARALAVKPKLMLF 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446125071 172 DEPTTGVDPLSRAQFWDLIDSIRQRqtNMSVLVATAYMEEAERF-DWLVAMNAGEILATGSAQQL 235
Cdd:PRK09493 161 DEPTSALDPELRHEVLKVMQDLAEE--GMTMVIVTHEIGFAEKVaSRLIFIDKGRIAEDGDPQVL 223
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
10-506 |
2.79e-26 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 113.87 E-value: 2.79e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 10 PPVAQLEGVSQHYGKTVALNNITLDIPARSMVGLIGPDGVGKSSLLSLISGarVIEQGNV---IVLGGDMRDAKHRRDVC 86
Cdd:PRK13549 3 EYLLEMKNITKTFGGVKALDNVSLKVRAGEIVSLCGENGAGKSTLMKVLSG--VYPHGTYegeIIFEGEELQASNIRDTE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 87 PR-IAWMPQGLgkNLYHTLSVYENVdFFARLFGH----DKAEREARITELLNSTGLAPFRDRPAGKLSGGMKQKLGLCCA 161
Cdd:PRK13549 81 RAgIAIIHQEL--ALVKELSVLENI-FLGNEITPggimDYDAMYLRAQKLLAQLKLDINPATPVGNLGLGQQQLVEIAKA 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 162 LIHDPELLILDEPTTgvdPLSRAQFWDLIDSIRQRQTNMsvlVATAYM-----EEAERFDWLVAMNAGEILATGSAQQLR 236
Cdd:PRK13549 158 LNKQARLLILDEPTA---SLTESETAVLLDIIRDLKAHG---IACIYIshklnEVKAISDTICVIRDGRHIGTRPAAGMT 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 237 akthsatlEQAFIALLPE---AQRQAHKPvvippyHAEQEEIaIEAKDLTM-----RFGKfvAVDHVNFRIPRGEIFGFL 308
Cdd:PRK13549 232 --------EDDIITMMVGrelTALYPREP------HTIGEVI-LEVRNLTAwdpvnPHIK--RVDDVSFSLRRGEILGIA 294
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 309 GSNGCGKSTTMKMLTGLLP-ASEGQAWLFGQPVD---------------PNDidtRRRVGYMSQAFSLYN-ELTVRQNLE 371
Cdd:PRK13549 295 GLVGAGRTELVQCLFGAYPgRWEGEIFIDGKPVKirnpqqaiaqgiamvPED---RKRDGIVPVMGVGKNiTLAALDRFT 371
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 372 LHARLFHipPAEIPArVAQMIERFMLTEVEDTLP-ASLPLGIRQRLSLAVAVIHRPEMLILDEPTSGVDPVARDMFWQLM 450
Cdd:PRK13549 372 GGSRIDD--AAELKT-ILESIQRLKVKTASPELAiARLSGGNQQKAVLAKCLLLNPKILILDEPTRGIDVGAKYEIYKLI 448
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*.
gi 446125071 451 VDLSRQDKVTIFISTHFMNEAERCDRMSLMHAGKVLASGTPQELVQQRgaaNLEAA 506
Cdd:PRK13549 449 NQLVQQGVAIIVISSELPEVLGLSDRVLVMHEGKLKGDLINHNLTQEQ---VMEAA 501
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
281-494 |
4.87e-26 |
|
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: 110.58 E-value: 4.87e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 281 DLTMRFGKFvAVDhVNFRIPRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGQAWLFGQPV--DPNDIDT---RRRVGYMS 355
Cdd:COG4148 6 DFRLRRGGF-TLD-VDFTLPGRGVTALFGPSGSGKTTLLRAIAGLERPDSGRIRLGGEVLqdSARGIFLpphRRRIGYVF 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 356 QAFSLYNELTVRQNLELHARlfHIPPAEIPARVAQMIERFMLTEVEDTLPASLPLGIRQRLSLAVAVIHRPEMLILDEPT 435
Cdd:COG4148 84 QEARLFPHLSVRGNLLYGRK--RAPRAERRISFDEVVELLGIGHLLDRRPATLSGGERQRVAIGRALLSSPRLLLMDEPL 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446125071 436 SGVDPVARDmfwQLM---VDLSRQDKVTIFISTHFMNEAER-CDRMSLMHAGKVLASGTPQEL 494
Cdd:COG4148 162 AALDLARKA---EILpylERLRDELDIPILYVSHSLDEVARlADHVVLLEQGRVVASGPLAEV 221
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
277-508 |
5.79e-26 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 110.81 E-value: 5.79e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 277 IEAKDLTMRFGKFVAVDHVNFRIPRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGQAWLFGQpvDPNDIDTRRR-VGYMS 355
Cdd:PRK09452 15 VELRGISKSFDGKEVISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLDGQ--DITHVPAENRhVNTVF 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 356 QAFSLYNELTVRQNLELHARLFHIPPAEIPARVAQMIERFMLTEVEDTLPASLPLGIRQRLSLAVAVIHRPEMLILDEPT 435
Cdd:PRK09452 93 QSYALFPHMTVFENVAFGLRMQKTPAAEITPRVMEALRMVQLEEFAQRKPHQLSGGQQQRVAIARAVVNKPKVLLLDESL 172
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446125071 436 SGVDPVARDMFWQLMVDLSRQDKVT-IFIsTHFMNEA-ERCDRMSLMHAGKVLASGTPQELVQQrgAANLEAA-FI 508
Cdd:PRK09452 173 SALDYKLRKQMQNELKALQRKLGITfVFV-THDQEEAlTMSDRIVVMRDGRIEQDGTPREIYEE--PKNLFVArFI 245
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
30-230 |
6.34e-26 |
|
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: 106.61 E-value: 6.34e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 30 NITLDIPArSMVGLIGPDGVGKSSLLSLISGARVIEQGNVIVLGGDMRDAKHRRDVCP---RIAWMPQGLGknLYHTLSV 106
Cdd:cd03297 16 KIDFDLNE-EVTGIFGASGAGKSTLLRCIAGLEKPDGGTIVLNGTVLFDSRKKINLPPqqrKIGLVFQQYA--LFPHLNV 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 107 YENVDFFARlfGHDKAEREARITELLNSTGLAPFRDRPAGKLSGGMKQKLGLCCALIHDPELLILDEPTTGVDPLSRAQf 186
Cdd:cd03297 93 RENLAFGLK--RKRNREDRISVDELLDLLGLDHLLNRYPAQLSGGEKQRVALARALAAQPELLLLDEPFSALDRALRLQ- 169
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 446125071 187 wdLIDSIRQRQT--NMSVLVATAYMEEAERF-DWLVAMNAGEILATG 230
Cdd:cd03297 170 --LLPELKQIKKnlNIPVIFVTHDLSEAEYLaDRIVVMEDGRLQYIG 214
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
276-494 |
8.49e-26 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 108.35 E-value: 8.49e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 276 AIEAKDLTMRF--GKFVAVDHVNFRIPRGEIFGFLGSNGCGKSTTMKMLTGLL---PASEGQAWLFGQPVDPNDI-DTRR 349
Cdd:PRK13640 5 IVEFKHVSFTYpdSKKPALNDISFSIPRGSWTALIGHNGSGKSTISKLINGLLlpdDNPNSKITVDGITLTAKTVwDIRE 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 350 RVGYMSQ---------------AFSLYNeltvRQnlelharlfhIPPAEIPARVAQMIERFMLTEVEDTLPASLPLGIRQ 414
Cdd:PRK13640 85 KVGIVFQnpdnqfvgatvgddvAFGLEN----RA----------VPRPEMIKIVRDVLADVGMLDYIDSEPANLSGGQKQ 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 415 RLSLAVAVIHRPEMLILDEPTSGVDPVARDMFWQLMVDLSRQDKVTIFISTHFMNEAERCDRMSLMHAGKVLASGTPQEL 494
Cdd:PRK13640 151 RVAIAGILAVEPKIIILDESTSMLDPAGKEQILKLIRKLKKKNNLTVISITHDIDEANMADQVLVLDDGKLLAQGSPVEI 230
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
277-497 |
1.17e-25 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 107.58 E-value: 1.17e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 277 IEAKDLTMRF-GKFVAVDHVNFRIPRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGQAWLFGQPVDPNDI-DTRRRVGYM 354
Cdd:PRK13652 4 IETRDLCYSYsGSKEALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIRGEPITKENIrEVRKFVGLV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 355 -----SQAFSLynelTVRQNLELHARLFHIPPAEIPARVAQMIERFMLTEVEDTLPASLPLGIRQRLSLAVAVIHRPEML 429
Cdd:PRK13652 84 fqnpdDQIFSP----TVEQDIAFGPINLGLDEETVAHRVSSALHMLGLEELRDRVPHHLSGGEKKRVAIAGVIAMEPQVL 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446125071 430 ILDEPTSGVDPVARDMFWQLMVDLSRQDKVTIFISTHFMN-EAERCDRMSLMHAGKVLASGTPQELVQQ 497
Cdd:PRK13652 160 VLDEPTAGLDPQGVKELIDFLNDLPETYGMTVIFSTHQLDlVPEMADYIYVMDKGRIVAYGTVEEIFLQ 228
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
14-212 |
1.43e-25 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 106.87 E-value: 1.43e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 14 QLEGVSQHYGK----TVALNNITLDIPARSMVGLIGPDGVGKSSLLSLISG-----ARVIEQGNVIVLGGDMRDA----K 80
Cdd:COG4525 5 TVRHVSVRYPGggqpQPALQDVSLTIESGEFVVALGASGCGKTTLLNLIAGflapsSGEITLDGVPVTGPGADRGvvfqK 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 81 HrrdvcpriAWMPQglgknlyhtLSVYENVDFFARLFGHDKAEREARITELLNSTGLAPFRDRPAGKLSGGMKQKLGLCC 160
Cdd:COG4525 85 D--------ALLPW---------LNVLDNVAFGLRLRGVPKAERRARAEELLALVGLADFARRRIWQLSGGMRQRVGIAR 147
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 446125071 161 ALIHDPELLILDEPTTGVDPLSRAQFWDLIDSIRQRqTNMSVLVATAYMEEA 212
Cdd:COG4525 148 ALAADPRFLLMDEPFGALDALTREQMQELLLDVWQR-TGKGVFLITHSVEEA 198
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
14-238 |
1.99e-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: 1.99e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 14 QLEGVSQHYG--KTVALNNITLDIPARSMVGLIGPDGVGKSSLLSLISGARVIEQGNVIVLGGDMR--DAKHRRDvcpRI 89
Cdd:COG2274 475 ELENVSFRYPgdSPPVLDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEPTSGRILIDGIDLRqiDPASLRR---QI 551
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 90 AWMPQGLgkNLYHTlSVYENVdffarLFGHDKAEREaRITELLNSTGLAPF-RDRPAG----------KLSGGMKQKLGL 158
Cdd:COG2274 552 GVVLQDV--FLFSG-TIRENI-----TLGDPDATDE-EIIEAARLAGLHDFiEALPMGydtvvgeggsNLSGGQRQRLAI 622
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 159 CCALIHDPELLILDEPTTGVDPLSRAQFwdlIDSIRQRQTNMSVLVATAYMEEAERFDWLVAMNAGEILATGSAQQLRAK 238
Cdd:COG2274 623 ARALLRNPRILILDEATSALDAETEAII---LENLRRLLKGRTVIIIAHRLSTIRLADRIIVLDKGRIVEDGTHEELLAR 699
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
279-496 |
2.04e-25 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 106.13 E-value: 2.04e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 279 AKDLTMRFGKFVAVDHVNFRIPRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGQAwlfgqPVDPNDID-------TRRRV 351
Cdd:PRK10895 6 AKNLAKAYKGRRVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNI-----IIDDEDISllplharARRGI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 352 GYMSQAFSLYNELTVRQNLELHARLFHIPPAEIPA-RVAQMIERFMLTEVEDTLPASLPLGIRQRLSLAVAVIHRPEMLI 430
Cdd:PRK10895 81 GYLPQEASIFRRLSVYDNLMAVLQIRDDLSAEQREdRANELMEEFHIEHLRDSMGQSLSGGERRRVEIARALAANPKFIL 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446125071 431 LDEPTSGVDPVARDMFWQLMVDLsRQDKVTIFISTHFMNEA-ERCDRMSLMHAGKVLASGTPQELVQ 496
Cdd:PRK10895 161 LDEPFAGVDPISVIDIKRIIEHL-RDSGLGVLITDHNVRETlAVCERAYIVSQGHLIAHGTPTEILQ 226
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
276-504 |
2.13e-25 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 108.67 E-value: 2.13e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 276 AIEAKDLTMRFGKFVAVDHVNFRIPRGEIFGFLGSNGCGKSTtmkmltGLLPA------SEGQAWLFGQPVdPNDIDTRR 349
Cdd:NF000106 13 AVEVRGLVKHFGEVKAVDGVDLDVREGTVLGVLGP*GAA**R------GALPAhv*gpdAGRRPWRF*TWC-ANRRALRR 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 350 RVGYMSQAFSLYNE-LTVRQNLELHARLFHIPPAEIPARVAQMIERFMLTEVEDTLPASLPLGIRQRLSLAVAVIHRPEM 428
Cdd:NF000106 86 TIG*HRPVR*GRREsFSGRENLYMIGR*LDLSRKDARARADELLERFSLTEAAGRAAAKYSGGMRRRLDLAASMIGRPAV 165
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446125071 429 LILDEPTSGVDPVARDMFWQLMVDLSRqDKVTIFISTHFMNEAER-CDRMSLMHAGKVLASGTPQELVQQRGAANLE 504
Cdd:NF000106 166 LYLDEPTTGLDPRTRNEVWDEVRSMVR-DGATVLLTTQYMEEAEQlAHELTVIDRGRVIADGKVDELKTKVGGRTLQ 241
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
290-499 |
2.14e-25 |
|
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a central component of the secretion machinery that translocates the toxin, hemolysin A, in a Sec-independent fashion across both membranes of E. coli. The hemolysin A (HlyA) transport machinery is composed of the ATP-binding cassette (ABC) transporter HlyB located in the inner membrane, hemolysin D (HlyD), also anchored in the inner membrane, and TolC, which resides in the outer membrane. HlyD apparently forms a continuous channel that bridges the entire periplasm, interacting with TolC and HlyB. This arrangement prevents the appearance of periplasmic intermediates of HlyA during substrate transport. Little is known about the molecular details of HlyA transport, but it is evident that ATP-hydrolysis by the ABC-transporter HlyB is a necessary source of energy.
Pssm-ID: 213219 [Multi-domain] Cd Length: 237 Bit Score: 105.65 E-value: 2.14e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 290 VAVDHVNFRIPRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGQAWlfgqpVDPNDIDT------RRRVGYMSQAFSLYNE 363
Cdd:cd03252 16 VILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVL-----VDGHDLALadpawlRRQVGVVLQENVLFNR 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 364 lTVRQNLELHARLFHIPPAEIPARVAQMIERFM-LTEVEDTL----PASLPLGIRQRLSLAVAVIHRPEMLILDEPTSGV 438
Cdd:cd03252 91 -SIRDNIALADPGMSMERVIEAAKLAGAHDFISeLPEGYDTIvgeqGAGLSGGQRQRIAIARALIHNPRILIFDEATSAL 169
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446125071 439 DPVARDMFWQLMVDLSrqDKVTIFISTHFMNEAERCDRMSLMHAGKVLASGTPQELVQQRG 499
Cdd:cd03252 170 DYESEHAIMRNMHDIC--AGRTVIIIAHRLSTVKNADRIIVMEKGRIVEQGSHDELLAENG 228
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
14-264 |
2.37e-25 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 108.35 E-value: 2.37e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 14 QLEGVSQHY----GKTVALNNITLDIPARSMVGLIGPDGVGKSSLLSLISGARVIEQGNVIVLGGDM--------RDAkh 81
Cdd:PRK11153 3 ELKNISKVFpqggRTIHALNNVSLHIPAGEIFGVIGASGAGKSTLIRCINLLERPTSGRVLVDGQDLtalsekelRKA-- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 82 RRdvcpRIAWMPQGLgkNLYHTLSVYENVDFFARLFGHDKAEREARITELLNSTGLAPFRDR-PAgKLSGGMKQKLGLCC 160
Cdd:PRK11153 81 RR----QIGMIFQHF--NLLSSRTVFDNVALPLELAGTPKAEIKARVTELLELVGLSDKADRyPA-QLSGGQKQRVAIAR 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 161 ALIHDPELLILDEPTTGVDPLSRAQFWDLIDSIrQRQTNMSVLVATAYMEEAERF-DWLVAMNAGEILATGS-------- 231
Cdd:PRK11153 154 ALASNPKVLLCDEATSALDPATTRSILELLKDI-NRELGLTIVLITHEMDVVKRIcDRVAVIDAGRLVEQGTvsevfshp 232
|
250 260 270
....*....|....*....|....*....|....*..
gi 446125071 232 ----AQQLRAKTHSATLEQAFIALLPEAQRQAHKPVV 264
Cdd:PRK11153 233 khplTREFIQSTLHLDLPEDYLARLQAEPTTGSGPLL 269
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
27-238 |
2.42e-25 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 107.87 E-value: 2.42e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 27 ALNNITLDIPARSMVGLIGPDGVGKSSLLSLISGARVIEQGNVIVLGgdMRDAKHRRDVCPRIAW-MPQglgKN-LYHTL 104
Cdd:COG4586 37 AVDDISFTIEPGEIVGFIGPNGAGKSTTIKMLTGILVPTSGEVRVLG--YVPFKRRKEFARRIGVvFGQ---RSqLWWDL 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 105 SVYENVDFFARLFGHDKAEREARI---TELLnstGLAPFRDRPAGKLSGGMKQKLGLCCALIHDPELLILDEPTTGVDPL 181
Cdd:COG4586 112 PAIDSFRLLKAIYRIPDAEYKKRLdelVELL---DLGELLDTPVRQLSLGQRMRCELAAALLHRPKILFLDEPTIGLDVV 188
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 446125071 182 SRAQFWDLIDSIRQRQtNMSVLVATAYMEEAERF-DWLVAMNAGEILATGSAQQLRAK 238
Cdd:COG4586 189 SKEAIREFLKEYNRER-GTTILLTSHDMDDIEALcDRVIVIDHGRIIYDGSLEELKER 245
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
6-231 |
2.67e-25 |
|
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim protein) in eukaryotes. It is the member of ABC transporter superfamily. Rim protein is a membrane glycoprotein which is localized in the photoreceptor outer segment discs. Mutation/s in its genetic loci is implicated in the recessive Stargardt's disease. [Transport and binding proteins, Other]
Pssm-ID: 130324 [Multi-domain] Cd Length: 2272 Bit Score: 113.57 E-value: 2.67e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 6 LVPVPPVAQLEGVSQHYGKTvALNNITLDIPARSMVGLIGPDGVGKSSLLSLISGARVIEQGNVIVLGGDMR---DA-KH 81
Cdd:TIGR01257 925 LVPGVCVKNLVKIFEPSGRP-AVDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGKDIEtnlDAvRQ 1003
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 82 RRDVCPRiawmpqglGKNLYHTLSVYENVDFFARLFGHDKAEREARITELLNSTGLAPFRDRPAGKLSGGMKQKLGLCCA 161
Cdd:TIGR01257 1004 SLGMCPQ--------HNILFHHLTVAEHILFYAQLKGRSWEEAQLEMEAMLEDTGLHHKRNEEAQDLSGGMQRKLSVAIA 1075
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446125071 162 LIHDPELLILDEPTTGVDPLSRAQFWDLIDSIRQRQTnmsVLVATAYMEEAERF-DWLVAMNAGEILATGS 231
Cdd:TIGR01257 1076 FVGDAKVVVLDEPTSGVDPYSRRSIWDLLLKYRSGRT---IIMSTHHMDEADLLgDRIAIISQGRLYCSGT 1143
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
14-206 |
4.36e-25 |
|
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: 104.03 E-value: 4.36e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 14 QLEGVSQHY-GKTVALNNITLDIPARSMVGLIGPDGVGKSSLLSLISGARVIEQGNVIVLGGDMRDAKHRRdvcprIAWM 92
Cdd:cd03292 2 EFINVTKTYpNGTAALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQDVSDLRGRA-----IPYL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 93 PQGLG------KNLYHtLSVYENVDFFARLFGHDKAEREARITELLNSTGLAPFRDRPAGKLSGGMKQKLGLCCALIHDP 166
Cdd:cd03292 77 RRKIGvvfqdfRLLPD-RNVYENVAFALEVTGVPPREIRKRVPAALELVGLSHKHRALPAELSGGEQQRVAIARAIVNSP 155
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 446125071 167 ELLILDEPTTGVDPLSRAQFWDLIDSIRQRQTnmSVLVAT 206
Cdd:cd03292 156 TILIADEPTGNLDPDTTWEIMNLLKKINKAGT--TVVVAT 193
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
14-212 |
7.24e-25 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 104.78 E-value: 7.24e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 14 QLEGVSQHYGKTVALNNITLDIPARSMVGLIGPDGVGKSSLLSLISGARVIEQGNVIVLGGDMRDAKHRRDVcpriawMP 93
Cdd:PRK11248 3 QISHLYADYGGKPALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDGKPVEGPGAERGV------VF 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 94 QGLGknLYHTLSVYENVDFFARLFGHDKAEREARITELLNSTGLAPFRDRPAGKLSGGMKQKLGLCCALIHDPELLILDE 173
Cdd:PRK11248 77 QNEG--LLPWRNVQDNVAFGLQLAGVEKMQRLEIAHQMLKKVGLEGAEKRYIWQLSGGQRQRVGIARALAANPQLLLLDE 154
|
170 180 190
....*....|....*....|....*....|....*....
gi 446125071 174 PTTGVDPLSRAQFWDLIDSIRQRqTNMSVLVATAYMEEA 212
Cdd:PRK11248 155 PFGALDAFTREQMQTLLLKLWQE-TGKQVLLITHDIEEA 192
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
277-494 |
7.78e-25 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 105.17 E-value: 7.78e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 277 IEAKDLTMRFGKFVAVDHVN---FRIPRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGQAWLFGQPVDPNDI-DTRRRVG 352
Cdd:PRK13642 5 LEVENLVFKYEKESDVNQLNgvsFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDGELLTAENVwNLRRKIG 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 353 YMSQ-AFSLYNELTVRQNLELHARLFHIPPAEIPARVAQMIERFMLTEVEDTLPASLPLGIRQRLSLAVAVIHRPEMLIL 431
Cdd:PRK13642 85 MVFQnPDNQFVGATVEDDVAFGMENQGIPREEMIKRVDEALLAVNMLDFKTREPARLSGGQKQRVAVAGIIALRPEIIIL 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446125071 432 DEPTSGVDPVARDMFWQLMVDLSRQDKVTIFISTHFMNEAERCDRMSLMHAGKVLASGTPQEL 494
Cdd:PRK13642 165 DESTSMLDPTGRQEIMRVIHEIKEKYQLTVLSITHDLDEAASSDRILVMKAGEIIKEAAPSEL 227
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
291-496 |
8.00e-25 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 105.49 E-value: 8.00e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 291 AVDHVNFRIPRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGQAWLfGQPV-----DPNDIDT-RRRVGYM-----SQAFs 359
Cdd:PRK13634 22 ALYDVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVTI-GERVitagkKNKKLKPlRKKVGIVfqfpeHQLF- 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 360 lynELTVRQNLELHARLFHIPPAEIPARVAQMIERFMLTE-VEDTLPASLPLGIRQRLSLAVAVIHRPEMLILDEPTSGV 438
Cdd:PRK13634 100 ---EETVEKDICFGPMNFGVSEEDAKQKAREMIELVGLPEeLLARSPFELSGGQMRRVAIAGVLAMEPEVLVLDEPTAGL 176
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446125071 439 DPVAR----DMFWQlmvdLSRQDKVTIFISTHFMNEAER-CDRMSLMHAGKVLASGTPQELVQ 496
Cdd:PRK13634 177 DPKGRkemmEMFYK----LHKEKGLTTVLVTHSMEDAARyADQIVVMHKGTVFLQGTPREIFA 235
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
291-499 |
9.36e-25 |
|
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan exporter ATP-binding protein. In A. tumefaciens cyclic beta-1, 2-glucan must be transported into the periplasmic space to exert its action as a virulence factor. This subfamily belongs to the MRP-like family and is involved in drug, peptide, and lipid export. The MRP-like family, similar to all ABC proteins, have a common four-domain core structure constituted by two membrane-spanning domains each composed of six transmembrane (TM) helices and two nucleotide-binding domains (NBD). ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213221 [Multi-domain] Cd Length: 229 Bit Score: 103.46 E-value: 9.36e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 291 AVDHVNFRIPRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGQAWLFGQPVdpNDIDT---RRRVGYMSQAFSLYNElTVR 367
Cdd:cd03254 18 VLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGIDI--RDISRkslRSMIGVVLQDTFLFSG-TIM 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 368 QNLelhaRLFH-IPPAE---IPARVAQMIERFM-LTEVEDTLP----ASLPLGIRQRLSLAVAVIHRPEMLILDEPTSGV 438
Cdd:cd03254 95 ENI----RLGRpNATDEeviEAAKEAGAHDFIMkLPNGYDTVLgengGNLSQGERQLLAIARAMLRDPKILILDEATSNI 170
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446125071 439 DPVARDMFWQLMVDLsRQDKVTIFIStHFMNEAERCDRMSLMHAGKVLASGTPQELVQQRG 499
Cdd:cd03254 171 DTETEKLIQEALEKL-MKGRTSIIIA-HRLSTIKNADKILVLDDGKIIEEGTHDELLAKKG 229
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
277-496 |
1.03e-24 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 104.02 E-value: 1.03e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 277 IEAKDLTMRFGKFVAVDHVNFRIPRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGQAWLFGQPVDPNDIDT---RRRVGY 353
Cdd:PRK09493 2 IEFKNVSKHFGPTQVLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGLKVNDPKVDErliRQEAGM 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 354 MSQAFSLYNELTVRQNL---ELHARLFHIPPAEIPARvaQMIERFMLTEVEDTLPASLPLGIRQRLSLAVAVIHRPEMLI 430
Cdd:PRK09493 82 VFQQFYLFPHLTALENVmfgPLRVRGASKEEAEKQAR--ELLAKVGLAERAHHYPSELSGGQQQRVAIARALAVKPKLML 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446125071 431 LDEPTSGVDPVARDMFWQLMVDLSrQDKVTIFISTHFMNEAERC-DRMSLMHAGKVLASGTPQELVQ 496
Cdd:PRK09493 160 FDEPTSALDPELRHEVLKVMQDLA-EEGMTMVIVTHEIGFAEKVaSRLIFIDKGRIAEDGDPQVLIK 225
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
14-226 |
2.09e-24 |
|
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: 102.22 E-value: 2.09e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 14 QLEGVSQHYGKTVALNNITLDIPARSMVGLIGPDGVGKSSLLSLISGARVIEQGNVIVLGGDMRDAKhrrdvcPRIAWMP 93
Cdd:cd03262 2 EIKNLHKSFGDFHVLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIDGLKLTDDK------KNINELR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 94 QGLGK-----NLYHTLSVYENVDFFAR-LFGHDKAEREARITELLNSTGLAPFRDRPAGKLSGGMKQKLGLCCALIHDPE 167
Cdd:cd03262 76 QKVGMvfqqfNLFPHLTVLENITLAPIkVKGMSKAEAEERALELLEKVGLADKADAYPAQLSGGQQQRVAIARALAMNPK 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446125071 168 LLILDEPTTGVDP-LSRaqfwDLIDSIRQ-RQTNMSVLVATAYMEEA-ERFDWLVAMNAGEI 226
Cdd:cd03262 156 VMLFDEPTSALDPeLVG----EVLDVMKDlAEEGMTMVVVTHEMGFArEVADRVIFMDDGRI 213
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
277-498 |
2.21e-24 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 103.17 E-value: 2.21e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 277 IEAKDLTMRFGKFVAVDHVNFRIPRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGQAWLFGQP----------------- 339
Cdd:PRK11231 3 LRTENLTVGYGTKRILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDKPismlssrqlarrlallp 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 340 ---VDPNDIDTRRRVGY-MSQAFSLYNELTVRQNlelharlfhippaeipARVAQMIERFMLTEVEDTLPASLPLGIRQR 415
Cdd:PRK11231 83 qhhLTPEGITVRELVAYgRSPWLSLWGRLSAEDN----------------ARVNQAMEQTRINHLADRRLTDLSGGQRQR 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 416 LSLAVAVIHRPEMLILDEPTSGVDPVARDMFWQLMVDLSRQDKvTIFISTHFMNEAER-CDRMSLMHAGKVLASGTPQEL 494
Cdd:PRK11231 147 AFLAMVLAQDTPVVLLDEPTTYLDINHQVELMRLMRELNTQGK-TVVTVLHDLNQASRyCDHLVVLANGHVMAQGTPEEV 225
|
....
gi 446125071 495 VQQR 498
Cdd:PRK11231 226 MTPG 229
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
281-503 |
2.52e-24 |
|
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding cassette (ABC) protein of the three subunit molybdate ABC transporter. The three proteins of this complex are homologous to proteins of the sulfate ABC transporter. Molybdenum may be used in nitrogenases of nitrogen-fixing bacteria and in molybdopterin cofactors. In some cases, molybdate may be transported by a sulfate transporter rather than by a specific molybdate transporter. [Transport and binding proteins, Anions]
Pssm-ID: 131197 [Multi-domain] Cd Length: 354 Bit Score: 105.58 E-value: 2.52e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 281 DLTMRFGKFvAVDhVNFRIPRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGQAWLFGQPVDPND--IDT---RRRVGYMS 355
Cdd:TIGR02142 4 RFSKRLGDF-SLD-ADFTLPGQGVTAIFGRSGSGKTTLIRLIAGLTRPDEGEIVLNGRTLFDSRkgIFLppeKRRIGYVF 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 356 QAFSLYNELTVRQNLELHARlfHIPPAEIPARVAQMIERFMLTEVEDTLPASLPLGIRQRLSLAVAVIHRPEMLILDEPT 435
Cdd:TIGR02142 82 QEARLFPHLSVRGNLRYGMK--RARPSERRISFERVIELLGIGHLLGRLPGRLSGGEKQRVAIGRALLSSPRLLLMDEPL 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446125071 436 SGVDPVARDMFWQLMVDLSRQDKVTIFISTHFMNEAER-CDRMSLMHAGKVLASGTPQElVQQRGAANL 503
Cdd:TIGR02142 160 AALDDPRKYEILPYLERLHAEFGIPILYVSHSLQEVLRlADRVVVLEDGRVAAAGPIAE-VWASPDLPW 227
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
22-235 |
3.02e-24 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 102.68 E-value: 3.02e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 22 YGKTVALNNITLDIPARSMVGLIGPDGVGKSSLLSLISgaRVIE-------QGNVIVLGGD---MRDAKHRRDVcPRIAW 91
Cdd:PRK14247 13 FGQVEVLDGVNLEIPDNTITALMGPSGSGKSTLLRVFN--RLIElypearvSGEVYLDGQDifkMDVIELRRRV-QMVFQ 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 92 MPqglgkNLYHTLSVYENVDFFARL--FGHDKAEREARITELLNSTGL-APFRDR---PAGKLSGGMKQKLGLCCALIHD 165
Cdd:PRK14247 90 IP-----NPIPNLSIFENVALGLKLnrLVKSKKELQERVRWALEKAQLwDEVKDRldaPAGKLSGGQQQRLCIARALAFQ 164
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446125071 166 PELLILDEPTTGVDPLSRAQFWDLIDSIRQrqtNMSVLVATAYMEEAERF-DWLVAMNAGEILATGSAQQL 235
Cdd:PRK14247 165 PEVLLADEPTANLDPENTAKIESLFLELKK---DMTIVLVTHFPQQAARIsDYVAFLYKGQIVEWGPTREV 232
|
|
| LPS_export_lptB |
TIGR04406 |
LPS export ABC transporter ATP-binding protein; Members of this fmaily are LptB, the ... |
14-235 |
3.22e-24 |
|
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: 102.35 E-value: 3.22e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 14 QLEGVSQHYGKTVALNNITLDIPARSMVGLIGPDGVGKSSLLSLISGARVIEQGNVIVLGGDMRDAK-HRRdvcPR--IA 90
Cdd:TIGR04406 3 VAENLIKSYKKRKVVNDVSLSVKSGEIVGLLGPNGAGKTTSFYMIVGLVRPDAGKILIDGQDITHLPmHER---ARlgIG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 91 WMPQGlgKNLYHTLSVYENVDFFARLFGH-DKAEREARITELLNSTGLAPFRDRPAGKLSGGMKQKLGLCCALIHDPELL 169
Cdd:TIGR04406 80 YLPQE--ASIFRKLTVEENIMAVLEIRKDlDRAEREERLEALLEEFQISHLRDNKAMSLSGGERRRVEIARALATNPKFI 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446125071 170 ILDEPTTGVDPLSRAQFWDLIDSIRQRqtNMSVLVA------------TAYMeeaerfdwlvaMNAGEILATGSAQQL 235
Cdd:TIGR04406 158 LLDEPFAGVDPIAVGDIKKIIKHLKER--GIGVLITdhnvretldicdRAYI-----------ISDGKVLAEGTPAEI 222
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
14-235 |
3.34e-24 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 102.41 E-value: 3.34e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 14 QLEGVSQHYGKTVALNNITLDIPARSMVGLIGPDGVGKSSLLSLISGARVIEQGNVIVLGGDM-RDAKHRRdvcpriAWM 92
Cdd:COG1137 5 EAENLVKSYGKRTVVKDVSLEVNQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGRIFLDGEDItHLPMHKR------ARL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 93 pqGLGknlY--------HTLSVYENVDFFARLFGHDKAEREARITELLNSTGLAPFRDRPAGKLSGGMKQKLGLCCALIH 164
Cdd:COG1137 79 --GIG---YlpqeasifRKLTVEDNILAVLELRKLSKKEREERLEELLEEFGITHLRKSKAYSLSGGERRRVEIARALAT 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 165 DPELLILDEPTTGVDPLSRAQFWDLIDSIRQRqtNMSVLVA------------TAYMeeaerfdwlvaMNAGEILATGSA 232
Cdd:COG1137 154 NPKFILLDEPFAGVDPIAVADIQKIIRHLKER--GIGVLITdhnvretlgicdRAYI-----------ISEGKVLAEGTP 220
|
...
gi 446125071 233 QQL 235
Cdd:COG1137 221 EEI 223
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
295-489 |
4.02e-24 |
|
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ABC transporters homologous to the Drosophila white gene, which acts as a dimeric importer for eye pigment precursors. The eye pigmentation of Drosophila is developed from the synthesis and deposition in the cells of red pigments, which are synthesized from guanine, and brown pigments, which are synthesized from tryptophan. The pigment precursors are encoded by the white, brown, and scarlet genes, respectively. Evidence from genetic and biochemical studies suggest that the White and Brown proteins function as heterodimers to import guanine, while the White and Scarlet proteins function to import tryptophan. However, a recent study also suggests that White may be involved in the transport of a metabolite, such as 3-hydroxykynurenine, across intracellular membranes. Mammalian ABC transporters belonging to the White subfamily (ABCG1, ABCG5, and ABCG8) have been shown to be involved in the regulation of lipid-trafficking mechanisms in macrophages, hepatocytes, and intestinal mucosa cells. ABCG1 (ABC8), the human homolog of the Drosophila white gene is induced in monocyte-derived macrophages during cholesterol influx mediated by acetylated low-density lipoprotein. It is possible that human ABCG1 forms heterodimers with several heterologous partners.
Pssm-ID: 213201 [Multi-domain] Cd Length: 226 Bit Score: 101.58 E-value: 4.02e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 295 VNFRIPRGEIFGFLGSNGCGKSTTMKMLTGLLP---ASEGQAWLFGQPVDPNDidTRRRVGYMSQAFSLYNELTVRQNLE 371
Cdd:cd03234 26 VSLHVESGQVMAILGSSGSGKTTLLDAISGRVEgggTTSGQILFNGQPRKPDQ--FQKCVAYVRQDDILLPGLTVRETLT 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 372 LHARL---FHIPPAEIPARVAQMIERFM-LTEVEDTLPASLPLGIRQRLSLAVAVIHRPEMLILDEPTSGVDPVARDMFW 447
Cdd:cd03234 104 YTAILrlpRKSSDAIRKKRVEDVLLRDLaLTRIGGNLVKGISGGERRRVSIAVQLLWDPKVLILDEPTSGLDSFTALNLV 183
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 446125071 448 QLMVDLSRQDKvTIFISTH------FmneaERCDRMSLMHAGKVLASG 489
Cdd:cd03234 184 STLSQLARRNR-IVILTIHqprsdlF----RLFDRILLLSSGEIVYSG 226
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
14-245 |
5.49e-24 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 104.43 E-value: 5.49e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 14 QLEGVSQHYGKTVALNNITLDIPARSMVGLIGPDGVG--KSSLLSLISGARVIEQGNVIVLGGDMRDAKHRRDVCPRiaw 91
Cdd:NF000106 15 EVRGLVKHFGEVKAVDGVDLDVREGTVLGVLGP*GAA**RGALPAHV*GPDAGRRPWRF*TWCANRRALRRTIG*HR--- 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 92 mPQGLGKNlyHTLSVYENVDFFARLFGHDKAEREARITELLNSTGLAPFRDRPAGKLSGGMKQKLGLCCALIHDPELLIL 171
Cdd:NF000106 92 -PVR*GRR--ESFSGRENLYMIGR*LDLSRKDARARADELLERFSLTEAAGRAAAKYSGGMRRRLDLAASMIGRPAVLYL 168
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446125071 172 DEPTTGVDPLSRAQFWDLIDSIrqRQTNMSVLVATAYMEEAERF-DWLVAMNAGEILATGSAQQLRAKTHSATLE 245
Cdd:NF000106 169 DEPTTGLDPRTRNEVWDEVRSM--VRDGATVLLTTQYMEEAEQLaHELTVIDRGRVIADGKVDELKTKVGGRTLQ 241
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
14-235 |
5.82e-24 |
|
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440743 [Multi-domain] Cd Length: 239 Bit Score: 101.61 E-value: 5.82e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 14 QLEGVSQHYGKTVALNNITLDIPARSMVGLIGPDGVGKSSLLSLISGARVIEQGNVIVLGGDM-RDAKHRRDVCPRIAWM 92
Cdd:COG1126 3 EIENLHKSFGDLEVLKGISLDVEKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTITVDGEDLtDSKKDINKLRRKVGMV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 93 PQGLgkNLYHTLSVYENVdFFA--RLFGHDKAEREARITELLNSTGLAPFRDRPAGKLSGGMKQKLGLCCALIHDPELLI 170
Cdd:COG1126 83 FQQF--NLFPHLTVLENV-TLApiKVKKMSKAEAEERAMELLERVGLADKADAYPAQLSGGQQQRVAIARALAMEPKVML 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446125071 171 LDEPTTGVDP-LSRaqfwDLIDSIRQ-RQTNMSVLVATAYMEEAER-FDWLVAMNAGEILATGSAQQL 235
Cdd:COG1126 160 FDEPTSALDPeLVG----EVLDVMRDlAKEGMTMVVVTHEMGFAREvADRVVFMDGGRIVEEGPPEEF 223
|
|
| anch_rpt_ABC |
TIGR03771 |
anchored repeat-type ABC transporter, ATP-binding subunit; This protein family is the ... |
297-494 |
8.87e-24 |
|
anchored repeat-type ABC transporter, ATP-binding subunit; This protein family is the ATP-binding cassette subunit of binding protein-dependent ABC transporter complex that strictly co-occurs with TIGR03769. TIGRFAMs model TIGR03769 describes a protein domain that occurs singly or as one of up to three repeats in proteins of a number of Actinobacteria, including Propionibacterium acnes KPA171202. The TIGR03769 domain occurs both in an adjacent gene for the substrate-binding protein and in additional (often nearby) proteins, often with LPXTG-like sortase recognition signals. Homologous ATP-binding subunits outside the scope of this family include manganese transporter MntA in Synechocystis sp. PCC 6803 and chelated iron transporter subunits. The function of this transporter complex is unknown. [Transport and binding proteins, Unknown substrate]
Pssm-ID: 163483 [Multi-domain] Cd Length: 223 Bit Score: 100.70 E-value: 8.87e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 297 FRIPRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGQAWLFGQPVDPNdidtRRRVGYMSQ--AFSLYNELTVRQNLeLHA 374
Cdd:TIGR03771 1 LSADKGELLGLLGPNGAGKTTLLRAILGLIPPAKGTVKVAGASPGKG----WRHIGYVPQrhEFAWDFPISVAHTV-MSG 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 375 RLFHIPPAEIPAR-----VAQMIERFMLTEVEDTLPASLPLGIRQRLSLAVAVIHRPEMLILDEPTSGVDPVARDMFWQL 449
Cdd:TIGR03771 76 RTGHIGWLRRPCVadfaaVRDALRRVGLTELADRPVGELSGGQRQRVLVARALATRPSVLLLDEPFTGLDMPTQELLTEL 155
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 446125071 450 MVDLSrQDKVTIFISTHFMNEA-ERCDRMSLMHaGKVLASGTPQEL 494
Cdd:TIGR03771 156 FIELA-GAGTAILMTTHDLAQAmATCDRVVLLN-GRVIADGTPQQL 199
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
277-536 |
9.26e-24 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 104.92 E-value: 9.26e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 277 IEAKDLTMRFGKFVAVDHVNFRIPRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGQAWLFGQPVDPNDIDT-RRRVGYMS 355
Cdd:PRK09536 4 IDVSDLSVEFGDTTVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGDDVEALSARAaSRRVASVP 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 356 QAFSLYNELTVRQNLEL----HARLFHIPPAEIPARVAQMIERFMLTEVEDTLPASLPLGIRQRLSLAVAVIHRPEMLIL 431
Cdd:PRK09536 84 QDTSLSFEFDVRQVVEMgrtpHRSRFDTWTETDRAAVERAMERTGVAQFADRPVTSLSGGERQRVLLARALAQATPVLLL 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 432 DEPTSGVDPVARDMFWQLMVDLSRQDKvTIFISTHFMNEAER-CDRMSLMHAGKVLASGTPQELVQqrgAANLEAAFISW 510
Cdd:PRK09536 164 DEPTASLDINHQVRTLELVRRLVDDGK-TAVAAIHDLDLAARyCDELVLLADGRVRAAGPPADVLT---ADTLRAAFDAR 239
|
250 260 270
....*....|....*....|....*....|
gi 446125071 511 L----QEAAGAAPETPIPPSQTPAASGKPS 536
Cdd:PRK09536 240 TavgtDPATGAPTVTPLPDPDRTEAAADTR 269
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
22-230 |
1.05e-23 |
|
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC transporter subfamily is involved in extracellular polysaccharide export. Among the variety of membrane-linked or extracellular polysaccharides excreted by bacteria, only capsular polysaccharides, lipopolysaccharides, and teichoic acids have been shown to be exported by ABC transporters. A typical system is made of a conserved integral membrane and an ABC. In addition to these proteins, capsular polysaccharide exporter systems require two 'accessory' proteins to perform their function: a periplasmic (E.coli) or a lipid-anchored outer membrane protein called OMA (Neisseria meningitidis and Haemophilus influenza) and a cytoplasmic membrane protein MPA2.
Pssm-ID: 213187 [Multi-domain] Cd Length: 224 Bit Score: 100.30 E-value: 1.05e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 22 YGKTVALNNITLDIPARSMVGLIGPDGVGKSSLLSLISGARVIEQGNVIVLGgdmrdakhrrdvcpRIAWMPqGLGKNLY 101
Cdd:cd03220 32 VGEFWALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVTVRG--------------RVSSLL-GLGGGFN 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 102 HTLSVYENVDFFARLFGHDKAEREARITELLNSTGLAPFRDRPAGKLSGGMKQKLGLCCALIHDPELLILDEPTTGVDPL 181
Cdd:cd03220 97 PELTGRENIYLNGRLLGLSRKEIDEKIDEIIEFSELGDFIDLPVKTYSSGMKARLAFAIATALEPDILLIDEVLAVGDAA 176
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 446125071 182 SRAQFWDLIDSIRQRqtNMSVLVATAYMEEAERF-DWLVAMNAGEILATG 230
Cdd:cd03220 177 FQEKCQRRLRELLKQ--GKTVILVSHDPSSIKRLcDRALVLEKGKIRFDG 224
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
11-485 |
1.09e-23 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 105.86 E-value: 1.09e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 11 PVAQLEGVSQHYGKTVALNNITLDI-PARSMvGLIGPDGVGKSSLLSLISGARVIEQGNVIVLGGDMRDAKHRRDVCPRI 89
Cdd:PRK10762 3 ALLQLKGIDKAFPGVKALSGAALNVyPGRVM-ALVGENGAGKSTMMKVLTGIYTRDAGSILYLGKEVTFNGPKSSQEAGI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 90 AWMPQGLgkNLYHTLSVYENVdFFARLFGH-------DKAEREAriTELLNSTGLAPFRDRPAGKLSGGMKQKLGLCCAL 162
Cdd:PRK10762 82 GIIHQEL--NLIPQLTIAENI-FLGREFVNrfgridwKKMYAEA--DKLLARLNLRFSSDKLVGELSIGEQQMVEIAKVL 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 163 IHDPELLILDEPTtgvDPLSRAQFWDLIDSIRQ-RQTNMSVLVATAYMEEA-ERFDWLVAMNAGEILATgsaqqlraKTH 240
Cdd:PRK10762 157 SFESKVIIMDEPT---DALTDTETESLFRVIRElKSQGRGIVYISHRLKEIfEICDDVTVFRDGQFIAE--------REV 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 241 SATLEQAFIALLP----EAQrqahkpvvIPPYHAEQEEIAIEAKDLTmrfGKfvAVDHVNFRIPRGEIFGFLGSNGCGKS 316
Cdd:PRK10762 226 ADLTEDSLIEMMVgrklEDQ--------YPRLDKAPGEVRLKVDNLS---GP--GVNDVSFTLRKGEILGVSGLMGAGRT 292
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 317 TTMKMLTGLLPASEGQAWLFGQPVDP--------NDI----DTRRRVGymsqafsLYNELTVRQNLELHA------RLFH 378
Cdd:PRK10762 293 ELMKVLYGALPRTSGYVTLDGHEVVTrspqdglaNGIvyisEDRKRDG-------LVLGMSVKENMSLTAlryfsrAGGS 365
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 379 IPPAEIPARVAQMIERFML-TEVEDTLPASLPLGIRQRLSLAVAVIHRPEMLILDEPTSGVDPVARDMFWQLmVDLSRQD 457
Cdd:PRK10762 366 LKHADEQQAVSDFIRLFNIkTPSMEQAIGLLSGGNQQKVAIARGLMTRPKVLILDEPTRGVDVGAKKEIYQL-INQFKAE 444
|
490 500
....*....|....*....|....*....
gi 446125071 458 KVTIFISTHFMNEA-ERCDRMSLMHAGKV 485
Cdd:PRK10762 445 GLSIILVSSEMPEVlGMSDRILVMHEGRI 473
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
277-494 |
1.46e-23 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 105.64 E-value: 1.46e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 277 IEAKDLTMRFGKFVAVDHVNFRIPRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGQAWLFGQPVDPND--IDTRRRVGYM 354
Cdd:PRK09700 6 ISMAGIGKSFGPVHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNINYNKLDhkLAAQLGIGII 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 355 SQAFSLYNELTVRQNL----ELHARLFHIPP---AEIPARVAQMIERFMLTEVEDTLPASLPLGIRQRLSLAVAVIHRPE 427
Cdd:PRK09700 86 YQELSVIDELTVLENLyigrHLTKKVCGVNIidwREMRVRAAMMLLRVGLKVDLDEKVANLSISHKQMLEIAKTLMLDAK 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446125071 428 MLILDEPTSGVDPVARDMFWQLMVDLSRQDKVTIFIStHFMNEAER-CDRMSLMHAGKVLASGTPQEL 494
Cdd:PRK09700 166 VIIMDEPTSSLTNKEVDYLFLIMNQLRKEGTAIVYIS-HKLAEIRRiCDRYTVMKDGSSVCSGMVSDV 232
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
33-230 |
1.88e-23 |
|
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: 99.49 E-value: 1.88e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 33 LDIPARSMVGLIGPDGVGKSSLLSLISGARVIEQGNVIVLGGDMRDAkhrrDVCPR-IAWMPQGlgKNLYHTLSVYENVD 111
Cdd:cd03298 19 LTFAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLINGVDVTAA----PPADRpVSMLFQE--NNLFAHLTVEQNVG 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 112 FFARLFGHDKAEREARITELLNSTGLAPFRDRPAGKLSGGMKQKLGLCCALIHDPELLILDEPTTGVDPLSRAQFWDLID 191
Cdd:cd03298 93 LGLSPGLKLTAEDRQAIEVALARVGLAGLEKRLPGELSGGERQRVALARVLVRDKPVLLLDEPFAALDPALRAEMLDLVL 172
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 446125071 192 SIRqRQTNMSVLVATAYMEEAER-FDWLVAMNAGEILATG 230
Cdd:cd03298 173 DLH-AETKMTVLMVTHQPEDAKRlAQRVVFLDNGRIAAQG 211
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
11-195 |
2.02e-23 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 99.95 E-value: 2.02e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 11 PVAQLEGVSQHYGKTVALNNITLDIPARSMVGLIGPDGVGKSSLLSLISGARVIEQGNVIVLGGDMRDAKHRRDVCPRIA 90
Cdd:PRK11614 4 VMLSFDKVSAHYGKIQALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDGKDITDWQTAKIMREAVA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 91 WMPQglGKNLYHTLSVYENV---DFFARlfGHDKAEREARITELLNStgLAPFRDRPAGKLSGGMKQKLGLCCALIHDPE 167
Cdd:PRK11614 84 IVPE--GRRVFSRMTVEENLamgGFFAE--RDQFQERIKWVYELFPR--LHERRIQRAGTMSGGEQQMLAIGRALMSQPR 157
|
170 180
....*....|....*....|....*...
gi 446125071 168 LLILDEPTTGVDPLSRAQFWDLIDSIRQ 195
Cdd:PRK11614 158 LLLLDEPSLGLAPIIIQQIFDTIEQLRE 185
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
31-237 |
2.09e-23 |
|
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding cassette (ABC) protein of the three subunit molybdate ABC transporter. The three proteins of this complex are homologous to proteins of the sulfate ABC transporter. Molybdenum may be used in nitrogenases of nitrogen-fixing bacteria and in molybdopterin cofactors. In some cases, molybdate may be transported by a sulfate transporter rather than by a specific molybdate transporter. [Transport and binding proteins, Anions]
Pssm-ID: 131197 [Multi-domain] Cd Length: 354 Bit Score: 102.88 E-value: 2.09e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 31 ITLDIPARSMVGLIGPDGVGKSSLLSLISGARVIEQGNVIVLGGDMRDAKHRRDVCP---RIAWMPQGlgKNLYHTLSVY 107
Cdd:TIGR02142 16 ADFTLPGQGVTAIFGRSGSGKTTLIRLIAGLTRPDEGEIVLNGRTLFDSRKGIFLPPekrRIGYVFQE--ARLFPHLSVR 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 108 ENVDF-FARLFGHDKAEREARITELLnstGLAPFRDRPAGKLSGGMKQKLGLCCALIHDPELLILDEPTTGVDPLSRAQF 186
Cdd:TIGR02142 94 GNLRYgMKRARPSERRISFERVIELL---GIGHLLGRLPGRLSGGEKQRVAIGRALLSSPRLLLMDEPLAALDDPRKYEI 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 446125071 187 WDLIDSIRQrQTNMSVLVATAYMEEAERF-DWLVAMNAGEILATGSAQQLRA 237
Cdd:TIGR02142 171 LPYLERLHA-EFGIPILYVSHSLQEVLRLaDRVVVLEDGRVAAAGPIAEVWA 221
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
8-221 |
2.24e-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: 2.24e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 8 PVPPVAQLEGVSQHY-GKTVALNNITLDIPARSMVGLIGPDGVGKSSLLSLISGARVIEQGNVIVLGGDMR--DAKHRRD 84
Cdd:TIGR02857 317 APASSLEFSGVSVAYpGRRPALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSIAVNGVPLAdaDADSWRD 396
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 85 vcpRIAWMPQGLGknLYHTlSVYENVDFfARLFGHDKAEREAritelLNSTGLAPF-RDRPAG----------KLSGGMK 153
Cdd:TIGR02857 397 ---QIAWVPQHPF--LFAG-TIAENIRL-ARPDASDAEIREA-----LERAGLDEFvAALPQGldtpigeggaGLSGGQA 464
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446125071 154 QKLGLCCALIHDPELLILDEPTTGVDPLSRAQfwdLIDSIRQRQTNMSVLVATAYMEEAERFDWLVAM 221
Cdd:TIGR02857 465 QRLALARAFLRDAPLLLLDEPTAHLDAETEAE---VLEALRALAQGRTVLLVTHRLALAALADRIVVL 529
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
25-231 |
2.88e-23 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 100.55 E-value: 2.88e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 25 TVALNNITLDIPARSMVGLIGPDGVGKSSLLSLISGARVIEQGNVIVLGGDMRDAKHRRDVCPRIAWMPQGLGKNLYHTL 104
Cdd:PRK13633 23 KLALDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVYVDGLDTSDEENLWDIRNKAGMVFQNPDNQIVATI 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 105 sVYENVDFFARLFGHDKAEREARITELLNSTGLAPFRDRPAGKLSGGMKQKLGLCCALIHDPELLILDEPTTGVDPLSRA 184
Cdd:PRK13633 103 -VEEDVAFGPENLGIPPEEIRERVDESLKKVGMYEYRRHAPHLLSGGQKQRVAIAGILAMRPECIIFDEPTAMLDPSGRR 181
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 446125071 185 QFWDLIDSIrQRQTNMSVLVATAYMEEAERFDWLVAMNAGEILATGS 231
Cdd:PRK13633 182 EVVNTIKEL-NKKYGITIILITHYMEEAVEADRIIVMDSGKVVMEGT 227
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
291-519 |
2.97e-23 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 100.25 E-value: 2.97e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 291 AVDHVNFRI-------------PRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGQAWLFGQPVDP-NDIDTRRRVGYMSQ 356
Cdd:PRK10575 13 ALRNVSFRVpgrtllhplsltfPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPLESwSSKAFARKVAYLPQ 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 357 AFSLYNELTVRQNLEL-----HARLFHIpPAEIPARVAQMIERFMLTEVEDTLPASLPLGIRQRLSLAVAVIHRPEMLIL 431
Cdd:PRK10575 93 QLPAAEGMTVRELVAIgrypwHGALGRF-GAADREKVEEAISLVGLKPLAHRLVDSLSGGERQRAWIAMLVAQDSRCLLL 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 432 DEPTSGVDPVARDMFWQLMVDLSRQDKVTIFISTHFMNEAER-CDRMSLMHAGKVLASGTPQELVQqrgAANLEAAF--- 507
Cdd:PRK10575 172 DEPTSALDIAHQVDVLALVHRLSQERGLTVIAVLHDINMAARyCDYLVALRGGEMIAQGTPAELMR---GETLEQIYgip 248
|
250
....*....|..
gi 446125071 508 ISWLQEAAGAAP 519
Cdd:PRK10575 249 MGILPHPAGAAP 260
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
276-471 |
3.30e-23 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 99.94 E-value: 3.30e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 276 AIEAKDLTMRFGKFV----AVDHVNFRIPRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGQAWLFGQPVDPNDIDtrRRV 351
Cdd:COG4525 3 MLTVRHVSVRYPGGGqpqpALQDVSLTIESGEFVVALGASGCGKTTLLNLIAGFLAPSSGEITLDGVPVTGPGAD--RGV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 352 GYmsQAFSLYNELTVRQNLELHARLFHIPPAEIPARVAQMIERFMLTEVEDTLPASLPLGIRQRLSLAVAVIHRPEMLIL 431
Cdd:COG4525 81 VF--QKDALLPWLNVLDNVAFGLRLRGVPKAERRARAEELLALVGLADFARRRIWQLSGGMRQRVGIARALAADPRFLLM 158
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 446125071 432 DEPTSGVDPVARDMFWQLMVDLSRQDKVTIFISTHFMNEA 471
Cdd:COG4525 159 DEPFGALDALTREQMQELLLDVWQRTGKGVFLITHSVEEA 198
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
273-489 |
3.32e-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: 98.01 E-value: 3.32e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 273 EEIAIEAKDLTMRFGKFVaVDHVNFRIPRGEIFGFLGSNGCGKSTTMKMLTGLL--PASEGQAWLFGQPVDPNDIdtRRR 350
Cdd:cd03213 7 RNLTVTVKSSPSKSGKQL-LKNVSGKAKPGELTAIMGPSGAGKSTLLNALAGRRtgLGVSGEVLINGRPLDKRSF--RKI 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 351 VGYMSQAFSLYNELTVRQNLELHARLfhippaeiparvaqmierfmltevedtlpASLPLGIRQRLSLAVAVIHRPEMLI 430
Cdd:cd03213 84 IGYVPQDDILHPTLTVRETLMFAAKL-----------------------------RGLSGGERKRVSIALELVSNPSLLF 134
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446125071 431 LDEPTSGVDPVardMFWQLMVDLSR--QDKVTIFISTH------FmneaERCDRMSLMHAGKVLASG 489
Cdd:cd03213 135 LDEPTSGLDSS---SALQVMSLLRRlaDTGRTIICSIHqpsseiF----ELFDKLLLLSQGRVIYFG 194
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
285-476 |
3.52e-23 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 98.07 E-value: 3.52e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 285 RFGKFVAVDHVNFRIPRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGQAwlfgqpvdpnDIDTRRRVGYMSQAFSLYNEL 364
Cdd:NF040873 1 GYGGRPVLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTV----------RRAGGARVAYVPQRSEVPDSL 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 365 --TVRQNLEL----HARLFHIPPAEIPARVAQMIERFMLTEVEDTLPASLPLGIRQRLSLAVAVIHRPEMLILDEPTSGV 438
Cdd:NF040873 71 plTVRDLVAMgrwaRRGLWRRLTRDDRAAVDDALERVGLADLAGRQLGELSGGQRQRALLAQGLAQEADLLLLDEPTTGL 150
|
170 180 190
....*....|....*....|....*....|....*...
gi 446125071 439 DPVARDMFWQLMVDLSRqDKVTIFISTHFMNEAERCDR 476
Cdd:NF040873 151 DAESRERIIALLAEEHA-RGATVVVVTHDLELVRRADP 187
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
14-235 |
4.13e-23 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 102.08 E-value: 4.13e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 14 QLEGVSQHYGKTVALNNITLDIPARSMVGLIGPDGVGKSSLLSLISGARVIEQGNVIVLGGDMRDAkHRRDvcPRIAWMP 93
Cdd:PRK10851 4 EIANIKKSFGRTQVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFHGTDVSRL-HARD--RKVGFVF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 94 QGLGknLYHTLSVYENVDFFARLFGH----DKAEREARITELLNSTGLAPFRDRPAGKLSGGMKQKLGLCCALIHDPELL 169
Cdd:PRK10851 81 QHYA--LFRHMTVFDNIAFGLTVLPRrerpNAAAIKAKVTQLLEMVQLAHLADRYPAQLSGGQKQRVALARALAVEPQIL 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446125071 170 ILDEPTTGVDPLSRAQF--WdlidsIRQRQTNM---SVLVaTAYMEEA-ERFDWLVAMNAGEILATGSAQQL 235
Cdd:PRK10851 159 LLDEPFGALDAQVRKELrrW-----LRQLHEELkftSVFV-THDQEEAmEVADRVVVMSQGNIEQAGTPDQV 224
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
276-509 |
4.28e-23 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 100.20 E-value: 4.28e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 276 AIEAKDLTMRFGKFV-AVDHVNFRIPRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGQAWLFGQPVDP-NDIDTRRRVGY 353
Cdd:PRK13647 4 IIEVEDLHFRYKDGTkALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGREVNAeNEKWVRSKVGL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 354 M-----SQAFSLynelTVRQNLELHARLFHIPPAEIPARVAQMIERFMLTEVEDTLPASLPLGIRQRLSLAVAVIHRPEM 428
Cdd:PRK13647 84 VfqdpdDQVFSS----TVWDDVAFGPVNMGLDKDEVERRVEEALKAVRMWDFRDKPPYHLSYGQKKRVAIAGVLAMDPDV 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 429 LILDEPTSGVDPVARDMFWQLMVDLSRQDKvTIFISTHFMN-EAERCDRMSLMHAGKVLASGTPQELVQQR--GAANLEA 505
Cdd:PRK13647 160 IVLDEPMAYLDPRGQETLMEILDRLHNQGK-TVIVATHDVDlAAEWADQVIVLKEGRVLAEGDKSLLTDEDivEQAGLRL 238
|
....
gi 446125071 506 AFIS 509
Cdd:PRK13647 239 PLVA 242
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
28-230 |
4.36e-23 |
|
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely related to ModC. ModC is an ABC-type transporter and the ATPase component of a molybdate transport system that also includes the periplasmic binding protein ModA and the membrane protein ModB. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213266 [Multi-domain] Cd Length: 235 Bit Score: 98.95 E-value: 4.36e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 28 LNNITLDIPARSMVGLIGPDGVGKSSLLSLISGARVIEQGNVIVLGGDMRDAK-HRRDvcprIAWMPQGlgKNLYHTLSV 106
Cdd:cd03299 15 LKNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNGKDITNLPpEKRD----ISYVPQN--YALFPHMTV 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 107 YENVDFFARLFGHDKAEREARITELLNSTGLAPFRDRPAGKLSGGMKQKLGLCCALIHDPELLILDEPTTGVDPLSRAQF 186
Cdd:cd03299 89 YKNIAYGLKKRKVDKKEIERKVLEIAEMLGIDHLLNRKPETLSGGEQQRVAIARALVVNPKILLLDEPFSALDVRTKEKL 168
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 446125071 187 WDLIDSIRqRQTNMSVLVATAYMEEAERF-DWLVAMNAGEILATG 230
Cdd:cd03299 169 REELKKIR-KEFGVTVLHVTHDFEEAWALaDKVAIMLNGKLIQVG 212
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
292-483 |
6.12e-23 |
|
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: 98.31 E-value: 6.12e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 292 VDHVNFRIPRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGQAWLFGQPVDPNDIDtrRRVGYmsQAFSLYNELTVRQNLE 371
Cdd:TIGR01184 1 LKGVNLTIQQGEFISLIGHSGCGKSTLLNLISGLAQPTSGGVILEGKQITEPGPD--RMVVF--QNYSLLPWLTVRENIA 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 372 L--HARLFHIPPAEIPARVAQMIERFMLTEVEDTLPASLPLGIRQRLSLAVAVIHRPEMLILDEPTSGVDPVARDMFWQL 449
Cdd:TIGR01184 77 LavDRVLPDLSKSERRAIVEEHIALVGLTEAADKRPGQLSGGMKQRVAIARALSIRPKVLLLDEPFGALDALTRGNLQEE 156
|
170 180 190
....*....|....*....|....*....|....*
gi 446125071 450 MVDLSRQDKVTIFISTHFMNEAE-RCDRMSLMHAG 483
Cdd:TIGR01184 157 LMQIWEEHRVTVLMVTHDVDEALlLSDRVVMLTNG 191
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
275-494 |
7.85e-23 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 100.93 E-value: 7.85e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 275 IAIEAKDLTMRFGKFVAVDHVNFRIPRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGQAWLFGQpvDPNDIDTR-RRVGY 353
Cdd:PRK10851 1 MSIEIANIKKSFGRTQVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFHGT--DVSRLHARdRKVGF 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 354 MSQAFSLYNELTVRQNLELHARLF--HIPP--AEIPARVAQMIERFMLTEVEDTLPASLPLGIRQRLSLAVAVIHRPEML 429
Cdd:PRK10851 79 VFQHYALFRHMTVFDNIAFGLTVLprRERPnaAAIKAKVTQLLEMVQLAHLADRYPAQLSGGQKQRVALARALAVEPQIL 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446125071 430 ILDEPTSGVDPVARDMFWQLMVDLSRQDKVTIFISTHFMNEA-ERCDRMSLMHAGKVLASGTPQEL 494
Cdd:PRK10851 159 LLDEPFGALDAQVRKELRRWLRQLHEELKFTSVFVTHDQEEAmEVADRVVVMSQGNIEQAGTPDQV 224
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
12-214 |
1.06e-22 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 98.70 E-value: 1.06e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 12 VAQLEGVSQHYGKTVALNNITLDIPARSMVGLIGPDGVGKSSLL-------SLISGARVieQGNVIVLGGDMRDAkhrrD 84
Cdd:PRK14243 10 VLRTENLNVYYGSFLAVKNVWLDIPKNQITAFIGPSGCGKSTILrcfnrlnDLIPGFRV--EGKVTFHGKNLYAP----D 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 85 VCP-----RIAWM---PQGLGKnlyhtlSVYENVDFFARLFGH--------DKAEREA----RITELLNSTGLApfrdrp 144
Cdd:PRK14243 84 VDPvevrrRIGMVfqkPNPFPK------SIYDNIAYGARINGYkgdmdelvERSLRQAalwdEVKDKLKQSGLS------ 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 145 agkLSGGMKQKLGLCCALIHDPELLILDEPTTGVDPLSRAQFWDLIDSIRQRQTnmsVLVATAYMEEAER 214
Cdd:PRK14243 152 ---LSGGQQQRLCIARAIAVQPEVILMDEPCSALDPISTLRIEELMHELKEQYT---IIIVTHNMQQAAR 215
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
277-495 |
1.17e-22 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 98.52 E-value: 1.17e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 277 IEAKDLTMRFGKFVAVDHVNFRIPRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGQAWLFGQPVDP-NDIDTRRRVGYMS 355
Cdd:PRK10253 8 LRGEQLTLGYGKYTVAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIQHyASKEVARRIGLLA 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 356 QAFSLYNELTVrQNLELHARLFHIP-----PAEIPARVAQMIERFMLTEVEDTLPASLPLGIRQRLSLAVAVIHRPEMLI 430
Cdd:PRK10253 88 QNATTPGDITV-QELVARGRYPHQPlftrwRKEDEEAVTKAMQATGITHLADQSVDTLSGGQRQRAWIAMVLAQETAIML 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446125071 431 LDEPTSGVDPVARDMFWQLMVDLSRQDKVTIFISTHFMNEAER-CDRMSLMHAGKVLASGTPQELV 495
Cdd:PRK10253 167 LDEPTTWLDISHQIDLLELLSELNREKGYTLAAVLHDLNQACRyASHLIALREGKIVAQGAPKEIV 232
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
14-235 |
1.22e-22 |
|
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: 99.74 E-value: 1.22e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 14 QLEGVSQHY----GKTVALNNITLDIPARSMVGLIGPDGVGKSSLLSLISG---ARVIEQGNVIVLGGDMRDA--KHRRD 84
Cdd:COG0444 3 EVRNLKVYFptrrGVVKAVDGVSFDVRRGETLGLVGESGSGKSTLARAILGllpPPGITSGEILFDGEDLLKLseKELRK 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 85 VCPR-IAWMPQGLGKNLYHTLSVYENVDFFARLFGH-DKAEREARITELLNSTGLAPFRDRpAGK----LSGGMKQKLGL 158
Cdd:COG0444 83 IRGReIQMIFQDPMTSLNPVMTVGDQIAEPLRIHGGlSKAEARERAIELLERVGLPDPERR-LDRypheLSGGMRQRVMI 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 159 CCALIHDPELLILDEPTTGVDPLSRAQFWDLIDSIrQRQTNMSVLVAT------AYMeeAERfdwlVA-MNAGEILATGS 231
Cdd:COG0444 162 ARALALEPKLLIADEPTTALDVTIQAQILNLLKDL-QRELGLAILFIThdlgvvAEI--ADR----VAvMYAGRIVEEGP 234
|
....
gi 446125071 232 AQQL 235
Cdd:COG0444 235 VEEL 238
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
282-501 |
1.36e-22 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 97.35 E-value: 1.36e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 282 LTMRFgkfvavdhvNFRIPRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGQAWLFGQpvdpNDIDT---RRRVGYMSQAF 358
Cdd:PRK10771 14 LPMRF---------DLTVERGERVAILGPSGAGKSTLLNLIAGFLTPASGSLTLNGQ----DHTTTppsRRPVSMLFQEN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 359 SLYNELTVRQN--LELHA--RLFHippaEIPARVAQMIERFMLTEVEDTLPASLPLGIRQRLSLAVAVIHRPEMLILDEP 434
Cdd:PRK10771 81 NLFSHLTVAQNigLGLNPglKLNA----AQREKLHAIARQMGIEDLLARLPGQLSGGQRQRVALARCLVREQPILLLDEP 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446125071 435 TSGVDPVARDMFWQLMVDLSRQDKVTIFISTHFMNEAERCDRMSLMHA-GKVLASGTPQELVQQRGAA 501
Cdd:PRK10771 157 FSALDPALRQEMLTLVSQVCQERQLTLLMVSHSLEDAARIAPRSLVVAdGRIAWDGPTDELLSGKASA 224
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
30-235 |
1.57e-22 |
|
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and metabolism]; ABC-type molybdate transport system, ATPase component ModC is part of the Pathway/BioSystem: Molybdopterin biosynthesis
Pssm-ID: 443319 [Multi-domain] Cd Length: 358 Bit Score: 100.18 E-value: 1.57e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 30 NITLDIPARSMVGLIGPDGVGKSSLLSLISGARVIEQGNVIVLGGDMRDAKHRRDVCP---RIAWMPQGlgKNLYHTLSV 106
Cdd:COG4148 17 DVDFTLPGRGVTALFGPSGSGKTTLLRAIAGLERPDSGRIRLGGEVLQDSARGIFLPPhrrRIGYVFQE--ARLFPHLSV 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 107 YENVDF-FARLFGHDKAEREARITELLnstGLAPFRDRPAGKLSGGMKQKLGLCCALIHDPELLILDEPTTGVDPLSRAQ 185
Cdd:COG4148 95 RGNLLYgRKRAPRAERRISFDEVVELL---GIGHLLDRRPATLSGGERQRVAIGRALLSSPRLLLMDEPLAALDLARKAE 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 446125071 186 FWDLIDSIRqRQTNMSVLVATAYMEEAERF-DWLVAMNAGEILATGSAQQL 235
Cdd:COG4148 172 ILPYLERLR-DELDIPILYVSHSLDEVARLaDHVVLLEQGRVVASGPLAEV 221
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
118-443 |
1.68e-22 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 102.02 E-value: 1.68e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 118 GHDKAEREARITELLnstGLAPFRDRPAGKLSGGMKQKLGLCCALIHDPELLILDEPTTGVDPLSRAQFWDLIDSIRQRQ 197
Cdd:PRK10938 109 EVKDPARCEQLAQQF---GITALLDRRFKYLSTGETRKTLLCQALMSEPDLLILDEPFDGLDVASRQQLAELLASLHQSG 185
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 198 TNMsVLVATaymeeaeRFDWL--VAMNAGeILA------TGSAQQLRAKTHSATL---EQAFIALLPEAQRQAHKPvVIP 266
Cdd:PRK10938 186 ITL-VLVLN-------RFDEIpdFVQFAG-VLAdctlaeTGEREEILQQALVAQLahsEQLEGVQLPEPDEPSARH-ALP 255
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 267 PyhaeqEEIAIEAKDLTMRFGKFVAVDHVNFRIPRGEIFGFLGSNGCGKSTTMKMLTGLLPasegQAW-----LFGQPVD 341
Cdd:PRK10938 256 A-----NEPRIVLNNGVVSYNDRPILHNLSWQVNPGEHWQIVGPNGAGKSTLLSLITGDHP----QGYsndltLFGRRRG 326
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 342 PNDI--DTRRRVGYMSQAFSL-YNELTVRQNLELHA-----RLFHIPPAEIPARVAQMIERF-MLTEVEDTLPASLPLGi 412
Cdd:PRK10938 327 SGETiwDIKKHIGYVSSSLHLdYRVSTSVRNVILSGffdsiGIYQAVSDRQQKLAQQWLDILgIDKRTADAPFHSLSWG- 405
|
330 340 350
....*....|....*....|....*....|..
gi 446125071 413 RQRLSLAV-AVIHRPEMLILDEPTSGVDPVAR 443
Cdd:PRK10938 406 QQRLALIVrALVKHPTLLILDEPLQGLDPLNR 437
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
25-273 |
1.77e-22 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 98.27 E-value: 1.77e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 25 TVALNNITLDIPARSMVGLIGPDGVGKSSLLSLISGARVIEQGNVIVLGGDMrDAKHRRDVCPRIAWMPQGLGKNLYhTL 104
Cdd:PRK13647 18 TKALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGREV-NAENEKWVRSKVGLVFQDPDDQVF-SS 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 105 SVYENVDFFARLFGHDKAEREARITELLNSTGLAPFRDRPAGKLSGGMKQKLGLCCALIHDPELLILDEPTTGVDPLSRA 184
Cdd:PRK13647 96 TVWDDVAFGPVNMGLDKDEVERRVEEALKAVRMWDFRDKPPYHLSYGQKKRVAIAGVLAMDPDVIVLDEPMAYLDPRGQE 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 185 QFWDLIDSIRQRQTnmSVLVATAYME-EAERFDWLVAMNAGEILATGSAQQLrakTHSATLEQAFIALlpeaqrqahkPV 263
Cdd:PRK13647 176 TLMEILDRLHNQGK--TVIVATHDVDlAAEWADQVIVLKEGRVLAEGDKSLL---TDEDIVEQAGLRL----------PL 240
|
250
....*....|
gi 446125071 264 VIPPYHAEQE 273
Cdd:PRK13647 241 VAQIFEDLPE 250
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
270-494 |
1.82e-22 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 99.42 E-value: 1.82e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 270 AEQEEIAIEAKDLTMRF----------GKFV-AVDHVNFRIPRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGQAWLFGQ 338
Cdd:COG4608 1 AAMAEPLLEVRDLKKHFpvrgglfgrtVGVVkAVDGVSFDIRRGETLGLVGESGCGKSTLGRLLLRLEEPTSGEILFDGQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 339 PV---DPNDI-DTRRRVGYMSQ---AfSLYNELTVRQNLELHARLFHI-PPAEIPARVAQMIERFML-TEVEDTLPASLP 409
Cdd:COG4608 81 DItglSGRELrPLRRRMQMVFQdpyA-SLNPRMTVGDIIAEPLRIHGLaSKAERRERVAELLELVGLrPEHADRYPHEFS 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 410 LGIRQRLSLAVAVIHRPEMLILDEPTSgvdpvARDMFWQ-----LMVDLSRQDKVT-IFIStHFMNEAER-CDRMSLMHA 482
Cdd:COG4608 160 GGQRQRIGIARALALNPKLIVCDEPVS-----ALDVSIQaqvlnLLEDLQDELGLTyLFIS-HDLSVVRHiSDRVAVMYL 233
|
250
....*....|..
gi 446125071 483 GKVLASGTPQEL 494
Cdd:COG4608 234 GKIVEIAPRDEL 245
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
22-216 |
2.03e-22 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 95.76 E-value: 2.03e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 22 YGKTVALNNITLDIPARSMVGLIGPDGVGKSSLLSLISGARVIEQGNVIVLGGDmrdakhrrdvcpRIAWMPQGLGKNLY 101
Cdd:NF040873 2 YGGRPVLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTVRRAGGA------------RVAYVPQRSEVPDS 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 102 HTLSVYENVD--FFAR--LFGHDKAEREARITELLNSTGLAPFRDRPAGKLSGGMKQKLGLCCALIHDPELLILDEPTTG 177
Cdd:NF040873 70 LPLTVRDLVAmgRWARrgLWRRLTRDDRAAVDDALERVGLADLAGRQLGELSGGQRQRALLAQGLAQEADLLLLDEPTTG 149
|
170 180 190
....*....|....*....|....*....|....*....
gi 446125071 178 VDPLSRAQFWDLIDSIRQRQTnmSVLVATAYMEEAERFD 216
Cdd:NF040873 150 LDAESRERIIALLAEEHARGA--TVVVVTHDLELVRRAD 186
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
272-478 |
2.08e-22 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 97.93 E-value: 2.08e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 272 QEEIAIEAKDLTMRFGKFVAVDHVNFRIPRGEIFGFLGSNGCGKSTTMK---MLTGLLPA--SEGQAWLFGQPVDPNDID 346
Cdd:PRK14243 6 GTETVLRTENLNVYYGSFLAVKNVWLDIPKNQITAFIGPSGCGKSTILRcfnRLNDLIPGfrVEGKVTFHGKNLYAPDVD 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 347 ---TRRRVGYMSQAFSLYNElTVRQNLELHARLfhippAEIPARVAQMIER-----FMLTEVEDTLPAS---LPLGIRQR 415
Cdd:PRK14243 86 pveVRRRIGMVFQKPNPFPK-SIYDNIAYGARI-----NGYKGDMDELVERslrqaALWDEVKDKLKQSglsLSGGQQQR 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446125071 416 LSLAVAVIHRPEMLILDEPTSGVDPVARDMFWQLMVDLSRQdkVTIFISTHFMNEAERCDRMS 478
Cdd:PRK14243 160 LCIARAIAVQPEVILMDEPCSALDPISTLRIEELMHELKEQ--YTIIIVTHNMQQAARVSDMT 220
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
10-231 |
2.94e-22 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 99.64 E-value: 2.94e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 10 PPVAQLEGVSQHYGKTVALNNITLDIPARSMVGLIGPDGVGKSSLLSLISGARVIEQGNVIVLGGDMRD--AKHR--RDV 85
Cdd:PRK09452 12 SPLVELRGISKSFDGKEVISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLDGQDITHvpAENRhvNTV 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 86 CPRIAWMPqglgknlyHtLSVYENVDFFARLFGHDKAEREARITELLNSTGLAPFRDRPAGKLSGGMKQKLGLCCALIHD 165
Cdd:PRK09452 92 FQSYALFP--------H-MTVFENVAFGLRMQKTPAAEITPRVMEALRMVQLEEFAQRKPHQLSGGQQQRVAIARAVVNK 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446125071 166 PELLILDEPTTGVDPLSRAQFWDLIDSIrQRQTNMSVLVATAYMEEAERF-DWLVAMNAGEILATGS 231
Cdd:PRK09452 163 PKVLLLDESLSALDYKLRKQMQNELKAL-QRKLGITFVFVTHDQEEALTMsDRIVVMRDGRIEQDGT 228
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
14-230 |
3.31e-22 |
|
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic bacteriocins of lactic acid bacteria are produced as precursors which have N-terminal leader peptides that share similarities in amino acid sequence and contain a conserved processing site of two glycine residues in positions -1 and -2. A dedicated ATP-binding cassette (ABC) transporter is responsible for the proteolytic cleavage of the leader peptides and subsequent translocation of the bacteriocins across the cytoplasmic membrane.
Pssm-ID: 213212 [Multi-domain] Cd Length: 220 Bit Score: 96.12 E-value: 3.31e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 14 QLEGVSQHY--GKTVALNNITLDIPARSMVGLIGPDGVGKSSLLSLISGARVIEQGNVIVLGGDMRDAkHRRDVCPRIAW 91
Cdd:cd03245 4 EFRNVSFSYpnQEIPALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGTDIRQL-DPADLRRNIGY 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 92 MPQGLgknlyhTL---SVYENVDFFARLfgHDkaerEARITELLNSTGLAPF-RDRPAG----------KLSGGMKQKLG 157
Cdd:cd03245 83 VPQDV------TLfygTLRDNITLGAPL--AD----DERILRAAELAGVTDFvNKHPNGldlqigergrGLSGGQRQAVA 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446125071 158 LCCALIHDPELLILDEPTTGVDPLSRAQFwdlIDSIRQRQTNMSVLVATAYMEEAERFDWLVAMNAGEILATG 230
Cdd:cd03245 151 LARALLNDPPILLLDEPTSAMDMNSEERL---KERLRQLLGDKTLIIITHRPSLLDLVDRIIVMDSGRIVADG 220
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
277-500 |
3.44e-22 |
|
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; MsbA is an essential ABC transporter, closely related to eukaryotic MDR proteins. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213218 [Multi-domain] Cd Length: 234 Bit Score: 96.15 E-value: 3.44e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 277 IEAKDLTMRFGK--FVAVDHVNFRIPRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGQAWLFGqpVDPNDI---DTRRRV 351
Cdd:cd03251 1 VEFKNVTFRYPGdgPPVLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDG--HDVRDYtlaSLRRQI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 352 GYMSQAFSLYNElTVRQNLELHARlfHIPPAEI--PARVA---QMIERFML---TEVEDTlPASLPLGIRQRLSLAVAVI 423
Cdd:cd03251 79 GLVSQDVFLFND-TVAENIAYGRP--GATREEVeeAARAAnahEFIMELPEgydTVIGER-GVKLSGGQRQRIAIARALL 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446125071 424 HRPEMLILDEPTSGVDPVARDMFWQLMVDLSrQDKVTIFIStHFMNEAERCDRMSLMHAGKVLASGTPQELVQQRGA 500
Cdd:cd03251 155 KDPPILILDEATSALDTESERLVQAALERLM-KNRTTFVIA-HRLSTIENADRIVVLEDGKIVERGTHEELLAQGGV 229
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
295-497 |
4.02e-22 |
|
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular trafficking, secretion, and vesicular transport];
Pssm-ID: 443660 [Multi-domain] Cd Length: 563 Bit Score: 101.75 E-value: 4.02e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 295 VNFRIPRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGQAWLFGQPVDPNDIDTR-RRVGYMSQAFSLYnELTVRQNLelh 373
Cdd:COG4618 351 VSFSLEPGEVLGVIGPSGSGKSTLARLLVGVWPPTAGSVRLDGADLSQWDREELgRHIGYLPQDVELF-DGTIAENI--- 426
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 374 ARLFHIPPAEI--PARVA---QMIERFML---TEVEDtlpASLPL--GIRQRLSLAVAVIHRPEMLILDEPTSGVDPVAR 443
Cdd:COG4618 427 ARFGDADPEKVvaAAKLAgvhEMILRLPDgydTRIGE---GGARLsgGQRQRIGLARALYGDPRLVVLDEPNSNLDDEGE 503
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 446125071 444 DMFWQLMVDLsRQDKVTIFISTHFMNEAERCDRMSLMHAGKVLASGTPQELVQQ 497
Cdd:COG4618 504 AALAAAIRAL-KARGATVVVITHRPSLLAAVDKLLVLRDGRVQAFGPRDEVLAR 556
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
25-234 |
4.88e-22 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 97.43 E-value: 4.88e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 25 TVALNNITLDIPARSMVGLIGPDGVGKSSLLSLISGARVIEQGNVIVLGGDMRDAKHR-RDVCPRIAWMPQGLGKNLYHT 103
Cdd:PRK13637 20 KKALDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDGVDITDKKVKlSDIRKKVGLVFQYPEYQLFEE 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 104 lSVYENVDFFARLFGHDKAEREARITELLNSTGLA--PFRDRPAGKLSGGMKQKLGLCCALIHDPELLILDEPTTGVDPL 181
Cdd:PRK13637 100 -TIEKDIAFGPINLGLSEEEIENRVKRAMNIVGLDyeDYKDKSPFELSGGQKRRVAIAGVVAMEPKILILDEPTAGLDPK 178
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 446125071 182 SRAQFWDLIDSIrQRQTNMSVLVATAYMEEAERF-DWLVAMNAGEILATGSAQQ 234
Cdd:PRK13637 179 GRDEILNKIKEL-HKEYNMTIILVSHSMEDVAKLaDRIIVMNKGKCELQGTPRE 231
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
295-476 |
6.53e-22 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 95.23 E-value: 6.53e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 295 VNFRIPRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGQAWLFGQPVDPNDIDTR-----RRVGYMSQAFSLYNELTVRQN 369
Cdd:PRK10584 29 VELVVKRGETIALIGESGSGKSTLLAILAGLDDGSSGEVSLVGQPLHQMDEEARaklraKHVGFVFQSFMLIPTLNALEN 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 370 LELHARLFHIPPAEIPARVAQMIERFMLTEVEDTLPASLPLGIRQRLSLAVAVIHRPEMLILDEPTSGVDPVARDMFWQL 449
Cdd:PRK10584 109 VELPALLRGESSRQSRNGAKALLEQLGLGKRLDHLPAQLSGGEQQRVALARAFNGRPDVLFADEPTGNLDRQTGDKIADL 188
|
170 180
....*....|....*....|....*..
gi 446125071 450 MVDLSRQDKVTIFISTHFMNEAERCDR 476
Cdd:PRK10584 189 LFSLNREHGTTLILVTHDLQLAARCDR 215
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
280-493 |
8.35e-22 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 94.47 E-value: 8.35e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 280 KDLTMRFGKFVAVDHVNFRIPRGEIFGFLGSNGCGKSTTMKMLTGLLPA---SEGQAWLFGQPVDPNDIDtRRRVGYMSQ 356
Cdd:COG4136 5 ENLTITLGGRPLLAPLSLTVAPGEILTLMGPSGSGKSTLLAAIAGTLSPafsASGEVLLNGRRLTALPAE-QRRIGILFQ 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 357 AFSLYNELTVRQNLelharLFHIPP----AEIPARVAQMIERFMLTEVEDTLPASLPLGIRQRLSLAVAVIHRPEMLILD 432
Cdd:COG4136 84 DDLLFPHLSVGENL-----AFALPPtigrAQRRARVEQALEEAGLAGFADRDPATLSGGQRARVALLRALLAEPRALLLD 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446125071 433 EPTSGVDPVARDMFWQLMVDLSRQDKVTIFISTHFMNEAERcdrmslmhAGKVLASGTPQE 493
Cdd:COG4136 159 EPFSKLDAALRAQFREFVFEQIRQRGIPALLVTHDEEDAPA--------AGRVLDLGNWQH 211
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
20-173 |
9.72e-22 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 95.15 E-value: 9.72e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 20 QHYGKTVALNNITLDIPARSMVGLIGPDGVGKSSLLSLISGarVIE--QGNVIVLGgdmrdakhrrdvcpRIAWmPQGLG 97
Cdd:COG1134 34 TRREEFWALKDVSFEVERGESVGIIGRNGAGKSTLLKLIAG--ILEptSGRVEVNG--------------RVSA-LLELG 96
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446125071 98 KNLYHTLSVYENVDFFARLFGHDKAEREARITELLNSTGLAPFRDRPAGKLSGGMKQKLGLCCALIHDPELLILDE 173
Cdd:COG1134 97 AGFHPELTGRENIYLNGRLLGLSRKEIDEKFDEIVEFAELGDFIDQPVKTYSSGMRARLAFAVATAVDPDILLVDE 172
|
|
| LolD_lipo_ex |
TIGR02211 |
lipoprotein releasing system, ATP-binding protein; This model represents LolD, a member of the ... |
277-485 |
9.75e-22 |
|
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: 94.73 E-value: 9.75e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 277 IEAKDLTMRF--GKF--VAVDHVNFRIPRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGQAWLFGQPV---DPNDIDTRR 349
Cdd:TIGR02211 2 LKCENLGKRYqeGKLdtRVLKGVSLSIGKGEIVAIVGSSGSGKSTLLHLLGGLDNPTSGEVLFNGQSLsklSSNERAKLR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 350 --RVGYMSQAFSLYNELTVRQNLELHARLFHIPPAEIPARVAQMIERFMLTEVEDTLPASLPLGIRQRLSLAVAVIHRPE 427
Cdd:TIGR02211 82 nkKLGFIYQFHHLLPDFTALENVAMPLLIGKKSVKEAKERAYEMLEKVGLEHRINHRPSELSGGERQRVAIARALVNQPS 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 446125071 428 MLILDEPTSGVDPVARDMFWQLMVDLSRQDKVTIFISTHFMNEAERCDRMSLMHAGKV 485
Cdd:TIGR02211 162 LVLADEPTGNLDNNNAKIIFDLMLELNRELNTSFLVVTHDLELAKKLDRVLEMKDGQL 219
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
10-485 |
2.21e-21 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 98.83 E-value: 2.21e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 10 PPVAQLEGVSQHYGKTVALNNITLDIPARSMVGLIGPDGVGKSSLLSLISGARVIEQGNVIVLGGDMRDAKHRRDVCPRI 89
Cdd:PRK11288 2 SPYLSFDGIGKTFPGVKALDDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSILIDGQEMRFASTTAALAAGV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 90 AWMPQGLgkNLYHTLSVYENVdFFARL---FGH-DKAEREARITELLNSTGLAPFRDRPAGKLSGGMKQKLGLCCALIHD 165
Cdd:PRK11288 82 AIIYQEL--HLVPEMTVAENL-YLGQLphkGGIvNRRLLNYEAREQLEHLGVDIDPDTPLKYLSIGQRQMVEIAKALARN 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 166 PELLILDEPTTGVDPLSRAQFWDLIDSIRQRQTnmSVLVATAYMEEAERF-DWLVAMNAGEILATGSAQqlrAKTHSATL 244
Cdd:PRK11288 159 ARVIAFDEPTSSLSAREIEQLFRVIRELRAEGR--VILYVSHRMEEIFALcDAITVFKDGRYVATFDDM---AQVDRDQL 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 245 EQAFIAllpeaqRQAHKpvvIPPYHA-EQEEIAIEAKDLTmrfGKFVAVDhVNFRIPRGEIFGFLGSNGCGKSTTMKMLT 323
Cdd:PRK11288 234 VQAMVG------REIGD---IYGYRPrPLGEVRLRLDGLK---GPGLREP-ISFSVRAGEIVGLFGLVGAGRSELMKLLY 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 324 GLLPASEGQAWLFGQPVDPNDIDTRRRVGYM-----SQAFSLYNELTVRQNLELHARLFHIPPAEI--PARVAQMIERFM 396
Cdd:PRK11288 301 GATRRTAGQVYLDGKPIDIRSPRDAIRAGIMlcpedRKAEGIIPVHSVADNINISARRHHLRAGCLinNRWEAENADRFI 380
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 397 L-----TEVEDTLPASLPLGIRQRLSLAVAVIHRPEMLILDEPTSGVDPVARDMFWQLMVDLSRQDKVTIFISTHFMNEA 471
Cdd:PRK11288 381 RslnikTPSREQLIMNLSGGNQQKAILGRWLSEDMKVILLDEPTRGIDVGAKHEIYNVIYELAAQGVAVLFVSSDLPEVL 460
|
490
....*....|....
gi 446125071 472 ERCDRMSLMHAGKV 485
Cdd:PRK11288 461 GVADRIVVMREGRI 474
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
11-266 |
2.36e-21 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 94.45 E-value: 2.36e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 11 PVAQLEGVSQHYGKTVALNNITLDIPARSMVGLIGPDGVGKSSLLSLISGARVIEQGNVIVLGGDMRD------AKHRrd 84
Cdd:PRK13548 1 AMLEARNLSVRLGGRTLLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLNGRPLADwspaelARRR-- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 85 vcpriAWMPQglgknlYHTLS----VYENVDFFARLFGHDKAEREARITELLNSTGLAPFRDRPAGKLSGGMKQKLGLCC 160
Cdd:PRK13548 79 -----AVLPQ------HSSLSfpftVEEVVAMGRAPHGLSRAEDDALVAAALAQVDLAHLAGRDYPQLSGGEQQRVQLAR 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 161 ALI------HDPELLILDEPTTGVDPlsrAQFWDLIDSIRQ--RQTNMSVLV-------ATAYmeeAERfdwLVAMNAGE 225
Cdd:PRK13548 148 VLAqlwepdGPPRWLLLDEPTSALDL---AHQHHVLRLARQlaHERGLAVIVvlhdlnlAARY---ADR---IVLLHQGR 218
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 446125071 226 ILATGSAQQ-LRAkthsATLEQAF-IALLPEAQRQAHKPVVIP 266
Cdd:PRK13548 219 LVADGTPAEvLTP----ETLRRVYgADVLVQPHPETGAPLVLP 257
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
287-495 |
2.92e-21 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 97.41 E-value: 2.92e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 287 GKFVAVDHVNFRIPRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGQAWLFGqpVDPNDIDT-------RRRVGYMSQAFS 359
Cdd:PRK10070 39 GLSLGVKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDG--VDIAKISDaelrevrRKKIAMVFQSFA 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 360 LYNELTVRQNLELHARLFHIPPAEIPARVAQMIERFMLTEVEDTLPASLPLGIRQRLSLAVAVIHRPEMLILDEPTSGVD 439
Cdd:PRK10070 117 LMPHMTVLDNTAFGMELAGINAEERREKALDALRQVGLENYAHSYPDELSGGMRQRVGLARALAINPDILLMDEAFSALD 196
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 446125071 440 PVARDMFWQLMVDLSRQDKVTIFISTHFMNEAERC-DRMSLMHAGKVLASGTPQELV 495
Cdd:PRK10070 197 PLIRTEMQDELVKLQAKHQRTIVFISHDLDEAMRIgDRIAIMQNGEVVQVGTPDEIL 253
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
15-238 |
3.00e-21 |
|
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; MsbA is an essential ABC transporter, closely related to eukaryotic MDR proteins. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213218 [Multi-domain] Cd Length: 234 Bit Score: 93.45 E-value: 3.00e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 15 LEGVSQHYGKTV--ALNNITLDIPARSMVGLIGPDGVGKSSLLSLISGARVIEQGNVIVLGGDMRD---AKHRRdvcpRI 89
Cdd:cd03251 3 FKNVTFRYPGDGppVLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDGHDVRDytlASLRR----QI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 90 AWMPQGLgkNLYHTlSVYENVDFFARLFGHDKAEREAR-------ITELLNstGL-APFRDRpAGKLSGGMKQKLGLCCA 161
Cdd:cd03251 79 GLVSQDV--FLFND-TVAENIAYGRPGATREEVEEAARaanahefIMELPE--GYdTVIGER-GVKLSGGQRQRIAIARA 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446125071 162 LIHDPELLILDEPTTGVDPLSRaqfwDLI-DSIRQRQTNMSVLVATAYMEEAERFDWLVAMNAGEILATGSAQQLRAK 238
Cdd:cd03251 153 LLKDPPILILDEATSALDTESE----RLVqAALERLMKNRTTFVIAHRLSTIENADRIVVLEDGKIVERGTHEELLAQ 226
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
22-234 |
3.05e-21 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 94.31 E-value: 3.05e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 22 YGKTVALNNITLDIPARSMVGLIGPDGVGKSSLLSLISGARVIEQGNVIVLGGDMRDAKHRRdVCPRIAWMPQglgknlY 101
Cdd:PRK11231 12 YGTKRILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDKPISMLSSRQ-LARRLALLPQ------H 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 102 HT----LSVYENV--------DFFARLFGHDkaerEARITELLNSTGLAPFRDRPAGKLSGGMKQKLGLCCALIHDPELL 169
Cdd:PRK11231 85 HLtpegITVRELVaygrspwlSLWGRLSAED----NARVNQAMEQTRINHLADRRLTDLSGGQRQRAFLAMVLAQDTPVV 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446125071 170 ILDEPTTGVDpLSRAQfwDLIDSIRQRQTNMSVLVATAY-MEEAERF-DWLVAMNAGEILATGSAQQ 234
Cdd:PRK11231 161 LLDEPTTYLD-INHQV--ELMRLMRELNTQGKTVVTVLHdLNQASRYcDHLVVLANGHVMAQGTPEE 224
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
276-490 |
3.23e-21 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 93.93 E-value: 3.23e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 276 AIEAKDLTMRFGKFVAVDHVNFRIPRGEIFGFLGSNGCGKSTTMKMLTGL-LPAS-----EGQAWLFGQPVDPNDI-DTR 348
Cdd:PRK11124 2 SIQLNGINCFYGAHQALFDITLDCPQGETLVLLGPSGAGKSSLLRVLNLLeMPRSgtlniAGNHFDFSKTPSDKAIrELR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 349 RRVGYMSQAFSLYNELTVRQNL-ELHARLFHIPPAEIPARVAQMIERFMLTEVEDTLPASLPLGIRQRLSLAVAVIHRPE 427
Cdd:PRK11124 82 RNVGMVFQQYNLWPHLTVQQNLiEAPCRVLGLSKDQALARAEKLLERLRLKPYADRFPLHLSGGQQQRVAIARALMMEPQ 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446125071 428 MLILDEPTSGVDPVARDMFWQLMVDLSrQDKVTIFISTHFMNEAER-CDRMSLMHAGKVLASGT 490
Cdd:PRK11124 162 VLLFDEPTAALDPEITAQIVSIIRELA-ETGITQVIVTHEVEVARKtASRVVYMENGHIVEQGD 224
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
294-489 |
3.77e-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: 92.56 E-value: 3.77e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 294 HVNFRIPRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGQAWLFGQPVDPNDIdTRRRVGYMSQAFSLYNELTVRQN--LE 371
Cdd:cd03298 16 HFDLTFAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLINGVDVTAAPP-ADRPVSMLFQENNLFAHLTVEQNvgLG 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 372 LHARLfHIPPaEIPARVAQMIERFMLTEVEDTLPASLPLGIRQRLSLAVAVIHRPEMLILDEPTSGVDPVARDMFWQLMV 451
Cdd:cd03298 95 LSPGL-KLTA-EDRQAIEVALARVGLAGLEKRLPGELSGGERQRVALARVLVRDKPVLLLDEPFAALDPALRAEMLDLVL 172
|
170 180 190
....*....|....*....|....*....|....*....
gi 446125071 452 DLSRQDKVTIFISTHFMNEAERCDRMSL-MHAGKVLASG 489
Cdd:cd03298 173 DLHAETKMTVLMVTHQPEDAKRLAQRVVfLDNGRIAAQG 211
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
274-485 |
4.44e-21 |
|
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: 91.34 E-value: 4.44e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 274 EIAIEAKDLTMRfgkfVAVDHVNFRIPRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGQAWLFGQPVDPNDIDTRRR--V 351
Cdd:cd03215 2 EPVLEVRGLSVK----GAVRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITLDGKPVTRRSPRDAIRagI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 352 GYMS---QAFSLYNELTVRQNLelharlfhippaeiparvaqmierfmltevedTLPASLPLGIRQRLSLAVAVIHRPEM 428
Cdd:cd03215 78 AYVPedrKREGLVLDLSVAENI--------------------------------ALSSLLSGGNQQKVVLARWLARDPRV 125
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 446125071 429 LILDEPTSGVDPVARDMFWQLMVDLSRQDKVTIFISTHfMNEAER-CDRMSLMHAGKV 485
Cdd:cd03215 126 LILDEPTRGVDVGAKAEIYRLIRELADAGKAVLLISSE-LDELLGlCDRILVMYEGRI 182
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
11-221 |
7.21e-21 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 93.20 E-value: 7.21e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 11 PVAqLEGVSQHYGKTVALNNITLDIPARSMVGLIGPDGVGKSSLLSLISGARVIEQGNVivLGGDMRDAKHRRDvcprIA 90
Cdd:PRK11247 12 PLL-LNAVSKRYGERTVLNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAGEL--LAGTAPLAEARED----TR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 91 WMPQGlgKNLYHTLSVYENVDFfaRLFGHDKAE-REAritelLNSTGLApfrDR----PAGkLSGGMKQKLGLCCALIHD 165
Cdd:PRK11247 85 LMFQD--ARLLPWKKVIDNVGL--GLKGQWRDAaLQA-----LAAVGLA---DRanewPAA-LSGGQKQRVALARALIHR 151
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 446125071 166 PELLILDEPTTGVDPLSRAQFWDLIDSIRQrQTNMSVLVATAYMEEAerfdwlVAM 221
Cdd:PRK11247 152 PGLLLLDEPLGALDALTRIEMQDLIESLWQ-QHGFTVLLVTHDVSEA------VAM 200
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
14-233 |
7.67e-21 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 92.77 E-value: 7.67e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 14 QLEGVSQHYGKTVALNNITLDIPARSMVGLIGPDGVGKSSLLSLISGARVIEQGNVIVlGGDMRDAKHRRDVcPRIAWMP 93
Cdd:PRK11124 4 QLNGINCFYGAHQALFDITLDCPQGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLNI-AGNHFDFSKTPSD-KAIRELR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 94 QGLGK-----NLYHTLSVYEN-VDFFARLFGHDKAEREARITELLNSTGLAPFRDRPAGKLSGGMKQKLGLCCALIHDPE 167
Cdd:PRK11124 82 RNVGMvfqqyNLWPHLTVQQNlIEAPCRVLGLSKDQALARAEKLLERLRLKPYADRFPLHLSGGQQQRVAIARALMMEPQ 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446125071 168 LLILDEPTTGVDPLSRAQFWDLIDSIrqRQTNMSVLVATAYMEEAERF-DWLVAMNAGEILATGSAQ 233
Cdd:PRK11124 162 VLLFDEPTAALDPEITAQIVSIIREL--AETGITQVIVTHEVEVARKTaSRVVYMENGHIVEQGDAS 226
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
12-439 |
9.42e-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: 97.31 E-value: 9.42e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 12 VAQLEGVSQHY-GKTVALNNITLDIPARSMVGLIGPDGVGKSSLLSLISGarvIEQGnvivLGGDMRDAKHRRdvcprIA 90
Cdd:TIGR03719 4 IYTMNRVSKVVpPKKEILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAG---VDKD----FNGEARPQPGIK-----VG 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 91 WMPQGlgKNLYHTLSVYENV--------DFFARL------FG-----HDK-AEREARITELLNSTGL------------- 137
Cdd:TIGR03719 72 YLPQE--PQLDPTKTVRENVeegvaeikDALDRFneisakYAepdadFDKlAAEQAELQEIIDAADAwdldsqleiamda 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 138 --APFRDRPAGKLSGGMKQKLGLCCALIHDPELLILDEPTTGVDPLSRAqfWdlIDSIRQRQTNMSVLV---------AT 206
Cdd:TIGR03719 150 lrCPPWDADVTKLSGGERRRVALCRLLLSKPDMLLLDEPTNHLDAESVA--W--LERHLQEYPGTVVAVthdryfldnVA 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 207 AYMEEAER----------FDWLVAMNAgEILATGSAQQLRAKTHSATLE-----------------QAFIALLPEAQRQA 259
Cdd:TIGR03719 226 GWILELDRgrgipwegnySSWLEQKQK-RLEQEEKEESARQKTLKRELEwvrqspkgrqakskarlARYEELLSQEFQKR 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 260 HKP--VVIPPyhAEQ-EEIAIEAKDLTMRFGKFVAVDHVNFRIPRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGqAWLF 336
Cdd:TIGR03719 305 NETaeIYIPP--GPRlGDKVIEAENLTKAFGDKLLIDDLSFKLPPGGIVGVIGPNGAGKSTLFRMITGQEQPDSG-TIEI 381
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 337 GQPVdpndidtrrRVGYMSQAF-SLYNELTVRQNLELHARLFHIPPAEIPARvaQMIERFMLTEVEDTLPAS-LPLGIRQ 414
Cdd:TIGR03719 382 GETV---------KLAYVDQSRdALDPNKTVWEEISGGLDIIKLGKREIPSR--AYVGRFNFKGSDQQKKVGqLSGGERN 450
|
490 500
....*....|....*....|....*
gi 446125071 415 RLSLAVAVIHRPEMLILDEPTSGVD 439
Cdd:TIGR03719 451 RVHLAKTLKSGGNVLLLDEPTNDLD 475
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
1-230 |
1.24e-20 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 94.71 E-value: 1.24e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 1 MTSLTLvpvppvaqlEGVSQHYGKTVALNNITLDIPARSMVGLIGPDGVGKSSLLSLISGARVIEQGNVIVlgGDMRdak 80
Cdd:PRK11000 1 MASVTL---------RNVTKAYGDVVISKDINLDIHEGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLFI--GEKR--- 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 81 hRRDVCPriawMPQGLGK-----NLYHTLSVYENVDFFARLFGHDKAEREARITELLNSTGLAPFRDRPAGKLSGGMKQK 155
Cdd:PRK11000 67 -MNDVPP----AERGVGMvfqsyALYPHLSVAENMSFGLKLAGAKKEEINQRVNQVAEVLQLAHLLDRKPKALSGGQRQR 141
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446125071 156 LGLCCALIHDPELLILDEPTTGVDPLSRAQFWDLIDSIRQRQTNMSVLVATAYMEEAERFDWLVAMNAGEILATG 230
Cdd:PRK11000 142 VAIGRTLVAEPSVFLLDEPLSNLDAALRVQMRIEISRLHKRLGRTMIYVTHDQVEAMTLADKIVVLDAGRVAQVG 216
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
14-235 |
1.37e-20 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 92.07 E-value: 1.37e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 14 QLEGVSQHYGKTVALNNITLDIPARSMVGLIGPDGVGKSSLLSLISGARVIEQGNVIVLGGDMRDAKhRRDVCPRIAWMP 93
Cdd:COG4604 3 EIKNVSKRYGGKVVLDDVSLTIPKGGITALIGPNGAGKSTLLSMISRLLPPDSGEVLVDGLDVATTP-SRELAKRLAILR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 94 QGLGKNLyhTLSVYENVdFFARlFGHDK----AEREARITELLNSTGLAPFRDRPAGKLSGGMKQKlglccALI-----H 164
Cdd:COG4604 82 QENHINS--RLTVRELV-AFGR-FPYSKgrltAEDREIIDEAIAYLDLEDLADRYLDELSGGQRQR-----AFIamvlaQ 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 165 DPELLILDEPTTGVDPL-SRAqfwdLIDSIRQ--RQTNMSVLV-------ATAYMeeaerfDWLVAMNAGEILATGSAQQ 234
Cdd:COG4604 153 DTDYVLLDEPLNNLDMKhSVQ----MMKLLRRlaDELGKTVVIvlhdinfASCYA------DHIVAMKDGRVVAQGTPEE 222
|
.
gi 446125071 235 L 235
Cdd:COG4604 223 I 223
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
20-235 |
1.37e-20 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 92.94 E-value: 1.37e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 20 QHYGKTVALNNITLDIPARSMVGLIGPDGVGKSSLLSLISGARVIEQGNVIVLGGDMrDAKHRRDVCPRIAWMPQGLGKN 99
Cdd:PRK13652 12 SYSGSKEALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIRGEPI-TKENIREVRKFVGLVFQNPDDQ 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 100 LYHTlSVYENVDFFARLFGHDKAEREARITELLNSTGLAPFRDRPAGKLSGGMKQKLGLCCALIHDPELLILDEPTTGVD 179
Cdd:PRK13652 91 IFSP-TVEQDIAFGPINLGLDEETVAHRVSSALHMLGLEELRDRVPHHLSGGEKKRVAIAGVIAMEPQVLVLDEPTAGLD 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 446125071 180 PLSRAQFWDLIDSIRQRQtNMSVLVATAYME-EAERFDWLVAMNAGEILATGSAQQL 235
Cdd:PRK13652 170 PQGVKELIDFLNDLPETY-GMTVIFSTHQLDlVPEMADYIYVMDKGRIVAYGTVEEI 225
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
266-476 |
1.50e-20 |
|
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: 96.59 E-value: 1.50e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 266 PPYHAEQEEI------AIEAKDLTMRF-GKFVAVDHVNFRIPRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGQAWLFGQ 338
Cdd:TIGR02857 305 PRPLAGKAPVtaapasSLEFSGVSVAYpGRRPALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSIAVNGV 384
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 339 PVDPNDIDT-RRRVGYMSQAFSLYNElTVRQNLeLHARlfhipPAEIPARVAQMIERFMLTEVEDTLPASLPL------- 410
Cdd:TIGR02857 385 PLADADADSwRDQIAWVPQHPFLFAG-TIAENI-RLAR-----PDASDAEIREALERAGLDEFVAALPQGLDTpigegga 457
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 411 ----GIRQRLSLAVAVIHRPEMLILDEPTSGVDPVARDMFWQLMVDLSRqdKVTIFISTHFMNEAERCDR 476
Cdd:TIGR02857 458 glsgGQAQRLALARAFLRDAPLLLLDEPTAHLDAETEAEVLEALRALAQ--GRTVLLVTHRLALAALADR 525
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
280-494 |
1.79e-20 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 94.33 E-value: 1.79e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 280 KDLTMRFGKFVAVDHVNFRIPRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGQAWLFGQPVdpNDID-TRRRVGYMSQAF 358
Cdd:PRK11000 7 RNVTKAYGDVVISKDINLDIHEGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLFIGEKRM--NDVPpAERGVGMVFQSY 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 359 SLYNELTVRQNLELHARLFHIPPAEIPARVAQMIERFMLTEVEDTLPASLPLGIRQRLSLAVAVIHRPEMLILDEPTSGV 438
Cdd:PRK11000 85 ALYPHLSVAENMSFGLKLAGAKKEEINQRVNQVAEVLQLAHLLDRKPKALSGGQRQRVAIGRTLVAEPSVFLLDEPLSNL 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 439 DPVARdmfWQLMVDLSRQDK---VTIFISTHFMNEA-ERCDRMSLMHAGKVLASGTPQEL 494
Cdd:PRK11000 165 DAALR---VQMRIEISRLHKrlgRTMIYVTHDQVEAmTLADKIVVLDAGRVAQVGKPLEL 221
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
10-226 |
2.77e-20 |
|
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: 89.41 E-value: 2.77e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 10 PPVAQLEGVSQHYgktvALNNITLDIPARSMVGLIGPDGVGKSSLLSLISGARVIEQGNVIVLGGDMrdakHRRDVCPRI 89
Cdd:cd03215 2 EPVLEVRGLSVKG----AVRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITLDGKPV----TRRSPRDAI 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 90 AwmpQGLG--------KNLYHTLSVYENVdFFARLfghdkaerearitellnstglapfrdrpagkLSGGMKQKLGLCCA 161
Cdd:cd03215 74 R---AGIAyvpedrkrEGLVLDLSVAENI-ALSSL-------------------------------LSGGNQQKVVLARW 118
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446125071 162 LIHDPELLILDEPTTGVDPLSRAQFWDLIDSIRQRqtNMSVLVATAYMEEAERF-DWLVAMNAGEI 226
Cdd:cd03215 119 LARDPRVLILDEPTRGVDVGAKAEIYRLIRELADA--GKAVLLISSELDELLGLcDRILVMYEGRI 182
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
291-495 |
2.96e-20 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 91.97 E-value: 2.96e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 291 AVDHVNFRIPRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGQAWLFGQPV-DPNDI-DTRRRVGYMSQ-AFSLYNELTVR 367
Cdd:PRK13644 17 ALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLVSGIDTgDFSKLqGIRKLVGIVFQnPETQFVGRTVE 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 368 QNLELHARLFHIPPAEIPARVAQMIERFMLTEVEDTLPASLPLGIRQRLSLAVAVIHRPEMLILDEPTSGVDPVARDMFW 447
Cdd:PRK13644 97 EDLAFGPENLCLPPIEIRKRVDRALAEIGLEKYRHRSPKTLSGGQGQCVALAGILTMEPECLIFDEVTSMLDPDSGIAVL 176
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 446125071 448 QLMVDLSRQDKVTIFIsTHFMNEAERCDRMSLMHAGKVLASGTPQELV 495
Cdd:PRK13644 177 ERIKKLHEKGKTIVYI-THNLEELHDADRIIVMDRGKIVLEGEPENVL 223
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
12-238 |
3.02e-20 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 91.83 E-value: 3.02e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 12 VAQLEGVSQHYGK-TVALNNITLDIPARSMVGLIGPDGVGKSSLLSLISGARVIEQGNvIVLGGDMRD--AKHRRDVCPR 88
Cdd:PRK13636 5 ILKVEELNYNYSDgTHALKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGR-ILFDGKPIDysRKGLMKLRES 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 89 IAWMPQGLGKNLYhTLSVYENVDFFARLFGHDKAEREARITELLNSTGLAPFRDRPAGKLSGGMKQKLGLCCALIHDPEL 168
Cdd:PRK13636 84 VGMVFQDPDNQLF-SASVYQDVSFGAVNLKLPEDEVRKRVDNALKRTGIEHLKDKPTHCLSFGQKKRVAIAGVLVMEPKV 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446125071 169 LILDEPTTGVDPLSRAQFWDLIDSIrQRQTNMSVLVATAYMEEAERF-DWLVAMNAGEILATGSAQQLRAK 238
Cdd:PRK13636 163 LVLDEPTAGLDPMGVSEIMKLLVEM-QKELGLTIIIATHDIDIVPLYcDNVFVMKEGRVILQGNPKEVFAE 232
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
277-498 |
3.57e-20 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 91.23 E-value: 3.57e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 277 IEAKDLTMRFGKFVAVDHVNFRIPRGEIFGFLGSNGCGKSTTMKMLTGLL---PASEGQAWLFGQPVD-----PNDI-DT 347
Cdd:PRK09984 5 IRVEKLAKTFNQHQALHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGLItgdKSAGSHIELLGRTVQregrlARDIrKS 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 348 RRRVGYMSQAFSLYNELTVRQNLELHA--------RLFHIPPAEIPARVAQMIERFMLTEVEDTLPASLPLGIRQRLSLA 419
Cdd:PRK09984 85 RANTGYIFQQFNLVNRLSVLENVLIGAlgstpfwrTCFSWFTREQKQRALQALTRVGMVHFAHQRVSTLSGGQQQRVAIA 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 420 VAVIHRPEMLILDEPTSGVDPVARDMFWQLMVDLSRQDKVTIFISTHFMNEAER-CDRMSLMHAGKVLASGTPQELVQQR 498
Cdd:PRK09984 165 RALMQQAKVILADEPIASLDPESARIVMDTLRDINQNDGITVVVTLHQVDYALRyCERIVALRQGHVFYDGSSQQFDNER 244
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
7-233 |
4.99e-20 |
|
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: 90.19 E-value: 4.99e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 7 VPVPPVAQLEGVSQHY----GKTVALNNITLDIPARSMVGLIGPDGVGKSSLLSLISGARVIEQGNVIVLGGDM----RD 78
Cdd:COG4181 3 SSSAPIIELRGLTKTVgtgaGELTILKGISLEVEAGESVAIVGASGSGKSTLLGLLAGLDRPTSGTVRLAGQDLfaldED 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 79 --AKHRRDvcpRIAWMPQGLgkNLYHTLSVYENVDFFARLFGHDKAEREARitELLNSTGLApfrDR----PAGkLSGGM 152
Cdd:COG4181 83 arARLRAR---HVGFVFQSF--QLLPTLTALENVMLPLELAGRRDARARAR--ALLERVGLG---HRldhyPAQ-LSGGE 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 153 KQKLGLCCALIHDPELLILDEPTTGVDPLSRAQFWDLIDSIRQRQTNMSVLVaTAYMEEAERFDWLVAMNAGEILATGSA 232
Cdd:COG4181 152 QQRVALARAFATEPAILFADEPTGNLDAATGEQIIDLLFELNRERGTTLVLV-THDPALAARCDRVLRLRAGRLVEDTAA 230
|
.
gi 446125071 233 Q 233
Cdd:COG4181 231 T 231
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
277-500 |
5.36e-20 |
|
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC transporter that is expressed in the mitochondria. Although the specific function of ATM1 is unknown, its disruption results in the accumulation of excess mitochondrial iron, loss of mitochondrial cytochromes, oxidative damage to mitochondrial DNA, and decreased levels of cytosolic heme proteins. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213220 [Multi-domain] Cd Length: 236 Bit Score: 89.98 E-value: 5.36e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 277 IEAKDLTMRF--GKFVaVDHVNFRIPRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGQAWLFGQPVDPNDIDT-RRRVGY 353
Cdd:cd03253 1 IEFENVTFAYdpGRPV-LKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDGQDIREVTLDSlRRAIGV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 354 MSQAFSLYNElTVRQNLElHARLfHIPPAEI--PARVAQMIERFM-LTEVEDTLPAS----LPLGIRQRLSLAVAVIHRP 426
Cdd:cd03253 80 VPQDTVLFND-TIGYNIR-YGRP-DATDEEVieAAKAAQIHDKIMrFPDGYDTIVGErglkLSGGEKQRVAIARAILKNP 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446125071 427 EMLILDEPTSGVDPVARDMFWQLMVDLSRqDKVTIFIsTHFMNEAERCDRMSLMHAGKVLASGTPQELVQQRGA 500
Cdd:cd03253 157 PILLLDEATSALDTHTEREIQAALRDVSK-GRTTIVI-AHRLSTIVNADKIIVLKDGRIVERGTHEELLAKGGL 228
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
292-545 |
5.51e-20 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 91.43 E-value: 5.51e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 292 VDHVNFRIPRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGQAWLFGQPVDPND-----IDTRRRVGYM-----SQAFsly 361
Cdd:PRK13641 23 LDNISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITIAGYHITPETgnknlKKLRKKVSLVfqfpeAQLF--- 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 362 nELTVRQNLELHARLFHIPPAEIPARVAQMIERFMLTE-VEDTLPASLPLGIRQRLSLAVAVIHRPEMLILDEPTSGVDP 440
Cdd:PRK13641 100 -ENTVLKDVEFGPKNFGFSEDEAKEKALKWLKKVGLSEdLISKSPFELSGGQMRRVAIAGVMAYEPEILCLDEPAAGLDP 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 441 VARDMFWQLMVDLSRQDKVTIFIsTHFMNE-AERCDRMSLMHAGKVLASGTPQELVQQRgaanleaafiSWLQEAAGAAP 519
Cdd:PRK13641 179 EGRKEMMQLFKDYQKAGHTVILV-THNMDDvAEYADDVLVLEHGKLIKHASPKEIFSDK----------EWLKKHYLDEP 247
|
250 260
....*....|....*....|....*.
gi 446125071 520 ETPIPPSQTPAASGKPSRQGLSFRRL 545
Cdd:PRK13641 248 ATSRFASKLEKGGFKFSEMPLTIDEL 273
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
43-206 |
6.78e-20 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 88.78 E-value: 6.78e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 43 LIGPDGVGKSSLLSLISGARVIEQGNVIVLGGDMRDAKHRrdvcPRIAWmpqgLG-KN-LYHTLSVYENVDFFARLFGhd 120
Cdd:PRK13539 33 LTGPNGSGKTTLLRLIAGLLPPAAGTIKLDGGDIDDPDVA----EACHY----LGhRNaMKPALTVAENLEFWAAFLG-- 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 121 kaEREARITELLNSTGLAPFRDRPAGKLSGGMKQKLGLCCALIHDPELLILDEPTTGVDPLSRAQFWDLIdSIRQRQTNM 200
Cdd:PRK13539 103 --GEELDIAAALEAVGLAPLAHLPFGYLSAGQKRRVALARLLVSNRPIWILDEPTAALDAAAVALFAELI-RAHLAQGGI 179
|
....*.
gi 446125071 201 sVLVAT 206
Cdd:PRK13539 180 -VIAAT 184
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
42-238 |
9.21e-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: 9.21e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 42 GLIGPDGVGKSSLLSLISGARVIEQGNVIVLGG----DMRDAKHRRDVCPRIAWMPQglgknlyhTLSVYENVDFFARLF 117
Cdd:TIGR01257 1969 GLLGVNGAGKTTTFKMLTGDTTVTSGDATVAGKsiltNISDVHQNMGYCPQFDAIDD--------LLTGREHLYLYARLR 2040
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 118 GHDKAEREARITELLNSTGLAPFRDRPAGKLSGGMKQKLGLCCALIHDPELLILDEPTTGVDPLSRAQFWDLIDSIRQRQ 197
Cdd:TIGR01257 2041 GVPAEEIEKVANWSIQSLGLSLYADRLAGTYSGGNKRKLSTAIALIGCPPLVLLDEPTTGMDPQARRMLWNTIVSIIREG 2120
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 446125071 198 TnmSVLVATAYMEEAERF-DWLVAMNAGEILATGSAQQLRAK 238
Cdd:TIGR01257 2121 R--AVVLTSHSMEECEALcTRLAIMVKGAFQCLGTIQHLKSK 2160
|
|
| PvdE |
COG4615 |
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ... |
243-485 |
1.29e-19 |
|
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: 93.71 E-value: 1.29e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 243 TLEQAFIAL---------LPEAQRQAHKPVVIPPYHAEQEeiaIEAKDLTMRF-----GKFVAVDHVNFRIPRGEIFGFL 308
Cdd:COG4615 288 TLSRANVALrkieelelaLAAAEPAAADAAAPPAPADFQT---LELRGVTYRYpgedgDEGFTLGPIDLTIRRGELVFIV 364
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 309 GSNGCGKSTTMKMLTGLLPASEGQAWLFGQPVDPNDIDTRRrvgymsQAFSlynelTVRQNLELHARLFHIPPAEIPARV 388
Cdd:COG4615 365 GGNGSGKSTLAKLLTGLYRPESGEILLDGQPVTADNREAYR------QLFS-----AVFSDFHLFDRLLGLDGEADPARA 433
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 389 AQMIERFML---TEVED----TLpaSLPLGIRQRLSLAVAVI-HRPeMLILDEPTSGVDPVARDMFW-QLMVDLSRQDKv 459
Cdd:COG4615 434 RELLERLELdhkVSVEDgrfsTT--DLSQGQRKRLALLVALLeDRP-ILVFDEWAADQDPEFRRVFYtELLPELKARGK- 509
|
250 260 270
....*....|....*....|....*....|
gi 446125071 460 TIFISTH----FmneaERCDRMSLMHAGKV 485
Cdd:COG4615 510 TVIAISHddryF----DLADRVLKMDYGKL 535
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
27-252 |
1.31e-19 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 89.94 E-value: 1.31e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 27 ALNNITLDIPARSMVGLIGPDGVGKSSLLSLISGARVIEQGNVIVLGGDMRDAKHRRdvcpRIAWMPQGLGKNLYHTLSV 106
Cdd:PRK15056 22 ALRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKISILGQPTRQALQKN----LVAYVPQSEEVDWSFPVLV 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 107 yENVDFFARlFGH------DKAEREARITELLNSTGLAPFRDRPAGKLSGGMKQKLGLCCALIHDPELLILDEPTTGVDP 180
Cdd:PRK15056 98 -EDVVMMGR-YGHmgwlrrAKKRDRQIVTAALARVDMVEFRHRQIGELSGGQKKRVFLARAIAQQGQVILLDEPFTGVDV 175
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446125071 181 LSRAQFWDLIDSIRQRQTNMsvLVATAYMEEAERFDWLVAMNAGEILATGSAqqlRAKTHSATLEQAFIALL 252
Cdd:PRK15056 176 KTEARIISLLRELRDEGKTM--LVSTHNLGSVTEFCDYTVMVKGTVLASGPT---ETTFTAENLELAFSGVL 242
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
277-488 |
1.52e-19 |
|
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: 92.97 E-value: 1.52e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 277 IEAKDLTMRFGKFVAVDHVNFRIPRGEIFGFLGSNGCGKSTTMKMLTGLLPAS--EGQAWLFGQPVDPNDI-DTRRR-VG 352
Cdd:TIGR02633 2 LEMKGIVKTFGGVKALDGIDLEVRPGECVGLCGENGAGKSTLMKILSGVYPHGtwDGEIYWSGSPLKASNIrDTERAgIV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 353 YMSQAFSLYNELTVRQNLELHARLFH----IPPAEIPARVAQMIERFMLTEVEDTLPAS-LPLGIRQRLSLAVAVIHRPE 427
Cdd:TIGR02633 82 IIHQELTLVPELSVAENIFLGNEITLpggrMAYNAMYLRAKNLLRELQLDADNVTRPVGdYGGGQQQLVEIAKALNKQAR 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446125071 428 MLILDEPTSGVDPVARDMFWQLMVDLSRQDKVTIFIStHFMNEAER-CDRMSLMHAGKVLAS 488
Cdd:TIGR02633 162 LLILDEPSSSLTEKETEILLDIIRDLKAHGVACVYIS-HKLNEVKAvCDTICVIRDGQHVAT 222
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
280-485 |
1.58e-19 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 89.35 E-value: 1.58e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 280 KDLTMRFGKFVAVDHVNFRIPRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGQAWLFGQPVDPNDIDTRrrvgYMSQAFS 359
Cdd:PRK11247 16 NAVSKRYGERTVLNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAGELLAGTAPLAEAREDTR----LMFQDAR 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 360 LYNELTVRQNLELHARLFHIPPAEiparvaQMIERFMLTEVEDTLPASLPLGIRQRLSLAVAVIHRPEMLILDEPTSGVD 439
Cdd:PRK11247 92 LLPWKKVIDNVGLGLKGQWRDAAL------QALAAVGLADRANEWPAALSGGQKQRVALARALIHRPGLLLLDEPLGALD 165
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 446125071 440 PVARDMFWQLMVDLSRQDKVTIFISTHFMNEA-ERCDRMSLMHAGKV 485
Cdd:PRK11247 166 ALTRIEMQDLIESLWQQHGFTVLLVTHDVSEAvAMADRVLLIEEGKI 212
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
11-235 |
1.62e-19 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 89.69 E-value: 1.62e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 11 PVAQLEGVSQHY--GKTVALNNITLDIPARSMVGLIGPDGVGKSSLLSLISGARVIEQGnVIVLGGDMRDAKHRRDVCPR 88
Cdd:PRK13635 4 EIIRVEHISFRYpdAATYALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAG-TITVGGMVLSEETVWDVRRQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 89 IAWMPQGlGKNLYHTLSVYENVDFFARLFGHDKAEREARITELLNSTGLAPFRDRPAGKLSGGMKQKLGLCCALIHDPEL 168
Cdd:PRK13635 83 VGMVFQN-PDNQFVGATVQDDVAFGLENIGVPREEMVERVDQALRQVGMEDFLNREPHRLSGGQKQRVAIAGVLALQPDI 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446125071 169 LILDEPTTGVDPLSRAQfwdLIDSIRQ--RQTNMSVLVATAYMEEAERFDWLVAMNAGEILATGSAQQL 235
Cdd:PRK13635 162 IILDEATSMLDPRGRRE---VLETVRQlkEQKGITVLSITHDLDEAAQADRVIVMNKGEILEEGTPEEI 227
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
293-500 |
1.76e-19 |
|
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: 88.37 E-value: 1.76e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 293 DHVNFRIPRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGQAWLFGQPVDPNDI-DTRRRVGYMSQAFSLYNeLTVRQNLE 371
Cdd:cd03249 20 KGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEILLDGVDIRDLNLrWLRSQIGLVSQEPVLFD-GTIAENIR 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 372 LHARLFHIPPAEIPARVAQmIERF--MLTEVEDTL----PASLPLGIRQRLSLAVAVIHRPEMLILDEPTSGVDpVARDM 445
Cdd:cd03249 99 YGKPDATDEEVEEAAKKAN-IHDFimSLPDGYDTLvgerGSQLSGGQKQRIAIARALLRNPKILLLDEATSALD-AESEK 176
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 446125071 446 FWQLMVDLSRQDKVTIFIStHFMNEAERCDRMSLMHAGKVLASGTPQELVQQRGA 500
Cdd:cd03249 177 LVQEALDRAMKGRTTIVIA-HRLSTIRNADLIAVLQNGQVVEQGTHDELMAQKGV 230
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
7-238 |
1.80e-19 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 93.31 E-value: 1.80e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 7 VPVPPVA---QLEGVSQHY-GKTVALNNITLDIPARSMVGLIGPDGVGKSSLLSLISGARVIEQGNVIVLGGDMRDAKH- 81
Cdd:COG1132 331 VPLPPVRgeiEFENVSFSYpGDRPVLKDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYDPTSGRILIDGVDIRDLTLe 410
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 82 --RRdvcpRIAWMPQglgKN-LYHTlSVYENVdffarLFGHDKAEREaRITELLNSTGLAPF-RDRPAG----------K 147
Cdd:COG1132 411 slRR----QIGVVPQ---DTfLFSG-TIRENI-----RYGRPDATDE-EVEEAAKAAQAHEFiEALPDGydtvvgergvN 476
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 148 LSGGMKQKLGLCCALIHDPELLILDEPTTGVDPLSRAQFWDLIDSIRQRQTnmSVLVA----TaymeeAERFDWLVAMNA 223
Cdd:COG1132 477 LSGGQRQRIAIARALLKDPPILILDEATSALDTETEALIQEALERLMKGRT--TIVIAhrlsT-----IRNADRILVLDD 549
|
250
....*....|....*
gi 446125071 224 GEILATGSAQQLRAK 238
Cdd:COG1132 550 GRIVEQGTHEELLAR 564
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
27-231 |
2.44e-19 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 89.41 E-value: 2.44e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 27 ALNNITLDIPARSMVGLIGPDGVGKSSLLSLISGARVIEQGNVIVLGGDMRDAKHRRDVCP---RIAWMPQGLGKNLYHT 103
Cdd:PRK13643 21 ALFDIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVTVGDIVVSSTSKQKEIKPvrkKVGVVFQFPESQLFEE 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 104 lSVYENVDFFARLFGHDKAEREARITELLNSTGLAP-FRDRPAGKLSGGMKQKLGLCCALIHDPELLILDEPTTGVDPLS 182
Cdd:PRK13643 101 -TVLKDVAFGPQNFGIPKEKAEKIAAEKLEMVGLADeFWEKSPFELSGGQMRRVAIAGILAMEPEVLVLDEPTAGLDPKA 179
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 446125071 183 RAQFWDLIDSIrqRQTNMSVLVATAYMEE-AERFDWLVAMNAGEILATGS 231
Cdd:PRK13643 180 RIEMMQLFESI--HQSGQTVVLVTHLMDDvADYADYVYLLEKGHIISCGT 227
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
23-206 |
2.81e-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: 2.81e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 23 GKTVALNNITLDIPARSMVGLIGPDGVGKSSLLSLISGARVIEQGNVIVLGGDM-RDAKHRRDVCPRIAWMPqGLgKNly 101
Cdd:TIGR01189 11 GERMLFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRWNGTPLaEQRDEPHENILYLGHLP-GL-KP-- 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 102 hTLSVYENVDFFARLfgHDKAEREarITELLNSTGLAPFRDRPAGKLSGGMKQKLGLCCALIHDPELLILDEPTTGVDPL 181
Cdd:TIGR01189 87 -ELSALENLHFWAAI--HGGAQRT--IEDALAAVGLTGFEDLPAAQLSAGQQRRLALARLWLSRRPLWILDEPTTALDKA 161
|
170 180
....*....|....*....|....*
gi 446125071 182 SRAQFWDLIDSIRQRQTnmSVLVAT 206
Cdd:TIGR01189 162 GVALLAGLLRAHLARGG--IVLLTT 184
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
295-490 |
3.12e-19 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 87.56 E-value: 3.12e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 295 VNFRIPRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGQAWLFGQPVDPNDIDTR-----RRVGYMSQAFSLYNELTVRQN 369
Cdd:PRK11629 28 VSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPMSKLSSAAKaelrnQKLGFIYQFHHLLPDFTALEN 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 370 LELHARLFHIPPAEIPARVAQMIERFMLTEVEDTLPASLPLGIRQRLSLAVAVIHRPEMLILDEPTSGVDPVARDMFWQL 449
Cdd:PRK11629 108 VAMPLLIGKKKPAEINSRALEMLAAVGLEHRANHRPSELSGGERQRVAIARALVNNPRLVLADEPTGNLDARNADSIFQL 187
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 446125071 450 MVDLSRQDKVTIFISTHFMNEAERCDRMSLMHAGKVLASGT 490
Cdd:PRK11629 188 LGELNRLQGTAFLVVTHDLQLAKRMSRQLEMRDGRLTAELS 228
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
27-239 |
3.16e-19 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 88.92 E-value: 3.16e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 27 ALNNITLDIPARSMVGLIGPDGVGKSSLLSLISG-----ARVIEQGN-VIVLGGDMRDAKHRRDVCPRIAWMPQglgknl 100
Cdd:PRK13634 22 ALYDVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGllqptSGTVTIGErVITAGKKNKKLKPLRKKVGIVFQFPE------ 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 101 yHTL---SVYENVDFFARLFGHDKAEREARITELLNSTGLAP-FRDRPAGKLSGGMKQKLGLCCALIHDPELLILDEPTT 176
Cdd:PRK13634 96 -HQLfeeTVEKDICFGPMNFGVSEEDAKQKAREMIELVGLPEeLLARSPFELSGGQMRRVAIAGVLAMEPEVLVLDEPTA 174
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446125071 177 GVDPLSRAQFWDLIDSIRQRQtNMSVLVATAYMEEAERF-DWLVAMNAGEILATGSAQQLRAKT 239
Cdd:PRK13634 175 GLDPKGRKEMMEMFYKLHKEK-GLTTVLVTHSMEDAARYaDQIVVMHKGTVFLQGTPREIFADP 237
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
11-236 |
3.72e-19 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 88.12 E-value: 3.72e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 11 PVAQLEGVSQHYGKTVALNNITLDIPARSMVGLIGPDGVGKSSLLSLISGARVIEQGNvIVLGGDmrdakhrrdvcpRIA 90
Cdd:PRK11300 4 PLLSVSGLMMRFGGLLAVNNVNLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGT-ILLRGQ------------HIE 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 91 WMP------QGLGKN-----LYHTLSVYENV----------DFFARLF---GHDKAEREA--RITELLNSTGLAPFRDRP 144
Cdd:PRK11300 71 GLPghqiarMGVVRTfqhvrLFREMTVIENLlvaqhqqlktGLFSGLLktpAFRRAESEAldRAATWLERVGLLEHANRQ 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 145 AGKLSGGMKQKLGLCCALIHDPELLILDEPTTGVDPLSRAQFWDLIDSIRqRQTNMSVLV----ATAYMEEAERfdwLVA 220
Cdd:PRK11300 151 AGNLAYGQQRRLEIARCMVTQPEILMLDEPAAGLNPKETKELDELIAELR-NEHNVTVLLiehdMKLVMGISDR---IYV 226
|
250
....*....|....*.
gi 446125071 221 MNAGEILATGSAQQLR 236
Cdd:PRK11300 227 VNQGTPLANGTPEEIR 242
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
28-258 |
3.76e-19 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 88.64 E-value: 3.76e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 28 LNNITLDIPARSMVGLIGPDGVGKSSLLSLISGARVIEQGNVIVLGgDMRDAKHRRDVCPRIAWMPQGlGKNLYHTLSVY 107
Cdd:PRK13650 23 LNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIIDG-DLLTEENVWDIRHKIGMVFQN-PDNQFVGATVE 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 108 ENVDFFARLFGHDKAEREARITELLNSTGLAPFRDRPAGKLSGGMKQKLGLCCALIHDPELLILDEPTTGVDPLSRAQFW 187
Cdd:PRK13650 101 DDVAFGLENKGIPHEEMKERVNEALELVGMQDFKEREPARLSGGQKQRVAIAGAVAMRPKIIILDEATSMLDPEGRLELI 180
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446125071 188 DLIDSIRQrQTNMSVLVATAYMEEAERFDWLVAMNAGEILATGSAQQLRAKTH---SATLEQAFIALLPEAQRQ 258
Cdd:PRK13650 181 KTIKGIRD-DYQMTVISITHDLDEVALSDRVLVMKNGQVESTSTPRELFSRGNdllQLGLDIPFTTSLVQSLRQ 253
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
277-485 |
3.84e-19 |
|
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: 85.73 E-value: 3.84e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 277 IEAKDLTMRFG--KFVAVDHVNFRIPRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGQAWLFGQPVDPNDIDT-RRRVGY 353
Cdd:cd03246 1 LEVENVSFRYPgaEPPVLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDGADISQWDPNElGDHVGY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 354 MSQAFSLYnELTVRQNLelharlfhippaeiparvaqmierfmltevedtlpasLPLGIRQRLSLAVAVIHRPEMLILDE 433
Cdd:cd03246 81 LPQDDELF-SGSIAENI-------------------------------------LSGGQRQRLGLARALYGNPRILVLDE 122
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 446125071 434 PTSGVDPVARDMFWQLMVDLSRQDKVTIFIsTHFMNEAERCDRMSLMHAGKV 485
Cdd:cd03246 123 PNSHLDVEGERALNQAIAALKAAGATRIVI-AHRPETLASADRILVLEDGRV 173
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
28-235 |
4.19e-19 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 88.18 E-value: 4.19e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 28 LNNITLDIPARSMVGLIGPDGVGKSSLLSLISgaRVIE--------QGNVIVLGGDMR--DAKHRRDVCPRIAWMPqglg 97
Cdd:PRK14246 26 LKDITIKIPNNSIFGIMGPSGSGKSTLLKVLN--RLIEiydskikvDGKVLYFGKDIFqiDAIKLRKEVGMVFQQP---- 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 98 kNLYHTLSVYENVDFFARLFG-HDKAEREARITELLNSTGL-APFRDR---PAGKLSGGMKQKLGLCCALIHDPELLILD 172
Cdd:PRK14246 100 -NPFPHLSIYDNIAYPLKSHGiKEKREIKKIVEECLRKVGLwKEVYDRlnsPASQLSGGQQQRLTIARALALKPKVLLMD 178
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446125071 173 EPTTGVDPLSRAQFWDLIDSIRQRQTnmSVLVATAYMEEAERFDWLVAMNAGEILATGSAQQL 235
Cdd:PRK14246 179 EPTSMIDIVNSQAIEKLITELKNEIA--IVIVSHNPQQVARVADYVAFLYNGELVEWGSSNEI 239
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
270-494 |
4.77e-19 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 88.28 E-value: 4.77e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 270 AEQEEIAIEAKDLTMRFGKFVAVDHVNFRIPRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGQAWLFGQPVDPND----I 345
Cdd:PRK11831 1 EQSVANLVDMRGVSFTRGNRCIFDNISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEILFDGENIPAMSrsrlY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 346 DTRRRVGYMSQAFSLYNELTVRQN----LELHARLfhiPPAEIPARVAQMIERFMLTEVEDTLPASLPLGIRQRLSLAVA 421
Cdd:PRK11831 81 TVRKRMSMLFQSGALFTDMNVFDNvaypLREHTQL---PAPLLHSTVMMKLEAVGLRGAAKLMPSELSGGMARRAALARA 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446125071 422 VIHRPEMLILDEPTSGVDPVARDMFWQLMVDLSRQDKVTIFISTHFMNEA-ERCDRMSLMHAGKVLASGTPQEL 494
Cdd:PRK11831 158 IALEPDLIMFDEPFVGQDPITMGVLVKLISELNSALGVTCVVVSHDVPEVlSIADHAYIVADKKIVAHGSAQAL 231
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
2-206 |
7.52e-19 |
|
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family transporter in which each gene contains an N-terminal membrane-spanning domain (pfam00664) and a C-terminal ATP-binding domain (pfam00005). In E. coli these genes were discovered as mutants which caused the terminal heme-copper oxidase complex cytochrome bd to fail to assemble. Recent work has shown that the transporter is involved in export of redox-active thiol compounds such as cysteine and glutathione. The linkage to assembly of the cytochrome bd complex is further supported by the conserved operon structure found outside the gammaproteobacteria (cydABCD) containing both the transporter and oxidase genes components. The genes used as the seed members for this model are all either found in the gammproteobacterial context or the CydABCD context. All members of this family scoring above trusted at the time of its creation were from genomes which encode a cytochrome bd complex.
Pssm-ID: 274331 [Multi-domain] Cd Length: 530 Bit Score: 91.27 E-value: 7.52e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 2 TSLTLVPVPPVAQLEGVSQHY-GKTVALNNITLDIPARSMVGLIGPDGVGKSSLLSLISGARVIEQGNVIVLGGDMRDAK 80
Cdd:TIGR02868 324 AAGAVGLGKPTLELRDLSAGYpGAPPVLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPLQGEVTLDGVPVSSLD 403
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 81 HRrDVCPRIAWMPQGlgKNLYHTlSVYENVdffaRLFGHDKAEREarITELLNSTGLAPF-RDRPAG----------KLS 149
Cdd:TIGR02868 404 QD-EVRRRVSVCAQD--AHLFDT-TVRENL----RLARPDATDEE--LWAALERVGLADWlRALPDGldtvlgeggaRLS 473
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 446125071 150 GGMKQKLGLCCALIHDPELLILDEPTTGVDPLSRAQfwdLIDSIRQRQTNMSVLVAT 206
Cdd:TIGR02868 474 GGERQRLALARALLADAPILLLDEPTEHLDAETADE---LLEDLLAALSGRTVVLIT 527
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
28-230 |
8.29e-19 |
|
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ABC transporters homologous to the Drosophila white gene, which acts as a dimeric importer for eye pigment precursors. The eye pigmentation of Drosophila is developed from the synthesis and deposition in the cells of red pigments, which are synthesized from guanine, and brown pigments, which are synthesized from tryptophan. The pigment precursors are encoded by the white, brown, and scarlet genes, respectively. Evidence from genetic and biochemical studies suggest that the White and Brown proteins function as heterodimers to import guanine, while the White and Scarlet proteins function to import tryptophan. However, a recent study also suggests that White may be involved in the transport of a metabolite, such as 3-hydroxykynurenine, across intracellular membranes. Mammalian ABC transporters belonging to the White subfamily (ABCG1, ABCG5, and ABCG8) have been shown to be involved in the regulation of lipid-trafficking mechanisms in macrophages, hepatocytes, and intestinal mucosa cells. ABCG1 (ABC8), the human homolog of the Drosophila white gene is induced in monocyte-derived macrophages during cholesterol influx mediated by acetylated low-density lipoprotein. It is possible that human ABCG1 forms heterodimers with several heterologous partners.
Pssm-ID: 213201 [Multi-domain] Cd Length: 226 Bit Score: 86.17 E-value: 8.29e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 28 LNNITLDIPARSMVGLIGPDGVGKSSLLSLISGaRVIEQGN---VIVLGGDMRDAKHRRDvcpRIAWMPQGlgKNLYHTL 104
Cdd:cd03234 23 LNDVSLHVESGQVMAILGSSGSGKTTLLDAISG-RVEGGGTtsgQILFNGQPRKPDQFQK---CVAYVRQD--DILLPGL 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 105 SVYENVDFFARLFGH---DKAEREARI-TELLNSTGLAPFRDRPAGKLSGGMKQKLGLCCALIHDPELLILDEPTTGVDP 180
Cdd:cd03234 97 TVRETLTYTAILRLPrksSDAIRKKRVeDVLLRDLALTRIGGNLVKGISGGERRRVSIAVQLLWDPKVLILDEPTSGLDS 176
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 446125071 181 LSRaqfWDLIDSIRQRQTNMSVLVATAYMEEAE---RFDWLVAMNAGEILATG 230
Cdd:cd03234 177 FTA---LNLVSTLSQLARRNRIVILTIHQPRSDlfrLFDRILLLSSGEIVYSG 226
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
27-235 |
8.35e-19 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 87.49 E-value: 8.35e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 27 ALNNITLDIPARSMVGLIGPDGVGKSSLLSLISGARVIEQGNVIVLGGDMRDAKHRRDVCP---RIAWMPQGLGKNLYHT 103
Cdd:PRK13649 22 ALFDVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDDTLITSTSKNKDIKQirkKVGLVFQFPESQLFEE 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 104 lSVYENVDFFARLFGHDKAEREARITELLNSTGLAP-FRDRPAGKLSGGMKQKLGLCCALIHDPELLILDEPTTGVDPLS 182
Cdd:PRK13649 102 -TVLKDVAFGPQNFGVSQEEAEALAREKLALVGISEsLFEKNPFELSGGQMRRVAIAGILAMEPKILVLDEPTAGLDPKG 180
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 446125071 183 RAQFWDLIDSIrqRQTNMSVLVATAYMEE-AERFDWLVAMNAGEILATGSAQQL 235
Cdd:PRK13649 181 RKELMTLFKKL--HQSGMTIVLVTHLMDDvANYADFVYVLEKGKLVLSGKPKDI 232
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
277-489 |
8.54e-19 |
|
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome bd biogenesis. The CydC and CydD proteins are important for the formation of cytochrome bd terminal oxidase of E. coli and it has been proposed that they were necessary for biosynthesis of the cytochrome bd quinol oxidase and for periplasmic c-type cytochromes. CydCD were proposed to determine a heterooligomeric complex important for heme export into the periplasm or to be involved in the maintenance of the proper redox state of the periplasmic space. In Bacillus subtilis, the absence of CydCD does not affect the presence of halo-cytochrome c in the membrane and this observation suggests that CydCD proteins are not involved in the export of heme in this organism.
Pssm-ID: 213214 [Multi-domain] Cd Length: 178 Bit Score: 84.67 E-value: 8.54e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 277 IEAKDLTMRFG--KFVAVDHVNFRIPRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGQAWLFGQPVDPNDIDTRRRVGYM 354
Cdd:cd03247 1 LSINNVSFSYPeqEQQVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDGVPVSDLEKALSSLISVL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 355 SQAFSLYNElTVRQNLElharlfhippaeiparvaqmiERFMLTEvedtlpaslplgiRQRLSLAVAVIHRPEMLILDEP 434
Cdd:cd03247 81 NQRPYLFDT-TLRNNLG---------------------RRFSGGE-------------RQRLALARILLQDAPIVLLDEP 125
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 446125071 435 TSGVDPVARDMFWQLMVDLSRqDKVTIFIsTHFMNEAERCDRMSLMHAGKVLASG 489
Cdd:cd03247 126 TVGLDPITERQLLSLIFEVLK-DKTLIWI-THHLTGIEHMDKILFLENGKIIMQG 178
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
22-247 |
8.97e-19 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 87.37 E-value: 8.97e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 22 YGKTVALNNITLDIPARSMVGLIGPDGVGKSSLLSLISGARVIEQGNVIVLGGDMrDAKHRRDVCPR--IAWMPQGLGKN 99
Cdd:PRK13638 11 YQDEPVLKGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLRPQKGAVLWQGKPL-DYSKRGLLALRqqVATVFQDPEQQ 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 100 LYHTlSVYENVDFFARLFGHDKAEREARITELLNSTGLAPFRDRPAGKLSGGMKQKLGLCCALIHDPELLILDEPTTGVD 179
Cdd:PRK13638 90 IFYT-DIDSDIAFSLRNLGVPEAEITRRVDEALTLVDAQHFRHQPIQCLSHGQKKRVAIAGALVLQARYLLLDEPTAGLD 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446125071 180 PLSRAQFWDLIDSIRQrQTNMSVLVATAYMEEAERFDWLVAMNAGEILATGSAQQLRAKTHsaTLEQA 247
Cdd:PRK13638 169 PAGRTQMIAIIRRIVA-QGNHVIISSHDIDLIYEISDAVYVLRQGQILTHGAPGEVFACTE--AMEQA 233
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
277-495 |
9.72e-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: 90.63 E-value: 9.72e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 277 IEAKDLTMRFGKFVAVDHVNFRIPRGEIFGFLGSNGCGKSTTMKMLTGL--LPASEGQ-----------AWL-------- 335
Cdd:TIGR03269 1 IEVKNLTKKFDGKEVLKNISFTIEEGEVLGILGRSGAGKSVLMHVLRGMdqYEPTSGRiiyhvalcekcGYVerpskvge 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 336 ---------------FGQPVDPNDIDTRRRVGYMSQ-AFSLYNELTVRQNLelharLFHIPPAEIPA-----RVAQMIER 394
Cdd:TIGR03269 81 pcpvcggtlepeevdFWNLSDKLRRRIRKRIAIMLQrTFALYGDDTVLDNV-----LEALEEIGYEGkeavgRAVDLIEM 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 395 FMLTEVEDTLPASLPLGIRQRLSLAVAVIHRPEMLILDEPTSGVDPVARDMFWQLMVDLSRQDKVTIFISTHFMNEAER- 473
Cdd:TIGR03269 156 VQLSHRITHIARDLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALEEAVKASGISMVLTSHWPEVIEDl 235
|
250 260
....*....|....*....|..
gi 446125071 474 CDRMSLMHAGKVLASGTPQELV 495
Cdd:TIGR03269 236 SDKAIWLENGEIKEEGTPDEVV 257
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
15-231 |
1.19e-18 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 87.37 E-value: 1.19e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 15 LEGVSQHYGKTV-----ALNNITLDIPARSMVGLIGPDGVGKSSLLSLISGARVIEQGNVIV----LGGDMRDAKHRRDV 85
Cdd:PRK13645 9 LDNVSYTYAKKTpfefkALNNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGLIISETGQTIVgdyaIPANLKKIKEVKRL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 86 CPRIAWMPQGLGKNLYHTlSVYENVDFFARLFGHDKAEREARITELLNSTGLA-PFRDRPAGKLSGGMKQKLGLCCALIH 164
Cdd:PRK13645 89 RKEIGLVFQFPEYQLFQE-TIEKDIAFGPVNLGENKQEAYKKVPELLKLVQLPeDYVKRSPFELSGGQKRRVALAGIIAM 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446125071 165 DPELLILDEPTTGVDPLSRAQFWDLIDSIRQRQTNMSVLVaTAYMEEAERF-DWLVAMNAGEILATGS 231
Cdd:PRK13645 168 DGNTLVLDEPTGGLDPKGEEDFINLFERLNKEYKKRIIMV-THNMDQVLRIaDEVIVMHEGKVISIGS 234
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
270-539 |
1.21e-18 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 86.86 E-value: 1.21e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 270 AEQEEIAIEAKDLTMRFGKfVAVDHVNFRIPRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGQAWLFGQPVdpNDIDTRR 349
Cdd:PRK15056 2 MQQAGIVVNDVTVTWRNGH-TALRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKISILGQPT--RQALQKN 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 350 RVGYMSQ------AFSLYNELTVRQNLELHARLFHIPPAEIPARVAQMIERFMLTEVEDTLPASLPLGIRQRLSLAVAVI 423
Cdd:PRK15056 79 LVAYVPQseevdwSFPVLVEDVVMMGRYGHMGWLRRAKKRDRQIVTAALARVDMVEFRHRQIGELSGGQKKRVFLARAIA 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 424 HRPEMLILDEPTSGVDPVARDMFWQLMVDLsRQDKVTIFISTHFMNE-AERCDrMSLMHAGKVLASGtPQELVQQrgAAN 502
Cdd:PRK15056 159 QQGQVILLDEPFTGVDVKTEARIISLLREL-RDEGKTMLVSTHNLGSvTEFCD-YTVMVKGTVLASG-PTETTFT--AEN 233
|
250 260 270
....*....|....*....|....*....|....*...
gi 446125071 503 LEAAFISWLQEAA-GAAPETPIPPSQTPAASGKPSRQG 539
Cdd:PRK15056 234 LELAFSGVLRHVAlNGSEESIITDDERPFISHRPAAVQ 271
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
14-232 |
1.23e-18 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 86.22 E-value: 1.23e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 14 QLEGVSQHYGKTVALNNITLDIPARSMVGLIGPDGVGKSSLLSLISGARVIEQGNVIVLGG--DMRDAKHRRdvcpRIAW 91
Cdd:COG4161 4 QLKNINCFYGSHQALFDINLECPSGETLVLLGPSGAGKSSLLRVLNLLETPDSGQLNIAGHqfDFSQKPSEK----AIRL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 92 MPQGLGK-----NLYHTLSVYEN-VDFFARLFGHDKAEREARITELLNSTGLAPFRDRPAGKLSGGMKQKLGLCCALIHD 165
Cdd:COG4161 80 LRQKVGMvfqqyNLWPHLTVMENlIEAPCKVLGLSKEQAREKAMKLLARLRLTDKADRFPLHLSGGQQQRVAIARALMME 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446125071 166 PELLILDEPTTGVDPLSRAQFWDLIDSIrqRQTNMSVLVATAYMEEAERF-DWLVAMNAGEILATGSA 232
Cdd:COG4161 160 PQVLLFDEPTAALDPEITAQVVEIIREL--SQTGITQVIVTHEVEFARKVaSQVVYMEKGRIIEQGDA 225
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
281-504 |
1.31e-18 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 86.56 E-value: 1.31e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 281 DLTMRFGKFVAVDHVNFRIPRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGQAWLFGQPV-------------DPNDIDT 347
Cdd:PRK10619 10 DLHKRYGEHEVLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNGQTInlvrdkdgqlkvaDKNQLRL 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 348 -RRRVGYMSQAFSLYNELTVRQN-LELHARLFHIPPAEIPARVAQMIERFMLTE-VEDTLPASLPLGIRQRLSLAVAVIH 424
Cdd:PRK10619 90 lRTRLTMVFQHFNLWSHMTVLENvMEAPIQVLGLSKQEARERAVKYLAKVGIDErAQGKYPVHLSGGQQQRVSIARALAM 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 425 RPEMLILDEPTSGVDPVARDMFWQLMVDLSRQDKvTIFISTHFMNEAERC-DRMSLMHAGKVLASGTPQELVQQRGAANL 503
Cdd:PRK10619 170 EPEVLLFDEPTSALDPELVGEVLRIMQQLAEEGK-TMVVVTHEMGFARHVsSHVIFLHQGKIEEEGAPEQLFGNPQSPRL 248
|
.
gi 446125071 504 E 504
Cdd:PRK10619 249 Q 249
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
288-494 |
1.55e-18 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 86.99 E-value: 1.55e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 288 KFVAVDHVNFRIPRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGQAwLFGQPVDPNDI-------DTRRRVGYMSQ--AF 358
Cdd:PRK13645 23 EFKALNNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGLIISETGQT-IVGDYAIPANLkkikevkRLRKEIGLVFQfpEY 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 359 SLYNElTVRQNLELHARLFHIPPAEIPARVAQMIERFML-TEVEDTLPASLPLGIRQRLSLAVAVIHRPEMLILDEPTSG 437
Cdd:PRK13645 102 QLFQE-TIEKDIAFGPVNLGENKQEAYKKVPELLKLVQLpEDYVKRSPFELSGGQKRRVALAGIIAMDGNTLVLDEPTGG 180
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 446125071 438 VDPVARDMFWQLMVDLSRQDKVTIFISTHFMNEAER-CDRMSLMHAGKVLASGTPQEL 494
Cdd:PRK13645 181 LDPKGEEDFINLFERLNKEYKKRIIMVTHNMDQVLRiADEVIVMHEGKVISIGSPFEI 238
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
218-466 |
1.66e-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: 90.11 E-value: 1.66e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 218 LVAMNAGEILA--TGSAQQL-RAKTHSATLEQAFIALLPEAQRQAHKPVVIPPyhaeqEEIAIEAKDLTMRF-GKFVAVD 293
Cdd:TIGR02868 278 LLPLAAFEAFAalPAAAQQLtRVRAAAERIVEVLDAAGPVAEGSAPAAGAVGL-----GKPTLELRDLSAGYpGAPPVLD 352
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 294 HVNFRIPRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGQAWLFGQPVDPNDID-TRRRVGYMSQAFSLYNElTVRQNLEL 372
Cdd:TIGR02868 353 GVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPLQGEVTLDGVPVSSLDQDeVRRRVSVCAQDAHLFDT-TVRENLRL 431
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 373 hARlfhipPAEIPARVAQMIERFMLTEVEDTLP-----------ASLPLGIRQRLSLAVAVIHRPEMLILDEPTSGVDPV 441
Cdd:TIGR02868 432 -AR-----PDATDEELWAALERVGLADWLRALPdgldtvlgeggARLSGGERQRLALARALLADAPILLLDEPTEHLDAE 505
|
250 260
....*....|....*....|....*..
gi 446125071 442 ARDmfwQLMVDLSRQD--KVTIFISTH 466
Cdd:TIGR02868 506 TAD---ELLEDLLAALsgRTVVLITHH 529
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
295-497 |
1.86e-18 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 86.72 E-value: 1.86e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 295 VNFRIPRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGQAWLFGQPVDPN----DIDT-RRRVGYM-----SQAFslynEL 364
Cdd:PRK13649 26 VNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDDTLITSTsknkDIKQiRKKVGLVfqfpeSQLF----EE 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 365 TVRQNLELHARLFHIPP--AEIPARvaqmiERFMLTEVEDTL----PASLPLGIRQRLSLAVAVIHRPEMLILDEPTSGV 438
Cdd:PRK13649 102 TVLKDVAFGPQNFGVSQeeAEALAR-----EKLALVGISESLfeknPFELSGGQMRRVAIAGILAMEPKILVLDEPTAGL 176
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 439 DPVARDMFWQLMVDLsRQDKVTIFISTHFMNE-AERCDRMSLMHAGKVLASGTPQELVQQ 497
Cdd:PRK13649 177 DPKGRKELMTLFKKL-HQSGMTIVLVTHLMDDvANYADFVYVLEKGKLVLSGKPKDIFQD 235
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
277-466 |
1.88e-18 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 84.54 E-value: 1.88e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 277 IEAKDLTMRFGKFVAVDHVNFRIPRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGQAWLFGQPVDpnDIDTRRRVGYMSQ 356
Cdd:PRK13539 3 LEGEDLACVRGGRVLFSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDGGDID--DPDVAEACHYLGH 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 357 AFSLYNELTVRQNLELHARLFHIPPAEIPArvaqMIERFMLTEVEDTLPASLPLGIRQRLSLA-VAVIHRPeMLILDEPT 435
Cdd:PRK13539 81 RNAMKPALTVAENLEFWAAFLGGEELDIAA----ALEAVGLAPLAHLPFGYLSAGQKRRVALArLLVSNRP-IWILDEPT 155
|
170 180 190
....*....|....*....|....*....|.
gi 446125071 436 SGVDPVARDMFWQLMVDLSRQDKvTIFISTH 466
Cdd:PRK13539 156 AALDAAAVALFAELIRAHLAQGG-IVIAATH 185
|
|
| thiQ |
TIGR01277 |
thiamine ABC transporter, ATP-binding protein; This model describes the energy-transducing ... |
274-485 |
1.92e-18 |
|
thiamine ABC transporter, ATP-binding protein; This model describes the energy-transducing ATPase subunit ThiQ of the ThiBPQ thiamine (and thiamine pyrophosphate) ABC transporter in several Proteobacteria. This protein is found so far only in Proteobacteria, and is found in complete genomes only if the ThiB and ThiP subunits are also found. [Transport and binding proteins, Other]
Pssm-ID: 130344 [Multi-domain] Cd Length: 213 Bit Score: 84.91 E-value: 1.92e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 274 EIAIEAKDLTMRFgkfvavdhvNFRIPRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGQAWLFGQPVdPNDIDTRRRVGY 353
Cdd:TIGR01277 5 KVRYEYEHLPMEF---------DLNVADGEIVAIMGPSGAGKSTLLNLIAGFIEPASGSIKVNDQSH-TGLAPYQRPVSM 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 354 MSQAFSLYNELTVRQNLELHARLFHIPPAEIPARVAQMIERFMLTEVEDTLPASLPLGIRQRLSLAVAVIHRPEMLILDE 433
Cdd:TIGR01277 75 LFQENNLFAHLTVRQNIGLGLHPGLKLNAEQQEKVVDAAQQVGIADYLDRLPEQLSGGQRQRVALARCLVRPNPILLLDE 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 446125071 434 PTSGVDPVARDMFWQLMVDLSRQDKVTIFISTHFMNEAER-CDRMSLMHAGKV 485
Cdd:TIGR01277 155 PFSALDPLLREEMLALVKQLCSERQRTLLMVTHHLSDARAiASQIAVVSQGKI 207
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
295-484 |
2.41e-18 |
|
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This subfamily is also known as MRP (multidrug resistance-associated protein). Some of the MRP members have five additional transmembrane segments in their N-terminus, but the function of these additional membrane-spanning domains is not clear. The MRP was found in the multidrug-resisting lung cancer cell in which p-glycoprotein was not overexpressed. MRP exports glutathione by drug stimulation, as well as, certain substrates in conjugated forms with anions, such as glutathione, glucuronate, and sulfate.
Pssm-ID: 213217 [Multi-domain] Cd Length: 204 Bit Score: 84.44 E-value: 2.41e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 295 VNFRIPRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGQAWLFGqpvdpndidtrrRVGYMSQAFSLYNElTVRQNLelha 374
Cdd:cd03250 24 INLEVPKGELVAIVGPVGSGKSSLLSALLGELEKLSGSVSVPG------------SIAYVSQEPWIQNG-TIRENI---- 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 375 rLFHIPpaEIPARVAQMIERFMLTEVEDTLPA-----------SLPLGIRQRLSLAVAVIHRPEMLILDEPTSGVDP-VA 442
Cdd:cd03250 87 -LFGKP--FDEERYEKVIKACALEPDLEILPDgdlteigekgiNLSGGQKQRISLARAVYSDADIYLLDDPLSAVDAhVG 163
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 446125071 443 RDMFWQLMVDLSRQDKvTIFISTHFMNEAERCDRMSLMHAGK 484
Cdd:cd03250 164 RHIFENCILGLLLNNK-TRILVTHQLQLLPHADQIVVLDNGR 204
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
12-235 |
2.61e-18 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 85.83 E-value: 2.61e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 12 VAQLEGVSQHYGKTVALNNITLDIPARSMVGLIGPDGVGKSSLL----SLISGARVIEQ-----GNVIVLGGDM-RDAKH 81
Cdd:PRK09984 4 IIRVEKLAKTFNQHQALHAVDLNIHHGEMVALLGPSGSGKSTLLrhlsGLITGDKSAGShiellGRTVQREGRLaRDIRK 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 82 RRdvcPRIAWMPQGLgkNLYHTLSVYENV--------DFFARLFGHDKAEREARITELLNSTGLAPFRDRPAGKLSGGMK 153
Cdd:PRK09984 84 SR---ANTGYIFQQF--NLVNRLSVLENVligalgstPFWRTCFSWFTREQKQRALQALTRVGMVHFAHQRVSTLSGGQQ 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 154 QKLGLCCALIHDPELLILDEPTTGVDPLSRAQFWDLIDSIRQRQtNMSVLVATAYMEEAERF-DWLVAMNAGEILATGSA 232
Cdd:PRK09984 159 QRVAIARALMQQAKVILADEPIASLDPESARIVMDTLRDINQND-GITVVVTLHQVDYALRYcERIVALRQGHVFYDGSS 237
|
...
gi 446125071 233 QQL 235
Cdd:PRK09984 238 QQF 240
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
5-238 |
2.72e-18 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 89.50 E-value: 2.72e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 5 TLVPVPPVAQLEGVSQHY--GKTVALNNITLDIPARSMVGLIGPDGVGKSSLLSLISGARVIEQGNvIVLGGdmrdakhr 82
Cdd:PRK11160 331 TAAADQVSLTLNNVSFTYpdQPQPVLKGLSLQIKAGEKVALLGRTGCGKSTLLQLLTRAWDPQQGE-ILLNG-------- 401
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 83 rdvCPRIAWMPQglgkNLYHTLSVY-ENVDFFA---R---LFGHDKAeREARITELLNSTGLAPFRDRPAG--------- 146
Cdd:PRK11160 402 ---QPIADYSEA----ALRQAISVVsQRVHLFSatlRdnlLLAAPNA-SDEALIEVLQQVGLEKLLEDDKGlnawlgegg 473
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 147 -KLSGGMKQKLGLCCALIHDPELLILDEPTTGVDPLSRAQFWDLidsIRQRQTNMSVLVATAYMEEAERFDWLVAMNAGE 225
Cdd:PRK11160 474 rQLSGGEQRRLGIARALLHDAPLLLLDEPTEGLDAETERQILEL---LAEHAQNKTVLMITHRLTGLEQFDRICVMDNGQ 550
|
250
....*....|...
gi 446125071 226 ILATGSAQQLRAK 238
Cdd:PRK11160 551 IIEQGTHQELLAQ 563
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
277-485 |
4.39e-18 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 85.14 E-value: 4.39e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 277 IEAKDLTMRFGK-----FVAVDHVNFRIPRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGQAWLFGQPVdpndidTR--- 348
Cdd:COG1101 2 LELKNLSKTFNPgtvneKRALDGLNLTIEEGDFVTVIGSNGAGKSTLLNAIAGSLPPDSGSILIDGKDV------TKlpe 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 349 -RRVGYMSQAFSlyN-------ELTVRQNLELHAR---LFHIPPAEIPARVAQMIERFmltevedtlpASLPLGI----- 412
Cdd:COG1101 76 yKRAKYIGRVFQ--DpmmgtapSMTIEENLALAYRrgkRRGLRRGLTKKRRELFRELL----------ATLGLGLenrld 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 413 ----------RQRLSLAVAVIHRPEMLILDEPTSGVDPVARDMFWQLMVDLSRQDKVTIFISTHFMNEAERC-DRMSLMH 481
Cdd:COG1101 144 tkvgllsggqRQALSLLMATLTKPKLLLLDEHTAALDPKTAALVLELTEKIVEENNLTTLMVTHNMEQALDYgNRLIMMH 223
|
....
gi 446125071 482 AGKV 485
Cdd:COG1101 224 EGRI 227
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
11-248 |
4.48e-18 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 87.59 E-value: 4.48e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 11 PVAQLEGVSQHYGKTVALNNITLDIPARSMVGLIGPDGVGKSSLLSLISGARVIEQGNVIVlGGDMRDAKHRRDVCPRIA 90
Cdd:PRK09536 2 PMIDVSDLSVEFGDTTVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLV-AGDDVEALSARAASRRVA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 91 WMPQGlgKNLYHTLSVYENVDF-----FARLFGHDKAEREArITELLNSTGLAPFRDRPAGKLSGGMKQKLGLCCALIHD 165
Cdd:PRK09536 81 SVPQD--TSLSFEFDVRQVVEMgrtphRSRFDTWTETDRAA-VERAMERTGVAQFADRPVTSLSGGERQRVLLARALAQA 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 166 PELLILDEPTTGVDPLSRAQFWDLIDsiRQRQTNMSVLVATAYMEEAERF-DWLVAMNAGEILATGSAqqlRAKTHSATL 244
Cdd:PRK09536 158 TPVLLLDEPTASLDINHQVRTLELVR--RLVDDGKTAVAAIHDLDLAARYcDELVLLADGRVRAAGPP---ADVLTADTL 232
|
....
gi 446125071 245 EQAF 248
Cdd:PRK09536 233 RAAF 236
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
15-204 |
4.59e-18 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 84.78 E-value: 4.59e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 15 LEGVSQHYGKTVALNNITLDIPARSMVGLIGPDGVGKSSLLSLISGARVIEQGNVivlggdmrdakhRRDVCPRIAWMPQ 94
Cdd:PRK09544 7 LENVSVSFGQRRVLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVI------------KRNGKLRIGYVPQ 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 95 GLgkNLYHTLSVyeNVDFFARLfghDKAEREARITELLNSTGLAPFRDRPAGKLSGGMKQKLGLCCALIHDPELLILDEP 174
Cdd:PRK09544 75 KL--YLDTTLPL--TVNRFLRL---RPGTKKEDILPALKRVQAGHLIDAPMQKLSGGETQRVLLARALLNRPQLLVLDEP 147
|
170 180 190
....*....|....*....|....*....|
gi 446125071 175 TTGVDPLSRAQFWDLIDSIRqRQTNMSVLV 204
Cdd:PRK09544 148 TQGVDVNGQVALYDLIDQLR-RELDCAVLM 176
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
24-239 |
5.19e-18 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 85.24 E-value: 5.19e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 24 KTVALNNITLDIPARSMVGLIGPDGVGKSSLLSLISGARVIEQGN--VIVLGGDMRDAKHRRDVCPRIAWMPQGlGKNLY 101
Cdd:PRK13640 19 KKPALNDISFSIPRGSWTALIGHNGSGKSTISKLINGLLLPDDNPnsKITVDGITLTAKTVWDIREKVGIVFQN-PDNQF 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 102 HTLSVYENVDFFARLFGHDKAEREARITELLNSTGLAPFRDRPAGKLSGGMKQKLGLCCALIHDPELLILDEPTTGVDPL 181
Cdd:PRK13640 98 VGATVGDDVAFGLENRAVPRPEMIKIVRDVLADVGMLDYIDSEPANLSGGQKQRVAIAGILAVEPKIIILDESTSMLDPA 177
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 446125071 182 SRAQFWDLIDSIrQRQTNMSVLVATAYMEEAERFDWLVAMNAGEILATGSAQQLRAKT 239
Cdd:PRK13640 178 GKEQILKLIRKL-KKKNNLTVISITHDIDEANMADQVLVLDDGKLLAQGSPVEIFSKV 234
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
25-230 |
5.52e-18 |
|
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: 82.36 E-value: 5.52e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 25 TVALNNITLDIPARSMVGLIGPDGVGKSSLLSLISGARVIEQGNVIVLGGDmrdakhrrdvcpriawmPQGLGKNLYHTL 104
Cdd:cd03247 15 QQVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDGVP-----------------VSDLEKALSSLI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 105 SVyenVDFFARLFGhdkaereariTELLNSTGLapfrdrpagKLSGGMKQKLGLCCALIHDPELLILDEPTTGVDPLSRA 184
Cdd:cd03247 78 SV---LNQRPYLFD----------TTLRNNLGR---------RFSGGERQRLALARILLQDAPIVLLDEPTVGLDPITER 135
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 446125071 185 QfwdLIDSIRQRQTNMSVLVATAYMEEAERFDWLVAMNAGEILATG 230
Cdd:cd03247 136 Q---LLSLIFEVLKDKTLIWITHHLTGIEHMDKILFLENGKIIMQG 178
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
25-235 |
5.82e-18 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 85.13 E-value: 5.82e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 25 TVALNNITLDIPARSMVGLIGPDGVGKSSLLSLISGARVIEQGNVIVLGGDMR-DAKHRRDVCPRIAWMPQGLGKNLYHT 103
Cdd:PRK13639 15 TEALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIKGEPIKyDKKSLLEVRKTVGIVFQNPDDQLFAP 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 104 lSVYENVDFFARLFGHDKAEREARITELLNSTGLAPFRDRPAGKLSGGMKQKLGLCCALIHDPELLILDEPTTGVDPLSR 183
Cdd:PRK13639 95 -TVEEDVAFGPLNLGLSKEEVEKRVKEALKAVGMEGFENKPPHHLSGGQKKRVAIAGILAMKPEIIVLDEPTSGLDPMGA 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 446125071 184 AQFWDLIDSIRQRqtNMSVLVATAYMEEAERF-DWLVAMNAGEILATGSAQQL 235
Cdd:PRK13639 174 SQIMKLLYDLNKE--GITIIISTHDVDLVPVYaDKVYVMSDGKIIKEGTPKEV 224
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
11-175 |
5.92e-18 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 88.20 E-value: 5.92e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 11 PVAQLEGVSQHYGKTVALNNITLDIPARSMVGLIGPDGVGKSSLLSLISGARVIEQGNVivlggdmrdaKHRRDVcpRIA 90
Cdd:COG0488 314 KVLELEGLSKSYGDKTLLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPDSGTV----------KLGETV--KIG 381
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 91 WMPQGLgKNLYHTLSVYENVdffaRLFGHDKAEREARitELLNSTGLAPFR-DRPAGKLSGGMKQKLGLCCALIHDPELL 169
Cdd:COG0488 382 YFDQHQ-EELDPDKTVLDEL----RDGAPGGTEQEVR--GYLGRFLFSGDDaFKPVGVLSGGEKARLALAKLLLSPPNVL 454
|
....*.
gi 446125071 170 ILDEPT 175
Cdd:COG0488 455 LLDEPT 460
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
269-499 |
6.18e-18 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 88.34 E-value: 6.18e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 269 HAEQEEIAIEAKDLTMRF--GKFVAVDHVNFRIPRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGQAWLFGQPV-DPNDI 345
Cdd:PRK11160 331 TAAADQVSLTLNNVSFTYpdQPQPVLKGLSLQIKAGEKVALLGRTGCGKSTLLQLLTRAWDPQQGEILLNGQPIaDYSEA 410
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 346 DTRRRVGYMSQAFSLYNElTVRQNLELHArlfhipPAEIPARVAQMIERF---MLTEVEDTLPASLPLGIRQ-------R 415
Cdd:PRK11160 411 ALRQAISVVSQRVHLFSA-TLRDNLLLAA------PNASDEALIEVLQQVgleKLLEDDKGLNAWLGEGGRQlsggeqrR 483
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 416 LSLAVAVIHRPEMLILDEPTSGVDPVARDMFWQLMVDLSrQDKVTIFIsTHFMNEAERCDRMSLMHAGKVLASGTPQELV 495
Cdd:PRK11160 484 LGIARALLHDAPLLLLDEPTEGLDAETERQILELLAEHA-QNKTVLMI-THRLTGLEQFDRICVMDNGQIIEQGTHQELL 561
|
....
gi 446125071 496 QQRG 499
Cdd:PRK11160 562 AQQG 565
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
14-266 |
7.39e-18 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 84.65 E-value: 7.39e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 14 QLEGVSQHYGK-TVALNNITLDIPARSMVGLIGPDGVGKSSLLSLISGARVIEQGNVIVLG---GDMRDAKHRRDVCPRI 89
Cdd:PRK13644 3 RLENVSYSYPDgTPALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLVSGidtGDFSKLQGIRKLVGIV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 90 AWMP--QGLGKnlyhtlSVYENVDFFARLFGHDKAEREARITELLNSTGLAPFRDRPAGKLSGGMKQKLGLCCALIHDPE 167
Cdd:PRK13644 83 FQNPetQFVGR------TVEEDLAFGPENLCLPPIEIRKRVDRALAEIGLEKYRHRSPKTLSGGQGQCVALAGILTMEPE 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 168 LLILDEPTTGVDPLSRAQFWDLIDSIRQRqtNMSVLVATAYMEEAERFDWLVAMNAGEILATGSAQQLRAKTHSATLEQA 247
Cdd:PRK13644 157 CLIFDEVTSMLDPDSGIAVLERIKKLHEK--GKTIVYITHNLEELHDADRIIVMDRGKIVLEGEPENVLSDVSLQTLGLT 234
|
250
....*....|....*....
gi 446125071 248 FIALLPEAQRQAHKPVVIP 266
Cdd:PRK13644 235 PPSLIELAENLKMHGVVIP 253
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
292-496 |
7.45e-18 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 84.37 E-value: 7.45e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 292 VDHVNFRIPRGEIFGFLGSNGCGKSTTMKMLTGLLPA----SEGQAWLFGQPVDPNDIDTRRRVGYMSQAFSLYNELtvr 367
Cdd:PRK10418 19 VHGVSLTLQRGRVLALVGGSGSGKSLTCAAALGILPAgvrqTAGRVLLDGKPVAPCALRGRKIATIMQNPRSAFNPL--- 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 368 QNLELHARLfHIPPAEIPARVAQMIERFMLTEVEDTL------PASLPLGIRQRLSLAVAVIHRPEMLILDEPTSGVDPV 441
Cdd:PRK10418 96 HTMHTHARE-TCLALGKPADDATLTAALEAVGLENAArvlklyPFEMSGGMLQRMMIALALLCEAPFIIADEPTTDLDVV 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 446125071 442 ARDMFWQLMVDLSRQDKVTIFISTHFMNEAERC-DRMSLMHAGKVLASGTPQELVQ 496
Cdd:PRK10418 175 AQARILDLLESIVQKRALGMLLVTHDMGVVARLaDDVAVMSHGRIVEQGDVETLFN 230
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
28-239 |
8.24e-18 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 84.76 E-value: 8.24e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 28 LNNITLDIPARSMVGLIGPDGVGKSSLLSLISGARVIEQGnVIVLGGDMRDAKHRRDVCPRIAWMPQGlGKNLYHTLSVY 107
Cdd:PRK13642 23 LNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEG-KVKIDGELLTAENVWNLRRKIGMVFQN-PDNQFVGATVE 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 108 ENVDFFARLFGHDKAEREARITELLNSTGLAPFRDRPAGKLSGGMKQKLGLCCALIHDPELLILDEPTTGVDPLSRAQFW 187
Cdd:PRK13642 101 DDVAFGMENQGIPREEMIKRVDEALLAVNMLDFKTREPARLSGGQKQRVAVAGIIALRPEIIILDESTSMLDPTGRQEIM 180
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 446125071 188 DLIDSIRQRQtNMSVLVATAYMEEAERFDWLVAMNAGEILATGSAQQLRAKT 239
Cdd:PRK13642 181 RVIHEIKEKY-QLTVLSITHDLDEAASSDRILVMKAGEIIKEAAPSELFATS 231
|
|
| nickel_nikE |
TIGR02769 |
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a ... |
15-262 |
8.39e-18 |
|
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a multisubunit nickel import ABC transporter complex. Nickel, once imported, may be used in urease and in certain classes of hydrogenase and superoxide dismutase. [Transport and binding proteins, Cations and iron carrying compounds]
Pssm-ID: 131816 [Multi-domain] Cd Length: 265 Bit Score: 84.47 E-value: 8.39e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 15 LEGVSQHygKTVaLNNITLDIPARSMVGLIGPDGVGKSSLLSLISGARVIEQGNVIVLGGDMRDAKH------RRDV--- 85
Cdd:TIGR02769 17 LFGAKQR--APV-LTNVSLSIEEGETVGLLGRSGCGKSTLARLLLGLEKPAQGTVSFRGQDLYQLDRkqrrafRRDVqlv 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 86 ---CPRiAWMPQG-----LGKNLYHTLSVyenvdffarlfghDKAEREARITELLNSTGLAP--FRDRPAgKLSGGMKQK 155
Cdd:TIGR02769 94 fqdSPS-AVNPRMtvrqiIGEPLRHLTSL-------------DESEQKARIAELLDMVGLRSedADKLPR-QLSGGQLQR 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 156 LGLCCALIHDPELLILDEPTTGVDPLSRAQFWDLIDSIRQrQTNMSVLVATAYMEEAERF-DWLVAMNAGEILATGSAQQ 234
Cdd:TIGR02769 159 INIARALAVKPKLIVLDEAVSNLDMVLQAVILELLRKLQQ-AFGTAYLFITHDLRLVQSFcQRVAVMDKGQIVEECDVAQ 237
|
250 260
....*....|....*....|....*...
gi 446125071 235 LRAKTHSATlEQAFIALLPEAQRQAHKP 262
Cdd:TIGR02769 238 LLSFKHPAG-RNLQSAVLPEHPVRRSIT 264
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
274-494 |
9.42e-18 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 85.29 E-value: 9.42e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 274 EIAIEAKDLTMRFG-----KFVAVDHVNFRIPRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGQAWL--------FGQPV 340
Cdd:PRK13631 19 DIILRVKNLYCVFDekqenELVALNNISYTFEKNKIYFIIGNSGSGKSTLVTHFNGLIKSKYGTIQVgdiyigdkKNNHE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 341 DPNDIDT---------RRRVGYMSQ--AFSLYNElTVRQNLELHARLFHIPPAEIPARVAQMIERFMLTE-VEDTLPASL 408
Cdd:PRK13631 99 LITNPYSkkiknfkelRRRVSMVFQfpEYQLFKD-TIEKDIMFGPVALGVKKSEAKKLAKFYLNKMGLDDsYLERSPFGL 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 409 PLGIRQRLSLAVAVIHRPEMLILDEPTSGVDPVARDMFWQLMVDLSRQDKvTIFISTHFM-NEAERCDRMSLMHAGKVLA 487
Cdd:PRK13631 178 SGGQKRRVAIAGILAIQPEILIFDEPTAGLDPKGEHEMMQLILDAKANNK-TVFVITHTMeHVLEVADEVIVMDKGKILK 256
|
....*..
gi 446125071 488 SGTPQEL 494
Cdd:PRK13631 257 TGTPYEI 263
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
14-262 |
1.04e-17 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 83.97 E-value: 1.04e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 14 QLEGVSQHYG----------KTVaLNNITLDIPARSMVGLIGPDGVGKSSLLSLISGARVIEQGNVIVLGGDM----RDA 79
Cdd:PRK10419 5 NVSGLSHHYAhgglsgkhqhQTV-LNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWRGEPLaklnRAQ 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 80 KH--RRD-----------VCPR--IAWMpqgLGKNLYHTLSVyenvdffarlfghDKAEREARITELLNSTGLAP-FRDR 143
Cdd:PRK10419 84 RKafRRDiqmvfqdsisaVNPRktVREI---IREPLRHLLSL-------------DKAERLARASEMLRAVDLDDsVLDK 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 144 PAGKLSGGMKQKLGLCCALIHDPELLILDEPTTGVDPLSRAQFWDLIDSIRQrQTNMSVLVATAYMEEAERFDWLVA-MN 222
Cdd:PRK10419 148 RPPQLSGGQLQRVCLARALAVEPKLLILDEAVSNLDLVLQAGVIRLLKKLQQ-QFGTACLFITHDLRLVERFCQRVMvMD 226
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 446125071 223 AGEILATGSAQQLRAKTHSAT--LEQAFIALLPEAQRQAHKP 262
Cdd:PRK10419 227 NGQIVETQPVGDKLTFSSPAGrvLQNAVLPAFPVRRRTTEKV 268
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
11-235 |
1.05e-17 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 83.67 E-value: 1.05e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 11 PVAQLEGVSQHYGKTVALNNITLDIPARSMVGLIGPDGVGKSSLLSLIS-----GARVIEQGNVIVLGGDM----RDAKH 81
Cdd:PRK14239 4 PILQVSDLSVYYNKKKALNSVSLDFYPNEITALIGPSGSGKSTLLRSINrmndlNPEVTITGSIVYNGHNIysprTDTVD 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 82 RRDVCPRIAWMPQGLgknlyhTLSVYENVDFFARLFG-HDKAEREARITELLNSTGL-APFRDR---PAGKLSGGMKQKL 156
Cdd:PRK14239 84 LRKEIGMVFQQPNPF------PMSIYENVVYGLRLKGiKDKQVLDEAVEKSLKGASIwDEVKDRlhdSALGLSGGQQQRV 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 157 GLCCALIHDPELLILDEPTTGVDPLSRAQFWDLIDSIRQRQTnmsVLVATAYMEEAERF-DWLVAMNAGEILATGSAQQL 235
Cdd:PRK14239 158 CIARVLATSPKIILLDEPTSALDPISAGKIEETLLGLKDDYT---MLLVTRSMQQASRIsDRTGFFLDGDLIEYNDTKQM 234
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
277-450 |
1.07e-17 |
|
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: 82.41 E-value: 1.07e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 277 IEAKDLTMRFGKFVAVDHVNFRIPRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGQAWLFGQPVDPNDIDTRRRVGYMSQ 356
Cdd:TIGR01189 1 LAARNLACSRGERMLFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRWNGTPLAEQRDEPHENILYLGH 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 357 AFSLYNELTVRQNLELHARLFHIPPAEIPARVAQMierfMLTEVEDTLPASLPLGIRQRLSLAVAVIHRPEMLILDEPTS 436
Cdd:TIGR01189 81 LPGLKPELSALENLHFWAAIHGGAQRTIEDALAAV----GLTGFEDLPAAQLSAGQQRRLALARLWLSRRPLWILDEPTT 156
|
170
....*....|....
gi 446125071 437 GVDPVARDMFWQLM 450
Cdd:TIGR01189 157 ALDKAGVALLAGLL 170
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
277-499 |
1.16e-17 |
|
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide chain transporter in the ATP-binding cassette (ABC) transporter family, MsbA, which exports lipid A. It may also act in multidrug resistance. Lipid A, a part of lipopolysaccharide, is found in the outer leaflet of the outer membrane of most Gram-negative bacteria. Members of this family are restricted to the Proteobacteria (although lipid A is more broadly distributed) and often are clustered with lipid A biosynthesis genes. [Cell envelope, Biosynthesis and degradation of surface polysaccharides and lipopolysaccharides, Transport and binding proteins, Other]
Pssm-ID: 131258 [Multi-domain] Cd Length: 571 Bit Score: 87.46 E-value: 1.16e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 277 IEAKDLTMRFG--KFVAVDHVNFRIPRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGQAWLFGQPV-DPNDIDTRRRVGY 353
Cdd:TIGR02203 331 VEFRNVTFRYPgrDRPALDSISLVIEPGETVALVGRSGSGKSTLVNLIPRFYEPDSGQILLDGHDLaDYTLASLRRQVAL 410
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 354 MSQAFSLYNElTVRQNLElHARLFHIPPAEIpARVAQMIErfmLTEVEDTLP-----------ASLPLGIRQRLSLAVAV 422
Cdd:TIGR02203 411 VSQDVVLFND-TIANNIA-YGRTEQADRAEI-ERALAAAY---AQDFVDKLPlgldtpigengVLLSGGQRQRLAIARAL 484
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446125071 423 IHRPEMLILDEPTSGVDPVARDMFwQLMVDLSRQDKVTIFIStHFMNEAERCDRMSLMHAGKVLASGTPQELVQQRG 499
Cdd:TIGR02203 485 LKDAPILILDEATSALDNESERLV-QAALERLMQGRTTLVIA-HRLSTIEKADRIVVMDDGRIVERGTHNELLARNG 559
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
302-496 |
1.38e-17 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 87.41 E-value: 1.38e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 302 GEIFGFLGSNGCGKSTTMKMLTGLLPA-SEGQAW--LFGQPVDPNDIdtRRRVGYMSQAFSLYNELTVRQNLELHARLF- 377
Cdd:TIGR00955 51 GELLAVMGSSGAGKTTLMNALAFRSPKgVKGSGSvlLNGMPIDAKEM--RAISAYVQQDDLFIPTLTVREHLMFQAHLRm 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 378 --HIPPAEIPARVAQMIERFMLTEVEDTL------PASLPLGIRQRLSLAVAVIHRPEMLILDEPTSGVDPVARDMFWQL 449
Cdd:TIGR00955 129 prRVTKKEKRERVDEVLQALGLRKCANTRigvpgrVKGLSGGERKRLAFASELLTDPPLLFCDEPTSGLDSFMAYSVVQV 208
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 446125071 450 MVDLSRQDKvTIFISTH------FmneaERCDRMSLMHAGKVLASGTPQELVQ 496
Cdd:TIGR00955 209 LKGLAQKGK-TIICTIHqpsselF----ELFDKIILMAEGRVAYLGSPDQAVP 256
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
15-238 |
1.64e-17 |
|
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: 82.92 E-value: 1.64e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 15 LEGVSQHYG--KTVALNNITLDIPARSMVGLIGPDGVGKSSLLSLISGARVIEQGNVIVLGGDMRDAKhrrdvcprIAWM 92
Cdd:cd03252 3 FEHVRFRYKpdGPVILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGHDLALAD--------PAWL 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 93 PQGLG----KNLYHTLSVYENVDFfarlfgHDKAEREARITELLNSTGLAPF-RDRPAG----------KLSGGMKQKLG 157
Cdd:cd03252 75 RRQVGvvlqENVLFNRSIRDNIAL------ADPGMSMERVIEAAKLAGAHDFiSELPEGydtivgeqgaGLSGGQRQRIA 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 158 LCCALIHDPELLILDEPTTGVDPLSRAqfwDLIDSIRQRQTNMSVLVATAYMEEAERFDWLVAMNAGEILATGSAQQLRA 237
Cdd:cd03252 149 IARALIHNPRILIFDEATSALDYESEH---AIMRNMHDICAGRTVIIIAHRLSTVKNADRIIVMEKGRIVEQGSHDELLA 225
|
.
gi 446125071 238 K 238
Cdd:cd03252 226 E 226
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
277-450 |
2.14e-17 |
|
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the bacterial CcmAB transporter. The CCM family is involved in bacterial cytochrome c biogenesis. Cytochrome c maturation in E. coli requires the ccm operon, which encodes eight membrane proteins (CcmABCDEFGH). CcmE is a periplasmic heme chaperon that binds heme covalently and transfers it onto apocytochrome c in the presence of CcmF, CcmG, and CcmH. The CcmAB proteins represent an ABC transporter and the CcmCD proteins participate in heme transfer to CcmE.
Pssm-ID: 213198 [Multi-domain] Cd Length: 201 Bit Score: 81.39 E-value: 2.14e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 277 IEAKDLTMRFGKFVAVDHVNFRIPRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGQAWLFGQPVDPNDIDTRRRVGYMSQ 356
Cdd:cd03231 1 LEADELTCERDGRALFSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNGGPLDFQRDSIARGLLYLGH 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 357 AFSLYNELTVRQNLelhaRLFHipPAEIPARVAQMIERFMLTEVEDTLPASLPLGIRQRLSLAVAVIHRPEMLILDEPTS 436
Cdd:cd03231 81 APGIKTTLSVLENL----RFWH--ADHSDEQVEEALARVGLNGFEDRPVAQLSAGQQRRVALARLLLSGRPLWILDEPTT 154
|
170
....*....|....
gi 446125071 437 GVDPVARDMFWQLM 450
Cdd:cd03231 155 ALDKAGVARFAEAM 168
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
290-507 |
2.28e-17 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 82.67 E-value: 2.28e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 290 VAVDH----VNFRIPRGEIFGFLGSNGCGKSTTMKMLTGLLPaSEGQAWLFGQPV---DPNDIDTRRrvGYMSQAFSLYN 362
Cdd:PRK03695 6 VAVSTrlgpLSAEVRAGEILHLVGPNGAGKSTLLARMAGLLP-GSGSIQFAGQPLeawSAAELARHR--AYLSQQQTPPF 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 363 ELTVRQNLELHaRLFHIPPAEIPARVAQMIERFMLTeveDTLPAS---LPLGIRQRLSLAVAV--IHR---PE--MLILD 432
Cdd:PRK03695 83 AMPVFQYLTLH-QPDKTRTEAVASALNEVAEALGLD---DKLGRSvnqLSGGEWQRVRLAAVVlqVWPdinPAgqLLLLD 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446125071 433 EPTSGVDPVARDMFWQLMVDLSRQDkVTIFISTHFMNE-AERCDRMSLMHAGKVLASGTPQELVQQRgaaNLEAAF 507
Cdd:PRK03695 159 EPMNSLDVAQQAALDRLLSELCQQG-IAVVMSSHDLNHtLRHADRVWLLKQGKLLASGRRDEVLTPE---NLAQVF 230
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
277-493 |
2.66e-17 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 83.60 E-value: 2.66e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 277 IEAKDLTMRFGK-----FVAVDHVNFRIPRGEIFGFLGSNGCGKSTTMKMLTGLLPASEG-------------QAWLFGQ 338
Cdd:PRK13651 3 IKVKNIVKIFNKklpteLKALDNVSVEINQGEFIAIIGQTGSGKTTFIEHLNALLLPDTGtiewifkdeknkkKTKEKEK 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 339 PVDPNDI------------DTRRRVGYMSQaFSLYN--ELTVRQNLELHARLFHIPPAEIPARVAQMIErfMLTEVEDTL 404
Cdd:PRK13651 83 VLEKLVIqktrfkkikkikEIRRRVGVVFQ-FAEYQlfEQTIEKDIIFGPVSMGVSKEEAKKRAAKYIE--LVGLDESYL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 405 PAS---LPLGIRQRLSLAVAVIHRPEMLILDEPTSGVDPVARDMFWQLMVDLSRQDKvTIFISTHFMNEA-ERCDRMSLM 480
Cdd:PRK13651 160 QRSpfeLSGGQKRRVALAGILAMEPDFLVFDEPTAGLDPQGVKEILEIFDNLNKQGK-TIILVTHDLDNVlEWTKRTIFF 238
|
250
....*....|...
gi 446125071 481 HAGKVLASGTPQE 493
Cdd:PRK13651 239 KDGKIIKDGDTYD 251
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
291-497 |
3.04e-17 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 83.24 E-value: 3.04e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 291 AVDHVNFRIPRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGQAWLFGQPVDPNDID-----TRRRVGYMSQ--AFSLYNE 363
Cdd:PRK13643 21 ALFDIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVTVGDIVVSSTSKQkeikpVRKKVGVVFQfpESQLFEE 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 364 lTVRQNLELHARLFHIPPAEIPARVAQMIERFMLT-EVEDTLPASLPLGIRQRLSLAVAVIHRPEMLILDEPTSGVDPVA 442
Cdd:PRK13643 101 -TVLKDVAFGPQNFGIPKEKAEKIAAEKLEMVGLAdEFWEKSPFELSGGQMRRVAIAGILAMEPEVLVLDEPTAGLDPKA 179
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 446125071 443 RDMFWQLMVDLsRQDKVTIFISTHFMNE-AERCDRMSLMHAGKVLASGTPQELVQQ 497
Cdd:PRK13643 180 RIEMMQLFESI-HQSGQTVVLVTHLMDDvADYADYVYLLEKGHIISCGTPSDVFQE 234
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
277-484 |
3.52e-17 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 85.79 E-value: 3.52e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 277 IEAKDLTMRFGK--FvAVDHVNFRIPRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGQAWLFGQPVDPNDIDTRRRVgyM 354
Cdd:PRK10522 323 LELRNVTFAYQDngF-SVGPINLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKPVTAEQPEDYRKL--F 399
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 355 SQAFS---LYNELTVRQNLelharlfhipPAEiPARVAQMIERFML---TEVEDTLPASLPL--GIRQRLSLAVAVIHRP 426
Cdd:PRK10522 400 SAVFTdfhLFDQLLGPEGK----------PAN-PALVEKWLERLKMahkLELEDGRISNLKLskGQKKRLALLLALAEER 468
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 446125071 427 EMLILDEPTSGVDPVARDMFWQLMVDLSRQDKVTIFISTHFMNEAERCDRMSLMHAGK 484
Cdd:PRK10522 469 DILLLDEWAADQDPHFRREFYQVLLPLLQEMGKTIFAISHDDHYFIHADRLLEMRNGQ 526
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
14-238 |
3.98e-17 |
|
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan exporter ATP-binding protein. In A. tumefaciens cyclic beta-1, 2-glucan must be transported into the periplasmic space to exert its action as a virulence factor. This subfamily belongs to the MRP-like family and is involved in drug, peptide, and lipid export. The MRP-like family, similar to all ABC proteins, have a common four-domain core structure constituted by two membrane-spanning domains each composed of six transmembrane (TM) helices and two nucleotide-binding domains (NBD). ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213221 [Multi-domain] Cd Length: 229 Bit Score: 81.50 E-value: 3.98e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 14 QLEGVSQHYGKTV-ALNNITLDIPARSMVGLIGPDGVGKSSLLSLISGARVIEQGNVIVLGGDMRDAKH---RRdvcpRI 89
Cdd:cd03254 4 EFENVNFSYDEKKpVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGIDIRDISRkslRS----MI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 90 AWMPQGLGknLYHTlSVYENVDffarlFGHDKAEREaRITELLNSTGLAPFRDR----------PAGK-LSGGMKQKLGL 158
Cdd:cd03254 80 GVVLQDTF--LFSG-TIMENIR-----LGRPNATDE-EVIEAAKEAGAHDFIMKlpngydtvlgENGGnLSQGERQLLAI 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 159 CCALIHDPELLILDEPTTGVDPLSRAQFWDLIDSIRQRQTnmSVLVA--TAYMEEAerfDWLVAMNAGEILATGSAQQLR 236
Cdd:cd03254 151 ARAMLRDPKILILDEATSNIDTETEKLIQEALEKLMKGRT--SIIIAhrLSTIKNA---DKILVLDDGKIIEEGTHDELL 225
|
..
gi 446125071 237 AK 238
Cdd:cd03254 226 AK 227
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
288-497 |
5.31e-17 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 82.52 E-value: 5.31e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 288 KFVAVDHVNFRIPRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGQawlfgqpVDPNDID------------TRRRVGYM- 354
Cdd:PRK13646 19 EHQAIHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGT-------VTVDDITithktkdkyirpVRKRIGMVf 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 355 ----SQAFslynELTVRQNLELHARLFHIPPAEIPARVAQMIERFMLT-EVEDTLPASLPLGIRQRLSLAVAVIHRPEML 429
Cdd:PRK13646 92 qfpeSQLF----EDTVEREIIFGPKNFKMNLDEVKNYAHRLLMDLGFSrDVMSQSPFQMSGGQMRKIAIVSILAMNPDII 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446125071 430 ILDEPTSGVDPVARDMFWQLMVDLSRQDKVTIFISTHFMNE-AERCDRMSLMHAGKVLASGTPQELVQQ 497
Cdd:PRK13646 168 VLDEPTAGLDPQSKRQVMRLLKSLQTDENKTIILVSHDMNEvARYADEVIVMKEGSIVSQTSPKELFKD 236
|
|
| type_I_sec_PrtD |
TIGR01842 |
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in ... |
274-497 |
5.61e-17 |
|
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: 85.09 E-value: 5.61e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 274 EIAIEAKDLTMRFGKFVAVDHVNFRIPRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGQAWLFGQPVDPNDIDT-RRRVG 352
Cdd:TIGR01842 316 HLSVENVTIVPPGGKKPTLRGISFSLQAGEALAIIGPSGSGKSTLARLIVGIWPPTSGSVRLDGADLKQWDRETfGKHIG 395
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 353 YMSQAFSLYnELTVRQNLelhARLFHIPPAE---IPARVAQ---MIERFMLTEVEDTLPASLPL--GIRQRLSLAVAVIH 424
Cdd:TIGR01842 396 YLPQDVELF-PGTVAENI---ARFGENADPEkiiEAAKLAGvheLILRLPDGYDTVIGPGGATLsgGQRQRIALARALYG 471
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446125071 425 RPEMLILDEPTSGVDPVARDMFWQLMVDLSRQDKVTIFIsTHFMNEAERCDRMSLMHAGKVLASGTPQELVQQ 497
Cdd:TIGR01842 472 DPKLVVLDEPNSNLDEEGEQALANAIKALKARGITVVVI-THRPSLLGCVDKILVLQDGRIARFGERDEVLAK 543
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
23-186 |
6.07e-17 |
|
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the bacterial CcmAB transporter. The CCM family is involved in bacterial cytochrome c biogenesis. Cytochrome c maturation in E. coli requires the ccm operon, which encodes eight membrane proteins (CcmABCDEFGH). CcmE is a periplasmic heme chaperon that binds heme covalently and transfers it onto apocytochrome c in the presence of CcmF, CcmG, and CcmH. The CcmAB proteins represent an ABC transporter and the CcmCD proteins participate in heme transfer to CcmE.
Pssm-ID: 213198 [Multi-domain] Cd Length: 201 Bit Score: 80.23 E-value: 6.07e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 23 GKTVALNNITLDIPARSMVGLIGPDGVGKSSLLSLISGARVIEQGNVIVLGGDmrDAKHRRDVCPRIAWMPQGLGknLYH 102
Cdd:cd03231 11 DGRALFSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNGGP--LDFQRDSIARGLLYLGHAPG--IKT 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 103 TLSVYENVDFFARLFGHDKAErearitELLNSTGLAPFRDRPAGKLSGGMKQKLGLCCALIHDPELLILDEPTTGVDPLS 182
Cdd:cd03231 87 TLSVLENLRFWHADHSDEQVE------EALARVGLNGFEDRPVAQLSAGQQRRVALARLLLSGRPLWILDEPTTALDKAG 160
|
....
gi 446125071 183 RAQF 186
Cdd:cd03231 161 VARF 164
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
28-212 |
6.49e-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: 80.97 E-value: 6.49e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 28 LNNITLDIPARSMVGLIGPDGVGKSSLLSLISGARVIEQGNVIVLGGDM-RDAKHRRDVCPRIAWMPQglgknlyhtLSV 106
Cdd:TIGR01184 1 LKGVNLTIQQGEFISLIGHSGCGKSTLLNLISGLAQPTSGGVILEGKQItEPGPDRMVVFQNYSLLPW---------LTV 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 107 YENVDFFARLFGHD--KAEREARITELLNSTGLAPFRDRPAGKLSGGMKQKLGLCCALIHDPELLILDEPTTGVDPLSRA 184
Cdd:TIGR01184 72 RENIALAVDRVLPDlsKSERRAIVEEHIALVGLTEAADKRPGQLSGGMKQRVAIARALSIRPKVLLLDEPFGALDALTRG 151
|
170 180
....*....|....*....|....*...
gi 446125071 185 QFWDLIDSIRQrQTNMSVLVATAYMEEA 212
Cdd:TIGR01184 152 NLQEELMQIWE-EHRVTVLMVTHDVDEA 178
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
287-508 |
8.02e-17 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 82.97 E-value: 8.02e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 287 GKFVAVDHVNFRIPRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGQAWLFGQPVdpNDIDTRRRVGYMS-QAFSLYNELT 365
Cdd:PRK11650 15 GKTQVIKGIDLDVADGEFIVLVGPSGCGKSTLLRMVAGLERITSGEIWIGGRVV--NELEPADRDIAMVfQNYALYPHMS 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 366 VRQNLELHARLFHIPPAEIPARV---AQMIErfmLTEVEDTLPASLPLGIRQRLSLAVAVIHRPEMLILDEPTSGVDPVA 442
Cdd:PRK11650 93 VRENMAYGLKIRGMPKAEIEERVaeaARILE---LEPLLDRKPRELSGGQRQRVAMGRAIVREPAVFLFDEPLSNLDAKL 169
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446125071 443 R-DMFWQLMvDLSRQDKVTIFISTHFMNEA-ERCDRMSLMHAGKVLASGTPQElVQQRGAANLEAAFI 508
Cdd:PRK11650 170 RvQMRLEIQ-RLHRRLKTTSLYVTHDQVEAmTLADRVVVMNGGVAEQIGTPVE-VYEKPASTFVASFI 235
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
11-231 |
1.19e-16 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 81.19 E-value: 1.19e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 11 PVAQLEGVSQHYG--KTVALNNITLDIPARSMVGLIGPDGVGKSSLLSLISGARVIEQGNVIVLGGDMRDA--KHRRDVC 86
Cdd:PRK13632 6 VMIKVENVSFSYPnsENNALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIDGITISKEnlKEIRKKI 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 87 PRIAWMPQglgkNLYHTLSVYENVDFFARLFGHDKAEREARITELLNSTGLAPFRDRPAGKLSGGMKQKLGLCCALIHDP 166
Cdd:PRK13632 86 GIIFQNPD----NQFIGATVEDDIAFGLENKKVPPKKMKDIIDDLAKKVGMEDYLDKEPQNLSGGQKQRVAIASVLALNP 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446125071 167 ELLILDEPTTGVDPLSRAQFWDLIDSIRQrQTNMSVLVATAYMEEAERFDWLVAMNAGEILATGS 231
Cdd:PRK13632 162 EIIIFDESTSMLDPKGKREIKKIMVDLRK-TRKKTLISITHDMDEAILADKVIVFSEGKLIAQGK 225
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
277-494 |
1.43e-16 |
|
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 443332 [Multi-domain] Cd Length: 533 Bit Score: 83.97 E-value: 1.43e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 277 IEAKDLTMRFGK----FVAVDHVNFRIPRGEIFGFLGSNGCGKSTTMKMLTGLLPAS----EGQAWLFGQPVDPNDIDTR 348
Cdd:COG4172 7 LSVEDLSVAFGQgggtVEAVKGVSFDIAAGETLALVGESGSGKSVTALSILRLLPDPaahpSGSILFDGQDLLGLSEREL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 349 RRV--GYMSQAF-----SLyNEL-TV-RQ---NLELHARLfhiPPAEIPARVAQMIERFMLTEVEDTL---PASLPLGIR 413
Cdd:COG4172 87 RRIrgNRIAMIFqepmtSL-NPLhTIgKQiaeVLRLHRGL---SGAAARARALELLERVGIPDPERRLdayPHQLSGGQR 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 414 QRLSLAVAVIHRPEMLILDEPTSGVDPVARDMFWQLMVDLSRQDKVTI-FIsTHFMNEAER-CDRMSLMHAGKVLASGTP 491
Cdd:COG4172 163 QRVMIAMALANEPDLLIADEPTTALDVTVQAQILDLLKDLQRELGMALlLI-THDLGVVRRfADRVAVMRQGEIVEQGPT 241
|
...
gi 446125071 492 QEL 494
Cdd:COG4172 242 AEL 244
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
14-229 |
1.64e-16 |
|
First domain of the ATP-binding cassette component of monosaccharide transport system; This family represents the domain I of the carbohydrate uptake proteins that transport only monosaccharides (Monos). The Carb_Monos family is involved in the uptake of monosaccharides, such as pentoses (such as xylose, arabinose, and ribose) and hexoses (such as xylose, arabinose, and ribose), that cannot be broken down to simple sugars by hydrolysis. Pentoses include xylose, arabinose, and ribose. Important hexoses include glucose, galactose, and fructose. In members of the Carb_monos family, the single hydrophobic gene product forms a homodimer while the ABC protein represents a fusion of two nucleotide-binding domains. However, it is assumed that two copies of the ABC domains are present in the assembled transporter.
Pssm-ID: 213183 [Multi-domain] Cd Length: 163 Bit Score: 77.85 E-value: 1.64e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 14 QLEGVSQHYGKTVALNNITLDIPARSMVGLIGPDGVGKSSLLSLISGARVIEQGNVIVLGgdmrdakhrrdvcpriawmp 93
Cdd:cd03216 2 ELRGITKRFGGVKALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVDG-------------------- 61
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 94 qglgknlyhtlsvyENVDFfarlfghdkaerearitellnstgLAPFRDRPAG-----KLSGGMKQKLGLCCALIHDPEL 168
Cdd:cd03216 62 --------------KEVSF------------------------ASPRDARRAGiamvyQLSVGERQMVEIARALARNARL 103
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446125071 169 LILDEPTTGVDPLSRAQFWDLIDSIRQRqtNMSVLVATAYMEEAERF-DWLVAMNAGEILAT 229
Cdd:cd03216 104 LILDEPTAALTPAEVERLFKVIRRLRAQ--GVAVIFISHRLDEVFEIaDRVTVLRDGRVVGT 163
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
270-494 |
1.72e-16 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 81.68 E-value: 1.72e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 270 AEQEEIAIEAKDLTMRFG-------------KFVAVDHVNFRIPRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGQ-AWL 335
Cdd:PRK15079 2 TEGKKVLLEVADLKVHFDikdgkqwfwqppkTLKAVDGVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGEvAWL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 336 FGQPVDPNDIDTRRRVGYMSQAF-----SLYNELTVRQNLELHARLFH--IPPAEIPARVAQMIERF-MLTEVEDTLPAS 407
Cdd:PRK15079 82 GKDLLGMKDDEWRAVRSDIQMIFqdplaSLNPRMTIGEIIAEPLRTYHpkLSRQEVKDRVKAMMLKVgLLPNLINRYPHE 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 408 LPLGIRQRLSLAVAVIHRPEMLILDEPTSGVDPVARDMFWQLMVDLSRQDKVT-IFISTHFMNEAERCDRMSLMHAGKVL 486
Cdd:PRK15079 162 FSGGQCQRIGIARALILEPKLIICDEPVSALDVSIQAQVVNLLQQLQREMGLSlIFIAHDLAVVKHISDRVLVMYLGHAV 241
|
....*...
gi 446125071 487 ASGTPQEL 494
Cdd:PRK15079 242 ELGTYDEV 249
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
15-485 |
2.48e-16 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 82.85 E-value: 2.48e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 15 LEGVSQHYGKTVALNNITLDIPARSMVGLIGPDGVGKSSLLSLISGARVIEQGNVIVLGG--DMRDAKHRRDvcPRIAWM 92
Cdd:PRK10982 1 MSNISKSFPGVKALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKeiDFKSSKEALE--NGISMV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 93 PQGLgkNLYHTLSVYENVdFFAR-----LF-GHDKAEREAR-ITELLNsTGLAPfRDRPAgKLSGGMKQKLGLCCALIHD 165
Cdd:PRK10982 79 HQEL--NLVLQRSVMDNM-WLGRyptkgMFvDQDKMYRDTKaIFDELD-IDIDP-RAKVA-TLSVSQMQMIEIAKAFSYN 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 166 PELLILDEPTTGVDPLSRAQFWDLIDSIRQRqtNMSVLVATAYMEEAERF-DWLVAMNAGEILATGSAQQLrakthsaTL 244
Cdd:PRK10982 153 AKIVIMDEPTSSLTEKEVNHLFTIIRKLKER--GCGIVYISHKMEEIFQLcDEITILRDGQWIATQPLAGL-------TM 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 245 EQaFIALL---PEAQRqahkpvvIPPYHAEQEEIAIEAKDLTMRfgKFVAVDHVNFRIPRGEIFGFLGSNGCGKSTTMKM 321
Cdd:PRK10982 224 DK-IIAMMvgrSLTQR-------FPDKENKPGEVILEVRNLTSL--RQPSIRDVSFDLHKGEILGIAGLVGAKRTDIVET 293
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 322 LTGLLPASEGQAWLFGQpvdpnDIDTRRRVGYMSQAFSLYNEltVRQNLELHARLfHIPPAEIPARVAQMIERFML---- 397
Cdd:PRK10982 294 LFGIREKSAGTITLHGK-----KINNHNANEAINHGFALVTE--ERRSTGIYAYL-DIGFNSLISNIRNYKNKVGLldns 365
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 398 ----------------TEVEDTLPASLPLGIRQRLSLAVAVIHRPEMLILDEPTSGVDPVARDMFWQLMVDLSRQDKVTI 461
Cdd:PRK10982 366 rmksdtqwvidsmrvkTPGHRTQIGSLSGGNQQKVIIGRWLLTQPEILMLDEPTRGIDVGAKFEIYQLIAELAKKDKGII 445
|
490 500
....*....|....*....|....
gi 446125071 462 FISTHFMNEAERCDRMSLMHAGKV 485
Cdd:PRK10982 446 IISSEMPELLGITDRILVMSNGLV 469
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
277-484 |
2.88e-16 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 78.99 E-value: 2.88e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 277 IEAKDLTMRFGKFVAVDHVNFRIPRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGQAWLFGQPVDPNDIDT-RRRVGYMS 355
Cdd:PRK10247 8 LQLQNVGYLAGDAKILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFEGEDISTLKPEIyRQQVSYCA 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 356 QAFSLYNElTVRQNLELHARLFHIPPAeiPARVAQMIERFMLTEVEDTLP-ASLPLGIRQRLSLAVAVIHRPEMLILDEP 434
Cdd:PRK10247 88 QTPTLFGD-TVYDNLIFPWQIRNQQPD--PAIFLDDLERFALPDTILTKNiAELSGGEKQRISLIRNLQFMPKVLLLDEI 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 446125071 435 TSGVDPVARDMFWQLMVDLSRQDKVTIFISTHFMNEAERCDRMSLM--HAGK 484
Cdd:PRK10247 165 TSALDESNKHNVNEIIHRYVREQNIAVLWVTHDKDEINHADKVITLqpHAGE 216
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
14-234 |
3.00e-16 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 78.29 E-value: 3.00e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 14 QLEGVSQHYGKTVALNNITLDIPARSMVGLIGPDGVGKSSLLSLISGA---RVIEQGNVIVLGGDMRD-AKHRRdvcpRI 89
Cdd:COG4136 3 SLENLTITLGGRPLLAPLSLTVAPGEILTLMGPSGSGKSTLLAAIAGTlspAFSASGEVLLNGRRLTAlPAEQR----RI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 90 AWMPQ-GLgknLYHTLSVYENVdffarLFG----HDKAEREARITELLNSTGLAPFRDRPAGKLSGGMKQKLGLCCALIH 164
Cdd:COG4136 79 GILFQdDL---LFPHLSVGENL-----AFAlpptIGRAQRRARVEQALEEAGLAGFADRDPATLSGGQRARVALLRALLA 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446125071 165 DPELLILDEPTTGVDPLSRAQFWDLI-DSIRQRqtNMSVLVATAYMEEAErfdwlvamNAGEILATGSAQQ 234
Cdd:COG4136 151 EPRALLLDEPFSKLDAALRAQFREFVfEQIRQR--GIPALLVTHDEEDAP--------AAGRVLDLGNWQH 211
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
295-494 |
3.01e-16 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 79.71 E-value: 3.01e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 295 VNFRIPRGEIFGFLGSNGCGKSTTMKMLTGLLP------ASEGQAWLFGQPVDPND-IDTRRRVGYMSQAFSLYNELTVR 367
Cdd:PRK14246 29 ITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLIEiydskiKVDGKVLYFGKDIFQIDaIKLRKEVGMVFQQPNPFPHLSIY 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 368 QNLELHARLFHIPPA-EIPARVAQMIERFML-TEVEDTL--PAS-LPLGIRQRLSLAVAVIHRPEMLILDEPTSGVDPVA 442
Cdd:PRK14246 109 DNIAYPLKSHGIKEKrEIKKIVEECLRKVGLwKEVYDRLnsPASqLSGGQQQRLTIARALALKPKVLLMDEPTSMIDIVN 188
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 446125071 443 RDMFWQLMVDLSRQdkVTIFISTHFMNEAER-CDRMSLMHAGKVLASGTPQEL 494
Cdd:PRK14246 189 SQAIEKLITELKNE--IAIVIVSHNPQQVARvADYVAFLYNGELVEWGSSNEI 239
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
20-248 |
3.12e-16 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 79.83 E-value: 3.12e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 20 QHYGKTVALNNITLDIPARSMV-------------GLIGPDGVGKSSLLSLISGARVIEQGNvIVLGGDMRDAKHRRDVC 86
Cdd:PRK10575 6 NHSDTTFALRNVSFRVPGRTLLhplsltfpagkvtGLIGHNGSGKSTLLKMLGRHQPPSEGE-ILLDAQPLESWSSKAFA 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 87 PRIAWMPQGLGKNlyHTLSVYENVDF----FARLFGHDKAEREARITELLNSTGLAPFRDRPAGKLSGGMKQKLGLCCAL 162
Cdd:PRK10575 85 RKVAYLPQQLPAA--EGMTVRELVAIgrypWHGALGRFGAADREKVEEAISLVGLKPLAHRLVDSLSGGERQRAWIAMLV 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 163 IHDPELLILDEPTTGVDPLSRAQFWDLIDSIRQrQTNMSVLVATAYMEEAERF-DWLVAMNAGEILATGSAQQLrakTHS 241
Cdd:PRK10575 163 AQDSRCLLLDEPTSALDIAHQVDVLALVHRLSQ-ERGLTVIAVLHDINMAARYcDYLVALRGGEMIAQGTPAEL---MRG 238
|
....*..
gi 446125071 242 ATLEQAF 248
Cdd:PRK10575 239 ETLEQIY 245
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
26-226 |
3.49e-16 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 79.36 E-value: 3.49e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 26 VALNNITLDIPARSMVGLIGPDGVGKSSLLSLISGARVIEQGNVIVLGGDM-RDAKHRR---------D----VCPRiaw 91
Cdd:COG1101 20 RALDGLNLTIEEGDFVTVIGSNGAGKSTLLNAIAGSLPPDSGSILIDGKDVtKLPEYKRakyigrvfqDpmmgTAPS--- 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 92 mpqglgknlyhtLSVYENVDFFAR-------LFGHDKAEREaRITELLNSTGLApFRDR---PAGKLSGGMKQKLGLCCA 161
Cdd:COG1101 97 ------------MTIEENLALAYRrgkrrglRRGLTKKRRE-LFRELLATLGLG-LENRldtKVGLLSGGQRQALSLLMA 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446125071 162 LIHDPELLILDEPTTGVDPLSRAQFWDLIDSIRQRQtNMSVLVATAYMEEAERF-DWLVAMNAGEI 226
Cdd:COG1101 163 TLTKPKLLLLDEHTAALDPKTAALVLELTEKIVEEN-NLTTLMVTHNMEQALDYgNRLIMMHEGRI 227
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
292-485 |
4.08e-16 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 79.35 E-value: 4.08e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 292 VDHVNFRIPRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGQAWLFGQPV---DPNDIDTRRRVGYM--SQAFSLYN-ELT 365
Cdd:PRK10419 28 LNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWRGEPLaklNRAQRKAFRRDIQMvfQDSISAVNpRKT 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 366 VRQNLELHAR-LFHIPPAEIPARVAQMIERFMLT-EVEDTLPASLPLGIRQRLSLAVAVIHRPEMLILDEPTSGVDPVAR 443
Cdd:PRK10419 108 VREIIREPLRhLLSLDKAERLARASEMLRAVDLDdSVLDKRPPQLSGGQLQRVCLARALAVEPKLLILDEAVSNLDLVLQ 187
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 446125071 444 DMFWQLMVDLSRQ-DKVTIFIsTHFMNEAER-CDRMSLMHAGKV 485
Cdd:PRK10419 188 AGVIRLLKKLQQQfGTACLFI-THDLRLVERfCQRVMVMDNGQI 230
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
16-240 |
4.14e-16 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 78.78 E-value: 4.14e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 16 EGVSQHYGKTVALNNITLDIPARSMVGLIGPDGVGKSSLLSLISGARVIEQGNVIVLGGDMR----DAKHRRDvcprIAW 91
Cdd:PRK10895 7 KNLAKAYKGRRVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEDISllplHARARRG----IGY 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 92 MPQGlgKNLYHTLSVYENVDFFARLFGHDKAE-REARITELLNSTGLAPFRDRPAGKLSGGMKQKLGLCCALIHDPELLI 170
Cdd:PRK10895 83 LPQE--ASIFRRLSVYDNLMAVLQIRDDLSAEqREDRANELMEEFHIEHLRDSMGQSLSGGERRRVEIARALAANPKFIL 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446125071 171 LDEPTTGVDPLSRAQFWDLIDSIRQRqtNMSVLVATAYMEEA----ERfDWLVAMnaGEILATGSAQQLRAKTH 240
Cdd:PRK10895 161 LDEPFAGVDPISVIDIKRIIEHLRDS--GLGVLITDHNVRETlavcER-AYIVSQ--GHLIAHGTPTEILQDEH 229
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
272-464 |
4.49e-16 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 80.39 E-value: 4.49e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 272 QEEIAIEAKDLT----MRFGKFV------AVDHVNFRIPRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGQAWLFGQPVD 341
Cdd:PRK11308 1 SQQPLLQAIDLKkhypVKRGLFKperlvkALDGVSFTLERGKTLAVVGESGCGKSTLARLLTMIETPTGGELYYQGQDLL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 342 PNDIDT----RRRVGYMSQafSLYNELTVRQN--------LELHARLfhiPPAEIPARVAQMIERFML-TEVEDTLPASL 408
Cdd:PRK11308 81 KADPEAqkllRQKIQIVFQ--NPYGSLNPRKKvgqileepLLINTSL---SAAERREKALAMMAKVGLrPEHYDRYPHMF 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 446125071 409 PLGIRQRLSLAVAVIHRPEMLILDEPTSGVDPVARDMFWQLMVDLSRQDKVT-IFIS 464
Cdd:PRK11308 156 SGGQRQRIAIARALMLDPDVVVADEPVSALDVSVQAQVLNLMMDLQQELGLSyVFIS 212
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
14-195 |
5.41e-16 |
|
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: 75.56 E-value: 5.41e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 14 QLEGVSQHYGKTVALNNITLDIPARSMVGLIGPDGVGKSSLLSLISGARVIEQGNVIVLGGdmrdakhrrdvcPRIAWMP 93
Cdd:cd03221 2 ELENLSKTYGGKLLLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIVTWGST------------VKIGYFE 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 94 QglgknlyhtlsvyenvdffarlfghdkaerearitellnstglapfrdrpagkLSGGMKQKLGLCCALIHDPELLILDE 173
Cdd:cd03221 70 Q-----------------------------------------------------LSGGEKMRLALAKLLLENPNLLLLDE 96
|
170 180
....*....|....*....|..
gi 446125071 174 PTTGVDPLSRAQfwdLIDSIRQ 195
Cdd:cd03221 97 PTNHLDLESIEA---LEEALKE 115
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
276-494 |
5.54e-16 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 78.64 E-value: 5.54e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 276 AIEAKDLTMRFGKFVAVDHVNFRIPRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGQAwlfgqPVDPNDIDT-------- 347
Cdd:PRK11264 3 AIEVKNLVKKFHGQTVLHGIDLEVKPGEVVAIIGPSGSGKTTLLRCINLLEQPEAGTI-----RVGDITIDTarslsqqk 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 348 ------RRRVGYMSQAFSLYNELTVRQN-LELHARLFHIPPAEIPARVAQMIERFMLTEVEDTLPASLPLGIRQRLSLAV 420
Cdd:PRK11264 78 glirqlRQHVGFVFQNFNLFPHRTVLENiIEGPVIVKGEPKEEATARARELLAKVGLAGKETSYPRRLSGGQQQRVAIAR 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446125071 421 AVIHRPEMLILDEPTSGVDPVARDMFWQLMVDLSrQDKVTIFISTHFMNEA-ERCDRMSLMHAGKVLASGTPQEL 494
Cdd:PRK11264 158 ALAMRPEVILFDEPTSALDPELVGEVLNTIRQLA-QEKRTMVIVTHEMSFArDVADRAIFMDQGRIVEQGPAKAL 231
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
277-499 |
6.26e-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: 82.48 E-value: 6.26e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 277 IEAKDLTMRFG-KFVAVDHVNFRIPRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGQAWLFGQPVDPNDIDT-RRRVGYM 354
Cdd:TIGR01193 474 IVINDVSYSYGyGSNILSDISLTIKMNSKTTIVGMSGSGKSTLAKLLVGFFQARSGEILLNGFSLKDIDRHTlRQFINYL 553
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 355 SQAFSLYNElTVRQNLELHAR--------LFHIPPAEIPARVAQMIERFMLTEVEDTlpASLPLGIRQRLSLAVAVIHRP 426
Cdd:TIGR01193 554 PQEPYIFSG-SILENLLLGAKenvsqdeiWAACEIAEIKDDIENMPLGYQTELSEEG--SSISGGQKQRIALARALLTDS 630
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446125071 427 EMLILDEPTSGVDPVARDMFWQLMVDLsrQDKVTIFIStHFMNEAERCDRMSLMHAGKVLASGTPQELVQQRG 499
Cdd:TIGR01193 631 KVLILDESTSNLDTITEKKIVNNLLNL--QDKTIIFVA-HRLSVAKQSDKIIVLDHGKIIEQGSHDELLDRNG 700
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
277-491 |
9.29e-16 |
|
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: 77.15 E-value: 9.29e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 277 IEAKDLTMRF--GKFVAVDHVNFRIPRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGQAWLFGqpVDPNDI---DTRRRV 351
Cdd:cd03244 3 IEFKNVSLRYrpNLPPVLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSILIDG--VDISKIglhDLRSRI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 352 GYMSQ---AFSLynelTVRQNLELHARLfhiPPAEIparvAQMIERFMLTEVEDTLPASLPL-----------GIRQRLS 417
Cdd:cd03244 81 SIIPQdpvLFSG----TIRSNLDPFGEY---SDEEL----WQALERVGLKEFVESLPGGLDTvveeggenlsvGQRQLLC 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 418 LAVAVIHRPEMLILDEPTSGVDP--------VARDMFwqlmvdlsrqDKVTIFISTHFMNEAERCDRMSLMHAGKVLASG 489
Cdd:cd03244 150 LARALLRKSKILVLDEATASVDPetdaliqkTIREAF----------KDCTVLTIAHRLDTIIDSDRILVLDKGRVVEFD 219
|
..
gi 446125071 490 TP 491
Cdd:cd03244 220 SP 221
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
28-235 |
1.02e-15 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 81.63 E-value: 1.02e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 28 LNNITLDIPARSMVGLIGPDGVGKSSLLSLISG--ARVIEQGNVIVLGGDMRDAKHRRDVCPRIawMPQGLgknLYHTLS 105
Cdd:TIGR00955 41 LKNVSGVAKPGELLAVMGSSGAGKTTLMNALAFrsPKGVKGSGSVLLNGMPIDAKEMRAISAYV--QQDDL---FIPTLT 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 106 VYENVDFFARLFGHD---KAEREARITELLNSTGLAPFRDRPAGK------LSGGMKQKLGLCCALIHDPELLILDEPTT 176
Cdd:TIGR00955 116 VREHLMFQAHLRMPRrvtKKEKRERVDEVLQALGLRKCANTRIGVpgrvkgLSGGERKRLAFASELLTDPPLLFCDEPTS 195
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 446125071 177 GVDPLSRAQFWDLIDSIRQRQTNMSVLVATAYMEEAERFDWLVAMNAGEILATGSAQQL 235
Cdd:TIGR00955 196 GLDSFMAYSVVQVLKGLAQKGKTIICTIHQPSSELFELFDKIILMAEGRVAYLGSPDQA 254
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
26-235 |
1.35e-15 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 78.74 E-value: 1.35e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 26 VALNNITLDIPARSMVGLIGPDGVGKSSLLSLISGARVIEQGNVIVlgGDMRDAKHRRDVCPRIAWMPQGLG--KNLYHT 103
Cdd:PRK13631 40 VALNNISYTFEKNKIYFIIGNSGSGKSTLVTHFNGLIKSKYGTIQV--GDIYIGDKKNNHELITNPYSKKIKnfKELRRR 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 104 LS--------------VYENVDFFARLFGHDKAEREARITELLNSTGL-APFRDRPAGKLSGGMKQKLGLCCALIHDPEL 168
Cdd:PRK13631 118 VSmvfqfpeyqlfkdtIEKDIMFGPVALGVKKSEAKKLAKFYLNKMGLdDSYLERSPFGLSGGQKRRVAIAGILAIQPEI 197
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446125071 169 LILDEPTTGVDPLSRAQFWDLI-DSIRQRQTnmsVLVATAYMEEA-ERFDWLVAMNAGEILATGSAQQL 235
Cdd:PRK13631 198 LIFDEPTAGLDPKGEHEMMQLIlDAKANNKT---VFVITHTMEHVlEVADEVIVMDKGKILKTGTPYEI 263
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
26-239 |
1.35e-15 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 78.28 E-value: 1.35e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 26 VALNNITLDIPARSMVGLIGPDGVGKSSLLSLISGARVIEQGNV----IVLGGDMRDaKHRRDVCPRIAWMPQGLGKNLY 101
Cdd:PRK13646 21 QAIHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVtvddITITHKTKD-KYIRPVRKRIGMVFQFPESQLF 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 102 HTlSVYENVDFFARLFGHDKAEREARITELLNSTG-------LAPFrdrpagKLSGGMKQKLGLCCALIHDPELLILDEP 174
Cdd:PRK13646 100 ED-TVEREIIFGPKNFKMNLDEVKNYAHRLLMDLGfsrdvmsQSPF------QMSGGQMRKIAIVSILAMNPDIIVLDEP 172
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446125071 175 TTGVDPLSRAQFWDLIDSIrQRQTNMSVLVATAYMEEAERF-DWLVAMNAGEILATGSAQQLRAKT 239
Cdd:PRK13646 173 TAGLDPQSKRQVMRLLKSL-QTDENKTIILVSHDMNEVARYaDEVIVMKEGSIVSQTSPKELFKDK 237
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
281-494 |
1.36e-15 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 78.13 E-value: 1.36e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 281 DLTMRFGKFVAVDHVNFRIPRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGQAWLFGQPVDPND---IDTRRRVGYMSQA 357
Cdd:PRK13638 6 DLWFRYQDEPVLKGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLRPQKGAVLWQGKPLDYSKrglLALRQQVATVFQD 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 358 FS---LYNEltVRQNLELHARLFHIPPAEIPARVAQMI-----ERFMLTEVEdtlpaSLPLGIRQRLSLAVAVIHRPEML 429
Cdd:PRK13638 86 PEqqiFYTD--IDSDIAFSLRNLGVPEAEITRRVDEALtlvdaQHFRHQPIQ-----CLSHGQKKRVAIAGALVLQARYL 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446125071 430 ILDEPTSGVDPVARDMFWQLMVDLSRQDKvTIFISTHFMNEA-ERCDRMSLMHAGKVLASGTPQEL 494
Cdd:PRK13638 159 LLDEPTAGLDPAGRTQMIAIIRRIVAQGN-HVIISSHDIDLIyEISDAVYVLRQGQILTHGAPGEV 223
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
28-227 |
1.89e-15 |
|
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette superfamily; ABCG transporters are involved in eye pigment (EP) precursor transport, regulation of lipid-trafficking mechanisms, and pleiotropic drug resistance (DR). DR is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. Compared to other members of the ABC transporter subfamilies, the ABCG transporter family is composed of proteins that have an ATP-binding cassette domain at the N-terminus and a TM (transmembrane) domain at the C-terminus.
Pssm-ID: 213180 [Multi-domain] Cd Length: 194 Bit Score: 75.67 E-value: 1.89e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 28 LNNITLDIPARSMVGLIGPDGVGKSSLLSLISGARVIEQ--GNVIVLGGDMRDAKHRRdvcpRIAWMPQGLgkNLYHTLS 105
Cdd:cd03213 25 LKNVSGKAKPGELTAIMGPSGAGKSTLLNALAGRRTGLGvsGEVLINGRPLDKRSFRK----IIGYVPQDD--ILHPTLT 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 106 VYENVDFFARLFGhdkaerearitellnstglapfrdrpagkLSGGMKQKLGLCCALIHDPELLILDEPTTGVDPLSRAQ 185
Cdd:cd03213 99 VRETLMFAAKLRG-----------------------------LSGGERKRVSIALELVSNPSLLFLDEPTSGLDSSSALQ 149
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 446125071 186 FWDLIDSIRQRQTNMSVLVATAYMEEAERFDWLVAMNAGEIL 227
Cdd:cd03213 150 VMSLLRRLADTGRTIICSIHQPSSEIFELFDKLLLLSQGRVI 191
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
277-494 |
1.93e-15 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 80.09 E-value: 1.93e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 277 IEAKDLTMRFGKFVAVDHVNFRIPRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGQAWLFGQPVDPNDIDTRRRVG-YM- 354
Cdd:PRK15439 12 LCARSISKQYSGVEVLKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIGGNPCARLTPAKAHQLGiYLv 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 355 SQAFSLYNELTVRQNLelharLFHIP-PAEIPARVAQMIERFMLTEVEDTLPASLPLGIRQRLSLAVAVIHRPEMLILDE 433
Cdd:PRK15439 92 PQEPLLFPNLSVKENI-----LFGLPkRQASMQKMKQLLAALGCQLDLDSSAGSLEVADRQIVEILRGLMRDSRILILDE 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446125071 434 PTSGVDPVARDMFWQLMVDLSRQDKVTIFIStHFMNEA-ERCDRMSLMHAGKVLASGTPQEL 494
Cdd:PRK15439 167 PTASLTPAETERLFSRIRELLAQGVGIVFIS-HKLPEIrQLADRISVMRDGTIALSGKTADL 227
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
277-494 |
1.99e-15 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 78.61 E-value: 1.99e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 277 IEAKDLTMRF----GKFVAVDHVNFRIPRGEIFGFLGSNGCGKSTTMKMLTGLLPAS---EGQAWLFGQPVD--PNDIDT 347
Cdd:PRK09473 13 LDVKDLRVTFstpdGDVTAVNDLNFSLRAGETLGIVGESGSGKSQTAFALMGLLAANgriGGSATFNGREILnlPEKELN 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 348 RRRVGYMSQAF-----SLYNELTVRQNL----ELHARLFHippAEIPARVAQMIERFMLTEVEDTL---PASLPLGIRQR 415
Cdd:PRK09473 93 KLRAEQISMIFqdpmtSLNPYMRVGEQLmevlMLHKGMSK---AEAFEESVRMLDAVKMPEARKRMkmyPHEFSGGMRQR 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 416 LSLAVAVIHRPEMLILDEPTSGVDPVARDMFWQLMVDLSRQDKVTIFISTHFMN-EAERCDRMSLMHAGKVLASGTPQEL 494
Cdd:PRK09473 170 VMIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKREFNTAIIMITHDLGvVAGICDKVLVMYAGRTMEYGNARDV 249
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
278-473 |
2.02e-15 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 80.22 E-value: 2.02e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 278 EAKDLTMRFGKFVAVDHVNFRIPRGEIFGFLGSNGCGKSTTMKMLTGLLPAS--EGQAWLFGQPVDPNDIDTRRRVG--Y 353
Cdd:NF040905 3 EMRGITKTFPGVKALDDVNLSVREGEIHALCGENGAGKSTLMKVLSGVYPHGsyEGEILFDGEVCRFKDIRDSEALGivI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 354 MSQAFSLYNELTVRQNLEL---HARLFHIPPAEIPARVAQMIERFMLTEVEDTLPASLPLGIRQRLSLAVAVIHRPEMLI 430
Cdd:NF040905 83 IHQELALIPYLSIAENIFLgneRAKRGVIDWNETNRRARELLAKVGLDESPDTLVTDIGVGKQQLVEIAKALSKDVKLLI 162
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 446125071 431 LDEPTSGVDPVARDMFWQLMVDLSRQDKVTIFIStHFMNEAER 473
Cdd:NF040905 163 LDEPTAALNEEDSAALLDLLLELKAQGITSIIIS-HKLNEIRR 204
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
282-471 |
2.13e-15 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 77.05 E-value: 2.13e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 282 LTMRFGKFVAVDHVNFRIPRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGQAWLFGQPVDpnDIDTRRRVGYMSQAfsLY 361
Cdd:PRK11248 7 LYADYGGKPALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDGKPVE--GPGAERGVVFQNEG--LL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 362 NELTVRQNLELHARLFHIPPAEIPARVAQMIERFMLTEVEDTLPASLPLGIRQRLSLAVAVIHRPEMLILDEPTSGVDPV 441
Cdd:PRK11248 83 PWRNVQDNVAFGLQLAGVEKMQRLEIAHQMLKKVGLEGAEKRYIWQLSGGQRQRVGIARALAANPQLLLLDEPFGALDAF 162
|
170 180 190
....*....|....*....|....*....|
gi 446125071 442 ARDMFWQLMVDLSRQDKVTIFISTHFMNEA 471
Cdd:PRK11248 163 TREQMQTLLLKLWQETGKQVLLITHDIEEA 192
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
18-259 |
2.27e-15 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 80.27 E-value: 2.27e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 18 VSQHYGKtVALNNITLDIPARSMVGLIGPDGVGKSSLLSLISGArVIEQGNVIVLGGDMRD---AKHRRdvcpRIAWmpq 94
Cdd:PRK11174 357 ILSPDGK-TLAGPLNFTLPAGQRIALVGPSGAGKTSLLNALLGF-LPYQGSLKINGIELREldpESWRK----HLSW--- 427
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 95 gLGKN--LYHTlSVYENVdffarLFGHDKAErEARITELLNSTGLAPFRDRP-----------AGKLSGGMKQKLGLCCA 161
Cdd:PRK11174 428 -VGQNpqLPHG-TLRDNV-----LLGNPDAS-DEQLQQALENAWVSEFLPLLpqgldtpigdqAAGLSVGQAQRLALARA 499
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 162 LIHDPELLILDEPTTGVDPLSRAQFWDLIDSIRQRQTnmsVLVATAYMEEAERFDWLVAMNAGEILATGSAQQLrakths 241
Cdd:PRK11174 500 LLQPCQLLLLDEPTASLDAHSEQLVMQALNAASRRQT---TLMVTHQLEDLAQWDQIWVMQDGQIVQQGDYAEL------ 570
|
250
....*....|....*...
gi 446125071 242 ATLEQAFIALLpeAQRQA 259
Cdd:PRK11174 571 SQAGGLFATLL--AHRQE 586
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
276-494 |
2.42e-15 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 77.44 E-value: 2.42e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 276 AIEAKDLTMRFGKFVAVDHVNFRIPRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGQAW-----LFGQPV-DPNDI-DTR 348
Cdd:PRK14271 21 AMAAVNLTLGFAGKTVLDQVSMGFPARAVTSLMGPTGSGKTTFLRTLNRMNDKVSGYRYsgdvlLGGRSIfNYRDVlEFR 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 349 RRVGYMSQAFSLYnELTVRQNLELHARLFHIPPAEIPARVAQ--MIERFMLTEVEDTL---PASLPLGIRQRLSLAVAVI 423
Cdd:PRK14271 101 RRVGMLFQRPNPF-PMSIMDNVLAGVRAHKLVPRKEFRGVAQarLTEVGLWDAVKDRLsdsPFRLSGGQQQLLCLARTLA 179
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446125071 424 HRPEMLILDEPTSGVDPVARDMFWQLMVDLSrqDKVTIFISTHFMNEAER-CDRMSLMHAGKVLASGTPQEL 494
Cdd:PRK14271 180 VNPEVLLLDEPTSALDPTTTEKIEEFIRSLA--DRLTVIIVTHNLAQAARiSDRAALFFDGRLVEEGPTEQL 249
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
217-535 |
2.62e-15 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 80.01 E-value: 2.62e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 217 WLVA---MNAGEILA-TGSAQ-------QLRAKTHSATLEQA----FIALLPEAQRQAHKPVVIPPyhaEQEEIAIEAKD 281
Cdd:PRK13657 263 ALVQkgqLRVGEVVAfVGFATlligrldQVVAFINQVFMAAPkleeFFEVEDAVPDVRDPPGAIDL---GRVKGAVEFDD 339
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 282 LTMRF-GKFVAVDHVNFRIPRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGQAwlfgqPVDPNDIDT------RRRVGYM 354
Cdd:PRK13657 340 VSFSYdNSRQGVEDVSFEAKPGQTVAIVGPTGAGKSTLINLLQRVFDPQSGRI-----LIDGTDIRTvtraslRRNIAVV 414
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 355 SQAFSLYNElTVRQNLEL------HARLfhippaEIPARVAQMIErFMLTEVE--DTLPA----SLPLGIRQRLSLAVAV 422
Cdd:PRK13657 415 FQDAGLFNR-SIEDNIRVgrpdatDEEM------RAAAERAQAHD-FIERKPDgyDTVVGergrQLSGGERQRLAIARAL 486
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 423 IHRPEMLILDEPTSGVDpVARDMFWQLMVDLSRQDKVTiFISTHFMNEAERCDRMSLMHAGKVLASGTPQELVQQRG--A 500
Cdd:PRK13657 487 LKDPPILILDEATSALD-VETEAKVKAALDELMKGRTT-FIIAHRLSTVRNADRILVFDNGRVVESGSFDELVARGGrfA 564
|
330 340 350
....*....|....*....|....*....|....*
gi 446125071 501 ANLEAAFIswLQEAAGAAPetpippsqtPAASGKP 535
Cdd:PRK13657 565 ALLRAQGM--LQEDERRKQ---------PAAEGAN 588
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
21-235 |
2.82e-15 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 76.80 E-value: 2.82e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 21 HYGKTVALNNITLDIPARSMVGLIGPDGVGKSSLL-------SLISGARVieQGNVIVLG-----GDMRDAKHRRDVCPR 88
Cdd:PRK14267 13 YYGSNHVIKGVDLKIPQNGVFALMGPSGCGKSTLLrtfnrllELNEEARV--EGEVRLFGrniysPDVDPIEVRREVGMV 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 89 IAWmpqglgKNLYHTLSVYENVDFFARLFG--HDKAEREARITELLNSTGL-APFRDR---PAGKLSGGMKQKLGLCCAL 162
Cdd:PRK14267 91 FQY------PNPFPHLTIYDNVAIGVKLNGlvKSKKELDERVEWALKKAALwDEVKDRlndYPSNLSGGQRQRLVIARAL 164
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446125071 163 IHDPELLILDEPTTGVDPLSRAQFWDLIDSIRQRQTnmSVLVATAYMEEAERFDWLVAMNAGEILATGSAQQL 235
Cdd:PRK14267 165 AMKPKILLMDEPTANIDPVGTAKIEELLFELKKEYT--IVLVTHSPAQAARVSDYVAFLYLGKLIEVGPTRKV 235
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
16-235 |
2.89e-15 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 78.92 E-value: 2.89e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 16 EGVSQHYGKTVALNNITLDIPARSMVGLIGPDGVGKSSLLSLISgaRVIE--QGNVIVLGGDM---RDAKHRRDVCPRIA 90
Cdd:PRK10070 32 EQILEKTGLSLGVKDASLAIEEGEIFVIMGLSGSGKSTMVRLLN--RLIEptRGQVLIDGVDIakiSDAELREVRRKKIA 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 91 WMPQGLGknLYHTLSVYENVDFFARLFGHDKAEREARITELLNSTGLAPFRDRPAGKLSGGMKQKLGLCCALIHDPELLI 170
Cdd:PRK10070 110 MVFQSFA--LMPHMTVLDNTAFGMELAGINAEERREKALDALRQVGLENYAHSYPDELSGGMRQRVGLARALAINPDILL 187
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446125071 171 LDEPTTGVDPLSRAQFWDLIDSIRQRQTNMSVLVATAyMEEAERF-DWLVAMNAGEILATGSAQQL 235
Cdd:PRK10070 188 MDEAFSALDPLIRTEMQDELVKLQAKHQRTIVFISHD-LDEAMRIgDRIAIMQNGEVVQVGTPDEI 252
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
14-239 |
3.42e-15 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 76.73 E-value: 3.42e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 14 QLEGVSQHYGKTVALNNITLDIPARSMVGLIGPDGVGKSSLLSLISGARVIEQGNVIVLGGDMRDAKHRR--DVCPRIAW 91
Cdd:PRK11831 9 DMRGVSFTRGNRCIFDNISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEILFDGENIPAMSRSRlyTVRKRMSM 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 92 MPQGlgKNLYHTLSVYENVDFFARlfghdkaEREARITELLNST--------GLAPFRDRPAGKLSGGMKQKLGLCCALI 163
Cdd:PRK11831 89 LFQS--GALFTDMNVFDNVAYPLR-------EHTQLPAPLLHSTvmmkleavGLRGAAKLMPSELSGGMARRAALARAIA 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446125071 164 HDPELLILDEPTTGVDPLSRAQFWDLIDSIRQRQTNMSVLVATAYMEEAERFDWLVAMNAGEILATGSAQQLRAKT 239
Cdd:PRK11831 160 LEPDLIMFDEPFVGQDPITMGVLVKLISELNSALGVTCVVVSHDVPEVLSIADHAYIVADKKIVAHGSAQALQANP 235
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
12-325 |
4.45e-15 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 79.39 E-value: 4.45e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 12 VAQLEGVSQHYG-KTVALNNITLDIPARSMVGLIGPDGVGKSSLLSLISGARVIEQGNVIVLGGdmrdakhrrdvcPRIA 90
Cdd:PRK11819 6 IYTMNRVSKVVPpKKQILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKEFEGEARPAPG------------IKVG 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 91 WMPQGlgKNLYHTLSVYENV--------DFFARL------FGHDKA------EREARITELLNSTGLA------------ 138
Cdd:PRK11819 74 YLPQE--PQLDPEKTVRENVeegvaevkAALDRFneiyaaYAEPDAdfdalaAEQGELQEIIDAADAWdldsqleiamda 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 139 ---PFRDRPAGKLSGGMKQKLGLCCALIHDPELLILDEPTTGVDPLSRA---QF-----------------------WDL 189
Cdd:PRK11819 152 lrcPPWDAKVTKLSGGERRRVALCRLLLEKPDMLLLDEPTNHLDAESVAwleQFlhdypgtvvavthdryfldnvagWIL 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 190 -IDsiRQR----QTNMSvlvatAYME------------EAER-------FDWlVAMNAgeilatgSAQQLRAKthsATLe 245
Cdd:PRK11819 232 eLD--RGRgipwEGNYS-----SWLEqkakrlaqeekqEAARqkalkreLEW-VRQSP-------KARQAKSK---ARL- 292
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 246 QAFIALLPEAQRQAHKP--VVIPPyhAEQ-EEIAIEAKDLTMRFGKFVAVDHVNFRIPRGEIFGFLGSNGCGKSTTMKML 322
Cdd:PRK11819 293 ARYEELLSEEYQKRNETneIFIPP--GPRlGDKVIEAENLSKSFGDRLLIDDLSFSLPPGGIVGIIGPNGAGKSTLFKMI 370
|
...
gi 446125071 323 TGL 325
Cdd:PRK11819 371 TGQ 373
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
20-246 |
4.80e-15 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 76.16 E-value: 4.80e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 20 QHYGKTVALNNITLDIPARSMVGLIGPDGVGKSSLLSLISGARVIEQGNVIVLGGDMR------------DAKHRRDVCP 87
Cdd:PRK10619 13 KRYGEHEVLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNGQTINlvrdkdgqlkvaDKNQLRLLRT 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 88 RIAWMPQGLgkNLYHTLSVYENV-DFFARLFGHDKAEREARITELLNSTGLApfrDRPAGK----LSGGMKQKLGLCCAL 162
Cdd:PRK10619 93 RLTMVFQHF--NLWSHMTVLENVmEAPIQVLGLSKQEARERAVKYLAKVGID---ERAQGKypvhLSGGQQQRVSIARAL 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 163 IHDPELLILDEPTTGVDPLSRAQFWDLIDSIRQRQTNMsvLVATAYMEEAERF-DWLVAMNAGEILATGSAQQLRAKTHS 241
Cdd:PRK10619 168 AMEPEVLLFDEPTSALDPELVGEVLRIMQQLAEEGKTM--VVVTHEMGFARHVsSHVIFLHQGKIEEEGAPEQLFGNPQS 245
|
....*
gi 446125071 242 ATLEQ 246
Cdd:PRK10619 246 PRLQQ 250
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
11-235 |
5.83e-15 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 77.57 E-value: 5.83e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 11 PVAQLEGVSQHYGKTVALNNITLDIPARSMVGLIGPDGVGKSSLLSLISGARVIEQGNVIVLGGDMRD-AKHRRDvcprI 89
Cdd:PRK11607 18 PLLEIRNLTKSFDGQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVDLSHvPPYQRP----I 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 90 AWMPQGLGknLYHTLSVYENVDFFARLFGHDKAEREARITELLNSTGLAPFRDRPAGKLSGGMKQKLGLCCALIHDPELL 169
Cdd:PRK11607 94 NMMFQSYA--LFPHMTVEQNIAFGLKQDKLPKAEIASRVNEMLGLVHMQEFAKRKPHQLSGGQRQRVALARSLAKRPKLL 171
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446125071 170 ILDEPTTGVDPLSRAQFWDLIDSIRQRQTNMSVLVaTAYMEEAERFDWLVA-MNAGEILATGSAQQL 235
Cdd:PRK11607 172 LLDEPMGALDKKLRDRMQLEVVDILERVGVTCVMV-THDQEEAMTMAGRIAiMNRGKFVQIGEPEEI 237
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
276-473 |
5.90e-15 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 75.84 E-value: 5.90e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 276 AIEAKDLTMRFGKFVAVDHVNFRIPRGEIFGFLGSNGCGKSTTMKMLTGLLPAS-----EGQAWLFGQPVDPNDIDTRRR 350
Cdd:PRK14258 7 AIKVNNLSFYYDTQKILEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLNRMNELEsevrvEGRVEFFNQNIYERRVNLNRL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 351 VGYMSQAFSLYN--ELTVRQNLELHARL--FHiPPAEIPARVAQMIERFML-TEVEDTLPAS---LPLGIRQRLSLAVAV 422
Cdd:PRK14258 87 RRQVSMVHPKPNlfPMSVYDNVAYGVKIvgWR-PKLEIDDIVESALKDADLwDEIKHKIHKSaldLSGGQQQRLCIARAL 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 446125071 423 IHRPEMLILDEPTSGVDPVARDMFWQLMVDLSRQDKVTIFISTHFMNEAER 473
Cdd:PRK14258 166 AVKPKVLLMDEPCFGLDPIASMKVESLIQSLRLRSELTMVIVSHNLHQVSR 216
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
14-226 |
6.44e-15 |
|
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: 73.40 E-value: 6.44e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 14 QLEGVSQHYG--KTVALNNITLDIPARSMVGLIGPDGVGKSSLLSLISGARVIEQGNVIVLGGDMRDAkHRRDVCPRIAW 91
Cdd:cd03246 2 EVENVSFRYPgaEPPVLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDGADISQW-DPNELGDHVGY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 92 MPQGLgkNLYhTLSVYENVdffarlfghdkaerearitellnstglapfrdrpagkLSGGMKQKLGLCCALIHDPELLIL 171
Cdd:cd03246 81 LPQDD--ELF-SGSIAENI-------------------------------------LSGGQRQRLGLARALYGNPRILVL 120
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 446125071 172 DEPTTGVDPLSRAQFWDLIDSIRQRQTnmSVLVATAYMEEAERFDWLVAMNAGEI 226
Cdd:cd03246 121 DEPNSHLDVEGERALNQAIAALKAAGA--TRIVIAHRPETLASADRILVLEDGRV 173
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
277-497 |
6.81e-15 |
|
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of iron-sulfur clusters (Fe-S) depends on multi-protein systems. The SUF system of E. coli and Erwinia chrysanthemi is important for Fe-S biogenesis under stressful conditions. The SUF system is made of six proteins: SufC is an atypical cytoplasmic ABC-ATPase, which forms a complex with SufB and SufD; SufA plays the role of a scaffold protein for assembly of iron-sulfur clusters and delivery to target proteins; SufS is a cysteine desulfurase which mobilizes the sulfur atom from cysteine and provides it to the cluster; SufE has no associated function yet.
Pssm-ID: 213184 [Multi-domain] Cd Length: 200 Bit Score: 74.10 E-value: 6.81e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 277 IEAKDLTMRFGKFVAVDHVNFRIPRGEIFGFLGSNGCGKSTTMKMLTGLlPASE---GQAWLFGQPVDPNDIDTRRRVG- 352
Cdd:cd03217 1 LEIKDLHVSVGGKEILKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMGH-PKYEvteGEILFKGEDITDLPPEERARLGi 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 353 YMSQafslyneltvrQNlelharlfhipPAEIPA-RVAqmierFMLTEVEDTLPAslplGIRQRLSLAVAVIHRPEMLIL 431
Cdd:cd03217 80 FLAF-----------QY-----------PPEIPGvKNA-----DFLRYVNEGFSG----GEKKRNEILQLLLLEPDLAIL 128
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446125071 432 DEPTSGVDPVARDMFWQLMVDLsRQDKVTIFISTHFMNEAE--RCDRMSLMHAGKVLASGtPQELVQQ 497
Cdd:cd03217 129 DEPDSGLDIDALRLVAEVINKL-REEGKSVLIITHYQRLLDyiKPDRVHVLYDGRIVKSG-DKELALE 194
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
27-235 |
9.65e-15 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 75.56 E-value: 9.65e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 27 ALNNITLDIPARSMVGLIGPDGVGKSSLLSLISGARVIEQGNvIVLGGDMRDAKHRRDVCPRIAWMPQGlGKNLYHTLSV 106
Cdd:PRK13648 24 TLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGE-IFYNNQAITDDNFEKLRKHIGIVFQN-PDNQFVGSIV 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 107 YENVDFFAR--LFGHDKAEReaRITELLNSTGLAPFRDRPAGKLSGGMKQKLGLCCALIHDPELLILDEPTTGVDPLSRA 184
Cdd:PRK13648 102 KYDVAFGLEnhAVPYDEMHR--RVSEALKQVDMLERADYEPNALSGGQKQRVAIAGVLALNPSVIILDEATSMLDPDARQ 179
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 446125071 185 QFWDLIDSIRQRQtNMSVLVATAYMEEAERFDWLVAMNAGEILATGSAQQL 235
Cdd:PRK13648 180 NLLDLVRKVKSEH-NITIISITHDLSEAMEADHVIVMNKGTVYKEGTPTEI 229
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
14-237 |
9.81e-15 |
|
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide chain transporter in the ATP-binding cassette (ABC) transporter family, MsbA, which exports lipid A. It may also act in multidrug resistance. Lipid A, a part of lipopolysaccharide, is found in the outer leaflet of the outer membrane of most Gram-negative bacteria. Members of this family are restricted to the Proteobacteria (although lipid A is more broadly distributed) and often are clustered with lipid A biosynthesis genes. [Cell envelope, Biosynthesis and degradation of surface polysaccharides and lipopolysaccharides, Transport and binding proteins, Other]
Pssm-ID: 131258 [Multi-domain] Cd Length: 571 Bit Score: 78.22 E-value: 9.81e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 14 QLEGVSQHYGKT--VALNNITLDIPARSMVGLIGPDGVGKSSLLSLISGARVIEQGNVIVLGGDMRDAKhRRDVCPRIAW 91
Cdd:TIGR02203 332 EFRNVTFRYPGRdrPALDSISLVIEPGETVALVGRSGSGKSTLVNLIPRFYEPDSGQILLDGHDLADYT-LASLRRQVAL 410
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 92 MPQGLgkNLYHTlSVYENVDFfARLFGHDKAE-----REARITELLNST--GLAPFRDRPAGKLSGGMKQKLGLCCALIH 164
Cdd:TIGR02203 411 VSQDV--VLFND-TIANNIAY-GRTEQADRAEieralAAAYAQDFVDKLplGLDTPIGENGVLLSGGQRQRLAIARALLK 486
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446125071 165 DPELLILDEPTTGVDPLSRAQFWDLIDSIRQRQTNMSVLVATAYMEEAERfdwLVAMNAGEILATGSAQQLRA 237
Cdd:TIGR02203 487 DAPILILDEATSALDNESERLVQAALERLMQGRTTLVIAHRLSTIEKADR---IVVMDDGRIVERGTHNELLA 556
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
277-491 |
1.11e-14 |
|
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type transporter 1). NFT1 belongs to the MRP (multidrug resistance-associated protein) family of ABC transporters. Some of the MRP members have five additional transmembrane segments in their N-terminus, but the function of these additional membrane-spanning domains is not clear. The MRP was found in the multidrug-resisting lung cancer cell in which p-glycoprotein was not overexpressed. MRP exports glutathione by drug stimulation, as well as, certain substrates in conjugated forms with anions such as glutathione, glucuronate, and sulfate.
Pssm-ID: 213269 [Multi-domain] Cd Length: 207 Bit Score: 73.60 E-value: 1.11e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 277 IEAKDLTMRFGKFV--AVDHVNFRIPRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGQAWLFGQPVDPNDI-DTRRRVGY 353
Cdd:cd03369 7 IEVENLSVRYAPDLppVLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDGIDISTIPLeDLRSSLTI 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 354 MSQAFSLYNElTVRQNLELHARLFHippaeiparvAQMIERFMLTEVEDTLPAslplGIRQRLSLAVAVIHRPEMLILDE 433
Cdd:cd03369 87 IPQDPTLFSG-TIRSNLDPFDEYSD----------EEIYGALRVSEGGLNLSQ----GQRQLLCLARALLKRPRVLVLDE 151
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 446125071 434 PTSGVDpVARDMFWQLMVDLSRQDkVTIFISTHFMNEAERCDRMSLMHAGKVLASGTP 491
Cdd:cd03369 152 ATASID-YATDALIQKTIREEFTN-STILTIAHRLRTIIDYDKILVMDAGEVKEYDHP 207
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
12-235 |
1.14e-14 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 75.02 E-value: 1.14e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 12 VAQLEG--VSQHYGKTVALNNITLDIPARSMVGLIGPDGVGKSSLLSLISGARVIEQGNVIvLGGDMRDAKHRRDVCPRI 89
Cdd:PRK10253 5 VARLRGeqLTLGYGKYTVAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVW-LDGEHIQHYASKEVARRI 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 90 AWMPQGlgKNLYHTLSVYENVdffAR-------LFGHDKAEREARITELLNSTGLAPFRDRPAGKLSGGMKQKLGLCCAL 162
Cdd:PRK10253 84 GLLAQN--ATTPGDITVQELV---ARgryphqpLFTRWRKEDEEAVTKAMQATGITHLADQSVDTLSGGQRQRAWIAMVL 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446125071 163 IHDPELLILDEPTTGVDPLSRAQFWDLIDSIrQRQTNMSVLVATAYMEEAERF-DWLVAMNAGEILATGSAQQL 235
Cdd:PRK10253 159 AQETAIMLLDEPTTWLDISHQIDLLELLSEL-NREKGYTLAAVLHDLNQACRYaSHLIALREGKIVAQGAPKEI 231
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
274-495 |
1.24e-14 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 75.21 E-value: 1.24e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 274 EIAIEAKDLTMRF----GKF-----VAVDHVNFRIPRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGQAWLFGQPVDPND 344
Cdd:PRK15112 2 ETLLEVRNLSKTFryrtGWFrrqtvEAVKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDHPLHFGD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 345 IDTRR---RVGYMSQAFSLYNELTVRQNLELHARL-FHIPPAEIPARVAQMIERF-MLTEVEDTLPASLPLGIRQRLSLA 419
Cdd:PRK15112 82 YSYRSqriRMIFQDPSTSLNPRQRISQILDFPLRLnTDLEPEQREKQIIETLRQVgLLPDHASYYPHMLAPGQKQRLGLA 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446125071 420 VAVIHRPEMLILDEPTSGVDPVARDMFWQLMVDLSRQDKVT-IFISTHFMNEAERCDRMSLMHAGKVLASGTPQELV 495
Cdd:PRK15112 162 RALILRPKVIIADEALASLDMSMRSQLINLMLELQEKQGISyIYVTQHLGMMKHISDQVLVMHQGEVVERGSTADVL 238
|
|
| CP_lyasePhnK |
TIGR02323 |
phosphonate C-P lyase system protein PhnK; Members of this family are the PhnK protein of C-P ... |
10-235 |
1.61e-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: 74.48 E-value: 1.61e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 10 PPVAQLEGVSQHYGKTVALNNITLDIPARSMVGLIGPDGVGKSSLLSLISGARVIEQGNVivlGGDMRD----------- 78
Cdd:TIGR02323 1 KPLLQVSGLSKSYGGGKGCRDVSFDLYPGEVLGIVGESGSGKSTLLGCLAGRLAPDHGTA---TYIMRSgaelelyqlse 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 79 AKHRRdvCPRIAW--MPQGLGKNLYHTLSVYENV-----DFFARLFGHDKAEREARITELlnSTGLAPFRDRPAgKLSGG 151
Cdd:TIGR02323 78 AERRR--LMRTEWgfVHQNPRDGLRMRVSAGANIgerlmAIGARHYGNIRATAQDWLEEV--EIDPTRIDDLPR-AFSGG 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 152 MKQKLGLCCALIHDPELLILDEPTTGVDPLSRAQFWDLIDSIrQRQTNMSVLVATAYMEEAERF-DWLVAMNAGEILATG 230
Cdd:TIGR02323 153 MQQRLQIARNLVTRPRLVFMDEPTGGLDVSVQARLLDLLRGL-VRDLGLAVIIVTHDLGVARLLaQRLLVMQQGRVVESG 231
|
....*
gi 446125071 231 SAQQL 235
Cdd:TIGR02323 232 LTDQV 236
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
33-439 |
2.46e-14 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 77.16 E-value: 2.46e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 33 LDIPARSMV-GLIGPDGVGKSSLLSLISGARVIEQGNVivLGGDMRDA--KHRRdvcpriawmpqglGKNLYHTLS-VYE 108
Cdd:PRK13409 93 LPIPKEGKVtGILGPNGIGKTTAVKILSGELIPNLGDY--EEEPSWDEvlKRFR-------------GTELQNYFKkLYN 157
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 109 N----------VDFFARLF-GH-----DKAEREARITELLNSTGLAPFRDRPAGKLSGGMKQKLGLCCALIHDPELLILD 172
Cdd:PRK13409 158 GeikvvhkpqyVDLIPKVFkGKvrellKKVDERGKLDEVVERLGLENILDRDISELSGGELQRVAIAAALLRDADFYFFD 237
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 173 EPTTGVDplsraqfwdlidsIRQRqtnmsVLVATAYMEEAER------------FDWL---VAMNAGEILATGSAQQLRA 237
Cdd:PRK13409 238 EPTSYLD-------------IRQR-----LNVARLIRELAEGkyvlvvehdlavLDYLadnVHIAYGEPGAYGVVSKPKG 299
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 238 kTHSATleQAFIA-LLPEAQ-RQAHKPV---VIPPYHAEQEEIAIEAKDLTMRFGKF-VAVDHVNFRipRGEIFGFLGSN 311
Cdd:PRK13409 300 -VRVGI--NEYLKgYLPEENmRIRPEPIefeERPPRDESERETLVEYPDLTKKLGDFsLEVEGGEIY--EGEVIGIVGPN 374
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 312 GCGKSTTMKMLTGLLPASEGqawlfgqpvdpnDIDTRRRVGYMSQAFSLYNELTVRQNLELHARLFHIPP--AEIPARVA 389
Cdd:PRK13409 375 GIGKTTFAKLLAGVLKPDEG------------EVDPELKISYKPQYIKPDYDGTVEDLLRSITDDLGSSYykSEIIKPLQ 442
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|
gi 446125071 390 qmIERFMLTEVEDtlpasLPLGIRQRLSLAVAVIHRPEMLILDEPTSGVD 439
Cdd:PRK13409 443 --LERLLDKNVKD-----LSGGELQRVAIAACLSRDADLYLLDEPSAHLD 485
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
277-484 |
3.66e-14 |
|
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: 70.56 E-value: 3.66e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 277 IEAKDLTMRFGKFVAVDHVNFRIPRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGQaWLFGQPVdpndidtrrRVGYMSQ 356
Cdd:cd03221 1 IELENLSKTYGGKLLLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGI-VTWGSTV---------KIGYFEQ 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 357 afslyneltvrqnlelharlfhippaeiparvaqmierfmltevedtlpasLPLGIRQRLSLAVAVIHRPEMLILDEPTS 436
Cdd:cd03221 71 ---------------------------------------------------LSGGEKMRLALAKLLLENPNLLLLDEPTN 99
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 446125071 437 GVDPVARDmfwQLMVDLSRQDKVTIFIS--THFMNEAerCDRMSLMHAGK 484
Cdd:cd03221 100 HLDLESIE---ALEEALKEYPGTVILVShdRYFLDQV--ATKIIELEDGK 144
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
291-473 |
3.84e-14 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 72.60 E-value: 3.84e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 291 AVDHVNFRIPRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGQAWLFGqpvdpNDIDT---------RRRVGYMSQAFSLY 361
Cdd:PRK10908 17 ALQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSG-----HDITRlknrevpflRRQIGMIFQDHHLL 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 362 NELTVRQNLELHARLFHIPPAEIPARVAQMIERFMLTEVEDTLPASLPLGIRQRLSLAVAVIHRPEMLILDEPTSGVDPV 441
Cdd:PRK10908 92 MDRTVYDNVAIPLIIAGASGDDIRRRVSAALDKVGLLDKAKNFPIQLSGGEQQRVGIARAVVNKPAVLLADEPTGNLDDA 171
|
170 180 190
....*....|....*....|....*....|..
gi 446125071 442 ARDMFWQLMVDLSRQDkVTIFISTHFMNEAER 473
Cdd:PRK10908 172 LSEGILRLFEEFNRVG-VTVLMATHDIGLISR 202
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
118-266 |
3.98e-14 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 74.39 E-value: 3.98e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 118 GHDKAEREARITELLNSTGL---APFRDRPAGKLSGGMKQKLGLCCALIHDPELLILDEPTTGVDPLSRAQFWDLIDSIr 194
Cdd:PRK11022 121 GGNKKTRRQRAIDLLNQVGIpdpASRLDVYPHQLSGGMSQRVMIAMAIACRPKLLIADEPTTALDVTIQAQIIELLLEL- 199
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446125071 195 QRQTNMSVLVATAYME-EAERFDWLVAMNAGEILATGSAQQL-RAKTHSATleQAFIALLPE----AQRQAHKPVVIP 266
Cdd:PRK11022 200 QQKENMALVLITHDLAlVAEAAHKIIVMYAGQVVETGKAHDIfRAPRHPYT--QALLRALPEfaqdKARLASLPGVVP 275
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
293-572 |
4.34e-14 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 76.30 E-value: 4.34e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 293 DHVNFRIPRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGQAWLFGQPVDPNDIDT-----RRRVGYMSQAFSLYNELTVR 367
Cdd:PRK10535 25 KGISLDIYAGEMVAIVGASGSGKSTLMNILGCLDKPTSGTYRVAGQDVATLDADAlaqlrREHFGFIFQRYHLLSHLTAA 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 368 QNLELHARLFHIPPAEIPARVAQMIERFMLTEVEDTLPASLPLGIRQRLSLAVAVIHRPEMLILDEPTSGVDPVARDMFW 447
Cdd:PRK10535 105 QNVEVPAVYAGLERKQRLLRAQELLQRLGLEDRVEYQPSQLSGGQQQRVSIARALMNGGQVILADEPTGALDSHSGEEVM 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 448 QLMVDLsRQDKVTIFISTHFMNEAERCDRMSLMHAGKVLASGTPQElvqqrgaanleaafiswlqeaagAAPETPIPPSQ 527
Cdd:PRK10535 185 AILHQL-RDRGHTVIIVTHDPQVAAQAERVIEIRDGEIVRNPPAQE-----------------------KVNVAGGTEPV 240
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 446125071 528 TPAASGkpsrqglsFRRLFSySRREAL-----ELRRDPVRSTLALLGTVI 572
Cdd:PRK10535 241 VNTASG--------WRQFVS-GFREALtmawrAMAANKMRTLLTMLGIII 281
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
273-495 |
4.48e-14 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 72.60 E-value: 4.48e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 273 EEIAIEAKDLTMRFGKFVAVDHVNFRIPRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGQAWLFGQPVD--PNDIDTRRR 350
Cdd:PRK11614 2 EKVMLSFDKVSAHYGKIQALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDGKDITdwQTAKIMREA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 351 VGYMSQAFSLYNELTVRQNLELHArlFHIPPAEIPARVAQMIERF-MLTEVEDTLPASLPLGIRQRLSLAVAVIHRPEML 429
Cdd:PRK11614 82 VAIVPEGRRVFSRMTVEENLAMGG--FFAERDQFQERIKWVYELFpRLHERRIQRAGTMSGGEQQMLAIGRALMSQPRLL 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446125071 430 ILDEPTSGVDPVARDMFWQLMVDLsRQDKVTIFISTHFMNEAER-CDRMSLMHAGKVLASGTPQELV 495
Cdd:PRK11614 160 LLDEPSLGLAPIIIQQIFDTIEQL-REQGMTIFLVEQNANQALKlADRGYVLENGHVVLEDTGDALL 225
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
18-237 |
8.47e-14 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 72.09 E-value: 8.47e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 18 VSQHYGKTVaLNNITLDIPARSMVGLIGPDGVGKSSLLSLISGARVIEQGNVIVLGGDMRDAKHRRDVCPRIAWMPQGLG 97
Cdd:PRK11264 10 VKKFHGQTV-LHGIDLEVKPGEVVAIIGPSGSGKTTLLRCINLLEQPEAGTIRVGDITIDTARSLSQQKGLIRQLRQHVG 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 98 K-----NLYHTLSVYENV-DFFARLFGHDKAEREARITELLNSTGLAPFRDRPAGKLSGGMKQKLGLCCALIHDPELLIL 171
Cdd:PRK11264 89 FvfqnfNLFPHRTVLENIiEGPVIVKGEPKEEATARARELLAKVGLAGKETSYPRRLSGGQQQRVAIARALAMRPEVILF 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446125071 172 DEPTTGVDPLSRAQFWDLIDSIRQRQTNMsvLVATAYMEEA-ERFDWLVAMNAGEILATGSAQQLRA 237
Cdd:PRK11264 169 DEPTSALDPELVGEVLNTIRQLAQEKRTM--VIVTHEMSFArDVADRAIFMDQGRIVEQGPAKALFA 233
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
14-226 |
9.78e-14 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 73.72 E-value: 9.78e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 14 QLEGVSQHY-GKTVALNNITLDIPARSMVGLIGPDGVGKSSLLSLISGARVIEQGNvIVLGGdmrdakhRR--DVCPR-- 88
Cdd:PRK11650 5 KLQAVRKSYdGKTQVIKGIDLDVADGEFIVLVGPSGCGKSTLLRMVAGLERITSGE-IWIGG-------RVvnELEPAdr 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 89 -IAWMPQglgkN--LYHTLSVYENVDFFARLFGHDKAEREARITELLNSTGLAPFRDRPAGKLSGGMKQKLGLCCALIHD 165
Cdd:PRK11650 77 dIAMVFQ----NyaLYPHMSVRENMAYGLKIRGMPKAEIEERVAEAARILELEPLLDRKPRELSGGQRQRVAMGRAIVRE 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446125071 166 PELLILDEPTTGVDPLSRAQFWDLIDSIRQRQTNMSVLVATAYMEEAERFDWLVAMNAGEI 226
Cdd:PRK11650 153 PAVFLFDEPLSNLDAKLRVQMRLEIQRLHRRLKTTSLYVTHDQVEAMTLADRVVVMNGGVA 213
|
|
| ABC2_membrane |
pfam01061 |
ABC-2 type transporter; |
726-876 |
1.02e-13 |
|
ABC-2 type transporter;
Pssm-ID: 426023 [Multi-domain] Cd Length: 204 Bit Score: 70.77 E-value: 1.02e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 726 LLLMMIPSMLSALSVVREKELGSMINLYVTPT-TRSEFLLGKQLPYIALGMLNFLLLCALSVFVFGVPL-KGSFLTLTLA 803
Cdd:pfam01061 53 SILFNAFSALSGISPVFEKERGVLYRELASPLySPSAYVLAKILSELPLSLLQSLIFLLIVYFMVGLPPsAGRFFLFLLV 132
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446125071 804 ALLYVIIATGLGLLISTFMKSQIAAIFGTSIITLiPATQFSGMIDPVASLEGPGRWIGEIYPTSHFLTIARGT 876
Cdd:pfam01061 133 LLLTALAASSLGLFISALAPSFEDASQLGPLVLL-PLLLLSGFFIPIDSMPVWWQWIYYLNPLTYAIEALRAN 204
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
11-214 |
1.18e-13 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 71.99 E-value: 1.18e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 11 PVAQLEGVSQHYGKTVALNNITLDIPARSMVGLIGPDGVGKSSLLSLISGARVIE-----QGNVIVLGGDMRDAKHRRDV 85
Cdd:PRK14258 6 PAIKVNNLSFYYDTQKILEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLNRMNELEsevrvEGRVEFFNQNIYERRVNLNR 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 86 CPRIAWM--PQglgKNLYhTLSVYENVDFFARLFG-HDKAEREARITELLNSTGL----APFRDRPAGKLSGGMKQKLGL 158
Cdd:PRK14258 86 LRRQVSMvhPK---PNLF-PMSVYDNVAYGVKIVGwRPKLEIDDIVESALKDADLwdeiKHKIHKSALDLSGGQQQRLCI 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 446125071 159 CCALIHDPELLILDEPTTGVDPLSRAQFWDLIDSIRQRqTNMSVLVATAYMEEAER 214
Cdd:PRK14258 162 ARALAVKPKVLLMDEPCFGLDPIASMKVESLIQSLRLR-SELTMVIVSHNLHQVSR 216
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
23-235 |
1.20e-13 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 72.44 E-value: 1.20e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 23 GKTVaLNNITLDIPARSMVGLIGPDGVGKSSLLSL-------ISGARVieQGNVIvLGGdmRDAKHRRDVCP---RIAWM 92
Cdd:PRK14271 33 GKTV-LDQVSMGFPARAVTSLMGPTGSGKTTFLRTlnrmndkVSGYRY--SGDVL-LGG--RSIFNYRDVLEfrrRVGML 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 93 PQglgKNLYHTLSVYENVdfFARLFGHDKAER-------EARITEL------LNSTGLAPFRdrpagkLSGGMKQKLGLC 159
Cdd:PRK14271 107 FQ---RPNPFPMSIMDNV--LAGVRAHKLVPRkefrgvaQARLTEVglwdavKDRLSDSPFR------LSGGQQQLLCLA 175
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446125071 160 CALIHDPELLILDEPTTGVDPLSRAQFWDLIDSIRQRqtnMSVLVATAYMEEAERF-DWLVAMNAGEILATGSAQQL 235
Cdd:PRK14271 176 RTLAVNPEVLLLDEPTSALDPTTTEKIEEFIRSLADR---LTVIIVTHNLAQAARIsDRAALFFDGRLVEEGPTEQL 249
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
254-506 |
1.30e-13 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 74.50 E-value: 1.30e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 254 EAQRQAHKPVvippyhAEQEEIAIEAKDLTMRF--GKfVAVDHVNFRIPRGEIFGFLGSNGCGKSTTMKMLTGLLPaSEG 331
Cdd:PRK11174 333 AHPQQGEKEL------ASNDPVTIEAEDLEILSpdGK-TLAGPLNFTLPAGQRIALVGPSGAGKTSLLNALLGFLP-YQG 404
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 332 QAWLFGQPVdpNDIDT---RRRVGYMSQAFSLYnELTVRQNLELHArlfhipPAEIPARVAQMIERFMLTEVEDTLP--- 405
Cdd:PRK11174 405 SLKINGIEL--RELDPeswRKHLSWVGQNPQLP-HGTLRDNVLLGN------PDASDEQLQQALENAWVSEFLPLLPqgl 475
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 406 --------ASLPLGIRQRLSLAVAVIHRPEMLILDEPTSGVDPVARDMFWQLMVDLSRQdKVTIFIsTHFMNEAERCDRM 477
Cdd:PRK11174 476 dtpigdqaAGLSVGQAQRLALARALLQPCQLLLLDEPTASLDAHSEQLVMQALNAASRR-QTTLMV-THQLEDLAQWDQI 553
|
250 260 270
....*....|....*....|....*....|
gi 446125071 478 SLMHAGKVLASGTPQELVQQRGA-ANLEAA 506
Cdd:PRK11174 554 WVMQDGQIVQQGDYAELSQAGGLfATLLAH 583
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
291-488 |
1.71e-13 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 74.18 E-value: 1.71e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 291 AVDHVNFRIPRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGQAWLFGQPVdpNDIDTRRR----VGYMSQAFSLYNELTV 366
Cdd:PRK11288 19 ALDDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSILIDGQEM--RFASTTAAlaagVAIIYQELHLVPEMTV 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 367 RQNL---ELHARLFHIPPAEIPARVAQMIERFMLTEVEDTLPASLPLGIRQRLSLAVAVIHRPEMLILDEPTSGVDPVAR 443
Cdd:PRK11288 97 AENLylgQLPHKGGIVNRRLLNYEAREQLEHLGVDIDPDTPLKYLSIGQRQMVEIAKALARNARVIAFDEPTSSLSAREI 176
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 446125071 444 DMFWQLMVDLSRQDKVTIFIStHFMNEAER-CDRMSLMHAGKVLAS 488
Cdd:PRK11288 177 EQLFRVIRELRAEGRVILYVS-HRMEEIFAlCDAITVFKDGRYVAT 221
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
22-439 |
1.76e-13 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 74.22 E-value: 1.76e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 22 YGKTVALNNITLDIPARSMVGLIGPDGVGKSSLLSLISGARVIEQGNVIvLGGDMRDAKHRRDVcPR---------IAWM 92
Cdd:PRK11147 13 FSDAPLLDNAELHIEDNERVCLVGRNGAGKSTLMKILNGEVLLDDGRII-YEQDLIVARLQQDP-PRnvegtvydfVAEG 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 93 PQGLGKNL--YHTLSvyenvdffaRLFGHDKAER--------------------EARITELLNSTGLAPfrDRPAGKLSG 150
Cdd:PRK11147 91 IEEQAEYLkrYHDIS---------HLVETDPSEKnlnelaklqeqldhhnlwqlENRINEVLAQLGLDP--DAALSSLSG 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 151 GMKQKLGLCCALIHDPELLILDEPTTGVDplsraqfwdlIDSI--------------------RQRQTNMS--------- 201
Cdd:PRK11147 160 GWLRKAALGRALVSNPDVLLLDEPTNHLD----------IETIewlegflktfqgsiifishdRSFIRNMAtrivdldrg 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 202 VLVA-----TAYM---EEAER--------FDWLVAM---------------NAGEILATGSAQQLRakthSATLEQ---A 247
Cdd:PRK11147 230 KLVSypgnyDQYLlekEEALRveelqnaeFDRKLAQeevwirqgikarrtrNEGRVRALKALRRER----SERREVmgtA 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 248 FIAlLPEAQRQAhkpvvippyhaeqeEIAIEAKDLTMRFGKFVAVDHVNFRIPRGEIFGFLGSNGCGKSTTMKMLTGLLP 327
Cdd:PRK11147 306 KMQ-VEEASRSG--------------KIVFEMENVNYQIDGKQLVKDFSAQVQRGDKIALIGPNGCGKTTLLKLMLGQLQ 370
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 328 ASEGQAwlfgqpvdpnDIDTRRRVGYMSQ-AFSLYNELTVRQNLelharlfhippAEIPARVaqMI---ERFMLTEVEDT 403
Cdd:PRK11147 371 ADSGRI----------HCGTKLEVAYFDQhRAELDPEKTVMDNL-----------AEGKQEV--MVngrPRHVLGYLQDF 427
|
490 500 510 520
....*....|....*....|....*....|....*....|....*
gi 446125071 404 L--P--ASLPL-----GIRQRLSLAVAVIHRPEMLILDEPTSGVD 439
Cdd:PRK11147 428 LfhPkrAMTPVkalsgGERNRLLLARLFLKPSNLLILDEPTNDLD 472
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
276-504 |
2.01e-13 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 74.77 E-value: 2.01e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 276 AIEAKDLTMRF-GKFVAVDH-VNFRIPRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGQAWlfgqpVDPNDI------DT 347
Cdd:PLN03130 1237 SIKFEDVVLRYrPELPPVLHgLSFEISPSEKVGIVGRTGAGKSSMLNALFRIVELERGRIL-----IDGCDIskfglmDL 1311
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 348 RRRVGYMSQAFSLYNElTVRQNLElharlfhiPPAE-IPARVAQMIERFMLTEVEDTLPASL-----------PLGIRQR 415
Cdd:PLN03130 1312 RKVLGIIPQAPVLFSG-TVRFNLD--------PFNEhNDADLWESLERAHLKDVIRRNSLGLdaevseagenfSVGQRQL 1382
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 416 LSLAVAVIHRPEMLILDEPTSGVDpVARDMFWQLMVdlsRQD--KVTIFISTHFMNEAERCDRMSLMHAGKVLASGTPQE 493
Cdd:PLN03130 1383 LSLARALLRRSKILVLDEATAAVD-VRTDALIQKTI---REEfkSCTMLIIAHRLNTIIDCDRILVLDAGRVVEFDTPEN 1458
|
250 260
....*....|....*....|..
gi 446125071 494 L-----------VQQRGAANLE 504
Cdd:PLN03130 1459 LlsnegsafskmVQSTGAANAQ 1480
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
23-568 |
2.02e-13 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 74.05 E-value: 2.02e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 23 GKTVALNNITLDIPARSMVGLIGPDGVGKSSLLSLISGARVIEQGNVIVLGGdmrdakhrrdvcPRIAWMPQGL------ 96
Cdd:PRK10636 12 GVRVLLDNATATINPGQKVGLVGKNGCGKSTLLALLKNEISADGGSYTFPGN------------WQLAWVNQETpalpqp 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 97 -------GKNLYHTLS-----VYENVDFFARLFGHDKAER------EARITELLNSTGLA-PFRDRPAGKLSGGMKQKLG 157
Cdd:PRK10636 80 aleyvidGDREYRQLEaqlhdANERNDGHAIATIHGKLDAidawtiRSRAASLLHGLGFSnEQLERPVSDFSGGWRMRLN 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 158 LCCALIHDPELLILDEPTTGVDplSRAQFW-------------------DLIDSIRQRQTNMSVLVATAYMEEAERFDWL 218
Cdd:PRK10636 160 LAQALICRSDLLLLDEPTNHLD--LDAVIWlekwlksyqgtlilishdrDFLDPIVDKIIHIEQQSLFEYTGNYSSFEVQ 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 219 VAMNAGEILATGSAQQ------------LRAKTHSATLEQAFIALLPEAQRQAHKPVVIPPYHAEQEEIAIEAKDLTMR- 285
Cdd:PRK10636 238 RATRLAQQQAMYESQQervahlqsyidrFRAKATKAKQAQSRIKMLERMELIAPAHVDNPFHFSFRAPESLPNPLLKMEk 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 286 ----FGKFVAVDHVNFRIPRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGQAWLfgqpvdPNDIdtrrRVGYMSQAFSLY 361
Cdd:PRK10636 318 vsagYGDRIILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELAPVSGEIGL------AKGI----KLGYFAQHQLEF 387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 362 neltVRQNLELHARLFHIPPAEIPARVAQMIERFMLTEVEDTLP-ASLPLGIRQRLSLAVAVIHRPEMLILDEPTSGVDP 440
Cdd:PRK10636 388 ----LRADESPLQHLARLAPQELEQKLRDYLGGFGFQGDKVTEEtRRFSGGEKARLVLALIVWQRPNLLLLDEPTNHLDL 463
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 441 VARDMFWQLMVDLsrqDKVTIFIS--THFMNEAerCDRMSLMHAGKVLASGTPQELVQQrgaanleaaFISWLQEAAGAA 518
Cdd:PRK10636 464 DMRQALTEALIDF---EGALVVVShdRHLLRST--TDDLYLVHDGKVEPFDGDLEDYQQ---------WLSDVQKQENQT 529
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|..
gi 446125071 519 PETPIPPSQTPAASGKPSRqglsfrrlfsysRREAlELRR--DPVRSTLALL 568
Cdd:PRK10636 530 DEAPKENNANSAQARKDQK------------RREA-ELRTqtQPLRKEIARL 568
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
186-541 |
2.37e-13 |
|
multi drug resistance-associated protein (MRP); This model describes multi drug resistance-associated protein (MRP) in eukaryotes. The multidrug resistance-associated protein is an integral membrane protein that causes multidrug resistance when overexpressed in mammalian cells. It belongs to ABC transporter superfamily. The protein topology and function was experimentally demonstrated by epitope tagging and immunofluorescence. Insertion of tags in the critical regions associated with drug efflux, abrogated its function. The C-terminal domain seem to highly conserved. [Transport and binding proteins, Other]
Pssm-ID: 188098 [Multi-domain] Cd Length: 1522 Bit Score: 74.60 E-value: 2.37e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 186 FWDLIDSIRQRQtnMSVLVATAYMEEAERFDW-----LVAMNAGEILATGSAQQ-LRAKTHSATLEQAFIALLP------ 253
Cdd:TIGR00957 518 FLDKVEGIRQEE--LKVLKKSAYLHAVGTFTWvctpfLVALITFAVYVTVDENNiLDAEKAFVSLALFNILRFPlnilpm 595
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 254 --EAQRQAH---KPVVIPPYHAEQEEIAIEAK--------DLTMRFGKFV-------AVDHVNFRIPRGEIFGFLGSNGC 313
Cdd:TIGR00957 596 viSSIVQASvslKRLRIFLSHEELEPDSIERRtikpgegnSITVHNATFTwardlppTLNGITFSIPEGALVAVVGQVGC 675
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 314 GKSTTMKMLTGLLPASEGQAWLFGQpvdpndidtrrrVGYMSQAFSLYNElTVRQNLelharLFHIPPAeiPARVAQMIE 393
Cdd:TIGR00957 676 GKSSLLSALLAEMDKVEGHVHMKGS------------VAYVPQQAWIQND-SLRENI-----LFGKALN--EKYYQQVLE 735
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 394 RFMLTEVEDTLPA-----------SLPLGIRQRLSLAVAVIHRPEMLILDEPTSGVDP-VARDMFWQLMVDLSRQDKVTI 461
Cdd:TIGR00957 736 ACALLPDLEILPSgdrteigekgvNLSGGQKQRVSLARAVYSNADIYLFDDPLSAVDAhVGKHIFEHVIGPEGVLKNKTR 815
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 462 FISTHFMNEAERCDRMSLMHAGKVLASGTPQELVQQRGA-ANLEAAFISwlQEAAGAAPETPIPPSQTPAASGKPSRQGL 540
Cdd:TIGR00957 816 ILVTHGISYLPQVDVIIVMSGGKISEMGSYQELLQRDGAfAEFLRTYAP--DEQQGHLEDSWTALVSGEGKEAKLIENGM 893
|
.
gi 446125071 541 S 541
Cdd:TIGR00957 894 L 894
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
296-500 |
2.89e-13 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 73.99 E-value: 2.89e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 296 NFRIPRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGQAWLFGQP-VDPNDIDTRRRVGYMSQAFSLYNElTVRQNLELHa 374
Cdd:TIGR00958 501 TFTLHPGEVVALVGPSGSGKSTVAALLQNLYQPTGGQVLLDGVPlVQYDHHYLHRQVALVGQEPVLFSG-SVRENIAYG- 578
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 375 rLFHIPPAEIPARVAQMIERFMLTEVEDTLPAS-------LPLGIRQRLSLAVAVIHRPEMLILDEPTSGVDPVARDMFW 447
Cdd:TIGR00958 579 -LTDTPDEEIMAAAKAANAHDFIMEFPNGYDTEvgekgsqLSGGQKQRIAIARALVRKPRVLILDEATSALDAECEQLLQ 657
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 446125071 448 QLMvdlSRQDKVTIFIsTHFMNEAERCDRMSLMHAGKVLASGTPQELVQQRGA 500
Cdd:TIGR00958 658 ESR---SRASRTVLLI-AHRLSTVERADQILVLKKGSVVEMGTHKQLMEDQGC 706
|
|
| tagH |
PRK13545 |
teichoic acids export protein ATP-binding subunit; Provisional |
280-500 |
3.00e-13 |
|
teichoic acids export protein ATP-binding subunit; Provisional
Pssm-ID: 184130 [Multi-domain] Cd Length: 549 Bit Score: 73.39 E-value: 3.00e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 280 KDLTMRFGKFV---AVDHVNFRIPRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGQawlfgqpvdpndIDTRRRVGYMSQ 356
Cdd:PRK13545 25 KDLFFRSKDGEyhyALNNISFEVPEGEIVGIIGLNGSGKSTLSNLIAGVTMPNKGT------------VDIKGSAALIAI 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 357 AFSLYNELTVRQNLELHARLFHIPPAEIPARVAQMIE-----RFMLTEVEdtlpaSLPLGIRQRLSLAVAVIHRPEMLIL 431
Cdd:PRK13545 93 SSGLNGQLTGIENIELKGLMMGLTKEKIKEIIPEIIEfadigKFIYQPVK-----TYSSGMKSRLGFAISVHINPDILVI 167
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 432 DEPTSGVDPVARDMFWQLMVDLSRQDKvTIFISTHFMNEAER-CDRMSLMHAGKVLASGTPQELVQQRGA 500
Cdd:PRK13545 168 DEALSVGDQTFTKKCLDKMNEFKEQGK-TIFFISHSLSQVKSfCTKALWLHYGQVKEYGDIKEVVDHYDE 236
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
32-214 |
3.00e-13 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 70.00 E-value: 3.00e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 32 TLDIPARSMVGLIGPDGVGKSSLLSLISGARVIEQGNVIVLGGDMRD-AKHRRDVcpriAWMPQGlgKNLYHTLSVYENV 110
Cdd:PRK10771 19 DLTVERGERVAILGPSGAGKSTLLNLIAGFLTPASGSLTLNGQDHTTtPPSRRPV----SMLFQE--NNLFSHLTVAQNI 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 111 ----DFFARLfghdKAEREARITELLNSTGLAPFRDRPAGKLSGGMKQKLGLCCALIHDPELLILDEPTTGVDPLSRAQF 186
Cdd:PRK10771 93 glglNPGLKL----NAAQREKLHAIARQMGIEDLLARLPGQLSGGQRQRVALARCLVREQPILLLDEPFSALDPALRQEM 168
|
170 180
....*....|....*....|....*....
gi 446125071 187 WDLIDSI-RQRQtnMSVLVATAYMEEAER 214
Cdd:PRK10771 169 LTLVSQVcQERQ--LTLLMVSHSLEDAAR 195
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
14-255 |
3.43e-13 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 73.60 E-value: 3.43e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 14 QLEGVSQHY----GKTVALNNITLDIPARSMVGLIGPDGVGKSSLLSLI-------SGARVIEQGNVIVLGGDMRdAKHR 82
Cdd:PRK10535 6 ELKDIRRSYpsgeEQVEVLKGISLDIYAGEMVAIVGASGSGKSTLMNILgcldkptSGTYRVAGQDVATLDADAL-AQLR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 83 RDVCpriawmpqGLGKNLYHTLS---VYENVDFFARLFGHDKAEREARITELLNSTGLAPFRDRPAGKLSGGMKQKLGLC 159
Cdd:PRK10535 85 REHF--------GFIFQRYHLLShltAAQNVEVPAVYAGLERKQRLLRAQELLQRLGLEDRVEYQPSQLSGGQQQRVSIA 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 160 CALIHDPELLILDEPTTGVDPLSRAQFWDLIDSIRQRqtNMSVLVATAYMEEAERFDWLVAMNAGEILATGSAQQLR--- 236
Cdd:PRK10535 157 RALMNGGQVILADEPTGALDSHSGEEVMAILHQLRDR--GHTVIIVTHDPQVAAQAERVIEIRDGEIVRNPPAQEKVnva 234
|
250 260
....*....|....*....|...
gi 446125071 237 ----AKTHSATLEQAFIALLPEA 255
Cdd:PRK10535 235 ggtePVVNTASGWRQFVSGFREA 257
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
33-439 |
4.00e-13 |
|
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: 73.28 E-value: 4.00e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 33 LDIPARSMV-GLIGPDGVGKSSLLSLISGA---------------RVIE--QGNVI------VLGGDMRdakhrrdvcpr 88
Cdd:COG1245 93 LPVPKKGKVtGILGPNGIGKSTALKILSGElkpnlgdydeepswdEVLKrfRGTELqdyfkkLANGEIK----------- 161
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 89 IAWMPQglgknlyhtlsvyeNVDFFARLF-GH-----DKAEREARITELLNSTGLAPFRDRPAGKLSGGMKQKLGLCCAL 162
Cdd:COG1245 162 VAHKPQ--------------YVDLIPKVFkGTvrellEKVDERGKLDELAEKLGLENILDRDISELSGGELQRVAIAAAL 227
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 163 IHDPELLILDEPTTGVDplsraqfwdlidsIRQRqtnmsVLVATAYMEEAER-------------FDWL---VAMNAGEI 226
Cdd:COG1245 228 LRDADFYFFDEPSSYLD-------------IYQR-----LNVARLIRELAEEgkyvlvvehdlaiLDYLadyVHILYGEP 289
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 227 LATGSAQQLRAkTHSATleQAFIA-LLPEAQ-RQAHKPV---VIPPYHAEQEEIAIEAKDLTMRFGKF-VAVDHVNFRip 300
Cdd:COG1245 290 GVYGVVSKPKS-VRVGI--NQYLDgYLPEENvRIRDEPIefeVHAPRREKEEETLVEYPDLTKSYGGFsLEVEGGEIR-- 364
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 301 RGEIFGFLGSNGCGKSTTMKMLTGLLPASEGqawlfgqpvdpnDIDTRRRVGYMSQAFSLYNELTVRQNLElharlfhip 380
Cdd:COG1245 365 EGEVLGIVGPNGIGKTTFAKILAGVLKPDEG------------EVDEDLKISYKPQYISPDYDGTVEEFLR--------- 423
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446125071 381 pAEIPARV------AQMIERFMLTEVEDTLPASLPLGIRQRLSLAVAVIHRPEMLILDEPTSGVD 439
Cdd:COG1245 424 -SANTDDFgssyykTEIIKPLGLEKLLDKNVKDLSGGELQRVAIAACLSRDADLYLLDEPSAHLD 487
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
277-500 |
6.61e-13 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 72.36 E-value: 6.61e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 277 IEAKDLTMRF-GKFV-AVDHVNFRIPRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGQAWLFGqpVDPNDI---DTRRRV 351
Cdd:PRK11176 342 IEFRNVTFTYpGKEVpALRNINFKIPAGKTVALVGRSGSGKSTIANLLTRFYDIDEGEILLDG--HDLRDYtlaSLRNQV 419
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 352 GYMSQAFSLYNElTVRQNLElHARLFHIPPAEI--PARVAQMIErFM--LTEVEDTL----PASLPLGIRQRLSLAVAVI 423
Cdd:PRK11176 420 ALVSQNVHLFND-TIANNIA-YARTEQYSREQIeeAARMAYAMD-FInkMDNGLDTVigenGVLLSGGQRQRIAIARALL 496
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446125071 424 HRPEMLILDEPTSGVDpVARDMFWQLMVDLSRQDKVTIFIStHFMNEAERCDRMSLMHAGKVLASGTPQELVQQRGA 500
Cdd:PRK11176 497 RDSPILILDEATSALD-TESERAIQAALDELQKNRTSLVIA-HRLSTIEKADEILVVEDGEIVERGTHAELLAQNGV 571
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
295-501 |
9.94e-13 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 72.70 E-value: 9.94e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 295 VNFRIPRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGQAWlfgqpVDPNDI------DTRRRVGYMSQAFSLYNElTVRQ 368
Cdd:PLN03232 1255 LSFFVSPSEKVGVVGRTGAGKSSMLNALFRIVELEKGRIM-----IDDCDVakfgltDLRRVLSIIPQSPVLFSG-TVRF 1328
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 369 NLElharlfhiPPAE-IPARVAQMIERFMLTEVEDTLP-----------ASLPLGIRQRLSLAVAVIHRPEMLILDEPTS 436
Cdd:PLN03232 1329 NID--------PFSEhNDADLWEALERAHIKDVIDRNPfgldaevseggENFSVGQRQLLSLARALLRRSKILVLDEATA 1400
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446125071 437 GVDpVARDMFWQLMVdlsRQD--KVTIFISTHFMNEAERCDRMSLMHAGKVLASGTPQELVQQRGAA 501
Cdd:PLN03232 1401 SVD-VRTDSLIQRTI---REEfkSCTMLVIAHRLNTIIDCDKILVLSSGQVLEYDSPQELLSRDTSA 1463
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
277-434 |
1.54e-12 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 67.52 E-value: 1.54e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 277 IEAKDLTMRFGKFVAVDHVNFRIPRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGQAWLFGQPVDPNDIDTRRRVGYMSQ 356
Cdd:PRK13538 2 LEARNLACERDERILFSGLSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVLWQGEPIRRQRDEYHQDLLYLGH 81
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446125071 357 AFSLYNELTVRQNLELHARLFHIPPAEipaRVAQMIERFMLTEVEDTLPASLPLGIRQRLSLAVAVIHRPEMLILDEP 434
Cdd:PRK13538 82 QPGIKTELTALENLRFYQRLHGPGDDE---ALWEALAQVGLAGFEDVPVRQLSAGQQRRVALARLWLTRAPLWILDEP 156
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
273-494 |
1.58e-12 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 68.65 E-value: 1.58e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 273 EEIaIEAKDLTMRFGKFVAVDHVNFRIPRGEIFGFLGSNGCGKSTTMKMLT---GLLP--ASEGQAWLFGQPVDPNDIDT 347
Cdd:PRK14239 3 EPI-LQVSDLSVYYNKKKALNSVSLDFYPNEITALIGPSGSGKSTLLRSINrmnDLNPevTITGSIVYNGHNIYSPRTDT 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 348 ---RRRVGYMSQA-----FSLYneltvrQNLELHARLFHIPPAEIPARVAQ--MIERFMLTEVEDTLPAS---LPLGIRQ 414
Cdd:PRK14239 82 vdlRKEIGMVFQQpnpfpMSIY------ENVVYGLRLKGIKDKQVLDEAVEksLKGASIWDEVKDRLHDSalgLSGGQQQ 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 415 RLSLAVAVIHRPEMLILDEPTSGVDPVARDMFWQLMVDLsrQDKVTIFISTHFMNEAER-CDRMSLMHAGKVLASGTPQE 493
Cdd:PRK14239 156 RVCIARVLATSPKIILLDEPTSALDPISAGKIEETLLGL--KDDYTMLLVTRSMQQASRiSDRTGFFLDGDLIEYNDTKQ 233
|
.
gi 446125071 494 L 494
Cdd:PRK14239 234 M 234
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
18-196 |
1.88e-12 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 70.89 E-value: 1.88e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 18 VSQHYgktvALNNITLDIPARSMVGLIGPDGVGKSS----LLSLISgarviEQGNvIVLGGDMRDAKHRRDVCP---RIA 90
Cdd:PRK15134 296 VDHNV----VVKNISFTLRPGETLGLVGESGSGKSTtglaLLRLIN-----SQGE-IWFDGQPLHNLNRRQLLPvrhRIQ 365
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 91 WMPQGLGKNLYHTLSVYENVDFFARLfgHDK----AEREARITELLNSTGLAP-FRDRPAGKLSGGMKQKLGLCCALIHD 165
Cdd:PRK15134 366 VVFQDPNSSLNPRLNVLQIIEEGLRV--HQPtlsaAQREQQVIAVMEEVGLDPeTRHRYPAEFSGGQRQRIAIARALILK 443
|
170 180 190
....*....|....*....|....*....|.
gi 446125071 166 PELLILDEPTTGVDPLSRAQFWDLIDSIRQR 196
Cdd:PRK15134 444 PSLIILDEPTSSLDKTVQAQILALLKSLQQK 474
|
|
| BtuD |
COG4138 |
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ... |
28-258 |
2.55e-12 |
|
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism];
Pssm-ID: 443313 [Multi-domain] Cd Length: 248 Bit Score: 67.94 E-value: 2.55e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 28 LNNITLDIPARSMVGLIGPDGVGKSSLLSLISGArVIEQGNVIVLGGDMRD------AKHRrdvcpriAWMPQglgknly 101
Cdd:COG4138 12 LGPISAQVNAGELIHLIGPNGAGKSTLLARMAGL-LPGQGEILLNGRPLSDwsaaelARHR-------AYLSQ------- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 102 HTLS-----VYENVDFFARLfGHDKAEREARITELLNSTGLAPFRDRPAGKLSGGMKQKLGLCCAL--IH---DPE--LL 169
Cdd:COG4138 77 QQSPpfampVFQYLALHQPA-GASSEAVEQLLAQLAEALGLEDKLSRPLTQLSGGEWQRVRLAAVLlqVWptiNPEgqLL 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 170 ILDEPTTGVDPLSRAQFWDLIDSIRQRQtnMSVLVATAYMEEAERF-D--WLvaMNAGEILATGSAQQ-LRAKTHSATLE 245
Cdd:COG4138 156 LLDEPMNSLDVAQQAALDRLLRELCQQG--ITVVMSSHDLNHTLRHaDrvWL--LKQGKLVASGETAEvMTPENLSEVFG 231
|
250
....*....|...
gi 446125071 246 QAFIALLPEAQRQ 258
Cdd:COG4138 232 VKFRRLEVEGHRW 244
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
28-204 |
2.58e-12 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 67.50 E-value: 2.58e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 28 LNNITLDIPARSMVGLIGPDGVGKSSLLSLISGARVIEQGNVIVLGGDMrdakHRRDVCPRIAWMPQGLGK-----NLYH 102
Cdd:PRK10584 26 LTGVELVVKRGETIALIGESGSGKSTLLAILAGLDDGSSGEVSLVGQPL----HQMDEEARAKLRAKHVGFvfqsfMLIP 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 103 TLSVYENVDFFARLFGHDKAEREARITELLNSTGLAPFRDRPAGKLSGGMKQKLGLCCALIHDPELLILDEPTTGVDPLS 182
Cdd:PRK10584 102 TLNALENVELPALLRGESSRQSRNGAKALLEQLGLGKRLDHLPAQLSGGEQQRVALARAFNGRPDVLFADEPTGNLDRQT 181
|
170 180
....*....|....*....|..
gi 446125071 183 RAQFWDLIDSIRQRQTNMSVLV 204
Cdd:PRK10584 182 GDKIADLLFSLNREHGTTLILV 203
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
14-238 |
2.68e-12 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 70.52 E-value: 2.68e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 14 QLEGVSQHYGK-TVALNNITLDIPARSMVGLIGPDGVGKSSLLSLISGARVIEQGNVIVLGGDMRDAKHR--RDVCPRIA 90
Cdd:PRK10790 342 DIDNVSFAYRDdNLVLQNINLSVPSRGFVALVGHTGSGKSTLASLLMGYYPLTEGEIRLDGRPLSSLSHSvlRQGVAMVQ 421
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 91 WMPQGLGKnlyhtlSVYENVDffarlFGHDKAerEARITELLNSTGLAPF-RDRPAG----------KLSGGMKQKLGLC 159
Cdd:PRK10790 422 QDPVVLAD------TFLANVT-----LGRDIS--EEQVWQALETVQLAELaRSLPDGlytplgeqgnNLSVGQKQLLALA 488
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 160 CALIHDPELLILDEPTTGVDPLSRAQFWDLIDSIRQRQTnmsvLVATAY----MEEAerfDWLVAMNAGEILATGSAQQL 235
Cdd:PRK10790 489 RVLVQTPQILILDEATANIDSGTEQAIQQALAAVREHTT----LVVIAHrlstIVEA---DTILVLHRGQAVEQGTHQQL 561
|
...
gi 446125071 236 RAK 238
Cdd:PRK10790 562 LAA 564
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
302-466 |
3.59e-12 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 70.29 E-value: 3.59e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 302 GEIFGFLGSNGCGKSTTMKMLTGLLPASEGQAWLF---GQPVDPndidTRRRVGYMSQAFSLYNELTVRQNLeLHARLFH 378
Cdd:PLN03211 94 GEILAVLGPSGSGKSTLLNALAGRIQGNNFTGTILannRKPTKQ----ILKRTGFVTQDDILYPHLTVRETL-VFCSLLR 168
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 379 IPPA---EIPARVAQ-MIERFMLTEVEDTLPA-SLPLGI----RQRLSLAVAVIHRPEMLILDEPTSGVDPVARDMFWQL 449
Cdd:PLN03211 169 LPKSltkQEKILVAEsVISELGLTKCENTIIGnSFIRGIsggeRKRVSIAHEMLINPSLLILDEPTSGLDATAAYRLVLT 248
|
170
....*....|....*..
gi 446125071 450 MVDLSRQDKvTIFISTH 466
Cdd:PLN03211 249 LGSLAQKGK-TIVTSMH 264
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
25-226 |
4.14e-12 |
|
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; TAP (Transporter Associated with Antigen Processing) is essential for peptide delivery from the cytosol into the lumen of the endoplasmic reticulum (ER), where these peptides are loaded on major histocompatibility complex (MHC) I molecules. Loaded MHC I leave the ER and display their antigenic cargo on the cell surface to cytotoxic T cells. Subsequently, virus-infected or malignantly transformed cells can be eliminated. TAP belongs to the large family of ATP-binding cassette (ABC) transporters, which translocate a vast variety of solutes across membranes.
Pssm-ID: 213215 [Multi-domain] Cd Length: 226 Bit Score: 66.73 E-value: 4.14e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 25 TVALNNITLDIPARSMVGLIGPDGVGKSSLLSLISGARVIEQGNVIVLGGDMRDAKHR--RDVCPRIAWMPQGLGKNLYH 102
Cdd:cd03248 27 TLVLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDGKPISQYEHKylHSKVSLVGQEPVLFARSLQD 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 103 TLSV-YENVDFFARLFGHDKAEREARITELlnSTGLAPFRDRPAGKLSGGMKQKLGLCCALIHDPELLILDEPTTGVDPL 181
Cdd:cd03248 107 NIAYgLQSCSFECVKEAAQKAHAHSFISEL--ASGYDTEVGEKGSQLSGGQKQRVAIARALIRNPQVLILDEATSALDAE 184
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 446125071 182 SRAQFWDLIDSIRQRQTnmsVLVATAYMEEAERFDWLVAMNAGEI 226
Cdd:cd03248 185 SEQQVQQALYDWPERRT---VLVIAHRLSTVERADQILVLDGGRI 226
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
265-494 |
4.36e-12 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 69.88 E-value: 4.36e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 265 IPPYHAEQEEIAIEAKDLTMRF----GKFVAVDHVNFRIPRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGQawlfgqpV 340
Cdd:PRK10261 1 MPHSDELDARDVLAVENLNIAFmqeqQKIAAVRNLSFSLQRGETLAIVGESGSGKSVTALALMRLLEQAGGL-------V 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 341 DPNDIDTRRR------VGYMSQA------------------FSLYNELTVRQNLELHARLFH-IPPAEIPARVAQMIERF 395
Cdd:PRK10261 74 QCDKMLLRRRsrqvieLSEQSAAqmrhvrgadmamifqepmTSLNPVFTVGEQIAESIRLHQgASREEAMVEAKRMLDQV 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 396 MLTEVEDTL---PASLPLGIRQRLSLAVAVIHRPEMLILDEPTSGVDPVARDMFWQLMVDLSRQDKVTIFISTHFMNE-A 471
Cdd:PRK10261 154 RIPEAQTILsryPHQLSGGMRQRVMIAMALSCRPAVLIADEPTTALDVTIQAQILQLIKVLQKEMSMGVIFITHDMGVvA 233
|
250 260
....*....|....*....|...
gi 446125071 472 ERCDRMSLMHAGKVLASGTPQEL 494
Cdd:PRK10261 234 EIADRVLVMYQGEAVETGSVEQI 256
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
11-185 |
4.48e-12 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 68.22 E-value: 4.48e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 11 PVAQLEGVSQHY-------GKTV----ALNNITLDIPARSMVGLIGPDGVGKSSLLSLIsgARVIE--QGNVIVLGGDMR 77
Cdd:COG4608 6 PLLEVRDLKKHFpvrgglfGRTVgvvkAVDGVSFDIRRGETLGLVGESGCGKSTLGRLL--LRLEEptSGEILFDGQDIT 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 78 DAKHR--RDVCPRIAWMPQglgkNLYHTL----SVYENVDFFARLFG-HDKAEREARITELLNSTGLAP-FRDRPAGKLS 149
Cdd:COG4608 84 GLSGRelRPLRRRMQMVFQ----DPYASLnprmTVGDIIAEPLRIHGlASKAERRERVAELLELVGLRPeHADRYPHEFS 159
|
170 180 190
....*....|....*....|....*....|....*..
gi 446125071 150 GGMKQKLGLCCALIHDPELLILDEPTTGVDpLS-RAQ 185
Cdd:COG4608 160 GGQRQRIGIARALALNPKLIVCDEPVSALD-VSiQAQ 195
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
11-226 |
5.67e-12 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 66.38 E-value: 5.67e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 11 PVAQLEGVSQHY--GK--TVALNNITLDIPARSMVGLIGPDGVGKSSLLSLISGARVIEQGNVIVLGGDMRDAKHRrdvc 86
Cdd:PRK11629 4 ILLQCDNLCKRYqeGSvqTDVLHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPMSKLSSA---- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 87 PRIAWMPQGLG--KNLYHTL---SVYENVDFFARLFGHDKAEREARITELLNSTGLAPFRDRPAGKLSGGMKQKLGLCCA 161
Cdd:PRK11629 80 AKAELRNQKLGfiYQFHHLLpdfTALENVAMPLLIGKKKPAEINSRALEMLAAVGLEHRANHRPSELSGGERQRVAIARA 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446125071 162 LIHDPELLILDEPTTGVDPLSRAQFWDLIDSIRQRQtNMSVLVATAYMEEAERFDWLVAMNAGEI 226
Cdd:PRK11629 160 LVNNPRLVLADEPTGNLDARNADSIFQLLGELNRLQ-GTAFLVVTHDLQLAKRMSRQLEMRDGRL 223
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
28-234 |
5.76e-12 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 69.26 E-value: 5.76e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 28 LNNITLDIPARSMVGLIGPDGVGKSSLLSLISGARVIEQGNVIVLGgdmrdakhrRDVCPRiawMPQ-GL---------- 96
Cdd:PRK10762 268 VNDVSFTLRKGEILGVSGLMGAGRTELMKVLYGALPRTSGYVTLDG---------HEVVTR---SPQdGLangivyised 335
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 97 --GKNLYHTLSVYEN-----VDFFARLFGH--DKAEREA--RITELLNSTglAPFRDRPAGKLSGGMKQKLGLCCALIHD 165
Cdd:PRK10762 336 rkRDGLVLGMSVKENmsltaLRYFSRAGGSlkHADEQQAvsDFIRLFNIK--TPSMEQAIGLLSGGNQQKVAIARGLMTR 413
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 166 PELLILDEPTTGVDPLSRAQFWDLIDSIRQRqtNMSVLVATAYMEEAERF-DWLVAMNAGEILATGSAQQ 234
Cdd:PRK10762 414 PKVLILDEPTRGVDVGAKKEIYQLINQFKAE--GLSIILVSSEMPEVLGMsDRILVMHEGRISGEFTREQ 481
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
26-200 |
6.29e-12 |
|
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion transport and metabolism];
Pssm-ID: 443809 [Multi-domain] Cd Length: 229 Bit Score: 66.30 E-value: 6.29e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 26 VALNNITLDIPARSMVGLIGPDGVGKSSLLSLISGARVIEQGNVIVLGG----DMRDAKHRR----------------DV 85
Cdd:COG4778 25 PVLDGVSFSVAAGECVALTGPSGAGKSTLLKCIYGNYLPDSGSILVRHDggwvDLAQASPREilalrrrtigyvsqflRV 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 86 CPRIAwmpqglgknlyhTLSVYENVdffARLFGHDKAEREARITELLNSTGLaPFR--DRPAGKLSGGMKQKLGLCCALI 163
Cdd:COG4778 105 IPRVS------------ALDVVAEP---LLERGVDREEARARARELLARLNL-PERlwDLPPATFSGGEQQRVNIARGFI 168
|
170 180 190
....*....|....*....|....*....|....*..
gi 446125071 164 HDPELLILDEPTTGVDPLSRAQFWDLIDSIRQRQTNM 200
Cdd:COG4778 169 ADPPLLLLDEPTASLDAANRAVVVELIEEAKARGTAI 205
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
10-254 |
7.04e-12 |
|
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: 68.94 E-value: 7.04e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 10 PPVAQLEGVSQHY-------GKTV----ALNNITLDIPARSMVGLIGPDGVGKSSL----LSLISGarvieQGNVIVLGG 74
Cdd:COG4172 273 PPLLEARDLKVWFpikrglfRRTVghvkAVDGVSLTLRRGETLGLVGESGSGKSTLglalLRLIPS-----EGEIRFDGQ 347
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 75 DMRDAKH------RRDV-----------CPR------IAwmpQGLgknlyHTLSVyenvdffarlfGHDKAEREARITEL 131
Cdd:COG4172 348 DLDGLSRralrplRRRMqvvfqdpfgslSPRmtvgqiIA---EGL-----RVHGP-----------GLSAAERRARVAEA 408
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 132 LNSTGLAP-FRDRPAGKLSGGMKQKLGLCCALIHDPELLILDEPTTGVDPLSRAQFWDLIDSIrQRQTNMSVLVAT---- 206
Cdd:COG4172 409 LEEVGLDPaARHRYPHEFSGGQRQRIAIARALILEPKLLVLDEPTSALDVSVQAQILDLLRDL-QREHGLAYLFIShdla 487
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 446125071 207 --AYMEeaerfDWLVAMNAGEILATGSAQQ-LRAKTHSATleQAFIALLPE 254
Cdd:COG4172 488 vvRALA-----HRVMVMKDGKVVEQGPTEQvFDAPQHPYT--RALLAAAPL 531
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
28-238 |
8.30e-12 |
|
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 (also known as ABCB6) is a mitochondrial ATP-binding cassette protein involved in iron homeostasis and one of four ABC transporters expressed in the mitochondrial inner membrane, the other three being MDL1(ABC7), MDL2, and ATM1. In fact, the yeast MDL1 (multidrug resistance-like protein 1) and MDL2 (multidrug resistance-like protein 2) transporters are also included in this CD. MDL1 is an ATP-dependent permease that acts as a high-copy suppressor of ATM1 and is thought to have a role in resistance to oxidative stress. Interestingly, subfamily B is more closely related to the carboxyl-terminal component of subfamily C than the two halves of ABCC molecules are with one another.
Pssm-ID: 213216 [Multi-domain] Cd Length: 238 Bit Score: 66.02 E-value: 8.30e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 28 LNNITLDIPARSMVGLIGPDGVGKSSLLSLISGARVIEQGNVIVLGGDMRD--AKHRRDvcpRIAWMPQGlgKNLYHTlS 105
Cdd:cd03249 19 LKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEILLDGVDIRDlnLRWLRS---QIGLVSQE--PVLFDG-T 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 106 VYENV---DFFARLFGHDKAEREARITELLNStgLAPFRDRPAG----KLSGGMKQKLGLCCALIHDPELLILDEPTTGV 178
Cdd:cd03249 93 IAENIrygKPDATDEEVEEAAKKANIHDFIMS--LPDGYDTLVGergsQLSGGQKQRIAIARALLRNPKILLLDEATSAL 170
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446125071 179 DPLSRAQFWDLIDSIRQRQTNMSVlvataymeeAERF------DWLVAMNAGEILATGSAQQLRAK 238
Cdd:cd03249 171 DAESEKLVQEALDRAMKGRTTIVI---------AHRLstirnaDLIAVLQNGQVVEQGTHDELMAQ 227
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
27-225 |
1.03e-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: 65.18 E-value: 1.03e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 27 ALNNITLDIPARSMVGLIGPDGVGKSSLLSLISGARVIEQGNVIVLGgdmRDAkhrrdVCPRIAWMPQGlgknlyhtlSV 106
Cdd:cd03250 20 TLKDINLEVPKGELVAIVGPVGSGKSSLLSALLGELEKLSGSVSVPG---SIA-----YVSQEPWIQNG---------TI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 107 YENVdffarLFGHDkaEREARITELLNSTGLAP-FRDRPAG----------KLSGGMKQKLGLCCALIHDPELLILDEPT 175
Cdd:cd03250 83 RENI-----LFGKP--FDEERYEKVIKACALEPdLEILPDGdlteigekgiNLSGGQKQRISLARAVYSDADIYLLDDPL 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 446125071 176 TGVDPLSRAQFWD--LIDSIRQRQTnmsVLVATAYMEEAERFDWLVAMNAGE 225
Cdd:cd03250 156 SAVDAHVGRHIFEncILGLLLNNKT---RILVTHQLQLLPHADQIVVLDNGR 204
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
11-230 |
1.28e-11 |
|
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in methanogenesis, methyl coenzyme M reductase, contains alpha, beta, and gamma chains. In older literature, the complex of alpha, beta, and gamma chains was termed component C, while this single chain protein was termed methyl coenzyme M reductase system component A2. [Energy metabolism, Methanogenesis]
Pssm-ID: 132313 [Multi-domain] Cd Length: 520 Bit Score: 68.29 E-value: 1.28e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 11 PVAQLEGVSQHY-----GKTVALNNITLDIPARSMVGLIGPDGVGKSSLLSLISGARVIEQGNVIVLGG----DMRD--A 79
Cdd:TIGR03269 278 PIIKVRNVSKRYisvdrGVVKAVDNVSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGEVNVRVGdewvDMTKpgP 357
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 80 KHRRDVCPRIAWMPQGLGknLYHTLSVYENV-DFFARLFGHDKAEREARITelLNSTGLAPFR-----DRPAGKLSGGMK 153
Cdd:TIGR03269 358 DGRGRAKRYIGILHQEYD--LYPHRTVLDNLtEAIGLELPDELARMKAVIT--LKMVGFDEEKaeeilDKYPDELSEGER 433
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446125071 154 QKLGLCCALIHDPELLILDEPTTGVDPLSRAQFWDLIDSIRQrQTNMSVLVATAYMEEA-ERFDWLVAMNAGEILATG 230
Cdd:TIGR03269 434 HRVALAQVLIKEPRIVILDEPTGTMDPITKVDVTHSILKARE-EMEQTFIIVSHDMDFVlDVCDRAALMRDGKIVKIG 510
|
|
| PRK13546 |
PRK13546 |
teichoic acids export ABC transporter ATP-binding subunit TagH; |
268-485 |
1.29e-11 |
|
teichoic acids export ABC transporter ATP-binding subunit TagH;
Pssm-ID: 184131 [Multi-domain] Cd Length: 264 Bit Score: 65.99 E-value: 1.29e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 268 YHAEQEEIaieaKDLTMRFGK---FVAVDHVNFRIPRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGqawlfgqpvdpnD 344
Cdd:PRK13546 17 YRTNKERM----KDALIPKHKnktFFALDDISLKAYEGDVIGLVGINGSGKSTLSNIIGGSLSPTVG------------K 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 345 IDTRRRVGYMSQAFSLYNELTVRQNLELHARLFHIPPAEIPARVAQMIERFMLTEVEDTLPASLPLGIRQRLSLAVAVIH 424
Cdd:PRK13546 81 VDRNGEVSVIAISAGLSGQLTGIENIEFKMLCMGFKRKEIKAMTPKIIEFSELGEFIYQPVKKYSSGMRAKLGFSINITV 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446125071 425 RPEMLILDEPTSGVDPVARDMFWQLMVDLSRQDKVTIFISTHFMNEAERCDRMSLMHAGKV 485
Cdd:PRK13546 161 NPDILVIDEALSVGDQTFAQKCLDKIYEFKEQNKTIFFVSHNLGQVRQFCTKIAWIEGGKL 221
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
23-234 |
1.34e-11 |
|
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: 68.24 E-value: 1.34e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 23 GKTVALNNITLDIPARSMVGLIGPDGVGKSSLLSLISGARVIEQGNVIVLGGDMRDAkHRRDVCPRIAWMPQGLGknlyh 102
Cdd:COG4618 343 SKRPILRGVSFSLEPGEVLGVIGPSGSGKSTLARLLVGVWPPTAGSVRLDGADLSQW-DREELGRHIGYLPQDVE----- 416
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 103 tL---SVYENVdffARLFGHD-----KAEREARITEL-----------LNSTGLApfrdrpagkLSGGMKQKLGLCCALI 163
Cdd:COG4618 417 -LfdgTIAENI---ARFGDADpekvvAAAKLAGVHEMilrlpdgydtrIGEGGAR---------LSGGQRQRIGLARALY 483
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446125071 164 HDPELLILDEPTTGVDPLSRAQFWDLIDSIRQRQTnmSVLVAT---AYMEEAerfDWLVAMNAGEILATGSAQQ 234
Cdd:COG4618 484 GDPRLVVLDEPNSNLDDEGEAALAAAIRALKARGA--TVVVIThrpSLLAAV---DKLLVLRDGRVQAFGPRDE 552
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
295-485 |
1.55e-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: 65.18 E-value: 1.55e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 295 VNFRIPRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGQAWLFGQPVdpNDIDTR---RRVGYMSQAFSLYNElTVRQNLE 371
Cdd:cd03248 33 VSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDGKPI--SQYEHKylhSKVSLVGQEPVLFAR-SLQDNIA 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 372 L---HARLFHIPPAEIPARVAQMIERFML---TEVeDTLPASLPLGIRQRLSLAVAVIHRPEMLILDEPTSGVDPVARDM 445
Cdd:cd03248 110 YglqSCSFECVKEAAQKAHAHSFISELASgydTEV-GEKGSQLSGGQKQRVAIARALIRNPQVLILDEATSALDAESEQQ 188
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 446125071 446 FWQLMVD-LSRQdkvTIFISTHFMNEAERCDRMSLMHAGKV 485
Cdd:cd03248 189 VQQALYDwPERR---TVLVIAHRLSTVERADQILVLDGGRI 226
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
279-494 |
1.56e-11 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 65.72 E-value: 1.56e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 279 AKDLTMRFGKFVAVDHVNFRIPRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGQAWLFGQPVDPNDIDT-----RRRVGY 353
Cdd:PRK11701 9 VRGLTKLYGPRKGCRDVSFDLYPGEVLGIVGESGSGKTTLLNALSARLAPDAGEVHYRMRDGQLRDLYAlseaeRRRLLR 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 354 MSQAFslyneltVRQNLELHARLfhippaEIPARvAQMIERFM-----------------LTEVE------DTLPASLPL 410
Cdd:PRK11701 89 TEWGF-------VHQHPRDGLRM------QVSAG-GNIGERLMavgarhygdiratagdwLERVEidaariDDLPTTFSG 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 411 GIRQRLSLAVAVIHRPEMLILDEPTSGVDpV---AR--DMFWQLMVDLSrqdkVTIFISTHFMNEAeR--CDRMSLMHAG 483
Cdd:PRK11701 155 GMQQRLQIARNLVTHPRLVFMDEPTGGLD-VsvqARllDLLRGLVRELG----LAVVIVTHDLAVA-RllAHRLLVMKQG 228
|
250
....*....|..
gi 446125071 484 KVLASG-TPQEL 494
Cdd:PRK11701 229 RVVESGlTDQVL 240
|
|
| nickel_nikD |
TIGR02770 |
nickel import ATP-binding protein NikD; This family represents the NikD subunit of a ... |
30-235 |
1.57e-11 |
|
nickel import ATP-binding protein NikD; This family represents the NikD subunit of a multisubunit nickel import ABC transporter complex. Nickel, once imported, may be used in urease and in certain classes of hydrogenase and superoxide dismutase. NikD and NikE are homologous. [Transport and binding proteins, Cations and iron carrying compounds]
Pssm-ID: 131817 [Multi-domain] Cd Length: 230 Bit Score: 65.08 E-value: 1.57e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 30 NITLDIPARSMVGLIGPDGVGKS----SLLSLISGARVIEQGNVIVLGGDMRDAKHR-RDVC-----PRIAWMP-QGLGK 98
Cdd:TIGR02770 4 DLNLSLKRGEVLALVGESGSGKSltclAILGLLPPGLTQTSGEILLDGRPLLPLSIRgRHIAtimqnPRTAFNPlFTMGN 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 99 NLYHTLsvyenvdffaRLFGHDKAEREARITELLNSTGLA---------PFrdrpagKLSGGMKQKLGLCCALIHDPELL 169
Cdd:TIGR02770 84 HAIETL----------RSLGKLSKQARALILEALEAVGLPdpeevlkkyPF------QLSGGMLQRVMIALALLLEPPFL 147
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446125071 170 ILDEPTTGVDPLSRAQFWDLIDSIRQRQtNMSVLVATAYMEE-AERFDWLVAMNAGEILATGSAQQL 235
Cdd:TIGR02770 148 IADEPTTDLDVVNQARVLKLLRELRQLF-GTGILLITHDLGVvARIADEVAVMDDGRIVERGTVKEI 213
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
24-235 |
1.68e-11 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 66.01 E-value: 1.68e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 24 KTVALNNITLDIPARSMVGLIGPDGVGKSSLLSLISGARVIEQGNVIVLGGDMR---DAKHRRDVCPRIAWMPQGLGKNL 100
Cdd:PRK13641 19 EKKGLDNISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITIAGYHITpetGNKNLKKLRKKVSLVFQFPEAQL 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 101 YHTlSVYENVDFFARLFGHDKAEREARITELLNSTGL-------APFrdrpagKLSGGMKQKLGLCCALIHDPELLILDE 173
Cdd:PRK13641 99 FEN-TVLKDVEFGPKNFGFSEDEAKEKALKWLKKVGLsedliskSPF------ELSGGQMRRVAIAGVMAYEPEILCLDE 171
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446125071 174 PTTGVDPLSRAQFWDLIDSIrQRQTNMSVLVATAYMEEAERFDWLVAMNAGEILATGSAQQL 235
Cdd:PRK13641 172 PAAGLDPEGRKEMMQLFKDY-QKAGHTVILVTHNMDDVAEYADDVLVLEHGKLIKHASPKEI 232
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
308-483 |
1.98e-11 |
|
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: 63.80 E-value: 1.98e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 308 LGSNGCGKSTTMKMLTGLLPAS--EGQAWLFGQPVDPNdidTRRRVGYMSQAFSLYNELTVRQNLELHARLFHIPPAEip 385
Cdd:cd03232 39 MGESGAGKTTLLDVLAGRKTAGviTGEILINGRPLDKN---FQRSTGYVEQQDVHSPNLTVREALRFSALLRGLSVEQ-- 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 386 arvaqmierfmltevedtlpaslplgiRQRLSLAVAVIHRPEMLILDEPTSGVDPVARDMFWQLMVDLSRQDKvTIFIST 465
Cdd:cd03232 114 ---------------------------RKRLTIGVELAAKPSILFLDEPTSGLDSQAAYNIVRFLKKLADSGQ-AILCTI 165
|
170 180
....*....|....*....|
gi 446125071 466 HFMNEA--ERCDRMSLMHAG 483
Cdd:cd03232 166 HQPSASifEKFDRLLLLKRG 185
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
277-439 |
2.19e-11 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 65.14 E-value: 2.19e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 277 IEAKDLTMRFGKFVAVDHVNFRIPRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGQAwlfgqpvdpnDIDTRRRVGYMSQ 356
Cdd:PRK09544 5 VSLENVSVSFGQRRVLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVI----------KRNGKLRIGYVPQ 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 357 AFSLYNE--LTVRQNLELH--ARLFHIPPAEIPARVAQMIERFMltevedtlpASLPLGIRQRLSLAVAVIHRPEMLILD 432
Cdd:PRK09544 75 KLYLDTTlpLTVNRFLRLRpgTKKEDILPALKRVQAGHLIDAPM---------QKLSGGETQRVLLARALLNRPQLLVLD 145
|
....*..
gi 446125071 433 EPTSGVD 439
Cdd:PRK09544 146 EPTQGVD 152
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
30-191 |
2.35e-11 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 64.05 E-value: 2.35e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 30 NITLDIPARSMVGLIGPDGVGKSSLLSLISGARVIEQGNVIVLGGDM---RDAKHRRdvcprIAWmpqgLG-----KNLy 101
Cdd:PRK13538 19 GLSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVLWQGEPIrrqRDEYHQD-----LLY----LGhqpgiKTE- 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 102 htLSVYENVDFFARLfgHDKAEREArITELLNSTGLAPFRDRPAGKLSGGMKQKLGLCCALIHDPELLILDEPTTGVDPL 181
Cdd:PRK13538 89 --LTALENLRFYQRL--HGPGDDEA-LWEALAQVGLAGFEDVPVRQLSAGQQRRVALARLWLTRAPLWILDEPFTAIDKQ 163
|
170
....*....|
gi 446125071 182 SRAQFWDLID 191
Cdd:PRK13538 164 GVARLEALLA 173
|
|
| ABC2_membrane_2 |
pfam12679 |
ABC-2 family transporter protein; This family is related to the ABC-2 membrane transporter ... |
726-907 |
2.76e-11 |
|
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: 65.11 E-value: 2.76e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 726 LLLMMIPSMLSALSVVREKELGSMINLYVTPTTRSEFLLGKQLPYIALGMLNFLLLCALSVFVFGVPLKGSFLTLTLAAL 805
Cdd:pfam12679 76 FLIPVIAALLGADAIAGERERGTIELLLSLPVSRSEILLGKFIGRLAIGLILAVALLAGVLLALAITLALGDPLDLGDLL 155
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 806 LYVI---------IATGLGLLISTFMKSQIAAIFGTSIITLIPATQFSGMIDPVASLEGPGRWIGEIYPTSHFLT----- 871
Cdd:pfam12679 156 LLVAasvllalalVFLSIGLLLSSVARSTRTAAAIALGLFFVLAILWPIVLYGLAELLAGPAPPQELLDFLLFLNptspy 235
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 446125071 872 -IARGTFSKALDLSDLWP-----LFMPLLIAVPVVMGLSILL 907
Cdd:pfam12679 236 nTLLSTILAGSDLSLYGStatnlLILLAWIAVPLALAYVLFK 277
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
28-238 |
3.08e-11 |
|
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: 64.17 E-value: 3.08e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 28 LNNITLDIPARSMVGLIGPDGVGKSSLLSLISGARVIEQGNVIVLGGDMRDAKH---RRdvcpRIAWMPQGLgkNLYHTl 104
Cdd:cd03253 17 LKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDGQDIREVTLdslRR----AIGVVPQDT--VLFND- 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 105 SVYENVDFfARLFGHD----KAEREARITELLNSTglaPFR-DRPAG----KLSGGMKQKLGLCCALIHDPELLILDEPT 175
Cdd:cd03253 90 TIGYNIRY-GRPDATDeeviEAAKAAQIHDKIMRF---PDGyDTIVGerglKLSGGEKQRVAIARAILKNPPILLLDEAT 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446125071 176 TGVDPLSRAQFWDLIDSIRQRQTnmSVLVATAyMEEAERFDWLVAMNAGEILATGSAQQLRAK 238
Cdd:cd03253 166 SALDTHTEREIQAALRDVSKGRT--TIVIAHR-LSTIVNADKIIVLKDGRIVERGTHEELLAK 225
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
28-238 |
3.48e-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: 67.66 E-value: 3.48e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 28 LNNITLDIPARSMVGLIGPDGVGKSSLLSLISGARVIEQGNVIVLGGdmrdakhrrdvcprIAWMPQglgKNLYHTLSVY 107
Cdd:TIGR00957 654 LNGITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVHMKGS--------------VAYVPQ---QAWIQNDSLR 716
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 108 ENVdffarLFGHDKAEREARIT----ELLNSTGLAPFRDR-----PAGKLSGGMKQKLGLCCALIHDPELLILDEPTTGV 178
Cdd:TIGR00957 717 ENI-----LFGKALNEKYYQQVleacALLPDLEILPSGDRteigeKGVNLSGGQKQRVSLARAVYSNADIYLFDDPLSAV 791
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 179 DPLSRAQFWDLIDSIRQRQTNMSVLVATAYMEEAERFDWLVAMNAGEILATGSAQQLRAK 238
Cdd:TIGR00957 792 DAHVGKHIFEHVIGPEGVLKNKTRILVTHGISYLPQVDVIIVMSGGKISEMGSYQELLQR 851
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
25-238 |
4.90e-11 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 66.58 E-value: 4.90e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 25 TVALNNITLDIPARSMVGLIGPDGVGKSSLLSLISGARVIEQGNVIVLGGDMRDAKHR--RDVCpriAWMPQGLgkNLYH 102
Cdd:PRK11176 356 VPALRNINFKIPAGKTVALVGRSGSGKSTIANLLTRFYDIDEGEILLDGHDLRDYTLAslRNQV---ALVSQNV--HLFN 430
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 103 -TLS---VYENVDFFARlfghDKAEREAR-------ITELLNstGLapfrDRPAGK----LSGGMKQKLGLCCALIHDPE 167
Cdd:PRK11176 431 dTIAnniAYARTEQYSR----EQIEEAARmayamdfINKMDN--GL----DTVIGEngvlLSGGQRQRIAIARALLRDSP 500
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446125071 168 LLILDEPTTGVDPLSRAQFWDLIDSIrqrQTNMSVLVATAYMEEAERFDWLVAMNAGEILATGSAQQLRAK 238
Cdd:PRK11176 501 ILILDEATSALDTESERAIQAALDEL---QKNRTSLVIAHRLSTIEKADEILVVEDGEIVERGTHAELLAQ 568
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
22-182 |
7.94e-11 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 62.27 E-value: 7.94e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 22 YGKTVALNNITLDIPARSMVGLIGPDGVGKSSLLSLISGARVIEQGNVIVLGGDMRD--AKHRRDVCpriaWMPQGLGKN 99
Cdd:PRK13540 11 YHDQPLLQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEILFERQSIKKdlCTYQKQLC----FVGHRSGIN 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 100 LYHTLSvyENVdffarLFGHDKAEREARITELLNSTGLAPFRDRPAGKLSGGMKQKLGLCCALIHDPELLILDEPTTGVD 179
Cdd:PRK13540 87 PYLTLR--ENC-----LYDIHFSPGAVGITELCRLFSLEHLIDYPCGLLSSGQKRQVALLRLWMSKAKLWLLDEPLVALD 159
|
...
gi 446125071 180 PLS 182
Cdd:PRK13540 160 ELS 162
|
|
| tagH |
PRK13545 |
teichoic acids export protein ATP-binding subunit; Provisional |
21-173 |
9.38e-11 |
|
teichoic acids export protein ATP-binding subunit; Provisional
Pssm-ID: 184130 [Multi-domain] Cd Length: 549 Bit Score: 65.30 E-value: 9.38e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 21 HYgktvALNNITLDIPARSMVGLIGPDGVGKSSLLSLISGARVIEQGNVIVLGGdmrdakhrrdvCPRIAwmpqgLGKNL 100
Cdd:PRK13545 37 HY----ALNNISFEVPEGEIVGIIGLNGSGKSTLSNLIAGVTMPNKGTVDIKGS-----------AALIA-----ISSGL 96
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446125071 101 YHTLSVYENVDFFARLFGHDKAEREARITELLNSTGLAPFRDRPAGKLSGGMKQKLGLCCALIHDPELLILDE 173
Cdd:PRK13545 97 NGQLTGIENIELKGLMMGLTKEKIKEIIPEIIEFADIGKFIYQPVKTYSSGMKSRLGFAISVHINPDILVIDE 169
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
292-483 |
9.42e-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: 62.73 E-value: 9.42e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 292 VDHVNFRIPRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGQA-WLFGQPVDPNDIDTRRR----VGYMSQAFSLYNElTV 366
Cdd:cd03290 17 LSNINIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVhWSNKNESEPSFEATRSRnrysVAYAAQKPWLLNA-TV 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 367 RQNLelharLFHIPPAEipARVAQMIERFMLTEVEDTLP-----------ASLPLGIRQRLSLAVAVIHRPEMLILDEPT 435
Cdd:cd03290 96 EENI-----TFGSPFNK--QRYKAVTDACSLQPDIDLLPfgdqteigergINLSGGQRQRICVARALYQNTNIVFLDDPF 168
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 446125071 436 SGVDPVARDMFWQL-MVDLSRQDKVTIFISTHFMNEAERCDRMSLMHAG 483
Cdd:cd03290 169 SALDIHLSDHLMQEgILKFLQDDKRTLVLVTHKLQYLPHADWIIAMKDG 217
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
295-440 |
1.42e-10 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 61.79 E-value: 1.42e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 295 VNFRIPRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGQAWLFGQPVdpNDIDTRRRVGYMSQAFSLYNELTVRQNLELHA 374
Cdd:PRK13543 30 LDFHVDAGEALLVQGDNGAGKTTLLRVLAGLLHVESGQIQIDGKTA--TRGDRSRFMAYLGHLPGLKADLSTLENLHFLC 107
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446125071 375 RLFHIPPAEIPARVAQMIErfmLTEVEDTLPASLPLGIRQRLSLAVAVIHRPEMLILDEPTSGVDP 440
Cdd:PRK13543 108 GLHGRRAKQMPGSALAIVG---LAGYEDTLVRQLSAGQKKRLALARLWLSPAPLWLLDEPYANLDL 170
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
14-235 |
2.04e-10 |
|
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: 64.76 E-value: 2.04e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 14 QLEGVSQHYG-KTVALNNITLDIPARSMVGLIGPDGVGKSSLLSLISGARVIEQGNvIVLGGDMRDAKHRRDVCPRIAWM 92
Cdd:TIGR01193 475 VINDVSYSYGyGSNILSDISLTIKMNSKTTIVGMSGSGKSTLAKLLVGFFQARSGE-ILLNGFSLKDIDRHTLRQFINYL 553
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 93 PQglgKNLYHTLSVYENVdffarLFGhdkAEREARITELLNSTGLAPFRD--------------RPAGKLSGGMKQKLGL 158
Cdd:TIGR01193 554 PQ---EPYIFSGSILENL-----LLG---AKENVSQDEIWAACEIAEIKDdienmplgyqtelsEEGSSISGGQKQRIAL 622
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446125071 159 CCALIHDPELLILDEPTTGVDPLSRAQfwdLIDSIRQRQTNMSVLVATAyMEEAERFDWLVAMNAGEILATGSAQQL 235
Cdd:TIGR01193 623 ARALLTDSKVLILDESTSNLDTITEKK---IVNNLLNLQDKTIIFVAHR-LSVAKQSDKIIVLDHGKIIEQGSHDEL 695
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
30-231 |
2.11e-10 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 63.35 E-value: 2.11e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 30 NITLDIPARSMVGLIGPDGVGKSSLLSLISGARVIEQGNvIVLGG----DMRD----AKHRRdvcpRIAWMPQGlgknly 101
Cdd:PRK11144 16 TVNLTLPAQGITAIFGRSGAGKTSLINAISGLTRPQKGR-IVLNGrvlfDAEKgiclPPEKR----RIGYVFQD------ 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 102 htlsvyenvdffARLFGH--------------DKAEREaRITELLnstGLAPFRDRPAGKLSGGMKQKLGLCCALIHDPE 167
Cdd:PRK11144 85 ------------ARLFPHykvrgnlrygmaksMVAQFD-KIVALL---GIEPLLDRYPGSLSGGEKQRVAIGRALLTAPE 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446125071 168 LLILDEPTTGVDpLSRAQfwDLIDSIRQ--RQTNMSVLVATAYMEEAERF-DWLVAMNAGEILATGS 231
Cdd:PRK11144 149 LLLMDEPLASLD-LPRKR--ELLPYLERlaREINIPILYVSHSLDEILRLaDRVVVLEQGKVKAFGP 212
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
239-499 |
2.41e-10 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 64.35 E-value: 2.41e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 239 THSATLEQAFIA-----LLPEAQRQAHKPVVIPpyhAEQEEIAIEAKDLTMRFGKFVaVDHVNFRIPRGEIFGFLGSNGC 313
Cdd:PRK10790 303 TQQSMLQQAVVAgervfELMDGPRQQYGNDDRP---LQSGRIDIDNVSFAYRDDNLV-LQNINLSVPSRGFVALVGHTGS 378
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 314 GKSTTMKMLTGLLPASEGQAWLFGQPVDPNDIDTRRRVGYMSQ------AFSLYNELTVRQNLElharlfhippaeiPAR 387
Cdd:PRK10790 379 GKSTLASLLMGYYPLTEGEIRLDGRPLSSLSHSVLRQGVAMVQqdpvvlADTFLANVTLGRDIS-------------EEQ 445
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 388 VAQMIERFMLTEVEDTLPA-----------SLPLGIRQRLSLAVAVIHRPEMLILDEPTSGVDPVARDMFWQLMVDLSRQ 456
Cdd:PRK10790 446 VWQALETVQLAELARSLPDglytplgeqgnNLSVGQKQLLALARVLVQTPQILILDEATANIDSGTEQAIQQALAAVREH 525
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 446125071 457 dkVTIFISTHFMNEAERCDRMSLMHAGKVLASGTPQELVQQRG 499
Cdd:PRK10790 526 --TTLVVIAHRLSTIVEADTILVLHRGQAVEQGTHQQLLAAQG 566
|
|
| PRK15093 |
PRK15093 |
peptide ABC transporter ATP-binding protein SapD; |
277-495 |
2.78e-10 |
|
peptide ABC transporter ATP-binding protein SapD;
Pssm-ID: 185049 [Multi-domain] Cd Length: 330 Bit Score: 62.90 E-value: 2.78e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 277 IEAKDLTMRF----GKFVAVDHVNFRIPRGEIFGFLGSNGCGKSTTMKMLTGLLPASegqaW-LFGQPVDPNDID----- 346
Cdd:PRK15093 4 LDIRNLTIEFktsdGWVKAVDRVSMTLTEGEIRGLVGESGSGKSLIAKAICGVTKDN----WrVTADRMRFDDIDllrls 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 347 --TRRRVgymsqafslyneltVRQNLELharLFHIP-----PAE---------IPA----------------RVAQMIER 394
Cdd:PRK15093 80 prERRKL--------------VGHNVSM---IFQEPqscldPSErvgrqlmqnIPGwtykgrwwqrfgwrkrRAIELLHR 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 395 FMLTEVED---TLPASLPLGIRQRLSLAVAVIHRPEMLILDEPTSGVDPVARDMFWQLMVDLSRQDKVTIFISTHFMNEA 471
Cdd:PRK15093 143 VGIKDHKDamrSFPYELTEGECQKVMIAIALANQPRLLIADEPTNAMEPTTQAQIFRLLTRLNQNNNTTILLISHDLQML 222
|
250 260
....*....|....*....|....*
gi 446125071 472 ER-CDRMSLMHAGKVLASGTPQELV 495
Cdd:PRK15093 223 SQwADKINVLYCGQTVETAPSKELV 247
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
14-179 |
3.01e-10 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 61.04 E-value: 3.01e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 14 QLEGVSQHY-GKTVALNNITLDIPARSMVGLIGPDGVGKSSLLSLISGARVIEQGNVIVLGGDMRDAKHRRdvcprIAWM 92
Cdd:PRK10908 3 RFEHVSKAYlGGRQALQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDITRLKNRE-----VPFL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 93 PQGLGKNL--YHTL---SVYENVDFFARLFGHDKAEREARITELLNSTGLAPFRDRPAGKLSGGMKQKLGLCCALIHDPE 167
Cdd:PRK10908 78 RRQIGMIFqdHHLLmdrTVYDNVAIPLIIAGASGDDIRRRVSAALDKVGLLDKAKNFPIQLSGGEQQRVGIARAVVNKPA 157
|
170
....*....|..
gi 446125071 168 LLILDEPTTGVD 179
Cdd:PRK10908 158 VLLADEPTGNLD 169
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
292-442 |
3.22e-10 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 60.73 E-value: 3.22e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 292 VDHVNFRIPRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGQAWLFGQPVDPNDIDTRRRVGYMSQAFSLYNELTVRQNLe 371
Cdd:PRK13540 17 LQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEILFERQSIKKDLCTYQKQLCFVGHRSGINPYLTLRENC- 95
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446125071 372 lharLFHIPPAEIPARVAQMIERFMLTEVEDTLPASLPLGIRQRLSLAVAVIHRPEMLILDEPTSGVDPVA 442
Cdd:PRK13540 96 ----LYDIHFSPGAVGITELCRLFSLEHLIDYPCGLLSSGQKRQVALLRLWMSKAKLWLLDEPLVALDELS 162
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
294-494 |
3.60e-10 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 64.37 E-value: 3.60e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 294 HVNFRIPRGEIFGFLGSNGCGKSTTMKMLTGLLPasegqawlfgqPVDPNDIDTRRRVGYMSQAFSLYNElTVRQNLelh 373
Cdd:PLN03130 635 NINLDVPVGSLVAIVGSTGEGKTSLISAMLGELP-----------PRSDASVVIRGTVAYVPQVSWIFNA-TVRDNI--- 699
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 374 arLFHIPPAeiPARVAQMIERFMLTEVEDTLPA-----------SLPLGIRQRLSLAVAVIHRPEMLILDEPTSGVDP-V 441
Cdd:PLN03130 700 --LFGSPFD--PERYERAIDVTALQHDLDLLPGgdlteigergvNISGGQKQRVSMARAVYSNSDVYIFDDPLSALDAhV 775
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 446125071 442 ARDMFWQLMVD-LSRQDKVTIFISTHFMNeaeRCDRMSLMHAGKVLASGTPQEL 494
Cdd:PLN03130 776 GRQVFDKCIKDeLRGKTRVLVTNQLHFLS---QVDRIILVHEGMIKEEGTYEEL 826
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
27-180 |
5.92e-10 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 61.64 E-value: 5.92e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 27 ALNNITLDIPARSMVGLIGPDGVGKSSLLSLISGARVIEQGNVIVLGGD-----------------------MRDAKHRR 83
Cdd:PRK13651 22 ALDNVSVEINQGEFIAIIGQTGSGKTTFIEHLNALLLPDTGTIEWIFKDeknkkktkekekvleklviqktrFKKIKKIK 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 84 DVCPRIAWMPQGLGKNLYHTlSVYENVDFFARLFGHDKAEREARITELLNSTGL-APFRDRPAGKLSGGMKQKLGLCCAL 162
Cdd:PRK13651 102 EIRRRVGVVFQFAEYQLFEQ-TIEKDIIFGPVSMGVSKEEAKKRAAKYIELVGLdESYLQRSPFELSGGQKRRVALAGIL 180
|
170
....*....|....*...
gi 446125071 163 IHDPELLILDEPTTGVDP 180
Cdd:PRK13651 181 AMEPDFLVFDEPTAGLDP 198
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
291-499 |
5.99e-10 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 62.81 E-value: 5.99e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 291 AVDHVNFRIPRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGQAWLFGQPVDPNDIDT-RRRVGYMSQAFSLYNElTVRQN 369
Cdd:PRK10789 330 ALENVNFTLKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGDIRFHDIPLTKLQLDSwRSRLAVVSQTPFLFSD-TVANN 408
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 370 LEL---HARLFHIPPAEIPARVAQMIERF---MLTEVEDTlPASLPLGIRQRLSLAVAVIHRPEMLILDEPTSGVDPVAR 443
Cdd:PRK10789 409 IALgrpDATQQEIEHVARLASVHDDILRLpqgYDTEVGER-GVMLSGGQKQRISIARALLLNAEILILDDALSAVDGRTE 487
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 446125071 444 dmfWQLMVDLSR-QDKVTIFISTHFMNEAERCDRMSLMHAGKVLASGTPQELVQQRG 499
Cdd:PRK10789 488 ---HQILHNLRQwGEGRTVIISAHRLSALTEASEILVMQHGHIAQRGNHDQLAQQSG 541
|
|
| NosY |
COG1277 |
ABC-type transport system involved in multi-copper enzyme maturation, permease component ... |
723-838 |
6.36e-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: 59.83 E-value: 6.36e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 723 VIPLLLMMIPSMLSALSVVREKELGSMINLYVTPTTRSEFLLGKqlpYIALGMLNFLLLCALSVFVFGV--PLKGSFLTL 800
Cdd:COG1277 56 LLSLLLPLLAPALGMDAISGERESGTLELLLTLPISRWEIVLGK---FLGALLVLLLALLITFLLALLLglLLFGSPPPD 132
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 446125071 801 TLAALLYVIIA-------TGLGLLISTFMKSQIAAIFGTSIITLI 838
Cdd:COG1277 133 LGAILGFYLGLlllglafLAIGLFISALTRNQIVAAILAIALWLL 177
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
291-494 |
6.88e-10 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 62.33 E-value: 6.88e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 291 AVDHVNFRIPRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGQAWLFGQPVD---PNDiDTRRRVGYMSQAFSLYNELTVR 367
Cdd:PRK10762 19 ALSGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSILYLGKEVTfngPKS-SQEAGIGIIHQELNLIPQLTIA 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 368 QNL----ELHARLFHIPPAEIPARVAQMIERFMLTEVEDTLPASLPLGIRQRLSLAVAVIHRPEMLILDEPTSGVDPVAR 443
Cdd:PRK10762 98 ENIflgrEFVNRFGRIDWKKMYAEADKLLARLNLRFSSDKLVGELSIGEQQMVEIAKVLSFESKVIIMDEPTDALTDTET 177
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 446125071 444 DMFWQLMVDLSRQDKVTIFIStHFMNEA-ERCDRMSLMHAGKVLASGTPQEL 494
Cdd:PRK10762 178 ESLFRVIRELKSQGRGIVYIS-HRLKEIfEICDDVTVFRDGQFIAEREVADL 228
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
27-231 |
7.36e-10 |
|
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C is also known as MRP (multidrug resistance-associated protein). Some of the MRP members have five additional transmembrane segments in their N-terminus, but the function of these additional membrane-spanning domains is not clear. The MRP was found in the multidrug-resistance lung cancer cell in which p-glycoprotein was not overexpressed. MRP exports glutathione by drug stimulation, as well as, certain substrates in conjugated forms with anions, such as glutathione, glucuronate, and sulfate.
Pssm-ID: 213211 [Multi-domain] Cd Length: 221 Bit Score: 59.81 E-value: 7.36e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 27 ALNNITLDIPARSMVGLIGPDGVGKSSL-LSLIsgaRVIE--QGNVIVLGGDM-----RDAKHRRDVCPRIAWMPQGlgk 98
Cdd:cd03244 19 VLKNISFSIKPGEKVGIVGRTGSGKSSLlLALF---RLVElsSGSILIDGVDIskiglHDLRSRISIIPQDPVLFSG--- 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 99 nlyhtlSVYENVDFFARlfgHDkaerEARITELLNSTGLAPFRDRPAGKL-----------SGGMKQKLGLCCALIHDPE 167
Cdd:cd03244 93 ------TIRSNLDPFGE---YS----DEELWQALERVGLKEFVESLPGGLdtvveeggenlSVGQRQLLCLARALLRKSK 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 168 LLILDEPTTGVDPLSRAQfwdLIDSIRQRQTNMSVLVAtaymeeAER------FDWLVAMNAGEILATGS 231
Cdd:cd03244 160 ILVLDEATASVDPETDAL---IQKTIREAFKDCTVLTI------AHRldtiidSDRILVLDKGRVVEFDS 220
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
282-494 |
8.44e-10 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 61.30 E-value: 8.44e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 282 LTMRFGK----FVAVDHVNFRIPRGEIFGFLGSNGCGKSTTMKMLTGLL--PASEGQAWLFGQPVDPNDIDTRRR---VG 352
Cdd:PRK11022 9 LSVHFGDesapFRAVDRISYSVKQGEVVGIVGESGSGKSVSSLAIMGLIdyPGRVMAEKLEFNGQDLQRISEKERrnlVG 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 353 Y-MSQAF-----SLYNELTV----RQNLELHArlfhipPAEIPARVAQMIErfMLTEVE--------DTLPASLPLGIRQ 414
Cdd:PRK11022 89 AeVAMIFqdpmtSLNPCYTVgfqiMEAIKVHQ------GGNKKTRRQRAID--LLNQVGipdpasrlDVYPHQLSGGMSQ 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 415 RLSLAVAVIHRPEMLILDEPTSGVDPVARDMFWQLMVDLSRQDKVTIFISTHFMN-EAERCDRMSLMHAGKVLASGTPQE 493
Cdd:PRK11022 161 RVMIAMAIACRPKLLIADEPTTALDVTIQAQIIELLLELQQKENMALVLITHDLAlVAEAAHKIIVMYAGQVVETGKAHD 240
|
.
gi 446125071 494 L 494
Cdd:PRK11022 241 I 241
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
241-464 |
9.51e-10 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 62.13 E-value: 9.51e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 241 SATLE--QAFIALLPEAQRQAHKPVVIppyhAEQEEIAIEAKDLTMRF--GKFVaVDHVNFRIPRGEifGFL--GSNGCG 314
Cdd:COG4178 329 RATVDrlAGFEEALEAADALPEAASRI----ETSEDGALALEDLTLRTpdGRPL-LEDLSLSLKPGE--RLLitGPSGSG 401
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 315 KSTTMKMLTGLLPASEGQAwlfGQPVDpndidtrRRVGYMSQafSLY-NELTVRQNLELHARLFHIPPAEIPA-----RV 388
Cdd:COG4178 402 KSTLLRAIAGLWPYGSGRI---ARPAG-------ARVLFLPQ--RPYlPLGTLREALLYPATAEAFSDAELREaleavGL 469
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446125071 389 AQMIERFmltEVEDTLPASLPLGIRQRLSLAVAVIHRPEMLILDEPTSGVDPVARDMFWQLmvdLSRQDKVTIFIS 464
Cdd:COG4178 470 GHLAERL---DEEADWDQVLSLGEQQRLAFARLLLHKPDWLFLDEATSALDEENEAALYQL---LREELPGTTVIS 539
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
203-499 |
1.09e-09 |
|
multi drug resistance-associated protein (MRP); This model describes multi drug resistance-associated protein (MRP) in eukaryotes. The multidrug resistance-associated protein is an integral membrane protein that causes multidrug resistance when overexpressed in mammalian cells. It belongs to ABC transporter superfamily. The protein topology and function was experimentally demonstrated by epitope tagging and immunofluorescence. Insertion of tags in the critical regions associated with drug efflux, abrogated its function. The C-terminal domain seem to highly conserved. [Transport and binding proteins, Other]
Pssm-ID: 188098 [Multi-domain] Cd Length: 1522 Bit Score: 62.66 E-value: 1.09e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 203 LVATAYMeeaerfDWLVAMNAGeiLATGSAQQLRAKTHSATLEQAfiallPEAQRQAHKPVVIPPYHAeqeeiaIEAKDL 282
Cdd:TIGR00957 1230 LQVTFYL------NWLVRMSSE--METNIVAVERLKEYSETEKEA-----PWQIQETAPPSGWPPRGR------VEFRNY 1290
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 283 TMRF--GKFVAVDHVNFRIPRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGQAWLFGqpVDPNDI---DTRRRVGYMSQ- 356
Cdd:TIGR00957 1291 CLRYreDLDLVLRHINVTIHGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDG--LNIAKIglhDLRFKITIIPQd 1368
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 357 -------------AFSLYNELTVRQNLEL-HARLF-HIPPAEIPARVAQMIErfmltevedtlpaSLPLGIRQRLSLAVA 421
Cdd:TIGR00957 1369 pvlfsgslrmnldPFSQYSDEEVWWALELaHLKTFvSALPDKLDHECAEGGE-------------NLSVGQRQLVCLARA 1435
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446125071 422 VIHRPEMLILDEPTSGVDpVARDMFWQLMVDlSRQDKVTIFISTHFMNEAERCDRMSLMHAGKVLASGTPQELVQQRG 499
Cdd:TIGR00957 1436 LLRKTKILVLDEATAAVD-LETDNLIQSTIR-TQFEDCTVLTIAHRLNTIMDYTRVIVLDKGEVAEFGAPSNLLQQRG 1511
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
11-230 |
1.30e-09 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 59.94 E-value: 1.30e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 11 PVAQLEGVSQHYGKTVALNNITLDIPARSMVGLIGPDGVGKSSLLSLISGARVIEQGNVI--VLGGDMRD----AKHRRD 84
Cdd:PRK11701 5 PLLSVRGLTKLYGPRKGCRDVSFDLYPGEVLGIVGESGSGKTTLLNALSARLAPDAGEVHyrMRDGQLRDlyalSEAERR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 85 VCPRIAW--MPQGLGKNLYHTLSVYENV-----DFFARLFGHDKAEReariTELLNSTGLAPFR--DRPAgKLSGGMKQK 155
Cdd:PRK11701 85 RLLRTEWgfVHQHPRDGLRMQVSAGGNIgerlmAVGARHYGDIRATA----GDWLERVEIDAARidDLPT-TFSGGMQQR 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446125071 156 LGLCCALIHDPELLILDEPTTGVDPLSRAQFWDLIDSIrQRQTNMSVLVATAYMEEAeRF--DWLVAMNAGEILATG 230
Cdd:PRK11701 160 LQIARNLVTHPRLVFMDEPTGGLDVSVQARLLDLLRGL-VRELGLAVVIVTHDLAVA-RLlaHRLLVMKQGRVVESG 234
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
287-521 |
2.18e-09 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 61.66 E-value: 2.18e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 287 GKFVAVDHVNFRIPRGEIFGFLGSNGCGKSTTMKML-----TGLLpaSEGQAWLFGQPVDPNdidTRRRVGYMSQAFSLY 361
Cdd:TIGR00956 774 EKRVILNNVDGWVKPGTLTALMGASGAGKTTLLNVLaervtTGVI--TGGDRLVNGRPLDSS---FQRSIGYVQQQDLHL 848
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 362 NELTVRQNLELHARLF---HIPPAEIPARVAQMIERFMLTEVEDTLPASLPLGI----RQRLSLAVAVIHRPEMLI-LDE 433
Cdd:TIGR00956 849 PTSTVRESLRFSAYLRqpkSVSKSEKMEYVEEVIKLLEMESYADAVVGVPGEGLnveqRKRLTIGVELVAKPKLLLfLDE 928
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 434 PTSGVDPVARDMFWQLMVDLSRQDKvTIFISTH-----FMNEAercDRMSLMH-AGKVLASG-------TPQELVQQRGA 500
Cdd:TIGR00956 929 PTSGLDSQTAWSICKLMRKLADHGQ-AILCTIHqpsaiLFEEF---DRLLLLQkGGQTVYFGdlgenshTIINYFEKHGA 1004
|
250 260
....*....|....*....|...
gi 446125071 501 ANL--EAAFISWLQEAAGAAPET 521
Cdd:TIGR00956 1005 PKCpeDANPAEWMLEVIGAAPGA 1027
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
266-466 |
2.24e-09 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 58.43 E-value: 2.24e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 266 PPYHAEQEEIAIEAKDLTMRFGKFVAVDHVNFRIPRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGQAWLfgqPVDPNDI 345
Cdd:COG2401 20 VLDLSERVAIVLEAFGVELRVVERYVLRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGALKGTPVAGCV---DVPDNQF 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 346 dtrrrvgymsqafslYNELTVrqnlelharLFHIPPAEIPARVAQMIERFMLTEVEDTL--PASLPLGIRQRLSLAVAVI 423
Cdd:COG2401 97 ---------------GREASL---------IDAIGRKGDFKDAVELLNAVGLSDAVLWLrrFKELSTGQKFRFRLALLLA 152
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 446125071 424 HRPEMLILDEPTSGVDP-----VARDmfwqlMVDLSRQDKVTIFISTH 466
Cdd:COG2401 153 ERPKLLVIDEFCSHLDRqtakrVARN-----LQKLARRAGITLVVATH 195
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
295-489 |
2.26e-09 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 60.27 E-value: 2.26e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 295 VNFRIPRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGQAWLFGQPVdpNDIDT-------RRRVGYMSQAFSLYNELTVR 367
Cdd:PRK11144 17 VNLTLPAQGITAIFGRSGAGKTSLINAISGLTRPQKGRIVLNGRVL--FDAEKgiclppeKRRIGYVFQDARLFPHYKVR 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 368 QNLELHARlfhippAEIPARVAQMIERFMLTEVEDTLPASLPLGIRQRLSLAVAVIHRPEMLILDEPTSGVD-PVARdmf 446
Cdd:PRK11144 95 GNLRYGMA------KSMVAQFDKIVALLGIEPLLDRYPGSLSGGEKQRVAIGRALLTAPELLLMDEPLASLDlPRKR--- 165
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 446125071 447 wQLMV---DLSRQDKVTIFISTHFMNEAER-CDRMSLMHAGKVLASG 489
Cdd:PRK11144 166 -ELLPyleRLAREINIPILYVSHSLDEILRlADRVVVLEQGKVKAFG 211
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
282-439 |
2.98e-09 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 60.57 E-value: 2.98e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 282 LTMRFGKFVAVDHVNFRIPRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGQ---------AWL------FGQPVDPNDID 346
Cdd:PRK10636 7 LQIRRGVRVLLDNATATINPGQKVGLVGKNGCGKSTLLALLKNEISADGGSytfpgnwqlAWVnqetpaLPQPALEYVID 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 347 TRRRVGYMSQAFSLYNELTVRQNLE-LHARLFHIPPAEIPARVAQMIERFMLTEVEDTLPAS-LPLGIRQRLSLAVAVIH 424
Cdd:PRK10636 87 GDREYRQLEAQLHDANERNDGHAIAtIHGKLDAIDAWTIRSRAASLLHGLGFSNEQLERPVSdFSGGWRMRLNLAQALIC 166
|
170
....*....|....*
gi 446125071 425 RPEMLILDEPTSGVD 439
Cdd:PRK10636 167 RSDLLLLDEPTNHLD 181
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
121-251 |
3.21e-09 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 58.56 E-value: 3.21e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 121 KAEREARITELLNSTGLA-PFR--DRPAGKLSGGMKQKLGLCCALIHDPELLILDEPTTGVDPLSRAQFWDLIDSIRQRQ 197
Cdd:PRK10418 111 KPADDATLTAALEAVGLEnAARvlKLYPFEMSGGMLQRMMIALALLCEAPFIIADEPTTDLDVVAQARILDLLESIVQKR 190
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 446125071 198 tNMSVLVATAYMEEAERF-DWLVAMNAGEILATGSAQQL-RAKTHSAT--LEQAFIAL 251
Cdd:PRK10418 191 -ALGMLLVTHDMGVVARLaDDVAVMSHGRIVEQGDVETLfNAPKHAVTrsLVSAHLAL 247
|
|
| PRK13546 |
PRK13546 |
teichoic acids export ABC transporter ATP-binding subunit TagH; |
18-173 |
3.84e-09 |
|
teichoic acids export ABC transporter ATP-binding subunit TagH;
Pssm-ID: 184131 [Multi-domain] Cd Length: 264 Bit Score: 58.67 E-value: 3.84e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 18 VSQHYGKTV-ALNNITLDIPARSMVGLIGPDGVGKSSLLSLISGARVIEQGNVivlggdmrdakhRRDVCPRIAWMPQGL 96
Cdd:PRK13546 29 IPKHKNKTFfALDDISLKAYEGDVIGLVGINGSGKSTLSNIIGGSLSPTVGKV------------DRNGEVSVIAISAGL 96
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446125071 97 GKNLyhtlSVYENVDFFARLFGHDKAEREARITELLNSTGLAPFRDRPAGKLSGGMKQKLGLCCALIHDPELLILDE 173
Cdd:PRK13546 97 SGQL----TGIENIEFKMLCMGFKRKEIKAMTPKIIEFSELGEFIYQPVKKYSSGMRAKLGFSINITVNPDILVIDE 169
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
292-548 |
4.12e-09 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 60.10 E-value: 4.12e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 292 VDHVNFRIPRGEIFGFLGSNGCGKSTTMKMLTGLLPAS-----EGQAWLFGQPVDPNDIDTRRRV--GYMSQAFS----- 359
Cdd:PRK15134 25 VNDVSLQIEAGETLALVGESGSGKSVTALSILRLLPSPpvvypSGDIRFHGESLLHASEQTLRGVrgNKIAMIFQepmvs 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 360 ---LYN-ELTVRQNLELHaRLFHIPPAEipARVAQMIERFMLTEVEDTL---PASLPLGIRQRLSLAVAVIHRPEMLILD 432
Cdd:PRK15134 105 lnpLHTlEKQLYEVLSLH-RGMRREAAR--GEILNCLDRVGIRQAAKRLtdyPHQLSGGERQRVMIAMALLTRPELLIAD 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 433 EPTSGVDPVARDMFWQLMVDLSRQDKVTIFISTHFMNEAER-CDRMSLMHAGKVLAsgtpqelvQQRGAANLEAAFISWL 511
Cdd:PRK15134 182 EPTTALDVSVQAQILQLLRELQQELNMGLLFITHNLSIVRKlADRVAVMQNGRCVE--------QNRAATLFSAPTHPYT 253
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 446125071 512 QEAAGAAPETPIPPSQTPAAS---------GKPSRQGLsFRRLFSY 548
Cdd:PRK15134 254 QKLLNSEPSGDPVPLPEPASPlldveqlqvAFPIRKGI-LKRTVDH 298
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
27-203 |
4.83e-09 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 58.95 E-value: 4.83e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 27 ALNNITLDIPARSMVGLIGPDGVGKSSLLSLISGARVIEQGNVIVLGGDMR--DAKHRRDVCPRIAWMPQGLGKNLYHTL 104
Cdd:PRK15079 36 AVDGVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGEVAWLGKDLLgmKDDEWRAVRSDIQMIFQDPLASLNPRM 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 105 SVYENV-----DFFARLfghDKAEREARITELLNSTGLAP-FRDRPAGKLSGGMKQKLGLCCALIHDPELLILDEPTTGV 178
Cdd:PRK15079 116 TIGEIIaeplrTYHPKL---SRQEVKDRVKAMMLKVGLLPnLINRYPHEFSGGQCQRIGIARALILEPKLIICDEPVSAL 192
|
170 180
....*....|....*....|....*
gi 446125071 179 DPLSRAQFWDLIDSIrQRQTNMSVL 203
Cdd:PRK15079 193 DVSIQAQVVNLLQQL-QREMGLSLI 216
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
25-238 |
9.26e-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: 9.26e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 25 TVALNNITLDIPARSMVGLIGPDGVGKSSLLSLISGARVIEQGNVivlggdmrdaKH--RRDVCPRIAW-MPQGLGKNLY 101
Cdd:TIGR01271 439 TPVLKNISFKLEKGQLLAVAGSTGSGKSSLLMMIMGELEPSEGKI----------KHsgRISFSPQTSWiMPGTIKDNII 508
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 102 HTLSvYEnvdffarlfghdkaerEARITELLNSTGLA------PFRDR-PAGK----LSGGMKQKLGLCCALIHDPELLI 170
Cdd:TIGR01271 509 FGLS-YD----------------EYRYTSVIKACQLEedialfPEKDKtVLGEggitLSGGQRARISLARAVYKDADLYL 571
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446125071 171 LDEPTTGVDPLSRAQFWDliDSIRQRQTNMSVLVATAYMEEAERFDWLVAMNAGEILATGSAQQLRAK 238
Cdd:TIGR01271 572 LDSPFTHLDVVTEKEIFE--SCLCKLMSNKTRILVTSKLEHLKKADKILLLHEGVCYFYGTFSELQAK 637
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
14-226 |
1.15e-08 |
|
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: 56.27 E-value: 1.15e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 14 QLEGVSQHYGKTV--ALNNITLDIPARSMVGLIGPDGVGKSSLLSLISGARVIEQGNVIVLGGDMRDAKhRRDVCPRIAW 91
Cdd:cd03369 8 EVENLSVRYAPDLppVLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDGIDISTIP-LEDLRSSLTI 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 92 MPQGlgknlyHTL---SVYENVDFFARLfgHDKAEREA-RITEllnsTGLapfrdrpagKLSGGMKQKLGLCCALIHDPE 167
Cdd:cd03369 87 IPQD------PTLfsgTIRSNLDPFDEY--SDEEIYGAlRVSE----GGL---------NLSQGQRQLLCLARALLKRPR 145
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 446125071 168 LLILDEPTTGVDPLSRAQfwdLIDSIRQRQTNMSVLVATAYMEEAERFDWLVAMNAGEI 226
Cdd:cd03369 146 VLVLDEATASIDYATDAL---IQKTIREEFTNSTILTIAHRLRTIIDYDKILVMDAGEV 201
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
42-331 |
1.67e-08 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 57.98 E-value: 1.67e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 42 GLIGPDGVGKSSLLSLISGARVIEQGNV-------------------------IVLGGD--MRDAKHRRDvcpRIAWMPQ 94
Cdd:PRK15064 31 GLIGANGCGKSTFMKILGGDLEPSAGNVsldpnerlgklrqdqfafeeftvldTVIMGHteLWEVKQERD---RIYALPE 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 95 GLGKNLYHtlsVYENVDFFARLFGHDKaerEARITELLNSTGLA-PFRDRPAGKLSGGMKQKLGLCCALIHDPELLILDE 173
Cdd:PRK15064 108 MSEEDGMK---VADLEVKFAEMDGYTA---EARAGELLLGVGIPeEQHYGLMSEVAPGWKLRVLLAQALFSNPDILLLDE 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 174 PTTGVDplsraqfwdlIDSIR-------QRQTNM-----------SVLVATAYMEEAE------RFD--WLVAMNAGEIL 227
Cdd:PRK15064 182 PTNNLD----------INTIRwledvlnERNSTMiiishdrhflnSVCTHMADLDYGElrvypgNYDeyMTAATQARERL 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 228 ATGSAqqlRAKTHSATLeQAFIALL---PEAQRQAH--------------KPV--VIPPYHAEQEE----IAIEAKDLTM 284
Cdd:PRK15064 252 LADNA---KKKAQIAEL-QSFVSRFsanASKAKQATsrakqidkikleevKPSsrQNPFIRFEQDKklhrNALEVENLTK 327
|
330 340 350 360
....*....|....*....|....*....|....*....|....*..
gi 446125071 285 RFGKFVAVDHVNFRIPRGEIFGFLGSNGCGKSTTMKMLTGLLPASEG 331
Cdd:PRK15064 328 GFDNGPLFKNLNLLLEAGERLAIIGENGVGKTTLLRTLVGELEPDSG 374
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
23-238 |
1.84e-08 |
|
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of iron-sulfur clusters (Fe-S) depends on multi-protein systems. The SUF system of E. coli and Erwinia chrysanthemi is important for Fe-S biogenesis under stressful conditions. The SUF system is made of six proteins: SufC is an atypical cytoplasmic ABC-ATPase, which forms a complex with SufB and SufD; SufA plays the role of a scaffold protein for assembly of iron-sulfur clusters and delivery to target proteins; SufS is a cysteine desulfurase which mobilizes the sulfur atom from cysteine and provides it to the cluster; SufE has no associated function yet.
Pssm-ID: 213184 [Multi-domain] Cd Length: 200 Bit Score: 55.23 E-value: 1.84e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 23 GKTVaLNNITLDIPARSMVGLIGPDGVGKSSLLSLISG---ARVIEqGNVIVLGGDMRDakhrrdvcpriawmpqglgkn 99
Cdd:cd03217 12 GKEI-LKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMGhpkYEVTE-GEILFKGEDITD--------------------- 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 100 lyhtLSVYENvdffARL-----FghdkaEREARITELLNSTGLapfRDRPAGkLSGGMKQKLGLCCALIHDPELLILDEP 174
Cdd:cd03217 69 ----LPPEER----ARLgiflaF-----QYPPEIPGVKNADFL---RYVNEG-FSGGEKKRNEILQLLLLEPDLAILDEP 131
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446125071 175 TTGVDplsraqfwdlIDSIRQ--------RQTNMSVLVATAYMEEAE--RFDWLVAMNAGEILATGS---AQQLRAK 238
Cdd:cd03217 132 DSGLD----------IDALRLvaevinklREEGKSVLIITHYQRLLDyiKPDRVHVLYDGRIVKSGDkelALEIEKK 198
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
27-243 |
2.00e-08 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 56.34 E-value: 2.00e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 27 ALNNITLDIPARSMVGLIGPDGVGKSSLLSLISGARVIEQGNVIVLGGDMR--DAKHRRDvcpRIAWMPQGLGKNLYHTL 104
Cdd:PRK15112 28 AVKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDHPLHfgDYSYRSQ---RIRMIFQDPSTSLNPRQ 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 105 SVYENVDFFARL-FGHDKAEREARITELLNSTGLAPfrDRPA---GKLSGGMKQKLGLCCALIHDPELLILDEPTTGVDP 180
Cdd:PRK15112 105 RISQILDFPLRLnTDLEPEQREKQIIETLRQVGLLP--DHASyypHMLAPGQKQRLGLARALILRPKVIIADEALASLDM 182
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446125071 181 LSRAQFWDLIDSIRQRQtNMSVLVATAYMEEAERF-DWLVAMNAGEILATGS-AQQLRAKTHSAT 243
Cdd:PRK15112 183 SMRSQLINLMLELQEKQ-GISYIYVTQHLGMMKHIsDQVLVMHQGEVVERGStADVLASPLHELT 246
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
28-239 |
2.01e-08 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 58.20 E-value: 2.01e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 28 LNNITLDIPARSMVGLIGPDGVGKSSLLSLISGARVIEQGNVIVLGGDMRDAKH---RRDVCPrIAWMPQGLGKnlyhtl 104
Cdd:TIGR00958 497 LKGLTFTLHPGEVVALVGPSGSGKSTVAALLQNLYQPTGGQVLLDGVPLVQYDHhylHRQVAL-VGQEPVLFSG------ 569
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 105 SVYENVdffarLFGHDKAEREaritELLNSTGLAPFRD-------------RPAG-KLSGGMKQKLGLCCALIHDPELLI 170
Cdd:TIGR00958 570 SVRENI-----AYGLTDTPDE----EIMAAAKAANAHDfimefpngydtevGEKGsQLSGGQKQRIAIARALVRKPRVLI 640
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446125071 171 LDEPTTGVDPLSRAQFWDLidsirQRQTNMSVLVATAYMEEAERFDWLVAMNAGEILATGSAQQLRAKT 239
Cdd:TIGR00958 641 LDEATSALDAECEQLLQES-----RSRASRTVLLIAHRLSTVERADQILVLKKGSVVEMGTHKQLMEDQ 704
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
299-466 |
2.11e-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: 55.88 E-value: 2.11e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 299 IPRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGQAwlfgqpvdPNDIDTrrrVGYMSQAFSLYNELTVRQNLELHARLFH 378
Cdd:cd03237 22 ISESEVIGILGPNGIGKTTFIKMLAGVLKPDEGDI--------EIELDT---VSYKPQYIKADYEGTVRDLLSSITKDFY 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 379 IPPaEIPARVAQ--MIERFMLTEVEDtlpasLPLGIRQRLSLAVAVIHRPEMLILDEPTSGVDPVARDMFWQLMVDLSRQ 456
Cdd:cd03237 91 THP-YFKTEIAKplQIEQILDREVPE-----LSGGELQRVAIAACLSKDADIYLLDEPSAYLDVEQRLMASKVIRRFAEN 164
|
170
....*....|
gi 446125071 457 DKVTIFISTH 466
Cdd:cd03237 165 NEKTAFVVEH 174
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
295-498 |
2.45e-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: 56.40 E-value: 2.45e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 295 VNFRIPRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGQawlfgqpvdpndIDTRRRVGYMSQaFSLYNELTVRQNLelha 374
Cdd:cd03291 56 INLKIEKGEMLAITGSTGSGKTSLLMLILGELEPSEGK------------IKHSGRISFSSQ-FSWIMPGTIKENI---- 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 375 rLFHIPPAEIpaRVAQMIERFMLTEVEDTLPA-----------SLPLGIRQRLSLAVAVIHRPEMLILDEPTSGVDPVAR 443
Cdd:cd03291 119 -IFGVSYDEY--RYKSVVKACQLEEDITKFPEkdntvlgeggiTLSGGQRARISLARAVYKDADLYLLDSPFGYLDVFTE 195
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 446125071 444 DMFWQLMVDLSRQDKVTIFIsTHFMNEAERCDRMSLMHAGKVLASGTPQELVQQR 498
Cdd:cd03291 196 KEIFESCVCKLMANKTRILV-TSKMEHLKKADKILILHEGSSYFYGTFSELQSLR 249
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
11-179 |
2.82e-08 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 57.49 E-value: 2.82e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 11 PVAQLEGVSQHYGKTVALNNITLDIPARSMVGLIGPDGVGKSSLLSLISGARVIEQGNV-----IVLGgdmRDAKH---- 81
Cdd:PRK10636 311 PLLKMEKVSAGYGDRIILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELAPVSGEIglakgIKLG---YFAQHqlef 387
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 82 -RRDVCP-----RIAwmPQGLGKNLYHTLSVYEnvdffarlFGHDKaerearITEllnstglapfrdrPAGKLSGGMKQK 155
Cdd:PRK10636 388 lRADESPlqhlaRLA--PQELEQKLRDYLGGFG--------FQGDK------VTE-------------ETRRFSGGEKAR 438
|
170 180
....*....|....*....|....
gi 446125071 156 LGLCCALIHDPELLILDEPTTGVD 179
Cdd:PRK10636 439 LVLALIVWQRPNLLLLDEPTNHLD 462
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
295-498 |
2.91e-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: 58.00 E-value: 2.91e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 295 VNFRIPRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGQawlfgqpvdpndIDTRRRVGYMSQaFSLYNELTVRQNLelha 374
Cdd:TIGR01271 445 ISFKLEKGQLLAVAGSTGSGKSSLLMMIMGELEPSEGK------------IKHSGRISFSPQ-TSWIMPGTIKDNI---- 507
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 375 rLFHIPPAEIPAR----VAQMIERFMLTEVEDTLP-----ASLPLGIRQRLSLAVAVIHRPEMLILDEPTSGVDPVA-RD 444
Cdd:TIGR01271 508 -IFGLSYDEYRYTsvikACQLEEDIALFPEKDKTVlgeggITLSGGQRARISLARAVYKDADLYLLDSPFTHLDVVTeKE 586
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 446125071 445 MF----WQLMVDLSRqdkvtiFISTHFMNEAERCDRMSLMHAGKVLASGTPQELVQQR 498
Cdd:TIGR01271 587 IFesclCKLMSNKTR------ILVTSKLEHLKKADKILLLHEGVCYFYGTFSELQAKR 638
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
248-541 |
3.91e-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: 57.61 E-value: 3.91e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 248 FIALLPEAQR--QAHKP------VVIPPYHAEQE---EIAIEAKDLTMRF---GKFVAVDhVNFRIPRGEIFGFLGSNGC 313
Cdd:TIGR01271 1178 FIDLPQEEPRpsGGGGKyqlstvLVIENPHAQKCwpsGGQMDVQGLTAKYteaGRAVLQD-LSFSVEGGQRVGLLGRTGS 1256
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 314 GKSTTMKMLTGLLpASEGQAWLFGQPVDPNDIDT-RRRVGYMSQAFSLYNElTVRQNLELHARLfhiPPAEIpARVAQ-- 390
Cdd:TIGR01271 1257 GKSTLLSALLRLL-STEGEIQIDGVSWNSVTLQTwRKAFGVIPQKVFIFSG-TFRKNLDPYEQW---SDEEI-WKVAEev 1330
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 391 ----MIERF--MLTEVEDTLPASLPLGIRQRLSLAVAVIHRPEMLILDEPTSGVDPVArdmfWQLMVDLSRQ--DKVTIF 462
Cdd:TIGR01271 1331 glksVIEQFpdKLDFVLVDGGYVLSNGHKQLMCLARSILSKAKILLLDEPSAHLDPVT----LQIIRKTLKQsfSNCTVI 1406
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446125071 463 ISTHFMNEAERCDRMSLMHAGKVLASGTPQELVQQRgaanleaafiSWLQEAAGAAPETPIPPSQTPAASGKPSRQGLS 541
Cdd:TIGR01271 1407 LSEHRVEALLECQQFLVIEGSSVKQYDSIQKLLNET----------SLFKQAMSAADRLKLFPLHRRNSSKRKPQPKIT 1475
|
|
| SapD |
COG4170 |
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms]; |
148-269 |
4.21e-08 |
|
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms];
Pssm-ID: 443330 [Multi-domain] Cd Length: 331 Bit Score: 56.07 E-value: 4.21e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 148 LSGGMKQKLGLCCALIHDPELLILDEPTTGVDPLSRAQFWDLIDSIRQRQtNMSVLVATAYMEE-AERFDWLVAMNAGEI 226
Cdd:COG4170 159 LTEGECQKVMIAMAIANQPRLLIADEPTNAMESTTQAQIFRLLARLNQLQ-GTSILLISHDLESiSQWADTITVLYCGQT 237
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 446125071 227 LATGSAQQLRAKT-HSATleQAFIALLPEAQRQ-AHK------PVVIPPYH 269
Cdd:COG4170 238 VESGPTEQILKSPhHPYT--KALLRSMPDFRQPlPHKsrlntlPGSIPPLQ 286
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
14-260 |
4.60e-08 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 56.89 E-value: 4.60e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 14 QLEGVSQHY-GKTVALNNITLDIPARSMVGLIGPDGVGKSSLLSLISGARVIEQGNVIVLGGDMRDAKHrrdvcpriawm 92
Cdd:PRK13657 336 EFDDVSFSYdNSRQGVEDVSFEAKPGQTVAIVGPTGAGKSTLINLLQRVFDPQSGRILIDGTDIRTVTR----------- 404
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 93 pQGLGKNLYhtlSVYENVDFFARLFG---------------HDKAEReARITELL--NSTGLAPFRDRPAGKLSGGMKQK 155
Cdd:PRK13657 405 -ASLRRNIA---VVFQDAGLFNRSIEdnirvgrpdatdeemRAAAER-AQAHDFIerKPDGYDTVVGERGRQLSGGERQR 479
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 156 LGLCCALIHDPELLILDEPTTGVDPLSRAQFWDLIDSIRQRQTNMSVLVATAYMEEAERfdwLVAMNAGEILATGSAQQL 235
Cdd:PRK13657 480 LAIARALLKDPPILILDEATSALDVETEAKVKAALDELMKGRTTFIIAHRLSTVRNADR---ILVFDNGRVVESGSFDEL 556
|
250 260
....*....|....*....|....*.
gi 446125071 236 RAKT-HSATLEQAFIALLPEAQRQAH 260
Cdd:PRK13657 557 VARGgRFAALLRAQGMLQEDERRKQP 582
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
11-206 |
4.91e-08 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 54.72 E-value: 4.91e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 11 PVAQLEGVSQHYGKTVALNNITLDIPARSMVGLIGPDGVGKSSLLSLISGARVIEQGNVIVLGGDMRDAK---HRRDV-- 85
Cdd:PRK10247 6 PLLQLQNVGYLAGDAKILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFEGEDISTLKpeiYRQQVsy 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 86 CpriAWMPQGLGKnlyhtlSVYENVdFFARLFGHDKAEREARITEL----LNSTGLapfrDRPAGKLSGGMKQKLGLCCA 161
Cdd:PRK10247 86 C---AQTPTLFGD------TVYDNL-IFPWQIRNQQPDPAIFLDDLerfaLPDTIL----TKNIAELSGGEKQRISLIRN 151
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 446125071 162 LIHDPELLILDEPTTGVDPLSRAQFWDLIDSIrQRQTNMSVLVAT 206
Cdd:PRK10247 152 LQFMPKVLLLDEITSALDESNKHNVNEIIHRY-VREQNIAVLWVT 195
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
295-494 |
5.12e-08 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 57.29 E-value: 5.12e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 295 VNFRIPRGEIFGFLGSNGCGKSTTMKMLTGLLPasegqawlfgqPVDPNDIDTRRRVGYMSQAFSLYNElTVRQNLeLHA 374
Cdd:PLN03232 636 INLEIPVGSLVAIVGGTGEGKTSLISAMLGELS-----------HAETSSVVIRGSVAYVPQVSWIFNA-TVRENI-LFG 702
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 375 RLFHippaeiPARVAQMIERFMLTEVEDTLPA-----------SLPLGIRQRLSLAVAVIHRPEMLILDEPTSGVDP-VA 442
Cdd:PLN03232 703 SDFE------SERYWRAIDVTALQHDLDLLPGrdlteigergvNISGGQKQRVSMARAVYSNSDIYIFDDPLSALDAhVA 776
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 446125071 443 RDMFWQLMVD-LSRQDKVTIFISTHFMNEAercDRMSLMHAGKVLASGTPQEL 494
Cdd:PLN03232 777 HQVFDSCMKDeLKGKTRVLVTNQLHFLPLM---DRIILVSEGMIKEEGTFAEL 826
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
7-179 |
5.47e-08 |
|
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: 56.48 E-value: 5.47e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 7 VPVPP-----VAQLEGVSQHYGKTVALNNITLDIPARSMVGLIGPDGVGKSSLLSLISGARVIEQGNVIVlgGDMrdakh 81
Cdd:TIGR03719 312 IPPGPrlgdkVIEAENLTKAFGDKLLIDDLSFKLPPGGIVGVIGPNGAGKSTLFRMITGQEQPDSGTIEI--GET----- 384
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 82 rrdvcPRIAWMPQ---GL--GKNLYHTLS------VYENVDFFAR----LFGHDKAEREARItellnstglapfrdrpaG 146
Cdd:TIGR03719 385 -----VKLAYVDQsrdALdpNKTVWEEISggldiiKLGKREIPSRayvgRFNFKGSDQQKKV-----------------G 442
|
170 180 190
....*....|....*....|....*....|...
gi 446125071 147 KLSGGMKQKLGLCCALIHDPELLILDEPTTGVD 179
Cdd:TIGR03719 443 QLSGGERNRVHLAKTLKSGGNVLLLDEPTNDLD 475
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
28-188 |
5.96e-08 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 56.91 E-value: 5.96e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 28 LNNITLDIPARSMVGLIGPDGVGKSSLLSLISGARVIEQGNVIVLGGDMRDAkhrrdvcPRIAWMpqglgknlyHTLSVY 107
Cdd:PLN03232 633 LSDINLEIPVGSLVAIVGGTGEGKTSLISAMLGELSHAETSSVVIRGSVAYV-------PQVSWI---------FNATVR 696
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 108 ENVdffarLFGHD-KAEREAR---ITELLNSTGLAPFRDRP-----AGKLSGGMKQKLGLCCALIHDPELLILDEPTTGV 178
Cdd:PLN03232 697 ENI-----LFGSDfESERYWRaidVTALQHDLDLLPGRDLTeigerGVNISGGQKQRVSMARAVYSNSDIYIFDDPLSAL 771
|
170
....*....|
gi 446125071 179 DPLSRAQFWD 188
Cdd:PLN03232 772 DAHVAHQVFD 781
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
277-439 |
9.67e-08 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 55.67 E-value: 9.67e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 277 IEAKDLTMRFGKFVAVDHVNFRIPRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGQAWLfgqpvDPNDidtrrRVGYMSQ 356
Cdd:PRK15064 2 LSTANITMQFGAKPLFENISVKFGGGNRYGLIGANGCGKSTFMKILGGDLEPSAGNVSL-----DPNE-----RLGKLRQ 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 357 ---AFSLYNEL-TVRQ-NLELHA------RLFHIPP---------AEIPARVAQM-----------------IErfmlTE 399
Cdd:PRK15064 72 dqfAFEEFTVLdTVIMgHTELWEvkqerdRIYALPEmseedgmkvADLEVKFAEMdgytaearagelllgvgIP----EE 147
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 446125071 400 VEDTLPASLPLGIRQRLSLAVAVIHRPEMLILDEPTSGVD 439
Cdd:PRK15064 148 QHYGLMSEVAPGWKLRVLLAQALFSNPDILLLDEPTNNLD 187
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
43-234 |
1.09e-07 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 53.78 E-value: 1.09e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 43 LIGPDGVGKSSLLSLISGArVIEQGNVIVLGGDMRD------AKHRRDVC----PRIAwMPqglgknLYHTLSvyenvdf 112
Cdd:PRK03695 27 LVGPNGAGKSTLLARMAGL-LPGSGSIQFAGQPLEAwsaaelARHRAYLSqqqtPPFA-MP------VFQYLT------- 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 113 farLFGHDKA---EREARITELLNSTGLAPFRDRPAGKLSGGMKQKLGLCCAL--IH---DPE--LLILDEPTTGVDPLS 182
Cdd:PRK03695 92 ---LHQPDKTrteAVASALNEVAEALGLDDKLGRSVNQLSGGEWQRVRLAAVVlqVWpdiNPAgqLLLLDEPMNSLDVAQ 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 446125071 183 RAQFWDLIDSIRQRqtNMSVLVAT----AYMEEAERFdWLvaMNAGEILATGSAQQ 234
Cdd:PRK03695 169 QAALDRLLSELCQQ--GIAVVMSShdlnHTLRHADRV-WL--LKQGKLLASGRRDE 219
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
290-496 |
1.19e-07 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 54.06 E-value: 1.19e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 290 VAVDHVNFRIPRGEIFGFLGSNGCGKSTTMKMLTGLLPAS--------EGQAWLFGQP---VDPNDIDTRRRVgyMSQAF 358
Cdd:PRK13547 15 AILRDLSLRIEPGRVTALLGRNGAGKSTLLKALAGDLTGGgaprgarvTGDVTLNGEPlaaIDAPRLARLRAV--LPQAA 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 359 SLYNELTVRQNLEL----HARlfhiPPAEIPARVAQMIERFMLTEVEDTLPA----SLPLGIRQRLSLA--VAVIH---- 424
Cdd:PRK13547 93 QPAFAFSAREIVLLgrypHAR----RAGALTHRDGEIAWQALALAGATALVGrdvtTLSGGELARVQFArvLAQLWpphd 168
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446125071 425 ---RPEMLILDEPTSGVDPVARDMFWQLMVDLSRQDKVTIFISTHFMNEAER-CDRMSLMHAGKVLASGTPQELVQ 496
Cdd:PRK13547 169 aaqPPRYLLLDEPTAALDLAHQHRLLDTVRRLARDWNLGVLAIVHDPNLAARhADRIAMLADGAIVAHGAPADVLT 244
|
|
| PRK13541 |
PRK13541 |
cytochrome c biogenesis protein CcmA; Provisional |
309-451 |
1.60e-07 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184128 [Multi-domain] Cd Length: 195 Bit Score: 52.57 E-value: 1.60e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 309 GSNGCGKSTTMKMLTGLLPASEGQawLFGQPVDPNDIdTRRRVGYMSQAFSLYNELTVRQNLELHARLFHiPPAEIPArv 388
Cdd:PRK13541 33 GANGCGKSSLLRMIAGIMQPSSGN--IYYKNCNINNI-AKPYCTYIGHNLGLKLEMTVFENLKFWSEIYN-SAETLYA-- 106
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446125071 389 aqMIERFMLTEVEDTLPASLPLGIRQRLSLAVAVIHRPEMLILDEPTSGVDPVARDMFWQLMV 451
Cdd:PRK13541 107 --AIHYFKLHDLLDEKCYSLSSGMQKIVAIARLIACQSDLWLLDEVETNLSKENRDLLNNLIV 167
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
12-181 |
1.86e-07 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 52.65 E-value: 1.86e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 12 VAQLEGVSQHYGKTVALNNITLDIPARSMVGLIGPDGVGKSSLLSLISGARVIEQGNVIVlggDMRDAKHRRDVcpriaw 91
Cdd:COG2401 30 VLEAFGVELRVVERYVLRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGALKGTPVAGCV---DVPDNQFGREA------ 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 92 mpqglgknlyhtlSVYENVdffarlfGHDKAEREAriTELLNSTGL--APFRDRPAGKLSGGMKQKLGLCCALIHDPELL 169
Cdd:COG2401 101 -------------SLIDAI-------GRKGDFKDA--VELLNAVGLsdAVLWLRRFKELSTGQKFRFRLALLLAERPKLL 158
|
170
....*....|..
gi 446125071 170 ILDEPTTGVDPL 181
Cdd:COG2401 159 VIDEFCSHLDRQ 170
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
14-190 |
2.11e-07 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 54.81 E-value: 2.11e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 14 QLEGVS-QHYGKTVALNNITLDIPARSMVGLIGPDGVGKSSLLSLISGARVIEQGNVIVLGGDmrdakhrrdvcpRIAWM 92
Cdd:COG4178 364 ALEDLTlRTPDGRPLLEDLSLSLKPGERLLITGPSGSGKSTLLRAIAGLWPYGSGRIARPAGA------------RVLFL 431
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 93 PQ----GLGkNLYHTLSvYENvdffarlfgHDKAEREARITELLNSTGLAPFRDRP------AGKLSGGMKQKLGLCCAL 162
Cdd:COG4178 432 PQrpylPLG-TLREALL-YPA---------TAEAFSDAELREALEAVGLGHLAERLdeeadwDQVLSLGEQQRLAFARLL 500
|
170 180
....*....|....*....|....*...
gi 446125071 163 IHDPELLILDEPTTGVDPLSRAQFWDLI 190
Cdd:COG4178 501 LHKPDWLFLDEATSALDEENEAALYQLL 528
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
306-435 |
2.46e-07 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 54.35 E-value: 2.46e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 306 GFLGSNGCGKSTTMKMLTGLLPASEGQAWLfgqpvDPNdidtrRRVGYMSQAFSLYNELTVRQNLE--------LHARLF 377
Cdd:PRK11819 37 GVLGLNGAGKSTLLRIMAGVDKEFEGEARP-----APG-----IKVGYLPQEPQLDPEKTVRENVEegvaevkaALDRFN 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 378 HI------PPAEIPARVAQM------IERFMLTEVE---------------DTLPASLPLGIRQRLSLAVAVIHRPEMLI 430
Cdd:PRK11819 107 EIyaayaePDADFDALAAEQgelqeiIDAADAWDLDsqleiamdalrcppwDAKVTKLSGGERRRVALCRLLLEKPDMLL 186
|
....*
gi 446125071 431 LDEPT 435
Cdd:PRK11819 187 LDEPT 191
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
277-498 |
4.21e-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: 52.55 E-value: 4.21e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 277 IEAKDLTMRF--GKFVAVDHVNFRIPRGEIFGFLGSNGCGKSTTMKMLTGLLpASEGQAWLFGqpVDPNDIDT---RRRV 351
Cdd:cd03289 3 MTVKDLTAKYteGGNAVLENISFSISPGQRVGLLGRTGSGKSTLLSAFLRLL-NTEGDIQIDG--VSWNSVPLqkwRKAF 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 352 GYMSQAFSLYNElTVRQNLELHARLfhipPAEIPARVAqmiERFMLTEVEDTLPASLPL-----------GIRQRLSLAV 420
Cdd:cd03289 80 GVIPQKVFIFSG-TFRKNLDPYGKW----SDEEIWKVA---EEVGLKSVIEQFPGQLDFvlvdggcvlshGHKQLMCLAR 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 421 AVIHRPEMLILDEPTSGVDPVArdmfWQLMVDLSRQ--DKVTIFISTHFMNEAERCDRMSLMHAGKVLASGTPQELVQQR 498
Cdd:cd03289 152 SVLSKAKILLLDEPSAHLDPIT----YQVIRKTLKQafADCTVILSEHRIEAMLECQRFLVIEENKVRQYDSIQKLLNEK 227
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
28-237 |
4.56e-07 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 53.97 E-value: 4.56e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 28 LNNITLDIPARSMVGLIGPDGVGKSSLLSLISGA-RVIEQGNVIVLGgdmrdakhrrdvcpRIAWMPQglgKNLYHTLSV 106
Cdd:PLN03130 633 LSNINLDVPVGSLVAIVGSTGEGKTSLISAMLGElPPRSDASVVIRG--------------TVAYVPQ---VSWIFNATV 695
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 107 YENVdFFARLFGHDKAEREARITELLNSTGLAPFRD-----RPAGKLSGGMKQKLGLCCALIHDPELLILDEPTTGVDPL 181
Cdd:PLN03130 696 RDNI-LFGSPFDPERYERAIDVTALQHDLDLLPGGDlteigERGVNISGGQKQRVSMARAVYSNSDVYIFDDPLSALDAH 774
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 446125071 182 SRAQFWD--LIDSIRQRqtnMSVLVaTAYMEEAERFDWLVAMNAGEILATGSAQQLRA 237
Cdd:PLN03130 775 VGRQVFDkcIKDELRGK---TRVLV-TNQLHFLSQVDRIILVHEGMIKEEGTYEELSN 828
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
291-488 |
5.69e-07 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 53.19 E-value: 5.69e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 291 AVDHVNFRIPRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGQAWLFGQPVdpnDIDTRRR-----VGYMSQAFSLYNELT 365
Cdd:PRK10982 13 ALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEI---DFKSSKEalengISMVHQELNLVLQRS 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 366 VRQNLELharlfhippAEIPARVAQMIERFMLTEVE--------DTLP----ASLPLGIRQRLSLAVAVIHRPEMLILDE 433
Cdd:PRK10982 90 VMDNMWL---------GRYPTKGMFVDQDKMYRDTKaifdeldiDIDPrakvATLSVSQMQMIEIAKAFSYNAKIVIMDE 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 446125071 434 PTSGVDPVARDMFWQLMVDLSRQDKVTIFIStHFMNEA-ERCDRMSLMHAGKVLAS 488
Cdd:PRK10982 161 PTSSLTEKEVNHLFTIIRKLKERGCGIVYIS-HKMEEIfQLCDEITILRDGQWIAT 215
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
5-238 |
6.16e-07 |
|
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 444078 [Multi-domain] Cd Length: 605 Bit Score: 53.29 E-value: 6.16e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 5 TLVPVPPVAQLEGVSQHY-GKTVALNNITLDIPARSMVGLIGPDGVGKSSLLSLISGARVIEQGNVIVLGGDMRDAKH-- 81
Cdd:COG5265 350 PLVVGGGEVRFENVSFGYdPERPILKGVSFEVPAGKTVAIVGPSGAGKSTLARLLFRFYDVTSGRILIDGQDIRDVTQas 429
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 82 -RRDvcprIAWMPQglgknlyHTL----SVYENVdffarLFGHDKAERE--------ARITELLNSTglapfrdrPAG-- 146
Cdd:COG5265 430 lRAA----IGIVPQ-------DTVlfndTIAYNI-----AYGRPDASEEeveaaaraAQIHDFIESL--------PDGyd 485
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 147 --------KLSGGMKQKLGLCCALIHDPELLILDEPTTGVDPLSRAQFWDLIDSIRQRQTNMSVlvataymeeAERF--- 215
Cdd:COG5265 486 trvgerglKLSGGEKQRVAIARTLLKNPPILIFDEATSALDSRTERAIQAALREVARGRTTLVI---------AHRLsti 556
|
250 260
....*....|....*....|....*.
gi 446125071 216 ---DWLVAMNAGEILATGSAQQLRAK 238
Cdd:COG5265 557 vdaDEILVLEAGRIVERGTHAELLAQ 582
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
28-236 |
7.97e-07 |
|
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The CFTR subfamily domain 1. The cystic fibrosis transmembrane regulator (CFTR), the product of the gene mutated in patients with cystic fibrosis, has adapted the ABC transporter structural motif to form a tightly regulated anion channel at the apical surface of many epithelia. Use of the term assembly of a functional ion channel implies the coming together of subunits, or at least smaller not-yet functional components of the active whole. In fact, on the basis of current knowledge only the CFTR polypeptide itself is required to form an ATP- and protein kinase A-dependent low-conductance chloride channel of the type present in the apical membrane of many epithelial cells. CFTR displays the typical organization (IM-ABC)2 and carries a characteristic hydrophilic R-domain that separates IM1-ABC1 from IM2-ABC2.
Pssm-ID: 213258 [Multi-domain] Cd Length: 282 Bit Score: 51.78 E-value: 7.97e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 28 LNNITLDIPARSMVGLIGPDGVGKSSLLSLISGARVIEQGNVivlggdmrdaKH--RRDVCPRIAW-MPQGLGKNLYHTL 104
Cdd:cd03291 53 LKNINLKIEKGEMLAITGSTGSGKTSLLMLILGELEPSEGKI----------KHsgRISFSSQFSWiMPGTIKENIIFGV 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 105 SvYENVDFFARLfghdKA-EREARITELlnstglaPFRDR-PAGK----LSGGMKQKLGLCCALIHDPELLILDEPTTGV 178
Cdd:cd03291 123 S-YDEYRYKSVV----KAcQLEEDITKF-------PEKDNtVLGEggitLSGGQRARISLARAVYKDADLYLLDSPFGYL 190
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 446125071 179 DPLSRAQFWDliDSIRQRQTNMSVLVATAYMEEAERFDWLVAMNAGEILATGSAQQLR 236
Cdd:cd03291 191 DVFTEKEIFE--SCVCKLMANKTRILVTSKMEHLKKADKILILHEGSSYFYGTFSELQ 246
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
28-224 |
8.62e-07 |
|
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The sulfonylurea receptor SUR is an ATP transporter of the ABCC/MRP family with tandem ATPase binding domains. Unlike other ABC proteins, it has no intrinsic transport function, neither active nor passive, but associates with the potassium channel proteins Kir6.1 or Kir6.2 to form the ATP-sensitive potassium (K(ATP)) channel. Within the channel complex, SUR serves as a regulatory subunit that fine-tunes the gating of Kir6.x in response to alterations in cellular metabolism. It constitutes a major pharmaceutical target as it binds numerous drugs, K(ATP) channel openers and blockers, capable of up- or down-regulating channel activity.
Pssm-ID: 213257 [Multi-domain] Cd Length: 218 Bit Score: 50.79 E-value: 8.62e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 28 LNNITLDIPARSMVGLIGPDGVGKSSLL-------SLISGARVIEQGNVIVLGGDMRDAKHRRDVcpriAWMPQglgKNL 100
Cdd:cd03290 17 LSNINIRIPTGQLTMIVGQVGCGKSSLLlailgemQTLEGKVHWSNKNESEPSFEATRSRNRYSV----AYAAQ---KPW 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 101 YHTLSVYENVDfFARLFGHDKAEREARITELLNSTGLAPFRDRP-----AGKLSGGMKQKLGLCCALIHDPELLILDEPT 175
Cdd:cd03290 90 LLNATVEENIT-FGSPFNKQRYKAVTDACSLQPDIDLLPFGDQTeigerGINLSGGQRQRICVARALYQNTNIVFLDDPF 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 446125071 176 TGVD-PLSRAQFWDLIDSIRQRQTNMSVLVaTAYMEEAERFDWLVAMNAG 224
Cdd:cd03290 169 SALDiHLSDHLMQEGILKFLQDDKRTLVLV-THKLQYLPHADWIIAMKDG 217
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
292-464 |
9.64e-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: 49.46 E-value: 9.64e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 292 VDHVNFRIPRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGQAwlfgqpvdpnDIDTRRRVGYMSQAfSLYNELTVRQNLe 371
Cdd:cd03223 17 LKDLSFEIKPGDRLLITGPSGTGKSSLFRALAGLWPWGSGRI----------GMPEGEDLLFLPQR-PYLPLGTLREQL- 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 372 lharlfhippaeiparvaqmierfmltevedTLPAS--LPLGIRQRLSLAVAVIHRPEMLILDEPTSGVDPVARDMFWQL 449
Cdd:cd03223 85 -------------------------------IYPWDdvLSGGEQQRLAFARLLLHKPKFVFLDEATSALDEESEDRLYQL 133
|
170
....*....|....*
gi 446125071 450 MvdlsrQDKVTIFIS 464
Cdd:cd03223 134 L-----KELGITVIS 143
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
295-545 |
1.11e-06 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 52.86 E-value: 1.11e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 295 VNFRIPRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGQAWlfgqpvdpndidTRRRVGYMSQAFSLYNElTVRQNLelha 374
Cdd:PTZ00243 679 VSVSVPRGKLTVVLGATGSGKSTLLQSLLSQFEISEGRVW------------AERSIAYVPQQAWIMNA-TVRGNI---- 741
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 375 rLFHIPpaEIPARVAQMIERFMLTEVEDTLPASLPLGI-----------RQRLSLAVAVIHRPEMLILDEPTSGVDP--- 440
Cdd:PTZ00243 742 -LFFDE--EDAARLADAVRVSQLEADLAQLGGGLETEIgekgvnlsggqKARVSLARAVYANRDVYLLDDPLSALDAhvg 818
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 441 --VARDMFwqlmvdLSRQDKVTIFISTHFMNEAERCDRMSLMHAGKVLASGTPQELVQ-----------------QRGAA 501
Cdd:PTZ00243 819 erVVEECF------LGALAGKTRVLATHQVHVVPRADYVVALGDGRVEFSGSSADFMRtslyatlaaelkenkdsKEGDA 892
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 446125071 502 NLEAAFISwLQEAAGAAPETPIPPSQTPAASGKPSRQGLSFRRL 545
Cdd:PTZ00243 893 DAEVAEVD-AAPGGAVDHEPPVAKQEGNAEGGDGAALDAAAGRL 935
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
5-198 |
1.26e-06 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 51.94 E-value: 1.26e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 5 TLVPVPPVAQLEGVSQHYGKTVALNNITLDIPARSMVGLIGPDGVGKSSLLSLISGARviEQG--NVIVLGGdmrdakHR 82
Cdd:PRK10938 253 ALPANEPRIVLNNGVVSYNDRPILHNLSWQVNPGEHWQIVGPNGAGKSTLLSLITGDH--PQGysNDLTLFG------RR 324
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 83 R-------DVCPRIAWMPQGLGKNlYHTLSVYENV---DFF----------ARLfgHDKAEREARITELLNSTGLAPFRD 142
Cdd:PRK10938 325 RgsgetiwDIKKHIGYVSSSLHLD-YRVSTSVRNVilsGFFdsigiyqavsDRQ--QKLAQQWLDILGIDKRTADAPFHS 401
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 143 rpagkLSGGmKQKLGLCC-ALIHDPELLILDEPTTGVDPLSRA---QFWDLIdsIRQRQT 198
Cdd:PRK10938 402 -----LSWG-QQRLALIVrALVKHPTLLILDEPLQGLDPLNRQlvrRFVDVL--ISEGET 453
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
295-464 |
1.33e-06 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 52.34 E-value: 1.33e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 295 VNFRIPRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGQAwLFGQPVDPNDIDT---RRRVGYMSQ-------------AF 358
Cdd:PTZ00265 404 LNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDI-IINDSHNLKDINLkwwRSKIGVVSQdpllfsnsiknniKY 482
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 359 SLY---------NEL------------------------------TVRQNLELHARLFH--IPPAEIpARVAQ--MIERF 395
Cdd:PTZ00265 483 SLYslkdlealsNYYnedgndsqenknkrnscrakcagdlndmsnTTDSNELIEMRKNYqtIKDSEV-VDVSKkvLIHDF 561
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446125071 396 M--LTEVEDTLPAS----LPLGIRQRLSLAVAVIHRPEMLILDEPTSGVDPVARDMFWQLMVDLS-RQDKVTIFIS 464
Cdd:PTZ00265 562 VsaLPDKYETLVGSnaskLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQKTINNLKgNENRITIIIA 637
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
7-71 |
1.56e-06 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 51.66 E-value: 1.56e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 7 VPVPP-----VAQLEGVSQHYGKTVALNNITLDIPARSMVGLIGPDGVGKSSLLSLISGARVIEQGNVIV 71
Cdd:PRK11819 314 IPPGPrlgdkVIEAENLSKSFGDRLLIDDLSFSLPPGGIVGIIGPNGAGKSTLFKMITGQEQPDSGTIKI 383
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
282-535 |
2.06e-06 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 51.17 E-value: 2.06e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 282 LTMRFGKFVAVDHVNFRIPR-----GEIFGFLGSNGCGKSTTMKMLTGLLPASEGQAwlfgqpvdpndIDTRRRVGYMS- 355
Cdd:PRK10938 4 LQISQGTFRLSDTKTLQLPSltlnaGDSWAFVGANGSGKSALARALAGELPLLSGER-----------QSQFSHITRLSf 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 356 -QAFSLYNELTVRQNLELharlfhIPP---------AEI-------PARVAQMIERFMLTEVEDTLPASLPLGIRQRLSL 418
Cdd:PRK10938 73 eQLQKLVSDEWQRNNTDM------LSPgeddtgrttAEIiqdevkdPARCEQLAQQFGITALLDRRFKYLSTGETRKTLL 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 419 AVAVIHRPEMLILDEPTSGVDPVARDMFWQLMVDLSRQDKVTIFISTHFMNEAERCDRMSLMHAGKVLASGTPQELVQQR 498
Cdd:PRK10938 147 CQALMSEPDLLILDEPFDGLDVASRQQLAELLASLHQSGITLVLVLNRFDEIPDFVQFAGVLADCTLAETGEREEILQQA 226
|
250 260 270
....*....|....*....|....*....|....*...
gi 446125071 499 GAANLEAAfiswlQEAAGAA-PETPIPPSQTPAASGKP 535
Cdd:PRK10938 227 LVAQLAHS-----EQLEGVQlPEPDEPSARHALPANEP 259
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
10-201 |
2.17e-06 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 50.73 E-value: 2.17e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 10 PPVAQLEGVSQHYG---------KTV-ALNNITLDIPARSMVGLIGPDGVGKSSL---LSLI----SGARVIEQGNVivL 72
Cdd:PRK11308 3 QPLLQAIDLKKHYPvkrglfkpeRLVkALDGVSFTLERGKTLAVVGESGCGKSTLarlLTMIetptGGELYYQGQDL--L 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 73 GGDMRDAKHRR------------DVCPRiawmpQGLGKNLYHTLSVyeNVDFfarlfghDKAEREARITELLNSTGLAP- 139
Cdd:PRK11308 81 KADPEAQKLLRqkiqivfqnpygSLNPR-----KKVGQILEEPLLI--NTSL-------SAAERREKALAMMAKVGLRPe 146
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446125071 140 FRDRPAGKLSGGMKQKLGLCCALIHDPELLILDEPTTGVDPLSRAQ----FWDLidsirQRQTNMS 201
Cdd:PRK11308 147 HYDRYPHMFSGGQRQRIAIARALMLDPDVVVADEPVSALDVSVQAQvlnlMMDL-----QQELGLS 207
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
104-222 |
2.19e-06 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 51.95 E-value: 2.19e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 104 LSVYENVDFfarlfGHDKAERE--------ARITELLNS------TGLAPFrdrpaGK-LSGGMKQKLGLCCALIHDPEL 168
Cdd:PTZ00265 1310 MSIYENIKF-----GKEDATREdvkrackfAAIDEFIESlpnkydTNVGPY-----GKsLSGGQKQRIAIARALLREPKI 1379
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 446125071 169 LILDEPTTGVDPLSRAQFWDLIDSIRQRqTNMSVLVATAYMEEAERFDWLVAMN 222
Cdd:PTZ00265 1380 LLLDEATSSLDSNSEKLIEKTIVDIKDK-ADKTIITIAHRIASIKRSDKIVVFN 1432
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
28-242 |
3.12e-06 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 51.13 E-value: 3.12e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 28 LNNITLDIPARSMVGLIGPDGVGKSSLLSLISGARVIEQGNVIVLGGDMrdAKH-RRDVCPRIAWMPQglgKNLYHTLSV 106
Cdd:PLN03232 1252 LHGLSFFVSPSEKVGVVGRTGAGKSSMLNALFRIVELEKGRIMIDDCDV--AKFgLTDLRRVLSIIPQ---SPVLFSGTV 1326
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 107 YENVDFFARLFGHD--KAEREARITELL--NSTGLAPFRDRPAGKLSGGMKQKLGLCCALIHDPELLILDEPTTGVDPLS 182
Cdd:PLN03232 1327 RFNIDPFSEHNDADlwEALERAHIKDVIdrNPFGLDAEVSEGGENFSVGQRQLLSLARALLRRSKILVLDEATASVDVRT 1406
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446125071 183 RAqfwdLID-SIRQRQTNMSVLVATAYMEEAERFDWLVAMNAGEILATGSAQQLRAKTHSA 242
Cdd:PLN03232 1407 DS----LIQrTIREEFKSCTMLVIAHRLNTIIDCDKILVLSSGQVLEYDSPQELLSRDTSA 1463
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
28-179 |
3.16e-06 |
|
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI), is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI's are not transport proteins and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLI's have an N-terminal Fe-S domain and two nucleotide-binding domains which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity of more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213204 [Multi-domain] Cd Length: 246 Bit Score: 49.33 E-value: 3.16e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 28 LNNITLDIPARS-----MVGLIGPDGVGKSSLLSLISGARVIEQGNVIVLGGDmrdakhrrdvcprIAWMPQglgknlYH 102
Cdd:cd03237 10 LGEFTLEVEGGSiseseVIGILGPNGIGKTTFIKMLAGVLKPDEGDIEIELDT-------------VSYKPQ------YI 70
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446125071 103 TLSVYENVDFFARLFGHDKAEREARITELLNSTGLAPFRDRPAGKLSGGMKQKLGLCCALIHDPELLILDEPTTGVD 179
Cdd:cd03237 71 KADYEGTVRDLLSSITKDFYTHPYFKTEIAKPLQIEQILDREVPELSGGELQRVAIAACLSKDADIYLLDEPSAYLD 147
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
149-235 |
3.24e-06 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 50.11 E-value: 3.24e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 149 SGGMKQKLGLCCALIHDPELLILDEPTTGVDPLSRAQFWDLIDSIRqRQTNMSVLVATAYME-EAERFDWLVAMNAGEIL 227
Cdd:PRK09473 163 SGGMRQRVMIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELK-REFNTAIIMITHDLGvVAGICDKVLVMYAGRTM 241
|
....*...
gi 446125071 228 ATGSAQQL 235
Cdd:PRK09473 242 EYGNARDV 249
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
285-464 |
3.79e-06 |
|
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette transporters; The pleiotropic drug resistance (PDR) is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. This PDR subfamily represents domain I of its (ABC-IM)2 organization. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds including sugars, ions, peptides, and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213200 [Multi-domain] Cd Length: 202 Bit Score: 48.80 E-value: 3.79e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 285 RFGKFVAVDHVNFRIPRGEIFGFLGSNGCGKSTTMKMLTGLLPAS---EGQAWLFGQPVDPNDIDTRRRVGYMSQAFSLY 361
Cdd:cd03233 16 GRSKIPILKDFSGVVKPGEMVLVLGRPGSGCSTLLKALANRTEGNvsvEGDIHYNGIPYKEFAEKYPGEIIYVSEEDVHF 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 362 NELTVRQNLELHARLfhippaeipaRVAQMIErfmltevedtlpaslplGI----RQRLSLAVAVIHRPEMLILDEPTSG 437
Cdd:cd03233 96 PTLTVRETLDFALRC----------KGNEFVR-----------------GIsggeRKRVSIAEALVSRASVLCWDNSTRG 148
|
170 180
....*....|....*....|....*..
gi 446125071 438 VDPVARDMFWQLMVDLSRQDKVTIFIS 464
Cdd:cd03233 149 LDSSTALEILKCIRTMADVLKTTTFVS 175
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
28-248 |
3.97e-06 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 50.65 E-value: 3.97e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 28 LNNITLDIPARSMVGLIGPDGVGKSSLLSLISGaRVieQGNVIVLGGDMRDAKHRRDVCPRIAWMPQGlgKNLYHTLSVY 107
Cdd:PLN03211 84 LNGVTGMASPGEILAVLGPSGSGKSTLLNALAG-RI--QGNNFTGTILANNRKPTKQILKRTGFVTQD--DILYPHLTVR 158
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 108 ENVDFFARLFGHDKAEREARIT---ELLNSTGLAPFRDRPAGK-----LSGGMKQKLGLCCALIHDPELLILDEPTTGVD 179
Cdd:PLN03211 159 ETLVFCSLLRLPKSLTKQEKILvaeSVISELGLTKCENTIIGNsfirgISGGERKRVSIAHEMLINPSLLILDEPTSGLD 238
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446125071 180 PLSRAQFWDLIDSIRQRQTNmsvlVATAYMEEAER----FDWLVAMNAGEILATGSAQQLRAKTHSATLEQAF 248
Cdd:PLN03211 239 ATAAYRLVLTLGSLAQKGKT----IVTSMHQPSSRvyqmFDSVLVLSEGRCLFFGKGSDAMAYFESVGFSPSF 307
|
|
| ABC_UvrA_II |
cd03271 |
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair ... |
15-231 |
4.53e-06 |
|
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: 49.15 E-value: 4.53e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 15 LEGVSQHygktvALNNITLDIPARSMVGLIGPDGVGKSSLL----------------------SLISGARVIEQgnVIVL 72
Cdd:cd03271 3 LKGAREN-----NLKNIDVDIPLGVLTCVTGVSGSGKSSLIndtlypalarrlhlkkeqpgnhDRIEGLEHIDK--VIVI 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 73 GGDMRDAKHRR-----------------DVCPRIAWMPQGL-----GKNLYHTL--SVYENVDFFArlfghdKAEREARI 128
Cdd:cd03271 76 DQSPIGRTPRSnpatytgvfdeirelfcEVCKGKRYNRETLevrykGKSIADVLdmTVEEALEFFE------NIPKIARK 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 129 TELLNSTGLAPFR-DRPAGKLSGGMKQKLGLCCALIH---DPELLILDEPTTGVDPLSRAQFWDLIDSIRQRQTnmSVLV 204
Cdd:cd03271 150 LQTLCDVGLGYIKlGQPATTLSGGEAQRIKLAKELSKrstGKTLYILDEPTTGLHFHDVKKLLEVLQRLVDKGN--TVVV 227
|
250 260 270
....*....|....*....|....*....|...
gi 446125071 205 ATAYMEEAERFDWLVAM------NAGEILATGS 231
Cdd:cd03271 228 IEHNLDVIKCADWIIDLgpeggdGGGQVVASGT 260
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
27-498 |
6.40e-06 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 49.79 E-value: 6.40e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 27 ALNNITLDIPARSMVGLIGPDGVGKSSLLSLISGarVIEQGNV---IVLGGDMRDAKHRRDVCPR-IAWMPQGLGknLYH 102
Cdd:NF040905 16 ALDDVNLSVREGEIHALCGENGAGKSTLMKVLSG--VYPHGSYegeILFDGEVCRFKDIRDSEALgIVIIHQELA--LIP 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 103 TLSVYENVdffarLFGHDKAER--------EARITELLNSTGLAPFRDRPAGKLSGGMKQKLGLCCALIHDPELLILDEP 174
Cdd:NF040905 92 YLSIAENI-----FLGNERAKRgvidwnetNRRARELLAKVGLDESPDTLVTDIGVGKQQLVEIAKALSKDVKLLILDEP 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 175 TTGVDPLSRAQFWDLIDSIRQRqtNMSVLVATAYMEEAERfdwlVAmNAGEILATG-SAQQLRAKTHSAT---------- 243
Cdd:NF040905 167 TAALNEEDSAALLDLLLELKAQ--GITSIIISHKLNEIRR----VA-DSITVLRDGrTIETLDCRADEVTedriirgmvg 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 244 --LEQAFiallpeaqrqahkpvviPPYHAEQEEIAIEAKDLTMRF----GKFVaVDHVNFRIPRGEIFGFLGSNGCGKsT 317
Cdd:NF040905 240 rdLEDRY-----------------PERTPKIGEVVFEVKNWTVYHplhpERKV-VDDVSLNVRRGEIVGIAGLMGAGR-T 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 318 TMKMltGLLPAS-----EGQAWLFGQPVDPNDIDTRRRVG--YMSQ---AFSLYNELTVRQNLELhARLFHIPP------ 381
Cdd:NF040905 301 ELAM--SVFGRSygrniSGTVFKDGKEVDVSTVSDAIDAGlaYVTEdrkGYGLNLIDDIKRNITL-ANLGKVSRrgvide 377
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 382 -AEIpaRVAQMIERFM-------LTEVEdtlpaSLPLGIRQRLSLAVAVIHRPEMLILDEPTSGVDPVARDMFWQLMVDL 453
Cdd:NF040905 378 nEEI--KVAEEYRKKMniktpsvFQKVG-----NLSGGNQQKVVLSKWLFTDPDVLILDEPTRGIDVGAKYEIYTIINEL 450
|
490 500 510 520
....*....|....*....|....*....|....*....|....*.
gi 446125071 454 SRQDKVTIFISTHfMNEA-ERCDRMSLMHAGKVLASGTPQELVQQR 498
Cdd:NF040905 451 AAEGKGVIVISSE-LPELlGMCDRIYVMNEGRITGELPREEASQER 495
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
14-230 |
6.79e-06 |
|
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins, and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213205 [Multi-domain] Cd Length: 176 Bit Score: 47.32 E-value: 6.79e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 14 QLEGVSQHygktvALNNITLDIPARSMVGLIGPDGVGKSSLLSLISGArvieqgnvivlggdmrdakhrrDVCPRIAWMP 93
Cdd:cd03238 2 TVSGANVH-----NLQNLDVSIPLNVLVVVTGVSGSGKSTLVNEGLYA----------------------SGKARLISFL 54
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 94 QglgknlyhtlsvyenvdffarLFGHDKAEREARITELLNsTGLAPFR-DRPAGKLSGGMKQKLGLCCALIHDPE--LLI 170
Cdd:cd03238 55 P---------------------KFSRNKLIFIDQLQFLID-VGLGYLTlGQKLSTLSGGELQRVKLASELFSEPPgtLFI 112
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446125071 171 LDEPTTGVDPLSRAQFWDLIDSIRQrQTNMSVLV--ATAYMEEAerfDWLVAM------NAGEILATG 230
Cdd:cd03238 113 LDEPSTGLHQQDINQLLEVIKGLID-LGNTVILIehNLDVLSSA---DWIIDFgpgsgkSGGKVVFSG 176
|
|
| PRK15093 |
PRK15093 |
peptide ABC transporter ATP-binding protein SapD; |
124-266 |
9.17e-06 |
|
peptide ABC transporter ATP-binding protein SapD;
Pssm-ID: 185049 [Multi-domain] Cd Length: 330 Bit Score: 48.65 E-value: 9.17e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 124 REARITELLNSTGLAPFRDRPAG---KLSGGMKQKLGLCCALIHDPELLILDEPTTGVDPLSRAQFWDLIDSIRQrQTNM 200
Cdd:PRK15093 132 RKRRAIELLHRVGIKDHKDAMRSfpyELTEGECQKVMIAIALANQPRLLIADEPTNAMEPTTQAQIFRLLTRLNQ-NNNT 210
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446125071 201 SVLVATAYMEEAERF-DWLVAMNAGEILATGSAQQLRAKTHSAtLEQAFIALLPEAQRQ-AHK------PVVIP 266
Cdd:PRK15093 211 TILLISHDLQMLSQWaDKINVLYCGQTVETAPSKELVTTPHHP-YTQALIRAIPDFGSAmPHKsrlntlPGAIP 283
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
28-199 |
1.28e-05 |
|
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: 46.38 E-value: 1.28e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 28 LNNITLDIPARSMVGLIGPDGVGKSSLLSLISGARVIEQGNVIVLGGdmrdakhrRDV--CPRIAWMPQGlgknlyhTLs 105
Cdd:cd03223 17 LKDLSFEIKPGDRLLITGPSGTGKSSLFRALAGLWPWGSGRIGMPEG--------EDLlfLPQRPYLPLG-------TL- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 106 vyenvdffarlfghdkaeREARITellnstglaPFRDRpagkLSGGMKQKLGLCCALIHDPELLILDEPTTGVDPLSRAQ 185
Cdd:cd03223 81 ------------------REQLIY---------PWDDV----LSGGEQQRLAFARLLLHKPKFVFLDEATSALDEESEDR 129
|
170 180
....*....|....*....|.
gi 446125071 186 FWDLID-------SIRQRQTN 199
Cdd:cd03223 130 LYQLLKelgitviSVGHRPSL 150
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
145-205 |
1.79e-05 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 48.87 E-value: 1.79e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446125071 145 AGKLSGGMKQKLGLCCALIHDPELLILDEPTTGVDPLSRAQFWDLIDSIRQRQTNMSVLVA 205
Cdd:PTZ00265 577 ASKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQKTINNLKGNENRITIIIA 637
|
|
| ABC_Rad50 |
cd03240 |
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ... |
280-440 |
1.82e-05 |
|
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: 46.45 E-value: 1.82e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 280 KDLTMR-FGKFVAVDHVNFRIPrgeIFGFLGSNGCGKSTTM---KM-LTGLLPASegqawLFGQPVDPNDIDTRRRVGYM 354
Cdd:cd03240 2 DKLSIRnIRSFHERSEIEFFSP---LTLIVGQNGAGKTTIIealKYaLTGELPPN-----SKGGAHDPKLIREGEVRAQV 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 355 SQAFSLYN--ELTVRQNLELHARLFHIPPAEIPARVAQMIERfmLTEVEDTLpASLPLgirqRLSLAVAVIHRPEMLILD 432
Cdd:cd03240 74 KLAFENANgkKYTITRSLAILENVIFCHQGESNWPLLDMRGR--CSGGEKVL-ASLII----RLALAETFGSNCGILALD 146
|
....*...
gi 446125071 433 EPTSGVDP 440
Cdd:cd03240 147 EPTTNLDE 154
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
280-498 |
1.88e-05 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 48.62 E-value: 1.88e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 280 KDLTMRF--GKFVAVDHVNFRIPRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGQAWLFGQPVDPNDI-DTRRRVGYMSQ 356
Cdd:PTZ00243 1312 EGVQMRYreGLPLVLRGVSFRIAPREKVGIVGRTGSGKSTLLLTFMRMVEVCGGEIRVNGREIGAYGLrELRRQFSMIPQ 1391
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 357 AFSLYNElTVRQNLE--LHARlfhipPAEIPA---------RVAQMIERFMLTEVEDTLPASlpLGIRQRLSLAVAVIHR 425
Cdd:PTZ00243 1392 DPVLFDG-TVRQNVDpfLEAS-----SAEVWAalelvglreRVASESEGIDSRVLEGGSNYS--VGQRQLMCMARALLKK 1463
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446125071 426 PEMLIL-DEPTSGVDPvARDMFWQLMVdLSRQDKVTIFISTHFMNEAERCDRMSLMHAGKVLASGTPQELVQQR 498
Cdd:PTZ00243 1464 GSGFILmDEATANIDP-ALDRQIQATV-MSAFSAYTVITIAHRLHTVAQYDKIIVMDHGAVAEMGSPRELVMNR 1535
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
40-244 |
2.49e-05 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 48.18 E-value: 2.49e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 40 MVGLIGPDGVGKSSLLSLISGARV---IEQGNVIVLGG----DMRdaKHRRDVCPRIAwmpqglgKNLYH--TLSVYENV 110
Cdd:TIGR00956 89 LTVVLGRPGSGCSTLLKTIASNTDgfhIGVEGVITYDGitpeEIK--KHYRGDVVYNA-------ETDVHfpHLTVGETL 159
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 111 DFFARL-------FGHDKAEREARITELLNST-GLAPFRDRPAGK-----LSGGMKQKLGLCCALIHDPELLILDEPTTG 177
Cdd:TIGR00956 160 DFAARCktpqnrpDGVSREEYAKHIADVYMATyGLSHTRNTKVGNdfvrgVSGGERKRVSIAEASLGGAKIQCWDNATRG 239
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446125071 178 VDPLSRAQFwdlidsIRQRQTNMSVLVATAYM------EEA-ERFDWLVAMNAGEILATGSAQqlRAKTHSATL 244
Cdd:TIGR00956 240 LDSATALEF------IRALKTSANILDTTPLVaiyqcsQDAyELFDKVIVLYEGYQIYFGPAD--KAKQYFEKM 305
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
407-495 |
2.69e-05 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 48.10 E-value: 2.69e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 407 SLPLGIRQRLSLAVAVIHRPEMLILDEPTSGVDPVARDMFWQLMVDLSRQDKVTIFISTHFMNEAERCDRMSLMH----- 481
Cdd:PTZ00265 1358 SLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDIKDKADKTIITIAHRIASIKRSDKIVVFNnpdrt 1437
|
90
....*....|....
gi 446125071 482 AGKVLASGTPQELV 495
Cdd:PTZ00265 1438 GSFVQAHGTHEELL 1451
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
8-179 |
3.55e-05 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 47.55 E-value: 3.55e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 8 PVPPVAQLEGVSQHY-GKTVALNNITLDIPARSMVGLIGPDGVGKSSLLSLISGARVIEQGNVivlggdMRDAKhrrdvc 86
Cdd:PLN03073 504 PGPPIISFSDASFGYpGGPLLFKNLNFGIDLDSRIAMVGPNGIGKSTILKLISGELQPSSGTV------FRSAK------ 571
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 87 PRIAWMPQGL--GKNLYHTLSVYenvdfFARLFghdKAEREARITELLNSTGLA-PFRDRPAGKLSGGMKQKLGLCCALI 163
Cdd:PLN03073 572 VRMAVFSQHHvdGLDLSSNPLLY-----MMRCF---PGVPEQKLRAHLGSFGVTgNLALQPMYTLSGGQKSRVAFAKITF 643
|
170
....*....|....*.
gi 446125071 164 HDPELLILDEPTTGVD 179
Cdd:PLN03073 644 KKPHILLLDEPSNHLD 659
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
84-235 |
3.99e-05 |
|
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of proteins of which all members for which functions are known except the UvrA proteins are involved in the transport of material through membranes. UvrA orthologs are involved in the recognition of DNA damage as a step in nucleotide excision repair. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 273184 [Multi-domain] Cd Length: 925 Bit Score: 47.70 E-value: 3.99e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 84 DVCPRIAWMPQGL-----GKNLYHTL--SVYENVDFFarlfghDKAEREARITELLNSTGLAPFR-DRPAGKLSGGMKQK 155
Cdd:TIGR00630 764 EVCKGKRYNRETLevkykGKNIADVLdmTVEEAYEFF------EAVPSISRKLQTLCDVGLGYIRlGQPATTLSGGEAQR 837
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 156 LGLCCALIHD---PELLILDEPTTGVDPLSRAQFWDLIDSIRQrQTNmSVLVATAYMEEAERFDWLV------AMNAGEI 226
Cdd:TIGR00630 838 IKLAKELSKRstgRTLYILDEPTTGLHFDDIKKLLEVLQRLVD-KGN-TVVVIEHNLDVIKTADYIIdlgpegGDGGGTV 915
|
....*....
gi 446125071 227 LATGSAQQL 235
Cdd:TIGR00630 916 VASGTPEEV 924
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
302-490 |
5.12e-05 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 47.15 E-value: 5.12e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 302 GEIFGFLGSNGCGKSTTMKMLTGLLPAS--EGQAWLFGQPvdpNDIDTRRRV-GYMSQAFSLYNELTVRQNLELHA--RL 376
Cdd:PLN03140 906 GVLTALMGVSGAGKTTLMDVLAGRKTGGyiEGDIRISGFP---KKQETFARIsGYCEQNDIHSPQVTVRESLIYSAflRL 982
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 377 fhipPAEIPAR-----VAQMIERFMLTEVEDT---LPASLPLGI--RQRLSLAVAVIHRPEMLILDEPTSGVDPVARDMF 446
Cdd:PLN03140 983 ----PKEVSKEekmmfVDEVMELVELDNLKDAivgLPGVTGLSTeqRKRLTIAVELVANPSIIFMDEPTSGLDARAAAIV 1058
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 446125071 447 WQLM---VDLSR-------QDKVTIFisthfmneaERCDRMSLM-HAGKVLASGT 490
Cdd:PLN03140 1059 MRTVrntVDTGRtvvctihQPSIDIF---------EAFDELLLMkRGGQVIYSGP 1104
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
45-180 |
5.69e-05 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 45.22 E-value: 5.69e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 45 GPDGVGKSSLLSLISGARVIEQGNVIVLGGDMRDAKHRRdvcpRIAWMPQGLGknLYHTLSVYENVDFFARLFGhdkaeR 124
Cdd:PRK13543 44 GDNGAGKTTLLRVLAGLLHVESGQIQIDGKTATRGDRSR----FMAYLGHLPG--LKADLSTLENLHFLCGLHG-----R 112
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 446125071 125 EARIT--ELLNSTGLAPFRDRPAGKLSGGMKQKLGLCCALIHDPELLILDEPTTGVDP 180
Cdd:PRK13543 113 RAKQMpgSALAIVGLAGYEDTLVRQLSAGQKKRLALARLWLSPAPLWLLDEPYANLDL 170
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
112-529 |
6.74e-05 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 47.13 E-value: 6.74e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 112 FFARLFGHDKAERE------ARITELLNsTGLAPFR-DRPAGKLSGGMKQKLGLCCALihDPELL----ILDEPTTGVDP 180
Cdd:PRK00635 435 FLSQLPSKSLSIEEvlqglkSRLSILID-LGLPYLTpERALATLSGGEQERTALAKHL--GAELIgityILDEPSIGLHP 511
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 181 LSRAQFWDLIDSIRQrQTNMSVLVataymEEAERF----DWLVAMN------AGEILATGSAQQLRAKTHSAT---LEQA 247
Cdd:PRK00635 512 QDTHKLINVIKKLRD-QGNTVLLV-----EHDEQMislaDRIIDIGpgagifGGEVLFNGSPREFLAKSDSLTakyLRQE 585
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 248 FIALLPEaqRQAHKPVVIPPYHAEQEEIaieaKDLTMrfgkfvavdhvnfRIPRGEIFGFLGSNGCGKSTTMKmlTGLLP 327
Cdd:PRK00635 586 LTIPIPE--KRTNSLGTLTLSKATKHNL----KDLTI-------------SLPLGRLTVVTGVSGSGKSSLIN--DTLVP 644
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 328 ASEGqawLFGQPVDPN----------------DIDTR--------------------------RRVGYMSQAFSLYNEL- 364
Cdd:PRK00635 645 AVEE---FIEQGFCSNlsiqwgaisrlvhitrDLPGRsqrsipltyikafddlrelfaeqprsKRLGLTKSHFSFNTPLg 721
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 365 -----------TVRQN------------------LELHARLFHIppAEIPARVAQMIERFMLTEVE-------------D 402
Cdd:PRK00635 722 acaecqglgsiTTTDNrtsipcpsclgkrflpqvLEVRYKGKNI--ADILEMTAYEAEKFFLDEPSihekihalcslglD 799
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 403 TLPASLPL-----GIRQRLSLA---VAVIHRPEMLILDEPTSGVDPVARDMFWQLMVDLSRQDKvTIFISTHFMNEAERC 474
Cdd:PRK00635 800 YLPLGRPLsslsgGEIQRLKLAyelLAPSKKPTLYVLDEPTTGLHTHDIKALIYVLQSLTHQGH-TVVIIEHNMHVVKVA 878
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446125071 475 DRMSLM------HAGKVLASGTPQELVQQRG-AANLEAAFISWLQEaagaAPETPIPPSQTP 529
Cdd:PRK00635 879 DYVLELgpeggnLGGYLLASCSPEELIHLHTpTAKALRPYLSSPQE----LPYLPDPSPKPP 936
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
299-461 |
7.57e-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: 45.44 E-value: 7.57e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 299 IPR-GEIFGFLGSNGCGKSTTMKMLTGLLPASEGQawlFGQPVDPNDIDTRRRVGYMSQAFSLYNELTVR-----QNLEL 372
Cdd:cd03236 22 VPReGQVLGLVGPNGIGKSTALKILAGKLKPNLGK---FDDPPDWDEILDEFRGSELQNYFTKLLEGDVKvivkpQYVDL 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 373 harlfhIPPAeIPARVAQMI----ERFMLTEVEDTLP---------ASLPLGIRQRLSLAVAVIHRPEMLILDEPTSGVD 439
Cdd:cd03236 99 ------IPKA-VKGKVGELLkkkdERGKLDELVDQLElrhvldrniDQLSGGELQRVAIAAALARDADFYFFDEPSSYLD 171
|
170 180
....*....|....*....|..
gi 446125071 440 PVARDMFWQLMVDLSRQDKVTI 461
Cdd:cd03236 172 IKQRLNAARLIRELAEDDNYVL 193
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
147-221 |
9.88e-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: 43.89 E-value: 9.88e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 147 KLSGGMKQKLGLCCALIH-----DPeLLILDEPTTGVDPLSRAQFWDLIdsIRQRQTNMSVLVATAYMEEAERFDWLVAM 221
Cdd:cd03227 77 QLSGGEKELSALALILALaslkpRP-LYILDEIDRGLDPRDGQALAEAI--LEHLVKGAQVIVITHLPELAELADKLIHI 153
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
15-238 |
1.01e-04 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 46.12 E-value: 1.01e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 15 LEGVSQHYGKT-VALNNITLDIPARSMVGLIGPDGVGKSSLLSLISGARVIEQGNvIVLGGDMRDAKHRRDvcpriawmp 93
Cdd:PRK10522 325 LRNVTFAYQDNgFSVGPINLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGE-ILLDGKPVTAEQPED--------- 394
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 94 qglgknlYHTL--SVYENVDFFARLFGHDKAERE-ARITELLNSTGLAPFRDRPAG-----KLSGGMKQKLGLCCALIHD 165
Cdd:PRK10522 395 -------YRKLfsAVFTDFHLFDQLLGPEGKPANpALVEKWLERLKMAHKLELEDGrisnlKLSKGQKKRLALLLALAEE 467
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446125071 166 PELLILDEPTTGVDPLSRAQFW-DLIDsiRQRQTNMSVLVAT---AYMEEAERfdwLVAMNAGEILA-TGSAQQLRAK 238
Cdd:PRK10522 468 RDILLLDEWAADQDPHFRREFYqVLLP--LLQEMGKTIFAIShddHYFIHADR---LLEMRNGQLSElTGEERDAASR 540
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
27-239 |
1.75e-04 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 45.09 E-value: 1.75e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 27 ALNNITLDIPARSMVGLIGPDGVGKSSLLSLISGARVIEQGNVivLGGDMRDAKHRRDVC-PRIAWMPQ-------GLGK 98
Cdd:PRK10789 330 ALENVNFTLKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGDI--RFHDIPLTKLQLDSWrSRLAVVSQtpflfsdTVAN 407
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 99 N--LYHTLSVYENVDFFARLFG-HDKAER--EARITELlNSTGLApfrdrpagkLSGGMKQKLGLCCALIHDPELLILDE 173
Cdd:PRK10789 408 NiaLGRPDATQQEIEHVARLASvHDDILRlpQGYDTEV-GERGVM---------LSGGQKQRISIARALLLNAEILILDD 477
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446125071 174 PTTGVDPLSRAQfwdLIDSIRQRQTNMSVLVATAYMEEAERFDWLVAMNAGEILATGSAQQLRAKT 239
Cdd:PRK10789 478 ALSAVDGRTEHQ---ILHNLRQWGEGRTVIISAHRLSALTEASEILVMQHGHIAQRGNHDQLAQQS 540
|
|
| PRK13541 |
PRK13541 |
cytochrome c biogenesis protein CcmA; Provisional |
30-190 |
1.82e-04 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184128 [Multi-domain] Cd Length: 195 Bit Score: 43.71 E-value: 1.82e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 30 NITLdIPaRSMVGLIGPDGVGKSSLLSLISGARVIEQGNVIVLGGDMRDAKHrrdvcPRIAWMPQGLGKNLyhTLSVYEN 109
Cdd:PRK13541 20 SITF-LP-SAITYIKGANGCGKSSLLRMIAGIMQPSSGNIYYKNCNINNIAK-----PYCTYIGHNLGLKL--EMTVFEN 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 110 VDFFARLFghDKAEreaRITELLNSTGLAPFRDRPAGKLSGGMKQKLGLCCALIHDPELLILDEPTTGVDPLSRAQFWDL 189
Cdd:PRK13541 91 LKFWSEIY--NSAE---TLYAAIHYFKLHDLLDEKCYSLSSGMQKIVAIARLIACQSDLWLLDEVETNLSKENRDLLNNL 165
|
.
gi 446125071 190 I 190
Cdd:PRK13541 166 I 166
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
280-439 |
2.78e-04 |
|
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440858 [Multi-domain] Cd Length: 592 Bit Score: 44.78 E-value: 2.78e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 280 KDLTMRFGK--FVAvdhvnFRIP---RGEIFGFLGSNGCGKSTTMKMLTGLL-PAsegqawlFGQPVDPNDIDT--RRRV 351
Cdd:COG1245 77 EDPVHRYGEngFRL-----YGLPvpkKGKVTGILGPNGIGKSTALKILSGELkPN-------LGDYDEEPSWDEvlKRFR 144
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 352 G-----YMSQafsLYN-ELTVR---QNLELHARLFHIPPAEIPARV------AQMIERFMLTEVEDTLPASLPLGIRQRL 416
Cdd:COG1245 145 GtelqdYFKK---LANgEIKVAhkpQYVDLIPKVFKGTVRELLEKVdergklDELAEKLGLENILDRDISELSGGELQRV 221
|
170 180
....*....|....*....|...
gi 446125071 417 SLAVAVIHRPEMLILDEPTSGVD 439
Cdd:COG1245 222 AIAAALLRDADFYFFDEPSSYLD 244
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
26-231 |
3.41e-04 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 43.66 E-value: 3.41e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 26 VALNNITLDIPARSMVGLIGPDGVGKSSLLSLISG----------ARVieQGNVIVLGGDMRDAKHRRDVCPRiAWMPQG 95
Cdd:PRK13547 15 AILRDLSLRIEPGRVTALLGRNGAGKSTLLKALAGdltgggaprgARV--TGDVTLNGEPLAAIDAPRLARLR-AVLPQA 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 96 LGKNLyhTLSVYENVDF----FARLFGHDKAEREARITELLNSTGLAPFRDRPAGKLSGGMKQKLGLCCAL--------- 162
Cdd:PRK13547 92 AQPAF--AFSAREIVLLgrypHARRAGALTHRDGEIAWQALALAGATALVGRDVTTLSGGELARVQFARVLaqlwpphda 169
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446125071 163 IHDPELLILDEPTTGVDPLSRAQfwdLIDSIRQ--RQTNMSVLVATAYMEEAERFDWLVAMNA-GEILATGS 231
Cdd:PRK13547 170 AQPPRYLLLDEPTAALDLAHQHR---LLDTVRRlaRDWNLGVLAIVHDPNLAARHADRIAMLAdGAIVAHGA 238
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
23-224 |
3.54e-04 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 44.71 E-value: 3.54e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 23 GKTVALNNITLDIPARSMVGLIGPDGVGKSSLLSLISGAR---VIEQGNVIVlGGDMRDAKHRRdvcpRIAWMPQglgkN 99
Cdd:TIGR00956 774 EKRVILNNVDGWVKPGTLTALMGASGAGKTTLLNVLAERVttgVITGGDRLV-NGRPLDSSFQR----SIGYVQQ----Q 844
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 100 LYH--TLSVYENVDFFARLFGHD---KAEREARITELLNSTGLAPFRDRPAGKLSGGM----KQKLGLCCALIHDPELLI 170
Cdd:TIGR00956 845 DLHlpTSTVRESLRFSAYLRQPKsvsKSEKMEYVEEVIKLLEMESYADAVVGVPGEGLnveqRKRLTIGVELVAKPKLLL 924
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 446125071 171 -LDEPTTGVDplSRAQfWDLIDSIRQRQTNMSVLVATAYMEEA---ERFDWLVAMNAG 224
Cdd:TIGR00956 925 fLDEPTSGLD--SQTA-WSICKLMRKLADHGQAILCTIHQPSAilfEEFDRLLLLQKG 979
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
97-317 |
3.89e-04 |
|
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of proteins of which all members for which functions are known except the UvrA proteins are involved in the transport of material through membranes. UvrA orthologs are involved in the recognition of DNA damage as a step in nucleotide excision repair. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 273184 [Multi-domain] Cd Length: 925 Bit Score: 44.23 E-value: 3.89e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 97 GKNL--YHTLSVYENVDFFARLfghDKAEREARITEL-----------LNSTGLAPFR-DRPAGKLSGGMKQKLGLC--- 159
Cdd:TIGR00630 427 GKSIadVSELSIREAHEFFNQL---TLTPEEKKIAEEvlkeirerlgfLIDVGLDYLSlSRAAGTLSGGEAQRIRLAtqi 503
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 160 -CALIHdpELLILDEPTTGVDPLSRAQfwdLIDSIRQ-RQTNMSVLVATAYMEEAERFDWLVAM------NAGEILATGS 231
Cdd:TIGR00630 504 gSGLTG--VLYVLDEPSIGLHQRDNRR---LINTLKRlRDLGNTLIVVEHDEDTIRAADYVIDIgpgageHGGEVVASGT 578
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 232 AQQLRAKTHSAT---LEQAFIALLPEAQRQAHKpvvippyhaeqeeiaieaKDLTMRFGKFVAVDHVNFRIPRGEIFGFL 308
Cdd:TIGR00630 579 PEEILANPDSLTgqyLSGRKKIEVPAERRPGNG------------------KFLTLKGARENNLKNITVSIPLGLFTCIT 640
|
....*....
gi 446125071 309 GSNGCGKST 317
Cdd:TIGR00630 641 GVSGSGKST 649
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
143-317 |
5.18e-04 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 44.05 E-value: 5.18e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 143 RPAGKLSGGMKQKLGLCCALIH---DPELLILDEPTTGVDPLSRAQFWDLIDSIRQRqtNMSVLVATAYMEEAERFDWLV 219
Cdd:PRK00635 805 RPLSSLSGGEIQRLKLAYELLApskKPTLYVLDEPTTGLHTHDIKALIYVLQSLTHQ--GHTVVIIEHNMHVVKVADYVL 882
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 220 AMN------AGEILATGSAQQLRAK-THSATLEQAFIA------LLPEAQRQAHKPVVIPPYHAEQEEIaieakdltmrf 286
Cdd:PRK00635 883 ELGpeggnlGGYLLASCSPEELIHLhTPTAKALRPYLSspqelpYLPDPSPKPPVPADITIKNAYQHNL----------- 951
|
170 180 190
....*....|....*....|....*....|.
gi 446125071 287 gkfvavDHVNFRIPRGEIFGFLGSNGCGKST 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 ... |
281-360 |
6.07e-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: 41.79 E-value: 6.07e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 281 DLTMRFGKFvavdHVNFRIP---RGEIFGFLGSNGCGKSTTMKMLTGLLpasegqawlfgQPVDPNDIDTRRRVGYMSQA 357
Cdd:cd03222 5 DCVKRYGVF----FLLVELGvvkEGEVIGIVGPNGTGKTTAVKILAGQL-----------IPNGDNDEWDGITPVYKPQY 69
|
...
gi 446125071 358 FSL 360
Cdd:cd03222 70 IDL 72
|
|
| ABCC_SUR2 |
cd03288 |
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The ... |
274-498 |
1.01e-03 |
|
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: 41.82 E-value: 1.01e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 274 EIAIEakDLTMRFGKFV--AVDHVNFRIPRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGQAWLFGQPVDPNDIDT-RRR 350
Cdd:cd03288 19 EIKIH--DLCVRYENNLkpVLKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVIDGIDISKLPLHTlRSR 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 351 VGYMSQAFSLYNElTVRQNLELHARLfhippaeIPARVAQMIERFMLTEVEDTLPASL-----------PLGIRQRLSLA 419
Cdd:cd03288 97 LSIILQDPILFSG-SIRFNLDPECKC-------TDDRLWEALEIAQLKNMVKSLPGGLdavvteggenfSVGQRQLFCLA 168
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446125071 420 VAVIHRPEMLILDEPTSGVDpVARDMFWQLMVDLSRQDKVTIFIStHFMNEAERCDRMSLMHAGKVLASGTPQELVQQR 498
Cdd:cd03288 169 RAFVRKSSILIMDEATASID-MATENILQKVVMTAFADRTVVTIA-HRVSTILDADLVLVLSRGILVECDTPENLLAQE 245
|
|
| PRK15369 |
PRK15369 |
two component system response regulator; |
158-249 |
1.04e-03 |
|
two component system response regulator;
Pssm-ID: 185267 [Multi-domain] Cd Length: 211 Bit Score: 41.60 E-value: 1.04e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 158 LCCALihDPELLILDEPTTGVDPLsraqfwDLIDSIRQRQTNMSVLVATAYMEEAERFDWLVAMNAGEILATGSAQQLRA 237
Cdd:PRK15369 44 ACRQL--EPDIVILDLGLPGMNGL------DVIPQLHQRWPAMNILVLTARQEEHMASRTLAAGALGYVLKKSPQQILLA 115
|
90
....*....|..
gi 446125071 238 KTHSATLEQAFI 249
Cdd:PRK15369 116 AIQTVAVGKRYI 127
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
280-439 |
1.72e-03 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 42.10 E-value: 1.72e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 280 KDLTMRFGK--FVAvdhvnFRIP---RGEIFGFLGSNGCGKSTTMKMLTG-LLPAsegqawlFGQPVDPNDIDT--RRRV 351
Cdd:PRK13409 77 EEPVHRYGVngFKL-----YGLPipkEGKVTGILGPNGIGKTTAVKILSGeLIPN-------LGDYEEEPSWDEvlKRFR 144
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 352 G-----YMSQafsLYN-ELTVR---QNLELHARLFHIPPAEIPARVA------QMIERFMLTEVEDTLPASLPLGIRQRL 416
Cdd:PRK13409 145 GtelqnYFKK---LYNgEIKVVhkpQYVDLIPKVFKGKVRELLKKVDergkldEVVERLGLENILDRDISELSGGELQRV 221
|
170 180
....*....|....*....|...
gi 446125071 417 SLAVAVIHRPEMLILDEPTSGVD 439
Cdd:PRK13409 222 AIAAALLRDADFYFFDEPTSYLD 244
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
15-179 |
4.03e-03 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 40.65 E-value: 4.03e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 15 LEGVSQHYGKTVALNNITLDIPARSMVGLIGPDGVGKSSLLSLISGARVIEQGNVivlggdmrdaKHRRDVcpRIAWMPQ 94
Cdd:PRK15064 322 VENLTKGFDNGPLFKNLNLLLEAGERLAIIGENGVGKTTLLRTLVGELEPDSGTV----------KWSENA--NIGYYAQ 389
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 95 GLGKNLYHTLSVYENVDFFaRLFGHDKAEREARITELLNSTGLAPfrdRPAGKLSGGMKQKLGLCCALIHDPELLILDEP 174
Cdd:PRK15064 390 DHAYDFENDLTLFDWMSQW-RQEGDDEQAVRGTLGRLLFSQDDIK---KSVKVLSGGEKGRMLFGKLMMQKPNVLVMDEP 465
|
....*
gi 446125071 175 TTGVD 179
Cdd:PRK15064 466 TNHMD 470
|
|
| YhgE |
COG1511 |
Uncharacterized membrane protein YhgE, phage infection protein (PIP) family [Function unknown]; ... |
550-696 |
4.45e-03 |
|
Uncharacterized membrane protein YhgE, phage infection protein (PIP) family [Function unknown];
Pssm-ID: 441120 Cd Length: 225 Bit Score: 39.54 E-value: 4.45e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 550 RREALELRRDPVrSTLALLGTVILMLIMG--YGISM-----DVENLRFAVLDRDQTVSSQAWSLN--------LAGSRYF 614
Cdd:COG1511 2 KRELKRLFKNKL-ALIALIALILVPLLYAglYLWAFwdpygNLDNLPVAVVNEDKGATVDGKTVNlgdelvdeLKDNDSF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 615 IEQppLASYDELDRRMRSGELAVAIEIPPNFGRDIAR-----GTPAQIGVWVDGAM----PSRAETVKGYVQAMHQSWLQ 685
Cdd:COG1511 81 DWQ--FVSEEEAEKGLKDGKYYAVIVIPEDFSANLASllsddPEKATITYYTNEANnylaSKITDTAATTVVDQVNSQVT 158
|
170
....*....|.
gi 446125071 686 EAASRQPNPVK 696
Cdd:COG1511 159 ETYAETVSPVA 169
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
277-324 |
5.51e-03 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 39.63 E-value: 5.51e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*...
gi 446125071 277 IEAKDLTMRFGKFVAVDHVNFRIPRGEIFGFLGSNGCGKSTTMKMLTG 324
Cdd:CHL00131 8 LEIKNLHASVNENEILKGLNLSINKGEIHAIMGPNGSGKSTLSKVIAG 55
|
|
| ABC_Rad50 |
cd03240 |
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ... |
143-206 |
7.72e-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: 38.74 E-value: 7.72e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446125071 143 RPAGKLSGGMKQKLGLC--CAL----IHDPELLILDEPTTGVDPLSRA-QFWDLIDSiRQRQTNMSVLVAT 206
Cdd:cd03240 111 DMRGRCSGGEKVLASLIirLALaetfGSNCGILALDEPTTNLDEENIEeSLAEIIEE-RKSQKNFQLIVIT 180
|
|
| ABC-2_lan_permease_MutG |
cd21808 |
lantibiotic immunity ABC transporter MutG family permease (also called ABC-2 transporter MutG ... |
722-821 |
8.55e-03 |
|
lantibiotic immunity ABC transporter MutG family permease (also called ABC-2 transporter MutG family permease) subunit; This subfamily includes lantibiotic ABC transporter permease subunit MutG which is a highly hydrophobic, integral membrane protein, and part of the bacitracin ABC transport system that confers resistance to the Gram-positive bacteria in which this system operates, specifically to lantibiotic mutacin. Lantibiotics are small peptides, produced by Gram-positive bacteria, which are ribosomally-synthesized as pre-peptides and act by disrupting membrane integrity. Genes encoding the lantibiotic ABC transporter subunits are highly organized in operons containing all the genes required for maturation, transport, immunity, and synthesis. For example, in Streptococcus mutans CH43, the lantibiotic mutacin is active against other Gram-positive bacteria via various modes of actions; however, its self-protection against the pore-forming mutacin is mediated by the ABC transporter composed of MutF, MutE, and MutG. This subfamily includes the MutG permease subunit that transports mutacin to the surface and expels it from the membrane.
Pssm-ID: 409633 Cd Length: 237 Bit Score: 39.06 E-value: 8.55e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446125071 722 AVIPLLLmmipSMLSALSVVREKELGSMINLYVTPTTRSEFLLGKqlpyiaLGMLNFLLLCA--LSVFVFGVPLKGSFLT 799
Cdd:cd21808 50 IAFPLLI----GIVCGLVVEQEEEAGNFQNLLGTPSSRSKAYLSK------LLLLLLLGLLSilLAVLIFGIGFKFLLGI 119
|
90 100
....*....|....*....|..
gi 446125071 800 LTLAALLYVIIAtgLGLLISTF 821
Cdd:cd21808 120 NIIPYGFYLLAA--LLLFLGSL 139
|
|
| |
