|
Name |
Accession |
Description |
Interval |
E-value |
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
8-623 |
3.44e-129 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 401.81 E-value: 3.44e-129
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857580 8 AIRLEGVVKTFpnpldaaRPIRAVDGISLK--AGgaeasdRLIALVGPDGAGKSTFMRLLCGLEAPDEGRLSVLGTtpDP 85
Cdd:NF033858 1 VARLEGVSHRY-------GKTVALDDVSLDipAG------CMVGLIGPDGVGKSSLLSLIAGARKIQQGRVEVLGG--DM 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857580 86 DN----EDFTTRIAFMPQTLG--LYKTLSCRENLEVFAGLRGFegeadGAAGLERRIAELLSMTGLAGFEERQAGKLSGG 159
Cdd:NF033858 66 ADarhrRAVCPRIAYMPQGLGknLYPTLSVFENLDFFGRLFGQ-----DAAERRRRIDELLRATGLAPFADRPAGKLSGG 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857580 160 MKQKLALASALLRIPDLLLLDEPTVGVDPLSRRELWSVVRRMLADTP-MTCVFSTAYLEEAEAADRVLLFESGRIIADEN 238
Cdd:NF033858 141 MKQKLGLCCALIHDPDLLILDEPTTGVDPLSRRQFWELIDRIRAERPgMSVLVATAYMEEAERFDWLVAMDAGRVLATGT 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857580 239 PQSfisrakgrtyllplanraehdaqmlcrrLSEETAAtrsdalfldivprmggaaattlaptlpvkdarvpsgfiprqP 318
Cdd:NF033858 221 PAE----------------------------LLARTGA-----------------------------------------D 231
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857580 319 SLEDAY-ALLtfPRAPKTANH-LASPPSDASGalaasaasaddtaERPVVIRADGIARKFGNFVAVADTSFEVRRGEIFG 396
Cdd:NF033858 232 TLEAAFiALL--PEEKRRGHQpVVIPPRPADD-------------DDEPAIEARGLTMRFGDFTAVDHVSFRIRRGEIFG 296
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857580 397 LLGPNGAGKTTTFRMLCGLLVPSKGQI-----EVAGYDLRTakagaRARIGYVAQKFSLYGKLSVEQNLRYFGRSYGFFG 471
Cdd:NF033858 297 FLGSNGCGKSTTMKMLTGLLPASEGEAwlfgqPVDAGDIAT-----RRRVGYMSQAFSLYGELTVRQNLELHARLFHLPA 371
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857580 472 QALQDRIDASLEDFGLTDRRDTTAGSLSFGAKQDLSMACGLIHSPEILFLDEATSGADLASRRAFWRRINALA-SAGTSV 550
Cdd:NF033858 372 AEIAARVAEMLERFDLADVADALPDSLPLGIRQRLSLAVAVIHKPELLILDEPTSGVDPVARDMFWRLLIELSrEDGVTI 451
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2553857580 551 VVTTHFLEEAEYCDRFLIQDAGKVLALGTPRE-VKQRAAvlsavsgQSLvvdrmsiEDAFVA-IVEAGRRSQETP 623
Cdd:NF033858 452 FISTHFMNEAERCDRISLMHAGRVLASDTPAAlVAARGA-------ATL-------EEAFIAyLEEAAGAAAAPA 512
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
367-618 |
1.71e-98 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 300.44 E-value: 1.71e-98
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857580 367 IRADGIARKFGNFVAVADTSFEVRRGEIFGLLGPNGAGKTTTFRMLCGLLVPSKGQIEVAGYDLRTAKAGARARIGYVAQ 446
Cdd:COG1131 1 IEVRGLTKRYGDKTALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRVLGEDVARDPAEVRRRIGYVPQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857580 447 KFSLYGKLSVEQNLRYFGRSYGFFGQALQDRIDASLEDFGLTDRRDTTAGSLSFGAKQDLSMACGLIHSPEILFLDEATS 526
Cdd:COG1131 81 EPALYPDLTVRENLRFFARLYGLPRKEARERIDELLELFGLTDAADRKVGTLSGGMKQRLGLALALLHDPELLILDEPTS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857580 527 GADLASRRAFWRRINALASAGTSVVVTTHFLEEAEY-CDRFLIQDAGKVLALGTPREVKQRAavlsavsgqslvvdrmsI 605
Cdd:COG1131 161 GLDPEARRELWELLRELAAEGKTVLLSTHYLEEAERlCDRVAIIDKGRIVADGTPDELKARL-----------------L 223
|
250
....*....|...
gi 2553857580 606 EDAFVAIVEAGRR 618
Cdd:COG1131 224 EDVFLELTGEEAR 236
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
366-613 |
6.72e-76 |
|
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: 242.07 E-value: 6.72e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857580 366 VIRADGIARKFGNFVAVADTSFEVRRGEIFGLLGPNGAGKTTTFRMLCGLLVPSKGQIEVAGYDLRTAKAGARARIGYVA 445
Cdd:COG4555 1 MIEVENLSKKYGKVPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIDGEDVRKEPREARRQIGVLP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857580 446 QKFSLYGKLSVEQNLRYFGRSYGFFGQALQDRIDASLEDFGLTDRRDTTAGSLSFGAKQDLSMACGLIHSPEILFLDEAT 525
Cdd:COG4555 81 DERGLYDRLTVRENIRYFAELYGLFDEELKKRIEELIELLGLEEFLDRRVGELSTGMKKKVALARALVHDPKVLLLDEPT 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857580 526 SGADLASRRAFWRRINALASAGTSVVVTTHFLEEAE-YCDRFLIQDAGKVLALGTPREVKQRaavlsavsgqslvVDRMS 604
Cdd:COG4555 161 NGLDVMARRLLREILRALKKEGKTVLFSSHIMQEVEaLCDRVVILHKGKVVAQGSLDELREE-------------IGEEN 227
|
....*....
gi 2553857580 605 IEDAFVAIV 613
Cdd:COG4555 228 LEDAFVALI 236
|
|
| drrA |
TIGR01188 |
daunorubicin resistance ABC transporter ATP-binding subunit; This model describes daunorubicin ... |
374-587 |
8.04e-74 |
|
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: 238.83 E-value: 8.04e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857580 374 RKFGNFVAVADTSFEVRRGEIFGLLGPNGAGKTTTFRMLCGLLVPSKGQIEVAGYDLRTAKAGARARIGYVAQKFSLYGK 453
Cdd:TIGR01188 1 KVYGDFKAVDGVNFKVREGEVFGFLGPNGAGKTTTIRMLTTLLRPTSGTARVAGYDVVREPRKVRRSIGIVPQYASVDED 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857580 454 LSVEQNLRYFGRSYGFFGQALQDRIDASLEDFGLTDRRDTTAGSLSFGAKQDLSMACGLIHSPEILFLDEATSGADLASR 533
Cdd:TIGR01188 81 LTGRENLEMMGRLYGLPKDEAEERAEELLELFELGEAADRPVGTYSGGMRRRLDIAASLIHQPDVLFLDEPTTGLDPRTR 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 2553857580 534 RAFWRRINALASAGTSVVVTTHFLEEAE-YCDRFLIQDAGKVLALGTPREVKQRA 587
Cdd:TIGR01188 161 RAIWDYIRALKEEGVTILLTTHYMEEADkLCDRIAIIDHGRIIAEGTPEELKRRL 215
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
367-584 |
2.84e-72 |
|
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein component of a bacterial exporter complex that confers resistance to the antibiotics daunorubicin and doxorubicin. In addition to DrrA, the complex includes an integral membrane protein called DrrB. DrrA belongs to the ABC family of transporters and shares sequence and functional similarities with a protein found in cancer cells called P-glycoprotein. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region in addition to the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213232 [Multi-domain] Cd Length: 220 Bit Score: 231.88 E-value: 2.84e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857580 367 IRADGIARKFGNFVAVADTSFEVRRGEIFGLLGPNGAGKTTTFRMLCGLLVPSKGQIEVAGYDLRTAKAGARARIGYVAQ 446
Cdd:cd03265 1 IEVENLVKKYGDFEAVRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATVAGHDVVREPREVRRRIGIVFQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857580 447 KFSLYGKLSVEQNLRYFGRSYGFFGQALQDRIDASLEDFGLTDRRDTTAGSLSFGAKQDLSMACGLIHSPEILFLDEATS 526
Cdd:cd03265 81 DLSVDDELTGWENLYIHARLYGVPGAERRERIDELLDFVGLLEAADRLVKTYSGGMRRRLEIARSLVHRPEVLFLDEPTI 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857580 527 GADLASRRAFWRRINAL-ASAGTSVVVTTHFLEEAE-YCDRFLIQDAGKVLALGTPREVK 584
Cdd:cd03265 161 GLDPQTRAHVWEYIEKLkEEFGMTILLTTHYMEEAEqLCDRVAIIDHGRIIAEGTPEELK 220
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
375-584 |
8.17e-71 |
|
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: 228.16 E-value: 8.17e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857580 375 KFGNFVAVADTSFEVRRGEIFGLLGPNGAGKTTTFRMLCGLLVPSKGQIEVAGYDLRTAKAGARARIGYVAQKFSLYGKL 454
Cdd:cd03263 11 KKGTKPAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYINGYSIRTDRKAARQSLGYCPQFDALFDEL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857580 455 SVEQNLRYFGRSYGFFGQALQDRIDASLEDFGLTDRRDTTAGSLSFGAKQDLSMACGLIHSPEILFLDEATSGADLASRR 534
Cdd:cd03263 91 TVREHLRFYARLKGLPKSEIKEEVELLLRVLGLTDKANKRARTLSGGMKRKLSLAIALIGGPSVLLLDEPTSGLDPASRR 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 2553857580 535 AFWRRINALASaGTSVVVTTHFLEEAEY-CDRFLIQDAGKVLALGTPREVK 584
Cdd:cd03263 171 AIWDLILEVRK-GRSIILTTHSMDEAEAlCDRIAIMSDGKLRCIGSPQELK 220
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
9-246 |
5.93e-67 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 218.39 E-value: 5.93e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857580 9 IRLEGVVKTFPNpldaarpIRAVDGISL--KAGgaeasdRLIALVGPDGAGKSTFMRLLCGLEAPDEGRLSVLGTTPDPD 86
Cdd:COG1131 1 IEVRGLTKRYGD-------KTALDGVSLtvEPG------EIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRVLGEDVARD 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857580 87 NEDFTTRIAFMPQTLGLYKTLSCRENLEVFAGLRGFEGEAdgaagLERRIAELLSMTGLAGFEERQAGKLSGGMKQKLAL 166
Cdd:COG1131 68 PAEVRRRIGYVPQEPALYPDLTVRENLRFFARLYGLPRKE-----ARERIDELLELFGLTDAADRKVGTLSGGMKQRLGL 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857580 167 ASALLRIPDLLLLDEPTVGVDPLSRRELWSVVRRmLADTPMTCVFSTAYLEEAEA-ADRVLLFESGRIIADENPQSFISR 245
Cdd:COG1131 143 ALALLHDPELLILDEPTSGLDPEARRELWELLRE-LAAEGKTVLLSTHYLEEAERlCDRVAIIDKGRIVADGTPDELKAR 221
|
.
gi 2553857580 246 A 246
Cdd:COG1131 222 L 222
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
367-574 |
1.04e-66 |
|
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: 215.34 E-value: 1.04e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857580 367 IRADGIARKFGNFVAVADTSFEVRRGEIFGLLGPNGAGKTTTFRMLCGLLVPSKGQIEVAGYDLRTAKAGARARIGYVAQ 446
Cdd:cd03230 1 IEVRNLSKRYGKKTALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVLGKDIKKEPEEVKRRIGYLPE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857580 447 KFSLYGKLSVEQNLRYfgrsygffgqalqdridasledfgltdrrdttagslSFGAKQDLSMACGLIHSPEILFLDEATS 526
Cdd:cd03230 81 EPSLYENLTVRENLKL------------------------------------SGGMKQRLALAQALLHDPELLILDEPTS 124
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 2553857580 527 GADLASRRAFWRRINALASAGTSVVVTTHFLEEAE-YCDRFLIQDAGKV 574
Cdd:cd03230 125 GLDPESRREFWELLRELKKEGKTILLSSHILEEAErLCDRVAILNNGRI 173
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
367-578 |
1.33e-59 |
|
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: 198.36 E-value: 1.33e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857580 367 IRADGIARKFGN----FVAVADTSFEVRRGEIFGLLGPNGAGKTTTFRMLCGLLVPSKGQIEVAGYDLRTAKAGARARIG 442
Cdd:cd03266 2 ITADALTKRFRDvkktVQAVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDGFDVVKEPAEARRRLG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857580 443 YVAQKFSLYGKLSVEQNLRYFGRSYGFFGQALQDRIDASLEDFGLTDRRDTTAGSLSFGAKQDLSMACGLIHSPEILFLD 522
Cdd:cd03266 82 FVSDSTGLYDRLTARENLEYFAGLYGLKGDELTARLEELADRLGMEELLDRRVGGFSTGMRQKVAIARALVHDPPVLLLD 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 2553857580 523 EATSGADLASRRAFWRRINALASAGTSVVVTTHFLEEAE-YCDRFLIQDAGKVLALG 578
Cdd:cd03266 162 EPTTGLDVMATRALREFIRQLRALGKCILFSTHIMQEVErLCDRVVVLHRGRVVYEG 218
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
366-588 |
8.84e-57 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 193.79 E-value: 8.84e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857580 366 VIRADGIARKFGNFVAVADTSFEVRRGEIFGLLGPNGAGKTTTFRMLCGLLVPSKGQIEVAGYDLRtakAGARARIGYVA 445
Cdd:COG4152 1 MLELKGLTKRFGDKTAVDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDSGEVLWDGEPLD---PEDRRRIGYLP 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857580 446 QKFSLYGKLSVEQNLRYFGRSYGFFGQALQDRIDASLEDFGLTDRRDTTAGSLSFGAKQDLSMACGLIHSPEILFLDEAT 525
Cdd:COG4152 78 EERGLYPKMKVGEQLVYLARLKGLSKAEAKRRADEWLERLGLGDRANKKVEELSKGNQQKVQLIAALLHDPELLILDEPF 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2553857580 526 SGADLASRRAFWRRINALASAGTSVVVTTHFLEEAE-YCDRFLIQDAGKVLALGTPREVKQRAA 588
Cdd:COG4152 158 SGLDPVNVELLKDVIRELAAKGTTVIFSSHQMELVEeLCDRIVIINKGRKVLSGSVDEIRRQFG 221
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
367-578 |
9.43e-55 |
|
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: 185.18 E-value: 9.43e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857580 367 IRADGIARKFGNFVAVADTSFEVRRGEIFGLLGPNGAGKTTTFRMLCGLLVPSKGQIEVAGYDLRTAkagARARIGYVAQ 446
Cdd:cd03269 1 LEVENVTKRFGRVTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDGKPLDIA---ARNRIGYLPE 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857580 447 KFSLYGKLSVEQNLRYFGRSYGFFGQALQDRIDASLEDFGLTDRRDTTAGSLSFGAKQDLSMACGLIHSPEILFLDEATS 526
Cdd:cd03269 78 ERGLYPKMKVIDQLVYLAQLKGLKKEEARRRIDEWLERLELSEYANKRVEELSKGNQQKVQFIAAVIHDPELLILDEPFS 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 2553857580 527 GADLASRRAFWRRINALASAGTSVVVTTHFLEEAE-YCDRFLIQDAGKVLALG 578
Cdd:cd03269 158 GLDPVNVELLKDVIRELARAGKTVILSTHQMELVEeLCDRVLLLNKGRAVLYG 210
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
6-583 |
7.66e-54 |
|
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: 192.04 E-value: 7.66e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857580 6 APAIRLEGVVKTFPnpldaARPIRAVDGISLKAGGAEAsdrlIALVGPDGAGKSTFMRLLCGLEAPD---EGRLSVLGTT 82
Cdd:COG1123 2 TPLLEVRDLSVRYP-----GGDVPAVDGVSLTIAPGET----VALVGESGSGKSTLALALMGLLPHGgriSGEVLLDGRD 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857580 83 PDPDNEDF-TTRIAFMPQtlglyktlscrENLEVFAGLR-------GFEGEADGAAGLERRIAELLSMTGLAGFEERQAG 154
Cdd:COG1123 73 LLELSEALrGRRIGMVFQ-----------DPMTQLNPVTvgdqiaeALENLGLSRAEARARVLELLEAVGLERRLDRYPH 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857580 155 KLSGGMKQKLALASALLRIPDLLLLDEPTVGVDPLSRRELWSVVRRMLADTPMTCVFSTAYLEE-AEAADRVLLFESGRI 233
Cdd:COG1123 142 QLSGGQRQRVAIAMALALDPDLLIADEPTTALDVTTQAEILDLLRELQRERGTTVLLITHDLGVvAEIADRVVVMDDGRI 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857580 234 IADENPQSFISRAkgrtyllplanraehdaQMLcrrlseetaatrSDALFLDIVPRMGGAAATTLAPTLPVKDARVpsgf 313
Cdd:COG1123 222 VEDGPPEEILAAP-----------------QAL------------AAVPRLGAARGRAAPAAAAAEPLLEVRNLSK---- 268
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857580 314 iprqpsledayallTFPRAPKTAnhlasppsdasgalaasaasaddtaerpvviradgiarkfgnFVAVADTSFEVRRGE 393
Cdd:COG1123 269 --------------RYPVRGKGG------------------------------------------VRAVDDVSLTLRRGE 292
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857580 394 IFGLLGPNGAGKTTTFRMLCGLLVPSKGQIEVAGYDLRTAKAGA----RARIGYVAQ--KFSLYGKLSVEQNLRYFGRSY 467
Cdd:COG1123 293 TLGLVGESGSGKSTLARLLLGLLRPTSGSILFDGKDLTKLSRRSlrelRRRVQMVFQdpYSSLNPRMTVGDIIAEPLRLH 372
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857580 468 GFF-GQALQDRIDASLEDFGL-TDRRDTTAGSLSFGAKQDLSMACGLIHSPEILFLDEATSGADLASRRAFWRRINAL-A 544
Cdd:COG1123 373 GLLsRAERRERVAELLERVGLpPDLADRYPHELSGGQRQRVAIARALALEPKLLILDEPTSALDVSVQAQILNLLRDLqR 452
|
570 580 590 600
....*....|....*....|....*....|....*....|
gi 2553857580 545 SAGTSVVVTTHFLEEAEY-CDRFLIQDAGKVLALGTPREV 583
Cdd:COG1123 453 ELGLTYLFISHDLAVVRYiADRVAVMYDGRIVEDGPTEEV 492
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
367-589 |
8.41e-51 |
|
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: 175.70 E-value: 8.41e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857580 367 IRADGIARKFGNFVAVADTSFEVRRGEIFGLLGPNGAGKTTTFRMLCGLLVPSKGQIEVAGYDLRTAKAGARARIGyVAQ 446
Cdd:cd03219 1 LEVRGLTKRFGGLVALDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFDGEDITGLPPHEIARLG-IGR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857580 447 KF---SLYGKLSVEQNLR---YFGRSYGFFG-------QALQDRIDASLEDFGLTDRRDTTAGSLSFGAKQDLSMACGLI 513
Cdd:cd03219 80 TFqipRLFPELTVLENVMvaaQARTGSGLLLararreeREARERAEELLERVGLADLADRPAGELSYGQQRRLEIARALA 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2553857580 514 HSPEILFLDEATSGADLASRRAFWRRINALASAGTSVVVTTHFLEE-AEYCDRFLIQDAGKVLALGTPREVKQRAAV 589
Cdd:cd03219 160 TDPKLLLLDEPAAGLNPEETEELAELIRELRERGITVLLVEHDMDVvMSLADRVTVLDQGRVIAEGTPDEVRNNPRV 236
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
377-583 |
1.74e-50 |
|
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: 174.44 E-value: 1.74e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857580 377 GNFVAVADTSFEVRRGEIFGLLGPNGAGKTTTFRMLCGLLVPSKGQIEVAGYDLRTAKAGA-RARIGYV-----AQKFSl 450
Cdd:COG1122 12 GGTPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVDGKDITKKNLRElRRKVGLVfqnpdDQLFA- 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857580 451 ygkLSVEQN----LRYFGRSygffGQALQDRIDASLEDFGLTDRRDTTAGSLSFGAKQDLSMACGLIHSPEILFLDEATS 526
Cdd:COG1122 91 ---PTVEEDvafgPENLGLP----REEIRERVEEALELVGLEHLADRPPHELSGGQKQRVAIAGVLAMEPEVLVLDEPTA 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 2553857580 527 GADLASRRAFWRRINALASAGTSVVVTTHFLEEA-EYCDRFLIQDAGKVLALGTPREV 583
Cdd:COG1122 164 GLDPRGRRELLELLKRLNKEGKTVIIVTHDLDLVaELADRVIVLDDGRIVADGTPREV 221
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
364-592 |
6.73e-50 |
|
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid transport and metabolism];
Pssm-ID: 440180 [Multi-domain] Cd Length: 257 Bit Score: 173.69 E-value: 6.73e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857580 364 PVVIRADGIARKFGNFVAVADTSFEVRRGEIFGLLGPNGAGKTTTFRMLCGLLVPSKGQIEVAGYDLRTAKAGARARIGy 443
Cdd:COG0411 2 DPLLEVRGLTKRFGGLVAVDDVSLEVERGEIVGLIGPNGAGKTTLFNLITGFYRPTSGRILFDGRDITGLPPHRIARLG- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857580 444 VAQKF---SLYGKLSVEQNLR---YFGRSYGFFG------------QALQDRIDASLEDFGLTDRRDTTAGSLSFGAKQD 505
Cdd:COG0411 81 IARTFqnpRLFPELTVLENVLvaaHARLGRGLLAallrlprarreeREARERAEELLERVGLADRADEPAGNLSYGQQRR 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857580 506 LSMACGLIHSPEILFLDEATSGADLASRRAFWRRINAL-ASAGTSVVVTTHFLEE-AEYCDRFLIQDAGKVLALGTPREV 583
Cdd:COG0411 161 LEIARALATEPKLLLLDEPAAGLNPEETEELAELIRRLrDERGITILLIEHDMDLvMGLADRIVVLDFGRVIAEGTPAEV 240
|
....*....
gi 2553857580 584 KQRAAVLSA 592
Cdd:COG0411 241 RADPRVIEA 249
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
366-583 |
7.95e-50 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 175.38 E-value: 7.95e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857580 366 VIRADGIARKFGNFVAVADTSFEVRRGEIFGLLGPNGAGKTTTFRMLCGLLVPSKGQIEVAGYDLRTAKAGARARIGYVA 445
Cdd:PRK13537 7 PIDFRNVEKRYGDKLVVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCGEPVPSRARHARQRVGVVP 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857580 446 QKFSLYGKLSVEQNLRYFGRSYGFFGQALQDRIDASLEDFGLTDRRDTTAGSLSFGAKQDLSMACGLIHSPEILFLDEAT 525
Cdd:PRK13537 87 QFDNLDPDFTVRENLLVFGRYFGLSAAAARALVPPLLEFAKLENKADAKVGELSGGMKRRLTLARALVNDPDVLVLDEPT 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 2553857580 526 SGADLASRRAFWRRINALASAGTSVVVTTHFLEEAE-YCDRFLIQDAGKVLALGTPREV 583
Cdd:PRK13537 167 TGLDPQARHLMWERLRSLLARGKTILLTTHFMEEAErLCDRLCVIEEGRKIAEGAPHAL 225
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
367-589 |
3.50e-49 |
|
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: 171.19 E-value: 3.50e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857580 367 IRADGIARKFGNFVAVADTSFEVRRGEIFGLLGPNGAGKTTTFRMLCGLLVPSKGQIEVAGYDLRTAKAGARAR--IGYV 444
Cdd:cd03218 1 LRAENLSKRYGKRKVVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDGQDITKLPMHKRARlgIGYL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857580 445 AQKFSLYGKLSVEQNLRYFGRSYGFFGQALQDRIDASLEDFGLTDRRDTTAGSLSFGAKQDLSMACGLIHSPEILFLDEA 524
Cdd:cd03218 81 PQEASIFRKLTVEENILAVLEIRGLSKKEREEKLEELLEEFHITHLRKSKASSLSGGERRRVEIARALATNPKFLLLDEP 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2553857580 525 TSGADLASRRAFWRRINALASAGTSVVVTTHFLEEA-EYCDRFLIQDAGKVLALGTPREVKQRAAV 589
Cdd:cd03218 161 FAGVDPIAVQDIQKIIKILKDRGIGVLITDHNVRETlSITDRAYIIYEGKVLAEGTPEEIAANELV 226
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
9-245 |
4.13e-49 |
|
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: 171.19 E-value: 4.13e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857580 9 IRLEGVVKTFPNpldaarpIRAVDGISLKAggaeASDRLIALVGPDGAGKSTFMRLLCGLEAPDEGRLSVLGTTPDPDNE 88
Cdd:COG4555 2 IEVENLSKKYGK-------VPALKDVSFTA----KDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIDGEDVRKEPR 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857580 89 DFTTRIAFMPQTLGLYKTLSCRENLEVFAGLRGFEGEAdgaagLERRIAELLSMTGLAGFEERQAGKLSGGMKQKLALAS 168
Cdd:COG4555 71 EARRQIGVLPDERGLYDRLTVRENIRYFAELYGLFDEE-----LKKRIEELIELLGLEEFLDRRVGELSTGMKKKVALAR 145
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2553857580 169 ALLRIPDLLLLDEPTVGVDPLSRRELWSVVRRmLADTPMTCVFSTAYLEEAEA-ADRVLLFESGRIIADENPQSFISR 245
Cdd:COG4555 146 ALVHDPKVLLLDEPTNGLDVMARRLLREILRA-LKKEGKTVLFSSHIMQEVEAlCDRVVILHKGKVVAQGSLDELREE 222
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
364-583 |
2.46e-47 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 169.63 E-value: 2.46e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857580 364 PVVIRADGIARKFGNFVAVADTSFEVRRGEIFGLLGPNGAGKTTTFRMLCGLLVPSKGQIEVAGYDLRTAKAGARARIGY 443
Cdd:PRK13536 39 TVAIDLAGVSKSYGDKAVVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKITVLGVPVPARARLARARIGV 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857580 444 VAQKFSLYGKLSVEQNLRYFGRSYGFFGQALQDRIDASLEDFGLTDRRDTTAGSLSFGAKQDLSMACGLIHSPEILFLDE 523
Cdd:PRK13536 119 VPQFDNLDLEFTVRENLLVFGRYFGMSTREIEAVIPSLLEFARLESKADARVSDLSGGMKRRLTLARALINDPQLLILDE 198
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2553857580 524 ATSGADLASRRAFWRRINALASAGTSVVVTTHFLEEAE-YCDRFLIQDAGKVLALGTPREV 583
Cdd:PRK13536 199 PTTGLDPHARHLIWERLRSLLARGKTILLTTHFMEEAErLCDRLCVLEAGRKIAEGRPHAL 259
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
366-571 |
3.51e-46 |
|
ABC-type transport system involved in cytochrome c biogenesis, ATPase component [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 443308 [Multi-domain] Cd Length: 206 Bit Score: 161.88 E-value: 3.51e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857580 366 VIRADGIARKFGNFVAVADTSFEVRRGEIFGLLGPNGAGKTTTFRMLCGLLVPSKGQIEVAGYDLRTAKAGARARIGYVA 445
Cdd:COG4133 2 MLEAENLSCRRGERLLFSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWNGEPIRDAREDYRRRLAYLG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857580 446 QKFSLYGKLSVEQNLRYFGRSYGFFGQAlqDRIDASLEDFGLTDRRDTTAGSLSFGAKQDLSMACGLIHSPEILFLDEAT 525
Cdd:COG4133 82 HADGLKPELTVRENLRFWAALYGLRADR--EAIDEALEAVGLAGLADLPVRQLSAGQKRRVALARLLLSPAPLWLLDEPF 159
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 2553857580 526 SGADLASRRAFWRRINALASAGTSVVVTTHFLEEAEYCDRFLIQDA 571
Cdd:COG4133 160 TALDAAGVALLAELIAAHLARGGAVLLTTHQPLELAAARVLDLGDF 205
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
9-233 |
5.08e-46 |
|
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: 160.26 E-value: 5.08e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857580 9 IRLEGVVKTFPNpldaarpIRAVDGISLK--AGgaeasdRLIALVGPDGAGKSTFMRLLCGLEAPDEGRLSVLGTTPDPD 86
Cdd:cd03230 1 IEVRNLSKRYGK-------KTALDDISLTveKG------EIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVLGKDIKKE 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857580 87 NEDFTTRIAFMPQTLGLYKTLSCRENLevfaglrgfegeadgaaglerriaellsmtglagfeerqagKLSGGMKQKLAL 166
Cdd:cd03230 68 PEEVKRRIGYLPEEPSLYENLTVRENL-----------------------------------------KLSGGMKQRLAL 106
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2553857580 167 ASALLRIPDLLLLDEPTVGVDPLSRRELWSVVRRmLADTPMTCVFSTAYLEEAEA-ADRVLLFESGRI 233
Cdd:cd03230 107 AQALLHDPELLILDEPTSGLDPESRREFWELLRE-LKKEGKTILLSSHILEEAERlCDRVAILNNGRI 173
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
367-578 |
5.66e-46 |
|
ABC-type multidrug transport system, ATPase component; The biological function of this family is not well characterized, but display ABC domains similar to members of ABCA subfamily. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213231 [Multi-domain] Cd Length: 211 Bit Score: 161.59 E-value: 5.66e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857580 367 IRADGIARKFGNFVAVADTSFEVRRGeIFGLLGPNGAGKTTTFRMLCGLLVPSKGQIEVAGYDLRTAKAGARARIGYVAQ 446
Cdd:cd03264 1 LQLENLTKRYGKKRALDGVSLTLGPG-MYGLLGPNGAGKTTLMRILATLTPPSSGTIRIDGQDVLKQPQKLRRRIGYLPQ 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857580 447 KFSLYGKLSVEQNLRYFGRSYGFFGQALQDRIDASLEDFGLTDRRDTTAGSLSFGAKQDLSMACGLIHSPEILFLDEATS 526
Cdd:cd03264 80 EFGVYPNFTVREFLDYIAWLKGIPSKEVKARVDEVLELVNLGDRAKKKIGSLSGGMRRRVGIAQALVGDPSILIVDEPTA 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 2553857580 527 GADLASRRAFwRRINALASAGTSVVVTTHFLEEAEY-CDRFLIQDAGKVLALG 578
Cdd:cd03264 160 GLDPEERIRF-RNLLSELGEDRIVILSTHIVEDVESlCNQVAVLNKGKLVFEG 211
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
366-583 |
1.24e-44 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 159.04 E-value: 1.24e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857580 366 VIRADGIARKFGNFVAVADTSFEVRRGEIFGLLGPNGAGKTTTFRMLCGLLVPSKGQIEVAGYDLRTAKAGARAR--IGY 443
Cdd:COG1137 3 TLEAENLVKSYGKRTVVKDVSLEVNQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGRIFLDGEDITHLPMHKRARlgIGY 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857580 444 VAQKFSLYGKLSVEQNLRYFGRSYGFFGQALQDRIDASLEDFGLTDRRDTTAGSLSFGAKQDLSMACGLIHSPEILFLDE 523
Cdd:COG1137 83 LPQEASIFRKLTVEDNILAVLELRKLSKKEREERLEELLEEFGITHLRKSKAYSLSGGERRRVEIARALATNPKFILLDE 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2553857580 524 ATSG------ADLasrrafwRR-INALASAGTSVVVTTHFLEEA-EYCDRFLIQDAGKVLALGTPREV 583
Cdd:COG1137 163 PFAGvdpiavADI-------QKiIRHLKERGIGVLITDHNVRETlGICDRAYIISEGKVLAEGTPEEI 223
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
9-239 |
2.76e-44 |
|
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: 157.53 E-value: 2.76e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857580 9 IRLEGVVKTFPNpldaarpIRAVDGISLKAGGAEasdrLIALVGPDGAGKSTFMRLLCGLEAPDEGRLSVLGTTPDPDNE 88
Cdd:cd03265 1 IEVENLVKKYGD-------FEAVRGVSFRVRRGE----IFGLLGPNGAGKTTTIKMLTTLLKPTSGRATVAGHDVVREPR 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857580 89 DFTTRIAFMPQTLGLYKTLSCRENLEVFAGLRGFEGEAdgaagLERRIAELLSMTGLAGFEERQAGKLSGGMKQKLALAS 168
Cdd:cd03265 70 EVRRRIGIVFQDLSVDDELTGWENLYIHARLYGVPGAE-----RRERIDELLDFVGLLEAADRLVKTYSGGMRRRLEIAR 144
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2553857580 169 ALLRIPDLLLLDEPTVGVDPLSRRELWSVVRRMLADTPMTCVFSTAYLEEAEA-ADRVLLFESGRIIADENP 239
Cdd:cd03265 145 SLVHRPEVLFLDEPTIGLDPQTRAHVWEYIEKLKEEFGMTILLTTHYMEEAEQlCDRVAIIDHGRIIAEGTP 216
|
|
| LPS_export_lptB |
TIGR04406 |
LPS export ABC transporter ATP-binding protein; Members of this fmaily are LptB, the ... |
366-583 |
8.63e-44 |
|
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: 156.67 E-value: 8.63e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857580 366 VIRADGIARKFGNFVAVADTSFEVRRGEIFGLLGPNGAGKTTTFRMLCGLLVPSKGQIEVAGYDLRTAKAGARAR--IGY 443
Cdd:TIGR04406 1 TLVAENLIKSYKKRKVVNDVSLSVKSGEIVGLLGPNGAGKTTSFYMIVGLVRPDAGKILIDGQDITHLPMHERARlgIGY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857580 444 VAQKFSLYGKLSVEQNLR-YFGRSYGFFGQALQDRIDASLEDFGLTDRRDTTAGSLSFGAKQDLSMACGLIHSPEILFLD 522
Cdd:TIGR04406 81 LPQEASIFRKLTVEENIMaVLEIRKDLDRAEREERLEALLEEFQISHLRDNKAMSLSGGERRRVEIARALATNPKFILLD 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2553857580 523 EATSGADLASRRAFWRRINALASAGTSVVVTTHFLEEA-EYCDRFLIQDAGKVLALGTPREV 583
Cdd:TIGR04406 161 EPFAGVDPIAVGDIKKIIKHLKERGIGVLITDHNVRETlDICDRAYIISDGKVLAEGTPAEI 222
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
367-575 |
6.17e-43 |
|
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: 153.14 E-value: 6.17e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857580 367 IRADGIARKFGNFVAVADTSFEVRRGEIFGLLGPNGAGKTTTFRMLCGLLVPSKGQIEVAGYDLrTAKAGARARIGYVAQ 446
Cdd:cd03268 1 LKTNDLTKTYGKKRVLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEITFDGKSY-QKNIEALRRIGALIE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857580 447 KFSLYGKLSVEQNLRYFGRSYGFfgqaLQDRIDASLEDFGLTDRRDTTAGSLSFGAKQDLSMACGLIHSPEILFLDEATS 526
Cdd:cd03268 80 APGFYPNLTARENLRLLARLLGI----RKKRIDEVLDVVGLKDSAKKKVKGFSLGMKQRLGIALALLGNPDLLILDEPTN 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 2553857580 527 GADLASRRAFWRRINALASAGTSVVVTTHFLEEAE-YCDRFLIQDAGKVL 575
Cdd:cd03268 156 GLDPDGIKELRELILSLRDQGITVLISSHLLSEIQkVADRIGIINKGKLI 205
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
364-602 |
9.70e-43 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 154.09 E-value: 9.70e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857580 364 PVVIRADGIARKFGNFVAVADTSFEVRRGEIFGLLGPNGAGKTTTFRMLCGLLVPSKGQIEVAGYDLRtakaGARARIGY 443
Cdd:COG1121 4 MPAIELENLTVSYGGRPVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLFGKPPR----RARRRIGY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857580 444 VAQKFSLYG--KLSVEQ----NLRYFGRSYGFFGQALQDRIDASLEDFGLTDRRDTTAGSLSFGAKQDLSMACGLIHSPE 517
Cdd:COG1121 80 VPQRAEVDWdfPITVRDvvlmGRYGRRGLFRRPSRADREAVDEALERVGLEDLADRPIGELSGGQQQRVLLARALAQDPD 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857580 518 ILFLDEATSGADLASRRAFWRRINALASAGTSVVVTTHFLEEA-EYCDR-FLIqdAGKVLALGTPREVkQRAAVLSAVSG 595
Cdd:COG1121 160 LLLLDEPFAGVDAATEEALYELLRELRREGKTILVVTHDLGAVrEYFDRvLLL--NRGLVAHGPPEEV-LTPENLSRAYG 236
|
....*..
gi 2553857580 596 QSLVVDR 602
Cdd:COG1121 237 GPVALLA 243
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
374-578 |
2.93e-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: 152.49 E-value: 2.93e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857580 374 RKFGNFVAVADTSFEVRRGEIFGLLGPNGAGKTTTFRMLCGLLVPSKGQIEVAGYDLRTAKAGARARIGYV-AQKFSLYG 452
Cdd:cd03267 29 RKYREVEALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRVAGLVPWKRRKKFLRRIGVVfGQKTQLWW 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857580 453 KLSVEQNLRYFGRSYGFFGQALQDRIDASLEDFGLTDRRDTTAGSLSFGAKQDLSMACGLIHSPEILFLDEATSGADLAS 532
Cdd:cd03267 109 DLPVIDSFYLLAAIYDLPPARFKKRLDELSELLDLEELLDTPVRQLSLGQRMRAEIAAALLHEPEILFLDEPTIGLDVVA 188
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 2553857580 533 R---RAFWRRINALasAGTSVVVTTHFLEEAE-YCDRFLIQDAGKVLALG 578
Cdd:cd03267 189 QeniRNFLKEYNRE--RGTTVLLTSHYMKDIEaLARRVLVIDKGRLLYDG 236
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
366-583 |
2.94e-42 |
|
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: 152.89 E-value: 2.94e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857580 366 VIRADGIARKFGNFVAVADTSFEVRRGEIFGLLGPNGAGKTTTFRMLCGLLVPSKGQIEVAGYDLRTAKAGARAR-IGYV 444
Cdd:COG1120 1 MLEAENLSVGYGGRPVLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDGRDLASLSRRELARrIAYV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857580 445 AQKFSLYGKLSVEQNLRYfGR-----SYGFFGQALQDRIDASLEDFGLTDRRDTTAGSLSFGAKQDLSMACGLIHSPEIL 519
Cdd:COG1120 81 PQEPPAPFGLTVRELVAL-GRyphlgLFGRPSAEDREAVEEALERTGLEHLADRPVDELSGGERQRVLIARALAQEPPLL 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2553857580 520 FLDEATSGADLASRRAFWRRINALA-SAGTSVVVTTHFLEEA-EYCDRFLIQDAGKVLALGTPREV 583
Cdd:COG1120 160 LLDEPTSHLDLAHQLEVLELLRRLArERGRTVVMVLHDLNLAaRYADRLVLLKDGRIVAQGPPEEV 225
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
384-573 |
1.24e-41 |
|
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ABC component of a cobalt transport family found in bacteria, archaea, and eukaryota. The transition metal cobalt is an essential component of many enzymes and must be transported into cells in appropriate amounts when needed. This ABC transport system of the CbiMNQO family is involved in cobalt transport in association with the cobalamin (vitamin B12) biosynthetic pathways. Most of cobalt (Cbi) transport systems possess a separate CbiN component, the cobalt-binding periplasmic protein, and they are encoded by the conserved gene cluster cbiMNQO. Both the CbiM and CbiQ proteins are integral cytoplasmic membrane proteins, and the CbiO protein has the linker peptide and the Walker A and B motifs commonly found in the ATPase components of the ABC-type transport systems.
Pssm-ID: 213192 [Multi-domain] Cd Length: 211 Bit Score: 149.92 E-value: 1.24e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857580 384 DTSFEVRRGEIFGLLGPNGAGKTTTFRMLCGLLVPSKGQIEVAGYDLRTAKAGARAR-IGYVAQK----FSlygKLSVEQ 458
Cdd:cd03225 19 DISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDLTKLSLKELRRkVGLVFQNpddqFF---GPTVEE 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857580 459 NLRYFGRSYGFFGQALQDRIDASLEDFGLTDRRDTTAGSLSFGAKQDLSMACGLIHSPEILFLDEATSGADLASRRAFWR 538
Cdd:cd03225 96 EVAFGLENLGLPEEEIEERVEEALELVGLEGLRDRSPFTLSGGQKQRVAIAGVLAMDPDILLLDEPTAGLDPAGRRELLE 175
|
170 180 190
....*....|....*....|....*....|....*.
gi 2553857580 539 RINALASAGTSVVVTTHFLEE-AEYCDRFLIQDAGK 573
Cdd:cd03225 176 LLKKLKAEGKTIIIVTHDLDLlLELADRVIVLEDGK 211
|
|
| drrA |
TIGR01188 |
daunorubicin resistance ABC transporter ATP-binding subunit; This model describes daunorubicin ... |
28-328 |
1.34e-41 |
|
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: 152.54 E-value: 1.34e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857580 28 IRAVDGISLKAGGAEasdrLIALVGPDGAGKSTFMRLLCGLEAPDEGRLSVLG--TTPDPDneDFTTRIAFMPQTLGLYK 105
Cdd:TIGR01188 6 FKAVDGVNFKVREGE----VFGFLGPNGAGKTTTIRMLTTLLRPTSGTARVAGydVVREPR--KVRRSIGIVPQYASVDE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857580 106 TLSCRENLEVFAGLRGFEGEAdgaagLERRIAELLSMTGLAGFEERQAGKLSGGMKQKLALASALLRIPDLLLLDEPTVG 185
Cdd:TIGR01188 80 DLTGRENLEMMGRLYGLPKDE-----AEERAEELLELFELGEAADRPVGTYSGGMRRRLDIAASLIHQPDVLFLDEPTTG 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857580 186 VDPLSRRELWSVVRRMlADTPMTCVFSTAYLEEAEA-ADRVLLFESGRIIADENPQSFISRAKGRTYLLPLanraeHDAQ 264
Cdd:TIGR01188 155 LDPRTRRAIWDYIRAL-KEEGVTILLTTHYMEEADKlCDRIAIIDHGRIIAEGTPEELKRRLGKDTLESRP-----RDIQ 228
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2553857580 265 MLCRRLSEETAATRSDALFLDIVPRMGGA----------AATTLAPTLPVKDARVPSgFIPRQPSLEDAYALLT 328
Cdd:TIGR01188 229 SLKVEVSMLIAELGETGLGLLAVTVDSDRikilvpdgdeTVPEIVEAAIRNGIRIRS-ISTERPSLDDVFLKLT 301
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
5-597 |
3.37e-41 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 156.33 E-value: 3.37e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857580 5 SAPAIRLEGVVKTFPnpldaarPIRAVDGISL--KAGgaeasdRLIALVGPDGAGKSTFMRLLCGLEAPDEGRLSVLGTT 82
Cdd:COG1129 1 AEPLLEMRGISKSFG-------GVKALDGVSLelRPG------EVHALLGENGAGKSTLMKILSGVYQPDSGEILLDGEP 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857580 83 PDPDNedftTR------IAFMPQTLGLYKTLSCRENLevFAG--LRGFeGEADGAAgLERRIAELLSMTGLAGFEERQAG 154
Cdd:COG1129 68 VRFRS----PRdaqaagIAIIHQELNLVPNLSVAENI--FLGrePRRG-GLIDWRA-MRRRARELLARLGLDIDPDTPVG 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857580 155 KLSGGMKQKLALASALLRIPDLLLLDEPTvgvDPLSRRE---LWSVVRRmLADTPMTCVFSTAYLEE-AEAADRVLLFES 230
Cdd:COG1129 140 DLSVAQQQLVEIARALSRDARVLILDEPT---ASLTEREverLFRIIRR-LKAQGVAIIYISHRLDEvFEIADRVTVLRD 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857580 231 GRIIAdenpqsfisrakgrtyllplanraehdaqmlcrrlSEETAATRSDALFLDIVPRmggaaattlaptlpvkdarvp 310
Cdd:COG1129 216 GRLVG-----------------------------------TGPVAELTEDELVRLMVGR--------------------- 239
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857580 311 sgfiprqpSLEDAYalltfPRAPKTANhlasppsdasgalaasaasaddtaerPVVIRADGIARKfgnfVAVADTSFEVR 390
Cdd:COG1129 240 --------ELEDLF-----PKRAAAPG--------------------------EVVLEVEGLSVG----GVVRDVSFSVR 276
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857580 391 RGEIFGLLGPNGAGKTTTFRMLCGLLVPSKGQIEVAG--YDLRTAKAGARARIGYVA---QKFSLYGKLSVEQN-----L 460
Cdd:COG1129 277 AGEILGIAGLVGAGRTELARALFGADPADSGEIRLDGkpVRIRSPRDAIRAGIAYVPedrKGEGLVLDLSIRENitlasL 356
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857580 461 RYFGRSyGFFGQALQDRI-DASLEDFGL-TDRRDTTAGSLSFGAKQDLSMACGLIHSPEILFLDEATSGADLASRRAFWR 538
Cdd:COG1129 357 DRLSRG-GLLDRRRERALaEEYIKRLRIkTPSPEQPVGNLSGGNQQKVVLAKWLATDPKVLILDEPTRGIDVGAKAEIYR 435
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857580 539 RINALASAGTSVVVTTHFLEE-AEYCDRFLIQDAGKVLALGTPREVKQrAAVLSAVSGQS 597
Cdd:COG1129 436 LIRELAAEGKAVIVISSELPElLGLSDRILVMREGRIVGELDREEATE-EAIMAAATGGA 494
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
374-586 |
1.60e-40 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 150.24 E-value: 1.60e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857580 374 RKFGNFVAVADTSFEVRRGEIFGLLGPNGAGKTTTFRMLCGLLVPSKGQIEVAGYD-LRTAKAGARaRIGYV-AQKFSLY 451
Cdd:COG4586 30 REYREVEAVDDISFTIEPGEIVGFIGPNGAGKSTTIKMLTGILVPTSGEVRVLGYVpFKRRKEFAR-RIGVVfGQRSQLW 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857580 452 GKLSVEQNLRYFGRSYGFFGQALQDRIDASLEDFGLTDRRDTTAGSLSFGA--KQDLSMAcgLIHSPEILFLDEATSGAD 529
Cdd:COG4586 109 WDLPAIDSFRLLKAIYRIPDAEYKKRLDELVELLDLGELLDTPVRQLSLGQrmRCELAAA--LLHRPKILFLDEPTIGLD 186
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2553857580 530 LASR---RAFWRRINalASAGTSVVVTTHFLEEAEY-CDRFLIQDAGKVLALGTPREVKQR 586
Cdd:COG4586 187 VVSKeaiREFLKEYN--RERGTTILLTSHDMDDIEAlCDRVIVIDHGRIIYDGSLEELKER 245
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
367-578 |
5.62e-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: 145.35 E-value: 5.62e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857580 367 IRADGIARKFGNFVAVADTSFEVRRGEIFGLLGPNGAGKTTTFRMLCGLLVPSKGQIEVAGYDLrTAKAGARARIGYVAQ 446
Cdd:cd03259 1 LELKGLSKTYGSVRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDGRDV-TGVPPERRNIGMVFQ 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857580 447 KFSLYGKLSVEQNLRYFGRSYGFFGQALQDRIDASLEDFGLTDRRDTTAGSLSFGAKQDLSMACGLIHSPEILFLDEATS 526
Cdd:cd03259 80 DYALFPHLTVAENIAFGLKLRGVPKAEIRARVRELLELVGLEGLLNRYPHELSGGQQQRVALARALAREPSLLLLDEPLS 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 2553857580 527 GADLASR---RAFWRRInaLASAGTSVVVTTHFLEEA-EYCDRFLIQDAGKVLALG 578
Cdd:cd03259 160 ALDAKLReelREELKEL--QRELGITTIYVTHDQEEAlALADRIAVMNEGRIVQVG 213
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
11-574 |
1.18e-39 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 152.53 E-value: 1.18e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857580 11 LEGVVKTFPnpldaARPIraVDGISLKAggaEASDRlIALVGPDGAGKSTFMRLLCGLEAPDEGRLSVlgttpDPDnedf 90
Cdd:COG0488 1 LENLSKSFG-----GRPL--LDDVSLSI---NPGDR-IGLVGRNGAGKSTLLKILAGELEPDSGEVSI-----PKG---- 60
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857580 91 tTRIAFMPQTLGLYKTLSCREnlEVFAGLRGF---------------EGEADGAA--------------GLERRIAELLS 141
Cdd:COG0488 61 -LRIGYLPQEPPLDDDLTVLD--TVLDGDAELraleaeleeleaklaEPDEDLERlaelqeefealggwEAEARAEEILS 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857580 142 MTGLAGFE-ERQAGKLSGGMKQKLALASALLRIPDLLLLDEPTVGVDPLSRRELwsvvRRMLADTPMTCVFSTayleeae 220
Cdd:COG0488 138 GLGFPEEDlDRPVSELSGGWRRRVALARALLSEPDLLLLDEPTNHLDLESIEWL----EEFLKNYPGTVLVVS------- 206
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857580 221 aADRVLLFE-SGRIIAdenpqsfISRAKGRTYLLP----LANRAEHDAQmlcrrlsEETAATRSDALF---LDIVPRMGG 292
Cdd:COG0488 207 -HDRYFLDRvATRILE-------LDRGKLTLYPGNysayLEQRAERLEQ-------EAAAYAKQQKKIakeEEFIRRFRA 271
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857580 293 AAATTLAPTLPVKDA-RVPSGFIPRqpslEDAYALLTFPRAPKTANhlasppsdasgalaasaasaddtaerpVVIRADG 371
Cdd:COG0488 272 KARKAKQAQSRIKALeKLEREEPPR----RDKTVEIRFPPPERLGK---------------------------KVLELEG 320
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857580 372 IARKFGNFVAVADTSFEVRRGEIFGLLGPNGAGKTTTFRMLCGLLVPSKGQIevagydlrtaKAGARARIGYVAQKF-SL 450
Cdd:COG0488 321 LSKSYGDKTLLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPDSGTV----------KLGETVKIGYFDQHQeEL 390
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857580 451 YGKLSVEQNLRYFGRSygffgqalQDRIDAS--LEDFGLT-DRRDTTAGSLSFGAKQDLSMACGLIHSPEILFLDEATSG 527
Cdd:COG0488 391 DPDKTVLDELRDGAPG--------GTEQEVRgyLGRFLFSgDDAFKPVGVLSGGEKARLALAKLLLSPPNVLLLDEPTNH 462
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|.
gi 2553857580 528 ADLASRRAFwrrINALAS-AGTsVVVTTH---FLEEAeyCDRFLIQDAGKV 574
Cdd:COG0488 463 LDIETLEAL---EEALDDfPGT-VLLVSHdryFLDRV--ATRILEFEDGGV 507
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
9-235 |
1.47e-39 |
|
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: 144.57 E-value: 1.47e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857580 9 IRLEGVVKTFPNpldaaRPIRAVDGISLKAGGAEasdrLIALVGPDGAGKSTFMRLLCGLEAPDEGRLSVLGTTPDPDNE 88
Cdd:cd03263 1 LQIRNLTKTYKK-----GTKPAVDDLSLNVYKGE----IFGLLGHNGAGKTTTLKMLTGELRPTSGTAYINGYSIRTDRK 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857580 89 DFTTRIAFMPQTLGLYKTLSCRENLEVFAGLRGFEGEadgaaGLERRIAELLSMTGLAGFEERQAGKLSGGMKQKLALAS 168
Cdd:cd03263 72 AARQSLGYCPQFDALFDELTVREHLRFYARLKGLPKS-----EIKEEVELLLRVLGLTDKANKRARTLSGGMKRKLSLAI 146
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2553857580 169 ALLRIPDLLLLDEPTVGVDPLSRRELWSVVRRMLADTPMtcVFSTAYLEEAEA-ADRVLLFESGRIIA 235
Cdd:cd03263 147 ALIGGPSVLLLDEPTSGLDPASRRAIWDLILEVRKGRSI--ILTTHSMDEAEAlCDRIAIMSDGKLRC 212
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
1-236 |
5.43e-38 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 141.38 E-value: 5.43e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857580 1 MTkASAPAIRLEGVVKTFPNPldaARPIRAVDGISLKAGGAEasdrLIALVGPDGAGKSTFMRLLCGLEAPDEGRLSVLG 80
Cdd:COG1116 1 MS-AAAPALELRGVSKRFPTG---GGGVTALDDVSLTVAAGE----FVALVGPSGCGKSTLLRLIAGLEKPTSGEVLVDG 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857580 81 ---TTPDPDnedfttrIAFMPQTLGLYKTLSCRENLEVfaGLRgFEGEADGAAglERRIAELLSMTGLAGFEERQAGKLS 157
Cdd:COG1116 73 kpvTGPGPD-------RGVVFQEPALLPWLTVLDNVAL--GLE-LRGVPKAER--RERARELLELVGLAGFEDAYPHQLS 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857580 158 GGMKQKLALASALLRIPDLLLLDEPTVGVDPLSRRELWSVVRRMLADTPMTCVFSTAYLEEAEA-ADRVLLFES--GRII 234
Cdd:COG1116 141 GGMRQRVAIARALANDPEVLLMDEPFGALDALTRERLQDELLRLWQETGKTVLFVTHDVDEAVFlADRVVVLSArpGRIV 220
|
..
gi 2553857580 235 AD 236
Cdd:COG1116 221 EE 222
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
9-236 |
6.95e-38 |
|
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a bacterial ABC-type Na+ transport system called NatAB, which catalyzes ATP-dependent electrogenic Na+ extrusion without mechanically coupled proton or K+ uptake. NatB possess six putative membrane spanning regions at its C-terminus. In B. subtilis, NatAB is inducible by agents such as ethanol and protonophores, which lower the proton-motive force across the membrane. The closest sequence similarity to NatA is exhibited by DrrA of the two-component daunorubicin- and doxorubicin-efflux system. Hence, the functional NatAB is presumably assembled with two copies of a single ATP-binding protein and a single integral membrane protein.
Pssm-ID: 213233 [Multi-domain] Cd Length: 218 Bit Score: 139.81 E-value: 6.95e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857580 9 IRLEGVVKTFPnplDAARPIRAVDGISLKAGGAEasdrLIALVGPDGAGKSTFMRLLCGLEAPDEGRLSVLGTTPDPDNE 88
Cdd:cd03266 2 ITADALTKRFR---DVKKTVQAVDGVSFTVKPGE----VTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDGFDVVKEPA 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857580 89 DFTTRIAFMPQTLGLYKTLSCRENLEVFAGLRGFEGEAdgaagLERRIAELLSMTGLAGFEERQAGKLSGGMKQKLALAS 168
Cdd:cd03266 75 EARRRLGFVSDSTGLYDRLTARENLEYFAGLYGLKGDE-----LTARLEELADRLGMEELLDRRVGGFSTGMRQKVAIAR 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2553857580 169 ALLRIPDLLLLDEPTVGVDPLSRRELWSVVRRmLADTPMTCVFSTAYLEEAEA-ADRVLLFESGRIIAD 236
Cdd:cd03266 150 ALVHDPPVLLLDEPTTGLDVMATRALREFIRQ-LRALGKCILFSTHIMQEVERlCDRVVVLHRGRVVYE 217
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
377-585 |
1.57e-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: 138.72 E-value: 1.57e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857580 377 GNFVAVADTSFEVRRGEIFGLLGPNGAGKTTTFRMLCGLLVPSKGQIEVAGYDLRTAKAGARAR--IGYVAQKFSLYGKL 454
Cdd:cd03224 11 GKSQILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDGRDITGLPPHERARagIGYVPEGRRIFPEL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857580 455 SVEQNLRyFGRsYGFFGQALQDRIDASLEDF-GLTDRRDTTAGSLSFGAKQDLSMACGLIHSPEILFLDEATSGadLAS- 532
Cdd:cd03224 91 TVEENLL-LGA-YARRRAKRKARLERVYELFpRLKERRKQLAGTLSGGEQQMLAIARALMSRPKLLLLDEPSEG--LAPk 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 2553857580 533 -RRAFWRRINALASAGTSVVVTTHFLEEA-EYCDRFLIQDAGKVLALGTPREVKQ 585
Cdd:cd03224 167 iVEEIFEAIRELRDEGVTILLVEQNARFAlEIADRAYVLERGRVVLEGTAAELLA 221
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
376-578 |
1.57e-37 |
|
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: 138.44 E-value: 1.57e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857580 376 FGNFVAVADTSFEVRRGEIFGLLGPNGAGKTTTFRMLCGLLVPSKGQIEVAGYDLRtakaGARARIGYVAQKFSL--YGK 453
Cdd:cd03235 9 YGGHPVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFGKPLE----KERKRIGYVPQRRSIdrDFP 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857580 454 LSVEQ----NLRYFGRSYGFFGQALQDRIDASLEDFGLTDRRDTTAGSLSFGAKQDLSMACGLIHSPEILFLDEATSGAD 529
Cdd:cd03235 85 ISVRDvvlmGLYGHKGLFRRLSKADKAKVDEALERVGLSELADRQIGELSGGQQQRVLLARALVQDPDLLLLDEPFAGVD 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 2553857580 530 LASRRAFWRRINALASAGTSVVVTTHFLEEA-EYCDRFLIQDaGKVLALG 578
Cdd:cd03235 165 PKTQEDIYELLRELRREGMTILVVTHDLGLVlEYFDRVLLLN-RTVVASG 213
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
367-574 |
4.94e-37 |
|
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: 137.24 E-value: 4.94e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857580 367 IRADGIARKFGN----FVAVADTSFEVRRGEIFGLLGPNGAGKTTTFRMLCGLLVPSKGQIEVAGYDLRTAKAGARAR-- 440
Cdd:cd03255 1 IELKNLSKTYGGggekVQALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRVDGTDISKLSEKELAAfr 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857580 441 ---IGYVAQKFSLYGKLSVEQNLRYFGRSYGFFGQALQDRIDASLEDFGLTDRRDTTAGSLSFGAKQDLSMACGLIHSPE 517
Cdd:cd03255 81 rrhIGFVFQSFNLLPDLTALENVELPLLLAGVPKKERRERAEELLERVGLGDRLNHYPSELSGGQQQRVAIARALANDPK 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 2553857580 518 ILFLDEATSGADLASRRAFWRRINALA-SAGTSVVVTTHFLEEAEYCDR-FLIQDaGKV 574
Cdd:cd03255 161 IILADEPTGNLDSETGKEVMELLRELNkEAGTTIVVVTHDPELAEYADRiIELRD-GKI 218
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
9-236 |
4.84e-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: 134.52 E-value: 4.84e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857580 9 IRLEGVVKTFPNpldAARPIRAVDGISLKAGGAEasdrLIALVGPDGAGKSTFMRLLCGLEAPDEGRLSVLG---TTPDP 85
Cdd:cd03293 1 LEVRNVSKTYGG---GGGAVTALEDISLSVEEGE----FVALVGPSGCGKSTLLRIIAGLERPTSGEVLVDGepvTGPGP 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857580 86 DnedfttrIAFMPQTLGLYKTLSCRENleVFAGLRgFEGEADGAAglERRIAELLSMTGLAGFEERQAGKLSGGMKQKLA 165
Cdd:cd03293 74 D-------RGYVFQQDALLPWLTVLDN--VALGLE-LQGVPKAEA--RERAEELLELVGLSGFENAYPHQLSGGMRQRVA 141
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2553857580 166 LASALLRIPDLLLLDEPTVGVDPLSRRELWSVVRRMLADTPMTCVFSTAYLEEAEA-ADRVLLFES--GRIIAD 236
Cdd:cd03293 142 LARALAVDPDVLLLDEPFSALDALTREQLQEELLDIWRETGKTVLLVTHDIDEAVFlADRVVVLSArpGRIVAE 215
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
363-583 |
5.02e-36 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 138.69 E-value: 5.02e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857580 363 RPVVIRADGIARKFGNFVAVADTSFEVRRGEIFGLLGPNGAGKTTTFRMLCGLLVPSKGQIEVAGYDLRTAKAGARaRIG 442
Cdd:COG3842 2 AMPALELENVSKRYGDVTALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRILLDGRDVTGLPPEKR-NVG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857580 443 YVAQKFSLYGKLSVEQNLRYFGRSYGFFGQALQDRIDASLEDFGLTDRRDTTAGSLSFGAKQDLSMACGLIHSPEILFLD 522
Cdd:COG3842 81 MVFQDYALFPHLTVAENVAFGLRMRGVPKAEIRARVAELLELVGLEGLADRYPHQLSGGQQQRVALARALAPEPRVLLLD 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2553857580 523 EATSGADLASRRAFW---RRInaLASAGTSVVVTTHFLEEA-EYCDRFLIQDAGKVLALGTPREV 583
Cdd:COG3842 161 EPLSALDAKLREEMReelRRL--QRELGITFIYVTHDQEEAlALADRIAVMNDGRIEQVGTPEEI 223
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
377-592 |
7.65e-36 |
|
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid transport and metabolism];
Pssm-ID: 440179 [Multi-domain] Cd Length: 236 Bit Score: 134.72 E-value: 7.65e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857580 377 GNFVAVADTSFEVRRGEIFGLLGPNGAGKTTTFRMLCGLLVPSKGQIEVAGYDLRTAKAGARAR--IGYVAQKFSLYGKL 454
Cdd:COG0410 14 GGIHVLHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRSGSIRFDGEDITGLPPHRIARlgIGYVPEGRRIFPSL 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857580 455 SVEQNLR---YFGRSygffGQALQDRIDASLEDF-GLTDRRDTTAGSLSFGAKQDLSMACGLIHSPEILFLDEATSGadL 530
Cdd:COG0410 94 TVEENLLlgaYARRD----RAEVRADLERVYELFpRLKERRRQRAGTLSGGEQQMLAIGRALMSRPKLLLLDEPSLG--L 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2553857580 531 ASR--RAFWRRINALASAGTSVVVTTHFLEEA-EYCDRFLIQDAGKVLALGTPREVKQRAAVLSA 592
Cdd:COG0410 168 APLivEEIFEIIRRLNREGVTILLVEQNARFAlEIADRAYVLERGRIVLEGTAAELLADPEVREA 232
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
367-585 |
1.06e-35 |
|
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: 134.17 E-value: 1.06e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857580 367 IRADGIARKFGNFVAVADTSFEVRRGEIFGLLGPNGAGKTTTFRMLCGLLVPSKGQIEVAGYDL----RTAKAGARARIG 442
Cdd:cd03261 1 IELRGLTKSFGGRTVLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGEDIsglsEAELYRLRRRMG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857580 443 YVAQKFSLYGKLSVEQNLRYFGRSYGFFGQALQDRIDAS-LEDFGLTDRRDTTAGSLSFGAKQDLSMACGLIHSPEILFL 521
Cdd:cd03261 81 MLFQSGALFDSLTVFENVAFPLREHTRLSEEEIREIVLEkLEAVGLRGAEDLYPAELSGGMKKRVALARALALDPELLLY 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2553857580 522 DEATSGADLASRRAFWRRINALASA-GTSVVVTTHFLEEA-EYCDRFLIQDAGKVLALGTPREVKQ 585
Cdd:cd03261 161 DEPTAGLDPIASGVIDDLIRSLKKElGLTSIMVTHDLDTAfAIADRIAVLYDGKIVAEGTPEELRA 226
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
366-583 |
1.61e-35 |
|
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: 133.48 E-value: 1.61e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857580 366 VIRADGIARKFGN----FVAVADTSFEVRRGEIFGLLGPNGAGKTTTFRMLCGLLVPSKGQIEVAGYDL-RTAKAG---A 437
Cdd:cd03258 1 MIELKNVSKVFGDtggkVTALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGSVLVDGTDLtLLSGKElrkA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857580 438 RARIGYVAQKFSLYGKLSVEQNLRYFGRSYGFFGQALQDRIDASLEDFGLTDRRDTTAGSLSFGAKQDLSMACGLIHSPE 517
Cdd:cd03258 81 RRRIGMIFQHFNLLSSRTVFENVALPLEIAGVPKAEIEERVLELLELVGLEDKADAYPAQLSGGQKQRVGIARALANNPK 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857580 518 ILFLDEATSGADLASRR---AFWRRINalASAGTSVVVTTHFLEEA-EYCDRFLIQDAGKVLALGTPREV 583
Cdd:cd03258 161 VLLCDEATSALDPETTQsilALLRDIN--RELGLTIVLITHEMEVVkRICDRVAVMEKGEVVEEGTVEEV 228
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
368-573 |
1.77e-35 |
|
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213179 [Multi-domain] Cd Length: 157 Bit Score: 130.83 E-value: 1.77e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857580 368 RADGIARKFGNFVAVADTSFEVRRGEIFGLLGPNGAGKTTTFRMLCGLLVPSKGQIEVAGYDLRTAK-AGARARIGYVAQ 446
Cdd:cd00267 1 EIENLSFRYGGRTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGKDIAKLPlEELRRRIGYVPQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857580 447 kfslygklsveqnlryfgrsygffgqalqdridasledfgltdrrdttagsLSFGAKQDLSMACGLIHSPEILFLDEATS 526
Cdd:cd00267 81 ---------------------------------------------------LSGGQRQRVALARALLLNPDLLLLDEPTS 109
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 2553857580 527 GADLASRRAFWRRINALASAGTSVVVTTHFLEEAE-YCDRFLIQDAGK 573
Cdd:cd00267 110 GLDPASRERLLELLRELAEEGRTVIIVTHDPELAElAADRVIVLKDGK 157
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
9-236 |
2.34e-35 |
|
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: 132.32 E-value: 2.34e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857580 9 IRLEGVVKTFPNPldaarpiRAVDGISLkaggaEASDRLIALVGPDGAGKSTFMRLLCGLEAPDEGRLSVLGTTPDPDNE 88
Cdd:cd03264 1 LQLENLTKRYGKK-------RALDGVSL-----TLGPGMYGLLGPNGAGKTTLMRILATLTPPSSGTIRIDGQDVLKQPQ 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857580 89 DFTTRIAFMPQTLGLYKTLSCRENLEVFAGLRGFEgeadgAAGLERRIAELLSMTGLAGFEERQAGKLSGGMKQKLALAS 168
Cdd:cd03264 69 KLRRRIGYLPQEFGVYPNFTVREFLDYIAWLKGIP-----SKEVKARVDEVLELVNLGDRAKKKIGSLSGGMRRRVGIAQ 143
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2553857580 169 ALLRIPDLLLLDEPTVGVDPLSRRELWSVVRRMLADTpmTCVFSTAYLEEAEA-ADRVLLFESGRIIAD 236
Cdd:cd03264 144 ALVGDPSILIVDEPTAGLDPEERIRFRNLLSELGEDR--IVILSTHIVEDVESlCNQVAVLNKGKLVFE 210
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
8-324 |
4.23e-35 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 134.47 E-value: 4.23e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857580 8 AIRLEGVVKTFPNpldaarpIRAVDGISL--KAGgaeasdRLIALVGPDGAGKSTFMRLLCGLEAPDEGRLSVLGTTPDP 85
Cdd:COG4152 1 MLELKGLTKRFGD-------KTAVDDVSFtvPKG------EIFGLLGPNGAGKTTTIRIILGILAPDSGEVLWDGEPLDP 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857580 86 DNEDfttRIAFMPQTLGLYKTLSCRENLEVFAGLRGFEgeadgAAGLERRIAELLSMTGLAGFEERQAGKLSGGMKQKLA 165
Cdd:COG4152 68 EDRR---RIGYLPEERGLYPKMKVGEQLVYLARLKGLS-----KAEAKRRADEWLERLGLGDRANKKVEELSKGNQQKVQ 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857580 166 LASALLRIPDLLLLDEPTVGVDPLSRRELWSVVRRmLADTPMTCVFSTAYLEEAEA-ADRVLLFESGRIIADENPQSFIS 244
Cdd:COG4152 140 LIAALLHDPELLILDEPFSGLDPVNVELLKDVIRE-LAAKGTTVIFSSHQMELVEElCDRIVIINKGRKVLSGSVDEIRR 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857580 245 RAKGRTYLLplanRAEHDAQMLCRRLSEETAATRSDALFLDIVPrmgGAAATTLAPTLpVKDARVPSgFIPRQPSLEDAY 324
Cdd:COG4152 219 QFGRNTLRL----EADGDAGWLRALPGVTVVEEDGDGAELKLED---GADAQELLRAL-LARGPVRE-FEEVRPSLNEIF 289
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
363-585 |
5.27e-35 |
|
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: 132.41 E-value: 5.27e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857580 363 RPVVIRADGIARKFGNFVAVADTSFEVRRGEIFGLLGPNGAGKTTTFRMLCGLLVPSKGQIEVAGYDLRTAKAGA----R 438
Cdd:COG1127 2 SEPMIEVRNLTKSFGDRVVLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEILVDGQDITGLSEKElyelR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857580 439 ARIGYVAQKFSLYGKLSVEQN----LRYFGRsygfFGQAL-QDRIDASLEDFGLTDRRDTTAGSLSFGAKQDLSMACGLI 513
Cdd:COG1127 82 RRIGMLFQGGALFDSLTVFENvafpLREHTD----LSEAEiRELVLEKLELVGLPGAADKMPSELSGGMRKRVALARALA 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2553857580 514 HSPEILFLDEATSGADLASRRAFWRRINALASA-GTSVVVTTHFLEEA-EYCDRFLIQDAGKVLALGTPREVKQ 585
Cdd:COG1127 158 LDPEILLYDEPTAGLDPITSAVIDELIRELRDElGLTSVVVTHDLDSAfAIADRVAVLADGKIIAEGTPEELLA 231
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
368-574 |
7.48e-35 |
|
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of the ABC component of a cobalt transport family found in bacteria, archaea, and eukaryota. The transition metal cobalt is an essential component of many enzymes and must be transported into cells in appropriate amounts when needed. The CbiMNQO family ABC transport system is involved in cobalt transport in association with the cobalamin (vitamin B12) biosynthetic pathways. Most cobalt (Cbi) transport systems possess a separate CbiN component, the cobalt-binding periplasmic protein, and they are encoded by the conserved gene cluster cbiMNQO. Both the CbiM and CbiQ proteins are integral cytoplasmic membrane proteins, and the CbiO protein has the linker peptide and the Walker A and B motifs commonly found in the ATPase components of the ABC-type transport systems.
Pssm-ID: 213193 [Multi-domain] Cd Length: 205 Bit Score: 130.84 E-value: 7.48e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857580 368 RADGIARKFG-NFVAVADTSFEVRRGEIFGLLGPNGAGKTTTFRMLCGLLVPSKGQIEVAGydlRTAKAGARAR-IGYVA 445
Cdd:cd03226 1 RIENISFSYKkGTEILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLNG---KPIKAKERRKsIGYVM 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857580 446 Q--KFSLYGKlSVEQNLRYFGRSYGffgqALQDRIDASLEDFGLTDRRDTTAGSLSFGAKQDLSMACGLIHSPEILFLDE 523
Cdd:cd03226 78 QdvDYQLFTD-SVREELLLGLKELD----AGNEQAETVLKDLDLYALKERHPLSLSGGQKQRLAIAAALLSGKDLLIFDE 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 2553857580 524 ATSGADLASRRAFWRRINALASAGTSVVVTTHFLE-EAEYCDRFLIQDAGKV 574
Cdd:cd03226 153 PTSGLDYKNMERVGELIRELAAQGKAVIVITHDYEfLAKVCDRVLLLANGAI 204
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
9-235 |
1.18e-34 |
|
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is comprised of proteins involved in the transport of apparently unrelated solutes and proteins specific for di- and oligosaccharides and polyols. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213226 [Multi-domain] Cd Length: 213 Bit Score: 130.72 E-value: 1.18e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857580 9 IRLEGVVKTFpnpldaaRPIRAVDGISLKAGGAEasdrLIALVGPDGAGKSTFMRLLCGLEAPDEGRLSVlgttpdpDNE 88
Cdd:cd03259 1 LELKGLSKTY-------GSVRALDDLSLTVEPGE----FLALLGPSGCGKTTLLRLIAGLERPDSGEILI-------DGR 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857580 89 DFTT------RIAFMPQTLGLYKTLSCRENLeVFAGLRGFEGEADgaagLERRIAELLSMTGLAGFEERQAGKLSGGMKQ 162
Cdd:cd03259 63 DVTGvpperrNIGMVFQDYALFPHLTVAENI-AFGLKLRGVPKAE----IRARVRELLELVGLEGLLNRYPHELSGGQQQ 137
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2553857580 163 KLALASALLRIPDLLLLDEPTVGVDPLSRRELWSVVRRMLADTPMTCVFSTAYLEEAEA-ADRVLLFESGRIIA 235
Cdd:cd03259 138 RVALARALAREPSLLLLDEPLSALDAKLREELREELKELQRELGITTIYVTHDQEEALAlADRIAVMNEGRIVQ 211
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
386-526 |
1.52e-34 |
|
ABC transporter; ABC transporters for a large family of proteins responsible for translocation of a variety of compounds across biological membranes. ABC transporters are the largest family of proteins in many completely sequenced bacteria. ABC transporters are composed of two copies of this domain and two copies of a transmembrane domain pfam00664. These four domains may belong to a single polypeptide or belong in different polypeptide chains.
Pssm-ID: 394964 [Multi-domain] Cd Length: 150 Bit Score: 128.15 E-value: 1.52e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857580 386 SFEVRRGEIFGLLGPNGAGKTTTFRMLCGLLVPSKGQIEVAGYDL-RTAKAGARARIGYVAQKFSLYGKLSVEQNLRYFG 464
Cdd:pfam00005 5 SLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDLtDDERKSLRKEIGYVFQDPQLFPRLTVRENLRLGL 84
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2553857580 465 RSYGFFGQALQDRIDASLEDFGLTDRRDTTAG----SLSFGAKQDLSMACGLIHSPEILFLDEATS 526
Cdd:pfam00005 85 LLKGLSKREKDARAEEALEKLGLGDLADRPVGerpgTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
9-247 |
3.58e-34 |
|
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: 129.76 E-value: 3.58e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857580 9 IRLEGVVKTFPNPldaarpIRAVDGISL--KAGgaeasdRLIALVGPDGAGKSTFMRLLCGLEAPDEGRLSVLGTTP--- 83
Cdd:COG1122 1 IELENLSFSYPGG------TPALDDVSLsiEKG------EFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVDGKDItkk 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857580 84 --------------DPDN--------EDfttrIAFMPqtlglyktlscrENLevfaglrGFEGEAdgaagLERRIAELLS 141
Cdd:COG1122 69 nlrelrrkvglvfqNPDDqlfaptveED----VAFGP------------ENL-------GLPREE-----IRERVEEALE 120
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857580 142 MTGLAGFEERQAGKLSGGMKQKLALASAllripdllllDEPTVGVDPLSRRELWSVVRRmLADTPMTCVFSTAYLEEA-E 220
Cdd:COG1122 121 LVGLEHLADRPPHELSGGQKQRVAIAGVlamepevlvlDEPTAGLDPRGRRELLELLKR-LNKEGKTVIIVTHDLDLVaE 199
|
250 260
....*....|....*....|....*..
gi 2553857580 221 AADRVLLFESGRIIADENPQSFISRAK 247
Cdd:COG1122 200 LADRVIVLDDGRIVADGTPREVFSDYE 226
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
367-573 |
5.72e-34 |
|
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is comprised of all BPD (Binding Protein Dependent) systems that are largely represented in archaea and eubacteria and are primarily involved in scavenging solutes from the environment. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213196 [Multi-domain] Cd Length: 178 Bit Score: 127.30 E-value: 5.72e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857580 367 IRADGIARKFGNFVAVADTSFEVRRGEIFGLLGPNGAGKTTTFRMLCGLLVPSKGQIEVAGYDLRTAKAG---ARARIGY 443
Cdd:cd03229 1 LELKNVSKRYGQKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGEDLTDLEDElppLRRRIGM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857580 444 VAQKFSLYGKLSVEQNLRYfgrsygffgqalqdridasledfgltdrrdttagSLSFGAKQDLSMACGLIHSPEILFLDE 523
Cdd:cd03229 81 VFQDFALFPHLTVLENIAL----------------------------------GLSGGQQQRVALARALAMDPDVLLLDE 126
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 2553857580 524 ATSGADLASRRAFWRRINAL-ASAGTSVVVTTHFLEEAEY-CDRFLIQDAGK 573
Cdd:cd03229 127 PTSALDPITRREVRALLKSLqAQLGITVVLVTHDLDEAARlADRVVVLRDGK 178
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
35-227 |
6.31e-34 |
|
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: 128.37 E-value: 6.31e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857580 35 SLKAGGAeasdrlIALVGPDGAGKSTFMRLLCGLEAPDEGRLSVLGTTPDPDNEDFTTRIAFMPQTLGLYKTLSCRENLE 114
Cdd:COG4133 24 TLAAGEA------LALTGPNGSGKTTLLRILAGLLPPSAGEVLWNGEPIRDAREDYRRRLAYLGHADGLKPELTVRENLR 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857580 115 VFAGLRGFEGEADgaaglerRIAELLSMTGLAGFEERQAGKLSGGMKQKLALASALLRIPDLLLLDEPTVGVDPLSRREL 194
Cdd:COG4133 98 FWAALYGLRADRE-------AIDEALEAVGLAGLADLPVRQLSAGQKRRVALARLLLSPAPLWLLDEPFTALDAAGVALL 170
|
170 180 190
....*....|....*....|....*....|...
gi 2553857580 195 WSVVRRMLADTPMtCVFSTAYLEEAEAADRVLL 227
Cdd:COG4133 171 AELIAAHLARGGA-VLLTTHQPLELAAARVLDL 202
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
367-583 |
1.91e-33 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 131.04 E-value: 1.91e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857580 367 IRADGIARKFGNFVAVADTSFEVRRGEIFGLLGPNGAGKTTTFRMLCGLLVPSKGQIEVAGYDLRTAKAgARAR-IGYVA 445
Cdd:COG1118 3 IEVRNISKRFGSFTLLDDVSLEIASGELVALLGPSGSGKTTLLRIIAGLETPDSGRIVLNGRDLFTNLP-PRERrVGFVF 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857580 446 QKFSLYGKLSVEQNLRYFGRSYGFFGQALQDRIDASLEDFGLTDRRDTTAGSLSFGAKQDLSMACGLIHSPEILFLDEAT 525
Cdd:COG1118 82 QHYALFPHMTVAENIAFGLRVRPPSKAEIRARVEELLELVQLEGLADRYPSQLSGGQRQRVALARALAVEPEVLLLDEPF 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2553857580 526 SGADLASR-------RAFWRRINalasaGTSVVVtTHFLEEA-EYCDRFLIQDAGKVLALGTPREV 583
Cdd:COG1118 162 GALDAKVRkelrrwlRRLHDELG-----GTTVFV-THDQEEAlELADRVVVMNQGRIEQVGTPDEV 221
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
9-233 |
2.52e-33 |
|
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: 126.84 E-value: 2.52e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857580 9 IRLEGVVKTFPNpldAARPIRAVDGISLKAGGAEasdrLIALVGPDGAGKSTFMRLLCGLEAPDEGRLSVLGTTPDPDNE 88
Cdd:cd03255 1 IELKNLSKTYGG---GGEKVQALKGVSLSIEKGE----FVAIVGPSGSGKSTLLNILGGLDRPTSGEVRVDGTDISKLSE 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857580 89 DFTTR-----IAFMPQTLGLYKTLSCRENLEV---FAGLRGFEgeadgaagLERRIAELLSMTGLAGFEERQAGKLSGGM 160
Cdd:cd03255 74 KELAAfrrrhIGFVFQSFNLLPDLTALENVELpllLAGVPKKE--------RRERAEELLERVGLGDRLNHYPSELSGGQ 145
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2553857580 161 KQKLALASALLRIPDLLLLDEPTVGVDPLSRRELWSVVRRMLADTPMTCVFSTAYLEEAEAADRVLLFESGRI 233
Cdd:cd03255 146 QQRVAIARALANDPKIILADEPTGNLDSETGKEVMELLRELNKEAGTTIVVVTHDPELAEYADRIIELRDGKI 218
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
9-235 |
5.13e-33 |
|
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: 125.86 E-value: 5.13e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857580 9 IRLEGVVKTFpnpldaaRPIRAVDGISLKAGGAEAsdrlIALVGPDGAGKSTFMRLLCGLEAPDEGRLSVLGTTPDPDNE 88
Cdd:cd03269 1 LEVENVTKRF-------GRVTALDDISFSVEKGEI----FGLLGPNGAGKTTTIRMILGIILPDSGEVLFDGKPLDIAAR 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857580 89 DfttRIAFMPQTLGLYKTLSCRENLEVFAGLRGFEGEAdgAAgleRRIAELLSMTGLAGFEERQAGKLSGGMKQKLALAS 168
Cdd:cd03269 70 N---RIGYLPEERGLYPKMKVIDQLVYLAQLKGLKKEE--AR---RRIDEWLERLELSEYANKRVEELSKGNQQKVQFIA 141
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2553857580 169 ALLRIPDLLLLDEPTVGVDPLSRRELWSVVRRmLADTPMTCVFSTAYLEEAEA-ADRVLLFESGRIIA 235
Cdd:cd03269 142 AVIHDPELLILDEPFSGLDPVNVELLKDVIRE-LARAGKTVILSTHQMELVEElCDRVLLLNKGRAVL 208
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
368-578 |
5.49e-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: 124.86 E-value: 5.49e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857580 368 RADGIARKFGNFVAVADTSFEVRRGEIFGLLGPNGAGKTTTFRMLCGLLVPSKGQIEVAGYDLRTAKAGARAR-IGYVAQ 446
Cdd:cd03214 1 EVENLSVGYGGRTVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDGKDLASLSPKELARkIAYVPQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857580 447 kfslygklsveqnlryfgrsygffgqalqdridaSLEDFGLTDRRDTTAGSLSFGAKQDLSMACGLIHSPEILFLDEATS 526
Cdd:cd03214 81 ----------------------------------ALELLGLAHLADRPFNELSGGERQRVLLARALAQEPPILLLDEPTS 126
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 2553857580 527 GADLASRRAFWRRINALA-SAGTSVVVTTHFLEEA-EYCDRFLIQDAGKVLALG 578
Cdd:cd03214 127 HLDIAHQIELLELLRRLArERGKTVVMVLHDLNLAaRYADRVILLKDGRIVAQG 180
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
9-236 |
1.22e-32 |
|
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily represents ABC transporters involved in peptide antibiotic resistance. Bacitracin is a dodecapeptide antibiotic produced by B. licheniformis and B. subtilis. The synthesis of bacitracin is non-ribosomally catalyzed by a multi-enzyme complex BcrABC. Bacitracin has potent antibiotic activity against gram-positive bacteria. The inhibition of peptidoglycan biosynthesis is the best characterized bacterial effect of bacitracin. The bacitracin resistance of B. licheniformis is mediated by the ABC transporter Bcr which is composed of two identical BcrA ATP-binding subunits and one each of the integral membrane proteins, BcrB and BcrC. B. subtilis cells carrying bcr genes on high-copy number plasmids develop collateral detergent sensitivity, a similar phenomenon in human cells with overexpressed multi-drug resistance P-glycoprotein.
Pssm-ID: 213235 [Multi-domain] Cd Length: 208 Bit Score: 124.64 E-value: 1.22e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857580 9 IRLEGVVKTFPNpldaarpIRAVDGISLKAGGAEasdrLIALVGPDGAGKSTFMRLLCGLEAPDEGRLSVLGTTPDpDNE 88
Cdd:cd03268 1 LKTNDLTKTYGK-------KRVLDDISLHVKKGE----IYGFLGPNGAGKTTTMKIILGLIKPDSGEITFDGKSYQ-KNI 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857580 89 DFTTRIAFMPQTLGLYKTLSCRENLEVFAGLRGFEgeadgaaglERRIAELLSMTGLAGFEERQAGKLSGGMKQKLALAS 168
Cdd:cd03268 69 EALRRIGALIEAPGFYPNLTARENLRLLARLLGIR---------KKRIDEVLDVVGLKDSAKKKVKGFSLGMKQRLGIAL 139
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2553857580 169 ALLRIPDLLLLDEPTVGVDPLSRRELWSVVRRmLADTPMTCVFSTAYLEEAE-AADRVLLFESGRIIAD 236
Cdd:cd03268 140 ALLGNPDLLILDEPTNGLDPDGIKELRELILS-LRDQGITVLISSHLLSEIQkVADRIGIINKGKLIEE 207
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
366-555 |
1.23e-32 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 125.16 E-value: 1.23e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857580 366 VIRADGIARKFGN-FVAVADTSFEVRRGEIFGLLGPNGAGKTTTFRMLCGLLVPSKGQIEVAGYDLRTAKAGA----RAR 440
Cdd:COG2884 1 MIRFENVSKRYPGgREALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLVNGQDLSRLKRREipylRRR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857580 441 IGYVAQKFSLYGKLSVEQN----LRYFGRSygffGQALQDRIDASLEDFGLTDRRDTTAGSLSFGAKQDLSMACGLIHSP 516
Cdd:COG2884 81 IGVVFQDFRLLPDRTVYENvalpLRVTGKS----RKEIRRRVREVLDLVGLSDKAKALPHELSGGEQQRVAIARALVNRP 156
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 2553857580 517 EILFLDEATSGADLASRRAFWR---RINALasaGTSVVVTTH 555
Cdd:COG2884 157 ELLLADEPTGNLDPETSWEIMElleEINRR---GTTVLIATH 195
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
9-242 |
2.31e-32 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 127.96 E-value: 2.31e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857580 9 IRLEGVVKTFPNpldaarpIRAVDGISLKAggaeASDRLIALVGPDGAGKSTFMRLLCGLEAPDEGRLSVlgttpdpDNE 88
Cdd:COG1118 3 IEVRNISKRFGS-------FTLLDDVSLEI----ASGELVALLGPSGSGKTTLLRIIAGLETPDSGRIVL-------NGR 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857580 89 DFTT-------RIAFMPQTLGLYKTLSCRENleVFAGLRgfeGEADGAAGLERRIAELLSMTGLAGFEERQAGKLSGGMK 161
Cdd:COG1118 65 DLFTnlpprerRVGFVFQHYALFPHMTVAEN--IAFGLR---VRPPSKAEIRARVEELLELVQLEGLADRYPSQLSGGQR 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857580 162 QKLALASALLRIPDLLLLDEPTVGVDPLSRRELWSVVRRMLADTPMTCVFSTAYLEEA-EAADRVLLFESGRIIAD---- 236
Cdd:COG1118 140 QRVALARALAVEPEVLLLDEPFGALDAKVRKELRRWLRRLHDELGGTTVFVTHDQEEAlELADRVVVMNQGRIEQVgtpd 219
|
....*....
gi 2553857580 237 ---ENPQSF 242
Cdd:COG1118 220 evyDRPATP 228
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
367-583 |
3.58e-32 |
|
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; Phosphonates are a class of organophosphorus compounds characterized by a chemically stable carbon-to-phosphorus (C-P) bond. Phosphonates are widespread among naturally occurring compounds in all kingdoms of wildlife, but only prokaryotic microorganisms are able to cleave this bond. Certain bacteria such as E. coli can use alkylphosphonates as a phosphorus source. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213223 [Multi-domain] Cd Length: 241 Bit Score: 124.60 E-value: 3.58e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857580 367 IRADGIARKFGN-FVAVADTSFEVRRGEIFGLLGPNGAGKTTTFRMLCGLLVPSKGQIEVAGYDLRTAKAGA----RARI 441
Cdd:cd03256 1 IEVENLSKTYPNgKKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGTDINKLKGKAlrqlRRQI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857580 442 GYVAQKFSLYGKLSVEQNL-------RYFGRS-YGFFGQALQDRIDASLEDFGLTDRRDTTAGSLSFGAKQDLSMACGLI 513
Cdd:cd03256 81 GMIFQQFNLIERLSVLENVlsgrlgrRSTWRSlFGLFPKEEKQRALAALERVGLLDKAYQRADQLSGGQQQRVAIARALM 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2553857580 514 HSPEILFLDEATSGADLASRRA---FWRRINalASAGTSVVVTTHFLEEA-EYCDRFLIQDAGKVLALGTPREV 583
Cdd:cd03256 161 QQPKLILADEPVASLDPASSRQvmdLLKRIN--REEGITVIVSLHQVDLArEYADRIVGLKDGRIVFDGPPAEL 232
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
364-602 |
7.06e-32 |
|
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA [Inorganic ion transport and metabolism];
Pssm-ID: 440736 [Multi-domain] Cd Length: 250 Bit Score: 124.04 E-value: 7.06e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857580 364 PVVIRADGIARKFGNFVAVADTSFEVRRGEIFGLLGPNGAGKTTTFRMLCGLLVPSKGQ-IEVAGYDLrtakaGA----- 437
Cdd:COG1119 1 DPLLELRNVTVRRGGKTILDDISWTVKPGEHWAILGPNGAGKSTLLSLITGDLPPTYGNdVRLFGERR-----GGedvwe 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857580 438 -RARIGYVAQkfSLYGKLSVEQNLR------YFGrSYGFFGQ---ALQDRIDASLEDFGLTDRRDTTAGSLSFGAKQDLS 507
Cdd:COG1119 76 lRKRIGLVSP--ALQLRFPRDETVLdvvlsgFFD-SIGLYREptdEQRERARELLELLGLAHLADRPFGTLSQGEQRRVL 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857580 508 MACGLIHSPEILFLDEATSGADLASRRAFWRRINALASAG-TSVVVTTHFLEEA-EYCDRFLIQDAGKVLALGTPREVkQ 585
Cdd:COG1119 153 IARALVKDPELLILDEPTAGLDLGARELLLALLDKLAAEGaPTLVLVTHHVEEIpPGITHVLLLKDGRVVAAGPKEEV-L 231
|
250
....*....|....*..
gi 2553857580 586 RAAVLSAVSGQSLVVDR 602
Cdd:COG1119 232 TSENLSEAFGLPVEVER 248
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
8-234 |
1.06e-31 |
|
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: 123.22 E-value: 1.06e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857580 8 AIRLEGVVKTFPNpldaarpIRAVDGISLKAGGAEasdrLIALVGPDGAGKSTFMRLLCGLEAPDEGRLSVLGTtpDPDN 87
Cdd:cd03296 2 SIEVRNVSKRFGD-------FVALDDVSLDIPSGE----LVALLGPSGSGKTTLLRLIAGLERPDSGTILFGGE--DATD 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857580 88 EDFTTR-IAFMPQTLGLYKTLSCRENleVFAGLRGFEG-EADGAAGLERRIAELLSMTGLAGFEERQAGKLSGGMKQKLA 165
Cdd:cd03296 69 VPVQERnVGFVFQHYALFRHMTVFDN--VAFGLRVKPRsERPPEAEIRAKVHELLKLVQLDWLADRYPAQLSGGQRQRVA 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857580 166 LASALLRIPDLLLLDEPTVGVDPLSRRELWSVVRRMLADTPMTCVFSTAYLEEA-EAADRVLLFESGRII 234
Cdd:cd03296 147 LARALAVEPKVLLLDEPFGALDAKVRKELRRWLRRLHDELHVTTVFVTHDQEEAlEVADRVVVMNKGRIE 216
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
367-583 |
3.94e-31 |
|
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: 121.19 E-value: 3.94e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857580 367 IRADGIARKFGNFVAVADTSFEVRRGEIFGLLGPNGAGKTTTFRMLCGLLVPSKGQIEVAGYDLRTAKAGARaRIGYVAQ 446
Cdd:cd03300 1 IELENVSKFYGGFVALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGKDITNLPPHKR-PVNTVFQ 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857580 447 KFSLYGKLSVEQNLRYFGRSYGFFGQALQDRIDASLEDFGLTDRRDTTAGSLSFGAKQDLSMACGLIHSPEILFLDEATS 526
Cdd:cd03300 80 NYALFPHLTVFENIAFGLRLKKLPKAEIKERVAEALDLVQLEGYANRKPSQLSGGQQQRVAIARALVNEPKVLLLDEPLG 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 2553857580 527 GADLASRRAFWRRINAL-ASAGTSVVVTTHFLEEA-EYCDRFLIQDAGKVLALGTPREV 583
Cdd:cd03300 160 ALDLKLRKDMQLELKRLqKELGITFVFVTHDQEEAlTMSDRIAVMNKGKIQQIGTPEEI 218
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
6-237 |
4.44e-31 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 120.92 E-value: 4.44e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857580 6 APAIRLEGVVKTFPnplDAARPIRAVDGISLKAGGAEasdrLIALVGPDGAGKSTFMRLLCGLEAPDEGRLSVLGTTPDP 85
Cdd:COG1136 2 SPLLELRNLTKSYG---TGEGEVTALRGVSLSIEAGE----FVAIVGPSGSGKSTLLNILGGLDRPTSGEVLIDGQDISS 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857580 86 DNEDFTTR-----IAFMPQTLGLYKTLSCRENLEVFAGLRGFEGEADgaaglERRIAELLSMTGLAGFEERQAGKLSGGM 160
Cdd:COG1136 75 LSERELARlrrrhIGFVFQFFNLLPELTALENVALPLLLAGVSRKER-----RERARELLERVGLGDRLDHRPSQLSGGQ 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2553857580 161 KQKLALASALLRIPDLLLLDEPTVGVDPLSRRELWSVVRRMLADTPMTCVFSTAYLEEAEAADRVLLFESGRIIADE 237
Cdd:COG1136 150 QQRVAIARALVNRPKLILADEPTGNLDSKTGEEVLELLRELNRELGTTIVMVTHDPELAARADRVIRLRDGRIVSDE 226
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
362-583 |
4.95e-31 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 127.07 E-value: 4.95e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857580 362 ERPVVIRADGIARKFGNFVAVADTSFEVRRGEIFGLLGPNGAGKTTTFRMLCGLLVPSKGQIEVAG--YDLRTAKAGARA 439
Cdd:COG3845 1 MMPPALELRGITKRFGGVVANDDVSLTVRPGEIHALLGENGAGKSTLMKILYGLYQPDSGEILIDGkpVRIRSPRDAIAL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857580 440 RIGYVAQKFSLYGKLSVEQN--LRYFGRSYGFFG-QALQDRIDASLEDFGLTDRRDTTAGSLSFGAKQDLSMACGLIHSP 516
Cdd:COG3845 81 GIGMVHQHFMLVPNLTVAENivLGLEPTKGGRLDrKAARARIRELSERYGLDVDPDAKVEDLSVGEQQRVEILKALYRGA 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2553857580 517 EILFLDEATSGADLASRRAFWRRINALASAGTSVVVTTHFLEEA-EYCDRFLIQDAGKVLALGTPREV 583
Cdd:COG3845 161 RILILDEPTAVLTPQEADELFEILRRLAAEGKSIIFITHKLREVmAIADRVTVLRRGKVVGTVDTAET 228
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
5-243 |
5.15e-31 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 124.17 E-value: 5.15e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857580 5 SAPAIRLEGVVKTFPNpldaaRPIraVDGISLKAGGAEAsdrlIALVGPDGAGKSTFMRLLCGLEAPDEGRLSVLGTtPD 84
Cdd:PRK13536 38 STVAIDLAGVSKSYGD-----KAV--VNGLSFTVASGEC----FGLLGPNGAGKSTIARMILGMTSPDAGKITVLGV-PV 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857580 85 PDNEDFT-TRIAFMPQTLGLYKTLSCRENLEVFAGLRGFEgeadgAAGLERRIAELLSMTGLAGFEERQAGKLSGGMKQK 163
Cdd:PRK13536 106 PARARLArARIGVVPQFDNLDLEFTVRENLLVFGRYFGMS-----TREIEAVIPSLLEFARLESKADARVSDLSGGMKRR 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857580 164 LALASALLRIPDLLLLDEPTVGVDPLSRRELWSVVRRMLADTpMTCVFSTAYLEEAEA-ADRVLLFESGRIIADENPQSF 242
Cdd:PRK13536 181 LTLARALINDPQLLILDEPTTGLDPHARHLIWERLRSLLARG-KTILLTTHFMEEAERlCDRLCVLEAGRKIAEGRPHAL 259
|
.
gi 2553857580 243 I 243
Cdd:PRK13536 260 I 260
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
366-583 |
7.40e-31 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 120.77 E-value: 7.40e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857580 366 VIRADGIARKFGNFVAVADTSFEVRRGEIFGLLGPNGAGKTTTFRMLCGLLVPSKGQIEVAGYDLRTAKAGARAR--IGY 443
Cdd:PRK10895 3 TLTAKNLAKAYKGRRVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEDISLLPLHARARrgIGY 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857580 444 VAQKFSLYGKLSVEQNLR-YFGRSYGFFGQALQDRIDASLEDFGLTDRRDTTAGSLSFGAKQDLSMACGLIHSPEILFLD 522
Cdd:PRK10895 83 LPQEASIFRRLSVYDNLMaVLQIRDDLSAEQREDRANELMEEFHIEHLRDSMGQSLSGGERRRVEIARALAANPKFILLD 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2553857580 523 EATSGADLASRRAFWRRINALASAGTSVVVTTHFLEEA-EYCDRFLIQDAGKVLALGTPREV 583
Cdd:PRK10895 163 EPFAGVDPISVIDIKRIIEHLRDSGLGVLITDHNVRETlAVCERAYIVSQGHLIAHGTPTEI 224
|
|
| COG4674 |
COG4674 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
370-589 |
7.44e-31 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443710 [Multi-domain] Cd Length: 250 Bit Score: 120.99 E-value: 7.44e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857580 370 DGIARKFGNFVAVADTSFEVRRGEIFGLLGPNGAGKTTTFRMLCGLLVPSKGQIEVAGYDLRTAKAGARARIGyVAQKF- 448
Cdd:COG4674 14 EDLTVSFDGFKALNDLSLYVDPGELRVIIGPNGAGKTTLMDVITGKTRPDSGSVLFGGTDLTGLDEHEIARLG-IGRKFq 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857580 449 --SLYGKLSVEQNLRY-FGRSYGFF-------GQALQDRIDASLEDFGLTDRRDTTAGSLSFGAKQDLSMACGLIHSPEI 518
Cdd:COG4674 93 kpTVFEELTVFENLELaLKGDRGVFaslfarlTAEERDRIEEVLETIGLTDKADRLAGLLSHGQKQWLEIGMLLAQDPKL 172
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2553857580 519 LFLDEATSGADLASRRAFWRRINALASaGTSVVVTTH---FLEeaEYCDRFLIQDAGKVLALGTPREVKQRAAV 589
Cdd:COG4674 173 LLLDEPVAGMTDAETERTAELLKSLAG-KHSVVVVEHdmeFVR--QIARKVTVLHQGSVLAEGSLDEVQADPRV 243
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
389-586 |
1.20e-30 |
|
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim protein) in eukaryotes. It is the member of ABC transporter superfamily. Rim protein is a membrane glycoprotein which is localized in the photoreceptor outer segment discs. Mutation/s in its genetic loci is implicated in the recessive Stargardt's disease. [Transport and binding proteins, Other]
Pssm-ID: 130324 [Multi-domain] Cd Length: 2272 Bit Score: 128.98 E-value: 1.20e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857580 389 VRRGEIFGLLGPNGAGKTTTFRMLCGLLVPSKGQIEVAGYDLRTAKAGARARIGYVAQKFSLYGKLSVEQNLRYFGRSYG 468
Cdd:TIGR01257 1962 VRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAGKSILTNISDVHQNMGYCPQFDAIDDLLTGREHLYLYARLRG 2041
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857580 469 FFGQALQDRIDASLEDFGLTDRRDTTAGSLSFGAKQDLSMACGLIHSPEILFLDEATSGADLASRRAFWRRINALASAGT 548
Cdd:TIGR01257 2042 VPAEEIEKVANWSIQSLGLSLYADRLAGTYSGGNKRKLSTAIALIGCPPLVLLDEPTTGMDPQARRMLWNTIVSIIREGR 2121
|
170 180 190
....*....|....*....|....*....|....*....
gi 2553857580 549 SVVVTTHFLEEAE-YCDRFLIQDAGKVLALGTPREVKQR 586
Cdd:TIGR01257 2122 AVVLTSHSMEECEaLCTRLAIMVKGAFQCLGTIQHLKSK 2160
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
4-266 |
1.70e-30 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 121.45 E-value: 1.70e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857580 4 ASAPAIRLEGVVKTFPNPLdaarpirAVDGISLKAGGAEAsdrlIALVGPDGAGKSTFMRLLCGLEAPDEGRLSVLGTtP 83
Cdd:PRK13537 3 MSVAPIDFRNVEKRYGDKL-------VVDGLSFHVQRGEC----FGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCGE-P 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857580 84 DPDNEDFT-TRIAFMPQTLGLYKTLSCRENLEVFAGLRGFEgeadgAAGLERRIAELLSMTGLAGFEERQAGKLSGGMKQ 162
Cdd:PRK13537 71 VPSRARHArQRVGVVPQFDNLDPDFTVRENLLVFGRYFGLS-----AAAARALVPPLLEFAKLENKADAKVGELSGGMKR 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857580 163 KLALASALLRIPDLLLLDEPTVGVDPLSRRELWSVVRRMLAdTPMTCVFSTAYLEEAEA-ADRVLLFESGRIIADENPQS 241
Cdd:PRK13537 146 RLTLARALVNDPDVLVLDEPTTGLDPQARHLMWERLRSLLA-RGKTILLTTHFMEEAERlCDRLCVIEEGRKIAEGAPHA 224
|
250 260 270
....*....|....*....|....*....|....*....
gi 2553857580 242 FISRAKG--------------RTYLLPLANRAEHDAQML 266
Cdd:PRK13537 225 LIESEIGcdvieiygpdpvalRDELAPLAERTEISGETL 263
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
386-586 |
2.48e-30 |
|
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: 126.87 E-value: 2.48e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857580 386 SFEVRRGEIFGLLGPNGAGKTTTFRMLCGLLVPSKGQIEVAGYDLRTAKAGA-RARIGYVAQKFSL-YGklSVEQNLRyF 463
Cdd:COG2274 495 SLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEPTSGRILIDGIDLRQIDPASlRRQIGVVLQDVFLfSG--TIRENIT-L 571
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857580 464 GRSygffgQALQDRIDASLEDFGLTD--RR-----DT----TAGSLSFGAKQDLSMACGLIHSPEILFLDEATSGADLAS 532
Cdd:COG2274 572 GDP-----DATDEEIIEAARLAGLHDfiEAlpmgyDTvvgeGGSNLSGGQRQRLAIARALLRNPRILILDEATSALDAET 646
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 2553857580 533 RRAFWRRINALAsAGTSVVVTTHFLEEAEYCDRFLIQDAGKVLALGTPREVKQR 586
Cdd:COG2274 647 EAIILENLRRLL-KGRTVIIIAHRLSTIRLADRIIVLDKGRIVEDGTHEELLAR 699
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
367-568 |
2.91e-30 |
|
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ATP-binding subunits of the bacterial ABC-type nitrate and sulfonate transport systems, respectively. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213260 [Multi-domain] Cd Length: 220 Bit Score: 118.34 E-value: 2.91e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857580 367 IRADGIARKFGN----FVAVADTSFEVRRGEIFGLLGPNGAGKTTTFRMLCGLLVPSKGQIEVAGYDLRtakaGARARIG 442
Cdd:cd03293 1 LEVRNVSKTYGGgggaVTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVDGEPVT----GPGPDRG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857580 443 YVAQKFSLYGKLSVEQNLRYFGRSYGFFGQALQDRIDASLEDFGLTDRRDTTAGSLSFGAKQDLSMACGLIHSPEILFLD 522
Cdd:cd03293 77 YVFQQDALLPWLTVLDNVALGLELQGVPKAEARERAEELLELVGLSGFENAYPHQLSGGMRQRVALARALAVDPDVLLLD 156
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 2553857580 523 EATSGADLASRRAFWRRI-NALASAGTSVVVTTHFLEEAEY-CDRFLI 568
Cdd:cd03293 157 EPFSALDALTREQLQEELlDIWRETGKTVLLVTHDIDEAVFlADRVVV 204
|
|
| COG4559 |
COG4559 |
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism]; |
367-600 |
4.01e-30 |
|
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443620 [Multi-domain] Cd Length: 258 Bit Score: 119.06 E-value: 4.01e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857580 367 IRADGIARKFGNFVAVADTSFEVRRGEIFGLLGPNGAGKTTTFRMLCGLLVPSKGQIEVAGYDLRTAKAGARARI-GYVA 445
Cdd:COG4559 2 LEAENLSVRLGGRTLLDDVSLTLRPGELTAIIGPNGAGKSTLLKLLTGELTPSSGEVRLNGRPLAAWSPWELARRrAVLP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857580 446 QKFSLYGKLSVEQNLRyFGRS-YGFFGQALQDRIDASLEDFGLTDRRDTTAGSLSFGAKQDLSMA-------CGLIHSPE 517
Cdd:COG4559 82 QHSSLAFPFTVEEVVA-LGRApHGSSAAQDRQIVREALALVGLAHLAGRSYQTLSGGEQQRVQLArvlaqlwEPVDGGPR 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857580 518 ILFLDEATSGADLASRRAFWRRINALASAGTSVVVTTHFLE-EAEYCDRFLIQDAGKVLALGTPREVKQrAAVLSAVSGQ 596
Cdd:COG4559 161 WLFLDEPTSALDLAHQHAVLRLARQLARRGGGVVAVLHDLNlAAQYADRILLLHQGRLVAQGTPEEVLT-DELLERVYGA 239
|
....
gi 2553857580 597 SLVV 600
Cdd:COG4559 240 DLRV 243
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
10-232 |
4.96e-30 |
|
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: 117.57 E-value: 4.96e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857580 10 RLEGVVKTFPnplDAARPirAVDGISLKAGGAEasdrLIALVGPDGAGKSTFMRLLCGLEAPDEGRLSVLGTTP------ 83
Cdd:cd03225 1 ELKNLSFSYP---DGARP--ALDDISLTIKKGE----FVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDLtklslk 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857580 84 -----------DPDNEDFTTR----IAFMPQTLGLYKTlscrenlEVfaglrgfegeadgaaglERRIAELLSMTGLAGF 148
Cdd:cd03225 72 elrrkvglvfqNPDDQFFGPTveeeVAFGLENLGLPEE-------EI-----------------EERVEEALELVGLEGL 127
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857580 149 EERQAGKLSGGMKQKLALASALLRIPDLLLLDEPTVGVDPLSRRELWSVVRRmLADTPMTCVFSTAYLEEAEA-ADRVLL 227
Cdd:cd03225 128 RDRSPFTLSGGQKQRVAIAGVLAMDPDILLLDEPTAGLDPAGRRELLELLKK-LKAEGKTIIIVTHDLDLLLElADRVIV 206
|
....*
gi 2553857580 228 FESGR 232
Cdd:cd03225 207 LEDGK 211
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
374-586 |
8.94e-30 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 117.88 E-value: 8.94e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857580 374 RKFGNFVAVADTSFEVRRGEIFGLLGPNGAGKTTTFRMLCGLLVPSKGQIEVAGydlRTAkagarARIGYVAqkfSLYGK 453
Cdd:COG1134 34 TRREEFWALKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTSGRVEVNG---RVS-----ALLELGA---GFHPE 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857580 454 LSVEQNLRYFGRSYGFFGQALQDRIDAsLEDF-GLTDRRDTTAGSLSFGAKQDLSMACGLIHSPEILFLDEATSGADLA- 531
Cdd:COG1134 103 LTGRENIYLNGRLLGLSRKEIDEKFDE-IVEFaELGDFIDQPVKTYSSGMRARLAFAVATAVDPDILLVDEVLAVGDAAf 181
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 2553857580 532 SRRAFwRRINALASAGTSVVVTTHFLEE-AEYCDRFLIQDAGKVLALGTPREVKQR 586
Cdd:COG1134 182 QKKCL-ARIRELRESGRTVIFVSHSMGAvRRLCDRAIWLEKGRLVMDGDPEEVIAA 236
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
9-583 |
9.94e-30 |
|
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: 123.37 E-value: 9.94e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857580 9 IRLEGVVKTFPNpldaarpIRAVDGISLKAGGAEasdrLIALVGPDGAGKSTFMRLLCGLEA--PDEGRL---------- 76
Cdd:TIGR03269 1 IEVKNLTKKFDG-------KEVLKNISFTIEEGE----VLGILGRSGAGKSVLMHVLRGMDQyePTSGRIiyhvalcekc 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857580 77 -------------SVLGTTPDPDNEDF-----------TTRIAFMPQ-TLGLYKTLSCRENleVFAGLRGFEGEADGAAG 131
Cdd:TIGR03269 70 gyverpskvgepcPVCGGTLEPEEVDFwnlsdklrrriRKRIAIMLQrTFALYGDDTVLDN--VLEALEEIGYEGKEAVG 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857580 132 lerRIAELLSMTGLAGFEERQAGKLSGGMKQKLALASALLRIPDLLLLDEPTVGVDPLSRRELWSVVRRMLADTPMTCVF 211
Cdd:TIGR03269 148 ---RAVDLIEMVQLSHRITHIARDLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALEEAVKASGISMVL 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857580 212 STAYLEE-AEAADRVLLFESGRIIADENPQSFISRakgrtyllplanraehdaqmlcrrlseetaatrsdalFLDIVPRm 290
Cdd:TIGR03269 225 TSHWPEViEDLSDKAIWLENGEIKEEGTPDEVVAV-------------------------------------FMEGVSE- 266
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857580 291 ggaaattlaptlPVKDARVPSGfiprQPSLedayalltfpRAPKTANHLASppsdasgalaasaasaddtAERPVVIRAD 370
Cdd:TIGR03269 267 ------------VEKECEVEVG----EPII----------KVRNVSKRYIS-------------------VDRGVVKAVD 301
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857580 371 GIarkfgnfvavadtSFEVRRGEIFGLLGPNGAGKTTTFRMLCGLLVPSKGQIEV-----------AGYDLRtakAGARA 439
Cdd:TIGR03269 302 NV-------------SLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGEVNVrvgdewvdmtkPGPDGR---GRAKR 365
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857580 440 RIGYVAQKFSLYGKLSVEQNLRyfgrsyGFFGQALQD---RIDA--SLEDFGLTDRR-----DTTAGSLSFGAKQDLSMA 509
Cdd:TIGR03269 366 YIGILHQEYDLYPHRTVLDNLT------EAIGLELPDelaRMKAviTLKMVGFDEEKaeeilDKYPDELSEGERHRVALA 439
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2553857580 510 CGLIHSPEILFLDEATSGADLASRRAFWRRI-NALASAGTSVVVTTHFLEEA-EYCDRFLIQDAGKVLALGTPREV 583
Cdd:TIGR03269 440 QVLIKEPRIVILDEPTGTMDPITKVDVTHSIlKAREEMEQTFIIVSHDMDFVlDVCDRAALMRDGKIVKIGDPEEI 515
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
377-593 |
1.36e-29 |
|
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440740 [Multi-domain] Cd Length: 514 Bit Score: 123.09 E-value: 1.36e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857580 377 GNFVAVADTSFEVRRGEIFGLLGPNGAGKTTTFRMLCGLLVPS---KGQIEVAGYDLRTAKAGARAR-IGYVAQKF--SL 450
Cdd:COG1123 17 GDVPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGLLPHGgriSGEVLLDGRDLLELSEALRGRrIGMVFQDPmtQL 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857580 451 YGkLSVEQNLRYFGRSYGFFGQALQDRIDASLEDFGLTDRRDTTAGSLSFGAKQDLSMACGLIHSPEILFLDEATSGADL 530
Cdd:COG1123 97 NP-VTVGDQIAEALENLGLSRAEARARVLELLEAVGLERRLDRYPHQLSGGQRQRVAIAMALALDPDLLIADEPTTALDV 175
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2553857580 531 ASRRAFWRRINALASA-GTSVVVTTHFLEE-AEYCDRFLIQDAGKVLALGTPREVKQRAAVLSAV 593
Cdd:COG1123 176 TTQAEILDLLRELQRErGTTVLLITHDLGVvAEIADRVVVMDDGRIVEDGPPEEILAAPQALAAV 240
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
367-576 |
1.99e-29 |
|
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: 114.06 E-value: 1.99e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857580 367 IRADGIARKFGNFVAVADTSFEVRRGEIFGLLGPNGAGKTTTFRMLCGLLVPSKGQIEVAG--YDLRTAKAGARARIGYV 444
Cdd:cd03216 1 LELRGITKRFGGVKALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVDGkeVSFASPRDARRAGIAMV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857580 445 AQkfslygklsveqnlryfgrsygffgqalqdridasledfgltdrrdttagsLSFGAKQDLSMACGLIHSPEILFLDEA 524
Cdd:cd03216 81 YQ---------------------------------------------------LSVGERQMVEIARALARNARLLILDEP 109
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 2553857580 525 TSGADLASRRAFWRRINALASAGTSVVVTTHFLEEA-EYCDRFLIQDAGKVLA 576
Cdd:cd03216 110 TAALTPAEVERLFKVIRRLRAQGVAVIFISHRLDEVfEIADRVTVLRDGRVVG 162
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
372-583 |
2.08e-29 |
|
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: 117.36 E-value: 2.08e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857580 372 IARKFGNFVAVADTSFEVRRGEIFGLLGPNGAGKTTTFRMLCGLLVPSKGQIEVAGYDLRTAKAGA-----RARIGYVAQ 446
Cdd:cd03294 30 ILKKTGQTVGVNDVSLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGKVLIDGQDIAAMSRKElrelrRKKISMVFQ 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857580 447 KFSLYGKLSVEQNLryfgrSYGF--FGQALQDRIDAS---LEDFGLTDRRDTTAGSLSFGAKQDLSMACGLIHSPEILFL 521
Cdd:cd03294 110 SFALLPHRTVLENV-----AFGLevQGVPRAEREERAaeaLELVGLEGWEHKYPDELSGGMQQRVGLARALAVDPDILLM 184
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2553857580 522 DEATSGADLASRRAFWRRINAL-ASAGTSVVVTTHFLEEA-EYCDRFLIQDAGKVLALGTPREV 583
Cdd:cd03294 185 DEAFSALDPLIRREMQDELLRLqAELQKTIVFITHDLDEAlRLGDRIAIMKDGRLVQVGTPEEI 248
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
377-578 |
4.84e-29 |
|
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: 4.84e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857580 377 GNFVAVADTSFEVRRGEIFGLLGPNGAGKTTTFRMLCGLLVPSKGQIEVAGydlrtakaGARARIGYVAqkfSLYGKLSV 456
Cdd:cd03220 33 GEFWALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVTVRG--------RVSSLLGLGG---GFNPELTG 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857580 457 EQNLRYFGRSYGFFGQALQDRIDaSLEDF-GLTDRRDTTAGSLSFGAKQDLSMACGLIHSPEILFLDEATSGADLASRRA 535
Cdd:cd03220 102 RENIYLNGRLLGLSRKEIDEKID-EIIEFsELGDFIDLPVKTYSSGMKARLAFAIATALEPDILLIDEVLAVGDAAFQEK 180
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 2553857580 536 FWRRINALASAGTSVVVTTHFLEE-AEYCDRFLIQDAGKVLALG 578
Cdd:cd03220 181 CQRRLRELLKQGKTVILVSHDPSSiKRLCDRALVLEKGKIRFDG 224
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
5-240 |
4.98e-29 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 118.66 E-value: 4.98e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857580 5 SAPAIRLEGVVKTFPNPldaarpiRAVDGISLKAGGAEasdrLIALVGPDGAGKSTFMRLLCGLEAPDEGRLSVlgttpd 84
Cdd:COG3842 2 AMPALELENVSKRYGDV-------TALDDVSLSIEPGE----FVALLGPSGCGKTTLLRMIAGFETPDSGRILL------ 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857580 85 pDNEDFTT------RIAFMPQTLGLYKTLSCRENLEvFaGLRgFEGEAdgAAGLERRIAELLSMTGLAGFEERQAGKLSG 158
Cdd:COG3842 65 -DGRDVTGlppekrNVGMVFQDYALFPHLTVAENVA-F-GLR-MRGVP--KAEIRARVAELLELVGLEGLADRYPHQLSG 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857580 159 GMKQKLALASAllripdllllDEPTVGVDPLSRRELWSVVRRMLADTPMTCVFSTAYLEEAEA-ADRVLLFESGRIIADE 237
Cdd:COG3842 139 GQQQRVALARAlapeprvlllDEPLSALDAKLREEMREELRRLQRELGITFIYVTHDQEEALAlADRIAVMNDGRIEQVG 218
|
...
gi 2553857580 238 NPQ 240
Cdd:COG3842 219 TPE 221
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
367-583 |
5.41e-29 |
|
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex cysAWTP involved in sulfate import. Responsible for energy coupling to the transport system. The complex is composed of two ATP-binding proteins (cysA), two transmembrane proteins (cysT and cysW), and a solute-binding protein (cysP). ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213263 [Multi-domain] Cd Length: 239 Bit Score: 115.51 E-value: 5.41e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857580 367 IRADGIARKFGNFVAVADTSFEVRRGEIFGLLGPNGAGKTTTFRMLCGLLVPSKGQIEVAGYDlrTAKAGARAR-IGYVA 445
Cdd:cd03296 3 IEVRNVSKRFGDFVALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGGED--ATDVPVQERnVGFVF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857580 446 QKFSLYGKLSVEQN----LRYFGRSYGFFGQALQDRIDASLEDFGLTDRRDTTAGSLSFGAKQDLSMACGLIHSPEILFL 521
Cdd:cd03296 81 QHYALFRHMTVFDNvafgLRVKPRSERPPEAEIRAKVHELLKLVQLDWLADRYPAQLSGGQRQRVALARALAVEPKVLLL 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2553857580 522 DEATSGADLASR---RAFWRRINALASAgTSVVVtTHFLEEA-EYCDRFLIQDAGKVLALGTPREV 583
Cdd:cd03296 161 DEPFGALDAKVRkelRRWLRRLHDELHV-TTVFV-THDQEEAlEVADRVVVMNKGRIEQVGTPDEV 224
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
47-235 |
5.56e-29 |
|
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: 114.55 E-value: 5.56e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857580 47 LIALVGPDGAGKSTFMRLLCGLEAPDEGRLSVLGTTPDPDNEdfttRIAFMPQTLGLYKT--LSCRE----NLEVFAGLR 120
Cdd:cd03235 27 FLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFGKPLEKERK----RIGYVPQRRSIDRDfpISVRDvvlmGLYGHKGLF 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857580 121 GFEGEADgaaglERRIAELLSMTGLAGFEERQAGKLSGGMKQKLALASALLRIPDLLLLDEPTVGVDPLSRRELWSVVRR 200
Cdd:cd03235 103 RRLSKAD-----KAKVDEALERVGLSELADRQIGELSGGQQQRVLLARALVQDPDLLLLDEPFAGVDPKTQEDIYELLRE 177
|
170 180 190
....*....|....*....|....*....|....*.
gi 2553857580 201 mLADTPMTCVFSTAYLEEAEA-ADRVLLFEsGRIIA 235
Cdd:cd03235 178 -LRREGMTILVVTHDLGLVLEyFDRVLLLN-RTVVA 211
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
42-236 |
8.55e-29 |
|
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type transporter and the ATPase component of a molybdate transport system that also includes the periplasmic binding protein ModA and the membrane protein ModB. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213264 [Multi-domain] Cd Length: 214 Bit Score: 113.93 E-value: 8.55e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857580 42 EASDRLIALVGPDGAGKSTFMRLLCGLEAPDEGRLSVLGTTPDPDNEDFTT-----RIAFMPQTLGLYKTLSCRENLEVf 116
Cdd:cd03297 20 DLNEEVTGIFGASGAGKSTLLRCIAGLEKPDGGTIVLNGTVLFDSRKKINLppqqrKIGLVFQQYALFPHLNVRENLAF- 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857580 117 aGLRGFEGEADgaaglERRIAELLSMTGLAGFEERQAGKLSGGMKQKLALASALLRIPDLLLLDEPTVGVDPLSRRELWS 196
Cdd:cd03297 99 -GLKRKRNRED-----RISVDELLDLLGLDHLLNRYPAQLSGGEKQRVALARALAAQPELLLLDEPFSALDRALRLQLLP 172
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 2553857580 197 VVRRMLADTPMTCVFSTAYLEEAEA-ADRVLLFESGRIIAD 236
Cdd:cd03297 173 ELKQIKKNLNIPVIFVTHDLSEAEYlADRIVVMEDGRLQYI 213
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
9-240 |
1.09e-28 |
|
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: 114.52 E-value: 1.09e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857580 9 IRLEGVVKTFpnpldAARPIraVDGISLKAGGAEAsdrlIALVGPDGAGKSTFMRLLCGLEAPDEGRLSVLGTTPDPDNE 88
Cdd:cd03261 1 IELRGLTKSF-----GGRTV--LKGVDLDVRRGEI----LAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGEDISGLSE 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857580 89 D----FTTRIAFMPQTLGLYKTLSCRENLEVFagLRgfEGEADGAAGLERRIAELLSMTGLAGFEERQAGKLSGGMKQKL 164
Cdd:cd03261 70 AelyrLRRRMGMLFQSGALFDSLTVFENVAFP--LR--EHTRLSEEEIREIVLEKLEAVGLRGAEDLYPAELSGGMKKRV 145
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2553857580 165 ALASALLRIPDLLLLDEPTVGVDPLSRRELWSVVRRMLADTPMTCVFSTAYLEEA-EAADRVLLFESGRIIADENPQ 240
Cdd:cd03261 146 ALARALALDPELLLYDEPTAGLDPIASGVIDDLIRSLKKELGLTSIMVTHDLDTAfAIADRIAVLYDGKIVAEGTPE 222
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
377-555 |
1.42e-28 |
|
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where FtsE is the ATPase and the membrane subunit FtsX resembles a permease subunit. But rather than transporting any substrate, the complex acts in cell division by undergoing conformational changes that alter the activity of cell wall hydrolases located outside the plasma membrane. The complex is widely conserved in bacteria, but also extremely divergent in sequence between different lineages
Pssm-ID: 213259 [Multi-domain] Cd Length: 214 Bit Score: 113.66 E-value: 1.42e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857580 377 GNFVAVADTSFEVRRGEIFGLLGPNGAGKTTTFRMLCGLLVPSKGQIEVAGYDL----RTAKAGARARIGYVAQKFSLYG 452
Cdd:cd03292 12 NGTAALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQDVsdlrGRAIPYLRRKIGVVFQDFRLLP 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857580 453 KLSVEQNLRYFGRSYGFFGQALQDRIDASLEDFGLTDRRDTTAGSLSFGAKQDLSMACGLIHSPEILFLDEATSGADLAS 532
Cdd:cd03292 92 DRNVYENVAFALEVTGVPPREIRKRVPAALELVGLSHKHRALPAELSGGEQQRVAIARAIVNSPTILIADEPTGNLDPDT 171
|
170 180
....*....|....*....|...
gi 2553857580 533 RRAFWRRINALASAGTSVVVTTH 555
Cdd:cd03292 172 TWEIMNLLKKINKAGTTVVVATH 194
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
367-586 |
2.25e-28 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 116.71 E-value: 2.25e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857580 367 IRADGIARKFGNFVAVADTSFEVRRGEIFGLLGPNGAGKTTTFRMLCGLLVPSKGQIEVAGYDLRTAKAGARaRIGYVAQ 446
Cdd:COG3839 4 LELENVSKSYGGVEALKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAGLEDPTSGEILIGGRDVTDLPPKDR-NIAMVFQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857580 447 KFSLYGKLSVEQNLRyFG-RSYGFFGQALQDRIDASLEDFGLTDRRDTTAGSLSFGAKQDLSMACGLIHSPEILFLDEAT 525
Cdd:COG3839 83 SYALYPHMTVYENIA-FPlKLRKVPKAEIDRRVREAAELLGLEDLLDRKPKQLSGGQRQRVALGRALVREPKVFLLDEPL 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2553857580 526 SGADLASR---RAFWRRInaLASAGTSVVVTTHFLEEAEY-CDRFLIQDAGKVLALGTPREVKQR 586
Cdd:COG3839 162 SNLDAKLRvemRAEIKRL--HRRLGTTTIYVTHDQVEAMTlADRIAVMNDGRIQQVGTPEELYDR 224
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
365-600 |
2.32e-28 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 114.10 E-value: 2.32e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857580 365 VVIRADGIARKFGNFVAVADTSFEVRRGEIFGLLGPNGAGKTTTFRMLCGLLVPSKGQIEVAGYDLRTAKAGARARIGYV 444
Cdd:PRK13548 1 AMLEARNLSVRLGGRTLLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLNGRPLADWSPAELARRRAV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857580 445 -AQKFSLYGKLSVEQNLRyFGRS-YGFFGQALQDRIDASLEDFGLTDRRDTTAGSLSFGAKQDLSMA---CGL---IHSP 516
Cdd:PRK13548 81 lPQHSSLSFPFTVEEVVA-MGRApHGLSRAEDDALVAAALAQVDLAHLAGRDYPQLSGGEQQRVQLArvlAQLwepDGPP 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857580 517 EILFLDEATSGADLASRRAFWRRINALA-SAGTSVVVTTHFLE-EAEYCDRFLIQDAGKVLALGTPREVkQRAAVLSAVS 594
Cdd:PRK13548 160 RWLLLDEPTSALDLAHQHHVLRLARQLAhERGLAVIVVLHDLNlAARYADRIVLLHQGRLVADGTPAEV-LTPETLRRVY 238
|
....*.
gi 2553857580 595 GQSLVV 600
Cdd:PRK13548 239 GADVLV 244
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
367-583 |
4.41e-28 |
|
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: 112.27 E-value: 4.41e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857580 367 IRADGIARKFGNFVAVADTSFEVRRGEIFGLLGPNGAGKTTTFRMLCGLL-----VPSKGQIEVAG---YDLRTAKAGAR 438
Cdd:cd03260 1 IELRDLNVYYGDKHALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRLNdlipgAPDEGEVLLDGkdiYDLDVDVLELR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857580 439 ARIGYVAQKFSLYgKLSVEQNLRYFGRSYGFFG-QALQDRIDASLEDFGLTDR--RDTTAGSLSFGAKQDLSMACGLIHS 515
Cdd:cd03260 81 RRVGMVFQKPNPF-PGSIYDNVAYGLRLHGIKLkEELDERVEEALRKAALWDEvkDRLHALGLSGGQQQRLCLARALANE 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2553857580 516 PEILFLDEATSGADLASRRAFWRRINALASAgTSVVVTTHFLEEAEYC-DRFLIQDAGKVLALGTPREV 583
Cdd:cd03260 160 PEVLLLDEPTSALDPISTAKIEELIAELKKE-YTIVIVTHNMQQAARVaDRTAFLLNGRLVEFGPTEQI 227
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
386-573 |
4.48e-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: 110.55 E-value: 4.48e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857580 386 SFEVRRGEIFGLLGPNGAGKTTTFRMLCGLLVPSKGQIEVAGYDLRTAKAGA-RARIGYVAQKFSLYgKLSVEQNLryfg 464
Cdd:cd03228 22 SLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGVDLRDLDLESlRKNIAYVPQDPFLF-SGTIRENI---- 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857580 465 rsygffgqalqdridasledfgltdrrdttagsLSFGAKQDLSMACGLIHSPEILFLDEATSGADLASRRAFWRRINALa 544
Cdd:cd03228 97 ---------------------------------LSGGQRQRIAIARALLRDPPILILDEATSALDPETEALILEALRAL- 142
|
170 180
....*....|....*....|....*....
gi 2553857580 545 SAGTSVVVTTHFLEEAEYCDRFLIQDAGK 573
Cdd:cd03228 143 AKGKTVIVIAHRLSTIRDADRIIVLDDGR 171
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
11-236 |
5.67e-28 |
|
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: 112.43 E-value: 5.67e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857580 11 LEGVVKTFPNPLdaARPIRAVDGISLKAGGAEasdrLIALVGPDGAGKSTFMRLLCGLEAPDEGRLSVLGTTPDPDNEDF 90
Cdd:cd03267 19 LIGSLKSLFKRK--YREVEALKGISFTIEKGE----IVGFIGPNGAGKTTTLKILSGLLQPTSGEVRVAGLVPWKRRKKF 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857580 91 TTRIAF-MPQTLGLYKTLSCRENLEVFAGLRGFEgeadgAAGLERRIAELLSMTGLAGFEERQAGKLSGGMKQKLALASA 169
Cdd:cd03267 93 LRRIGVvFGQKTQLWWDLPVIDSFYLLAAIYDLP-----PARFKKRLDELSELLDLEELLDTPVRQLSLGQRMRAEIAAA 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2553857580 170 LLRIPDLLLLDEPTVGVDPLSRRELWSVVRRMLADTPMTCVFSTAYLEEAEA-ADRVLLFESGRIIAD 236
Cdd:cd03267 168 LLHEPEILFLDEPTIGLDVVAQENIRNFLKEYNRERGTTVLLTSHYMKDIEAlARRVLVIDKGRLLYD 235
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
370-583 |
7.45e-28 |
|
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely related to ModC. ModC is an ABC-type transporter and the ATPase component of a molybdate transport system that also includes the periplasmic binding protein ModA and the membrane protein ModB. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213266 [Multi-domain] Cd Length: 235 Bit Score: 112.04 E-value: 7.45e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857580 370 DGIARKFGNFVaVADTSFEVRRGEIFGLLGPNGAGKTTTFRMLCGLLVPSKGQIEVAGYDLRTAKAGARaRIGYVAQKFS 449
Cdd:cd03299 4 ENLSKDWKEFK-LKNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNGKDITNLPPEKR-DISYVPQNYA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857580 450 LYGKLSVEQNLRYFGRSYGFFGQALQDRIDASLEDFGLTDRRDTTAGSLSFGAKQDLSMACGLIHSPEILFLDEATSGAD 529
Cdd:cd03299 82 LFPHMTVYKNIAYGLKKRKVDKKEIERKVLEIAEMLGIDHLLNRKPETLSGGEQQRVAIARALVVNPKILLLDEPFSALD 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2553857580 530 ------LASRRAFWRRinalaSAGTSVVVTTHFLEEAEY-CDRFLIQDAGKVLALGTPREV 583
Cdd:cd03299 162 vrtkekLREELKKIRK-----EFGVTVLHVTHDFEEAWAlADKVAIMLNGKLIQVGKPEEV 217
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
393-580 |
1.52e-27 |
|
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim protein) in eukaryotes. It is the member of ABC transporter superfamily. Rim protein is a membrane glycoprotein which is localized in the photoreceptor outer segment discs. Mutation/s in its genetic loci is implicated in the recessive Stargardt's disease. [Transport and binding proteins, Other]
Pssm-ID: 130324 [Multi-domain] Cd Length: 2272 Bit Score: 118.96 E-value: 1.52e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857580 393 EIFGLLGPNGAGKTTTFRMLCGLLVPSKGQIEVAGYDLRTAKAGARARIGYVAQKFSLYGKLSVEQNLRYFGRSYGFFGQ 472
Cdd:TIGR01257 957 QITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGKDIETNLDAVRQSLGMCPQHNILFHHLTVAEHILFYAQLKGRSWE 1036
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857580 473 ALQDRIDASLEDFGLTDRRDTTAGSLSFGAKQDLSMACGLIHSPEILFLDEATSGADLASRRAFWRRINALASaGTSVVV 552
Cdd:TIGR01257 1037 EAQLEMEAMLEDTGLHHKRNEEAQDLSGGMQRKLSVAIAFVGDAKVVVLDEPTSGVDPYSRRSIWDLLLKYRS-GRTIIM 1115
|
170 180
....*....|....*....|....*....
gi 2553857580 553 TTHFLEEAEYC-DRFLIQDAGKVLALGTP 580
Cdd:TIGR01257 1116 STHHMDEADLLgDRIAIISQGRLYCSGTP 1144
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
367-583 |
2.54e-27 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 113.25 E-value: 2.54e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857580 367 IRADGIARKF----GNFVAVADTSFEVRRGEIFGLLGPNGAGKTTTFRMLCGLLVPSKGQIEVAGYDLRTAKAG----AR 438
Cdd:COG1135 2 IELENLSKTFptkgGPVTALDDVSLTIEKGEIFGIIGYSGAGKSTLIRCINLLERPTSGSVLVDGVDLTALSERelraAR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857580 439 ARIGYVAQKFSLYGKLSVEQN----LRYFGRSygffGQALQDRIDASLEDFGLTDRRDTTAGSLSFGAKQDLSMACGLIH 514
Cdd:COG1135 82 RKIGMIFQHFNLLSSRTVAENvalpLEIAGVP----KAEIRKRVAELLELVGLSDKADAYPSQLSGGQKQRVGIARALAN 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2553857580 515 SPEILFLDEATSGADLASRR---AFWRRINA-LasaGTSVVVTTHfleEAE----YCDRFLIQDAGKVLALGTPREV 583
Cdd:COG1135 158 NPKVLLCDEATSALDPETTRsilDLLKDINReL---GLTIVLITH---EMDvvrrICDRVAVLENGRIVEQGPVLDV 228
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
381-598 |
2.68e-27 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 111.62 E-value: 2.68e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857580 381 AVADTSFEVRRGEIFGLLGPNGAGKTTTFRMLCGLLVPSKGQIEVAGYDL--RTAKAGARARIGYVAQ--KFSLYGKlSV 456
Cdd:PRK13644 17 ALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLVSGIDTgdFSKLQGIRKLVGIVFQnpETQFVGR-TV 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857580 457 EQNLRYFGRSYGFFGQALQDRIDASLEDFGLTDRRDTTAGSLSFGAKQDLSMACGLIHSPEILFLDEATSGADLASRRAF 536
Cdd:PRK13644 96 EEDLAFGPENLCLPPIEIRKRVDRALAEIGLEKYRHRSPKTLSGGQGQCVALAGILTMEPECLIFDEVTSMLDPDSGIAV 175
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2553857580 537 WRRINALASAGTSVVVTTHFLEEAEYCDRFLIQDAGKVLALGTPREvkqraaVLSAVSGQSL 598
Cdd:PRK13644 176 LERIKKLHEKGKTIVYITHNLEELHDADRIIVMDRGKIVLEGEPEN------VLSDVSLQTL 231
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
367-622 |
2.86e-27 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 116.04 E-value: 2.86e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857580 367 IRADGIARKFGNFVAVADTSFEVRRGEIFGLLGPNGAGKTTTFRMLCGLLVPSKGQIEVAG--YDLRTAKAGARARIGYV 444
Cdd:PRK09700 6 ISMAGIGKSFGPVHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNinYNKLDHKLAAQLGIGII 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857580 445 AQKFSLYGKLSVEQNLrYFGR--SYGFFGQALQD----RIDAS--LEDFGLTDRRDTTAGSLSFGAKQDLSMACGLIHSP 516
Cdd:PRK09700 86 YQELSVIDELTVLENL-YIGRhlTKKVCGVNIIDwremRVRAAmmLLRVGLKVDLDEKVANLSISHKQMLEIAKTLMLDA 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857580 517 EILFLDEATSGADLASRRAFWRRINALASAGTSVVVTTHFLEE-AEYCDRFLIQDAGKVLALGTPREVKQRAAVlsavsg 595
Cdd:PRK09700 165 KVIIMDEPTSSLTNKEVDYLFLIMNQLRKEGTAIVYISHKLAEiRRICDRYTVMKDGSSVCSGMVSDVSNDDIV------ 238
|
250 260
....*....|....*....|....*...
gi 2553857580 596 qSLVVDRmSIEDAFVAIVEA-GRRSQET 622
Cdd:PRK09700 239 -RLMVGR-ELQNRFNAMKENvSNLAHET 264
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
380-583 |
3.89e-27 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 111.33 E-value: 3.89e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857580 380 VAVADTSFEVRRGEIFGLLGPNGAGKTTTFRMLCGLLVPSKGQIEVAGYDLRTAKA--GARARIGYVAQK--FSLYGKLs 455
Cdd:PRK13633 24 LALDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVYVDGLDTSDEENlwDIRNKAGMVFQNpdNQIVATI- 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857580 456 VEQNLRYFGRSYGFFGQALQDRIDASLEDFGLTDRRDTTAGSLSFGAKQDLSMACGLIHSPEILFLDEATSGADLASRRA 535
Cdd:PRK13633 103 VEEDVAFGPENLGIPPEEIRERVDESLKKVGMYEYRRHAPHLLSGGQKQRVAIAGILAMRPECIIFDEPTAMLDPSGRRE 182
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 2553857580 536 FWRRINALAS-AGTSVVVTTHFLEEAEYCDRFLIQDAGKVLALGTPREV 583
Cdd:PRK13633 183 VVNTIKELNKkYGITIILITHYMEEAVEADRIIVMDSGKVVMEGTPKEI 231
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
4-261 |
9.92e-27 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 109.02 E-value: 9.92e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857580 4 ASAPAIRLEGVVKTFPNpldaaRPIraVDGISL--KAGgaeasdRLIALVGPDGAGKSTFMRLLCGLEAPDEGRLSVLGT 81
Cdd:COG1121 2 MMMPAIELENLTVSYGG-----RPV--LEDVSLtiPPG------EFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLFGK 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857580 82 TPDPDNEdfttRIAFMPQ----------------TLGLYKTLscrenlevfaGLRGFEGEADgaaglERRIAELLSMTGL 145
Cdd:COG1121 69 PPRRARR----RIGYVPQraevdwdfpitvrdvvLMGRYGRR----------GLFRRPSRAD-----REAVDEALERVGL 129
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857580 146 AGFEERQAGKLSGGMKQKLALASALLRIPDLLLLDEPTVGVDPLSRRELWSVVRRmLADTPMTCVFSTAYLEEA-EAADR 224
Cdd:COG1121 130 EDLADRPIGELSGGQQQRVLLARALAQDPDLLLLDEPFAGVDAATEEALYELLRE-LRREGKTILVVTHDLGAVrEYFDR 208
|
250 260 270
....*....|....*....|....*....|....*...
gi 2553857580 225 VLLFeSGRIIADENPQSFISRAK-GRTYLLPLANRAEH 261
Cdd:COG1121 209 VLLL-NRGLVAHGPPEEVLTPENlSRAYGGPVALLAHG 245
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
9-242 |
1.46e-26 |
|
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: 108.42 E-value: 1.46e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857580 9 IRLEGVVKTFPNPldaarpIRAVDGISLKAGGAEasdrLIALVGPDGAGKSTFMRLLCGLEAPDEGRLSVLGTT----PD 84
Cdd:cd03256 1 IEVENLSKTYPNG------KKALKDVSLSINPGE----FVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGTDinklKG 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857580 85 PDNEDFTTRIAFMPQTLGLYKTLSCRENleVFAGLRGFEGEADGAAGL----ERRIA-ELLSMTGLAGFEERQAGKLSGG 159
Cdd:cd03256 71 KALRQLRRQIGMIFQQFNLIERLSVLEN--VLSGRLGRRSTWRSLFGLfpkeEKQRAlAALERVGLLDKAYQRADQLSGG 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857580 160 MKQKLALASALLRIPDLLLLDEPTVGVDPLSRRELWSVVRRMLADTPMTCVFSTAYLEEAEA-ADRVLLFESGRIIADEN 238
Cdd:cd03256 149 QQQRVAIARALMQQPKLILADEPVASLDPASSRQVMDLLKRINREEGITVIVSLHQVDLAREyADRIVGLKDGRIVFDGP 228
|
....
gi 2553857580 239 PQSF 242
Cdd:cd03256 229 PAEL 232
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
4-583 |
1.51e-26 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 113.58 E-value: 1.51e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857580 4 ASAPAIRLEGVVKTFPnpldaarPIRAVDGISLKAGGAEasdrlI-ALVGPDGAGKSTFMRLLCGLEAPDEGRLSVLGTT 82
Cdd:COG3845 1 MMPPALELRGITKRFG-------GVVANDDVSLTVRPGE-----IhALLGENGAGKSTLMKILYGLYQPDSGEILIDGKP 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857580 83 PDPDNedftTRIA-----------FMpqtlgLYKTLSCRENleVFAGLRGFEGEADGAAGLERRIAELLSMTGLAGFEER 151
Cdd:COG3845 69 VRIRS----PRDAialgigmvhqhFM-----LVPNLTVAEN--IVLGLEPTKGGRLDRKAARARIRELSERYGLDVDPDA 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857580 152 QAGKLSGGMKQK-------------LALasallripdllllDEPTVGVDPLSRRELWSVVRRmLADTPMTCVFSTAYLEE 218
Cdd:COG3845 138 KVEDLSVGEQQRveilkalyrgariLIL-------------DEPTAVLTPQEADELFEILRR-LAAEGKSIIFITHKLRE 203
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857580 219 A-EAADRVLLFESGRIIADENPqsfisrakgrtyllplanraehdaqmlcrrlSEETAAtrsdalflDIVPRMGGAaatt 297
Cdd:COG3845 204 VmAIADRVTVLRRGKVVGTVDT-------------------------------AETSEE--------ELAELMVGR---- 240
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857580 298 lAPTLPVKDARVPSGfiprqpsledayalltfprapktanhlasppsdasgalaasaasaddtaerPVVIRADGI-ARKF 376
Cdd:COG3845 241 -EVLLRVEKAPAEPG---------------------------------------------------EVVLEVENLsVRDD 268
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857580 377 GNFVAVADTSFEVRRGEIFGLLGPNGAGKTTTFRMLCGLLVPSKGQIEVAGYDLRTAKAGAR--ARIGYVA---QKFSLY 451
Cdd:COG3845 269 RGVPALKDVSLEVRAGEILGIAGVAGNGQSELAEALAGLRPPASGSIRLDGEDITGLSPRERrrLGVAYIPedrLGRGLV 348
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857580 452 GKLSVEQNL---RYFGRSYGFFG----QALQDRIDASLEDFGL-TDRRDTTAGSLSFGAKQDLSMACGLIHSPEILFLDE 523
Cdd:COG3845 349 PDMSVAENLilgRYRRPPFSRGGfldrKAIRAFAEELIEEFDVrTPGPDTPARSLSGGNQQKVILARELSRDPKLLIAAQ 428
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2553857580 524 ATSGADLASRRAFWRRINALASAGTSVVVTTHFLEEA-EYCDRFLIQDAGKVLALGTPREV 583
Cdd:COG3845 429 PTRGLDVGAIEFIHQRLLELRDAGAAVLLISEDLDEIlALSDRIAVMYEGRIVGEVPAAEA 489
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
9-245 |
1.74e-26 |
|
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: 108.16 E-value: 1.74e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857580 9 IRLEGVVKTFPNpldaARPirAVDGISLKAGGAEasdrLIALVGPDGAGKSTFMRLLCGLEAPDEGRLSVLG-TTPDPDN 87
Cdd:cd03295 1 IEFENVTKRYGG----GKK--AVNNLNLEIAKGE----FLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGeDIREQDP 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857580 88 EDFTTRIAFMPQTLGLYKTLSCRENLEVFAGLRGFEGEAdgaagLERRIAELLSMTGL--AGFEERQAGKLSGGMKQKLA 165
Cdd:cd03295 71 VELRRKIGYVIQQIGLFPHMTVEENIALVPKLLKWPKEK-----IRERADELLALVGLdpAEFADRYPHELSGGQQQRVG 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857580 166 LASALLRIPDLLLLDEPTVGVDPLSRRELWSVVRRMLADTPMTCVFSTAYLEEA-EAADRVLLFESGRIIADENPQSFIS 244
Cdd:cd03295 146 VARALAADPPLLLMDEPFGALDPITRDQLQEEFKRLQQELGKTIVFVTHDIDEAfRLADRIAIMKNGEIVQVGTPDEILR 225
|
.
gi 2553857580 245 R 245
Cdd:cd03295 226 S 226
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
367-583 |
2.63e-26 |
|
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: 107.77 E-value: 2.63e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857580 367 IRADGIARKFGN-FVAVADTSFEVRRGEIFGLLGPNGAGKTTTFRMLCGLLVPSKGQIEVAGYDLRTAKAGA-RARIGYV 444
Cdd:cd03295 1 IEFENVTKRYGGgKKAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGEDIREQDPVElRRKIGYV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857580 445 AQKFSLYGKLSVEQNLRYFGRSYGFFGQALQDRIDASLEDFGLTDR--RDTTAGSLSFGAKQDLSMACGLIHSPEILFLD 522
Cdd:cd03295 81 IQQIGLFPHMTVEENIALVPKLLKWPKEKIRERADELLALVGLDPAefADRYPHELSGGQQQRVGVARALAADPPLLLMD 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2553857580 523 EATSGADLASRRAFWRRINALASA-GTSVVVTTHFLEEA-EYCDRFLIQDAGKVLALGTPREV 583
Cdd:cd03295 161 EPFGALDPITRDQLQEEFKRLQQElGKTIVFVTHDIDEAfRLADRIAIMKNGEIVQVGTPDEI 223
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
9-232 |
2.98e-26 |
|
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is comprised of all BPD (Binding Protein Dependent) systems that are largely represented in archaea and eubacteria and are primarily involved in scavenging solutes from the environment. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213196 [Multi-domain] Cd Length: 178 Bit Score: 105.73 E-value: 2.98e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857580 9 IRLEGVVKTFPNpldaarpIRAVDGISLKAGGAEasdrLIALVGPDGAGKSTFMRLLCGLEAPDEGRLSVLG---TTPDP 85
Cdd:cd03229 1 LELKNVSKRYGQ-------KTVLNDVSLNIEAGE----IVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGedlTDLED 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857580 86 DNEDFTTRIAFMPQTLGLYKTLSCRENLeVFAglrgfegeadgaaglerriaellsmtglagfeerqagkLSGGMKQKLA 165
Cdd:cd03229 70 ELPPLRRRIGMVFQDFALFPHLTVLENI-ALG--------------------------------------LSGGQQQRVA 110
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2553857580 166 LASALLRIPDLLLLDEPTVGVDPLSRRELWSVVRRMLADTPMTCVFSTAYLEEAEA-ADRVLLFESGR 232
Cdd:cd03229 111 LARALAMDPDVLLLDEPTSALDPITRREVRALLKSLQAQLGITVVLVTHDLDEAARlADRVVVLRDGK 178
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
362-586 |
3.16e-26 |
|
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: 113.31 E-value: 3.16e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857580 362 ERPVVIRADGIA-RKFGNFVAVADTSFEVRRGEIFGLLGPNGAGKTTTFRMLCGLLVPSKGQIEVAGYDLRTAKAGA-RA 439
Cdd:COG4988 332 AGPPSIELEDVSfSYPGGRPALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPPYSGSILINGVDLSDLDPASwRR 411
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857580 440 RIGYVAQKFSLYgKLSVEQNLRyFGRSygffgQALQDRIDASLEDFGLTD--RR-----DTTAGS----LSFGAKQDLSM 508
Cdd:COG4988 412 QIAWVPQNPYLF-AGTIRENLR-LGRP-----DASDEELEAALEAAGLDEfvAAlpdglDTPLGEggrgLSGGQAQRLAL 484
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2553857580 509 ACGLIHSPEILFLDEATSGADLASRRAFWRRINALAsAGTSVVVTTHFLEEAEYCDRFLIQDAGKVLALGTPREVKQR 586
Cdd:COG4988 485 ARALLRDAPLLLLDEPTAHLDAETEAEILQALRRLA-KGRTVILITHRLALLAQADRILVLDDGRIVEQGTHEELLAK 561
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
374-578 |
5.52e-26 |
|
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: 106.44 E-value: 5.52e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857580 374 RKFGNFVAVADTSFEVRRGEIFGLLGPNGAGKTTTFRMLCGLLVPSKGQIEVAGYDLRTAKAGA----RARIGYVAQK-- 447
Cdd:cd03257 13 TGGGSVKALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGKDLLKLSRRLrkirRKEIQMVFQDpm 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857580 448 FSLYGKLSVEQN----LRYFGRSYGffGQALQDRIDASLEDFGLTDRR-DTTAGSLSFGAKQDLSMACGLIHSPEILFLD 522
Cdd:cd03257 93 SSLNPRMTIGEQiaepLRIHGKLSK--KEARKEAVLLLLVGVGLPEEVlNRYPHELSGGQRQRVAIARALALNPKLLIAD 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 2553857580 523 EATSGADLASRRAFWRRINALASA-GTSVVVTTHFLEEAEY-CDRFLIQDAGKVLALG 578
Cdd:cd03257 171 EPTSALDVSVQAQILDLLKKLQEElGLTLLFITHDLGVVAKiADRVAVMYAGKIVEEG 228
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
381-583 |
6.28e-26 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 107.79 E-value: 6.28e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857580 381 AVADTSFEVRRGEIFGLLGPNGAGKTTTFRMLCGLLVPSKGQIEVAGYDLRTAKA-GARARIGYVAQ----KFslYGKlS 455
Cdd:PRK13635 22 ALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGGMVLSEETVwDVRRQVGMVFQnpdnQF--VGA-T 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857580 456 VEQNLRYFGRSYGFFGQALQDRIDASLEDFGLTDRRDTTAGSLSFGAKQDLSMACGLIHSPEILFLDEATSGADLASRR- 534
Cdd:PRK13635 99 VQDDVAFGLENIGVPREEMVERVDQALRQVGMEDFLNREPHRLSGGQKQRVAIAGVLALQPDIIILDEATSMLDPRGRRe 178
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 2553857580 535 --AFWRRINalASAGTSVVVTTHFLEEAEYCDRFLIQDAGKVLALGTPREV 583
Cdd:PRK13635 179 vlETVRQLK--EQKGITVLSITHDLDEAAQADRVIVMNKGEILEEGTPEEI 227
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
381-578 |
2.96e-25 |
|
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic bacteriocins of lactic acid bacteria are produced as precursors which have N-terminal leader peptides that share similarities in amino acid sequence and contain a conserved processing site of two glycine residues in positions -1 and -2. A dedicated ATP-binding cassette (ABC) transporter is responsible for the proteolytic cleavage of the leader peptides and subsequent translocation of the bacteriocins across the cytoplasmic membrane.
Pssm-ID: 213212 [Multi-domain] Cd Length: 220 Bit Score: 104.21 E-value: 2.96e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857580 381 AVADTSFEVRRGEIFGLLGPNGAGKTTTFRMLCGLLVPSKGQIEVAGYDLRTAK-AGARARIGYVAQKFSL-YGklSVEQ 458
Cdd:cd03245 19 ALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGTDIRQLDpADLRRNIGYVPQDVTLfYG--TLRD 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857580 459 NLRYFGRSygffgqALQDRIDASLEDFGLTD-RRDTTAG----------SLSFGAKQDLSMACGLIHSPEILFLDEATSG 527
Cdd:cd03245 97 NITLGAPL------ADDERILRAAELAGVTDfVNKHPNGldlqigergrGLSGGQRQAVALARALLNDPPILLLDEPTSA 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 2553857580 528 ADLASRRAFWRRINALAsAGTSVVVTTHFLEEAEYCDRFLIQDAGKVLALG 578
Cdd:cd03245 171 MDMNSEERLKERLRQLL-GDKTLIIITHRPSLLDLVDRIIVMDSGRIVADG 220
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
386-582 |
4.44e-25 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 109.87 E-value: 4.44e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857580 386 SFEVRRGEIFGLLGPNGAGKTTTFRMLCGLLVPSKGQIEVAGYDLRTAKAGA-RARIGYVAQKFSLYgKLSVEQNLRYfG 464
Cdd:COG1132 360 SLTIPPGETVALVGPSGSGKSTLVNLLLRFYDPTSGRILIDGVDIRDLTLESlRRQIGVVPQDTFLF-SGTIRENIRY-G 437
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857580 465 RSygffgQALQDRI-----DASLEDF--GLTDRRDTTAG----SLSFGAKQDLSMACGLIHSPEILFLDEATSGADLASR 533
Cdd:COG1132 438 RP-----DATDEEVeeaakAAQAHEFieALPDGYDTVVGergvNLSGGQRQRIAIARALLKDPPILILDEATSALDTETE 512
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 2553857580 534 RAFWRRINALaSAGTSVVVTTHFLEEAEYCDRFLIQDAGKVLALGTPRE 582
Cdd:COG1132 513 ALIQEALERL-MKGRTTIVIAHRLSTIRNADRILVLDDGRIVEQGTHEE 560
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
9-234 |
4.50e-25 |
|
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: 103.81 E-value: 4.50e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857580 9 IRLEGVVKTFPnplDAARPIRAVDGISLKAGGAEasdrLIALVGPDGAGKSTFMRLLCGLEAPDEGRLSVLGT----TPD 84
Cdd:cd03258 2 IELKNVSKVFG---DTGGKVTALKDVSLSVPKGE----IFGIIGRSGAGKSTLIRCINGLERPTSGSVLVDGTdltlLSG 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857580 85 PDNEDFTTRIAFMPQTLGLYKTLSCREN----LEVfAGLRGFEgeadgaagLERRIAELLSMTGLAGFEERQAGKLSGGM 160
Cdd:cd03258 75 KELRKARRRIGMIFQHFNLLSSRTVFENvalpLEI-AGVPKAE--------IEERVLELLELVGLEDKADAYPAQLSGGQ 145
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2553857580 161 KQKLALASALLRIPDLLLLDEPTVGVDPLSRRELWSVVRRMLADTPMTCVFSTAYLEEA-EAADRVLLFESGRII 234
Cdd:cd03258 146 KQRVGIARALANNPKVLLCDEATSALDPETTQSILALLRDINRELGLTIVLITHEMEVVkRICDRVAVMEKGEVV 220
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
9-236 |
4.66e-25 |
|
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: 104.06 E-value: 4.66e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857580 9 IRLEGVVKTFpnpldaaRPIRAVDGISLKAGGAEasdrLIALVGPDGAGKSTFMRLLCGLEAPDEGRLSVLGttpdpdnE 88
Cdd:cd03219 1 LEVRGLTKRF-------GGLVALDDVSFSVRPGE----IHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFDG-------E 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857580 89 DFTT----RIA-------FmpQTLGLYKTLSCRENLEVFAGLRG-----FEGEADGAAGLERRIAELLSMTGLAGFEERQ 152
Cdd:cd03219 63 DITGlpphEIArlgigrtF--QIPRLFPELTVLENVMVAAQARTgsgllLARARREEREARERAEELLERVGLADLADRP 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857580 153 AGKLSGGMKQKLALASALLRIPDLLLLDEPTVGVDPLSRRELWSVVRRmLADTPMTCVfstayLEE------AEAADRVL 226
Cdd:cd03219 141 AGELSYGQQRRLEIARALATDPKLLLLDEPAAGLNPEETEELAELIRE-LRERGITVL-----LVEhdmdvvMSLADRVT 214
|
250
....*....|
gi 2553857580 227 LFESGRIIAD 236
Cdd:cd03219 215 VLDQGRVIAE 224
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
380-583 |
6.98e-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: 103.72 E-value: 6.98e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857580 380 VAVADTSFEVRRGEIFGLLGPNGAGKTTTFRMLCGLLVPSKGQIEVAGYDLRTA-KAGARARIGYVAQKFSLYGKlSVEQ 458
Cdd:cd03252 16 VILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGHDLALAdPAWLRRQVGVVLQENVLFNR-SIRD 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857580 459 NLryfgrSYGFFGQALQDRIDAS----LEDF--GLTDRRDTTAG----SLSFGAKQDLSMACGLIHSPEILFLDEATSGA 528
Cdd:cd03252 95 NI-----ALADPGMSMERVIEAAklagAHDFisELPEGYDTIVGeqgaGLSGGQRQRIAIARALIHNPRILIFDEATSAL 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 2553857580 529 DLASRRAFWRRINALaSAGTSVVVTTHFLEEAEYCDRFLIQDAGKVLALGTPREV 583
Cdd:cd03252 170 DYESEHAIMRNMHDI-CAGRTVIIIAHRLSTVKNADRIIVMEKGRIVEQGSHDEL 223
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
384-586 |
9.35e-25 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 104.43 E-value: 9.35e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857580 384 DTSFEVRRGEIFGLLGPNGAGKTTTFRMLCGLLVPSKGQIEVAGyDLRTAKA--GARARIGYVAQK-FSLYGKLSVEQNL 460
Cdd:PRK13650 25 DVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIIDG-DLLTEENvwDIRHKIGMVFQNpDNQFVGATVEDDV 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857580 461 RYFGRSYGFFGQALQDRIDASLEDFGLTDRRDTTAGSLSFGAKQDLSMACGLIHSPEILFLDEATSGADLASRRAFWRRI 540
Cdd:PRK13650 104 AFGLENKGIPHEEMKERVNEALELVGMQDFKEREPARLSGGQKQRVAIAGAVAMRPKIIILDEATSMLDPEGRLELIKTI 183
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 2553857580 541 NAL-ASAGTSVVVTTHFLEEAEYCDRFLIQDAGKVLALGTPREVKQR 586
Cdd:PRK13650 184 KGIrDDYQMTVISITHDLDEVALSDRVLVMKNGQVESTSTPRELFSR 230
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
371-578 |
1.90e-24 |
|
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type transporter and the ATPase component of a molybdate transport system that also includes the periplasmic binding protein ModA and the membrane protein ModB. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213264 [Multi-domain] Cd Length: 214 Bit Score: 101.60 E-value: 1.90e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857580 371 GIARKFGNFVAVADTSFEvrrGEIFGLLGPNGAGKTTTFRMLCGLLVPSKGQIEVAGYDLRTAKAGA-----RARIGYVA 445
Cdd:cd03297 5 DIEKRLPDFTLKIDFDLN---EEVTGIFGASGAGKSTLLRCIAGLEKPDGGTIVLNGTVLFDSRKKInlppqQRKIGLVF 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857580 446 QKFSLYGKLSVEQNLRYfgrSYGFFGQA-LQDRIDASLEDFGLTDRRDTTAGSLSFGAKQDLSMACGLIHSPEILFLDEA 524
Cdd:cd03297 82 QQYALFPHLNVRENLAF---GLKRKRNReDRISVDELLDLLGLDHLLNRYPAQLSGGEKQRVALARALAAQPELLLLDEP 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 2553857580 525 TSGADLASR---RAFWRRInaLASAGTSVVVTTHFLEEAEY-CDRFLIQDAGKVLALG 578
Cdd:cd03297 159 FSALDRALRlqlLPELKQI--KKNLNIPVIFVTHDLSEAEYlADRIVVMEDGRLQYIG 214
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
367-578 |
2.16e-24 |
|
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: 101.56 E-value: 2.16e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857580 367 IRADGIARKFGNFVAVADTSFEVRRGEIFGLLGPNGAGKTTTFRMLCGLLVPSKGQIEVAGYDLRTAKAGARaRIGYVAQ 446
Cdd:cd03301 1 VELENVTKRFGNVTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGRDVTDLPPKDR-DIAMVFQ 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857580 447 KFSLYGKLSVEQNLRYFGRSYGFFGQALQDRIDASLEDFGLTDRRDTTAGSLSFGAKQDLSMACGLIHSPEILFLDEATS 526
Cdd:cd03301 80 NYALYPHMTVYDNIAFGLKLRKVPKDEIDERVREVAELLQIEHLLDRKPKQLSGGQRQRVALGRAIVREPKVFLMDEPLS 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 2553857580 527 GADLASRRAFWRRINALASA-GTSVVVTTHFLEEAE-YCDRFLIQDAGKVLALG 578
Cdd:cd03301 160 NLDAKLRVQMRAELKRLQQRlGTTTIYVTHDQVEAMtMADRIAVMNDGQIQQIG 213
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
367-574 |
2.91e-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: 101.07 E-value: 2.91e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857580 367 IRADGIARKFGNFVAVADTSFEVRRGEIFGLLGPNGAGKTTTFRMLCGLLVPSKGQIEVAGYDLRTAKAGA---RARIGY 443
Cdd:cd03262 1 IEIKNLHKSFGDFHVLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIDGLKLTDDKKNInelRQKVGM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857580 444 VAQKFSLYGKLSVEQNL-----RYFGRSygffGQALQDRIDASLEDFGLTDRRDTTAGSLSFGAKQDLSMACGLIHSPEI 518
Cdd:cd03262 81 VFQQFNLFPHLTVLENItlapiKVKGMS----KAEAEERALELLEKVGLADKADAYPAQLSGGQQQRVAIARALAMNPKV 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 2553857580 519 LFLDEATSGADLASRRAFWRRINALASAGTSVVVTTHFLEEA-EYCDRFLIQDAGKV 574
Cdd:cd03262 157 MLFDEPTSALDPELVGEVLDVMKDLAEEGMTMVVVTHEMGFArEVADRVIFMDDGRI 213
|
|
| galliderm_ABC |
TIGR03740 |
gallidermin-class lantibiotic protection ABC transporter, ATP-binding subunit; Model TIGR03731 ... |
30-234 |
3.21e-24 |
|
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: 101.32 E-value: 3.21e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857580 30 AVDGISLKAggaeASDRLIALVGPDGAGKSTFMRLLCGLEAPDEGRLSVlgttpdpDNEDFTTR----IAFMPQTLGLYK 105
Cdd:TIGR03740 15 AVNNISLTV----PKNSVYGLLGPNGAGKSTLLKMITGILRPTSGEIIF-------DGHPWTRKdlhkIGSLIESPPLYE 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857580 106 TLSCRENLEVFAGLRGFEgeadgaaglERRIAELLSMTGLAGFEERQAGKLSGGMKQKLALASALLRIPDLLLLDEPTVG 185
Cdd:TIGR03740 84 NLTARENLKVHTTLLGLP---------DSRIDEVLNIVDLTNTGKKKAKQFSLGMKQRLGIAIALLNHPKLLILDEPTNG 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 2553857580 186 VDPLSRRELWSVVrRMLADTPMTCVFSTAYLEEAEA-ADRVLLFESGRII 234
Cdd:TIGR03740 155 LDPIGIQELRELI-RSFPEQGITVILSSHILSEVQQlADHIGIISEGVLG 203
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
4-240 |
3.26e-24 |
|
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: 101.59 E-value: 3.26e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857580 4 ASAPAIRLEGVVKTFpnpldAARPIraVDGISL--KAGgaeasdRLIALVGPDGAGKSTFMRLLCGLEAPDEGRLSVLGt 81
Cdd:COG1127 1 MSEPMIEVRNLTKSF-----GDRVV--LDGVSLdvPRG------EILAIIGGSGSGKSVLLKLIIGLLRPDSGEILVDG- 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857580 82 tpdpdnEDFTT-----------RIAFMPQTLGLYKTLSCRENLEVfaGLRgfEGEADGAAGLERRIAELLSMTGLAGFEE 150
Cdd:COG1127 67 ------QDITGlsekelyelrrRIGMLFQGGALFDSLTVFENVAF--PLR--EHTDLSEAEIRELVLEKLELVGLPGAAD 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857580 151 RQAGKLSGGMKQKLALASAllripdllllDEPTVGVDPLSRRELWSVVRRMLADTPMTCVFSTAYLEEA-EAADRVLLFE 229
Cdd:COG1127 137 KMPSELSGGMRKRVALARAlaldpeillyDEPTAGLDPITSAVIDELIRELRDELGLTSVVVTHDLDSAfAIADRVAVLA 216
|
250
....*....|.
gi 2553857580 230 SGRIIADENPQ 240
Cdd:COG1127 217 DGKIIAEGTPE 227
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
381-593 |
4.09e-24 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 102.62 E-value: 4.09e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857580 381 AVADTSFEVRRGEIFGLLGPNGAGKTTTFRMLCGLLVPSKGQIEVAGYDLRTAKAGA---RARIGYVAQK-----FSLyg 452
Cdd:PRK13636 21 ALKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGKPIDYSRKGLmklRESVGMVFQDpdnqlFSA-- 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857580 453 klSVEQNLRYFGRSYGFFGQALQDRIDASLEDFGLTDRRDTTAGSLSFGAKQDLSMACGLIHSPEILFLDEATSGADLAS 532
Cdd:PRK13636 99 --SVYQDVSFGAVNLKLPEDEVRKRVDNALKRTGIEHLKDKPTHCLSFGQKKRVAIAGVLVMEPKVLVLDEPTAGLDPMG 176
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2553857580 533 RRAFWRRINALASA-GTSVVVTTHFLEE-AEYCDRFLIQDAGKVLALGTPREVKQRAAVLSAV 593
Cdd:PRK13636 177 VSEIMKLLVEMQKElGLTIIIATHDIDIvPLYCDNVFVMKEGRVILQGNPKEVFAEKEMLRKV 239
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
8-233 |
4.46e-24 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 104.00 E-value: 4.46e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857580 8 AIRLEGVVKTFPNpldaarpIRAVDGISL--KAGGaeasdrLIALVGPDGAGKSTFMRLLCGLEAPDEGRLSVlgttpdp 85
Cdd:COG3839 3 SLELENVSKSYGG-------VEALKDIDLdiEDGE------FLVLLGPSGCGKSTLLRMIAGLEDPTSGEILI------- 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857580 86 DNEDFTT------RIAFMPQTLGLYKTLSCRENLEvFaGLRgfegeadgAAGL-----ERRIAELLSMTGLAGFEERQAG 154
Cdd:COG3839 63 GGRDVTDlppkdrNIAMVFQSYALYPHMTVYENIA-F-PLK--------LRKVpkaeiDRRVREAAELLGLEDLLDRKPK 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857580 155 KLSGGMKQKLALASALLRIPDLLLLDEPTVGVDPLSRRELWSVVRRMLADTPMTCVFSTAYLEEAEA-ADRVLLFESGRI 233
Cdd:COG3839 133 QLSGGQRQRVALGRALVREPKVFLLDEPLSNLDAKLRVEMRAEIKRLHRRLGTTTIYVTHDQVEAMTlADRIAVMNDGRI 212
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
9-576 |
4.52e-24 |
|
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose isomerase and xylulokinase enzymes for xylose utilization. Members of this protein family are the ATP-binding cassette (ABC) subunit of the known or predicted high-affinity xylose ABC transporter for xylose import. These genes, which closely resemble other sugar transport ABC transporter genes, typically are encoded near xylose utilization enzymes and regulatory proteins. Note that this form of the transporter contains two copies of the ABC transporter domain (pfam00005). [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 131681 [Multi-domain] Cd Length: 500 Bit Score: 106.06 E-value: 4.52e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857580 9 IRLEGVVKTFPNpldaarpIRAVDGISLKAGGAEasdrLIALVGPDGAGKSTFMRLLCGL--EAPDEGRLSVLGTTPDPD 86
Cdd:TIGR02633 2 LEMKGIVKTFGG-------VKALDGIDLEVRPGE----CVGLCGENGAGKSTLMKILSGVypHGTWDGEIYWSGSPLKAS 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857580 87 NEDFTTR--IAFMPQTLGLYKTLSCRENleVFAGLR-GFEGEADGAAGLERRIAELLSMTGL-AGFEERQAGKLSGGMKQ 162
Cdd:TIGR02633 71 NIRDTERagIVIIHQELTLVPELSVAEN--IFLGNEiTLPGGRMAYNAMYLRAKNLLRELQLdADNVTRPVGDYGGGQQQ 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857580 163 KLALASALLRIPDLLLLDEPTVGVDPLSRRELWSVVRRMLADTpMTCVFSTAYLEEAEA-ADRVLLFESGRIIADENpqs 241
Cdd:TIGR02633 149 LVEIAKALNKQARLLILDEPSSSLTEKETEILLDIIRDLKAHG-VACVYISHKLNEVKAvCDTICVIRDGQHVATKD--- 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857580 242 fisrakgrtyllplanraehdaqmlCRRLSEEtaatrsdalflDIVPRMGGAAATTLAPTLP--VKDArvpsgfIPRQPS 319
Cdd:TIGR02633 225 -------------------------MSTMSED-----------DIITMMVGREITSLYPHEPheIGDV------ILEARN 262
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857580 320 LedayalltfprapkTANHLASPPsdasgalaasaasaddtaerpvviradgIARkfgnfvaVADTSFEVRRGEIFGLLG 399
Cdd:TIGR02633 263 L--------------TCWDVINPH----------------------------RKR-------VDDVSFSLRRGEILGVAG 293
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857580 400 PNGAGKTTTFRMLCGLLvPSK--GQIEVAGY--DLRTAKAGARARIGYVAQKFSLYG---KLSVEQNLRYFG-RSYGFFG 471
Cdd:TIGR02633 294 LVGAGRTELVQALFGAY-PGKfeGNVFINGKpvDIRNPAQAIRAGIAMVPEDRKRHGivpILGVGKNITLSVlKSFCFKM 372
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857580 472 Q----ALQDRIDASLEDFGL-TDRRDTTAGSLSFGAKQDLSMACGLIHSPEILFLDEATSGADLASRRAFWRRINALASA 546
Cdd:TIGR02633 373 RidaaAELQIIGSAIQRLKVkTASPFLPIGRLSGGNQQKAVLAKMLLTNPRVLILDEPTRGVDVGAKYEIYKLINQLAQE 452
|
570 580 590
....*....|....*....|....*....|.
gi 2553857580 547 GTSVVVTTHFLEEA-EYCDRFLIQDAGKVLA 576
Cdd:TIGR02633 453 GVAIIVVSSELAEVlGLSDRVLVIGEGKLKG 483
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
371-597 |
4.66e-24 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 101.61 E-value: 4.66e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857580 371 GIARKFGNFVAVADTSFEVRRGEIFGLLGPNGAGKTTTFRMLCGLLVPSKGQIEVAGYDLRTAKAGARARIGYVA--QKF 448
Cdd:PRK11300 10 GLMMRFGGLLAVNNVNLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTILLRGQHIEGLPGHQIARMGVVRtfQHV 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857580 449 SLYGKLSVEQNL-----RYFGRSY--GFF---------GQALqDRIDASLEDFGLTDRRDTTAGSLSFGAKQDLSMACGL 512
Cdd:PRK11300 90 RLFREMTVIENLlvaqhQQLKTGLfsGLLktpafrraeSEAL-DRAATWLERVGLLEHANRQAGNLAYGQQRRLEIARCM 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857580 513 IHSPEILFLDEATSGADLASRRAFWRRINALASA-GTSVVVTTHFLEEA-EYCDRFLIQDAGKVLALGTPREVKQRAAVL 590
Cdd:PRK11300 169 VTQPEILMLDEPAAGLNPKETKELDELIAELRNEhNVTVLLIEHDMKLVmGISDRIYVVNQGTPLANGTPEEIRNNPDVI 248
|
....*..
gi 2553857580 591 SAVSGQS 597
Cdd:PRK11300 249 KAYLGEA 255
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
5-240 |
5.08e-24 |
|
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: 101.65 E-value: 5.08e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857580 5 SAPAIRLEGVVKTFpnpldaaRPIRAVDGISLKAGGAEasdrLIALVGPDGAGKSTFMRLLCGLEAPDEGRLSVLGttpd 84
Cdd:COG0411 1 SDPLLEVRGLTKRF-------GGLVAVDDVSLEVERGE----IVGLIGPNGAGKTTLFNLITGFYRPTSGRILFDG---- 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857580 85 pdnEDFTT----RIA-------FmpQTLGLYKTLSCRENLEV----------FAGLRGFEGEADGAAGLERRIAELLSMT 143
Cdd:COG0411 66 ---RDITGlpphRIArlgiartF--QNPRLFPELTVLENVLVaaharlgrglLAALLRLPRARREEREARERAEELLERV 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857580 144 GLAGFEERQAGKLSGGMKQKLALASALLRIPDLLLLDEPTVGVDPLSRRELWSVVRRMLADTPMTC---------VFSTa 214
Cdd:COG0411 141 GLADRADEPAGNLSYGQQRRLEIARALATEPKLLLLDEPAAGLNPEETEELAELIRRLRDERGITIlliehdmdlVMGL- 219
|
250 260
....*....|....*....|....*.
gi 2553857580 215 yleeaeaADRVLLFESGRIIADENPQ 240
Cdd:COG0411 220 -------ADRIVVLDFGRVIAEGTPA 238
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
7-600 |
6.58e-24 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 105.47 E-value: 6.58e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857580 7 PAIRLEGVVKTFPNpldaarpIRAVDGISLK--AGgaeasdRLIALVGPDGAGKSTFMRLLCGLEAPDEGRLSVLG---- 80
Cdd:PRK10762 3 ALLQLKGIDKAFPG-------VKALSGAALNvyPG------RVMALVGENGAGKSTMMKVLTGIYTRDAGSILYLGkevt 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857580 81 -TTPDPDNEdftTRIAFMPQTLGLYKTLSCRENleVFAGlRGFEGeADGAAGLERRIAE---LLSMTGLAGFEERQAGKL 156
Cdd:PRK10762 70 fNGPKSSQE---AGIGIIHQELNLIPQLTIAEN--IFLG-REFVN-RFGRIDWKKMYAEadkLLARLNLRFSSDKLVGEL 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857580 157 SGGMKQKLALASALLRIPDLLLLDEPTvgvDPLSRRE---LWSVVRRmLADTPMTCVFSTAYLEEA-EAADRVLLFESGR 232
Cdd:PRK10762 143 SIGEQQMVEIAKVLSFESKVIIMDEPT---DALTDTEtesLFRVIRE-LKSQGRGIVYISHRLKEIfEICDDVTVFRDGQ 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857580 233 IIAdENPQSfisrakgrtyllplanraehdaqmlcrRLSEETaatrsdalfldIVPRMGGaaattlaptlpvkdarvpsg 312
Cdd:PRK10762 219 FIA-EREVA---------------------------DLTEDS-----------LIEMMVG-------------------- 239
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857580 313 fipRQpsLEDAYALLTFPRAPK--TANHLASPpsdasgalaasaasaddtaerpvviradgiarkfgnfvAVADTSFEVR 390
Cdd:PRK10762 240 ---RK--LEDQYPRLDKAPGEVrlKVDNLSGP--------------------------------------GVNDVSFTLR 276
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857580 391 RGEIFGLLGPNGAGKTTTFRMLCGLLVPSKGQIEVAGYDL--RTAKAGARARIGYVAQ---KFSLYGKLSVEQN-----L 460
Cdd:PRK10762 277 KGEILGVSGLMGAGRTELMKVLYGALPRTSGYVTLDGHEVvtRSPQDGLANGIVYISEdrkRDGLVLGMSVKENmsltaL 356
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857580 461 RYFGRSYGFFG-----QALQDRIDAsledFGL-TDRRDTTAGSLSFGAKQDLSMACGLIHSPEILFLDEATSGADLASRR 534
Cdd:PRK10762 357 RYFSRAGGSLKhadeqQAVSDFIRL----FNIkTPSMEQAIGLLSGGNQQKVAIARGLMTRPKVLILDEPTRGVDVGAKK 432
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2553857580 535 AFWRRINALASAGTSVV-VTTHFLEEAEYCDRFLIQDAGKVLALGTPREVKQRAAVLSAVSGQSLVV 600
Cdd:PRK10762 433 EIYQLINQFKAEGLSIIlVSSEMPEVLGMSDRILVMHEGRISGEFTREQATQEKLMAAAVGKLNRVN 499
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
384-582 |
7.28e-24 |
|
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: 100.77 E-value: 7.28e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857580 384 DTSFEVRRGEIFGLLGPNGAGKTTTFRMLCGLLVPSKGQIEVAGYDLRTAKAGA-RARIGYVAQKFSLYGKlSVEQNLRY 462
Cdd:cd03253 19 DVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDGQDIREVTLDSlRRAIGVVPQDTVLFND-TIGYNIRY 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857580 463 fgrsygffgqalqDRIDASLEDF--------------GLTDRRDTTAGS----LSFGAKQDLSMACGLIHSPEILFLDEA 524
Cdd:cd03253 98 -------------GRPDATDEEVieaakaaqihdkimRFPDGYDTIVGErglkLSGGEKQRVAIARAILKNPPILLLDEA 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 2553857580 525 TSGADLASRRAFWRRINALASAGTSVVVtTHFLEEAEYCDRFLIQDAGKVLALGTPRE 582
Cdd:cd03253 165 TSALDTHTEREIQAALRDVSKGRTTIVI-AHRLSTIVNADKIIVLKDGRIVERGTHEE 221
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
26-244 |
1.18e-23 |
|
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: 100.50 E-value: 1.18e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857580 26 RPIraVDGISL--KAGgaeasdRLIALVGPDGAGKSTFMRLLCGLEAPDEGRLSVLGT-TPDPDNEDFTTRIAFMPQTLG 102
Cdd:COG1120 14 RPV--LDDVSLslPPG------EVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDGRdLASLSRRELARRIAYVPQEPP 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857580 103 LYKTLSCRENLEV----FAGLRGFEGEADgaaglERRIAELLSMTGLAGFEERQAGKLSGGMKQKLALASALLRIPDLLL 178
Cdd:COG1120 86 APFGLTVRELVALgrypHLGLFGRPSAED-----REAVEEALERTGLEHLADRPVDELSGGERQRVLIARALAQEPPLLL 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2553857580 179 LDEPTVGVDPLSRRELWSVVRRMLADTPMTCVFSTAYLEEA-EAADRVLLFESGRIIADENPQSFIS 244
Cdd:COG1120 161 LDEPTSHLDLAHQLEVLELLRRLARERGRTVVMVLHDLNLAaRYADRLVLLKDGRIVAQGPPEEVLT 227
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
8-247 |
1.19e-23 |
|
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: 100.26 E-value: 1.19e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857580 8 AIRLEGVVKTFPNpldAARPIRAVDGISL--KAGGAeasdrlIALVGPDGAGKSTFMRLLCGLEAPDEGRLSVLGTT-PD 84
Cdd:COG1124 1 MLEVRNLSVSYGQ---GGRRVPVLKDVSLevAPGES------FGLVGESGSGKSTLLRALAGLERPWSGEVTFDGRPvTR 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857580 85 PDNEDFTTRIAFMPQ----------TLGlyKTLScrenlEVFAGLRGFEgeadgaagLERRIAELLSMTGL-AGFEERQA 153
Cdd:COG1124 72 RRRKAFRRRVQMVFQdpyaslhprhTVD--RILA-----EPLRIHGLPD--------REERIAELLEQVGLpPSFLDRYP 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857580 154 GKLSGGMKQKLALASALLRIPDLLLLDEPTVGVDPLSRRELWSVVRRMLADTPMTCVFSTAYLEEAEA-ADRVLLFESGR 232
Cdd:COG1124 137 HQLSGGQRQRVAIARALILEPELLLLDEPTSALDVSVQAEILNLLKDLREERGLTYLFVSHDLAVVAHlCDRVAVMQNGR 216
|
250
....*....|....*
gi 2553857580 233 IIADENPQSFISRAK 247
Cdd:COG1124 217 IVEELTVADLLAGPK 231
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
7-240 |
1.51e-23 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 100.86 E-value: 1.51e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857580 7 PAIRLEGVVKTFPnplDAARPirAVDGISLKAGGAEasdrLIALVGPDGAGKSTFMRLLCGLEAPDEGRLSVLGTTPDPD 86
Cdd:PRK13635 4 EIIRVEHISFRYP---DAATY--ALKDVSFSVYEGE----WVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGGMVLSEE 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857580 87 NE-DFTTRIAFMPQTlglyktlscRENLEVfaglrGFEGEADGAAGLE----------RRIAELLSMTGLAGFEERQAGK 155
Cdd:PRK13635 75 TVwDVRRQVGMVFQN---------PDNQFV-----GATVQDDVAFGLEnigvpreemvERVDQALRQVGMEDFLNREPHR 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857580 156 LSGGMKQKLALASALLRIPDLLLLDEPTVGVDPLSRRELWSVVRRMLADTPMTCVFSTAYLEEAEAADRVLLFESGRIIA 235
Cdd:PRK13635 141 LSGGQKQRVAIAGVLALQPDIIILDEATSMLDPRGRREVLETVRQLKEQKGITVLSITHDLDEAAQADRVIVMNKGEILE 220
|
....*
gi 2553857580 236 DENPQ 240
Cdd:PRK13635 221 EGTPE 225
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
31-184 |
1.72e-23 |
|
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: 96.95 E-value: 1.72e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857580 31 VDGISL--KAGgaeasdRLIALVGPDGAGKSTFMRLLCGLEAPDEGRLSVLGTTPDPDNEDFT-TRIAFMPQTLGLYKTL 107
Cdd:pfam00005 1 LKNVSLtlNPG------EILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDLTDDERKSLrKEIGYVFQDPQLFPRL 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857580 108 SCRENLEVFAGLRGFEGEADgaaglERRIAELLSMTGLAGFEER----QAGKLSGGMKQKLALASALLRIPDLLLLDEPT 183
Cdd:pfam00005 75 TVRENLRLGLLLKGLSKREK-----DARAEEALEKLGLGDLADRpvgeRPGTLSGGQRQRVAIARALLTKPKLLLLDEPT 149
|
.
gi 2553857580 184 V 184
Cdd:pfam00005 150 A 150
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
381-582 |
1.96e-23 |
|
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; MsbA is an essential ABC transporter, closely related to eukaryotic MDR proteins. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213218 [Multi-domain] Cd Length: 234 Bit Score: 99.23 E-value: 1.96e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857580 381 AVADTSFEVRRGEIFGLLGPNGAGKTTtfrmLCGLLV----PSKGQIEVAGYDLRTAKAGA-RARIGYVAQKFSLYGKlS 455
Cdd:cd03251 17 VLRDISLDIPAGETVALVGPSGSGKST----LVNLIPrfydVDSGRILIDGHDVRDYTLASlRRQIGLVSQDVFLFND-T 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857580 456 VEQNLRYfgrsyGFFGQALQDRIDAS----LEDF--GLTDRRDTTAGS----LSFGAKQDLSMACGLIHSPEILFLDEAT 525
Cdd:cd03251 92 VAENIAY-----GRPGATREEVEEAAraanAHEFimELPEGYDTVIGErgvkLSGGQRQRIAIARALLKDPPILILDEAT 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 2553857580 526 SGADLASRRAFWRRINALASAGTSVVVtTHFLEEAEYCDRFLIQDAGKVLALGTPRE 582
Cdd:cd03251 167 SALDTESERLVQAALERLMKNRTTFVI-AHRLSTIENADRIVVLEDGKIVERGTHEE 222
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
380-583 |
2.04e-23 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 100.54 E-value: 2.04e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857580 380 VAVADTSFEVRRGEIFGLLGPNGAGKTTTFRMLCGLLVPSKGQIEVAGYDLRTAKAG---ARARIGYVAQK--FSLYGKl 454
Cdd:PRK13639 16 EALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIKGEPIKYDKKSlleVRKTVGIVFQNpdDQLFAP- 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857580 455 SVEQNLRYFGRSYGFFGQALQDRIDASLEDFGLTDRRDTTAGSLSFGAKQDLSMACGLIHSPEILFLDEATSGADLASRR 534
Cdd:PRK13639 95 TVEEDVAFGPLNLGLSKEEVEKRVKEALKAVGMEGFENKPPHHLSGGQKKRVAIAGILAMKPEIIVLDEPTSGLDPMGAS 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 2553857580 535 AFWRRINALASAGTSVVVTTHFLEEAE-YCDRFLIQDAGKVLALGTPREV 583
Cdd:PRK13639 175 QIMKLLYDLNKEGITIIISTHDVDLVPvYADKVYVMSDGKIIKEGTPKEV 224
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
369-555 |
2.26e-23 |
|
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein encoded by ccmA in bacteria. An exception is, an arabidopsis protein. Quite likely this is encoded by an organelle. Bacterial c-type cytocromes are located on the periplasmic side of the cytoplasmic membrane. Several gene products encoded in a locus designated as 'ccm' are implicated in the transport and assembly of the functional cytochrome C. This cluster includes genes: ccmA;B;C;D;E;F;G and H. The posttranslational pathway includes the transport of heme moiety, the secretion of the apoprotein and the covalent attachment of the heme with the apoprotein. The proteins ccmA and B represent an ABC transporter; ccmC and D participate in heme transfer to ccmE, which function as a periplasmic heme chaperone. The presence of ccmF, G and H is suggested to be obligatory for the final functional assembly of cytochrome c. [Protein fate, Protein and peptide secretion and trafficking, Transport and binding proteins, Other]
Pssm-ID: 273491 [Multi-domain] Cd Length: 198 Bit Score: 98.20 E-value: 2.26e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857580 369 ADGIARKFGNFVAVADTSFEVRRGEIFGLLGPNGAGKTTTFRMLCGLLVPSKGQIEVAGYDLRTAKAGARARIGYVAQKF 448
Cdd:TIGR01189 3 ARNLACSRGERMLFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRWNGTPLAEQRDEPHENILYLGHLP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857580 449 SLYGKLSVEQNLRYFGRsygfFGQALQDRIDASLEDFGLTDRRDTTAGSLSFGAKQDLSMACGLIHSPEILFLDEATSGA 528
Cdd:TIGR01189 83 GLKPELSALENLHFWAA----IHGGAQRTIEDALAAVGLTGFEDLPAAQLSAGQQRRLALARLWLSRRPLWILDEPTTAL 158
|
170 180
....*....|....*....|....*..
gi 2553857580 529 DLASRRAFWRRINALASAGTSVVVTTH 555
Cdd:TIGR01189 159 DKAGVALLAGLLRAHLARGGIVLLTTH 185
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
364-574 |
3.55e-23 |
|
Second domain of the ATP-binding cassette component of monosaccharide transport system; This family represents domain II of the carbohydrate uptake proteins that transport only monosaccharides (Monos). The Carb_Monos family is involved in the uptake of monosaccharides, such as pentoses (such as xylose, arabinose, and ribose) and hexoses (such as xylose, arabinose, and ribose), that cannot be broken down to simple sugars by hydrolysis. In members of Carb_Monos family the single hydrophobic gene product forms a homodimer, while the ABC protein represents a fusion of two nucleotide-binding domains. However, it is assumed that two copies of the ABC domains are present in the assembled transporter.
Pssm-ID: 213182 [Multi-domain] Cd Length: 182 Bit Score: 97.12 E-value: 3.55e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857580 364 PVVIRADGIARKfgnfVAVADTSFEVRRGEIFGLLGPNGAGKTTTFRMLCGLLVPSKGQIEVAG--YDLRTAKAGARARI 441
Cdd:cd03215 2 EPVLEVRGLSVK----GAVRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITLDGkpVTRRSPRDAIRAGI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857580 442 GYVA---QKFSLYGKLSVEQNLryfgrsygffgqalqdridasledfgltdrrdTTAGSLSFGAKQDLSMACGLIHSPEI 518
Cdd:cd03215 78 AYVPedrKREGLVLDLSVAENI--------------------------------ALSSLLSGGNQQKVVLARWLARDPRV 125
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 2553857580 519 LFLDEATSGADLASRRAFWRRINALASAGTSVVVTTHFLEEA-EYCDRFLIQDAGKV 574
Cdd:cd03215 126 LILDEPTRGVDVGAKAEIYRLIRELADAGKAVLLISSELDELlGLCDRILVMYEGRI 182
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
1-246 |
3.60e-23 |
|
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: 103.44 E-value: 3.60e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857580 1 MTKASAPAIRLEGVVKTFPnpLDAARPIRAVDGISL--KAGgaeasdRLIALVGPDGAGKSTFMRLLCGLEAPDEGRLSV 78
Cdd:COG1123 253 AAAAAEPLLEVRNLSKRYP--VRGKGGVRAVDDVSLtlRRG------ETLGLVGESGSGKSTLARLLLGLLRPTSGSILF 324
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857580 79 LGTTPDPDNE----DFTTRIAFMPQ--TLGLYKTLSCRENLEvfAGLRGFeGEADGAAgLERRIAELLSMTGL-AGFEER 151
Cdd:COG1123 325 DGKDLTKLSRrslrELRRRVQMVFQdpYSSLNPRMTVGDIIA--EPLRLH-GLLSRAE-RRERVAELLERVGLpPDLADR 400
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857580 152 QAGKLSGGMKQKLALASALLRIPDLLLLDEPTVGVDPLSRRELWSVVRRMLADTPMTCVFSTAYLEEAEA-ADRVLLFES 230
Cdd:COG1123 401 YPHELSGGQRQRVAIARALALEPKLLILDEPTSALDVSVQAQILNLLRDLQRELGLTYLFISHDLAVVRYiADRVAVMYD 480
|
250 260
....*....|....*....|...
gi 2553857580 231 GRIIAD-------ENPQSFISRA 246
Cdd:COG1123 481 GRIVEDgpteevfANPQHPYTRA 503
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
384-586 |
4.17e-23 |
|
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan exporter ATP-binding protein. In A. tumefaciens cyclic beta-1, 2-glucan must be transported into the periplasmic space to exert its action as a virulence factor. This subfamily belongs to the MRP-like family and is involved in drug, peptide, and lipid export. The MRP-like family, similar to all ABC proteins, have a common four-domain core structure constituted by two membrane-spanning domains each composed of six transmembrane (TM) helices and two nucleotide-binding domains (NBD). ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213221 [Multi-domain] Cd Length: 229 Bit Score: 98.07 E-value: 4.17e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857580 384 DTSFEVRRGEIFGLLGPNGAGKTTTFRMLCGLLVPSKGQIEVAGYDLRT-AKAGARARIGYVAQKFSLYGKlSVEQNLRY 462
Cdd:cd03254 21 DINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGIDIRDiSRKSLRSMIGVVLQDTFLFSG-TIMENIRL 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857580 463 fGRSYgffgqALQDRIDASLEDFGLTD--RR-----DTTAG----SLSFGAKQDLSMACGLIHSPEILFLDEATSGADLA 531
Cdd:cd03254 100 -GRPN-----ATDEEVIEAAKEAGAHDfiMKlpngyDTVLGenggNLSQGERQLLAIARAMLRDPKILILDEATSNIDTE 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 2553857580 532 SRRAFWRRINALASAGTSVVVtTHFLEEAEYCDRFLIQDAGKVLALGTPREVKQR 586
Cdd:cd03254 174 TEKLIQEALEKLMKGRTSIII-AHRLSTIKNADKILVLDDGKIIEEGTHDELLAK 227
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
48-236 |
5.75e-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: 97.18 E-value: 5.75e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857580 48 IALVGPDGAGKSTFMRLLCGLEAPDEGRLSVLG---TTPDPDNEDfttrIAFMPQTLGLYKTLSCREN--LEVFAGLRGF 122
Cdd:cd03298 27 TAIVGPSGSGKSTLLNLIAGFETPQSGRVLINGvdvTAAPPADRP----VSMLFQENNLFAHLTVEQNvgLGLSPGLKLT 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857580 123 EGEadgaaglERRIAELLSMTGLAGFEERQAGKLSGGMKQKLALASALLRIPDLLLLDEPTVGVDPLSRRELWSVVRRML 202
Cdd:cd03298 103 AED-------RQAIEVALARVGLAGLEKRLPGELSGGERQRVALARVLVRDKPVLLLDEPFAALDPALRAEMLDLVLDLH 175
|
170 180 190
....*....|....*....|....*....|....*
gi 2553857580 203 ADTPMTCVFSTAYLEEAEA-ADRVLLFESGRIIAD 236
Cdd:cd03298 176 AETKMTVLMVTHQPEDAKRlAQRVVFLDNGRIAAQ 210
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
377-555 |
6.42e-23 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 96.87 E-value: 6.42e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857580 377 GNFVAVADTSFEVRRGEIFGLLGPNGAGKTTTFRMLCGLLVPSKGQIEVAGYDLRTAKagARARIGYVAQKFSLYGKLSV 456
Cdd:PRK13539 13 GGRVLFSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDGGDIDDPD--VAEACHYLGHRNAMKPALTV 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857580 457 EQNLRYFGRsygFFGQALQDrIDASLEDFGLTDRRDTTAGSLSFGAKQDLSMACGLIHSPEILFLDEATSGADLASRRAF 536
Cdd:PRK13539 91 AENLEFWAA---FLGGEELD-IAAALEAVGLAPLAHLPFGYLSAGQKRRVALARLLVSNRPIWILDEPTAALDAAAVALF 166
|
170
....*....|....*....
gi 2553857580 537 WRRINALASAGTSVVVTTH 555
Cdd:PRK13539 167 AELIRAHLAQGGIVIAATH 185
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
367-583 |
1.03e-22 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 100.16 E-value: 1.03e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857580 367 IRADGIARKFGNFVAVADTSFEVRRGEIFGLLGPNGAGKTTTFRMLCGLLVPSKGQIEVAGYDLRTAKAGARaRIGYVAQ 446
Cdd:PRK10851 3 IEIANIKKSFGRTQVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFHGTDVSRLHARDR-KVGFVFQ 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857580 447 KFSLYGKLSVEQN----LRYFGRSYGFFGQALQDRIDASLEDFGLTDRRDTTAGSLSFGAKQDLSMACGLIHSPEILFLD 522
Cdd:PRK10851 82 HYALFRHMTVFDNiafgLTVLPRRERPNAAAIKAKVTQLLEMVQLAHLADRYPAQLSGGQKQRVALARALAVEPQILLLD 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2553857580 523 EATSGADLASRRAFWRRINALAS--AGTSVVVtTHFLEEA-EYCDRFLIQDAGKVLALGTPREV 583
Cdd:PRK10851 162 EPFGALDAQVRKELRRWLRQLHEelKFTSVFV-THDQEEAmEVADRVVVMSQGNIEQAGTPDQV 224
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
28-236 |
1.35e-22 |
|
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: 96.35 E-value: 1.35e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857580 28 IRAVDGISLKAGGAEAsdrlIALVGPDGAGKSTFMRLLCGLEAPDEGRLSVLGttpdpdnEDFTTR---------IAFMP 98
Cdd:cd03224 13 SQILFGVSLTVPEGEI----VALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDG-------RDITGLppheraragIGYVP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857580 99 QTLGLYKTLSCRENLEVFAGLRGFEGEadgaaglERRIAELLSM-TGLAGFEERQAGKLSGGMKQKLALASALLRIPDLL 177
Cdd:cd03224 82 EGRRIFPELTVEENLLLGAYARRRAKR-------KARLERVYELfPRLKERRKQLAGTLSGGEQQMLAIARALMSRPKLL 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857580 178 LLDEPTVGVDPLSRRELWSVVRRmLADTPMTCVFSTAYLEEA-EAADRVLLFESGRIIAD 236
Cdd:cd03224 155 LLDEPSEGLAPKIVEEIFEAIRE-LRDEGVTILLVEQNARFAlEIADRAYVLERGRVVLE 213
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
8-236 |
2.18e-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: 95.73 E-value: 2.18e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857580 8 AIRLEGVVKTFPNpldaaRPIRAVDGISLKAGGAEAsdrlIALVGPDGAGKSTFMRLLCGLEAPDEGRLSVLGT---TPD 84
Cdd:cd03245 2 RIEFRNVSFSYPN-----QEIPALDNVSLTIRAGEK----VAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGTdirQLD 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857580 85 PDneDFTTRIAFMPQTLGL-YKTLscRENLEVFAGlrgfegEADGAAGLerRIAELLSMTGLA-----GFE----ERQAG 154
Cdd:cd03245 73 PA--DLRRNIGYVPQDVTLfYGTL--RDNITLGAP------LADDERIL--RAAELAGVTDFVnkhpnGLDlqigERGRG 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857580 155 kLSGGMKQKLALASALLRIPDLLLLDEPTVGVDPLSRRELWSVVRRMLADTpmTCVFSTAYLEEAEAADRVLLFESGRII 234
Cdd:cd03245 141 -LSGGQRQAVALARALLNDPPILLLDEPTSAMDMNSEERLKERLRQLLGDK--TLIIITHRPSLLDLVDRIIVMDSGRIV 217
|
..
gi 2553857580 235 AD 236
Cdd:cd03245 218 AD 219
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
381-583 |
2.22e-22 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 99.52 E-value: 2.22e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857580 381 AVADTSFEVRRGEIFGLLGPNGAGKTTTFRMLCGLLVPSKGQIEVAGYDLRTAKAGARArIGYVAQKFSLYGKLSVEQNL 460
Cdd:PRK11607 34 AVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVDLSHVPPYQRP-INMMFQSYALFPHMTVEQNI 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857580 461 RyFGRSYGFFGQA-LQDRIDASLEDFGLTDRRDTTAGSLSFGAKQDLSMACGLIHSPEILFLDEATSGADLASR-RAFWR 538
Cdd:PRK11607 113 A-FGLKQDKLPKAeIASRVNEMLGLVHMQEFAKRKPHQLSGGQRQRVALARSLAKRPKLLLLDEPMGALDKKLRdRMQLE 191
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 2553857580 539 RINALASAGTSVVVTTHFLEEA-EYCDRFLIQDAGKVLALGTPREV 583
Cdd:PRK11607 192 VVDILERVGVTCVMVTHDQEEAmTMAGRIAIMNRGKFVQIGEPEEI 237
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
376-583 |
2.46e-22 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 96.62 E-value: 2.46e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857580 376 FGNFVAVADTSFEVRRGEIFGLLGPNGAGKTTTFRMLCGLLVPSKGQIEVAGYDLR--TAKAGARaRIGYVAQKFSLYGK 453
Cdd:PRK11231 12 YGTKRILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDKPISmlSSRQLAR-RLALLPQHHLTPEG 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857580 454 LSVEQNLRYfGRS-----YGFFGQALQDRIDASLEDFGLTDRRDTTAGSLSFGAKQDLSMACGLIHSPEILFLDEATSGA 528
Cdd:PRK11231 91 ITVRELVAY-GRSpwlslWGRLSAEDNARVNQAMEQTRINHLADRRLTDLSGGQRQRAFLAMVLAQDTPVVLLDEPTTYL 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 2553857580 529 DLASRRAFWRRINALASAGTSVVVTTHFLEEA-EYCDRFLIQDAGKVLALGTPREV 583
Cdd:PRK11231 170 DINHQVELMRLMRELNTQGKTVVTVLHDLNQAsRYCDHLVVLANGHVMAQGTPEEV 225
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
385-595 |
3.08e-22 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 96.16 E-value: 3.08e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857580 385 TSFEVRRGEIFGLLGPNGAGKTTTFRMLCGLLvPSKGQIEVAGYDLRTAKAGARARI-GYVAQKFSLYGKLSVEQNLRYF 463
Cdd:PRK03695 15 LSAEVRAGEILHLVGPNGAGKSTLLARMAGLL-PGSGSIQFAGQPLEAWSAAELARHrAYLSQQQTPPFAMPVFQYLTLH 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857580 464 gRSYGFFGQALQDRIDASLEDFGLTDRRDTTAGSLSFGAKQ--DLSMACGLIHsPEI------LFLDEATSGADLASRRA 535
Cdd:PRK03695 94 -QPDKTRTEAVASALNEVAEALGLDDKLGRSVNQLSGGEWQrvRLAAVVLQVW-PDInpagqlLLLDEPMNSLDVAQQAA 171
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2553857580 536 FWRRINALASAGTSVVVTTHFLEE-AEYCDRFLIQDAGKVLALGTPREVkQRAAVLSAVSG 595
Cdd:PRK03695 172 LDRLLSELCQQGIAVVMSSHDLNHtLRHADRVWLLKQGKLLASGRRDEV-LTPENLAQVFG 231
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
10-232 |
4.08e-22 |
|
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: 93.08 E-value: 4.08e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857580 10 RLEGVVKTFPNPldaarpiRAVDGISLKAGGAEasdrLIALVGPDGAGKSTFMRLLCGLEAPDEGRLSVLGT-TPDPDNE 88
Cdd:cd00267 1 EIENLSFRYGGR-------TALDNVSLTLKAGE----IVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGKdIAKLPLE 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857580 89 DFTTRIAFMPQtlglyktlscrenlevfaglrgfegeadgaaglerriaellsmtglagfeerqagkLSGGMKQKLALAS 168
Cdd:cd00267 70 ELRRRIGYVPQ--------------------------------------------------------LSGGQRQRVALAR 93
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2553857580 169 ALLRIPDLLLLDEPTVGVDPLSRRELWSVVRRmLADTPMTCVFSTAYLEEAE-AADRVLLFESGR 232
Cdd:cd00267 94 ALLLNPDLLLLDEPTSGLDPASRERLLELLRE-LAEEGRTVIIVTHDPELAElAADRVIVLKDGK 157
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
366-583 |
4.95e-22 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 97.56 E-value: 4.95e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857580 366 VIRADGIARKF----GNFVAVADTSFEVRRGEIFGLLGPNGAGKTTTFRMLCGLLVPSKGQIEVAGYDLRTAKAG----A 437
Cdd:PRK11153 1 MIELKNISKVFpqggRTIHALNNVSLHIPAGEIFGVIGASGAGKSTLIRCINLLERPTSGRVLVDGQDLTALSEKelrkA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857580 438 RARIGYVAQKFSLYGKLSVEQN----LRYFGRSygffGQALQDRIDASLEDFGLTDRRDTTAGSLSFGAKQDLSMACGLI 513
Cdd:PRK11153 81 RRQIGMIFQHFNLLSSRTVFDNvalpLELAGTP----KAEIKARVTELLELVGLSDKADRYPAQLSGGQKQRVAIARALA 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2553857580 514 HSPEILFLDEATSGADLASRRA---FWRRINALasAGTSVVVTTHFLEEA-EYCDRFLIQDAGKVLALGTPREV 583
Cdd:PRK11153 157 SNPKVLLCDEATSALDPATTRSileLLKDINRE--LGLTIVLITHEMDVVkRICDRVAVIDAGRLVEQGTVSEV 228
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
5-574 |
4.97e-22 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 100.00 E-value: 4.97e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857580 5 SAPAIRLEGVVKTFPNpldaarpIRAVDGISLKAGGAEasdrLIALVGPDGAGKSTFMRLLCGLeAPD---EGRLSVLGT 81
Cdd:PRK13549 2 MEYLLEMKNITKTFGG-------VKALDNVSLKVRAGE----IVSLCGENGAGKSTLMKVLSGV-YPHgtyEGEIIFEGE 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857580 82 TPDPDNEDFTTR--IAFMPQTLGLYKTLSCRENLevFAG---LRGfeGEADGAAgLERRIAELLSMTGLAGFEERQAGKL 156
Cdd:PRK13549 70 ELQASNIRDTERagIAIIHQELALVKELSVLENI--FLGneiTPG--GIMDYDA-MYLRAQKLLAQLKLDINPATPVGNL 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857580 157 SGGMKQKLALASALLRIPDLLLLDEPTVgvdPLSRRE---LWSVVRRmLADTPMTCVFSTAYLEEAEA-ADRVLLFESGR 232
Cdd:PRK13549 145 GLGQQQLVEIAKALNKQARLLILDEPTA---SLTESEtavLLDIIRD-LKAHGIACIYISHKLNEVKAiSDTICVIRDGR 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857580 233 IIADEnpqsfisrakgrtyllPLANraehdaqmlcrrLSEEtaatrsdalflDIVPRMGGAAATTLaptlpvkdarvpsg 312
Cdd:PRK13549 221 HIGTR----------------PAAG------------MTED-----------DIITMMVGRELTAL-------------- 247
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857580 313 fiprqpsledayalltFPRAPKTANHlasppsdasgalaasaasaddtaerpVVIRADGIA--------RKfgnfvAVAD 384
Cdd:PRK13549 248 ----------------YPREPHTIGE--------------------------VILEVRNLTawdpvnphIK-----RVDD 280
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857580 385 TSFEVRRGEIFGLLGPNGAGKTTTFRMLCGLLV-PSKGQIEVAG--YDLRTAKAGARARIGYVAQ---KFSLYGKLSVEQ 458
Cdd:PRK13549 281 VSFSLRRGEILGIAGLVGAGRTELVQCLFGAYPgRWEGEIFIDGkpVKIRNPQQAIAQGIAMVPEdrkRDGIVPVMGVGK 360
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857580 459 NL------RYFGRSygffgqalqdRIDASLE----DFGLTDRRDTTA------GSLSFGAKQDLSMACGLIHSPEILFLD 522
Cdd:PRK13549 361 NItlaaldRFTGGS----------RIDDAAElktiLESIQRLKVKTAspelaiARLSGGNQQKAVLAKCLLLNPKILILD 430
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|...
gi 2553857580 523 EATSGADLASRRAFWRRINALASAGTSVVVTTHFLEEA-EYCDRFLIQDAGKV 574
Cdd:PRK13549 431 EPTRGIDVGAKYEIYKLINQLVQQGVAIIVISSELPEVlGLSDRVLVMHEGKL 483
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
382-574 |
6.14e-22 |
|
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: 93.05 E-value: 6.14e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857580 382 VADTSFEVRRGEIFGLLGPNGAGKTTTFRMLCGLLVPSKGQIEVAGYDLRTAKAGA-RARIGYVAQKFSLygklsveqnl 460
Cdd:cd03246 18 LRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDGADISQWDPNElGDHVGYLPQDDEL---------- 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857580 461 ryfgrsygfFGQALQDRIdasledfgltdrrdttagsLSFGAKQDLSMACGLIHSPEILFLDEATSGADLASRRAFWRRI 540
Cdd:cd03246 88 ---------FSGSIAENI-------------------LSGGQRQRLGLARALYGNPRILVLDEPNSHLDVEGERALNQAI 139
|
170 180 190
....*....|....*....|....*....|....
gi 2553857580 541 NALASAGTSVVVTTHFLEEAEYCDRFLIQDAGKV 574
Cdd:cd03246 140 AALKAAGATRIVIAHRPETLASADRILVLEDGRV 173
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
377-593 |
8.74e-22 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 95.64 E-value: 8.74e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857580 377 GNFVAVADTSFEVRRGEIFGLLGPNGAGKTTTFRMLCGLLVPSKGQIEVAGYDLRTAKAG-ARARIGYVAQK-----FSL 450
Cdd:PRK13652 15 GSKEALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIRGEPITKENIReVRKFVGLVFQNpddqiFSP 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857580 451 ygklSVEQNLRYFGRSYGFFGQALQDRIDASLEDFGLTDRRDTTAGSLSFGAKQDLSMACGLIHSPEILFLDEATSGADL 530
Cdd:PRK13652 95 ----TVEQDIAFGPINLGLDEETVAHRVSSALHMLGLEELRDRVPHHLSGGEKKRVAIAGVIAMEPQVLVLDEPTAGLDP 170
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2553857580 531 ASRRAFWRRINALASA-GTSVVVTTHFLE-EAEYCDRFLIQDAGKVLALGTPREVKQRAAVLSAV 593
Cdd:PRK13652 171 QGVKELIDFLNDLPETyGMTVIFSTHQLDlVPEMADYIYVMDKGRIVAYGTVEEIFLQPDLLARV 235
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
381-583 |
9.70e-22 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 95.64 E-value: 9.70e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857580 381 AVADTSFEVRRGEIFGLLGPNGAGKTTTFRMLCGLLVP---SKGQIEVAGYDLrTAKA--GARARIGYVAQK-FSLYGKL 454
Cdd:PRK13640 22 ALNDISFSIPRGSWTALIGHNGSGKSTISKLINGLLLPddnPNSKITVDGITL-TAKTvwDIREKVGIVFQNpDNQFVGA 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857580 455 SVEQNLRYFGRSYGFFGQALQDRIDASLEDFGLTDRRDTTAGSLSFGAKQDLSMACGLIHSPEILFLDEATSGADLASRR 534
Cdd:PRK13640 101 TVGDDVAFGLENRAVPRPEMIKIVRDVLADVGMLDYIDSEPANLSGGQKQRVAIAGILAVEPKIIILDESTSMLDPAGKE 180
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 2553857580 535 AFWRRINALA-SAGTSVVVTTHFLEEAEYCDRFLIQDAGKVLALGTPREV 583
Cdd:PRK13640 181 QILKLIRKLKkKNNLTVISITHDIDEANMADQVLVLDDGKLLAQGSPVEI 230
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
365-590 |
1.06e-21 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 97.10 E-value: 1.06e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857580 365 VVIRadGIARKFGNFVAVADTSFEVRRGEIFGLLGPNGAGKTTTFRMLCGLLVPSKGQIEVAGYDLrTAKAGARARIGYV 444
Cdd:PRK11432 7 VVLK--NITKRFGSNTVIDNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIFIDGEDV-THRSIQQRDICMV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857580 445 AQKFSLYGKLSVEQNLRYFGRSYGFFGQALQDRIDASLEDFGLTDRRDTTAGSLSFGAKQDLSMACGLIHSPEILFLDEA 524
Cdd:PRK11432 84 FQSYALFPHMSLGENVGYGLKMLGVPKEERKQRVKEALELVDLAGFEDRYVDQISGGQQQRVALARALILKPKVLLFDEP 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2553857580 525 TSGADLASRRAFWRRINALASAG--TSVVVtTHFLEEA-EYCDRFLIQDAGKVLALGTPREVKQRAAVL 590
Cdd:PRK11432 164 LSNLDANLRRSMREKIRELQQQFniTSLYV-THDQSEAfAVSDTVIVMNKGKIMQIGSPQELYRQPASR 231
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
43-233 |
1.24e-21 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 96.69 E-value: 1.24e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857580 43 ASDRLIALVGPDGAGKSTFMRLLCGLEAPDEGRLSVLGTtpdpdneDFT------TRIAFMPQTLGLYKTLSCRENleVF 116
Cdd:PRK10851 26 PSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFHGT-------DVSrlhardRKVGFVFQHYALFRHMTVFDN--IA 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857580 117 AGLRGF-EGEADGAAGLERRIAELLSMTGLAGFEERQAGKLSGGMKQKLALASALLRIPDLLLLDEPTVGVDPLSRRELW 195
Cdd:PRK10851 97 FGLTVLpRRERPNAAAIKAKVTQLLEMVQLAHLADRYPAQLSGGQKQRVALARALAVEPQILLLDEPFGALDAQVRKELR 176
|
170 180 190
....*....|....*....|....*....|....*....
gi 2553857580 196 SVVRRMLADTPMTCVFSTAYLEEA-EAADRVLLFESGRI 233
Cdd:PRK10851 177 RWLRQLHEELKFTSVFVTHDQEEAmEVADRVVVMSQGNI 215
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
1-262 |
1.35e-21 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 96.73 E-value: 1.35e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857580 1 MTKASAPAIRLEGVVKTFPNpldaarpIRAVDGISLKAggaeASDRLIALVGPDGAGKSTFMrLLCGLEAPDEGRLSVLG 80
Cdd:NF000106 6 ISNGARNAVEVRGLVKHFGE-------VKAVDGVDLDV----REGTVLGVLGP*GAA**RGA-LPAHV*GPDAGRRPWRF 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857580 81 TTPDPDNEDFTTRIAF-MPQTLGLYKTLSCRENLEVFAglRGFEGEADGAAGLERRIAELLSMTGLAGfeeRQAGKLSGG 159
Cdd:NF000106 74 *TWCANRRALRRTIG*hRPVR*GRRESFSGRENLYMIG--R*LDLSRKDARARADELLERFSLTEAAG---RAAAKYSGG 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857580 160 MKQKLALASALLRIPDLLLLDEPTVGVDPLSRRELWSVVRRMLADTPmTCVFSTAYLEEAEA-ADRVLLFESGRIIADEN 238
Cdd:NF000106 149 MRRRLDLAASMIGRPAVLYLDEPTTGLDPRTRNEVWDEVRSMVRDGA-TVLLTTQYMEEAEQlAHELTVIDRGRVIADGK 227
|
250 260
....*....|....*....|....
gi 2553857580 239 PQSFISRAKGRTYLLPLANRAEHD 262
Cdd:NF000106 228 VDELKTKVGGRTLQIRPAHAAELD 251
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
4-245 |
1.73e-21 |
|
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: 98.68 E-value: 1.73e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857580 4 ASAPAIRLEGVVKTFPNpldaARPirAVDGISL--KAGgaeasdRLIALVGPDGAGKSTFMRLLCGLEAPDEGRLSVLGT 81
Cdd:COG4988 332 AGPPSIELEDVSFSYPG----GRP--ALDGLSLtiPPG------ERVALVGPSGAGKSTLLNLLLGFLPPYSGSILINGV 399
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857580 82 T-PDPDNEDFTTRIAFMPQTLGLYK-TLscRENLevfaglRGFEGEADGAAglerrIAELLSMTGLAGFEER-------- 151
Cdd:COG4988 400 DlSDLDPASWRRQIAWVPQNPYLFAgTI--RENL------RLGRPDASDEE-----LEAALEAAGLDEFVAAlpdgldtp 466
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857580 152 ---QAGKLSGGMKQKLALASALLRIPDLLLLDEPTVGVDPLSRRELWSVVRRMLADTpmTCVFSTAYLEEAEAADRVLLF 228
Cdd:COG4988 467 lgeGGRGLSGGQAQRLALARALLRDAPLLLLDEPTAHLDAETEAEILQALRRLAKGR--TVILITHRLALLAQADRILVL 544
|
250
....*....|....*..
gi 2553857580 229 ESGRIIADENPQSFISR 245
Cdd:COG4988 545 DDGRIVEQGTHEELLAK 561
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
9-233 |
2.78e-21 |
|
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ATP-binding components of the bacterial periplasmic histidine and glutamine permeases, respectively. Histidine permease is a multi-subunit complex containing the HisQ and HisM integral membrane subunits and two copies of HisP. HisP has properties intermediate between those of integral and peripheral membrane proteins and is accessible from both sides of the membrane, presumably by its interaction with HisQ and HisM. The two HisP subunits form a homodimer within the complex. The domain structure of the amino acid uptake systems is typical for prokaryotic extracellular solute binding protein-dependent uptake systems. All of the amino acid uptake systems also have at least one, and in a few cases, two extracellular solute binding proteins located in the periplasm of Gram-negative bacteria, or attached to the cell membrane of Gram-positive bacteria. The best-studied member of the PAAT (polar amino acid transport) family is the HisJQMP system of S. typhimurium, where HisJ is the extracellular solute binding proteins and HisP is the ABC protein.
Pssm-ID: 213229 [Multi-domain] Cd Length: 213 Bit Score: 92.59 E-value: 2.78e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857580 9 IRLEGVVKTFPNpldaarpIRAVDGISLKAGGAEasdrLIALVGPDGAGKSTFMRLLCGLEAPDEGRLSVLGTTPDPDNE 88
Cdd:cd03262 1 IEIKNLHKSFGD-------FHVLKGIDLTVKKGE----VVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIDGLKLTDDKK 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857580 89 DFTT---RIAFMPQTLGLYKTLSCRENLEVfaGLRGFEGEADGAAglERRIAELLSMTGLAGFEERQAGKLSGGMKQKLA 165
Cdd:cd03262 70 NINElrqKVGMVFQQFNLFPHLTVLENITL--APIKVKGMSKAEA--EERALELLEKVGLADKADAYPAQLSGGQQQRVA 145
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2553857580 166 LASALLRIPDLLLLDEPTVGVDPLSRRELWSVVRRmLADTPMTCVFSTAYLEEA-EAADRVLLFESGRI 233
Cdd:cd03262 146 IARALAMNPKVMLFDEPTSALDPELVGEVLDVMKD-LAEEGMTMVVVTHEMGFArEVADRVIFMDDGRI 213
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
9-233 |
2.95e-21 |
|
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: 92.32 E-value: 2.95e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857580 9 IRLEGVVKTFPNpldaarpIRAVDGISLKAGGAEasdrLIALVGPDGAGKSTFMRLLCGLEAPDEGRLSVLG---TTPDP 85
Cdd:cd03301 1 VELENVTKRFGN-------VTALDDLNLDIADGE----FVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGrdvTDLPP 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857580 86 DNEDfttrIAFMPQTLGLYKTLSCRENLEVFAGLRGFEGEAdgaagLERRIAELLSMTGLAGFEERQAGKLSGGMKQKLA 165
Cdd:cd03301 70 KDRD----IAMVFQNYALYPHMTVYDNIAFGLKLRKVPKDE-----IDERVREVAELLQIEHLLDRKPKQLSGGQRQRVA 140
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2553857580 166 LASALLRIPDLLLLDEPTVGVDPLSRRELWSVVRRMLADTPMTCVFSTAYLEEAEA-ADRVLLFESGRI 233
Cdd:cd03301 141 LGRAIVREPKVFLMDEPLSNLDAKLRVQMRAELKRLQQRLGTTTIYVTHDQVEAMTmADRIAVMNDGQI 209
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
384-578 |
2.95e-21 |
|
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette superfamily; ABCG transporters are involved in eye pigment (EP) precursor transport, regulation of lipid-trafficking mechanisms, and pleiotropic drug resistance (DR). DR is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. Compared to other members of the ABC transporter subfamilies, the ABCG transporter family is composed of proteins that have an ATP-binding cassette domain at the N-terminus and a TM (transmembrane) domain at the C-terminus.
Pssm-ID: 213180 [Multi-domain] Cd Length: 194 Bit Score: 91.84 E-value: 2.95e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857580 384 DTSFEVRRGEIFGLLGPNGAGKTTTFRMLCGLLVPS--KGQIEVAGYDLRtaKAGARARIGYVAQKFSLYGKLSVEQNLR 461
Cdd:cd03213 27 NVSGKAKPGELTAIMGPSGAGKSTLLNALAGRRTGLgvSGEVLINGRPLD--KRSFRKIIGYVPQDDILHPTLTVRETLM 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857580 462 YfgrsygffgqALQDRidasledfgltdrrdttagSLSFGAKQDLSMACGLIHSPEILFLDEATSGADLASRRAFWRRIN 541
Cdd:cd03213 105 F----------AAKLR-------------------GLSGGERKRVSIALELVSNPSLLFLDEPTSGLDSSSALQVMSLLR 155
|
170 180 190
....*....|....*....|....*....|....*....
gi 2553857580 542 ALASAGTSVVVTTHFL--EEAEYCDRFLIQDAGKVLALG 578
Cdd:cd03213 156 RLADTGRTIICSIHQPssEIFELFDKLLLLSQGRVIYFG 194
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
384-586 |
3.26e-21 |
|
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: 92.99 E-value: 3.26e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857580 384 DTSFEVRRGEIFGLLGPNGAGKTTTFRMLCGLLVPSKGQIEVAGYDLRT-AKAGARARIGYVAQKFSLYGKlSVEQNLRY 462
Cdd:cd03249 21 GLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEILLDGVDIRDlNLRWLRSQIGLVSQEPVLFDG-TIAENIRY 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857580 463 fGRSYGFFGQALQDRIDASLEDF--GLTDRRDTTAG----SLSFGAKQDLSMACGLIHSPEILFLDEATSGADLASRRAF 536
Cdd:cd03249 100 -GKPDATDEEVEEAAKKANIHDFimSLPDGYDTLVGergsQLSGGQKQRIAIARALLRNPKILLLDEATSALDAESEKLV 178
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 2553857580 537 WRRINAlASAGTSVVVTTHFLEEAEYCDRFLIQDAGKVLALGTPREVKQR 586
Cdd:cd03249 179 QEALDR-AMKGRTTIVIAHRLSTIRNADLIAVLQNGQVVEQGTHDELMAQ 227
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
9-242 |
4.85e-21 |
|
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: 92.24 E-value: 4.85e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857580 9 IRLEGVVKTFpnpldaaRPIRAVDGISLKAggaeASDRLIALVGPDGAGKSTFMRLLCGL-----EAPDEGRLSVLGT-- 81
Cdd:cd03260 1 IELRDLNVYY-------GDKHALKDISLDI----PKGEITALIGPSGCGKSTLLRLLNRLndlipGAPDEGEVLLDGKdi 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857580 82 -TPDPDNEDFTTRIAFMPQTLGLYKtLSCRENLEVfaGLRgFEGEADGAAgLERRIAELLSMTGLAGFEERQ--AGKLSG 158
Cdd:cd03260 70 yDLDVDVLELRRRVGMVFQKPNPFP-GSIYDNVAY--GLR-LHGIKLKEE-LDERVEEALRKAALWDEVKDRlhALGLSG 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857580 159 GMKQKLALASALLRIPDLLLLDEPTVGVDPLSRRELWSVVRRMlaDTPMTCVFSTAYLEEAE-AADRVLLFESGRIIADE 237
Cdd:cd03260 145 GQQQRLCLARALANEPEVLLLDEPTSALDPISTAKIEELIAEL--KKEYTIVIVTHNMQQAArVADRTAFLLNGRLVEFG 222
|
....*
gi 2553857580 238 NPQSF 242
Cdd:cd03260 223 PTEQI 227
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
9-233 |
5.82e-21 |
|
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: 91.91 E-value: 5.82e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857580 9 IRLEGVVKTFPNpldaarpIRAVDGISL--KAGgaeasdRLIALVGPDGAGKSTFMRLLCGLEAPDEGRLSVLGT--TPD 84
Cdd:cd03300 1 IELENVSKFYGG-------FVALDGVSLdiKEG------EFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGKdiTNL 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857580 85 PDNEdftTRIAFMPQTLGLYKTLSCRENLEVFAGLRGFegeadGAAGLERRIAELLSMTGLAGFEERQAGKLSGGMKQKL 164
Cdd:cd03300 68 PPHK---RPVNTVFQNYALFPHLTVFENIAFGLRLKKL-----PKAEIKERVAEALDLVQLEGYANRKPSQLSGGQQQRV 139
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857580 165 ALASALLRIPDLLLLDEPTVGVDPLSRRELWSVVRRMLADTPMTCVFSTAYLEEAEA-ADRVLLFESGRI 233
Cdd:cd03300 140 AIARALVNEPKVLLLDEPLGALDLKLRKDMQLELKRLQKELGITFVFVTHDQEEALTmSDRIAVMNKGKI 209
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
9-245 |
6.27e-21 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 92.08 E-value: 6.27e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857580 9 IRLEGVVKTFPnpldaarPIRAVDGISLKAGGAEasdrLIALVGPDGAGKSTFMRLLCGLEAPDEGRLSVLG-TTPDPDN 87
Cdd:PRK09493 2 IEFKNVSKHFG-------PTQVLHNIDLNIDQGE----VVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGlKVNDPKV 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857580 88 EDFTTRI-AFMP-QTLGLYKTLSCRENleVFAGLRGFEGEADGAAglERRIAELLSMTGLAGFEERQAGKLSGGMKQKLA 165
Cdd:PRK09493 71 DERLIRQeAGMVfQQFYLFPHLTALEN--VMFGPLRVRGASKEEA--EKQARELLAKVGLAERAHHYPSELSGGQQQRVA 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857580 166 LASALLRIPDLLLLDEPTVGVDPLSRRELWSVVRRmLADTPMTCVFSTAYLEEAE-AADRVLLFESGRIIADENPQSFIS 244
Cdd:PRK09493 147 IARALAVKPKLMLFDEPTSALDPELRHEVLKVMQD-LAEEGMTMVIVTHEIGFAEkVASRLIFIDKGRIAEDGDPQVLIK 225
|
.
gi 2553857580 245 R 245
Cdd:PRK09493 226 N 226
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
46-252 |
6.51e-21 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 91.74 E-value: 6.51e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857580 46 RLIALVGPDGAGKSTFMRLLCGLEAPDEGRLSVlgttpdpDNEDFTTR------IAFMPQTLGLYKTLSCREN--LEVFA 117
Cdd:COG3840 26 ERVAILGPSGAGKSTLLNLIAGFLPPDSGRILW-------NGQDLTALppaerpVSMLFQENNLFPHLTVAQNigLGLRP 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857580 118 GLRGFEGEadgaaglERRIAELLSMTGLAGFEERQAGKLSGGMKQKLALASALLRIPDLLLLDEPTVGVDPLSRRELWSV 197
Cdd:COG3840 99 GLKLTAEQ-------RAQVEQALERVGLAGLLDRLPGQLSGGQRQRVALARCLVRKRPILLLDEPFSALDPALRQEMLDL 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 2553857580 198 VRRMLADTPMTCVFSTAYLEEAEA-ADRVLLFESGRIIADENPQSFISR---AKGRTYL 252
Cdd:COG3840 172 VDELCRERGLTVLMVTHDPEDAARiADRVLLVADGRIAADGPTAALLDGeppPALAAYL 230
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
31-247 |
8.17e-21 |
|
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: 91.63 E-value: 8.17e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857580 31 VDGISLKAggaEASDRLIaLVGPDGAGKSTFMRLLCGLEAPDEGRLSVLG---TTPDPDNEDfttrIAFMPQTLGLYKTL 107
Cdd:cd03299 15 LKNVSLEV---ERGDYFV-ILGPTGSGKSVLLETIAGFIKPDSGKILLNGkdiTNLPPEKRD----ISYVPQNYALFPHM 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857580 108 SCRENLEVfaGLRGFEGEAdgaAGLERRIAELLSMTGLAGFEERQAGKLSGGMKQKLALASALLRIPDLLLLDEPTVGVD 187
Cdd:cd03299 87 TVYKNIAY--GLKKRKVDK---KEIERKVLEIAEMLGIDHLLNRKPETLSGGEQQRVAIARALVVNPKILLLDEPFSALD 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2553857580 188 PLSRRELWSVVRRMLADTPMTCVFSTAYLEEAEA-ADRVLLFESGRIIADENPQSFISRAK 247
Cdd:cd03299 162 VRTKEKLREELKKIRKEFGVTVLHVTHDFEEAWAlADKVAIMLNGKLIQVGKPEEVFKKPK 222
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
26-234 |
9.57e-21 |
|
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: 90.78 E-value: 9.57e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857580 26 RPIRAVDGISLKAGGAEasdrLIALVGPDGAGKSTFMRLLCGLEAPDEGRLSVLGttPDPDNEDFTTRIAFMPQTLGlYK 105
Cdd:cd03226 11 KGTEILDDLSLDLYAGE----IIALTGKNGAGKTTLAKILAGLIKESSGSILLNG--KPIKAKERRKSIGYVMQDVD-YQ 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857580 106 TLSCRENLEVFAGLRgfegeaDGAAGLERrIAELLSMTGLAGFEERQAGKLSGGMKQKLALASALLRIPDLLLLDEPTVG 185
Cdd:cd03226 84 LFTDSVREELLLGLK------ELDAGNEQ-AETVLKDLDLYALKERHPLSLSGGQKQRLAIAAALLSGKDLLIFDEPTSG 156
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 2553857580 186 VDPLSRRELWSVVRRMLADTPMTCVFSTAYLEEAEAADRVLLFESGRII 234
Cdd:cd03226 157 LDYKNMERVGELIRELAAQGKAVIVITHDYEFLAKVCDRVLLLANGAIV 205
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
386-592 |
1.03e-20 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 92.49 E-value: 1.03e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857580 386 SFEVRRGEIFGLLGPNGAGKTTTFRMLCGLLVPSKGQIEVAGYDL--RTAKAgARARIGYVAQK-----FSLygklSVEQ 458
Cdd:PRK13647 25 SLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGREVnaENEKW-VRSKVGLVFQDpddqvFSS----TVWD 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857580 459 NLRYFGRSYGFFGQALQDRIDASLEDFGLTDRRDTTAGSLSFGAKQDLSMACGLIHSPEILFLDEATSGADLASRRAFWR 538
Cdd:PRK13647 100 DVAFGPVNMGLDKDEVERRVEEALKAVRMWDFRDKPPYHLSYGQKKRVAIAGVLAMDPDVIVLDEPMAYLDPRGQETLME 179
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 2553857580 539 RINALASAGTSVVVTTHFLE-EAEYCDRFLIQDAGKVLALGTPREVKQRAAVLSA 592
Cdd:PRK13647 180 ILDRLHNQGKTVIVATHDVDlAAEWADQVIVLKEGRVLAEGDKSLLTDEDIVEQA 234
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
28-245 |
1.07e-20 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 92.56 E-value: 1.07e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857580 28 IRAVDGISLKAGgaeaSDRLIALVGPDGAGKSTFMRLLCGLEAPDEGRLSVLGTT-----------------PDPDNEDF 90
Cdd:PRK13652 17 KEALNNINFIAP----RNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIRGEPitkenirevrkfvglvfQNPDDQIF 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857580 91 TTR----IAFMPQTLGLyktlscrenlevfaglrgfegeadGAAGLERRIAELLSMTGLAGFEERQAGKLSGGMKQKLAL 166
Cdd:PRK13652 93 SPTveqdIAFGPINLGL------------------------DEETVAHRVSSALHMLGLEELRDRVPHHLSGGEKKRVAI 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857580 167 ASALLRIPDLLLLDEPTVGVDPLSRRELWSVVRRMLADTPMTCVFSTAYLE-EAEAADRVLLFESGRIIADENPQSFISR 245
Cdd:PRK13652 149 AGVIAMEPQVLVLDEPTAGLDPQGVKELIDFLNDLPETYGMTVIFSTHQLDlVPEMADYIYVMDKGRIVAYGTVEEIFLQ 228
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
5-251 |
1.27e-20 |
|
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: 95.99 E-value: 1.27e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857580 5 SAPAIRLEGVVKTFPnplDAARPirAVDGISL--KAGgaeasdRLIALVGPDGAGKSTFMRLLCGLEAPDEGRLSVLGT- 81
Cdd:COG4987 330 GGPSLELEDVSFRYP---GAGRP--VLDGLSLtlPPG------ERVAIVGPSGSGKSTLLALLLRFLDPQSGSITLGGVd 398
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857580 82 TPDPDNEDFTTRIAFMPQTLGLYKTlSCRENLEVfaglrgfegeADGAAGlERRIAELLSMTGLAGFEERQAG------- 154
Cdd:COG4987 399 LRDLDEDDLRRRIAVVPQRPHLFDT-TLRENLRL----------ARPDAT-DEELWAALERVGLGDWLAALPDgldtwlg 466
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857580 155 ----KLSGGMKQKLALASALLRIPDLLLLDEPTVGVDPLSRRELWSVVRRMLADtpMTCVFSTAYLEEAEAADRVLLFES 230
Cdd:COG4987 467 eggrRLSGGERRRLALARALLRDAPILLLDEPTEGLDAATEQALLADLLEALAG--RTVLLITHRLAGLERMDRILVLED 544
|
250 260
....*....|....*....|.
gi 2553857580 231 GRIIADENPQSFISRaKGRTY 251
Cdd:COG4987 545 GRIVEQGTHEELLAQ-NGRYR 564
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
49-245 |
1.42e-20 |
|
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding cassette (ABC) protein of the three subunit molybdate ABC transporter. The three proteins of this complex are homologous to proteins of the sulfate ABC transporter. Molybdenum may be used in nitrogenases of nitrogen-fixing bacteria and in molybdopterin cofactors. In some cases, molybdate may be transported by a sulfate transporter rather than by a specific molybdate transporter. [Transport and binding proteins, Anions]
Pssm-ID: 131197 [Multi-domain] Cd Length: 354 Bit Score: 93.64 E-value: 1.42e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857580 49 ALVGPDGAGKSTFMRLLCGLEAPDEGRLSVLGTT-PDPDNEDFTT----RIAFMPQTLGLYKTLSCRENLEVfaGLRgfe 123
Cdd:TIGR02142 27 AIFGRSGSGKTTLIRLIAGLTRPDEGEIVLNGRTlFDSRKGIFLPpekrRIGYVFQEARLFPHLSVRGNLRY--GMK--- 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857580 124 gEADGAaglERRI--AELLSMTGLAGFEERQAGKLSGGMKQKLALASALLRIPDLLLLDEPTVGVDPLSRRELWSVVRRM 201
Cdd:TIGR02142 102 -RARPS---ERRIsfERVIELLGIGHLLGRLPGRLSGGEKQRVAIGRALLSSPRLLLMDEPLAALDDPRKYEILPYLERL 177
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 2553857580 202 LADTPMTCVFSTAYLEE-AEAADRVLLFESGRIIADENPQSFISR 245
Cdd:TIGR02142 178 HAEFGIPILYVSHSLQEvLRLADRVVVLEDGRVAAAGPIAEVWAS 222
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
29-236 |
1.54e-20 |
|
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: 89.42 E-value: 1.54e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857580 29 RAVDGISLKAggaeASDRLIALVGPDGAGKSTFMRLLCGLEAPDEGRLSVLGT-TPDPDNEDFTTRIAFMPQtlglyktl 107
Cdd:cd03214 13 TVLDDLSLSI----EAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDGKdLASLSPKELARKIAYVPQ-------- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857580 108 screnlevfaglrgfegeadgaaglerriaeLLSMTGLAGFEERQAGKLSGGMKQKLALASALLRIPDLLLLDEPTVGVD 187
Cdd:cd03214 81 -------------------------------ALELLGLAHLADRPFNELSGGERQRVLLARALAQEPPILLLDEPTSHLD 129
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 2553857580 188 PLSRRELWSVVRRMLADTPMTCVFSTAYLEEAEA-ADRVLLFESGRIIAD 236
Cdd:cd03214 130 IAHQIELLELLRRLARERGKTVVMVLHDLNLAARyADRVILLKDGRIVAQ 179
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
7-258 |
1.88e-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: 96.62 E-value: 1.88e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857580 7 PAIRLEGVVKTFPnplDAARPirAVDGISLKAggaeASDRLIALVGPDGAGKSTFMRLLCGLEAPDEGRLSVLGTTPDPD 86
Cdd:TIGR01257 927 PGVCVKNLVKIFE---PSGRP--AVDRLNITF----YENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGKDIETN 997
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857580 87 NEDFTTRIAFMPQTLGLYKTLSCRENLEVFAGLRGFEGEAdgaAGLErrIAELLSMTGLAGFEERQAGKLSGGMKQKLAL 166
Cdd:TIGR01257 998 LDAVRQSLGMCPQHNILFHHLTVAEHILFYAQLKGRSWEE---AQLE--MEAMLEDTGLHHKRNEEAQDLSGGMQRKLSV 1072
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857580 167 ASALLRIPDLLLLDEPTVGVDPLSRRELWSVVRRMLADTpmTCVFSTAYLEEAEA-ADRVLLFESGRIIADENPQsFISR 245
Cdd:TIGR01257 1073 AIAFVGDAKVVVLDEPTSGVDPYSRRSIWDLLLKYRSGR--TIIMSTHHMDEADLlGDRIAIISQGRLYCSGTPL-FLKN 1149
|
250
....*....|...
gi 2553857580 246 AKGRTYLLPLANR 258
Cdd:TIGR01257 1150 CFGTGFYLTLVRK 1162
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
367-593 |
1.90e-20 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 90.91 E-value: 1.90e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857580 367 IRADGIARKFGNFVAVADTSFEVRRGEIFGLLGPNGAGKTTTFRMLCGLLVPSKGQIEVAGYDLRTAKAGARARIgyVA- 445
Cdd:COG4604 2 IEIKNVSKRYGGKVVLDDVSLTIPKGGITALIGPNGAGKSTLLSMISRLLPPDSGEVLVDGLDVATTPSRELAKR--LAi 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857580 446 --QKFSLYGKLSVEQnLRYFGR---SYGFFGQALQDRIDASLEDFGLTDRRDTTAGSLSFGAKQDLSMACGLIHSPEILF 520
Cdd:COG4604 80 lrQENHINSRLTVRE-LVAFGRfpySKGRLTAEDREIIDEAIAYLDLEDLADRYLDELSGGQRQRAFIAMVLAQDTDYVL 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2553857580 521 LDEATSGADLASRRAFWRRINALA-SAGTSVVVTTH---FleEAEYCDRFLIQDAGKVLALGTPREVKQrAAVLSAV 593
Cdd:COG4604 159 LDEPLNNLDMKHSVQMMKLLRRLAdELGKTVVIVLHdinF--ASCYADHIVAMKDGRVVAQGTPEEIIT-PEVLSDI 232
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
380-593 |
2.04e-20 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 92.03 E-value: 2.04e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857580 380 VAVADTSFEVRRGEIFGLLGPNGAGKTTTFRMLCGLLVPSKGQIEVAGYDLRTAKAGA---RARIGYVAQ--KFSLYGKl 454
Cdd:PRK13637 21 KALDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDGVDITDKKVKLsdiRKKVGLVFQypEYQLFEE- 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857580 455 SVEQNLRYFGRSYGFFGQALQDRIDASLEDFGLT--DRRDTTAGSLSFGAKQDLSMACGLIHSPEILFLDEATSGADLAS 532
Cdd:PRK13637 100 TIEKDIAFGPINLGLSEEEIENRVKRAMNIVGLDyeDYKDKSPFELSGGQKRRVAIAGVVAMEPKILILDEPTAGLDPKG 179
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2553857580 533 RRAFWRRINALASA-GTSVVVTTHFLEE-AEYCDRFLIQDAGKVLALGTPREVKQRAAVLSAV 593
Cdd:PRK13637 180 RDEILNKIKELHKEyNMTIILVSHSMEDvAKLADRIIVMNKGKCELQGTPREVFKEVETLESI 242
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
367-616 |
2.18e-20 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 92.88 E-value: 2.18e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857580 367 IRADGIARKFGNFVAVADTSFEVRRGEIFGLLGPNGAGKTTTfRMLCGLLVPSKGQIEVAGYDLRTAKAGARARIG-YVA 445
Cdd:NF000106 14 VEVRGLVKHFGEVKAVDGVDLDVREGTVLGVLGP*GAA**RG-ALPAHV*GPDAGRRPWRF*TWCANRRALRRTIG*HRP 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857580 446 QKFSLYGKLSVEQNLRYFGRSYGFFGQALQDRIDASLEDFGLTDRRDTTAGSLSFGAKQDLSMACGLIHSPEILFLDEAT 525
Cdd:NF000106 93 VR*GRRESFSGRENLYMIGR*LDLSRKDARARADELLERFSLTEAAGRAAAKYSGGMRRRLDLAASMIGRPAVLYLDEPT 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857580 526 SGADLASRRAFWRRINALASAGTSVVVTTHFLEEAE-YCDRFLIQDAGKVLALGTPREVKQRAA--VLSAVSGQSLVVDR 602
Cdd:NF000106 173 TGLDPRTRNEVWDEVRSMVRDGATVLLTTQYMEEAEqLAHELTVIDRGRVIADGKVDELKTKVGgrTLQIRPAHAAELDR 252
|
250
....*....|....
gi 2553857580 603 MsiedaFVAIVEAG 616
Cdd:NF000106 253 M-----VGAIAQAG 261
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
9-232 |
2.46e-20 |
|
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: 88.59 E-value: 2.46e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857580 9 IRLEGVVKTFPNpldaaRPIRAVDGISL--KAGgaeasdRLIALVGPDGAGKSTFMRLLCGLEAPDEGRLSVLGT-TPDP 85
Cdd:cd03228 1 IEFKNVSFSYPG-----RPKPVLKDVSLtiKPG------EKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGVdLRDL 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857580 86 DNEDFTTRIAFMPQTLGLYKTlSCRENLevfaglrgfegeadgaaglerriaellsmtglagfeerqagkLSGGMKQKLA 165
Cdd:cd03228 70 DLESLRKNIAYVPQDPFLFSG-TIRENI------------------------------------------LSGGQRQRIA 106
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2553857580 166 LASALLRIPDLLLLDEPTVGVDPLSRRELWSVVRRMLADtpMTCVFSTAYLEEAEAADRVLLFESGR 232
Cdd:cd03228 107 IARALLRDPPILILDEATSALDPETEALILEALRALAKG--KTVIVIAHRLSTIRDADRIIVLDDGR 171
|
|
| BtuD |
COG4138 |
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ... |
386-593 |
2.58e-20 |
|
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism];
Pssm-ID: 443313 [Multi-domain] Cd Length: 248 Bit Score: 90.67 E-value: 2.58e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857580 386 SFEVRRGEIFGLLGPNGAGKTTTFRMLCGLLvPSKGQIEVAGYDLRTAKAGARARI-GYVAQKFSLYGKLSVEQNLRYFG 464
Cdd:COG4138 16 SAQVNAGELIHLIGPNGAGKSTLLARMAGLL-PGQGEILLNGRPLSDWSAAELARHrAYLSQQQSPPFAMPVFQYLALHQ 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857580 465 RSyGFFGQALQDRIDASLEDFGLTDRRDTTAGSLSFGAKQDLSMACGL--IHsPEI------LFLDEATSGADLASRRAF 536
Cdd:COG4138 95 PA-GASSEAVEQLLAQLAEALGLEDKLSRPLTQLSGGEWQRVRLAAVLlqVW-PTInpegqlLLLDEPMNSLDVAQQAAL 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 2553857580 537 WRRINALASAGTSVVVTTHFLEEA-EYCDRFLIQDAGKVLALGTPREVKQrAAVLSAV 593
Cdd:COG4138 173 DRLLRELCQQGITVVMSSHDLNHTlRHADRVWLLKQGKLVASGETAEVMT-PENLSEV 229
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
367-583 |
2.59e-20 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 93.37 E-value: 2.59e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857580 367 IRADGIARKFGNFVAVADTSFEVRRGEIFGLLGPNGAGKTTTFRMLCGLLVPSKGQIEVAGYDLRTAKAGARAR-IGYVA 445
Cdd:PRK09536 4 IDVSDLSVEFGDTTVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGDDVEALSARAASRrVASVP 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857580 446 QKFSLYGKLSVEQNLRyFGRS-----YGFFGQALQDRIDASLEDFGLTDRRDTTAGSLSFGAKQDLSMACGLIHSPEILF 520
Cdd:PRK09536 84 QDTSLSFEFDVRQVVE-MGRTphrsrFDTWTETDRAAVERAMERTGVAQFADRPVTSLSGGERQRVLLARALAQATPVLL 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2553857580 521 LDEATSGADLASRRAFWRRINALASAGTSVVVTTHFLE-EAEYCDRFLIQDAGKVLALGTPREV 583
Cdd:PRK09536 163 LDEPTASLDINHQVRTLELVRRLVDDGKTAVAAIHDLDlAARYCDELVLLADGRVRAAGPPADV 226
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
9-237 |
3.53e-20 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 89.73 E-value: 3.53e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857580 9 IRLEGVVKTFPNPldaarpIRAVDGISLKaggaeasdrlIA------LVGPDGAGKSTFMRLLCGLEAPDEGRLSVLGtt 82
Cdd:COG2884 2 IRFENVSKRYPGG------REALSDVSLE----------IEkgefvfLTGPSGAGKSTLLKLLYGEERPTSGQVLVNG-- 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857580 83 pdpdnEDFTT----RIAFMPQTLG-------LYKTLSCRENLEvFAgLR--GFEGEAdgaagLERRIAELLSMTGLAGFE 149
Cdd:COG2884 64 -----QDLSRlkrrEIPYLRRRIGvvfqdfrLLPDRTVYENVA-LP-LRvtGKSRKE-----IRRRVREVLDLVGLSDKA 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857580 150 ERQAGKLSGGMKQKLALASALLRIPDLLLLDEPTVGVDPLSRRELWSVVRRmLADTPMTCVFSTAYLEEAEAAD-RVLLF 228
Cdd:COG2884 132 KALPHELSGGEQQRVAIARALVNRPELLLADEPTGNLDPETSWEIMELLEE-INRRGTTVLIATHDLELVDRMPkRVLEL 210
|
....*....
gi 2553857580 229 ESGRIIADE 237
Cdd:COG2884 211 EDGRLVRDE 219
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
27-236 |
3.60e-20 |
|
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: 90.04 E-value: 3.60e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857580 27 PIRAVDGISLKAGGAEasdrLIALVGPDGAGKSTFMRLLCGLEAPDEGRLSVLGttpdpdnEDFTTR---------IAFM 97
Cdd:COG0410 15 GIHVLHGVSLEVEEGE----IVALLGRNGAGKTTLLKAISGLLPPRSGSIRFDG-------EDITGLpphriarlgIGYV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857580 98 PQTLGLYKTLSCRENLEVFAGLRGfeGEADGAAGLER------RIAELLSmtglagfeeRQAGKLSGGMKQKLALASALL 171
Cdd:COG0410 84 PEGRRIFPSLTVEENLLLGAYARR--DRAEVRADLERvyelfpRLKERRR---------QRAGTLSGGEQQMLAIGRALM 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2553857580 172 RIPDLLLLDEPTVGVDPLSRRELWSVVRRmLADTPMTCVFSTAYLEEA-EAADRVLLFESGRIIAD 236
Cdd:COG0410 153 SRPKLLLLDEPSLGLAPLIVEEIFEIIRR-LNREGVTILLVEQNARFAlEIADRAYVLERGRIVLE 217
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
9-234 |
4.92e-20 |
|
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: 89.10 E-value: 4.92e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857580 9 IRLEGVVKTFPNPldaARPIRAVDGISL--KAGgaeasdRLIALVGPDGAGKSTFMRLLCGLEAPDEGRLSVLGT----T 82
Cdd:cd03257 2 LEVKNLSVSFPTG---GGSVKALDDVSFsiKKG------ETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGKdllkL 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857580 83 PDPDNEDFTTRIAFMPQ--TLGLYKTLSCRENLEvfAGLRgFEGEADGAAGLERRIAELLSMTGL-AGFEERQAGKLSGG 159
Cdd:cd03257 73 SRRLRKIRRKEIQMVFQdpMSSLNPRMTIGEQIA--EPLR-IHGKLSKKEARKEAVLLLLVGVGLpEEVLNRYPHELSGG 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857580 160 MKQKLALASALLRIPDLLLLDEPTVGVDPLSRRELWSVVRRMLADTPMTCVFST------AYLeeaeaADRVLLFESGRI 233
Cdd:cd03257 150 QRQRVAIARALALNPKLLIADEPTSALDVSVQAQILDLLKKLQEELGLTLLFIThdlgvvAKI-----ADRVAVMYAGKI 224
|
.
gi 2553857580 234 I 234
Cdd:cd03257 225 V 225
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
1-237 |
1.48e-19 |
|
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase component [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 443338 [Multi-domain] Cd Length: 233 Bit Score: 87.87 E-value: 1.48e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857580 1 MTKASAPAIRLEGVVKTFPnplDAARPIRAVDGISLKAGGAEAsdrlIALVGPDGAGKSTFMRLLCGLEAPDEGRLSVLG 80
Cdd:COG4181 1 MSSSSAPIIELRGLTKTVG---TGAGELTILKGISLEVEAGES----VAIVGASGSGKSTLLGLLAGLDRPTSGTVRLAG 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857580 81 TTPDPDNEDFTTR-----IAFMPQTLGLYKTLSCRENLEVFAGLRGfEGEADGAAglerriAELLSMTGLAGFEERQAGK 155
Cdd:COG4181 74 QDLFALDEDARARlrarhVGFVFQSFQLLPTLTALENVMLPLELAG-RRDARARA------RALLERVGLGHRLDHYPAQ 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857580 156 LSGGMKQKLALASALLRIPDLLLLDEPTVGVDPLSRRELWSVVRRMLADTPMTCVFSTAYLEEAEAADRVLLFESGRIIA 235
Cdd:COG4181 147 LSGGEQQRVALARAFATEPAILFADEPTGNLDAATGEQIIDLLFELNRERGTTLVLVTHDPALAARCDRVLRLRAGRLVE 226
|
..
gi 2553857580 236 DE 237
Cdd:COG4181 227 DT 228
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
9-240 |
1.74e-19 |
|
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: 88.85 E-value: 1.74e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857580 9 IRLEGVVKTFPNpldaaRPIRAVDGISLKAGGAE---ASDRLIA---------------LVGPDGAGKSTFMRLLCGLEA 70
Cdd:cd03294 1 IKIKGLYKIFGK-----NPQKAFKLLAKGKSKEEilkKTGQTVGvndvsldvregeifvIMGLSGSGKSTLLRCINRLIE 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857580 71 PDEGRLSVlgttpdpDNEDFTT------------RIAFMPQTLGLYKTLSCRENLEVfaglrGFEGEADGAAGLERRIAE 138
Cdd:cd03294 76 PTSGKVLI-------DGQDIAAmsrkelrelrrkKISMVFQSFALLPHRTVLENVAF-----GLEVQGVPRAEREERAAE 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857580 139 LLSMTGLAGFEERQAGKLSGGMKQKLALASALLRIPDLLLLDEPTVGVDPLSRRELWSVVRRMLADTPMTCVFSTAYLEE 218
Cdd:cd03294 144 ALELVGLEGWEHKYPDELSGGMQQRVGLARALAVDPDILLMDEAFSALDPLIRREMQDELLRLQAELQKTIVFITHDLDE 223
|
250 260
....*....|....*....|...
gi 2553857580 219 A-EAADRVLLFESGRIIADENPQ 240
Cdd:cd03294 224 AlRLGDRIAIMKDGRLVQVGTPE 246
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
8-236 |
1.96e-19 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 89.76 E-value: 1.96e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857580 8 AIRLEGVVKTFPNP-----LDAA---------RPIRAVDGISLKAGGAEasdrLIALVGPDGAGKSTFMRLLCGLEAPDE 73
Cdd:COG4586 1 IIEVENLSKTYRVYekepgLKGAlkglfrreyREVEAVDDISFTIEPGE----IVGFIGPNGAGKSTTIKMLTGILVPTS 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857580 74 GRLSVLGTTPDPDNEDFTTRIAF-MPQtlglyKT-----LSCRENLEVFAGLRGFEgeadgAAGLERRIAELLSMTGLAG 147
Cdd:COG4586 77 GEVRVLGYVPFKRRKEFARRIGVvFGQ-----RSqlwwdLPAIDSFRLLKAIYRIP-----DAEYKKRLDELVELLDLGE 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857580 148 FEERQAGKLSGG--MKQKLALAsallripdllllDEPTVGVDPLSRRELWSVVRRMLADTPMTCVFSTAYLEEAEA-ADR 224
Cdd:COG4586 147 LLDTPVRQLSLGqrMRCELAAAllhrp--kilflDEPTIGLDVVSKEAIREFLKEYNRERGTTILLTSHDMDDIEAlCDR 224
|
250
....*....|..
gi 2553857580 225 VLLFESGRIIAD 236
Cdd:COG4586 225 VIVIDHGRIIYD 236
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
362-590 |
2.18e-19 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 90.39 E-value: 2.18e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857580 362 ERPVVIRADGIARKFGNFVAVADTSFEVRRGEIFGLLGPNGAGKTTTFRMLCGLLVPSKGQIEVAGYDLRTAKAGARaRI 441
Cdd:PRK09452 10 SLSPLVELRGISKSFDGKEVISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLDGQDITHVPAENR-HV 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857580 442 GYVAQKFSLYGKLSVEQNLRYFGRSYGFFGQALQDRI-DA----SLEDFGltDRRDTtagSLSFGAKQDLSMACGLIHSP 516
Cdd:PRK09452 89 NTVFQSYALFPHMTVFENVAFGLRMQKTPAAEITPRVmEAlrmvQLEEFA--QRKPH---QLSGGQQQRVAIARAVVNKP 163
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2553857580 517 EILFLDEATSGADLASRRAFWRRINALA-SAGTSVVVTTHFLEEA-EYCDRFLIQDAGKVLALGTPREVKQRAAVL 590
Cdd:PRK09452 164 KVLLLDESLSALDYKLRKQMQNELKALQrKLGITFVFVTHDQEEAlTMSDRIVVMRDGRIEQDGTPREIYEEPKNL 239
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
48-245 |
2.30e-19 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 88.64 E-value: 2.30e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857580 48 IALVGPDGAGKSTFMRLLCGLEAPDEGRLSVLGTTPDPDNE-DFTTRIAFMPQTlglyktlscRENLEVFAGLrgfegEA 126
Cdd:PRK13650 36 LSIIGHNGSGKSTTVRLIDGLLEAESGQIIIDGDLLTEENVwDIRHKIGMVFQN---------PDNQFVGATV-----ED 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857580 127 DGAAGLE----------RRIAELLSMTGLAGFEERQAGKLSGGMKQKLALASALLRIPDLLLLDEPTVGVDPLSRRELWS 196
Cdd:PRK13650 102 DVAFGLEnkgipheemkERVNEALELVGMQDFKEREPARLSGGQKQRVAIAGAVAMRPKIIILDEATSMLDPEGRLELIK 181
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 2553857580 197 VVRRMLADTPMTCVFSTAYLEEAEAADRVLLFESGRIIADENPQSFISR 245
Cdd:PRK13650 182 TIKGIRDDYQMTVISITHDLDEVALSDRVLVMKNGQVESTSTPRELFSR 230
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
48-233 |
3.29e-19 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 86.41 E-value: 3.29e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857580 48 IALVGPDGAGKSTFMRLLCGLEAPDEGRLSVLG---TTPDPdnEDFTTRIAFMPQTLGLYKTlSCRENLEVFAGLRGFEG 124
Cdd:COG4619 29 VAITGPSGSGKSTLLRALADLDPPTSGEIYLDGkplSAMPP--PEWRRQVAYVPQEPALWGG-TVRDNLPFPFQLRERKF 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857580 125 EADgaaglerRIAELLSMTGL-AGFEERQAGKLSGGMKQKLALASALLRIPDLLLLDEPTVGVDPLSRRELWSVVRRMLA 203
Cdd:COG4619 106 DRE-------RALELLERLGLpPDILDKPVERLSGGERQRLALIRALLLQPDVLLLDEPTSALDPENTRRVEELLREYLA 178
|
170 180 190
....*....|....*....|....*....|.
gi 2553857580 204 DTPMTCVFSTAYLEEAEA-ADRVLLFESGRI 233
Cdd:COG4619 179 EEGRAVLWVSHDPEQIERvADRVLTLEAGRL 209
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
367-560 |
3.97e-19 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 86.99 E-value: 3.97e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857580 367 IRADGIARKFGNFVAVADTSFEVRRGEIFGLLGPNGAGKTTTFRMLCGLLVPSKGQIEVAG--YDLRT---AKAGARAR- 440
Cdd:PRK11124 3 IQLNGINCFYGAHQALFDITLDCPQGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLNIAGnhFDFSKtpsDKAIRELRr 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857580 441 -IGYVAQKFSLYGKLSVEQNL-----RYFGRSygffGQALQDRIDASLEDFGLTDRRDTTAGSLSFGAKQDLSMACGLIH 514
Cdd:PRK11124 83 nVGMVFQQYNLWPHLTVQQNLieapcRVLGLS----KDQALARAEKLLERLRLKPYADRFPLHLSGGQQQRVAIARALMM 158
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 2553857580 515 SPEILFLDEATSGADLASRRAFWRRINALASAGTSVVVTTHFLEEA 560
Cdd:PRK11124 159 EPQVLLFDEPTAALDPEITAQIVSIIRELAETGITQVIVTHEVEVA 204
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
384-583 |
4.24e-19 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 87.96 E-value: 4.24e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857580 384 DTSFEVRRGEIFGLLGPNGAGKTTTFRMLCGLLVPSKGQIEVAGYDLrTAKAGA------RARIGYVAQ--KFSLYGKlS 455
Cdd:PRK13641 25 NISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITIAGYHI-TPETGNknlkklRKKVSLVFQfpEAQLFEN-T 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857580 456 VEQNLRYFGRSYGFFGQALQDRIDASLEDFGL-TDRRDTTAGSLSFGAKQDLSMACGLIHSPEILFLDEATSGADLASRR 534
Cdd:PRK13641 103 VLKDVEFGPKNFGFSEDEAKEKALKWLKKVGLsEDLISKSPFELSGGQMRRVAIAGVMAYEPEILCLDEPAAGLDPEGRK 182
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 2553857580 535 AFWRRINALASAGTSVVVTTHFLEE-AEYCDRFLIQDAGKVLALGTPREV 583
Cdd:PRK13641 183 EMMQLFKDYQKAGHTVILVTHNMDDvAEYADDVLVLEHGKLIKHASPKEI 232
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
9-252 |
4.94e-19 |
|
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: 86.44 E-value: 4.94e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857580 9 IRLEGVVKTFpnpldAARPIraVDGISLKAGGAEAsdrlIALVGPDGAGKSTFMRLLCGLEAPDEGRLSVlgttpdpDNE 88
Cdd:cd03218 1 LRAENLSKRY-----GKRKV--VNGVSLSVKQGEI----VGLLGPNGAGKTTTFYMIVGLVKPDSGKILL-------DGQ 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857580 89 DFTT-----R----IAFMPQTLGLYKTLSCRENLEVFAGLRGfegeaDGAAGLERRIAELLSMTGLAGFEERQAGKLSGG 159
Cdd:cd03218 63 DITKlpmhkRarlgIGYLPQEASIFRKLTVEENILAVLEIRG-----LSKKEREEKLEELLEEFHITHLRKSKASSLSGG 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857580 160 MKQKLALASALLRIPDLLLLDEPTVGVDPLSRRELWSVVRRmLADTPMTcVFST--AYLEEAEAADRVLLFESGRIIADE 237
Cdd:cd03218 138 ERRRVEIARALATNPKFLLLDEPFAGVDPIAVQDIQKIIKI-LKDRGIG-VLITdhNVRETLSITDRAYIIYEGKVLAEG 215
|
250
....*....|....*.
gi 2553857580 238 NPQSFISRAKGR-TYL 252
Cdd:cd03218 216 TPEEIAANELVRkVYL 231
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
7-253 |
6.16e-19 |
|
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: 91.05 E-value: 6.16e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857580 7 PAIRLEGVVKTFPnplDAARPIraVDGISLKAggaEASDRlIALVGPDGAGKSTFMRLLCGLEAPDEGRLSVLGTtpDP- 85
Cdd:COG2274 472 GDIELENVSFRYP---GDSPPV--LDNISLTI---KPGER-VAIVGRSGSGKSTLLKLLLGLYEPTSGRILIDGI--DLr 540
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857580 86 --DNEDFTTRIAFMPQTLGLYK-TLscRENLevfaglRGFEGEADgaaglERRIAELLSMTGLAGF------------EE 150
Cdd:COG2274 541 qiDPASLRRQIGVVLQDVFLFSgTI--RENI------TLGDPDAT-----DEEIIEAARLAGLHDFiealpmgydtvvGE 607
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857580 151 RQAGkLSGGMKQKLALASALLRIPDLLLLDEPTVGVDPLSRRELWSVVRRMLADtpMTCVFSTAYLEEAEAADRVLLFES 230
Cdd:COG2274 608 GGSN-LSGGQRQRLAIARALLRNPRILILDEATSALDAETEAIILENLRRLLKG--RTVIIIAHRLSTIRLADRIIVLDK 684
|
250 260
....*....|....*....|...
gi 2553857580 231 GRIIADENPQSFISRaKGRTYLL 253
Cdd:COG2274 685 GRIVEDGTHEELLAR-KGLYAEL 706
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
9-247 |
6.85e-19 |
|
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440743 [Multi-domain] Cd Length: 239 Bit Score: 86.20 E-value: 6.85e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857580 9 IRLEGVVKTFPNpldaarpIRAVDGISL--KAGgaeasdRLIALVGPDGAGKSTFMRLLCGLEAPDEGRLSVLGTTPDPD 86
Cdd:COG1126 2 IEIENLHKSFGD-------LEVLKGISLdvEKG------EVVVIIGPSGSGKSTLLRCINLLEEPDSGTITVDGEDLTDS 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857580 87 NEDFT---TRIAFMPQTLGLYKTLSCRENLEVfaGLRGFEGEADGAAglERRIAELLSMTGLAGFEERQAGKLSGGMKQK 163
Cdd:COG1126 69 KKDINklrRKVGMVFQQFNLFPHLTVLENVTL--APIKVKKMSKAEA--EERAMELLERVGLADKADAYPAQLSGGQQQR 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857580 164 LALASALLRIPDLLLLDEPTVGVDPLSRRELWSVVRRmLADTPMTCVFST-----AyleeAEAADRVLLFESGRIIADEN 238
Cdd:COG1126 145 VAIARALAMEPKVMLFDEPTSALDPELVGEVLDVMRD-LAKEGMTMVVVThemgfA----REVADRVVFMDGGRIVEEGP 219
|
....*....
gi 2553857580 239 PQSFISRAK 247
Cdd:COG1126 220 PEEFFENPQ 228
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
47-240 |
6.87e-19 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 88.62 E-value: 6.87e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857580 47 LIALVGPDGAGKSTFMRLLCGLEAPDEGRLSVlgttpdpDNEDFTTR------IAFMPQTLGLYKTLSCRENleVFAGLR 120
Cdd:PRK11432 34 MVTLLGPSGCGKTTVLRLVAGLEKPTEGQIFI-------DGEDVTHRsiqqrdICMVFQSYALFPHMSLGEN--VGYGLK 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857580 121 gfegeADGAAGLER--RIAELLSMTGLAGFEERQAGKLSGGMKQKLALASALLRIPDLLLLDEPTVGVDPLSRRELWSVV 198
Cdd:PRK11432 105 -----MLGVPKEERkqRVKEALELVDLAGFEDRYVDQISGGQQQRVALARALILKPKVLLFDEPLSNLDANLRRSMREKI 179
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 2553857580 199 RRMLADTPMTCVFSTAYLEEAEA-ADRVLLFESGRIIADENPQ 240
Cdd:PRK11432 180 RELQQQFNITSLYVTHDQSEAFAvSDTVIVMNKGKIMQIGSPQ 222
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
386-555 |
7.26e-19 |
|
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the bacterial CcmAB transporter. The CCM family is involved in bacterial cytochrome c biogenesis. Cytochrome c maturation in E. coli requires the ccm operon, which encodes eight membrane proteins (CcmABCDEFGH). CcmE is a periplasmic heme chaperon that binds heme covalently and transfers it onto apocytochrome c in the presence of CcmF, CcmG, and CcmH. The CcmAB proteins represent an ABC transporter and the CcmCD proteins participate in heme transfer to CcmE.
Pssm-ID: 213198 [Multi-domain] Cd Length: 201 Bit Score: 85.24 E-value: 7.26e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857580 386 SFEVRRGEIFGLLGPNGAGKTTTFRMLCGLLVPSKGQIEVAGYDLRTAKAGARARIGYVAQKFSLYGKLSVEQNLRYFGR 465
Cdd:cd03231 20 SFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNGGPLDFQRDSIARGLLYLGHAPGIKTTLSVLENLRFWHA 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857580 466 SYGffgqalQDRIDASLEDFGLTDRRDTTAGSLSFGAKQDLSMACGLIHSPEILFLDEATSGADLASRRAFWRRINALAS 545
Cdd:cd03231 100 DHS------DEQVEEALARVGLNGFEDRPVAQLSAGQQRRVALARLLLSGRPLWILDEPTTALDKAGVARFAEAMAGHCA 173
|
170
....*....|
gi 2553857580 546 AGTSVVVTTH 555
Cdd:cd03231 174 RGGMVVLTTH 183
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
381-586 |
1.06e-18 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 90.02 E-value: 1.06e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857580 381 AVADTSFEVRRGEIFGLLGPNGAGKTTTFRMLCGLLVPSKGQIEVAGYDLRT-AKAGARARIGYVAQKFSLYGKlSVEQN 459
Cdd:PRK13657 350 GVEDVSFEAKPGQTVAIVGPTGAGKSTLINLLQRVFDPQSGRILIDGTDIRTvTRASLRRNIAVVFQDAGLFNR-SIEDN 428
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857580 460 LRyFGRSygffgQALQDRIDASLE-----DFGLT--DRRDTTAG----SLSFGAKQDLSMACGLIHSPEILFLDEATSGA 528
Cdd:PRK13657 429 IR-VGRP-----DATDEEMRAAAEraqahDFIERkpDGYDTVVGergrQLSGGERQRLAIARALLKDPPILILDEATSAL 502
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 2553857580 529 DLASRRAFWRRINALASAGTSVVVtTHFLEEAEYCDRFLIQDAGKVLALGTPREVKQR 586
Cdd:PRK13657 503 DVETEAKVKAALDELMKGRTTFII-AHRLSTVRNADRILVFDNGRVVESGSFDELVAR 559
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
366-582 |
1.11e-18 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 86.22 E-value: 1.11e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857580 366 VIRADGIARKFGNFVAVADTSFEVRRGEIFGLLGPNGAGKTTTFRMLCGLLVPSK---GQIEVAGYDLRTAKAGA----- 437
Cdd:PRK09984 4 IIRVEKLAKTFNQHQALHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGLITGDKsagSHIELLGRTVQREGRLArdirk 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857580 438 -RARIGYVAQKFSLYGKLSVEQNLRY-------FGRS-YGFFGQALQDRIDASLEDFGLTDRRDTTAGSLSFGAKQDLSM 508
Cdd:PRK09984 84 sRANTGYIFQQFNLVNRLSVLENVLIgalgstpFWRTcFSWFTREQKQRALQALTRVGMVHFAHQRVSTLSGGQQQRVAI 163
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2553857580 509 ACGLIHSPEILFLDEATSGADLASRRAFW---RRINalASAGTSVVVTTHFLEEA-EYCDRFLIQDAGKVLALGTPRE 582
Cdd:PRK09984 164 ARALMQQAKVILADEPIASLDPESARIVMdtlRDIN--QNDGITVVVTLHQVDYAlRYCERIVALRQGHVFYDGSSQQ 239
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
381-583 |
1.32e-18 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 86.20 E-value: 1.32e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857580 381 AVADTSFEVRRGEIFGLLGPNGAGKTTTFRMLCGLLVPSKGQIEVAGYDL-RTAKAGARARIGYVAQ----KFslYGkLS 455
Cdd:PRK13632 24 ALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIDGITIsKENLKEIRKKIGIIFQnpdnQF--IG-AT 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857580 456 VEQNLRyfgrsygfFG--------QALQDRIDASLEDFGLTDRRDTTAGSLSFGAKQDLSMACGLIHSPEILFLDEATSG 527
Cdd:PRK13632 101 VEDDIA--------FGlenkkvppKKMKDIIDDLAKKVGMEDYLDKEPQNLSGGQKQRVAIASVLALNPEIIIFDESTSM 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 2553857580 528 ADLASRRAFWRRINALASAGTSVVVT-THFLEEAEYCDRFLIQDAGKVLALGTPREV 583
Cdd:PRK13632 173 LDPKGKREIKKIMVDLRKTRKKTLISiTHDMDEAILADKVIVFSEGKLIAQGKPKEI 229
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
386-583 |
1.51e-18 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 86.30 E-value: 1.51e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857580 386 SFEVRRGEIFGLLGPNGAGKTTTFRMLCGLLVPSKGQIEVAGYDLRTAKA-GARARIGYVAQK-FSLYGKLSVEQNLRYF 463
Cdd:PRK13642 27 SFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDGELLTAENVwNLRRKIGMVFQNpDNQFVGATVEDDVAFG 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857580 464 GRSYGFFGQALQDRIDASLEDFGLTDRRDTTAGSLSFGAKQDLSMACGLIHSPEILFLDEATSGADLASRRAFWRRINAL 543
Cdd:PRK13642 107 MENQGIPREEMIKRVDEALLAVNMLDFKTREPARLSGGQKQRVAVAGIIALRPEIIILDESTSMLDPTGRQEIMRVIHEI 186
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 2553857580 544 ASA-GTSVVVTTHFLEEAEYCDRFLIQDAGKVLALGTPREV 583
Cdd:PRK13642 187 KEKyQLTVLSITHDLDEAASSDRILVMKAGEIIKEAAPSEL 227
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
381-592 |
1.55e-18 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 86.33 E-value: 1.55e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857580 381 AVADTSFEVRRGEIFGLLGPNGAGKTTTFRMLCGLLVPSKGQIEVAGYDLRTAKAG-----ARARIGYVAQ--KFSLYGK 453
Cdd:PRK13643 21 ALFDIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVTVGDIVVSSTSKQkeikpVRKKVGVVFQfpESQLFEE 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857580 454 lSVEQNLRYFGRSYGFFGQALQDRIDASLEDFGLTDR-RDTTAGSLSFGAKQDLSMACGLIHSPEILFLDEATSGADLAS 532
Cdd:PRK13643 101 -TVLKDVAFGPQNFGIPKEKAEKIAAEKLEMVGLADEfWEKSPFELSGGQMRRVAIAGILAMEPEVLVLDEPTAGLDPKA 179
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2553857580 533 RRAFWRRINALASAGTSVVVTTHFLEE-AEYCDRFLIQDAGKVLALGTPREVKQRAAVLSA 592
Cdd:PRK13643 180 RIEMMQLFESIHQSGQTVVLVTHLMDDvADYADYVYLLEKGHIISCGTPSDVFQEVDFLKA 240
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
8-245 |
1.90e-18 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 86.01 E-value: 1.90e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857580 8 AIRLEGVVKTFPnplDAARPirAVDGISLKAggaeASDRLIALVGPDGAGKSTFMRLLCGLEAPDE---GRLSVLGTTPD 84
Cdd:PRK13640 5 IVEFKHVSFTYP---DSKKP--ALNDISFSI----PRGSWTALIGHNGSGKSTISKLINGLLLPDDnpnSKITVDGITLT 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857580 85 PDNE-DFTTRIAFMPQTlglyktlscRENLEVFAGLrgfegEADGAAGLERR----------IAELLSMTGLAGFEERQA 153
Cdd:PRK13640 76 AKTVwDIREKVGIVFQN---------PDNQFVGATV-----GDDVAFGLENRavprpemikiVRDVLADVGMLDYIDSEP 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857580 154 GKLSGGMKQKLALASALLRIPDLLLLDEPTVGVDPLSRRELWSVVRRMLADTPMTCVFSTAYLEEAEAADRVLLFESGRI 233
Cdd:PRK13640 142 ANLSGGQKQRVAIAGILAVEPKIIILDESTSMLDPAGKEQILKLIRKLKKKNNLTVISITHDIDEANMADQVLVLDDGKL 221
|
250
....*....|..
gi 2553857580 234 IADENPQSFISR 245
Cdd:PRK13640 222 LAQGSPVEIFSK 233
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
9-234 |
2.29e-18 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 86.67 E-value: 2.29e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857580 9 IRLEGVVKTFPNpldAARPIRAVDGISLKAGGAEasdrlI-ALVGPDGAGKSTFMRLLCGLEAPDEGRLSVlgttpdpDN 87
Cdd:COG1135 2 IELENLSKTFPT---KGGPVTALDDVSLTIEKGE-----IfGIIGYSGAGKSTLIRCINLLERPTSGSVLV-------DG 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857580 88 EDFTT-----------RIAFMPQTLGLYKTLSCREN----LEVfAGLrgfegeadGAAGLERRIAELLSMTGLAGFEERQ 152
Cdd:COG1135 67 VDLTAlserelraarrKIGMIFQHFNLLSSRTVAENvalpLEI-AGV--------PKAEIRKRVAELLELVGLSDKADAY 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857580 153 AGKLSGGMKQKL----ALAS------AllripdllllDEPTVGVDP------LS-----RREL----------WSVVRRm 201
Cdd:COG1135 138 PSQLSGGQKQRVgiarALANnpkvllC----------DEATSALDPettrsiLDllkdiNRELgltivlitheMDVVRR- 206
|
250 260 270
....*....|....*....|....*....|...
gi 2553857580 202 ladtpmtcvfstayleeaeAADRVLLFESGRII 234
Cdd:COG1135 207 -------------------ICDRVAVLENGRIV 220
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
372-588 |
2.34e-18 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 87.78 E-value: 2.34e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857580 372 IARKFGNFVAVADTSFEVRRGEIFGLLGPNGAGKTTTFRMLCGLLVPSKGQIEVAGYDLRTAKAGA-----RARIGYVAQ 446
Cdd:PRK10070 34 ILEKTGLSLGVKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAKISDAElrevrRKKIAMVFQ 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857580 447 KFSLYGKLSVEQNLRYFGRSYGFFGQALQDRIDASLEDFGLTDRRDTTAGSLSFGAKQDLSMACGLIHSPEILFLDEATS 526
Cdd:PRK10070 114 SFALMPHMTVLDNTAFGMELAGINAEERREKALDALRQVGLENYAHSYPDELSGGMRQRVGLARALAINPDILLMDEAFS 193
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2553857580 527 GADLASRRAFWRRINAL-ASAGTSVVVTTHFLEEA-EYCDRFLIQDAGKVLALGTPREVKQRAA 588
Cdd:PRK10070 194 ALDPLIRTEMQDELVKLqAKHQRTIVFISHDLDEAmRIGDRIAIMQNGEVVQVGTPDEILNNPA 257
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
7-574 |
2.59e-18 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 88.18 E-value: 2.59e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857580 7 PAIRLEGVVKTFpnplDAARPIRAVDgISLKAGgaeasdRLIALVGPDGAGKSTFMRLLCGLEAPDEGRLSVLGT----- 81
Cdd:PRK15439 10 PLLCARSISKQY----SGVEVLKGID-FTLHAG------EVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIGGNpcarl 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857580 82 TPdpdNEDFTTRIAFMPQTLGLYKTLSCRENLevfagLRGFEGEADGAAGLERRIAELLSMTGLagfeERQAGKLSGGMK 161
Cdd:PRK15439 79 TP---AKAHQLGIYLVPQEPLLFPNLSVKENI-----LFGLPKRQASMQKMKQLLAALGCQLDL----DSSAGSLEVADR 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857580 162 QKLALASALLRIPDLLLLDEPTVGVDPLSRRELWSVVRrMLADTPMTCVFSTAYLEEA-EAADRVLLFESGRIIadenpq 240
Cdd:PRK15439 147 QIVEILRGLMRDSRILILDEPTASLTPAETERLFSRIR-ELLAQGVGIVFISHKLPEIrQLADRISVMRDGTIA------ 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857580 241 sfisrakgrtyllplanraehdaqmlcrrLSEETAATRSDALFLDIVPRmggaaattlaptlpVKDArvpsgfiprqpSL 320
Cdd:PRK15439 220 -----------------------------LSGKTADLSTDDIIQAITPA--------------AREK-----------SL 245
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857580 321 EDAYAL-LTFPrapktANHLASPPsdasgalaasaasaddtaERPVVIRADGIARKFgnfvavADTSFEVRRGEIFGLLG 399
Cdd:PRK15439 246 SASQKLwLELP-----GNRRQQAA------------------GAPVLTVEDLTGEGF------RNISLEVRAGEILGLAG 296
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857580 400 PNGAGKTTTFRMLCGLLVPSKGQIEVAGYDLRTAKAGARARIGYV-----AQKFSLYGKLSVEQNL-RYFGRSYGFFGQA 473
Cdd:PRK15439 297 VVGAGRTELAETLYGLRPARGGRIMLNGKEINALSTAQRLARGLVylpedRQSSGLYLDAPLAWNVcALTHNRRGFWIKP 376
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857580 474 LQDRidASLEDFgltdRR---------DTTAGSLSFGAKQDLSMACGLIHSPEILFLDEATSGADLASRRAFWRRINALA 544
Cdd:PRK15439 377 AREN--AVLERY----RRalnikfnhaEQAARTLSGGNQQKVLIAKCLEASPQLLIVDEPTRGVDVSARNDIYQLIRSIA 450
|
570 580 590
....*....|....*....|....*....|.
gi 2553857580 545 SAGTSVVVTTHFLEEAE-YCDRFLIQDAGKV 574
Cdd:PRK15439 451 AQNVAVLFISSDLEEIEqMADRVLVMHQGEI 481
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
362-594 |
2.83e-18 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 88.18 E-value: 2.83e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857580 362 ERPVVIRADGIARKFGNFVAVADTSFEVRRGEIFGLLGPNGAGKTTTFRMLCGLLVPSKGQIEVAG---YDLRTAKAGAR 438
Cdd:PRK15439 7 TAPPLLCARSISKQYSGVEVLKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIGGnpcARLTPAKAHQL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857580 439 ArIGYVAQKFSLYGKLSVEQNLryfgrsygFFG----QALQDRIDASLEDFGLTDRRDTTAGSLSFGAKQDLSMACGLIH 514
Cdd:PRK15439 87 G-IYLVPQEPLLFPNLSVKENI--------LFGlpkrQASMQKMKQLLAALGCQLDLDSSAGSLEVADRQIVEILRGLMR 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857580 515 SPEILFLDEATSGADLASRRAFWRRINALASAGTSVVVTTHFLEEA-EYCDRFLIQDAGKVlALGTPREVKQRAAVLSAV 593
Cdd:PRK15439 158 DSRILILDEPTASLTPAETERLFSRIRELLAQGVGIVFISHKLPEIrQLADRISVMRDGTI-ALSGKTADLSTDDIIQAI 236
|
.
gi 2553857580 594 S 594
Cdd:PRK15439 237 T 237
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
384-580 |
3.07e-18 |
|
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: 83.62 E-value: 3.07e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857580 384 DTSFEVRRGEIFGLLGPNGAGKTTTFRMLCGLLVPSKGQIEVAGYDLRTAKAGA-RARIGYVAQKFSLYGKlSVEQNLRY 462
Cdd:cd03369 26 NVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDGIDISTIPLEDlRSSLTIIPQDPTLFSG-TIRSNLDP 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857580 463 FGRsYGffgqalQDRIDASLedfgltdrRDTTAGS-LSFGAKQDLSMACGLIHSPEILFLDEATSGADLASRRAFWRRIN 541
Cdd:cd03369 105 FDE-YS------DEEIYGAL--------RVSEGGLnLSQGQRQLLCLARALLKRPRVLVLDEATASIDYATDALIQKTIR 169
|
170 180 190
....*....|....*....|....*....|....*....
gi 2553857580 542 ALASaGTSVVVTTHFLEEAEYCDRFLIQDAGKVLALGTP 580
Cdd:cd03369 170 EEFT-NSTILTIAHRLRTIIDYDKILVMDAGEVKEYDHP 207
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
370-565 |
3.17e-18 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 88.04 E-value: 3.17e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857580 370 DGIARKFGNFVAVADTSFEVRRGEIFGLLGPNGAGKTTTFRMLCGLLVPSKGQIEVAGYDLR--TAKAGARARIGYVAQK 447
Cdd:PRK11288 8 DGIGKTFPGVKALDDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSILIDGQEMRfaSTTAALAAGVAIIYQE 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857580 448 FSLYGKLSVEQNLrYFGR---SYGFFGQ-ALQDRIDASLEDFGLTDRRDTTAGSLSFGAKQDLSMACGLIHSPEILFLDE 523
Cdd:PRK11288 88 LHLVPEMTVAENL-YLGQlphKGGIVNRrLLNYEAREQLEHLGVDIDPDTPLKYLSIGQRQMVEIAKALARNARVIAFDE 166
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 2553857580 524 ATSgaDLASR--RAFWRRINALASAGTSVVVTTHFLEEA-EYCDR 565
Cdd:PRK11288 167 PTS--SLSAReiEQLFRVIRELRAEGRVILYVSHRMEEIfALCDA 209
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
384-583 |
3.68e-18 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 84.80 E-value: 3.68e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857580 384 DTSFEVRRGEIFGLLGPNGAGKTTTFRMLCGLLVPSKGQI-----EVAGYDLRTAkagaRARIGYVAQ----KF--SLYg 452
Cdd:PRK13648 27 DVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIfynnqAITDDNFEKL----RKHIGIVFQnpdnQFvgSIV- 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857580 453 KLSVEQNLRYFGRSYgffgQALQDRIDASLEDFGLTDRRDTTAGSLSFGAKQDLSMACGLIHSPEILFLDEATSGADLAS 532
Cdd:PRK13648 102 KYDVAFGLENHAVPY----DEMHRRVSEALKQVDMLERADYEPNALSGGQKQRVAIAGVLALNPSVIILDEATSMLDPDA 177
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 2553857580 533 RRAFWRRINAL-ASAGTSVVVTTHFLEEAEYCDRFLIQDAGKVLALGTPREV 583
Cdd:PRK13648 178 RQNLLDLVRKVkSEHNITIISITHDLSEAMEADHVIVMNKGTVYKEGTPTEI 229
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
380-565 |
4.08e-18 |
|
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family transporter in which each gene contains an N-terminal membrane-spanning domain (pfam00664) and a C-terminal ATP-binding domain (pfam00005). In E. coli these genes were discovered as mutants which caused the terminal heme-copper oxidase complex cytochrome bd to fail to assemble. Recent work has shown that the transporter is involved in export of redox-active thiol compounds such as cysteine and glutathione. The linkage to assembly of the cytochrome bd complex is further supported by the conserved operon structure found outside the gammaproteobacteria (cydABCD) containing both the transporter and oxidase genes components. The genes used as the seed members for this model are all either found in the gammproteobacterial context or the CydABCD context. All members of this family scoring above trusted at the time of its creation were from genomes which encode a cytochrome bd complex. Unfortunately, the gene symbol nomenclature adopted based on this operon in B. subtilis assigns cydC to the third gene in the operon where this gene is actually homologous to the E. coli cydD gene. We have chosen to name all homologs in this family in accordance with the precedence of publication of the E. coli name, CydD
Pssm-ID: 274323 [Multi-domain] Cd Length: 529 Bit Score: 87.73 E-value: 4.08e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857580 380 VAVADTSFEVRRGEIFGLLGPNGAGKTTTFRMLCGLLVPSKGQIEVAGYDLRTAK-AGARARIGYVAQKFSLYGKlSVEQ 458
Cdd:TIGR02857 336 PALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSIAVNGVPLADADaDSWRDQIAWVPQHPFLFAG-TIAE 414
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857580 459 NLRyFGRSYGFFGQALQDRIDASLEDF--GLTDRRDTTAGS----LSFGAKQDLSMACGLIHSPEILFLDEATSGADLAS 532
Cdd:TIGR02857 415 NIR-LARPDASDAEIREALERAGLDEFvaALPQGLDTPIGEggagLSGGQAQRLALARAFLRDAPLLLLDEPTAHLDAET 493
|
170 180 190
....*....|....*....|....*....|...
gi 2553857580 533 RRAFWRRINALASaGTSVVVTTHFLEEAEYCDR 565
Cdd:TIGR02857 494 EAEVLEALRALAQ-GRTVLLVTHRLALAALADR 525
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
372-583 |
4.15e-18 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 83.99 E-value: 4.15e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857580 372 IARKFGNFVAVADTSFEVRRGEIFGLLGPNGAGKTTTFRMLCGLLVPSKGQIEVAGYDLRTAKAGARA---RIGYVAQKF 448
Cdd:PRK09493 7 VSKHFGPTQVLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGLKVNDPKVDERLirqEAGMVFQQF 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857580 449 SLYGKLSVEQNLrYFG--RSYGFFGQALQDRIDASLEDFGLTDRRDTTAGSLSFGAKQDLSMACGLIHSPEILFLDEATS 526
Cdd:PRK09493 87 YLFPHLTALENV-MFGplRVRGASKEEAEKQARELLAKVGLAERAHHYPSELSGGQQQRVAIARALAVKPKLMLFDEPTS 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 2553857580 527 GADLASRRAFWRRINALASAGTSVVVTTHFLEEAE-YCDRFLIQDAGKVLALGTPREV 583
Cdd:PRK09493 166 ALDPELRHEVLKVMQDLAEEGMTMVIVTHEIGFAEkVASRLIFIDKGRIAEDGDPQVL 223
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
384-574 |
4.39e-18 |
|
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: 83.67 E-value: 4.39e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857580 384 DTSFEVRRGEIFGLLGPNGAGKTTTFRMLCGLLVPSKGQIEVAGYDLRTAKAG-ARARIGYVAQKFSLYGKlSVEQNLRY 462
Cdd:cd03248 32 DVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDGKPISQYEHKyLHSKVSLVGQEPVLFAR-SLQDNIAY 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857580 463 fGRSYGFFGQALQDRIDASLEDF--GLTDRRDTTAGS----LSFGAKQDLSMACGLIHSPEILFLDEATSGADLASRRAF 536
Cdd:cd03248 111 -GLQSCSFECVKEAAQKAHAHSFisELASGYDTEVGEkgsqLSGGQKQRVAIARALIRNPQVLILDEATSALDAESEQQV 189
|
170 180 190
....*....|....*....|....*....|....*...
gi 2553857580 537 WRRINALASAgTSVVVTTHFLEEAEYCDRFLIQDAGKV 574
Cdd:cd03248 190 QQALYDWPER-RTVLVIAHRLSTVERADQILVLDGGRI 226
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
389-578 |
4.59e-18 |
|
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: 83.31 E-value: 4.59e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857580 389 VRRGEIFGLLGPNGAGKTTTFRMLCGLLVPSKGQIEVAGYDLRTAKAGARArIGYVAQKFSLYGKLSVEQNLRyFGRSYG 468
Cdd:cd03298 21 FAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLINGVDVTAAPPADRP-VSMLFQENNLFAHLTVEQNVG-LGLSPG 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857580 469 FFGQAL-QDRIDASLEDFGLTDRRDTTAGSLSFGAKQDLSMACGLIHSPEILFLDEATSGADLASRRAFWRRINAL-ASA 546
Cdd:cd03298 99 LKLTAEdRQAIEVALARVGLAGLEKRLPGELSGGERQRVALARVLVRDKPVLLLDEPFAALDPALRAEMLDLVLDLhAET 178
|
170 180 190
....*....|....*....|....*....|...
gi 2553857580 547 GTSVVVTTHFLEEAEYCDRFLIQ-DAGKVLALG 578
Cdd:cd03298 179 KMTVLMVTHQPEDAKRLAQRVVFlDNGRIAAQG 211
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
8-234 |
4.60e-18 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 84.03 E-value: 4.60e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857580 8 AIRLEGVVKTFPNPldaarpiRAVDGISLKAGGAEasdrLIALVGPDGAGKSTFMRLLCGLEAPDEGRLSVLGTTPDPDN 87
Cdd:PRK11264 3 AIEVKNLVKKFHGQ-------TVLHGIDLEVKPGE----VVAIIGPSGSGKTTLLRCINLLEQPEAGTIRVGDITIDTAR 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857580 88 ---------EDFTTRIAFMPQTLGLYKTLSCRENleVFAGLRGFEGEADGAAglERRIAELLSMTGLAGFEERQAGKLSG 158
Cdd:PRK11264 72 slsqqkgliRQLRQHVGFVFQNFNLFPHRTVLEN--IIEGPVIVKGEPKEEA--TARARELLAKVGLAGKETSYPRRLSG 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2553857580 159 GMKQKLALASALLRIPDLLLLDEPTVGVDPLSRRELWSVVRRmLADTPMTCVFSTAYLEEA-EAADRVLLFESGRII 234
Cdd:PRK11264 148 GQQQRVAIARALAMRPEVILFDEPTSALDPELVGEVLNTIRQ-LAQEKRTMVIVTHEMSFArDVADRAIFMDQGRIV 223
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
384-592 |
4.76e-18 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 88.24 E-value: 4.76e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857580 384 DTSFEVRRGEIFGLLGPNGAGKTTTFRMLCGLLVPSKGQIEVAGYDLRTAKAGA-RARIGYVAQKFSLYGKlSVEQNLRY 462
Cdd:TIGR00958 499 GLTFTLHPGEVVALVGPSGSGKSTVAALLQNLYQPTGGQVLLDGVPLVQYDHHYlHRQVALVGQEPVLFSG-SVRENIAY 577
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857580 463 fGRSYGFFGQALQDRIDASLEDF--GLTDRRDTTAGS----LSFGAKQDLSMACGLIHSPEILFLDEATSGADLASRRAF 536
Cdd:TIGR00958 578 -GLTDTPDEEIMAAAKAANAHDFimEFPNGYDTEVGEkgsqLSGGQKQRIAIARALVRKPRVLILDEATSALDAECEQLL 656
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 2553857580 537 --WRRinalaSAGTSVVVTTHFLEEAEYCDRFLIQDAGKVLALGTPREVKQRAAVLSA 592
Cdd:TIGR00958 657 qeSRS-----RASRTVLLIAHRLSTVERADQILVLKKGSVVEMGTHKQLMEDQGCYKH 709
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
30-236 |
6.46e-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: 81.59 E-value: 6.46e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857580 30 AVDGISL--KAGgaeasdRLIALVGPDGAGKSTFMRLLCGLEAPDEGRLSVLGTTPDPDNEDFTTRIAFMPQTLGLYKTl 107
Cdd:cd03247 17 VLKNLSLelKQG------EKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDGVPVSDLEKALSSLISVLNQRPYLFDT- 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857580 108 SCRENLevfaGLRgfegeadgaaglerriaellsmtglagfeerqagkLSGGMKQKLALASALLRIPDLLLLDEPTVGVD 187
Cdd:cd03247 90 TLRNNL----GRR-----------------------------------FSGGERQRLALARILLQDAPIVLLDEPTVGLD 130
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 2553857580 188 PLSRRELWSVVRRMLADTpmTCVFSTAYLEEAEAADRVLLFESGRIIAD 236
Cdd:cd03247 131 PITERQLLSLIFEVLKDK--TLIWITHHLTGIEHMDKILFLENGKIIMQ 177
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
366-557 |
7.14e-18 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 83.62 E-value: 7.14e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857580 366 VIRADGIARKFGNFVAVADTSFEVRRGEIFGLLGPNGAGKTTTFRMLCGLLVPSKGQIEvagydlRTAKagarARIGYVA 445
Cdd:PRK09544 4 LVSLENVSVSFGQRRVLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIK------RNGK----LRIGYVP 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857580 446 QKFSLYGK--LSVEQNLRYF-GRSYGFFGQALQDRIDASLEDFGLTdrrdttagSLSFGAKQDLSMACGLIHSPEILFLD 522
Cdd:PRK09544 74 QKLYLDTTlpLTVNRFLRLRpGTKKEDILPALKRVQAGHLIDAPMQ--------KLSGGETQRVLLARALLNRPQLLVLD 145
|
170 180 190
....*....|....*....|....*....|....*.
gi 2553857580 523 EATSGADLASRRAFWRRINALASA-GTSVVVTTHFL 557
Cdd:PRK09544 146 EPTQGVDVNGQVALYDLIDQLRRElDCAVLMVSHDL 181
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
41-241 |
1.04e-17 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 82.75 E-value: 1.04e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857580 41 AEASDRLIaLVGPDGAGKSTFMRLLCGLEAPDEGRLSV------LGTTPDPdnedftTRIAFMPQTLG-------LYKTL 107
Cdd:PRK11124 25 CPQGETLV-LLGPSGAGKSSLLRVLNLLEMPRSGTLNIagnhfdFSKTPSD------KAIRELRRNVGmvfqqynLWPHL 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857580 108 SCRENLeVFAGLRgfegeadgAAGLERRIA-----ELLSMTGLAGFEERQAGKLSGGMKQKLALASALLRIPDLLLLDEP 182
Cdd:PRK11124 98 TVQQNL-IEAPCR--------VLGLSKDQAlaraeKLLERLRLKPYADRFPLHLSGGQQQRVAIARALMMEPQVLLFDEP 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2553857580 183 TVGVDPLSRRELWSVVRRmLADTPMTCVFSTAYLEEA-EAADRVLLFESGRII----AD--ENPQS 241
Cdd:PRK11124 169 TAALDPEITAQIVSIIRE-LAETGITQVIVTHEVEVArKTASRVVYMENGHIVeqgdAScfTQPQT 233
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
46-228 |
1.13e-17 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 81.51 E-value: 1.13e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857580 46 RLIALVGPDGAGKSTFMRLLCGLEAPDEGRLSVLGTTpdpdnedfttRIAFMPQTLGLYKTLSCRENLEVFAGL---RGF 122
Cdd:NF040873 19 SLTAVVGPNGSGKSTLLKVLAGVLRPTSGTVRRAGGA----------RVAYVPQRSEVPDSLPLTVRDLVAMGRwarRGL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857580 123 EGEADGAAglERRIAELLSMTGLAGFEERQAGKLSGGMKQKLALASALLRIPDLLLLDEPTVGVDPLSRRELWSVVRRmL 202
Cdd:NF040873 89 WRRLTRDD--RAAVDDALERVGLADLAGRQLGELSGGQRQRALLAQGLAQEADLLLLDEPTTGLDAESRERIIALLAE-E 165
|
170 180
....*....|....*....|....*.
gi 2553857580 203 ADTPMTCVFSTAYLEEAEAADRVLLF 228
Cdd:NF040873 166 HARGATVVVVTHDLELVRRADPCVLL 191
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
22-226 |
1.18e-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: 81.77 E-value: 1.18e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857580 22 LDAARPIRAV-DGISLKAGGAEAsdrlIALVGPDGAGKSTFMRLLCGLEAPDEGRLSVLGTTPDPDNEDFTTRIAFMPQT 100
Cdd:cd03231 6 LTCERDGRALfSGLSFTLAAGEA----LQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNGGPLDFQRDSIARGLLYLGHA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857580 101 LGLYKTLSCRENLEVFAGLRGFEGeadgaaglerrIAELLSMTGLAGFEERQAGKLSGGMKQKLALASALLRIPDLLLLD 180
Cdd:cd03231 82 PGIKTTLSVLENLRFWHADHSDEQ-----------VEEALARVGLNGFEDRPVAQLSAGQQRRVALARLLLSGRPLWILD 150
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 2553857580 181 EPTVGVDPLSRRELWSVVRRMLADTPMTCVFSTAYLEEAEAADRVL 226
Cdd:cd03231 151 EPTTALDKAGVARFAEAMAGHCARGGMVVLTTHQDLGLSEAGAREL 196
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
384-582 |
2.75e-17 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 85.48 E-value: 2.75e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857580 384 DTSFEVRRGEIFGLLGPNGAGKTT-----TFRMLCGLLVpsKGQIEVAGydLRTAKAGARARIGYVAQKFSLYGKLSVEQ 458
Cdd:TIGR00955 43 NVSGVAKPGELLAVMGSSGAGKTTlmnalAFRSPKGVKG--SGSVLLNG--MPIDAKEMRAISAYVQQDDLFIPTLTVRE 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857580 459 NLRY-----FGRSYGFFGQalQDRIDASLEDFGLTDRRDTTAG------SLSFGAKQDLSMACGLIHSPEILFLDEATSG 527
Cdd:TIGR00955 119 HLMFqahlrMPRRVTKKEK--RERVDEVLQALGLRKCANTRIGvpgrvkGLSGGERKRLAFASELLTDPPLLFCDEPTSG 196
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 2553857580 528 ADLASRRAFWRRINALASAGTSVVVTTHFLEEAEYC--DRFLIQDAGKVLALGTPRE 582
Cdd:TIGR00955 197 LDSFMAYSVVQVLKGLAQKGKTIICTIHQPSSELFElfDKIILMAEGRVAYLGSPDQ 253
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
5-574 |
2.91e-17 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 84.96 E-value: 2.91e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857580 5 SAPAIRLEGVVKTFPNpldaarpIRAVDGISLKAGGAEASdrliALVGPDGAGKSTFMRLLCGLEAPDEGRLSVLGTTPD 84
Cdd:PRK11288 1 SSPYLSFDGIGKTFPG-------VKALDDISFDCRAGQVH----ALMGENGAGKSTLLKILSGNYQPDAGSILIDGQEMR 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857580 85 PDN--EDFTTRIAFMPQTLGLYKTLSCRENLEV--FAGLRGFEGEADgaagLERRIAELLSMTGLAGFEERQAGKLSGGM 160
Cdd:PRK11288 70 FASttAALAAGVAIIYQELHLVPEMTVAENLYLgqLPHKGGIVNRRL----LNYEAREQLEHLGVDIDPDTPLKYLSIGQ 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857580 161 KQKLALASALLRIPDLLLLDEPTvgvDPLSRRE---LWSVVRRMLADTPMTcVFSTAYLEEA-EAADRVLLFESGRIIAd 236
Cdd:PRK11288 146 RQMVEIAKALARNARVIAFDEPT---SSLSAREieqLFRVIRELRAEGRVI-LYVSHRMEEIfALCDAITVFKDGRYVA- 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857580 237 enpqSFISRAKgrtyllplANRAEHDAQMLCRRLSeetaatrsdalflDIVprmggaaattlaptlpvkdarvpsGFIPR 316
Cdd:PRK11288 221 ----TFDDMAQ--------VDRDQLVQAMVGREIG-------------DIY------------------------GYRPR 251
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857580 317 QPSledayalltfprapktanhlasppsdasgalaasaasaddtaerPVVIRADGIArkfGNFVAvADTSFEVRRGEIFG 396
Cdd:PRK11288 252 PLG--------------------------------------------EVRLRLDGLK---GPGLR-EPISFSVRAGEIVG 283
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857580 397 LLGPNGAGKTTTFRMLCGLLVPSKGQIEVAG--YDLRTAKAGARARI----------GYVAQKfslygklSVEQNL---- 460
Cdd:PRK11288 284 LFGLVGAGRSELMKLLYGATRRTAGQVYLDGkpIDIRSPRDAIRAGImlcpedrkaeGIIPVH-------SVADNInisa 356
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857580 461 RyfgRSYGFFGQALQDRIDASLEDFGL------TDRRDTTAGSLSFGAKQDLSMACGLIHSPEILFLDEATSGADLASRR 534
Cdd:PRK11288 357 R---RHHLRAGCLINNRWEAENADRFIrslnikTPSREQLIMNLSGGNQQKAILGRWLSEDMKVILLDEPTRGIDVGAKH 433
|
570 580 590 600
....*....|....*....|....*....|....*....|.
gi 2553857580 535 AFWRRINALASAGTSVVVTTHFLEEA-EYCDRFLIQDAGKV 574
Cdd:PRK11288 434 EIYNVIYELAAQGVAVLFVSSDLPEVlGVADRIVVMREGRI 474
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
9-244 |
4.18e-17 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 81.96 E-value: 4.18e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857580 9 IRLEGVVKTFPNPLDAARPIravdGISLKAGgaeasdRLIALVGPDGAGKSTFMRLLCGLEAPDEGRLSVLGTtpdpDNE 88
Cdd:PRK13644 2 IRLENVSYSYPDGTPALENI----NLVIKKG------EYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLVSGI----DTG 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857580 89 DFT--------TRIAFM-PQTLGLYKTLscRENLEVfaglrGFEGEADGAAGLERRIAELLSMTGLAGFEERQAGKLSGG 159
Cdd:PRK13644 68 DFSklqgirklVGIVFQnPETQFVGRTV--EEDLAF-----GPENLCLPPIEIRKRVDRALAEIGLEKYRHRSPKTLSGG 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857580 160 MKQKLALASALLRIPDLLLLDEPTVGVDPLSRRELWSVVRRmLADTPMTCVFSTAYLEEAEAADRVLLFESGRIIADENP 239
Cdd:PRK13644 141 QGQCVALAGILTMEPECLIFDEVTSMLDPDSGIAVLERIKK-LHEKGKTIVYITHNLEELHDADRIIVMDRGKIVLEGEP 219
|
....*
gi 2553857580 240 QSFIS 244
Cdd:PRK13644 220 ENVLS 224
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
19-278 |
4.29e-17 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 81.26 E-value: 4.29e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857580 19 PNPLDAARPIrAVDGISLKAGGAEASDRL---------IALVGPDGAGKSTFMRLLCGLEAPDEGRLsVLGTTPDPDNED 89
Cdd:PRK11247 4 TARLNQGTPL-LLNAVSKRYGERTVLNQLdlhipagqfVAVVGRSGCGKSTLLRLLAGLETPSAGEL-LAGTAPLAEARE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857580 90 fTTRIAFMPQTLGLYKTLScrENleVFAGLRGF----EGEADGAAGLERRIAELlsmtglagfeerqAGKLSGGMKQKLA 165
Cdd:PRK11247 82 -DTRLMFQDARLLPWKKVI--DN--VGLGLKGQwrdaALQALAAVGLADRANEW-------------PAALSGGQKQRVA 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857580 166 LASALLRIPDLLLLDEPTVGVDPLSRRELWSVVRRMLADTPMTCVFSTAYLEEAEA-ADRVLLFESGRIIADENPQSFIS 244
Cdd:PRK11247 144 LARALIHRPGLLLLDEPLGALDALTRIEMQDLIESLWQQHGFTVLLVTHDVSEAVAmADRVLLIEEGKIGLDLTVDLPRP 223
|
250 260 270
....*....|....*....|....*....|....*
gi 2553857580 245 RAKGRTYLlplanrAEHDAQMLCRRLSE-ETAATR 278
Cdd:PRK11247 224 RRRGSARL------AELEAEVLQRVMSRgESEPTR 252
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
9-194 |
4.71e-17 |
|
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: 80.14 E-value: 4.71e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857580 9 IRLEGVVKTFPNPldaarpIRAVDGISLKAGGAEasdrLIALVGPDGAGKSTFMRLLCGLEAPDEGRLSVLGTtpdPDNE 88
Cdd:cd03292 1 IEFINVTKTYPNG------TAALDGINISISAGE----FVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQ---DVSD 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857580 89 DFTTRIAFMPQTLGL-YKTLSCRENLEVFAGLrGFEGEADGAAGLE--RRIAELLSMTGLAGFEERQAGKLSGGMKQKLA 165
Cdd:cd03292 68 LRGRAIPYLRRKIGVvFQDFRLLPDRNVYENV-AFALEVTGVPPREirKRVPAALELVGLSHKHRALPAELSGGEQQRVA 146
|
170 180
....*....|....*....|....*....
gi 2553857580 166 LASALLRIPDLLLLDEPTVGVDPLSRREL 194
Cdd:cd03292 147 IARAIVNSPTILIADEPTGNLDPDTTWEI 175
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
7-240 |
7.53e-17 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 82.69 E-value: 7.53e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857580 7 PAIRLEGVVKTFPNPldaarpiRAVDGISLKAGGAEasdrLIALVGPDGAGKSTFMRLLCGLEAPDEGRLSVLG---TTP 83
Cdd:PRK09452 13 PLVELRGISKSFDGK-------EVISNLDLTINNGE----FLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLDGqdiTHV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857580 84 DPDNEDFTTriAFmpQTLGLYKTLSCRENleVFAGLRGfegEADGAAGLERRIAELLSMTGLAGFEERQAGKLSGGMKQK 163
Cdd:PRK09452 82 PAENRHVNT--VF--QSYALFPHMTVFEN--VAFGLRM---QKTPAAEITPRVMEALRMVQLEEFAQRKPHQLSGGQQQR 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2553857580 164 LALASALLRIPDLLLLDEPTVGVDPLSRRELWSVVRRMLADTPMTCVFSTAYLEEAEA-ADRVLLFESGRIIADENPQ 240
Cdd:PRK09452 153 VAIARAVVNKPKVLLLDESLSALDYKLRKQMQNELKALQRKLGITFVFVTHDQEEALTmSDRIVVMRDGRIEQDGTPR 230
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
9-221 |
9.57e-17 |
|
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: 84.68 E-value: 9.57e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857580 9 IRLEGVVKTFPNpldAARPirAVDGISLKAGGAEAsdrlIALVGPDGAGKSTFMRLLCGLEAPDEGRLSVLGTTPDPDNE 88
Cdd:TIGR01257 1938 LRLNELTKVYSG---TSSP--AVDRLCVGVRPGEC----FGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAGKSILTNIS 2008
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857580 89 DFTTRIAFMPQTLGLYKTLSCRENLEVFAGLRGFEGEAdgaagLERRIAELLSMTGLAGFEERQAGKLSGGMKQKLALAS 168
Cdd:TIGR01257 2009 DVHQNMGYCPQFDAIDDLLTGREHLYLYARLRGVPAEE-----IEKVANWSIQSLGLSLYADRLAGTYSGGNKRKLSTAI 2083
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 2553857580 169 ALLRIPDLLLLDEPTVGVDPLSRRELWSVVRRMLADTpMTCVFSTAYLEEAEA 221
Cdd:TIGR01257 2084 ALIGCPPLVLLDEPTTGMDPQARRMLWNTIVSIIREG-RAVVLTSHSMEECEA 2135
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
365-576 |
9.73e-17 |
|
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: 83.45 E-value: 9.73e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857580 365 VVIRADGIARKFGNFVAVADTSFEVRRGEIFGLLGPNGAGKTTTFRMLCGLLVPSKGQIEVagydlrtakaGARARIGYV 444
Cdd:TIGR03719 321 KVIEAENLTKAFGDKLLIDDLSFKLPPGGIVGVIGPNGAGKSTLFRMITGQEQPDSGTIEI----------GETVKLAYV 390
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857580 445 AQ-KFSLYGKLSV----------------EQNLR-YFGRsYGFFGQALQDRIdasledfgltdrrdttaGSLSFGAKQDL 506
Cdd:TIGR03719 391 DQsRDALDPNKTVweeisggldiiklgkrEIPSRaYVGR-FNFKGSDQQKKV-----------------GQLSGGERNRV 452
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2553857580 507 SMACGLIHSPEILFLDEATSGADLASRRAFWrriNALASAGTSVVVTTHfleeaeycDR-FLIQDAGKVLA 576
Cdd:TIGR03719 453 HLAKTLKSGGNVLLLDEPTNDLDVETLRALE---EALLNFAGCAVVISH--------DRwFLDRIATHILA 512
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
9-236 |
1.11e-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: 1.11e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857580 9 IRLEGVVKTFPNpldaarpIRAVDGISLKAGGAEasdrLIALVGPDGAGKSTFMRLLCGLEAPDEGRLSVLGTTPDPDN- 87
Cdd:cd03216 1 LELRGITKRFGG-------VKALDGVSLSVRRGE----VHALLGENGAGKSTLMKILSGLYKPDSGEILVDGKEVSFASp 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857580 88 -EDFTTRIAFMPQtlglyktlscrenlevfaglrgfegeadgaaglerriaellsmtglagfeerqagkLSGGMKQKLAL 166
Cdd:cd03216 70 rDARRAGIAMVYQ--------------------------------------------------------LSVGERQMVEI 93
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2553857580 167 ASALLRIPDLLLLDEPTVGVDPLSRRELWSVVRRmLADTPMTCVFSTAYLEEA-EAADRVLLFESGRIIAD 236
Cdd:cd03216 94 ARALARNARLLILDEPTAALTPAEVERLFKVIRR-LRAQGVAVIFISHRLDEVfEIADRVTVLRDGRVVGT 163
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
2-247 |
1.12e-16 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 80.42 E-value: 1.12e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857580 2 TKASAPAIRLEGVVKTFPNpldAARPirAVDGISLKAGGAEasdrLIALVGPDGAGKSTFMRLLCGLEAPDEGRLSVLGT 81
Cdd:PRK13632 1 IKNKSVMIKVENVSFSYPN---SENN--ALKNVSFEINEGE----YVAILGHNGSGKSTISKILTGLLKPQSGEIKIDGI 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857580 82 TPDPDNEDFTtriafmpqtlglyktlscRENLEV--------FAGLrgfEGEADGAAGLERR----------IAELLSMT 143
Cdd:PRK13632 72 TISKENLKEI------------------RKKIGIifqnpdnqFIGA---TVEDDIAFGLENKkvppkkmkdiIDDLAKKV 130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857580 144 GLAGFEERQAGKLSGGMKQKLALASALLRIPDLLLLDEPTVGVDPLSRRELWSVVRRmLADTPMTCVFS-TAYLEEAEAA 222
Cdd:PRK13632 131 GMEDYLDKEPQNLSGGQKQRVAIASVLALNPEIIIFDESTSMLDPKGKREIKKIMVD-LRKTRKKTLISiTHDMDEAILA 209
|
250 260 270
....*....|....*....|....*....|.
gi 2553857580 223 DRVLLFESGRIIADENPQS------FISRAK 247
Cdd:PRK13632 210 DKVIVFSEGKLIAQGKPKEilnnkeILEKAK 240
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
362-564 |
1.18e-16 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 79.37 E-value: 1.18e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857580 362 ERPVVIRADGIARKFGNFVAVADTSFEVRRGEIFGLLGPNGAGKTTTFRMLCGLLVPSKGQIEVAGYDLRTAKAGA-RAR 440
Cdd:PRK10247 3 ENSPLLQLQNVGYLAGDAKILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFEGEDISTLKPEIyRQQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857580 441 IGYVAQKFSLYGKlSVEQNLRYfgrSYGFFGQALQ-DRIDASLEDFGLTDRR-DTTAGSLSFGAKQDLSMACGLIHSPEI 518
Cdd:PRK10247 83 VSYCAQTPTLFGD-TVYDNLIF---PWQIRNQQPDpAIFLDDLERFALPDTIlTKNIAELSGGEKQRISLIRNLQFMPKV 158
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 2553857580 519 LFLDEATSGADLASRRAFWRRINALAS-AGTSVVVTTHFLEEAEYCD 564
Cdd:PRK10247 159 LLLDEITSALDESNKHNVNEIIHRYVReQNIAVLWVTHDKDEINHAD 205
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
29-240 |
1.21e-16 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 80.55 E-value: 1.21e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857580 29 RAVDGISLkagGAEASDRlIALVGPDGAGKSTFMRLLCGLEAPDEGRLSVLGTT-----------------PDPDNEDFT 91
Cdd:PRK13647 19 KALKGLSL---SIPEGSK-TALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGREvnaenekwvrskvglvfQDPDDQVFS 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857580 92 TRI----AFMPQTLGLyktlscrenlevfaglrgfegeadGAAGLERRIAELLSMTGLAGFEERQAGKLSGGMKQKLALA 167
Cdd:PRK13647 95 STVwddvAFGPVNMGL------------------------DKDEVERRVEEALKAVRMWDFRDKPPYHLSYGQKKRVAIA 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2553857580 168 SALLRIPDLLLLDEPTVGVDPLSRRELWSVVRRmLADTPMTCVFSTAYLE-EAEAADRVLLFESGRIIADENPQ 240
Cdd:PRK13647 151 GVLAMDPDVIVLDEPMAYLDPRGQETLMEILDR-LHNQGKTVIVATHDVDlAAEWADQVIVLKEGRVLAEGDKS 223
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
386-590 |
1.39e-16 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 80.44 E-value: 1.39e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857580 386 SFEVRRGEIFGLLGPNGAGKTTTFRMLCGLLVPSKGQIEVAGYDLRTAKAGARARIGYVAQKFS------LYgkLSVEQN 459
Cdd:PRK13638 21 NLDFSLSPVTGLVGANGCGKSTLFMNLSGLLRPQKGAVLWQGKPLDYSKRGLLALRQQVATVFQdpeqqiFY--TDIDSD 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857580 460 LRYFGRSYGFFGQALQDRIDASLEDFGLTDRRDTTAGSLSFGAKQDLSMACGLIHSPEILFLDEATSGADLASRRAFWRR 539
Cdd:PRK13638 99 IAFSLRNLGVPEAEITRRVDEALTLVDAQHFRHQPIQCLSHGQKKRVAIAGALVLQARYLLLDEPTAGLDPAGRTQMIAI 178
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 2553857580 540 INALASAGTSVVVTTHFLEEA-EYCDRFLIQDAGKVLALGTPREVKQRAAVL 590
Cdd:PRK13638 179 IRRIVAQGNHVIISSHDIDLIyEISDAVYVLRQGQILTHGAPGEVFACTEAM 230
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
31-231 |
1.40e-16 |
|
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits of nitrate transport in bacteria and archaea. This protein belongs to the ATP-binding cassette (ABC) superfamily. It is thought that the two subunits encoded by ntrC and ntrD form the binding surface for interaction with ATP. This model is restricted in identifying ATP binding subunit associated with the nitrate transport. Nitrate assimilation is aided by other proteins derived from the operon which among others include products of ntrA - a regulatory protein; ntrB - a hydropbobic transmembrane permease and narB - a reductase. [Transport and binding proteins, Anions, Transport and binding proteins, Other]
Pssm-ID: 130252 [Multi-domain] Cd Length: 230 Bit Score: 79.43 E-value: 1.40e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857580 31 VDGISLKAGGAEasdrLIALVGPDGAGKSTFMRLLCGLEAPDEGRLSVLG---TTPDPDNedfttRIAFmpQTLGLYKTL 107
Cdd:TIGR01184 1 LKGVNLTIQQGE----FISLIGHSGCGKSTLLNLISGLAQPTSGGVILEGkqiTEPGPDR-----MVVF--QNYSLLPWL 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857580 108 SCREN--LEVFAGLRGFEGEadgaaglERR--IAELLSMTGLAGFEERQAGKLSGGMKQKLALASALLRIPDLLLLDEPT 183
Cdd:TIGR01184 70 TVRENiaLAVDRVLPDLSKS-------ERRaiVEEHIALVGLTEAADKRPGQLSGGMKQRVAIARALSIRPKVLLLDEPF 142
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 2553857580 184 VGVDPLSRRELWSVVRRMLADTPMTCVFSTAYLEEAE-AADRVLLFESG 231
Cdd:TIGR01184 143 GALDALTRGNLQEELMQIWEEHRVTVLMVTHDVDEALlLSDRVVMLTNG 191
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
33-203 |
1.47e-16 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 78.76 E-value: 1.47e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857580 33 GISLKAGGAEAsdrlIALVGPDGAGKSTFMRLLCGLEAPDEGRLSVLGttPDPDNEDFTTRIAFMPQTLGLYKTLSCREN 112
Cdd:PRK13539 20 GLSFTLAAGEA----LVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDG--GDIDDPDVAEACHYLGHRNAMKPALTVAEN 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857580 113 LEVFAGLRGfegeadgaaGLERRIAELLSMTGLAGFEERQAGKLSGGMKQKLALASALLRIPDLLLLDEPTVGVDPLSRR 192
Cdd:PRK13539 94 LEFWAAFLG---------GEELDIAAALEAVGLAPLAHLPFGYLSAGQKRRVALARLLVSNRPIWILDEPTAALDAAAVA 164
|
170
....*....|.
gi 2553857580 193 ELWSVVRRMLA 203
Cdd:PRK13539 165 LFAELIRAHLA 175
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
3-240 |
1.66e-16 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 81.81 E-value: 1.66e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857580 3 KASAPAIRLEGVVKTFPNpldaarpIRAVDGISLKAGGAEasdrLIALVGPDGAGKSTFMRLLCGLEAPDEGRLsVLGTT 82
Cdd:PRK11607 14 KALTPLLEIRNLTKSFDG-------QHAVDDVSLTIYKGE----IFALLGASGCGKSTLLRMLAGFEQPTAGQI-MLDGV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857580 83 PDPDNEDFTTRIAFMPQTLGLYKTLSCRENLEVfaglrGFEGEADGAAGLERRIAELLSMTGLAGFEERQAGKLSGGMKQ 162
Cdd:PRK11607 82 DLSHVPPYQRPINMMFQSYALFPHMTVEQNIAF-----GLKQDKLPKAEIASRVNEMLGLVHMQEFAKRKPHQLSGGQRQ 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2553857580 163 KLALASALLRIPDLLLLDEPTVGVDPLSRRELWSVVRRMLADTPMTCVFSTAYLEEA-EAADRVLLFESGRIIADENPQ 240
Cdd:PRK11607 157 RVALARSLAKRPKLLLLDEPMGALDKKLRDRMQLEVVDILERVGVTCVMVTHDQEEAmTMAGRIAIMNRGKFVQIGEPE 235
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
367-588 |
1.72e-16 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 79.03 E-value: 1.72e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857580 367 IRADGIARKFGNFVAVADtsFEVRRGEIFGLLGPNGAGKTTTFRMLCGLLVPSKGQIEVAGYDLrTAKAGARARIGYVAQ 446
Cdd:COG3840 2 LRLDDLTYRYGDFPLRFD--LTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILWNGQDL-TALPPAERPVSMLFQ 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857580 447 KFSLYGKLSVEQNLrYFGRSYGF-FGQALQDRIDASLEDFGLTDRRDTTAGSLSFGAKQDLSMACGLIHSPEILFLDEAT 525
Cdd:COG3840 79 ENNLFPHLTVAQNI-GLGLRPGLkLTAEQRAQVEQALERVGLAGLLDRLPGQLSGGQRQRVALARCLVRKRPILLLDEPF 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2553857580 526 SGADLASRRAFWRRINALASA-GTSVVVTTHFLEEAE-YCDRFLIQDAGKVLALGTPREVKQRAA 588
Cdd:COG3840 158 SALDPALRQEMLDLVDELCRErGLTVLMVTHDPEDAArIADRVLLVADGRIAADGPTAALLDGEP 222
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
30-244 |
1.83e-16 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 80.12 E-value: 1.83e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857580 30 AVDGISLKAGGAEasdrLIALVGPDGAGKSTFMRLLCGLEAPDEGRLSVLGTTPD-------------------PDNEDF 90
Cdd:PRK13639 17 ALKGINFKAEKGE----MVALLGPNGAGKSTLFLHFNGILKPTSGEVLIKGEPIKydkksllevrktvgivfqnPDDQLF 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857580 91 TTR----IAFMPQTLGLYKTlscrenlEVfaglrgfegeadgaaglERRIAELLSMTGLAGFEERQAGKLSGGMKQKLAL 166
Cdd:PRK13639 93 APTveedVAFGPLNLGLSKE-------EV-----------------EKRVKEALKAVGMEGFENKPPHHLSGGQKKRVAI 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2553857580 167 ASALLRIPDLLLLDEPTVGVDPLSRRELWSVVRRmLADTPMTCVFSTAYLEEAEA-ADRVLLFESGRIIADENPQSFIS 244
Cdd:PRK13639 149 AGILAMKPEIIVLDEPTSGLDPMGASQIMKLLYD-LNKEGITIIISTHDVDLVPVyADKVYVMSDGKIIKEGTPKEVFS 226
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
7-582 |
2.14e-16 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 82.52 E-value: 2.14e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857580 7 PAIRLEGVVKTFPnpldaarPIRAVDGISLKAGGAEASdrliALVGPDGAGKSTFMRLLCGLEAPDEGRLSVLGTTPDPD 86
Cdd:PRK09700 4 PYISMAGIGKSFG-------PVHALKSVNLTVYPGEIH----ALLGENGAGKSTLMKVLSGIHEPTKGTITINNINYNKL 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857580 87 NEDFTTR--IAFMPQTLGLYKTLSCRENLevFAG---LRGFEG-EADGAAGLERRIAELLSMTGLAGFEERQAGKLSGGM 160
Cdd:PRK09700 73 DHKLAAQlgIGIIYQELSVIDELTVLENL--YIGrhlTKKVCGvNIIDWREMRVRAAMMLLRVGLKVDLDEKVANLSISH 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857580 161 KQKLALASALLRIPDLLLLDEPTVGVDPLSRRELWSVVRRMLADTPMTCVFSTAYLEEAEAADRVLLFESG-----RIIA 235
Cdd:PRK09700 151 KQMLEIAKTLMLDAKVIIMDEPTSSLTNKEVDYLFLIMNQLRKEGTAIVYISHKLAEIRRICDRYTVMKDGssvcsGMVS 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857580 236 DENPQSFISRAKGRTyllpLANRaehdaqmlcrrlseetaatrsdalfldivprmggaaattlaptlpvkdarvpsgFIP 315
Cdd:PRK09700 231 DVSNDDIVRLMVGRE----LQNR------------------------------------------------------FNA 252
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857580 316 RQPSLEDayalltfprapktanhlasppsdasgalaasaasaddtAERPVVIRADGIARKfgNFVAVADTSFEVRRGEIF 395
Cdd:PRK09700 253 MKENVSN--------------------------------------LAHETVFEVRNVTSR--DRKKVRDISFSVCRGEIL 292
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857580 396 GLLGPNGAGKTTTFRMLCGLLVPSKGQIEVAGYDL--RTAKAGARARIGYVAQ---------KFSLYGKLSVEQNLRY-- 462
Cdd:PRK09700 293 GFAGLVGSGRTELMNCLFGVDKRAGGEIRLNGKDIspRSPLDAVKKGMAYITEsrrdngffpNFSIAQNMAISRSLKDgg 372
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857580 463 FGRSYGFFGQALQDRI-DASLEDFGLT-DRRDTTAGSLSFGAKQDLSMACGLIHSPEILFLDEATSGADLASRRAFWRRI 540
Cdd:PRK09700 373 YKGAMGLFHEVDEQRTaENQRELLALKcHSVNQNITELSGGNQQKVLISKWLCCCPEVIIFDEPTRGIDVGAKAEIYKVM 452
|
570 580 590 600
....*....|....*....|....*....|....*....|...
gi 2553857580 541 NALASAGTSV-VVTTHFLEEAEYCDRFLIQDAGKVLALGTPRE 582
Cdd:PRK09700 453 RQLADDGKVIlMVSSELPEIITVCDRIAVFCEGRLTQILTNRD 495
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
366-555 |
2.20e-16 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 78.38 E-value: 2.20e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857580 366 VIRADGIARKF-GNFVAVADTSFEVRRGEIFGLLGPNGAGKTTTFRMLCGLLVPSKGQIEVAGYDLRTAKAGA----RAR 440
Cdd:PRK10908 1 MIRFEHVSKAYlGGRQALQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDITRLKNREvpflRRQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857580 441 IGYVAQKFSLYGKLSVEQNLRYFGRSYGFFGQALQDRIDASLEDFGLTDRRDTTAGSLSFGAKQDLSMACGLIHSPEILF 520
Cdd:PRK10908 81 IGMIFQDHHLLMDRTVYDNVAIPLIIAGASGDDIRRRVSAALDKVGLLDKAKNFPIQLSGGEQQRVGIARAVVNKPAVLL 160
|
170 180 190
....*....|....*....|....*....|....*
gi 2553857580 521 LDEATSGADLASRRAFWRRINALASAGTSVVVTTH 555
Cdd:PRK10908 161 ADEPTGNLDDALSEGILRLFEEFNRVGVTVLMATH 195
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
386-555 |
2.40e-16 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 77.92 E-value: 2.40e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857580 386 SFEVRRGEIFGLLGPNGAGKTTTFRMLCGLLVPSKGQIEVAGYDLRTAKAGARARIGYVAQKFSLYGKLSVEQNLRYFGR 465
Cdd:PRK13538 21 SFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVLWQGEPIRRQRDEYHQDLLYLGHQPGIKTELTALENLRFYQR 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857580 466 sygFFGQALQDRIDASLEDFGLTDRRDTTAGSLSFGAKQDLSMACGLIHSPEILFLDEATSGADLASRRAFWRRINALAS 545
Cdd:PRK13538 101 ---LHGPGDDEALWEALAQVGLAGFEDVPVRQLSAGQQRRVALARLWLTRAPLWILDEPFTAIDKQGVARLEALLAQHAE 177
|
170
....*....|
gi 2553857580 546 AGTSVVVTTH 555
Cdd:PRK13538 178 QGGMVILTTH 187
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
365-595 |
3.08e-16 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 78.38 E-value: 3.08e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857580 365 VVIRADGIARKFGNFVAVADTSFEVRRGEIFGLLGPNGAGKTTTFRMLCGLLVPSKGQIEVAGYDL---RTAKAgARARI 441
Cdd:PRK11614 4 VMLSFDKVSAHYGKIQALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDGKDItdwQTAKI-MREAV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857580 442 GYVAQKFSLYGKLSVEQNLRYfgrsYGFFG--QALQDRIDASLEDFG-LTDRRDTTAGSLSFGAKQDLSMACGLIHSPEI 518
Cdd:PRK11614 83 AIVPEGRRVFSRMTVEENLAM----GGFFAerDQFQERIKWVYELFPrLHERRIQRAGTMSGGEQQMLAIGRALMSQPRL 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2553857580 519 LFLDEATSGADLASRRAFWRRINALASAGTSVVVTTHFLEEA-EYCDRFLIQDAGKVLALGTPREVKQRAAVLSAVSG 595
Cdd:PRK11614 159 LLLDEPSLGLAPIIIQQIFDTIEQLREQGMTIFLVEQNANQAlKLADRGYVLENGHVVLEDTGDALLANEAVRSAYLG 236
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
9-237 |
3.40e-16 |
|
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: 77.96 E-value: 3.40e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857580 9 IRLEGVVKTFP---------------NPLDAARPIRAVDGISLKAGGAEAsdrlIALVGPDGAGKSTFMRLLCGLEAPDE 73
Cdd:cd03220 1 IELENVSKSYPtykggssslkklgilGRKGEVGEFWALKDVSFEVPRGER----IGLIGRNGAGKSTLLRLLAGIYPPDS 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857580 74 GRLSVLGTTpdpdnedfTTRIAFmpqTLGLYKTLSCRENLEVFAGLRGFEGEADGAaglerRIAELLSMTGLAGFEERQA 153
Cdd:cd03220 77 GTVTVRGRV--------SSLLGL---GGGFNPELTGRENIYLNGRLLGLSRKEIDE-----KIDEIIEFSELGDFIDLPV 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857580 154 GKLSGGMKQKLALASALLRIPDLLLLDEPTVGVDPLSRRELWSVVRRMLADTPMTCVFSTAYLEEAEAADRVLLFESGRI 233
Cdd:cd03220 141 KTYSSGMKARLAFAIATALEPDILLIDEVLAVGDAAFQEKCQRRLRELLKQGKTVILVSHDPSSIKRLCDRALVLEKGKI 220
|
....
gi 2553857580 234 IADE 237
Cdd:cd03220 221 RFDG 224
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
367-569 |
4.89e-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: 75.18 E-value: 4.89e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857580 367 IRADGIARKFGNFVAVADTSFEVRRGEIFGLLGPNGAGKTTTFRMLCGLLVPSKGQIEVagydlrtakaGARARIGYVAQ 446
Cdd:cd03221 1 IELENLSKTYGGKLLLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIVTW----------GSTVKIGYFEQ 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857580 447 kfslygklsveqnlryfgrsygffgqalqdridasledfgltdrrdttagsLSFGAKQDLSMACGLIHSPEILFLDEATS 526
Cdd:cd03221 71 ---------------------------------------------------LSGGEKMRLALAKLLLENPNLLLLDEPTN 99
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 2553857580 527 GADLASRRAFwrrINALASAGTSVVVTTHfleeaeycDRFLIQ 569
Cdd:cd03221 100 HLDLESIEAL---EEALKEYPGTVILVSH--------DRYFLD 131
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
31-240 |
5.12e-16 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 78.27 E-value: 5.12e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857580 31 VDGISLKAGGAEasdrLIALVGPDGAGKSTFMRLLCGLEAPDEGRLSVLGTtpdpDNEDFTT-----RIAFMPQTLGLYK 105
Cdd:PRK13548 18 LDDVSLTLRPGE----VVAILGPNGAGKSTLLRALSGELSPDSGEVRLNGR----PLADWSPaelarRRAVLPQHSSLSF 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857580 106 TLSCRENLEVFAGLRGFEGEADGAAglerrIAELLSMTGLAGFEERQAGKLSGGMKQKLALA------SALLRIPDLLLL 179
Cdd:PRK13548 90 PFTVEEVVAMGRAPHGLSRAEDDAL-----VAAALAQVDLAHLAGRDYPQLSGGEQQRVQLArvlaqlWEPDGPPRWLLL 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2553857580 180 DEPTVGVDPLSRRELWSVVRRMLADTPMT--CVF-----STAYleeaeaADRVLLFESGRIIADENPQ 240
Cdd:PRK13548 165 DEPTSALDLAHQHHVLRLARQLAHERGLAviVVLhdlnlAARY------ADRIVLLHQGRLVADGTPA 226
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
362-583 |
6.52e-16 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 78.10 E-value: 6.52e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857580 362 ERPVVIRADGIARKFGNFVAVADTSFEVRRGEIFGLLGPNGAGKTTTFRMLCGLLVPSKGQIEVAGYDLR--TAKAGARa 439
Cdd:PRK10253 3 ESVARLRGEQLTLGYGKYTVAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIQhyASKEVAR- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857580 440 RIGYVAQKFSLYGKLSVeQNLRYFGRS-----YGFFGQALQDRIDASLEDFGLTDRRDTTAGSLSFGAKQDLSMACGLIH 514
Cdd:PRK10253 82 RIGLLAQNATTPGDITV-QELVARGRYphqplFTRWRKEDEEAVTKAMQATGITHLADQSVDTLSGGQRQRAWIAMVLAQ 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2553857580 515 SPEILFLDEATSGADLASRRAFWRRINAL-ASAGTSVVVTTHFLEEA-EYCDRFLIQDAGKVLALGTPREV 583
Cdd:PRK10253 161 ETAIMLLDEPTTWLDISHQIDLLELLSELnREKGYTLAAVLHDLNQAcRYASHLIALREGKIVAQGAPKEI 231
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
49-260 |
7.52e-16 |
|
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: 79.37 E-value: 7.52e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857580 49 ALVGPDGAGKSTFMRLLCGLEAPDEGRLSVLGTT-PDPDNEDFTT----RIAFMPQTLGLYKTLSCRENLEvfAGLRgFE 123
Cdd:COG4148 29 ALFGPSGSGKTTLLRAIAGLERPDSGRIRLGGEVlQDSARGIFLPphrrRIGYVFQEARLFPHLSVRGNLL--YGRK-RA 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857580 124 GEADGAAGLERrIAELLsmtGLAGFEERQAGKLSGGMKQKLALASALLRIPDLLLLDEPTVGVDPLSRRELWSVVRRmLA 203
Cdd:COG4148 106 PRAERRISFDE-VVELL---GIGHLLDRRPATLSGGERQRVAIGRALLSSPRLLLMDEPLAALDLARKAEILPYLER-LR 180
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2553857580 204 D---TPMtcVFSTAYLEEAEA-ADRVLLFESGRIIADENPQSFISRAkgrtYLLPLANRAE 260
Cdd:COG4148 181 DeldIPI--LYVSHSLDEVARlADHVVLLEQGRVVASGPLAEVLSRP----DLLPLAGGEE 235
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
30-247 |
9.51e-16 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 77.82 E-value: 9.51e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857580 30 AVDGISLKAGGAEasdrLIALVGPDGAGKSTFMRLLCGLEAPDEGRLSVLG-TTPD-----------------PDNEDFT 91
Cdd:PRK13633 25 ALDDVNLEVKKGE----FLVILGRNGSGKSTIAKHMNALLIPSEGKVYVDGlDTSDeenlwdirnkagmvfqnPDNQIVA 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857580 92 T----RIAFMPQTLGLyktlscrENLEVfaglrgfegeadgaaglERRIAELLSMTGLAGFEERQAGKLSGGMKQKLALA 167
Cdd:PRK13633 101 TiveeDVAFGPENLGI-------PPEEI-----------------RERVDESLKKVGMYEYRRHAPHLLSGGQKQRVAIA 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857580 168 SALLRIPDLLLLDEPTVGVDPLSRRELWSVVRRMLADTPMTCVFSTAYLEEAEAADRVLLFESGRIIADENPQSFISRAK 247
Cdd:PRK13633 157 GILAMRPECIIFDEPTAMLDPSGRREVVNTIKELNKKYGITIILITHYMEEAVEADRIIVMDSGKVVMEGTPKEIFKEVE 236
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
48-234 |
9.67e-16 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 76.98 E-value: 9.67e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857580 48 IALVGPDGAGKSTFMRLLCGLEAPDEGRLSVLGTTPDPDNEDFTTRIAFMPQTLG-------LYKTLSCRENLeVFAGLR 120
Cdd:COG4161 31 LVLLGPSGAGKSSLLRVLNLLETPDSGQLNIAGHQFDFSQKPSEKAIRLLRQKVGmvfqqynLWPHLTVMENL-IEAPCK 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857580 121 gfegeadgAAGLERRIA-----ELLSMTGLAGFEERQAGKLSGGMKQKLALASALLRIPDLLLLDEPTVGVDPLSRRELW 195
Cdd:COG4161 110 --------VLGLSKEQArekamKLLARLRLTDKADRFPLHLSGGQQQRVAIARALMMEPQVLLFDEPTAALDPEITAQVV 181
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 2553857580 196 SVVRRmLADTPMTCVFSTAYLEEA-EAADRVLLFESGRII 234
Cdd:COG4161 182 EIIRE-LSQTGITQVIVTHEVEFArKVASQVVYMEKGRII 220
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
364-529 |
1.13e-15 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 77.38 E-value: 1.13e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857580 364 PVVIRADGIARKFGNFVAVADTSFEVRRGEIFGLLGPNGAGKTTTFRMLCGL--LVPS---KGQIEVAGYDLRTAK---A 435
Cdd:COG1117 9 EPKIEVRNLNVYYGDKQALKDINLDIPENKVTALIGPSGCGKSTLLRCLNRMndLIPGarvEGEILLDGEDIYDPDvdvV 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857580 436 GARARIGYVAQK---FSLygklSVEQN----LRYFG-RSygffGQALQDRIDASLEDFGL----TDRRDTTAGSLSFGAK 503
Cdd:COG1117 89 ELRRRVGMVFQKpnpFPK----SIYDNvaygLRLHGiKS----KSELDEIVEESLRKAALwdevKDRLKKSALGLSGGQQ 160
|
170 180
....*....|....*....|....*.
gi 2553857580 504 QDLSMACGLIHSPEILFLDEATSGAD 529
Cdd:COG1117 161 QRLCIARALAVEPEVLLMDEPTSALD 186
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
384-580 |
1.18e-15 |
|
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C is also known as MRP (multidrug resistance-associated protein). Some of the MRP members have five additional transmembrane segments in their N-terminus, but the function of these additional membrane-spanning domains is not clear. The MRP was found in the multidrug-resistance lung cancer cell in which p-glycoprotein was not overexpressed. MRP exports glutathione by drug stimulation, as well as, certain substrates in conjugated forms with anions, such as glutathione, glucuronate, and sulfate.
Pssm-ID: 213211 [Multi-domain] Cd Length: 221 Bit Score: 76.38 E-value: 1.18e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857580 384 DTSFEVRRGEIFGLLGPNGAGKTTTFRMLCGLLVPSKGQIEVAGYDLRT-AKAGARARIGYVAQK---FSlyGklSVEQN 459
Cdd:cd03244 22 NISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSILIDGVDISKiGLHDLRSRISIIPQDpvlFS--G--TIRSN 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857580 460 LryfgrsyGFFGQALQDRIDASLEDFGLTDRRDTTAGSL-----------SFGAKQDLSMACGLIHSPEILFLDEATSGA 528
Cdd:cd03244 98 L-------DPFGEYSDEELWQALERVGLKEFVESLPGGLdtvveeggenlSVGQRQLLCLARALLRKSKILVLDEATASV 170
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857580 529 DLAS--------RRAFwrrinalasAGTSVVVTTHFLEEAEYCDRFLIQDAGKVLALGTP 580
Cdd:cd03244 171 DPETdaliqktiREAF---------KDCTVLTIAHRLDTIIDSDRILVLDKGRVVEFDSP 221
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
2-226 |
1.41e-15 |
|
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: 80.02 E-value: 1.41e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857580 2 TKASAPAIRLEGVVKTFPNPLDAARPIravdGISLKAGgaeasdRLIALVGPDGAGKSTFMRLLCGLEAPDEGRLSVLG- 80
Cdd:TIGR02857 315 TAAPASSLEFSGVSVAYPGRRPALRPV----SFTVPPG------ERVALVGPSGAGKSTLLNLLLGFVDPTEGSIAVNGv 384
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857580 81 TTPDPDNEDFTTRIAFMPQTLGLYKTlSCRENLevfaglRGFEGEADGAAglerrIAELLSMTGLAGFE-------ERQA 153
Cdd:TIGR02857 385 PLADADADSWRDQIAWVPQHPFLFAG-TIAENI------RLARPDASDAE-----IREALERAGLDEFVaalpqglDTPI 452
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2553857580 154 GK----LSGGMKQKLALASALLRIPDLLLLDEPTVGVDPLSRRELWSVVRRmLADTpMTCVFSTAYLEEAEAADRVL 226
Cdd:TIGR02857 453 GEggagLSGGQAQRLALARAFLRDAPLLLLDEPTAHLDAETEAEVLEALRA-LAQG-RTVLLVTHRLALAALADRIV 527
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
384-583 |
1.52e-15 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 77.01 E-value: 1.52e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857580 384 DTSFEVRRGEIFGLLGPNGAGKTTTFRMLCGLLVPSKGQIEVAGYDLRTAK-------AGARARIGYVAQKFSLYGKLSV 456
Cdd:PRK14246 28 DITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLIEIYDSKIKVDGKVLYFGKdifqidaIKLRKEVGMVFQQPNPFPHLSI 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857580 457 EQNLRYFGRSYGFFGQ-ALQDRIDASLEDFGL----TDRRDTTAGSLSFGAKQDLSMACGLIHSPEILFLDEATSGADLA 531
Cdd:PRK14246 108 YDNIAYPLKSHGIKEKrEIKKIVEECLRKVGLwkevYDRLNSPASQLSGGQQQRLTIARALALKPKVLLMDEPTSMIDIV 187
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 2553857580 532 SRRAFWRRINALASAGTSVVVTTHFLEEAEYCDRFLIQDAGKVLALGTPREV 583
Cdd:PRK14246 188 NSQAIEKLITELKNEIAIVIVSHNPQQVARVADYVAFLYNGELVEWGSSNEI 239
|
|
| COG4559 |
COG4559 |
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism]; |
31-241 |
2.06e-15 |
|
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443620 [Multi-domain] Cd Length: 258 Bit Score: 76.31 E-value: 2.06e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857580 31 VDGISLKAGGAEasdrLIALVGPDGAGKSTFMRLLCGLEAPDEGRLSVLGTtpdpDNEDFTT-----RIAFMPQTLGLYK 105
Cdd:COG4559 17 LDDVSLTLRPGE----LTAIIGPNGAGKSTLLKLLTGELTPSSGEVRLNGR----PLAAWSPwelarRRAVLPQHSSLAF 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857580 106 TLSCREnlevFAGLrGFEGEADGAAGLERRIAELLSMTGLAGFEERQAGKLSGGMKQKLALA-------SALLRIPDLLL 178
Cdd:COG4559 89 PFTVEE----VVAL-GRAPHGSSAAQDRQIVREALALVGLAHLAGRSYQTLSGGEQQRVQLArvlaqlwEPVDGGPRWLF 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2553857580 179 LDEPTVGVDPLSRRELWSVVRRmLADTPMTCVfstAYLEE----AEAADRVLLFESGRIIADENPQS 241
Cdd:COG4559 164 LDEPTSALDLAHQHAVLRLARQ-LARRGGGVV---AVLHDlnlaAQYADRILLLHQGRLVAQGTPEE 226
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
374-583 |
2.40e-15 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 76.16 E-value: 2.40e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857580 374 RKFGNFVAVADTSFEVRRGEIFGLLGPNGAGKTTTFRMLCGLLVPSKGQIEVAGYDLRTAKAG--------------ARA 439
Cdd:PRK10619 13 KRYGEHEVLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNGQTINLVRDKdgqlkvadknqlrlLRT 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857580 440 RIGYVAQKFSLYGKLSVEQN-LRYFGRSYGFFGQALQDRIDASLEDFGLTDR-RDTTAGSLSFGAKQDLSMACGLIHSPE 517
Cdd:PRK10619 93 RLTMVFQHFNLWSHMTVLENvMEAPIQVLGLSKQEARERAVKYLAKVGIDERaQGKYPVHLSGGQQQRVSIARALAMEPE 172
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2553857580 518 ILFLDEATSGADLASRRAFWRRINALASAGTSVVVTTHFLEEAEYCDRFLI-QDAGKVLALGTPREV 583
Cdd:PRK10619 173 VLLFDEPTSALDPELVGEVLRIMQQLAEEGKTMVVVTHEMGFARHVSSHVIfLHQGKIEEEGAPEQL 239
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
387-555 |
2.50e-15 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 75.27 E-value: 2.50e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857580 387 FEVRRGEIFGLLGPNGAGKTTTFRMLCGLLVPSKGQIEVAGYDLRTAKagaRAR-IGYVAQKFSLYGKLSVEQNLRYFGr 465
Cdd:PRK13543 32 FHVDAGEALLVQGDNGAGKTTLLRVLAGLLHVESGQIQIDGKTATRGD---RSRfMAYLGHLPGLKADLSTLENLHFLC- 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857580 466 syGFFGQALQDRIDASLEDFGLTDRRDTTAGSLSFGAKQDLSMACGLIHSPEILFLDEATSGADLASRRAFWRRINALAS 545
Cdd:PRK13543 108 --GLHGRRAKQMPGSALAIVGLAGYEDTLVRQLSAGQKKRLALARLWLSPAPLWLLDEPYANLDLEGITLVNRMISAHLR 185
|
170
....*....|
gi 2553857580 546 AGTSVVVTTH 555
Cdd:PRK13543 186 GGGAALVTTH 195
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
9-264 |
2.82e-15 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 76.20 E-value: 2.82e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857580 9 IRLEGVVKTFpnplDAARPIRAVDgISLKAGgaeasdRLIALVGPDGAGKSTFMRLLCGLEAPD---EGRLSVLGTTPD- 84
Cdd:PRK09984 5 IRVEKLAKTF----NQHQALHAVD-LNIHHG------EMVALLGPSGSGKSTLLRHLSGLITGDksaGSHIELLGRTVQr 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857580 85 -----PDNEDFTTRIAFMPQTLGLYKTLSCRENLEVFA---------GLRGFEGEAdgaaglERRIAELLSMTGLAGFEE 150
Cdd:PRK09984 74 egrlaRDIRKSRANTGYIFQQFNLVNRLSVLENVLIGAlgstpfwrtCFSWFTREQ------KQRALQALTRVGMVHFAH 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857580 151 RQAGKLSGGMKQKLALASALLRIPDLLLLDEPTVGVDPLSRRELWSVVRRMLADTPMTCVFSTAYLEEA-EAADRVLLFE 229
Cdd:PRK09984 148 QRVSTLSGGQQQRVAIARALMQQAKVILADEPIASLDPESARIVMDTLRDINQNDGITVVVTLHQVDYAlRYCERIVALR 227
|
250 260 270
....*....|....*....|....*....|....*
gi 2553857580 230 SGRIIADENPQSFISRAKGRTYllPLANRAEHDAQ 264
Cdd:PRK09984 228 QGHVFYDGSSQQFDNERFDHLY--RSINRVEENAK 260
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
6-240 |
3.29e-15 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 79.00 E-value: 3.29e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857580 6 APAIRLEGVVKTFPNpldAARPIRAVDGISLKAGGAEasdrLIALVGPDGAGKSTFMRLLCGLEAPDEGRLSVLGTTPDP 85
Cdd:PRK10535 2 TALLELKDIRRSYPS---GEEQVEVLKGISLDIYAGE----MVAIVGASGSGKSTLMNILGCLDKPTSGTYRVAGQDVAT 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857580 86 DNEDFTTRI-----AFMPQTLGLYKTLSCRENLEVFAGLRGFEGEADgaaglERRIAELLSMTGLAGFEERQAGKLSGGM 160
Cdd:PRK10535 75 LDADALAQLrrehfGFIFQRYHLLSHLTAAQNVEVPAVYAGLERKQR-----LLRAQELLQRLGLEDRVEYQPSQLSGGQ 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857580 161 KQKLALASALLRIPDLLLLDEPTVGVDPLSRRELWSVVRRmLADTPMTCVFSTAYLEEAEAADRVLLFESGRIIADENPQ 240
Cdd:PRK10535 150 QQRVSIARALMNGGQVILADEPTGALDSHSGEEVMAILHQ-LRDRGHTVIIVTHDPQVAAQAERVIEIRDGEIVRNPPAQ 228
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
7-239 |
3.69e-15 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 75.67 E-value: 3.69e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857580 7 PAIRLEGVVKTFPNPldaARPIRAVDGISLKAGgaeaSDRLIALVGPDGAGKSTFMRLLCGLEAPDEGRLSVLG---TTP 83
Cdd:COG4525 2 SMLTVRHVSVRYPGG---GQPQPALQDVSLTIE----SGEFVVALGASGCGKTTLLNLIAGFLAPSSGEITLDGvpvTGP 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857580 84 DPDNedfttriAFMPQTLGLYKTLSCRENLEVFAGLRGFegeadGAAGLERRIAELLSMTGLAGFEERQAGKLSGGMKQK 163
Cdd:COG4525 75 GADR-------GVVFQKDALLPWLNVLDNVAFGLRLRGV-----PKAERRARAEELLALVGLADFARRRIWQLSGGMRQR 142
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2553857580 164 LALASALLRIPDLLLLDEPTVGVDPLSRRELWSVVRRMLADTPMTCVFSTAYLEEA--EAADRVLLFES-GRIIADENP 239
Cdd:COG4525 143 VGIARALAADPRFLLMDEPFGALDALTREQMQELLLDVWQRTGKGVFLITHSVEEAlfLATRLVVMSPGpGRIVERLEL 221
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
49-241 |
4.31e-15 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 75.94 E-value: 4.31e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857580 49 ALVGPDGAGKSTFMRLLCGLEAPDEGRLSVLGT--TPDPDNEDfttrIAFMPQTLGLYKTLSCRENLE------VFAGLR 120
Cdd:PRK13649 37 AFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDDTliTSTSKNKD----IKQIRKKVGLVFQFPESQLFEetvlkdVAFGPQ 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857580 121 GFEGEADGAAGLERriaELLSMTGLA-GFEERQAGKLSGGMKQKLALASALLRIPDLLLLDEPTVGVDPLSRRELWSVVR 199
Cdd:PRK13649 113 NFGVSQEEAEALAR---EKLALVGISeSLFEKNPFELSGGQMRRVAIAGILAMEPKILVLDEPTAGLDPKGRKELMTLFK 189
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 2553857580 200 RmLADTPMTCVFSTAYLEE-AEAADRVLLFESGRIIADENPQS 241
Cdd:PRK13649 190 K-LHQSGMTIVLVTHLMDDvANYADFVYVLEKGKLVLSGKPKD 231
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
49-236 |
4.78e-15 |
|
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: 75.12 E-value: 4.78e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857580 49 ALVGPDGAGKSTFMRLLCGLEAPDEG-RLSVLGTTPDPDN-EDFTTRIAFMPQTLGLY--KTLSCREnleV-----FA-- 117
Cdd:COG1119 33 AILGPNGAGKSTLLSLITGDLPPTYGnDVRLFGERRGGEDvWELRKRIGLVSPALQLRfpRDETVLD---VvlsgfFDsi 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857580 118 GLRGFEGEADgaaglERRIAELLSMTGLAGFEERQAGKLSGGMKQKLALASALLRIPDLLLLDEPTVGVDPLSRRELWSV 197
Cdd:COG1119 110 GLYREPTDEQ-----RERARELLELLGLAHLADRPFGTLSQGEQRRVLIARALVKDPELLILDEPTAGLDLGARELLLAL 184
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 2553857580 198 VRRMLADTPMTCVFSTAYLEEA-EAADRVLLFESGRIIAD 236
Cdd:COG1119 185 LDKLAAEGAPTLVLVTHHVEEIpPGITHVLLLKDGRVVAA 224
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
381-590 |
6.08e-15 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 75.55 E-value: 6.08e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857580 381 AVADTSFEVRRGEIFGLLGPNGAGKTTTFRMLCGLLVPSKGQIEVAGYDLRTAKAGA-----RARIGYVAQ--KFSLYGK 453
Cdd:PRK13649 22 ALFDVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDDTLITSTSKNKdikqiRKKVGLVFQfpESQLFEE 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857580 454 lSVEQNLRYFGRSYGFFGQALQDRIDASLEDFGLTDR-RDTTAGSLSFGAKQDLSMACGLIHSPEILFLDEATSGADLAS 532
Cdd:PRK13649 102 -TVLKDVAFGPQNFGVSQEEAEALAREKLALVGISESlFEKNPFELSGGQMRRVAIAGILAMEPKILVLDEPTAGLDPKG 180
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 2553857580 533 RRAFWRRINALASAGTSVVVTTHFLEE-AEYCDRFLIQDAGKVLALGTPREVKQRAAVL 590
Cdd:PRK13649 181 RKELMTLFKKLHQSGMTIVLVTHLMDDvANYADFVYVLEKGKLVLSGKPKDIFQDVDFL 239
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
381-595 |
6.52e-15 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 75.30 E-value: 6.52e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857580 381 AVADTSFEVRRGEIFGLLGPNGAGKTTTFRMLCGLLVPSKGQIEVAGYDLRtaKAGARARIGYVAQKFSLYGKLSV-EQN 459
Cdd:PRK15056 22 ALRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKISILGQPTR--QALQKNLVAYVPQSEEVDWSFPVlVED 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857580 460 LRYFGRsYGFFG------QALQDRIDASLEDFGLTDRRDTTAGSLSFGAKQDLSMACGLIHSPEILFLDEATSGADLASR 533
Cdd:PRK15056 100 VVMMGR-YGHMGwlrrakKRDRQIVTAALARVDMVEFRHRQIGELSGGQKKRVFLARAIAQQGQVILLDEPFTGVDVKTE 178
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2553857580 534 RAFWRRINALASAGTSVVVTTHFLEE-AEYCDrFLIQDAGKVLALGtPREVKQRAAVLS-AVSG 595
Cdd:PRK15056 179 ARIISLLRELRDEGKTMLVSTHNLGSvTEFCD-YTVMVKGTVLASG-PTETTFTAENLElAFSG 240
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
365-560 |
6.57e-15 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 75.20 E-value: 6.57e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857580 365 VVIRADGIARKFGNFVAVADTSFEVRRGEIFGLLGPNGAGKTTTFRMLCGL--LVPS---KGQIEVAG---YDLRTAKAG 436
Cdd:PRK14243 9 TVLRTENLNVYYGSFLAVKNVWLDIPKNQITAFIGPSGCGKSTILRCFNRLndLIPGfrvEGKVTFHGknlYAPDVDPVE 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857580 437 ARARIGYVAQKFSLYGKlSVEQNLRYFGRSYGFFGQaLQDRIDASLEDFGL----TDRRDTTAGSLSFGAKQDLSMACGL 512
Cdd:PRK14243 89 VRRRIGMVFQKPNPFPK-SIYDNIAYGARINGYKGD-MDELVERSLRQAALwdevKDKLKQSGLSLSGGQQQRLCIARAI 166
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 2553857580 513 IHSPEILFLDEATSGADLASRRAFWRRINALASAGTSVVVtTHFLEEA 560
Cdd:PRK14243 167 AVQPEVILMDEPCSALDPISTLRIEELMHELKEQYTIIIV-THNMQQA 213
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
9-200 |
7.60e-15 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 74.30 E-value: 7.60e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857580 9 IRLEGVVKTFPNpldaaRPIraVDGISLKAGGAEAsdrlIALVGPDGAGKSTFMRLLCGLEAPDEGRLSVlgttpdpDNE 88
Cdd:COG1137 4 LEAENLVKSYGK-----RTV--VKDVSLEVNQGEI----VGLLGPNGAGKTTTFYMIVGLVKPDSGRIFL-------DGE 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857580 89 DFTT-----R----IAFMPQTLGLYKTLSCRENLEVFAGLRGFegeadGAAGLERRIAELLSMTGLAGFEERQAGKLSGG 159
Cdd:COG1137 66 DITHlpmhkRarlgIGYLPQEASIFRKLTVEDNILAVLELRKL-----SKKEREERLEELLEEFGITHLRKSKAYSLSGG 140
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 2553857580 160 MKQKLALASALLRIPDLLLLDEPTVGVDPLSRRELWSVVRR 200
Cdd:COG1137 141 ERRRVEIARALATNPKFILLDEPFAGVDPIAVADIQKIIRH 181
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
386-579 |
1.18e-14 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 77.19 E-value: 1.18e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857580 386 SFEVRRGEIFGLLGPNGAGKTTTFRMLCGLLvPSKGQIEVAGYDLRT-AKAGARARIGYVAQKFSLYgKLSVEQNLRyFG 464
Cdd:PRK11174 370 NFTLPAGQRIALVGPSGAGKTSLLNALLGFL-PYQGSLKINGIELRElDPESWRKHLSWVGQNPQLP-HGTLRDNVL-LG 446
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857580 465 RSygffgQALQDRIDASLE-----DF--GLTDRRDTT----AGSLSFGAKQDLSMACGLIHSPEILFLDEATSGADLASR 533
Cdd:PRK11174 447 NP-----DASDEQLQQALEnawvsEFlpLLPQGLDTPigdqAAGLSVGQAQRLALARALLQPCQLLLLDEPTASLDAHSE 521
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 2553857580 534 RAFWRRINAlASAGTSVVVTTHFLEEAEYCDRFLIQDAGKVLALGT 579
Cdd:PRK11174 522 QLVMQALNA-ASRRQTTLMVTHQLEDLAQWDQIWVMQDGQIVQQGD 566
|
|
| LPS_export_lptB |
TIGR04406 |
LPS export ABC transporter ATP-binding protein; Members of this fmaily are LptB, the ... |
30-252 |
2.02e-14 |
|
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: 73.08 E-value: 2.02e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857580 30 AVDGISLKAGGAEasdrLIALVGPDGAGKSTFMRLLCGLEAPDEGRLSVlgttpdpDNEDFTTR---------IAFMPQT 100
Cdd:TIGR04406 16 VVNDVSLSVKSGE----IVGLLGPNGAGKTTSFYMIVGLVRPDAGKILI-------DGQDITHLpmherarlgIGYLPQE 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857580 101 LGLYKTLSCRENLEVFAGLRgfegEADGAAGLERRIAELLSMTGLAGFEERQAGKLSGGMKQKLALASALLRIPDLLLLD 180
Cdd:TIGR04406 85 ASIFRKLTVEENIMAVLEIR----KDLDRAEREERLEALLEEFQISHLRDNKAMSLSGGERRRVEIARALATNPKFILLD 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2553857580 181 EPTVGVDPLSRRELWSVVrRMLADTPMTCVFSTAYLEEA-EAADRVLLFESGRIIADENPQSFISRAKGR-TYL 252
Cdd:TIGR04406 161 EPFAGVDPIAVGDIKKII-KHLKERGIGVLITDHNVRETlDICDRAYIISDGKVLAEGTPAEIVANEKVRrVYL 233
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
28-247 |
2.07e-14 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 73.97 E-value: 2.07e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857580 28 IRAVDGISLKAGGAEasdrLIALVGPDGAGKSTFMRLLCGLEAPDEGRLSVLGTTPDPDNE-DFTTRIAFMPQTLGLYKT 106
Cdd:PRK13642 20 VNQLNGVSFSITKGE----WVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDGELLTAENVwNLRRKIGMVFQNPDNQFV 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857580 107 LSCRENLEVFaglrGFEGEADGAAGLERRIAELLSMTGLAGFEERQAGKLSGGMKQKLALASALLRIPDLLLLDEPTVGV 186
Cdd:PRK13642 96 GATVEDDVAF----GMENQGIPREEMIKRVDEALLAVNMLDFKTREPARLSGGQKQRVAVAGIIALRPEIIILDESTSML 171
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2553857580 187 DPLSRRELWSVVRRMLADTPMTCVFSTAYLEEAEAADRVLLFESGRIIADENPQSFISRAK 247
Cdd:PRK13642 172 DPTGRQEIMRVIHEIKEKYQLTVLSITHDLDEAASSDRILVMKAGEIIKEAAPSELFATSE 232
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
384-578 |
2.42e-14 |
|
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ABC transporters homologous to the Drosophila white gene, which acts as a dimeric importer for eye pigment precursors. The eye pigmentation of Drosophila is developed from the synthesis and deposition in the cells of red pigments, which are synthesized from guanine, and brown pigments, which are synthesized from tryptophan. The pigment precursors are encoded by the white, brown, and scarlet genes, respectively. Evidence from genetic and biochemical studies suggest that the White and Brown proteins function as heterodimers to import guanine, while the White and Scarlet proteins function to import tryptophan. However, a recent study also suggests that White may be involved in the transport of a metabolite, such as 3-hydroxykynurenine, across intracellular membranes. Mammalian ABC transporters belonging to the White subfamily (ABCG1, ABCG5, and ABCG8) have been shown to be involved in the regulation of lipid-trafficking mechanisms in macrophages, hepatocytes, and intestinal mucosa cells. ABCG1 (ABC8), the human homolog of the Drosophila white gene is induced in monocyte-derived macrophages during cholesterol influx mediated by acetylated low-density lipoprotein. It is possible that human ABCG1 forms heterodimers with several heterologous partners.
Pssm-ID: 213201 [Multi-domain] Cd Length: 226 Bit Score: 72.69 E-value: 2.42e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857580 384 DTSFEVRRGEIFGLLGPNGAGKTTTFRMLCGLLVPSK---GQIEVAGYDLRTAKAgaRARIGYVAQKFSLYGKLSVEQNL 460
Cdd:cd03234 25 DVSLHVESGQVMAILGSSGSGKTTLLDAISGRVEGGGttsGQILFNGQPRKPDQF--QKCVAYVRQDDILLPGLTVRETL 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857580 461 RYFG--RSYGFFGQALQDRIDA--SLEDFGLTDRRDTTAGSLSFGAKQDLSMACGLIHSPEILFLDEATSGADlaSRRAF 536
Cdd:cd03234 103 TYTAilRLPRKSSDAIRKKRVEdvLLRDLALTRIGGNLVKGISGGERRRVSIAVQLLWDPKVLILDEPTSGLD--SFTAL 180
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 2553857580 537 --WRRINALASAGTSVVVTTH------FleeaEYCDRFLIQDAGKVLALG 578
Cdd:cd03234 181 nlVSTLSQLARRNRIVILTIHqprsdlF----RLFDRILLLSSGEIVYSG 226
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
392-595 |
3.14e-14 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 73.28 E-value: 3.14e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857580 392 GEIFGLLGPNGAGKTTTFRMLCGLLVPSKGQIEVAGYDLRTAKAGARAR-IGYVAQKFSLYGKLSVEQnLRYFGR----- 465
Cdd:PRK10575 37 GKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPLESWSSKAFARkVAYLPQQLPAAEGMTVRE-LVAIGRypwhg 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857580 466 SYGFFGQALQDRIDASLEDFGLTDRRDTTAGSLSFGAKQDLSMACGLIHSPEILFLDEATSGADLASRRAFWRRINALAS 545
Cdd:PRK10575 116 ALGRFGAADREKVEEAISLVGLKPLAHRLVDSLSGGERQRAWIAMLVAQDSRCLLLDEPTSALDIAHQVDVLALVHRLSQ 195
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 2553857580 546 A-GTSVVVTTHFLE-EAEYCDRFLIQDAGKVLALGTPREVKQrAAVLSAVSG 595
Cdd:PRK10575 196 ErGLTVIAVLHDINmAARYCDYLVALRGGEMIAQGTPAELMR-GETLEQIYG 246
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
49-250 |
3.78e-14 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 72.86 E-value: 3.78e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857580 49 ALVGPDGAGKSTFMRLLCGLEAPDEGRLSVLGTTPDPDN-EDFTTRIAFMPQTlglyktlscRENLEVfaglrGFEGEAD 127
Cdd:PRK13648 39 SIVGHNGSGKSTIAKLMIGIEKVKSGEIFYNNQAITDDNfEKLRKHIGIVFQN---------PDNQFV-----GSIVKYD 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857580 128 GAAGLE----------RRIAELLSMTGLAGFEERQAGKLSGGMKQKLALASALLRIPDLLLLDEPTVGVDPLSRRELWSV 197
Cdd:PRK13648 105 VAFGLEnhavpydemhRRVSEALKQVDMLERADYEPNALSGGQKQRVAIAGVLALNPSVIILDEATSMLDPDARQNLLDL 184
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 2553857580 198 VRRMLADTPMTCVFSTAYLEEAEAADRVLLFESGRIIADENPQSFISRAKGRT 250
Cdd:PRK13648 185 VRKVKSEHNITIISITHDLSEAMEADHVIVMNKGTVYKEGTPTEIFDHAEELT 237
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
384-582 |
4.57e-14 |
|
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: 75.24 E-value: 4.57e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857580 384 DTSFEVRRGEIFGLLGPNGAGKTTTFRMLCGLLVPSKGQIEVAGYDLRT-AKAGARARIGYVAQKFSLYGKlSVEQNLRY 462
Cdd:COG5265 376 GVSFEVPAGKTVAIVGPSGAGKSTLARLLFRFYDVTSGRILIDGQDIRDvTQASLRAAIGIVPQDTVLFND-TIAYNIAY 454
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857580 463 fGRSygffgQALQDRID-----ASLEDF--GLTDRRDTTAGS----LSFGAKQDLSMACGLIHSPEILFLDEATSGADLA 531
Cdd:COG5265 455 -GRP-----DASEEEVEaaaraAQIHDFieSLPDGYDTRVGErglkLSGGEKQRVAIARTLLKNPPILIFDEATSALDSR 528
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 2553857580 532 SRRAFWRRINALASAGTSVVVtTHFLEEAEYCDRFLIQDAGKVLALGTPRE 582
Cdd:COG5265 529 TERAIQAALREVARGRTTLVI-AHRLSTIVDADEILVLEAGRIVERGTHAE 578
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
6-169 |
5.44e-14 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 72.04 E-value: 5.44e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857580 6 APAIRLEGVVKTFPNPLDAARPIR---------------AVDGISLKAggaEASDRlIALVGPDGAGKSTFMRLLCGLEA 70
Cdd:COG1134 2 SSMIEVENVSKSYRLYHEPSRSLKelllrrrrtrreefwALKDVSFEV---ERGES-VGIIGRNGAGKSTLLKLIAGILE 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857580 71 PDEGRLSVLGttpdpdnedfttRIA--------FMPQtlglyktLSCRENLEVFAGLRGFEGEAdgaagLERRIAELLSM 142
Cdd:COG1134 78 PTSGRVEVNG------------RVSallelgagFHPE-------LTGRENIYLNGRLLGLSRKE-----IDEKFDEIVEF 133
|
170 180
....*....|....*....|....*..
gi 2553857580 143 TGLAGFEERQAGKLSGGMKQKLALASA 169
Cdd:COG1134 134 AELGDFIDQPVKTYSSGMRARLAFAVA 160
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
365-557 |
6.27e-14 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 74.77 E-value: 6.27e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857580 365 VVIRADGIARKFGNFVAVADTSFEVRRGEIFGLLGPNGAGKTTTFRMLCGLLVPSKGQIEVagydlrtakaGARARIGYV 444
Cdd:PRK11819 323 KVIEAENLSKSFGDRLLIDDLSFSLPPGGIVGIIGPNGAGKSTLFKMITGQEQPDSGTIKI----------GETVKLAYV 392
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857580 445 AQ-KFSLYGKLSV----------------EQNLR-YFGRsYGFFGQALQDRIdasledfgltdrrdttaGSLSFGAKQDL 506
Cdd:PRK11819 393 DQsRDALDPNKTVweeisggldiikvgnrEIPSRaYVGR-FNFKGGDQQKKV-----------------GVLSGGERNRL 454
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 2553857580 507 SMACGLIHSPEILFLDEATSGADLASRRAFWrriNALASAGTSVVVTTH---FL 557
Cdd:PRK11819 455 HLAKTLKQGGNVLLLDEPTNDLDVETLRALE---EALLEFPGCAVVISHdrwFL 505
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
378-578 |
6.39e-14 |
|
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: 70.42 E-value: 6.39e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857580 378 NFVAVADTSFEVRRGEIFGLLGPNGAGKTTTFRMLCGLLVPSKGQIEVAGYDLRTAKAGARARIGYVAQKFSLYGKlSVE 457
Cdd:cd03247 14 EQQVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDGVPVSDLEKALSSLISVLNQRPYLFDT-TLR 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857580 458 QNLryfGRsygffgqalqdridasledfgltdrrdttagSLSFGAKQDLSMACGLIHSPEILFLDEATSGADLASRRAFW 537
Cdd:cd03247 93 NNL---GR-------------------------------RFSGGERQRLALARILLQDAPIVLLDEPTVGLDPITERQLL 138
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 2553857580 538 RRINALASaGTSVVVTTHFLEEAEYCDRFLIQDAGKVLALG 578
Cdd:cd03247 139 SLIFEVLK-DKTLIWITHHLTGIEHMDKILFLENGKIIMQG 178
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
8-169 |
8.93e-14 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 72.95 E-value: 8.93e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857580 8 AIRLEGVVKTFPNPldaarpIRAVDGISLKAGGAEasdrLIALVGPDGAGKSTFMRLLCGLEAPDEGRLSVLG---TTPD 84
Cdd:PRK11650 3 GLKLQAVRKSYDGK------TQVIKGIDLDVADGE----FIVLVGPSGCGKSTLLRMVAGLERITSGEIWIGGrvvNELE 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857580 85 PDNEDfttrIAFMPQTLGLYKTLSCRENLEVfaGL--RGFegeadGAAGLERRIAELLSMTGLAGFEERQAGKLSGGMKQ 162
Cdd:PRK11650 73 PADRD----IAMVFQNYALYPHMSVRENMAY--GLkiRGM-----PKAEIEERVAEAARILELEPLLDRKPRELSGGQRQ 141
|
....*..
gi 2553857580 163 KLALASA 169
Cdd:PRK11650 142 RVAMGRA 148
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
379-583 |
9.81e-14 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 72.58 E-value: 9.81e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857580 379 FVAVADTSFEVRRGEIFGLLGPNGAGKTTTFRMLCGLLVPSKGQIEV----AGYDLRTAKAGA-------------RARI 441
Cdd:PRK13631 39 LVALNNISYTFEKNKIYFIIGNSGSGKSTLVTHFNGLIKSKYGTIQVgdiyIGDKKNNHELITnpyskkiknfkelRRRV 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857580 442 GYVAQ--KFSLYgKLSVEQNLRYFGRSYGFFGQALQDRIDASLEDFGLTDR-RDTTAGSLSFGAKQDLSMACGLIHSPEI 518
Cdd:PRK13631 119 SMVFQfpEYQLF-KDTIEKDIMFGPVALGVKKSEAKKLAKFYLNKMGLDDSyLERSPFGLSGGQKRRVAIAGILAIQPEI 197
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2553857580 519 LFLDEATSGADLASRRAFWRRINALASAGTSVVVTTHFLEEA-EYCDRFLIQDAGKVLALGTPREV 583
Cdd:PRK13631 198 LIFDEPTAGLDPKGEHEMMQLILDAKANNKTVFVITHTMEHVlEVADEVIVMDKGKILKTGTPYEI 263
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
29-241 |
1.98e-13 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 71.23 E-value: 1.98e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857580 29 RAVDGISLKAGGAEasdrLIALVGPDGAGKSTFMRLLCGLEAPDEGRLSVlgttpdpDNEDFTTR--------------- 93
Cdd:PRK13637 21 KALDNVNIEIEDGE----FVGLIGHTGSGKSTLIQHLNGLLKPTSGKIII-------DGVDITDKkvklsdirkkvglvf 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857580 94 ---------------IAFMPQTLGLYktlscrenlevfaglrgfEGEadgaagLERRIAELLSMTGLA--GFEERQAGKL 156
Cdd:PRK13637 90 qypeyqlfeetiekdIAFGPINLGLS------------------EEE------IENRVKRAMNIVGLDyeDYKDKSPFEL 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857580 157 SGGMKQKLALASALLRIPDLLLLDEPTVGVDPLSRRELWSVVRRMLADTPMTCVFSTAYLEE-AEAADRVLLFESGRIIA 235
Cdd:PRK13637 146 SGGQKRRVAIAGVVAMEPKILILDEPTAGLDPKGRDEILNKIKELHKEYNMTIILVSHSMEDvAKLADRIIVMNKGKCEL 225
|
....*.
gi 2553857580 236 DENPQS 241
Cdd:PRK13637 226 QGTPRE 231
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
367-583 |
2.49e-13 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 70.16 E-value: 2.49e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857580 367 IRADGIARKFGNFVAVADTSFEVRRGEIFGLLGPNGAGKTTTFRMLCGLLVPSKGQIEVAGYDLRTAKA---------GA 437
Cdd:PRK11264 4 IEVKNLVKKFHGQTVLHGIDLEVKPGEVVAIIGPSGSGKTTLLRCINLLEQPEAGTIRVGDITIDTARSlsqqkglirQL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857580 438 RARIGYVAQKFSLYGKLSVEQNL-------RYFGRsygffGQALQdRIDASLEDFGLTDRRDTTAGSLSFGAKQDLSMAC 510
Cdd:PRK11264 84 RQHVGFVFQNFNLFPHRTVLENIiegpvivKGEPK-----EEATA-RARELLAKVGLAGKETSYPRRLSGGQQQRVAIAR 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2553857580 511 GLIHSPEILFLDEATSGADLASRRAFWRRINALASAGTSVVVTTHFLEEA-EYCDRFLIQDAGKVLALGTPREV 583
Cdd:PRK11264 158 ALAMRPEVILFDEPTSALDPELVGEVLNTIRQLAQEKRTMVIVTHEMSFArDVADRAIFMDQGRIVEQGPAKAL 231
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
362-526 |
2.66e-13 |
|
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: 72.79 E-value: 2.66e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857580 362 ERPVVIRADGIARKF-----------GNFVAVADTSFEVRRGEIFGLLGPNGAGKTTTFRMLCGlLVPSKGQIEVAGYDL 430
Cdd:COG4172 271 DAPPLLEARDLKVWFpikrglfrrtvGHVKAVDGVSLTLRRGETLGLVGESGSGKSTLGLALLR-LIPSEGEIRFDGQDL 349
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857580 431 RTAKAGA----RARIGYVAQK-F-SLYGKLSVEQ----NLRYFGRSYGffGQALQDRIDASLEDFGLT-DRRDTTAGSLS 499
Cdd:COG4172 350 DGLSRRAlrplRRRMQVVFQDpFgSLSPRMTVGQiiaeGLRVHGPGLS--AAERRARVAEALEEVGLDpAARHRYPHEFS 427
|
170 180
....*....|....*....|....*..
gi 2553857580 500 FGAKQDLSMACGLIHSPEILFLDEATS 526
Cdd:COG4172 428 GGQRQRIAIARALILEPKLLVLDEPTS 454
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
377-557 |
2.82e-13 |
|
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family transporter in which each gene contains an N-terminal membrane-spanning domain (pfam00664) and a C-terminal ATP-binding domain (pfam00005). In E. coli these genes were discovered as mutants which caused the terminal heme-copper oxidase complex cytochrome bd to fail to assemble. Recent work has shown that the transporter is involved in export of redox-active thiol compounds such as cysteine and glutathione. The linkage to assembly of the cytochrome bd complex is further supported by the conserved operon structure found outside the gammaproteobacteria (cydABCD) containing both the transporter and oxidase genes components. The genes used as the seed members for this model are all either found in the gammproteobacterial context or the CydABCD context. All members of this family scoring above trusted at the time of its creation were from genomes which encode a cytochrome bd complex.
Pssm-ID: 274331 [Multi-domain] Cd Length: 530 Bit Score: 72.39 E-value: 2.82e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857580 377 GNFVAVADTSFEVRRGEIFGLLGPNGAGKTTTFRMLCGLLVPSKGQIEVAGYDLRTAKAGA-RARIGYVAQKFSLYGKlS 455
Cdd:TIGR02868 346 GAPPVLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPLQGEVTLDGVPVSSLDQDEvRRRVSVCAQDAHLFDT-T 424
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857580 456 VEQNLRyFGRsygffGQALQDRIDASLEDFGLTDRRD-----------TTAGSLSFGAKQDLSMACGLIHSPEILFLDEA 524
Cdd:TIGR02868 425 VRENLR-LAR-----PDATDEELWAALERVGLADWLRalpdgldtvlgEGGARLSGGERQRLALARALLADAPILLLDEP 498
|
170 180 190
....*....|....*....|....*....|...
gi 2553857580 525 TSGADLASRRAFWRRINAlASAGTSVVVTTHFL 557
Cdd:TIGR02868 499 TEHLDAETADELLEDLLA-ALSGRTVVLITHHL 530
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
379-583 |
3.04e-13 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 70.89 E-value: 3.04e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857580 379 FVAVADTSFEVRRGEIFGLLGPNGAGKTTTFRMLCGLLVPSKGQIEVAGYDLRTAKA----------------------- 435
Cdd:PRK13651 20 LKALDNVSVEINQGEFIAIIGQTGSGKTTFIEHLNALLLPDTGTIEWIFKDEKNKKKtkekekvleklviqktrfkkikk 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857580 436 --GARARIGYVAQkFSLYG--KLSVEQNLRYFGRSYGFFGQALQDRIDASLEDFGL-TDRRDTTAGSLSFGAKQDLSMAC 510
Cdd:PRK13651 100 ikEIRRRVGVVFQ-FAEYQlfEQTIEKDIIFGPVSMGVSKEEAKKRAAKYIELVGLdESYLQRSPFELSGGQKRRVALAG 178
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2553857580 511 GLIHSPEILFLDEATSGADLASRRAFWRRINALASAGTSVVVTTHFLEEA-EYCDRFLIQDAGKVLALGTPREV 583
Cdd:PRK13651 179 ILAMEPDFLVFDEPTAGLDPQGVKEILEIFDNLNKQGKTIILVTHDLDNVlEWTKRTIFFKDGKIIKDGDTYDI 252
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
9-239 |
3.48e-13 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 70.53 E-value: 3.48e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857580 9 IRLEGVVKTF-PNPLDAARPIRAVDgISLKAGGaeasdrLIALVGPDGAGKSTFMRLLCGLEAPDEG------------- 74
Cdd:PRK13643 2 IKFEKVNYTYqPNSPFASRALFDID-LEVKKGS------YTALIGHTGSGKSTLLQHLNGLLQPTEGkvtvgdivvssts 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857580 75 ----------RLSVLGTTPDPD--NEDFTTRIAFMPQTLGLYKTlscrenlevfaglrgfegEAdgaaglERRIAELLSM 142
Cdd:PRK13643 75 kqkeikpvrkKVGVVFQFPESQlfEETVLKDVAFGPQNFGIPKE------------------KA------EKIAAEKLEM 130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857580 143 TGLAG-FEERQAGKLSGGMKQKLALASALLRIPDLLLLDEPTVGVDPLSRRELWSVVRRmLADTPMTCVFSTAYLEE-AE 220
Cdd:PRK13643 131 VGLADeFWEKSPFELSGGQMRRVAIAGILAMEPEVLVLDEPTAGLDPKARIEMMQLFES-IHQSGQTVVLVTHLMDDvAD 209
|
250
....*....|....*....
gi 2553857580 221 AADRVLLFESGRIIADENP 239
Cdd:PRK13643 210 YADYVYLLEKGHIISCGTP 228
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
50-247 |
4.10e-13 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 70.04 E-value: 4.10e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857580 50 LVGPDGAGKSTFMRLLCGLEAPDEG-------------------RLSVLGTTPDPDNEDFTTRI----AFMPQTLGLykt 106
Cdd:PRK13638 32 LVGANGCGKSTLFMNLSGLLRPQKGavlwqgkpldyskrgllalRQQVATVFQDPEQQIFYTDIdsdiAFSLRNLGV--- 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857580 107 lscrenlevfaglrgfeGEADgaagLERRIAELLSMTGLAGFEERQAGKLSGGMKQKLALASALLRIPDLLLLDEPTVGV 186
Cdd:PRK13638 109 -----------------PEAE----ITRRVDEALTLVDAQHFRHQPIQCLSHGQKKRVAIAGALVLQARYLLLDEPTAGL 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2553857580 187 DPLSRRELWSVVRRMLADTPMTCVFSTAYLEEAEAADRVLLFESGRIIADENPQSFISRAK 247
Cdd:PRK13638 168 DPAGRTQMIAIIRRIVAQGNHVIISSHDIDLIYEISDAVYVLRQGQILTHGAPGEVFACTE 228
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
9-233 |
1.05e-12 |
|
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: 66.47 E-value: 1.05e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857580 9 IRLEGVVKTFPnplDAARPIraVDGISLKAGGAEAsdrlIALVGPDGAGKSTFMRLLCGLEAPDEGRLSVLGTTPDP-DN 87
Cdd:cd03246 1 LEVENVSFRYP---GAEPPV--LRNVSFSIEPGES----LAIIGPSGSGKSTLARLILGLLRPTSGRVRLDGADISQwDP 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857580 88 EDFTTRIAFMPQtlglyktlscreNLEVFAGlrgfegeadgaaglerRIAELLsmtglagfeerqagkLSGGMKQKLALA 167
Cdd:cd03246 72 NELGDHVGYLPQ------------DDELFSG----------------SIAENI---------------LSGGQRQRLGLA 108
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2553857580 168 SALLRIPDLLLLDEPTVGVDPLSRRELWSVVRRMLAdTPMTCVFSTAYLEEAEAADRVLLFESGRI 233
Cdd:cd03246 109 RALYGNPRILVLDEPNSHLDVEGERALNQAIAALKA-AGATRIVIAHRPETLASADRILVLEDGRV 173
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
384-602 |
1.05e-12 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 70.91 E-value: 1.05e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857580 384 DTSFEVRRGEIFGLLGPNGAGKTTTFRMLCGLLVPSKGQIEVAGYDLRTAKAGARARI-----GYVAQKFSLYGKLSVEQ 458
Cdd:PRK10535 26 GISLDIYAGEMVAIVGASGSGKSTLMNILGCLDKPTSGTYRVAGQDVATLDADALAQLrrehfGFIFQRYHLLSHLTAAQ 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857580 459 NLRYFGRSYGFFGQALQDRIDASLEDFGLTDRRDTTAGSLSFGAKQDLSMACGLIHSPEILFLDEATSGADLASRRAFWR 538
Cdd:PRK10535 106 NVEVPAVYAGLERKQRLLRAQELLQRLGLEDRVEYQPSQLSGGQQQRVSIARALMNGGQVILADEPTGALDSHSGEEVMA 185
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2553857580 539 RINALASAGTSVVVTTHFLEEAEYCDRFL-IQDaGKVL----ALGTPREVKQRAAVLSAVSGQSLVVDR 602
Cdd:PRK10535 186 ILHQLRDRGHTVIIVTHDPQVAAQAERVIeIRD-GEIVrnppAQEKVNVAGGTEPVVNTASGWRQFVSG 253
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
31-234 |
1.21e-12 |
|
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: 66.81 E-value: 1.21e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857580 31 VDGISLKAGgaeaSDRLIALVGPDGAGKSTFMRLLCGL--EAPDEGRLSVLGTTPDPDNedFTTRIAFMPQTLGLYKTLS 108
Cdd:cd03213 25 LKNVSGKAK----PGELTAIMGPSGAGKSTLLNALAGRrtGLGVSGEVLINGRPLDKRS--FRKIIGYVPQDDILHPTLT 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857580 109 CRENLEVFAGLRGfegeadgaaglerriaellsmtglagfeerqagkLSGGMKQKLALASALLRIPDLLLLDEPTVGVDP 188
Cdd:cd03213 99 VRETLMFAAKLRG----------------------------------LSGGERKRVSIALELVSNPSLLFLDEPTSGLDS 144
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 2553857580 189 LSRRELWSVVRRmLADTPMTCVFSTAYL--EEAEAADRVLLFESGRII 234
Cdd:cd03213 145 SSALQVMSLLRR-LADTGRTIICSIHQPssEIFELFDKLLLLSQGRVI 191
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
386-586 |
1.24e-12 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 71.16 E-value: 1.24e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857580 386 SFEVRRGEIFGLLGPNGAGKTTTFRMLCGLLVPSKGQIEVAGYDLrtAKAG---ARARIGYVAQKFSLYGKlSVEQNLRY 462
Cdd:PLN03232 1256 SFFVSPSEKVGVVGRTGAGKSSMLNALFRIVELEKGRIMIDDCDV--AKFGltdLRRVLSIIPQSPVLFSG-TVRFNIDP 1332
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857580 463 FGRS-----YGFFGQA-LQDRIDASleDFGLTDRRDTTAGSLSFGAKQDLSMACGLIHSPEILFLDEATSGADLASRRAF 536
Cdd:PLN03232 1333 FSEHndadlWEALERAhIKDVIDRN--PFGLDAEVSEGGENFSVGQRQLLSLARALLRRSKILVLDEATASVDVRTDSLI 1410
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 2553857580 537 WRRINALASAGTSVVVtTHFLEEAEYCDRFLIQDAGKVLALGTPREVKQR 586
Cdd:PLN03232 1411 QRTIREEFKSCTMLVI-AHRLNTIIDCDKILVLSSGQVLEYDSPQELLSR 1459
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
48-187 |
1.57e-12 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 67.50 E-value: 1.57e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857580 48 IALVGPDGAGKSTFMRLLCGLEAPDEGRLSVLGTTPDPDNEDFTTR-----IAFMPQTLGLYKTLSCRENLEVFAGLRGf 122
Cdd:PRK10584 39 IALIGESGSGKSTLLAILAGLDDGSSGEVSLVGQPLHQMDEEARAKlrakhVGFVFQSFMLIPTLNALENVELPALLRG- 117
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2553857580 123 egEADGAAglERRIAELLSMTGLAGFEERQAGKLSGGMKQKLALASALLRIPDLLLLDEPTVGVD 187
Cdd:PRK10584 118 --ESSRQS--RNGAKALLEQLGLGKRLDHLPAQLSGGEQQRVALARAFNGRPDVLFADEPTGNLD 178
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
386-582 |
1.59e-12 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 70.92 E-value: 1.59e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857580 386 SFEVRRGEIFGLLGPNGAGKTTTFRMLCGLLVPSKGQIEVAGYDLRT-AKAGARARIGYVAQKFSLYGKlSVEQNLRYFG 464
Cdd:PLN03130 1259 SFEISPSEKVGIVGRTGAGKSSMLNALFRIVELERGRILIDGCDISKfGLMDLRKVLGIIPQAPVLFSG-TVRFNLDPFN 1337
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857580 465 R-SYGFFGQALQdriDASLED------FGLtDRRDTTAG-SLSFGAKQDLSMACGLIHSPEILFLDEATSGADLASRRAF 536
Cdd:PLN03130 1338 EhNDADLWESLE---RAHLKDvirrnsLGL-DAEVSEAGeNFSVGQRQLLSLARALLRRSKILVLDEATAAVDVRTDALI 1413
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 2553857580 537 WRRINALASAGTSVVVtTHFLEEAEYCDRFLIQDAGKVLALGTPRE 582
Cdd:PLN03130 1414 QKTIREEFKSCTMLII-AHRLNTIIDCDRILVLDAGRVVEFDTPEN 1458
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
386-533 |
1.73e-12 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 67.30 E-value: 1.73e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857580 386 SFEVRRGEIFGLLGPNGAGKTTTFRMLCGLLVPSKGQIEVAGYDlRTAKAGARARIGYVAQKFSLYGKLSVEQNLRyFGR 465
Cdd:PRK10771 19 DLTVERGERVAILGPSGAGKSTLLNLIAGFLTPASGSLTLNGQD-HTTTPPSRRPVSMLFQENNLFSHLTVAQNIG-LGL 96
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2553857580 466 SYGF-FGQALQDRIDASLEDFGLTDRRDTTAGSLSFGAKQDLSMACGLIHSPEILFLDEATSGADLASR 533
Cdd:PRK10771 97 NPGLkLNAAQREKLHAIARQMGIEDLLARLPGQLSGGQRQRVALARCLVREQPILLLDEPFSALDPALR 165
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
389-572 |
1.78e-12 |
|
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding cassette transporters; The pleiotropic drug resistance (PDR) is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. This PDR subfamily represents domain I of its (ABC-IM)2 organization. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds including sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213199 [Multi-domain] Cd Length: 192 Bit Score: 66.50 E-value: 1.78e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857580 389 VRRGEIFGLLGPNGAGKTTTFRMLCGLLVPS--KGQIEVAGYDLrtaKAGARARIGYVAQKFSLYGKLSVEQNLRYfgrs 466
Cdd:cd03232 30 VKPGTLTALMGESGAGKTTLLDVLAGRKTAGviTGEILINGRPL---DKNFQRSTGYVEQQDVHSPNLTVREALRF---- 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857580 467 ygffgqalqdriDASLEDFGLTDRRDttagslsfgakqdLSMACGLIHSPEILFLDEATSGADLASRRAFWRRINALASA 546
Cdd:cd03232 103 ------------SALLRGLSVEQRKR-------------LTIGVELAAKPSILFLDEPTSGLDSQAAYNIVRFLKKLADS 157
|
170 180 190
....*....|....*....|....*....|..
gi 2553857580 547 GTSVVVTTH------FleeaEYCDRFLIQDAG 572
Cdd:cd03232 158 GQAILCTIHqpsasiF----EKFDRLLLLKRG 185
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
29-252 |
1.94e-12 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 67.23 E-value: 1.94e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857580 29 RAVDGISLKAGGAEasdrLIALVGPDGAGKSTFMRLLCGLEAPDEGRLSVlgttpdpDNEDFT-----TR----IAFMPQ 99
Cdd:PRK10895 17 RVVEDVSLTVNSGE----IVGLLGPNGAGKTTTFYMVVGIVPRDAGNIII-------DDEDISllplhARarrgIGYLPQ 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857580 100 TLGLYKTLSCRENLEVFAGLRgfegEADGAAGLERRIAELLSMTGLAGFEERQAGKLSGGMKQKLALASALLRIPDLLLL 179
Cdd:PRK10895 86 EASIFRRLSVYDNLMAVLQIR----DDLSAEQREDRANELMEEFHIEHLRDSMGQSLSGGERRRVEIARALAANPKFILL 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2553857580 180 DEPTVGVDPLSRRELWSVVRRmLADTPMTCVFSTAYLEEA-EAADRVLLFESGRIIADENPQSFISRAK-GRTYL 252
Cdd:PRK10895 162 DEPFAGVDPISVIDIKRIIEH-LRDSGLGVLITDHNVRETlAVCERAYIVSQGHLIAHGTPTEILQDEHvKRVYL 235
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
30-235 |
2.15e-12 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 69.81 E-value: 2.15e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857580 30 AVDGISL--KAGgaeasdRLIALVGPDGAGKSTFMRLLCGLEAPDEGRLSVLGTtpdpDNEDFTT-----RIAFMPQTLG 102
Cdd:COG1132 355 VLKDISLtiPPG------ETVALVGPSGSGKSTLVNLLLRFYDPTSGRILIDGV----DIRDLTLeslrrQIGVVPQDTF 424
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857580 103 LYKTlSCRENL----------EVFAGLRgfegeadgAAGLERRIAELLsmtglAGFE----ERqAGKLSGGMKQKLALAS 168
Cdd:COG1132 425 LFSG-TIRENIrygrpdatdeEVEEAAK--------AAQAHEFIEALP-----DGYDtvvgER-GVNLSGGQRQRIAIAR 489
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2553857580 169 ALLRIPDLLLLDEPTVGVDPLSRRELWSVVRRMLADTpmTCV-----FSTayleeAEAADRVLLFESGRIIA 235
Cdd:COG1132 490 ALLKDPPILILDEATSALDTETEALIQEALERLMKGR--TTIviahrLST-----IRNADRILVLDDGRIVE 554
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
389-567 |
2.17e-12 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 67.11 E-value: 2.17e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857580 389 VRRGEIFGLLGPNGAGKTTTFRMLCGLLVPSKGQIEVAGYDLRT----AKAGARAR-IGYVAQKFSLYGKLSVEQNLRYF 463
Cdd:PRK10584 33 VKRGETIALIGESGSGKSTLLAILAGLDDGSSGEVSLVGQPLHQmdeeARAKLRAKhVGFVFQSFMLIPTLNALENVELP 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857580 464 GRSYGFFGQALQDRIDASLEDFGLTDRRDTTAGSLSFGAKQDLSMACGLIHSPEILFLDEATSGADlasRRAFWRRINAL 543
Cdd:PRK10584 113 ALLRGESSRQSRNGAKALLEQLGLGKRLDHLPAQLSGGEQQRVALARAFNGRPDVLFADEPTGNLD---RQTGDKIADLL 189
|
170 180
....*....|....*....|....*...
gi 2553857580 544 ASA----GTSVVVTTHFLEEAEYCDRFL 567
Cdd:PRK10584 190 FSLnrehGTTLILVTHDLQLAARCDRRL 217
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
7-234 |
2.26e-12 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 69.71 E-value: 2.26e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857580 7 PAIRLEGVVKTFPNpldaaRPIraVDGISL--KAGgaeasDRlIALVGPDGAGKSTFMRLLCGLEAPDEGRLsVLGTtpd 84
Cdd:COG0488 314 KVLELEGLSKSYGD-----KTL--LDDLSLriDRG-----DR-IGLIGPNGAGKSTLLKLLAGELEPDSGTV-KLGE--- 376
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857580 85 pdnedfTTRIAFMPQTL-GLYKTLSCRENLevfaglrgfegeADGAAGLERRiaELLSMTGLAGFE----ERQAGKLSGG 159
Cdd:COG0488 377 ------TVKIGYFDQHQeELDPDKTVLDEL------------RDGAPGGTEQ--EVRGYLGRFLFSgddaFKPVGVLSGG 436
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2553857580 160 MKQKLALASALLRIPDLLLLDEPTVGVDPLSRRELwsvvRRMLADTPMTCVFST---AYLEeaEAADRVLLFESGRII 234
Cdd:COG0488 437 EKARLALAKLLLSPPNVLLLDEPTNHLDIETLEAL----EEALDDFPGTVLLVShdrYFLD--RVATRILEFEDGGVR 508
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
381-592 |
2.26e-12 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 68.12 E-value: 2.26e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857580 381 AVADTSFEVRRGEIFGLLGPNGAGKTTTFRMLCGLLVPSKGQIEVaGYDLRTAKAGA------RARIGYVAQ--KFSLYG 452
Cdd:PRK13634 22 ALYDVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVTI-GERVITAGKKNkklkplRKKVGIVFQfpEHQLFE 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857580 453 KlSVEQNLRYFGRSYGFFGQALQDRIDASLEDFGLT-DRRDTTAGSLSFGAKQDLSMACGLIHSPEILFLDEATSGADLA 531
Cdd:PRK13634 101 E-TVEKDICFGPMNFGVSEEDAKQKAREMIELVGLPeELLARSPFELSGGQMRRVAIAGVLAMEPEVLVLDEPTAGLDPK 179
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2553857580 532 SRRAFWRRINAL-ASAGTSVVVTTHFLEE-AEYCDRFLIQDAGKVLALGTPREVKQRAAVLSA 592
Cdd:PRK13634 180 GRKEMMEMFYKLhKEKGLTTVLVTHSMEDaARYADQIVVMHKGTVFLQGTPREIFADPDELEA 242
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
9-247 |
2.31e-12 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 68.19 E-value: 2.31e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857580 9 IRLEGVVKTFpnplDAARP--IRAVDGISLKAGGAEAsdrlIALVGPDGAGKSTFMRLLCGLEAPDEGRL------SVLG 80
Cdd:PRK13651 3 IKVKNIVKIF----NKKLPteLKALDNVSVEINQGEF----IAIIGQTGSGKTTFIEHLNALLLPDTGTIewifkdEKNK 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857580 81 TTPDPDNEDFTTRIAFMPQTLGLYKTLSCRENLEV---FAGLRGFEG--EADGAAG----------LERRIAELLSMTGL 145
Cdd:PRK13651 75 KKTKEKEKVLEKLVIQKTRFKKIKKIKEIRRRVGVvfqFAEYQLFEQtiEKDIIFGpvsmgvskeeAKKRAAKYIELVGL 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857580 146 -AGFEERQAGKLSGGMKQKLALASALLRIPDLLLLDEPTVGVDPLSRRELWSVVRRmLADTPMTCVFSTAYLEEA-EAAD 223
Cdd:PRK13651 155 dESYLQRSPFELSGGQKRRVALAGILAMEPDFLVFDEPTAGLDPQGVKEILEIFDN-LNKQGKTIILVTHDLDNVlEWTK 233
|
250 260
....*....|....*....|....
gi 2553857580 224 RVLLFESGRIIADENPQSFISRAK 247
Cdd:PRK13651 234 RTIFFKDGKIIKDGDTYDILSDNK 257
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
9-188 |
2.52e-12 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 68.67 E-value: 2.52e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857580 9 IRLEGVVKTFPNPldaARPIRAVDGISLKAGGAEasdrLIALVGPDGAGKSTFMRLLCGLEAPDEGRLSVlgttpdpDNE 88
Cdd:PRK11153 2 IELKNISKVFPQG---GRTIHALNNVSLHIPAGE----IFGVIGASGAGKSTLIRCINLLERPTSGRVLV-------DGQ 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857580 89 DFTT-----------RIAFMPQTLGLyktLSCR---EN----LEVfAGLRgfegeadgAAGLERRIAELLSMTGLAGFEE 150
Cdd:PRK11153 68 DLTAlsekelrkarrQIGMIFQHFNL---LSSRtvfDNvalpLEL-AGTP--------KAEIKARVTELLELVGLSDKAD 135
|
170 180 190
....*....|....*....|....*....|....*...
gi 2553857580 151 RQAGKLSGGMKQKLALASALLRIPDLLLLDEPTVGVDP 188
Cdd:PRK11153 136 RYPAQLSGGQKQRVAIARALASNPKVLLCDEATSALDP 173
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
41-244 |
2.62e-12 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 66.91 E-value: 2.62e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857580 41 AEASDRlIALVGPDGAGKSTFMRLLCGLEAPDEGRLSVlgttpdpDNEDFT-TRIAFMP-----QTLGLYKTLSCRENLE 114
Cdd:PRK10771 22 VERGER-VAILGPSGAGKSTLLNLIAGFLTPASGSLTL-------NGQDHTtTPPSRRPvsmlfQENNLFSHLTVAQNIG 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857580 115 VfaGLR-GFEGEADGAAGLeRRIAELLsmtGLAGFEERQAGKLSGGMKQKLALASALLRIPDLLLLDEPTVGVDPLSRRE 193
Cdd:PRK10771 94 L--GLNpGLKLNAAQREKL-HAIARQM---GIEDLLARLPGQLSGGQRQRVALARCLVREQPILLLDEPFSALDPALRQE 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 2553857580 194 LWSVVRRMLADTPMTCVFSTAYLEEA-EAADRVLLFESGRIIADENPQSFIS 244
Cdd:PRK10771 168 MLTLVSQVCQERQLTLLMVSHSLEDAaRIAPRSLVVADGRIAWDGPTDELLS 219
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
28-244 |
2.91e-12 |
|
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in methanogenesis, methyl coenzyme M reductase, contains alpha, beta, and gamma chains. In older literature, the complex of alpha, beta, and gamma chains was termed component C, while this single chain protein was termed methyl coenzyme M reductase system component A2. [Energy metabolism, Methanogenesis]
Pssm-ID: 132313 [Multi-domain] Cd Length: 520 Bit Score: 69.45 E-value: 2.91e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857580 28 IRAVDGISLKAGGAEasdrLIALVGPDGAGKSTFMRLLCGLEAPDEGRLSV-LG------TTPDPDNEDFTTR-IAFMPQ 99
Cdd:TIGR03269 297 VKAVDNVSLEVKEGE----IFGIVGTSGAGKTTLSKIIAGVLEPTSGEVNVrVGdewvdmTKPGPDGRGRAKRyIGILHQ 372
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857580 100 TLGLYKTLSCRENLEVFAGLrgfegEADGAAGLERRIAELLSmtglAGFEERQA--------GKLSGGMKQKLALASALL 171
Cdd:TIGR03269 373 EYDLYPHRTVLDNLTEAIGL-----ELPDELARMKAVITLKM----VGFDEEKAeeildkypDELSEGERHRVALAQVLI 443
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2553857580 172 RIPDLLLLDEPTVGVDPLSRRELWSVVRRMLADTPMTCVFSTAYLEEA-EAADRVLLFESGRIIADENPQSFIS 244
Cdd:TIGR03269 444 KEPRIVILDEPTGTMDPITKVDVTHSILKAREEMEQTFIIVSHDMDFVlDVCDRAALMRDGKIVKIGDPEEIVE 517
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
377-583 |
2.94e-12 |
|
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: 68.16 E-value: 2.94e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857580 377 GNFVAVADTSFEVRRGEIFGLLGPNGAGKTTTFRMLCGLLVP---SKGQIEVAGYDLRTAKAGAR-----ARIGYVaqkF 448
Cdd:COG0444 16 GVVKAVDGVSFDVRRGETLGLVGESGSGKSTLARAILGLLPPpgiTSGEILFDGEDLLKLSEKELrkirgREIQMI---F 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857580 449 -----SLYGKLSVEQNLRYFGRSYGFF-GQALQDRIDASLEDFGLTDRRDtTAGS----LSFGAKQDLSMACGLIHSPEI 518
Cdd:COG0444 93 qdpmtSLNPVMTVGDQIAEPLRIHGGLsKAEARERAIELLERVGLPDPER-RLDRypheLSGGMRQRVMIARALALEPKL 171
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857580 519 LFLDEATSGADLASRRAFwrrINAL----ASAGTSVVVTTHFLEEAEY-CDRFLIQDAGKVLALGTPREV 583
Cdd:COG0444 172 LIADEPTTALDVTIQAQI---LNLLkdlqRELGLAILFITHDLGVVAEiADRVAVMYAGRIVEEGPVEEL 238
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
379-583 |
3.91e-12 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 67.11 E-value: 3.91e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857580 379 FVAVADTSFEVRRGEIFGLLGPNGAGKTTTFRMLCGLLVPSKGQIEVAGYDLrTAKAG------ARARIGYVAQ--KFSL 450
Cdd:PRK13646 20 HQAIHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVDDITI-THKTKdkyirpVRKRIGMVFQfpESQL 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857580 451 YgKLSVEQNLRYFGRSYGFFGQALQDRIDASLEDFGLTdrRDTTAGS---LSFGAKQDLSMACGLIHSPEILFLDEATSG 527
Cdd:PRK13646 99 F-EDTVEREIIFGPKNFKMNLDEVKNYAHRLLMDLGFS--RDVMSQSpfqMSGGQMRKIAIVSILAMNPDIIVLDEPTAG 175
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 2553857580 528 ADLASRRAFWRRINALA-SAGTSVVVTTHFLEE-AEYCDRFLIQDAGKVLALGTPREV 583
Cdd:PRK13646 176 LDPQSKRQVMRLLKSLQtDENKTIILVSHDMNEvARYADEVIVMKEGSIVSQTSPKEL 233
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
52-203 |
4.20e-12 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 66.03 E-value: 4.20e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857580 52 GPDGAGKSTFMRLLCGLEAPDEGRLSVlgTTPDPDNEDFTTRIAFMPQTLGLYKTLSCRENLEVFAGLRGFEGEadgaag 131
Cdd:PRK13543 44 GDNGAGKTTLLRVLAGLLHVESGQIQI--DGKTATRGDRSRFMAYLGHLPGLKADLSTLENLHFLCGLHGRRAK------ 115
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2553857580 132 leRRIAELLSMTGLAGFEERQAGKLSGGMKQKLALASALLRIPDLLLLDEPTVGVDPlsrrELWSVVRRMLA 203
Cdd:PRK13543 116 --QMPGSALAIVGLAGYEDTLVRQLSAGQKKRLALARLWLSPAPLWLLDEPYANLDL----EGITLVNRMIS 181
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
32-229 |
4.29e-12 |
|
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: 66.28 E-value: 4.29e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857580 32 DGISLKAGGAEASD-RLIALVGPDGAGKSTFMRLLCGLEAPDEGrlsvlgttpdpDNEDFTTRIAFMPQTLGLYKTLSCR 110
Cdd:cd03237 11 GEFTLEVEGGSISEsEVIGILGPNGIGKTTFIKMLAGVLKPDEG-----------DIEIELDTVSYKPQYIKADYEGTVR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857580 111 ENLEvfaglrgfeGEADGAAGLERRIAELLSMTGLAGFEERQAGKLSGGMKQKLALASALLRIPDLLLLDEPTVGVDPLS 190
Cdd:cd03237 80 DLLS---------SITKDFYTHPYFKTEIAKPLQIEQILDREVPELSGGELQRVAIAACLSKDADIYLLDEPSAYLDVEQ 150
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 2553857580 191 RRELWSVVRRMLADTPMTC------VFSTAYLeeaeaADRVLLFE 229
Cdd:cd03237 151 RLMASKVIRRFAENNEKTAfvvehdIIMIDYL-----ADRLIVFE 190
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
29-194 |
4.35e-12 |
|
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: 68.93 E-value: 4.35e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857580 29 RAVDGISLKAggaEASDRlIALVGPDGAGKSTFMRLLCGLEAPDEGRLSVLGTTP-DPDNEDFTTRIAFMPQTLGLYKTl 107
Cdd:TIGR02868 349 PVLDGVSLDL---PPGER-VAILGPSGSGKSTLLATLAGLLDPLQGEVTLDGVPVsSLDQDEVRRRVSVCAQDAHLFDT- 423
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857580 108 SCRENLEVFAGLRGFE--GEADGAAGLERRIAELLSmtGLAGFEERQAGKLSGGMKQKLALASALLRIPDLLLLDEPTVG 185
Cdd:TIGR02868 424 TVRENLRLARPDATDEelWAALERVGLADWLRALPD--GLDTVLGEGGARLSGGERQRLALARALLADAPILLLDEPTEH 501
|
....*....
gi 2553857580 186 VDPLSRREL 194
Cdd:TIGR02868 502 LDAETADEL 510
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
381-583 |
4.53e-12 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 66.74 E-value: 4.53e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857580 381 AVADTSFEVRRGEIFGLLGPNGAGKTTTFRMLCGLLVPSKGQIEVAGYDLRTAKAGARA-RIGYVAQ--KFSLYGKLSVE 457
Cdd:PRK15112 28 AVKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDHPLHFGDYSYRSqRIRMIFQdpSTSLNPRQRIS 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857580 458 QNLRYFGR-SYGFFGQALQDRIDASLEDFGL-TDRRDTTAGSLSFGAKQDLSMACGLIHSPEILFLDEATSGADLASRRA 535
Cdd:PRK15112 108 QILDFPLRlNTDLEPEQREKQIIETLRQVGLlPDHASYYPHMLAPGQKQRLGLARALILRPKVIIADEALASLDMSMRSQ 187
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 2553857580 536 FwrrINAL----ASAGTSVV-VTTHFLEEAEYCDRFLIQDAGKVLALGTPREV 583
Cdd:PRK15112 188 L---INLMlelqEKQGISYIyVTQHLGMMKHISDQVLVMHQGEVVERGSTADV 237
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
384-567 |
4.80e-12 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 65.99 E-value: 4.80e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857580 384 DTSFEVRRGEIFGLLGPNGAGKTTTFRMLCGLLVPSKGQIEVAGYDLRTAKAGARA-----RIGYVAQKFSLYGKLSVEQ 458
Cdd:PRK11629 27 NVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPMSKLSSAAKAelrnqKLGFIYQFHHLLPDFTALE 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857580 459 NLRYFGRSYGFFGQALQDRIDASLEDFGLTDRRDTTAGSLSFGAKQDLSMACGLIHSPEILFLDEATSGADLASRRAFWR 538
Cdd:PRK11629 107 NVAMPLLIGKKKPAEINSRALEMLAAVGLEHRANHRPSELSGGERQRVAIARALVNNPRLVLADEPTGNLDARNADSIFQ 186
|
170 180 190
....*....|....*....|....*....|
gi 2553857580 539 RINAL-ASAGTSVVVTTHFLEEAEYCDRFL 567
Cdd:PRK11629 187 LLGELnRLQGTAFLVVTHDLQLAKRMSRQL 216
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
35-167 |
5.91e-12 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 65.21 E-value: 5.91e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857580 35 SLKAGGaeasdrLIALVGPDGAGKSTFMRLLCGLEAPDEGRLSVLGTTPDPDNEDFTTRIAFMPQTLGLYKTLSCRENLE 114
Cdd:PRK13538 23 TLNAGE------LVQIEGPNGAGKTSLLRILAGLARPDAGEVLWQGEPIRRQRDEYHQDLLYLGHQPGIKTELTALENLR 96
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 2553857580 115 VFAGLRGFEGEADgaaglerrIAELLSMTGLAGFEERQAGKLSGGMKQKLALA 167
Cdd:PRK13538 97 FYQRLHGPGDDEA--------LWEALAQVGLAGFEDVPVRQLSAGQQRRVALA 141
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
377-585 |
6.41e-12 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 66.33 E-value: 6.41e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857580 377 GNFVAVADTSFEVRRGEIFGLLGPNGAGKTTTFRMLCGLLVPSKGQIEVAGYDL----RTAKAGARARIGYVAQKFSLYG 452
Cdd:PRK11831 18 GNRCIFDNISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEILFDGENIpamsRSRLYTVRKRMSMLFQSGALFT 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857580 453 KLSVEQNLRYFGRSYGFFGQA-LQDRIDASLEDFGLTDRRDTTAGSLSFGAKQDLSMACGLIHSPEILFLDEATSGADLA 531
Cdd:PRK11831 98 DMNVFDNVAYPLREHTQLPAPlLHSTVMMKLEAVGLRGAAKLMPSELSGGMARRAALARAIALEPDLIMFDEPFVGQDPI 177
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 2553857580 532 SRRAFWRRINALASA-GTSVVVTTHFLEE----AEYCdrFLIQDAgKVLALGTPREVKQ 585
Cdd:PRK11831 178 TMGVLVKLISELNSAlGVTCVVVSHDVPEvlsiADHA--YIVADK-KIVAHGSAQALQA 233
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
33-247 |
6.61e-12 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 66.15 E-value: 6.61e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857580 33 GISLKAGGAEasdrLIALVGPDGAGKSTFMRLLCGLEAPDEGRLSVLGT----TPDPDNE----------DFTTRIAFMP 98
Cdd:PRK10619 23 GVSLQANAGD----VISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNGQtinlVRDKDGQlkvadknqlrLLRTRLTMVF 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857580 99 QTLGLYKTLSCREN-LEVFAGLRGFEGeadgAAGLERRIAELLSMtglaGFEERQAGK----LSGGMKQKLALASALLRI 173
Cdd:PRK10619 99 QHFNLWSHMTVLENvMEAPIQVLGLSK----QEARERAVKYLAKV----GIDERAQGKypvhLSGGQQQRVSIARALAME 170
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2553857580 174 PDLLLLDEPTVGVDPlsrrELWSVVRRM---LADTPMTCVFSTAYLEEA-EAADRVLLFESGRIIADENPQSFISRAK 247
Cdd:PRK10619 171 PEVLLFDEPTSALDP----ELVGEVLRImqqLAEEGKTMVVVTHEMGFArHVSSHVIFLHQGKIEEEGAPEQLFGNPQ 244
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
34-187 |
7.41e-12 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 65.91 E-value: 7.41e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857580 34 ISLKAGgaeasdRLIALVGPDGAGKSTFMRLLCGLEAPDEGRLSvlgttpdpdnEDFTTRIAFMPQTLGLYKTLSCreNL 113
Cdd:PRK09544 25 LELKPG------KILTLLGPNGAGKSTLVRVVLGLVAPDEGVIK----------RNGKLRIGYVPQKLYLDTTLPL--TV 86
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2553857580 114 EVFAGLRGFEGEADGAAGLER-RIAELLsmtglagfeERQAGKLSGGMKQKLALASALLRIPDLLLLDEPTVGVD 187
Cdd:PRK09544 87 NRFLRLRPGTKKEDILPALKRvQAGHLI---------DAPMQKLSGGETQRVLLARALLNRPQLLVLDEPTQGVD 152
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
29-529 |
7.86e-12 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 67.81 E-value: 7.86e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857580 29 RAVDGISLKAGGAEAsdrlIALVGPDGAGKSTfmrllcgleapdeGRLSVLGTTPDPDNEDFTTRIAFMPQTLglyktLS 108
Cdd:PRK15134 23 TVVNDVSLQIEAGET----LALVGESGSGKSV-------------TALSILRLLPSPPVVYPSGDIRFHGESL-----LH 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857580 109 CREnlevfAGLRGFEGEA------------DGAAGLERRIAELLS----MTGLAGFEE----------RQAGK------- 155
Cdd:PRK15134 81 ASE-----QTLRGVRGNKiamifqepmvslNPLHTLEKQLYEVLSlhrgMRREAARGEilncldrvgiRQAAKrltdyph 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857580 156 -LSGGMKQKLALASALLRIPDLLLLDEPTVGVDPLSRRELWSVVRRMLADTPMTCVFSTAYLEEA-EAADRVLLFESGRI 233
Cdd:PRK15134 156 qLSGGERQRVMIAMALLTRPELLIADEPTTALDVSVQAQILQLLRELQQELNMGLLFITHNLSIVrKLADRVAVMQNGRC 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857580 234 IADENPQsfisrakgrtyllPLANRAEHDaqmLCRRL--SEETAatrsdalflDIVPrmggaAATTLAPTLPVKDARVps 311
Cdd:PRK15134 236 VEQNRAA-------------TLFSAPTHP---YTQKLlnSEPSG---------DPVP-----LPEPASPLLDVEQLQV-- 283
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857580 312 gfiprqpsledayallTFPrapktanhlasppsdasgalaasaasaddtaerpvvIRADGIARKFGNFVAVADTSFEVRR 391
Cdd:PRK15134 284 ----------------AFP------------------------------------IRKGILKRTVDHNVVVKNISFTLRP 311
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857580 392 GEIFGLLGPNGAGKTTTfrmlcGL----LVPSKGQIEVAGYDL----RTAKAGARARIGYVAQ--KFSLYGKLSVEQ--- 458
Cdd:PRK15134 312 GETLGLVGESGSGKSTT-----GLallrLINSQGEIWFDGQPLhnlnRRQLLPVRHRIQVVFQdpNSSLNPRLNVLQiie 386
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2553857580 459 -NLRYFGRSYGffGQALQDRIDASLEDFGL-TDRRDTTAGSLSFGAKQDLSMACGLIHSPEILFLDEATSGAD 529
Cdd:PRK15134 387 eGLRVHQPTLS--AAQREQQVIAVMEEVGLdPETRHRYPAEFSGGQRQRIAIARALILKPSLIILDEPTSSLD 457
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
9-236 |
8.69e-12 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 65.88 E-value: 8.69e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857580 9 IRLEGVVKTFpNPlDAARPIRAVDGISLKAggaEASDrLIALVGPDGAGKSTFMRLLCGLEAPDEGRLSVlgttpdpDNE 88
Cdd:COG1101 2 LELKNLSKTF-NP-GTVNEKRALDGLNLTI---EEGD-FVTVIGSNGAGKSTLLNAIAGSLPPDSGSILI-------DGK 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857580 89 DFTT-----RIAFM------PQtLGLYKTLSCRENLeVFAGLRGfegeadGAAGLERRI--------AELLSMTGLaGFE 149
Cdd:COG1101 69 DVTKlpeykRAKYIgrvfqdPM-MGTAPSMTIEENL-ALAYRRG------KRRGLRRGLtkkrrelfRELLATLGL-GLE 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857580 150 ER---QAGKLSGGMKQKLALASALLRIPDLLLLDEPTVGVDPLSRRELWSVVRRMLADTPMTCVFSTAYLEEA-EAADRV 225
Cdd:COG1101 140 NRldtKVGLLSGGQRQALSLLMATLTKPKLLLLDEHTAALDPKTAALVLELTEKIVEENNLTTLMVTHNMEQAlDYGNRL 219
|
250
....*....|.
gi 2553857580 226 LLFESGRIIAD 236
Cdd:COG1101 220 IMMHEGRIILD 230
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
381-585 |
9.40e-12 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 67.45 E-value: 9.40e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857580 381 AVADTSFEVRRGEIFGLLGPNGAGKTTTFRMLCGLLVPSKGQIEVAGYDLRTAKAGARARIGYV-----AQKFSLYGKLS 455
Cdd:PRK10982 263 SIRDVSFDLHKGEILGIAGLVGAKRTDIVETLFGIREKSAGTITLHGKKINNHNANEAINHGFAlvteeRRSTGIYAYLD 342
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857580 456 VEQNlryfgrsygffgqALQDRIDASLEDFGLTDRRD--------------------TTAGSLSFGAKQDLSMACGLIHS 515
Cdd:PRK10982 343 IGFN-------------SLISNIRNYKNKVGLLDNSRmksdtqwvidsmrvktpghrTQIGSLSGGNQQKVIIGRWLLTQ 409
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2553857580 516 PEILFLDEATSGADLASRRAFWRRINALASAGTSVV-VTTHFLEEAEYCDRFLIQDAGKVLALGTPREVKQ 585
Cdd:PRK10982 410 PEILMLDEPTRGIDVGAKFEIYQLIAELAKKDKGIIiISSEMPELLGITDRILVMSNGLVAGIVDTKTTTQ 480
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
25-233 |
9.90e-12 |
|
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: 63.99 E-value: 9.90e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857580 25 ARPIRAVDGISLKAGGAEASDRL-----IALVGPDGAGKSTFMRLLCGLEAPDEGRLSVLGTTpdpdnedfttriafmpq 99
Cdd:cd03215 1 GEPVLEVRGLSVKGAVRDVSFEVrageiVGIAGLVGNGQTELAEALFGLRPPASGEITLDGKP----------------- 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857580 100 tlglYKTLSCRENLEvfAGLrGF--EGEADGAAGLERRIAELLSMTGLagfeerqagkLSGGMKQKLALASALLRIPDLL 177
Cdd:cd03215 64 ----VTRRSPRDAIR--AGI-AYvpEDRKREGLVLDLSVAENIALSSL----------LSGGNQQKVVLARWLARDPRVL 126
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 2553857580 178 LLDEPTVGVDPLSRRELWSVVRRmLADTPMTCVFSTAYLEEAEA-ADRVLLFESGRI 233
Cdd:cd03215 127 ILDEPTRGVDVGAKAEIYRLIRE-LADAGKAVLLISSELDELLGlCDRILVMYEGRI 182
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
386-585 |
1.04e-11 |
|
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of iron-sulfur clusters (Fe-S) depends on multi-protein systems. The SUF system of E. coli and Erwinia chrysanthemi is important for Fe-S biogenesis under stressful conditions. The SUF system is made of six proteins: SufC is an atypical cytoplasmic ABC-ATPase, which forms a complex with SufB and SufD; SufA plays the role of a scaffold protein for assembly of iron-sulfur clusters and delivery to target proteins; SufS is a cysteine desulfurase which mobilizes the sulfur atom from cysteine and provides it to the cluster; SufE has no associated function yet.
Pssm-ID: 213184 [Multi-domain] Cd Length: 200 Bit Score: 64.47 E-value: 1.04e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857580 386 SFEVRRGEIFGLLGPNGAGKTTTFRMLCGllVPS----KGQIEVAGYDLRTAKAGARARIG-YVA-QKFSLYGKLSVEQN 459
Cdd:cd03217 20 NLTIKKGEVHALMGPNGSGKSTLAKTIMG--HPKyevtEGEILFKGEDITDLPPEERARLGiFLAfQYPPEIPGVKNADF 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857580 460 LRYFGrsYGFFGqalqdridasledfgltdrrdttagslsfGAKQDLSMACGLIHSPEILFLDEATSGADLASRRAFWRR 539
Cdd:cd03217 98 LRYVN--EGFSG-----------------------------GEKKRNEILQLLLLEPDLAILDEPDSGLDIDALRLVAEV 146
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 2553857580 540 INALASAGTSVVVTTHFLEEAEYC--DRFLIQDAGKVLALGTPREVKQ 585
Cdd:cd03217 147 INKLREEGKSVLIITHYQRLLDYIkpDRVHVLYDGRIVKSGDKELALE 194
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
366-583 |
1.34e-11 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 64.93 E-value: 1.34e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857580 366 VIRADGIARKFGNFVAVADTSFEVRRGEIFGLLGPNGAGKTTTFRMLCGL--LVPS---KGQIEVAGYDL-RTAKAGARA 439
Cdd:PRK14247 3 KIEIRDLKVSFGQVEVLDGVNLEIPDNTITALMGPSGSGKSTLLRVFNRLieLYPEarvSGEVYLDGQDIfKMDVIELRR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857580 440 RIGYVAQ------KFSLYGKLSVEQNLRYFGRSygffGQALQDRIDASLEDFGL----TDRRDTTAGSLSFGAKQDLSMA 509
Cdd:PRK14247 83 RVQMVFQipnpipNLSIFENVALGLKLNRLVKS----KKELQERVRWALEKAQLwdevKDRLDAPAGKLSGGQQQRLCIA 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2553857580 510 CGLIHSPEILFLDEATSGADLASRrafwRRINAL---ASAGTSVVVTTHFLEE-AEYCDRFLIQDAGKVLALGTPREV 583
Cdd:PRK14247 159 RALAFQPEVLLADEPTANLDPENT----AKIESLfleLKKDMTIVLVTHFPQQaARISDYVAFLYKGQIVEWGPTREV 232
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
364-602 |
1.57e-11 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 65.08 E-value: 1.57e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857580 364 PVVIRadGIARKFGNFVAVADTSFEVRRGEIFGLLGPNGAGKTTTFRMLCGLLVPSKGQIeVAGydlRTAKAGARARIGY 443
Cdd:PRK11247 12 PLLLN--AVSKRYGERTVLNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAGEL-LAG---TAPLAEAREDTRL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857580 444 VAQKFSLYGKLSVEQNLRyFGRSYGFFGQALQdridaSLEDFGLTDRRDTTAGSLSFGAKQDLSMACGLIHSPEILFLDE 523
Cdd:PRK11247 86 MFQDARLLPWKKVIDNVG-LGLKGQWRDAALQ-----ALAAVGLADRANEWPAALSGGQKQRVALARALIHRPGLLLLDE 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857580 524 ATSGADLASRRAFWRRINAL-ASAGTSVVVTTHFLEEA-EYCDRFLIQDAGKV---LALGTPREVKQRAAVLSAVSGQsl 598
Cdd:PRK11247 160 PLGALDALTRIEMQDLIESLwQQHGFTVLLVTHDVSEAvAMADRVLLIEEGKIgldLTVDLPRPRRRGSARLAELEAE-- 237
|
....
gi 2553857580 599 VVDR 602
Cdd:PRK11247 238 VLQR 241
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
368-574 |
1.61e-11 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 65.09 E-value: 1.61e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857580 368 RADGIARKFGNFVAVADTSFEVRRGEIFGLLGPNGAGKTTTFRMLCGLLVPSKGQIEVAGYDL-RTAKAGARA------- 439
Cdd:PRK10419 14 AHGGLSGKHQHQTVLNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWRGEPLaKLNRAQRKAfrrdiqm 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857580 440 ----RIGYVAQKFSLygKLSVEQNLRYFgrsYGFFGQALQDRIDASLEDFGLTDR-RDTTAGSLSFGAKQDLSMACGLIH 514
Cdd:PRK10419 94 vfqdSISAVNPRKTV--REIIREPLRHL---LSLDKAERLARASEMLRAVDLDDSvLDKRPPQLSGGQLQRVCLARALAV 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2553857580 515 SPEILFLDEATSGADLASRRAFWRRINAL-ASAGTSVVVTTHFLEEAEY-CDRFLIQDAGKV 574
Cdd:PRK10419 169 EPKLLILDEAVSNLDLVLQAGVIRLLKKLqQQFGTACLFITHDLRLVERfCQRVMVMDNGQI 230
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
388-570 |
2.06e-11 |
|
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: 64.35 E-value: 2.06e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857580 388 EVRRGEIFGLLGPNGAGKTTTFRMLCGLLVPSKGQIEVAGYDlrtakagararIGYVAQKFSLYGKLSVEQNLRYFGRSY 467
Cdd:cd03237 21 SISESEVIGILGPNGIGKTTFIKMLAGVLKPDEGDIEIELDT-----------VSYKPQYIKADYEGTVRDLLSSITKDF 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857580 468 GFFGQALQDRIDaSLEDFGLTDRRDTTagsLSFGAKQDLSMACGLIHSPEILFLDEATSGADLASRRAFWRRIN--ALAS 545
Cdd:cd03237 90 YTHPYFKTEIAK-PLQIEQILDREVPE---LSGGELQRVAIAACLSKDADIYLLDEPSAYLDVEQRLMASKVIRrfAENN 165
|
170 180
....*....|....*....|....*
gi 2553857580 546 AGTSVVVTTHFLEEAEYCDRFLIQD 570
Cdd:cd03237 166 EKTAFVVEHDIIMIDYLADRLIVFE 190
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
46-239 |
2.32e-11 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 64.42 E-value: 2.32e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857580 46 RLIALVGPDGAGKSTFMRLLCGLEAPDEGRLsVLGTTP--DPDNEDFTTRIAFMPQTLGLYKTLSCRENLEV----FAGL 119
Cdd:PRK10575 38 KVTGLIGHNGSGKSTLLKMLGRHQPPSEGEI-LLDAQPleSWSSKAFARKVAYLPQQLPAAEGMTVRELVAIgrypWHGA 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857580 120 RGFEGEADgaaglERRIAELLSMTGLAGFEERQAGKLSGGMKQKLALASALLRIPDLLLLDEPTVGVDPLSRRELWSVVR 199
Cdd:PRK10575 117 LGRFGAAD-----REKVEEAISLVGLKPLAHRLVDSLSGGERQRAWIAMLVAQDSRCLLLDEPTSALDIAHQVDVLALVH 191
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 2553857580 200 RMLADTPMTCVfstAYLEE----AEAADRVLLFESGRIIADENP 239
Cdd:PRK10575 192 RLSQERGLTVI---AVLHDinmaARYCDYLVALRGGEMIAQGTP 232
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
382-555 |
2.61e-11 |
|
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: 62.17 E-value: 2.61e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857580 382 VADTSFEVRRGEIFGLLGPNGAGKTTTFRMLCGLLVPSKGQIEVAgydlrtakagARARIGYVAQKfslygklsveqnlR 461
Cdd:cd03223 17 LKDLSFEIKPGDRLLITGPSGTGKSSLFRALAGLWPWGSGRIGMP----------EGEDLLFLPQR-------------P 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857580 462 YFGRsyGFFGQALQ---DRIdasledfgltdrrdttagsLSFGAKQDLSMACGLIHSPEILFLDEATSGADLASRRAFWR 538
Cdd:cd03223 74 YLPL--GTLREQLIypwDDV-------------------LSGGEQQRLAFARLLLHKPKFVFLDEATSALDEESEDRLYQ 132
|
170
....*....|....*..
gi 2553857580 539 RINALasaGTSVVVTTH 555
Cdd:cd03223 133 LLKEL---GITVISVGH 146
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
368-578 |
2.91e-11 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 64.18 E-value: 2.91e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857580 368 RADGIARKFGNFVAVADTSFEVRRGEIFGLLGPNGAGKTTTFRMLCGLLVPSKGQIEVAG-----YDLRTAKAGARARI- 441
Cdd:PRK11701 8 SVRGLTKLYGPRKGCRDVSFDLYPGEVLGIVGESGSGKTTLLNALSARLAPDAGEVHYRMrdgqlRDLYALSEAERRRLl 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857580 442 ----GYVAQ--KFSLYGKLSVEQNL---------RYFGRSYGFFGQALQD-RIDAsledfgltDRRDTTAGSLSFGAKQD 505
Cdd:PRK11701 88 rtewGFVHQhpRDGLRMQVSAGGNIgerlmavgaRHYGDIRATAGDWLERvEIDA--------ARIDDLPTTFSGGMQQR 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2553857580 506 LSMACGLIHSPEILFLDEATSGADLASRRAFWRRINAL-ASAGTSVVVTTHFLEEAE-YCDRFLIQDAGKVLALG 578
Cdd:PRK11701 160 LQIARNLVTHPRLVFMDEPTGGLDVSVQARLLDLLRGLvRELGLAVVIVTHDLAVARlLAHRLLVMKQGRVVESG 234
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
381-582 |
3.36e-11 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 66.20 E-value: 3.36e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857580 381 AVADTSFEVRRGEIFGLLGPNGAGKTTTFRMLCGLLVPSKGQIEVAGYDLRTAK-AGARARIGYVAQKFSLYGKlSVEQN 459
Cdd:PRK11176 358 ALRNINFKIPAGKTVALVGRSGSGKSTIANLLTRFYDIDEGEILLDGHDLRDYTlASLRNQVALVSQNVHLFND-TIANN 436
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857580 460 LryfgrSYGFFGQALQDRIDASLE-----DF--GLTDRRDTTAG----SLSFGAKQDLSMACGLIHSPEILFLDEATSGA 528
Cdd:PRK11176 437 I-----AYARTEQYSREQIEEAARmayamDFinKMDNGLDTVIGengvLLSGGQRQRIAIARALLRDSPILILDEATSAL 511
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 2553857580 529 DLASRRAFWRRINALASAGTSVVVtTHFLEEAEYCDRFLIQDAGKVLALGTPRE 582
Cdd:PRK11176 512 DTESERAIQAALDELQKNRTSLVI-AHRLSTIEKADEILVVEDGEIVERGTHAE 564
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
362-555 |
4.18e-11 |
|
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: 65.96 E-value: 4.18e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857580 362 ERPVVIRADGIARKFGNFVAVADtSFEVRRGEIFGLLGPNGAGKTTTFRMLCGLLVPSKGQIEVAgydlrtakagarARI 441
Cdd:COG1245 337 EEETLVEYPDLTKSYGGFSLEVE-GGEIREGEVLGIVGPNGIGKTTFAKILAGVLKPDEGEVDED------------LKI 403
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857580 442 GYVAQKFSLYGKLSVEQNLRyfgrsygffgQALQDRIDAS------LEDFGLTDRRDTTAGSLSFGAKQDLSMACGLIHS 515
Cdd:COG1245 404 SYKPQYISPDYDGTVEEFLR----------SANTDDFGSSyykteiIKPLGLEKLLDKNVKDLSGGELQRVAIAACLSRD 473
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 2553857580 516 PEILFLDEATSGADLASRRAFWRRINALA-SAGTSVVVTTH 555
Cdd:COG1245 474 ADLYLLDEPSAHLDVEQRLAVAKAIRRFAeNRGKTAMVVDH 514
|
|
| nickel_nikE |
TIGR02769 |
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a ... |
31-234 |
4.56e-11 |
|
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a multisubunit nickel import ABC transporter complex. Nickel, once imported, may be used in urease and in certain classes of hydrogenase and superoxide dismutase. [Transport and binding proteins, Cations and iron carrying compounds]
Pssm-ID: 131816 [Multi-domain] Cd Length: 265 Bit Score: 63.67 E-value: 4.56e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857580 31 VDGISLKAGGAEAsdrlIALVGPDGAGKSTFMRLLCGLEAPDEGRLSVLGTtpDPDNEDFTTRIAFMpQTLGL-----YK 105
Cdd:TIGR02769 27 LTNVSLSIEEGET----VGLLGRSGCGKSTLARLLLGLEKPAQGTVSFRGQ--DLYQLDRKQRRAFR-RDVQLvfqdsPS 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857580 106 TLSCRENLEVFAG--LRGFEGEAdgAAGLERRIAELLSMTGL-AGFEERQAGKLSGGMKQKLALASALLRIPDLLLLDEP 182
Cdd:TIGR02769 100 AVNPRMTVRQIIGepLRHLTSLD--ESEQKARIAELLDMVGLrSEDADKLPRQLSGGQLQRINIARALAVKPKLIVLDEA 177
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 2553857580 183 TVGVDPLSRRELWSVVRRMLADTPMTCVFSTAYLEEAEA-ADRVLLFESGRII 234
Cdd:TIGR02769 178 VSNLDMVLQAVILELLRKLQQAFGTAYLFITHDLRLVQSfCQRVAVMDKGQIV 230
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
29-227 |
4.58e-11 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 63.57 E-value: 4.58e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857580 29 RAVDGISLKAGGAEasdrLIALVGPDGAGKSTFMRLLCGLEAPDEGRLSVLGT-TPDPDNEDfttriAFMPQTLGLYKTL 107
Cdd:PRK11248 15 PALEDINLTLESGE----LLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDGKpVEGPGAER-----GVVFQNEGLLPWR 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857580 108 SCRENLEVFAGLRGFEGEADgaaglERRIAELLSMTGLAGFEERQAGKLSGGMKQKLALASALLRIPDLLLLDEPTVGVD 187
Cdd:PRK11248 86 NVQDNVAFGLQLAGVEKMQR-----LEIAHQMLKKVGLEGAEKRYIWQLSGGQRQRVGIARALAANPQLLLLDEPFGALD 160
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 2553857580 188 PLSRRELWSVVRRMLADTPMTCVFSTAYLEEA--EAADRVLL 227
Cdd:PRK11248 161 AFTREQMQTLLLKLWQETGKQVLLITHDIEEAvfMATELVLL 202
|
|
| tagH |
PRK13545 |
teichoic acids export protein ATP-binding subunit; Provisional |
381-583 |
5.17e-11 |
|
teichoic acids export protein ATP-binding subunit; Provisional
Pssm-ID: 184130 [Multi-domain] Cd Length: 549 Bit Score: 65.30 E-value: 5.17e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857580 381 AVADTSFEVRRGEIFGLLGPNGAGKTTTFRMLCGLLVPSKGQIEVAGydlrtakagaraRIGYVAQKFSLYGKLSVEQNL 460
Cdd:PRK13545 39 ALNNISFEVPEGEIVGIIGLNGSGKSTLSNLIAGVTMPNKGTVDIKG------------SAALIAISSGLNGQLTGIENI 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857580 461 RYFGRSYGFFGQALQDRIDASLEDFGLTDRRDTTAGSLSFGAKQDLSMACGLIHSPEILFLDEATSGADLASRRAFWRRI 540
Cdd:PRK13545 107 ELKGLMMGLTKEKIKEIIPEIIEFADIGKFIYQPVKTYSSGMKSRLGFAISVHINPDILVIDEALSVGDQTFTKKCLDKM 186
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 2553857580 541 NALASAGTSVVVTTHFLEEAE-YCDRFLIQDAGKVLALGTPREV 583
Cdd:PRK13545 187 NEFKEQGKTIFFISHSLSQVKsFCTKALWLHYGQVKEYGDIKEV 230
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
394-583 |
5.28e-11 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 64.51 E-value: 5.28e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857580 394 IFGLlgpNGAGKTTTFRMLCGLLVPSKGQIEVAGYDLRTAKAGA-----RARIGYVAQKFSLYGKLSVEQNLRYfgrSYG 468
Cdd:PRK11144 29 IFGR---SGAGKTSLINAISGLTRPQKGRIVLNGRVLFDAEKGIclppeKRRIGYVFQDARLFPHYKVRGNLRY---GMA 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857580 469 FFGQALQDRIDASLedfGLTDRRDTTAGSLSFGAKQDLSMACGLIHSPEILFLDEATSGADLASRRAFWRRINALA-SAG 547
Cdd:PRK11144 103 KSMVAQFDKIVALL---GIEPLLDRYPGSLSGGEKQRVAIGRALLTAPELLLMDEPLASLDLPRKRELLPYLERLArEIN 179
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 2553857580 548 TSVVVTTHFLEE----AeycDRFLIQDAGKVLALGTPREV 583
Cdd:PRK11144 180 IPILYVSHSLDEilrlA---DRVVVLEQGKVKAFGPLEEV 216
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
384-573 |
5.38e-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: 62.49 E-value: 5.38e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857580 384 DTSFEVRRGEIFGLLGPNGAGKTTTFRMLCGLLVPSKGQIEVAGydlrtakagaraRIGYVAQK-FSLYGklSVEQNLRy 462
Cdd:cd03250 23 DINLEVPKGELVAIVGPVGSGKSSLLSALLGELEKLSGSVSVPG------------SIAYVSQEpWIQNG--TIRENIL- 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857580 463 FGRSYgffgqaLQDRIDASLE------DFGLTDRRD-TTAG----SLSFGAKQDLSMACGLIHSPEILFLDEATSGADLA 531
Cdd:cd03250 88 FGKPF------DEERYEKVIKacalepDLEILPDGDlTEIGekgiNLSGGQKQRISLARAVYSDADIYLLDDPLSAVDAH 161
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 2553857580 532 SRRAFWRR-INALASAGTSVVVTTHFLEEAEYCDRFLIQDAGK 573
Cdd:cd03250 162 VGRHIFENcILGLLLNNKTRILVTHQLQLLPHADQIVVLDNGR 204
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
386-555 |
6.19e-11 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 62.27 E-value: 6.19e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857580 386 SFEVRRGEIFGLLGPNGAGKTTTFRMLCGLLVPSKGQIEVAGYDLRTAKAGARARIGYVAQKFSLYGKLSVEQNLRYfgr 465
Cdd:PRK13540 21 SFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEILFERQSIKKDLCTYQKQLCFVGHRSGINPYLTLRENCLY--- 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857580 466 SYGFFGQALQdrIDASLEDFGLTDRRDTTAGSLSFGAKQDLSMACGLIHSPEILFLDEATSGADLASRRAFWRRINALAS 545
Cdd:PRK13540 98 DIHFSPGAVG--ITELCRLFSLEHLIDYPCGLLSSGQKRQVALLRLWMSKAKLWLLDEPLVALDELSLLTIITKIQEHRA 175
|
170
....*....|
gi 2553857580 546 AGTSVVVTTH 555
Cdd:PRK13540 176 KGGAVLLTSH 185
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
382-567 |
6.33e-11 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 65.21 E-value: 6.33e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857580 382 VADTSFEVRRGEifGLL--GPNGAGKTTTFRMLCGLLVPSKGQIEVAgydlrtakagARARIGYVAQKfsLY---Gklsv 456
Cdd:COG4178 379 LEDLSLSLKPGE--RLLitGPSGSGKSTLLRAIAGLWPYGSGRIARP----------AGARVLFLPQR--PYlplG---- 440
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857580 457 eqNLRyfgrsygffgQAL----------QDRIDASLEDFGL---TDRRDTTAG---SLSFGAKQDLSMACGLIHSPEILF 520
Cdd:COG4178 441 --TLR----------EALlypataeafsDAELREALEAVGLghlAERLDEEADwdqVLSLGEQQRLAFARLLLHKPDWLF 508
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 2553857580 521 LDEATSGADLASRRAFWRRINAlASAGTSVVVTTHFLEEAEYCDRFL 567
Cdd:COG4178 509 LDEATSALDEENEAALYQLLRE-ELPGTTVISVGHRSTLAAFHDRVL 554
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
6-241 |
6.62e-11 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 64.48 E-value: 6.62e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857580 6 APAIRLEGVVKTFPNpldaarpIRAVDGISLKAGGAEasdrLIALVGPDGAGKSTFMRLLCGLEAPDEGRLSVLGTtpDP 85
Cdd:PRK09536 1 MPMIDVSDLSVEFGD-------TTVLDGVDLSVREGS----LVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGD--DV 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857580 86 DNEDFTT---RIAFMPQTLGLYKTLSCRENLEVfaGLRGFEGEADGAAGLERRIAE-LLSMTGLAGFEERQAGKLSGGMK 161
Cdd:PRK09536 68 EALSARAasrRVASVPQDTSLSFEFDVRQVVEM--GRTPHRSRFDTWTETDRAAVErAMERTGVAQFADRPVTSLSGGER 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857580 162 QKLALASALLRIPDLLLLDEPTVGVDPLSRRELWSVVRRmLADTPMTCVFSTAYLE-EAEAADRVLLFESGRIIADENPQ 240
Cdd:PRK09536 146 QRVLLARALAQATPVLLLDEPTASLDINHQVRTLELVRR-LVDDGKTAVAAIHDLDlAARYCDELVLLADGRVRAAGPPA 224
|
.
gi 2553857580 241 S 241
Cdd:PRK09536 225 D 225
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
365-582 |
8.34e-11 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 63.90 E-value: 8.34e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857580 365 VVIRadGIARKFGNFVAVADTSFEVRRGEIFGLLGPNGAGKTTTFRMLCGLLVPSKGQIEVAGY---DLRTAKAGararI 441
Cdd:PRK11000 4 VTLR--NVTKAYGDVVISKDINLDIHEGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLFIGEKrmnDVPPAERG----V 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857580 442 GYVAQKFSLYGKLSVEQNLRyFGRSYGFFGQA-LQDRIDASLEDFGLTDRRDTTAGSLSFGAKQDLSMACGLIHSPEILF 520
Cdd:PRK11000 78 GMVFQSYALYPHLSVAENMS-FGLKLAGAKKEeINQRVNQVAEVLQLAHLLDRKPKALSGGQRQRVAIGRTLVAEPSVFL 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2553857580 521 LDEATSGADLASRRAFWRRINAL-ASAGTSVVVTTHFLEEA-EYCDRFLIQDAGKVLALGTPRE 582
Cdd:PRK11000 157 LDEPLSNLDAALRVQMRIEISRLhKRLGRTMIYVTHDQVEAmTLADKIVVLDAGRVAQVGKPLE 220
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
9-234 |
9.24e-11 |
|
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: 64.74 E-value: 9.24e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857580 9 IRLEGVVKTFPnpldaARPIRAVDGISLKAGGAEasdrLIALVGPDGAGKSTFMRLLCGLEAPDEGRLSVLGTtpdpDNE 88
Cdd:TIGR02203 331 VEFRNVTFRYP-----GRDRPALDSISLVIEPGE----TVALVGRSGSGKSTLVNLIPRFYEPDSGQILLDGH----DLA 397
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857580 89 DFTTR-----IAFMPQTLGLYktlscreNLEVFAGLR-GFEGEADGAaglerRIAELLSMTGLAGFEER----------- 151
Cdd:TIGR02203 398 DYTLAslrrqVALVSQDVVLF-------NDTIANNIAyGRTEQADRA-----EIERALAAAYAQDFVDKlplgldtpige 465
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857580 152 QAGKLSGGMKQKLALASALLRIPDLLLLDEPTVGVDPLSRRELWSVVRRMLADTpmTCVFSTAYLEEAEAADRVLLFESG 231
Cdd:TIGR02203 466 NGVLLSGGQRQRLAIARALLKDAPILILDEATSALDNESERLVQAALERLMQGR--TTLVIAHRLSTIEKADRIVVMDDG 543
|
...
gi 2553857580 232 RII 234
Cdd:TIGR02203 544 RIV 546
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
47-244 |
1.33e-10 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 63.51 E-value: 1.33e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857580 47 LIALVGPDGAGKSTFMRLLCGLEAPDEGRLSVLGT----TPDPD-NEDFTTRIAFMPQTLGLYKTLSCRENlevfaglRG 121
Cdd:PRK10070 56 IFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVdiakISDAElREVRRKKIAMVFQSFALMPHMTVLDN-------TA 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857580 122 FEGEADGAAGLERRIAEL--LSMTGLAGFEERQAGKLSGGMKQKLALASALLRIPDLLLLDEPTVGVDPLSRRELWSVVR 199
Cdd:PRK10070 129 FGMELAGINAEERREKALdaLRQVGLENYAHSYPDELSGGMRQRVGLARALAINPDILLMDEAFSALDPLIRTEMQDELV 208
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 2553857580 200 RMLADTPMTCVFSTAYLEEA-EAADRVLLFESGRIIADENPQSFIS 244
Cdd:PRK10070 209 KLQAKHQRTIVFISHDLDEAmRIGDRIAIMQNGEVVQVGTPDEILN 254
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
22-236 |
1.43e-10 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 62.40 E-value: 1.43e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857580 22 LDAARPIRAV-DGISLKAGGAEAsdrlIALVGPDGAGKSTFMRLLCGLEAPDEGRLSVLGTT----PDPDNEDFTTRI-- 94
Cdd:PRK10419 18 LSGKHQHQTVlNNVSLSLKSGET----VALLGRSGCGKSTLARLLVGLESPSQGNVSWRGEPlaklNRAQRKAFRRDIqm 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857580 95 -------AFMPQtlglyKTL--SCRENLEVFAGLRgfegeadgAAGLERRIAELLSMTGLA-GFEERQAGKLSGGMKQKL 164
Cdd:PRK10419 94 vfqdsisAVNPR-----KTVreIIREPLRHLLSLD--------KAERLARASEMLRAVDLDdSVLDKRPPQLSGGQLQRV 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2553857580 165 ALASALLRIPDLLLLDEPTVGVDPLSRRELWSVVRRMLADTPMTCVFSTAYLEEAEA-ADRVLLFESGRIIAD 236
Cdd:PRK10419 161 CLARALAVEPKLLILDEAVSNLDLVLQAGVIRLLKKLQQQFGTACLFITHDLRLVERfCQRVMVMDNGQIVET 233
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
28-253 |
1.56e-10 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 61.82 E-value: 1.56e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857580 28 IRAVDGISLKAGGAEasdrLIALVGPDGAGKSTFMRLLCGLEAPDEGRLSVLGT--TPDPDNEDFTTRIAFMPQTLGLYK 105
Cdd:PRK11614 18 IQALHEVSLHINQGE----IVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDGKdiTDWQTAKIMREAVAIVPEGRRVFS 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857580 106 TLSCRENLevfaGLRGFEGEADGAAGLERRIAELLSMTglagFEER--QAGKLSGGMKQKLALASALLRIPDLLLLDEPT 183
Cdd:PRK11614 94 RMTVEENL----AMGGFFAERDQFQERIKWVYELFPRL----HERRiqRAGTMSGGEQQMLAIGRALMSQPRLLLLDEPS 165
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2553857580 184 VGVDPLSRRELWSVVRRmLADTPMTCVFSTAYLEEA-EAADRVLLFESGRIIADENPQSFISRAKGRTYLL 253
Cdd:PRK11614 166 LGLAPIIIQQIFDTIEQ-LREQGMTIFLVEQNANQAlKLADRGYVLENGHVVLEDTGDALLANEAVRSAYL 235
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
381-589 |
2.37e-10 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 63.45 E-value: 2.37e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857580 381 AVADTSFEVRRGEIFGLLGPNGAGKTTTFRMLCGLLVPSKGQIEVAGYDLRTAKAGA-RARIGYVAQKFSLYGKLSVEQN 459
Cdd:PRK10522 338 SVGPINLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKPVTAEQPEDyRKLFSAVFTDFHLFDQLLGPEG 417
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857580 460 lryfgrsygffGQALQDRIDASLEDFGLTDRRDTTAG-----SLSFGAKQDLSMACGLIHSPEILFLDEATSGADLASRR 534
Cdd:PRK10522 418 -----------KPANPALVEKWLERLKMAHKLELEDGrisnlKLSKGQKKRLALLLALAEERDILLLDEWAADQDPHFRR 486
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 2553857580 535 AFWRR-INALASAGTSVVVTTHFLEEAEYCDRFLIQDAGKVLAL-GTPREVKQRAAV 589
Cdd:PRK10522 487 EFYQVlLPLLQEMGKTIFAISHDDHYFIHADRLLEMRNGQLSELtGEERDAASRDAV 543
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
377-588 |
2.70e-10 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 62.17 E-value: 2.70e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857580 377 GNFVAVADTSFEVRRGEIFGLLGPNGAGKTTTFRMLCGLLVPSKGQIEVAGYDLRTAKAGARArIGYVAQKFSLYGKLSV 456
Cdd:PRK11650 15 GKTQVIKGIDLDVADGEFIVLVGPSGCGKSTLLRMVAGLERITSGEIWIGGRVVNELEPADRD-IAMVFQNYALYPHMSV 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857580 457 EQNLRYFGRSYGFFGQALQDRIDA---SLEDFGLTDRRDTtagSLSFGAKQDLSMACGLIHSPEILFLDEATSGADLASR 533
Cdd:PRK11650 94 RENMAYGLKIRGMPKAEIEERVAEaarILELEPLLDRKPR---ELSGGQRQRVAMGRAIVREPAVFLFDEPLSNLDAKLR 170
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2553857580 534 -------RAFWRRINAlasagTSVVVTTHFLEEAEYCDRFLIQDAGKVLALGTPREVKQRAA 588
Cdd:PRK11650 171 vqmrleiQRLHRRLKT-----TSLYVTHDQVEAMTLADRVVVMNGGVAEQIGTPVEVYEKPA 227
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
11-233 |
2.88e-10 |
|
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; TAP (Transporter Associated with Antigen Processing) is essential for peptide delivery from the cytosol into the lumen of the endoplasmic reticulum (ER), where these peptides are loaded on major histocompatibility complex (MHC) I molecules. Loaded MHC I leave the ER and display their antigenic cargo on the cell surface to cytotoxic T cells. Subsequently, virus-infected or malignantly transformed cells can be eliminated. TAP belongs to the large family of ATP-binding cassette (ABC) transporters, which translocate a vast variety of solutes across membranes.
Pssm-ID: 213215 [Multi-domain] Cd Length: 226 Bit Score: 60.56 E-value: 2.88e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857580 11 LEGVVK----TFPNPLDAARPIRAVDGISLKAGgaeasdRLIALVGPDGAGKSTFMRLLCGLEAPDEGRLSVLGT-TPDP 85
Cdd:cd03248 8 LKGIVKfqnvTFAYPTRPDTLVLQDVSFTLHPG------EVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDGKpISQY 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857580 86 DNEDFTTRIAFMPQTLGLYKTlSCRENLEVFAGLRGFEG--EADGAAGLERRIAELLSmtglaGFEE---RQAGKLSGGM 160
Cdd:cd03248 82 EHKYLHSKVSLVGQEPVLFAR-SLQDNIAYGLQSCSFECvkEAAQKAHAHSFISELAS-----GYDTevgEKGSQLSGGQ 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2553857580 161 KQKLALASALLRIPDLLLLDEPTVGVDPLSRRelwsVVRRMLADTP--MTCVFSTAYLEEAEAADRVLLFESGRI 233
Cdd:cd03248 156 KQRVAIARALIRNPQVLILDEATSALDAESEQ----QVQQALYDWPerRTVLVIAHRLSTVERADQILVLDGGRI 226
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
29-244 |
3.41e-10 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 60.80 E-value: 3.41e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857580 29 RAVDGISLkaggAEASDRLIALVGPDGAGKSTFMRLLCGLEAPDEGRLSVLGTtpdpDNEDFTTR-----IAFMPQTLGL 103
Cdd:PRK11231 16 RILNDLSL----SLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDK----PISMLSSRqlarrLALLPQHHLT 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857580 104 YKTLSCRENLEV----FAGLRGFEGEADgaaglERRIAELLSMTGLAGFEERQAGKLSGGMKQKLALASALLRIPDLLLL 179
Cdd:PRK11231 88 PEGITVRELVAYgrspWLSLWGRLSAED-----NARVNQAMEQTRINHLADRRLTDLSGGQRQRAFLAMVLAQDTPVVLL 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2553857580 180 DEPTVGVDpLSRR-ELWSVVRRMlADTPMTCVFSTAYLEEA-EAADRVLLFESGRIIADENPQSFIS 244
Cdd:PRK11231 163 DEPTTYLD-INHQvELMRLMREL-NTQGKTVVTVLHDLNQAsRYCDHLVVLANGHVMAQGTPEEVMT 227
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
30-240 |
3.81e-10 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 61.02 E-value: 3.81e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857580 30 AVDGISLKAGGAEASdrliALVGPDGAGKSTFMRLLCGLEAPDEGRLsVLGTTP--------------------DPDNED 89
Cdd:PRK13636 21 ALKGININIKKGEVT----AILGGNGAGKSTLFQNLNGILKPSSGRI-LFDGKPidysrkglmklresvgmvfqDPDNQL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857580 90 FTTR----IAFMPQTLGLYKTlscrenlEVfaglrgfegeadgaaglERRIAELLSMTGLAGFEERQAGKLSGGMKQKLA 165
Cdd:PRK13636 96 FSASvyqdVSFGAVNLKLPED-------EV-----------------RKRVDNALKRTGIEHLKDKPTHCLSFGQKKRVA 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2553857580 166 LASALLRIPDLLLLDEPTVGVDPLSRRELWSVVRRMLADTPMTCVFSTAYLEE-AEAADRVLLFESGRIIADENPQ 240
Cdd:PRK13636 152 IAGVLVMEPKVLVLDEPTAGLDPMGVSEIMKLLVEMQKELGLTIIIATHDIDIvPLYCDNVFVMKEGRVILQGNPK 227
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
392-582 |
3.94e-10 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 62.97 E-value: 3.94e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857580 392 GEIFGLLGPNGAGKTTTFRMLCGLLVPSKGQIEVAGYDLRTAKAGARaRIGYVAQKFSLYGKLSVEQNLRYFGRSYGFFG 471
Cdd:PLN03211 94 GEILAVLGPSGSGKSTLLNALAGRIQGNNFTGTILANNRKPTKQILK-RTGFVTQDDILYPHLTVRETLVFCSLLRLPKS 172
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857580 472 QALQDRI---DASLEDFGLTDRRDTTAGS-----LSFGAKQDLSMACGLIHSPEILFLDEATSGADLASRRAFWRRINAL 543
Cdd:PLN03211 173 LTKQEKIlvaESVISELGLTKCENTIIGNsfirgISGGERKRVSIAHEMLINPSLLILDEPTSGLDATAAYRLVLTLGSL 252
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 2553857580 544 ASAGTSVVVTTHFLEEAEY--CDRFLIQDAGKVLALGTPRE 582
Cdd:PLN03211 253 AQKGKTIVTSMHQPSSRVYqmFDSVLVLSEGRCLFFGKGSD 293
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
3-253 |
3.95e-10 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 62.53 E-value: 3.95e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857580 3 KASAPAIRLEGVVKTFPNpldaaRPIRAVDGISL--KAGgaeasdRLIALVGPDGAGKSTFMRLLCGLEAPDEGRLSVLG 80
Cdd:PRK11160 333 AADQVSLTLNNVSFTYPD-----QPQPVLKGLSLqiKAG------EKVALLGRTGCGKSTLLQLLTRAWDPQQGEILLNG 401
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857580 81 TT-PDPDNEDFTTRIAFMPQTLGLYKTlSCRENLEVfaglrgfegeADGAAGLERrIAELLSMTGLAGFEERQAG----- 154
Cdd:PRK11160 402 QPiADYSEAALRQAISVVSQRVHLFSA-TLRDNLLL----------AAPNASDEA-LIEVLQQVGLEKLLEDDKGlnawl 469
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857580 155 -----KLSGGMKQKLALASALLRIPDLLLLDEPTVGVDPLSRRELWSVVRRMLADTpmTCVFSTAYLEEAEAADRVLLFE 229
Cdd:PRK11160 470 geggrQLSGGEQRRLGIARALLHDAPLLLLDEPTEGLDAETERQILELLAEHAQNK--TVLMITHRLTGLEQFDRICVMD 547
|
250 260
....*....|....*....|....
gi 2553857580 230 SGRIIADENPQSFISRaKGRTYLL 253
Cdd:PRK11160 548 NGQIIEQGTHQELLAQ-QGRYYQL 570
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
48-236 |
4.26e-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: 62.83 E-value: 4.26e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857580 48 IALVGPDGAGKSTFMRLLCGLEAPDEGRLSVLGTT-PDPDNEDFTTRIAFMPQTLGLYkTLSCRENLEVFAGLRGFEGEA 126
Cdd:TIGR01193 503 TTIVGMSGSGKSTLAKLLVGFFQARSGEILLNGFSlKDIDRHTLRQFINYLPQEPYIF-SGSILENLLLGAKENVSQDEI 581
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857580 127 DGAAglerRIAEL------LSMtglaGFEER---QAGKLSGGMKQKLALASALLRIPDLLLLDEPTVGVDPLSRRElwsV 197
Cdd:TIGR01193 582 WAAC----EIAEIkddienMPL----GYQTElseEGSSISGGQKQRIALARALLTDSKVLILDESTSNLDTITEKK---I 650
|
170 180 190
....*....|....*....|....*....|....*....
gi 2553857580 198 VRRMLADTPMTCVFSTAYLEEAEAADRVLLFESGRIIAD 236
Cdd:TIGR01193 651 VNNLLNLQDKTIIFVAHRLSVAKQSDKIIVLDHGKIIEQ 689
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
379-593 |
5.15e-10 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 60.79 E-value: 5.15e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857580 379 FVAVADTSFEVRRGEIFGLLGPNGAGKTTTFRMLCGLLVPSKGQIEVAGY----DLRTAKAGARAR--IGYVAQ--KFSL 450
Cdd:PRK13645 24 FKALNNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGLIISETGQTIVGDYaipaNLKKIKEVKRLRkeIGLVFQfpEYQL 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857580 451 YGKlSVEQNLRYFGRSYGFFGQALQDRIDASLEDFGL-TDRRDTTAGSLSFGAKQDLSMACGLIHSPEILFLDEATSGAD 529
Cdd:PRK13645 104 FQE-TIEKDIAFGPVNLGENKQEAYKKVPELLKLVQLpEDYVKRSPFELSGGQKRRVALAGIIAMDGNTLVLDEPTGGLD 182
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2553857580 530 LASRRAF---WRRINalASAGTSVVVTTHFLEEA-EYCDRFLIQDAGKVLALGTPREVKQRAAVLSAV 593
Cdd:PRK13645 183 PKGEEDFinlFERLN--KEYKKRIIMVTHNMDQVlRIADEVIVMHEGKVISIGSPFEIFSNQELLTKI 248
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
23-234 |
5.38e-10 |
|
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC transporter that is expressed in the mitochondria. Although the specific function of ATM1 is unknown, its disruption results in the accumulation of excess mitochondrial iron, loss of mitochondrial cytochromes, oxidative damage to mitochondrial DNA, and decreased levels of cytosolic heme proteins. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213220 [Multi-domain] Cd Length: 236 Bit Score: 59.94 E-value: 5.38e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857580 23 DAARPIraVDGISLKAGGAEAsdrlIALVGPDGAGKSTFMRLLCGLEAPDEGRLSVLGT-TPDPDNEDFTTRIAFMPQTL 101
Cdd:cd03253 11 DPGRPV--LKDVSFTIPAGKK----VAIVGPSGSGKSTILRLLFRFYDVSSGSILIDGQdIREVTLDSLRRAIGVVPQDT 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857580 102 GLYKTlSCRENL----------EVFaglrgfegEADGAAGLERRIAELL----SMTGlagfeERqaG-KLSGGMKQKLAL 166
Cdd:cd03253 85 VLFND-TIGYNIrygrpdatdeEVI--------EAAKAAQIHDKIMRFPdgydTIVG-----ER--GlKLSGGEKQRVAI 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2553857580 167 ASALLRIPDLLLLDEPTVGVDPLSRRELWSVVRRMLADTpmTCVFSTAYLEEAEAADRVLLFESGRII 234
Cdd:cd03253 149 ARAILKNPPILLLDEATSALDTHTEREIQAALRDVSKGR--TTIVIAHRLSTIVNADKIIVLKDGRIV 214
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
47-253 |
7.01e-10 |
|
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: 59.81 E-value: 7.01e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857580 47 LIALVGPDGAGKSTFMRLLCGLEAPDEGRLSVLG---TTPDPdnEDFTTRIAFMPQTLGLYKTlSCRENLEVfaglrgfe 123
Cdd:cd03252 30 VVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGhdlALADP--AWLRRQVGVVLQENVLFNR-SIRDNIAL-------- 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857580 124 geADGAAGLERrIAELLSMTGLAGF------------EERQAGkLSGGMKQKLALASALLRIPDLLLLDEPTVGVDPLSR 191
Cdd:cd03252 99 --ADPGMSMER-VIEAAKLAGAHDFiselpegydtivGEQGAG-LSGGQRQRIAIARALIHNPRILIFDEATSALDYESE 174
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2553857580 192 RELWSVVRRMLADTpmTCVFSTAYLEEAEAADRVLLFESGRIIADENPQSFISRaKGRTYLL 253
Cdd:cd03252 175 HAIMRNMHDICAGR--TVIIIAHRLSTVKNADRIIVMEKGRIVEQGSHDELLAE-NGLYAYL 233
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
30-245 |
7.47e-10 |
|
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: 59.55 E-value: 7.47e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857580 30 AVDGISLKAGGAEasdrLIALVGPDGAGKSTFMRLLCGLEAPDEGRLSVLGTtpdpDNEDFT-----TRIAFMPQTLGLY 104
Cdd:cd03254 18 VLKDINFSIKPGE----TVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGI----DIRDISrkslrSMIGVVLQDTFLF 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857580 105 KTlSCRENLevfaglRGFEGEADgaaglERRIAELLSMTGLAGFEER-----------QAGKLSGGMKQKLALASALLRI 173
Cdd:cd03254 90 SG-TIMENI------RLGRPNAT-----DEEVIEAAKEAGAHDFIMKlpngydtvlgeNGGNLSQGERQLLAIARAMLRD 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2553857580 174 PDLLLLDEPTVGVDPLSRRELWSVVRRMLADTpmTCVFSTAYLEEAEAADRVLLFESGRIIADENPQSFISR 245
Cdd:cd03254 158 PKILILDEATSNIDTETEKLIQEALEKLMKGR--TSIIIAHRLSTIKNADKILVLDDGKIIEEGTHDELLAK 227
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
376-583 |
1.42e-09 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 59.09 E-value: 1.42e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857580 376 FGNFVAVADTSFEVRRGEIFGLLGPNGAGKTTTFRMLCGLL-----VPSKGQIEVAGYDLRTAKAGA---RARIGYVAQK 447
Cdd:PRK14267 14 YGSNHVIKGVDLKIPQNGVFALMGPSGCGKSTLLRTFNRLLelneeARVEGEVRLFGRNIYSPDVDPievRREVGMVFQY 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857580 448 FSLYGKLSVEQN----LRYFGRSYGffGQALQDRIDASLEDFGL----TDRRDTTAGSLSFGAKQDLSMACGLIHSPEIL 519
Cdd:PRK14267 94 PNPFPHLTIYDNvaigVKLNGLVKS--KKELDERVEWALKKAALwdevKDRLNDYPSNLSGGQRQRLVIARALAMKPKIL 171
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2553857580 520 FLDEATSGADLASRRAFWRRINALASAGTSVVVTTHFLEEAEYCDRFLIQDAGKVLALGTPREV 583
Cdd:PRK14267 172 LMDEPTANIDPVGTAKIEELLFELKKEYTIVLVTHSPAQAARVSDYVAFLYLGKLIEVGPTRKV 235
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
9-162 |
1.58e-09 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 58.94 E-value: 1.58e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857580 9 IRLEGVVKTFpnpldAARPIraVDGISL--KAGGaeasdrLIALVGPDGAGKSTFMRLLCGLEAPDEGRLSV----LGTT 82
Cdd:COG4604 2 IEIKNVSKRY-----GGKVV--LDDVSLtiPKGG------ITALIGPNGAGKSTLLSMISRLLPPDSGEVLVdgldVATT 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857580 83 PdpdNEDFTTRIAFMPQTLGLYKTLSCREnlevfagLRGF------EG---EADgaaglERRIAELLSMTGLAGFEERQA 153
Cdd:COG4604 69 P---SRELAKRLAILRQENHINSRLTVRE-------LVAFgrfpysKGrltAED-----REIIDEAIAYLDLEDLADRYL 133
|
....*....
gi 2553857580 154 GKLSGGMKQ 162
Cdd:COG4604 134 DELSGGQRQ 142
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
48-246 |
1.59e-09 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 59.26 E-value: 1.59e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857580 48 IALVGPDGAGKSTFMRLLCGLEAPDEGRLSVLGT--TPDPDNEDFTT-----------------------RIAFMPQTLG 102
Cdd:PRK13634 36 VAIIGHTGSGKSTLLQHLNGLLQPTSGTVTIGERviTAGKKNKKLKPlrkkvgivfqfpehqlfeetvekDICFGPMNFG 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857580 103 LYktlscrenlevfaglrgfEGEAdgaaglERRIAELLSMTGL-AGFEERQAGKLSGGMKQKLALASALLRIPDLLLLDE 181
Cdd:PRK13634 116 VS------------------EEDA------KQKAREMIELVGLpEELLARSPFELSGGQMRRVAIAGVLAMEPEVLVLDE 171
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2553857580 182 PTVGVDPLSRRELWSVVRRMLADTPMTCVFSTAYLEEAEA-ADRVLLFESGRIIADENPQSFISRA 246
Cdd:PRK13634 172 PTAGLDPKGRKEMMEMFYKLHKEKGLTTVLVTHSMEDAARyADQIVVMHKGTVFLQGTPREIFADP 237
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
28-234 |
2.16e-09 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 58.39 E-value: 2.16e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857580 28 IRAVDGISLkaggaEASDRLI-ALVGPDGAGKSTFMRLLCGL-----EAPDEGRLSVLGTTP-DPDNEDFTTRIAFMPQT 100
Cdd:PRK14247 16 VEVLDGVNL-----EIPDNTItALMGPSGSGKSTLLRVFNRLielypEARVSGEVYLDGQDIfKMDVIELRRRVQMVFQI 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857580 101 LGLYKTLSCRENleVFAGLRgFEGEADGAAGLERRIAELLSMTGLagFEERQ------AGKLSGGMKQKLALASALLRIP 174
Cdd:PRK14247 91 PNPIPNLSIFEN--VALGLK-LNRLVKSKKELQERVRWALEKAQL--WDEVKdrldapAGKLSGGQQQRLCIARALAFQP 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2553857580 175 DLLLLDEPTVGVDPLSRRELWSVVRRMLADtpMTCVFSTAYLEE-AEAADRVLLFESGRII 234
Cdd:PRK14247 166 EVLLADEPTANLDPENTAKIESLFLELKKD--MTIVLVTHFPQQaARISDYVAFLYKGQIV 224
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
24-239 |
2.18e-09 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 58.46 E-value: 2.18e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857580 24 AARPIRAVDGISLKAGGAEASD---------RLIALVGPDGAGKSTFMRLLCGLEAPDEGRLSVLGTtpdpdnedfttRI 94
Cdd:PRK11300 1 MSQPLLSVSGLMMRFGGLLAVNnvnlevreqEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTILLRGQ-----------HI 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857580 95 AFMP-------------QTLGLYKTLSCRENLEV----------FAGL------RGFEGEAdgaagLERrIAELLSMTGL 145
Cdd:PRK11300 70 EGLPghqiarmgvvrtfQHVRLFREMTVIENLLVaqhqqlktglFSGLlktpafRRAESEA-----LDR-AATWLERVGL 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857580 146 AGFEERQAGKLSGGMKQKLALASALLRIPDLLLLDEPTVGVDPLSRRELWSVV---RR------MLADTPMTCVFSTayl 216
Cdd:PRK11300 144 LEHANRQAGNLAYGQQRRLEIARCMVTQPEILMLDEPAAGLNPKETKELDELIaelRNehnvtvLLIEHDMKLVMGI--- 220
|
250 260
....*....|....*....|...
gi 2553857580 217 eeaeaADRVLLFESGRIIADENP 239
Cdd:PRK11300 221 -----SDRIYVVNQGTPLANGTP 238
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
381-565 |
2.30e-09 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 58.25 E-value: 2.30e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857580 381 AVADTSFEVRRGEIFGLLGPNGAGKTTTFRML--CGLLVPS---KGQIEVAGYDL---RTAKAGARARIGYVAQKFSLYg 452
Cdd:PRK14239 20 ALNSVSLDFYPNEITALIGPSGSGKSTLLRSInrMNDLNPEvtiTGSIVYNGHNIyspRTDTVDLRKEIGMVFQQPNPF- 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857580 453 KLSVEQNLRYFGRSYGFFGQALQDR------IDASLEDfGLTDRRDTTAGSLSFGAKQDLSMACGLIHSPEILFLDEATS 526
Cdd:PRK14239 99 PMSIYENVVYGLRLKGIKDKQVLDEavekslKGASIWD-EVKDRLHDSALGLSGGQQQRVCIARVLATSPKIILLDEPTS 177
|
170 180 190
....*....|....*....|....*....|....*....
gi 2553857580 527 GADLASRRAFWRRINALASAGTSVVVTTHFLEEAEYCDR 565
Cdd:PRK14239 178 ALDPISAGKIEETLLGLKDDYTMLLVTRSMQQASRISDR 216
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
32-201 |
2.59e-09 |
|
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: 60.18 E-value: 2.59e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857580 32 DGISLKAGGAEAS-DRLIALVGPDGAGKSTFMRLLCGLEAPDEGRLsvlgttpdpdneDFTTRIAFMPQtlglYktLSCR 110
Cdd:COG1245 352 GGFSLEVEGGEIReGEVLGIVGPNGIGKTTFAKILAGVLKPDEGEV------------DEDLKISYKPQ----Y--ISPD 413
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857580 111 ENLEVFAGLRGFEGEADGAAGLERRIAELLSMTGLAgfeERQAGKLSGGMKQKLALASALLRIPDLLLLDEPTVGVDPLS 190
Cdd:COG1245 414 YDGTVEEFLRSANTDDFGSSYYKTEIIKPLGLEKLL---DKNVKDLSGGELQRVAIAACLSRDADLYLLDEPSAHLDVEQ 490
|
170
....*....|.
gi 2553857580 191 RRELWSVVRRM 201
Cdd:COG1245 491 RLAVAKAIRRF 501
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
362-523 |
3.10e-09 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 59.82 E-value: 3.10e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857580 362 ERPVVIRADGIARKFGNFVAVADTSfEVRRGEIFGLLGPNGAGKTTTFRMLCGLLVPSKGQIEVagyDLrtakagaraRI 441
Cdd:PRK13409 336 ERETLVEYPDLTKKLGDFSLEVEGG-EIYEGEVIGIVGPNGIGKTTFAKLLAGVLKPDEGEVDP---EL---------KI 402
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857580 442 GYVAQKFSLYGKLSVEQNLRyfgrsygffgqALQDRIDAS------LEDFGLTDRRDTTAGSLSFGAKQDLSMACGLIHS 515
Cdd:PRK13409 403 SYKPQYIKPDYDGTVEDLLR-----------SITDDLGSSyykseiIKPLQLERLLDKNVKDLSGGELQRVAIAACLSRD 471
|
....*...
gi 2553857580 516 PEILFLDE 523
Cdd:PRK13409 472 ADLYLLDE 479
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
4-213 |
3.33e-09 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 58.36 E-value: 3.33e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857580 4 ASAPAIRLEGVVKTFPNPLDAARpiravDGISLKAGGAEAsdrliALVGPDGAGKSTFMRLLCGLEAPDEGRLSVLGTtp 83
Cdd:PRK15056 2 MQQAGIVVNDVTVTWRNGHTALR-----DASFTVPGGSIA-----ALVGVNGSGKSTLFKALMGFVRLASGKISILGQ-- 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857580 84 dPDNEDFTTR-IAFMPQTLGLYKTLSCRENLEVFAGLRGFEGEADGAAGLERRIA-ELLSMTGLAGFEERQAGKLSGGMK 161
Cdd:PRK15056 70 -PTRQALQKNlVAYVPQSEEVDWSFPVLVEDVVMMGRYGHMGWLRRAKKRDRQIVtAALARVDMVEFRHRQIGELSGGQK 148
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 2553857580 162 QKLALASALLRIPDLLLLDEPTVGVDPLSRRELWSVVRRmLADTPMTCVFST 213
Cdd:PRK15056 149 KRVFLARAIAQQGQVILLDEPFTGVDVKTEARIISLLRE-LRDEGKTMLVST 199
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
9-234 |
3.81e-09 |
|
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: 57.63 E-value: 3.81e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857580 9 IRLEGVVKTFPnplDAARPIraVDGISLKAGGAEasdrLIALVGPDGAGKSTFMRLLCGLEAPDEGRLSVLGTtpdpDNE 88
Cdd:cd03251 1 VEFKNVTFRYP---GDGPPV--LRDISLDIPAGE----TVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDGH----DVR 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857580 89 DFTTR-----IAFMPQTLGLYKTlSCRENLeVFAGLRGFEGEADGAAglerRIAELLS--MTGLAGFE----ERqAGKLS 157
Cdd:cd03251 68 DYTLAslrrqIGLVSQDVFLFND-TVAENI-AYGRPGATREEVEEAA----RAANAHEfiMELPEGYDtvigER-GVKLS 140
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2553857580 158 GGMKQKLALASALLRIPDLLLLDEPTVGVDPLSRRELWSVVRRMLADtpmTCVFSTAY-LEEAEAADRVLLFESGRII 234
Cdd:cd03251 141 GGQRQRIAIARALLKDPPILILDEATSALDTESERLVQAALERLMKN---RTTFVIAHrLSTIENADRIVVLEDGKIV 215
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
40-234 |
3.82e-09 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 59.68 E-value: 3.82e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857580 40 GAEASDRLIALVGPDGAGKSTFMRLLCGLEAPD-EGRLSVLGTTPDPDNEDFTTRIAFMPQTLGLYKTLSCRENLEVFAG 118
Cdd:TIGR00955 46 GVAKPGELLAVMGSSGAGKTTLMNALAFRSPKGvKGSGSVLLNGMPIDAKEMRAISAYVQQDDLFIPTLTVREHLMFQAH 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857580 119 LRgfEGEADGAAGLERRIAELLSMTGLA-------GFEERQAGkLSGGMKQKLALASALLRIPDLLLLDEPTVGVDPLSR 191
Cdd:TIGR00955 126 LR--MPRRVTKKEKRERVDEVLQALGLRkcantriGVPGRVKG-LSGGERKRLAFASELLTDPPLLFCDEPTSGLDSFMA 202
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 2553857580 192 RELWSVVRRmLADTPMTCVFS----TAYLeeAEAADRVLLFESGRII 234
Cdd:TIGR00955 203 YSVVQVLKG-LAQKGKTIICTihqpSSEL--FELFDKIILMAEGRVA 246
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
371-573 |
5.22e-09 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 58.97 E-value: 5.22e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857580 371 GIARKFGNFVAVADTSFEVRRGEIFGLLGPNGAGKTTTFRMLCGLLVPSKGQIEVAG--YDLRTAKAGARARIGYVAQKF 448
Cdd:PRK10982 3 NISKSFPGVKALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGkeIDFKSSKEALENGISMVHQEL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857580 449 SLYGKLSVEQNLrYFGR--SYGFF---GQALQDRIdASLEDFGL-TDRRDTTAgSLSFGAKQDLSMACGLIHSPEILFLD 522
Cdd:PRK10982 83 NLVLQRSVMDNM-WLGRypTKGMFvdqDKMYRDTK-AIFDELDIdIDPRAKVA-TLSVSQMQMIEIAKAFSYNAKIVIMD 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 2553857580 523 EATSGADLASRRAFWRRINALASAGTSVVVTTHFLEEA-EYCDRFLIQDAGK 573
Cdd:PRK10982 160 EPTSSLTEKEVNHLFTIIRKLKERGCGIVYISHKMEEIfQLCDEITILRDGQ 211
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
22-247 |
5.61e-09 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 57.41 E-value: 5.61e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857580 22 LDAARPIRAVDGISLKAGGAEASDRL---------IALVGPDGAGKSTFMRLLCGLEAPDEG-RLS---VLGTTPDPDNE 88
Cdd:PRK14271 15 VDAAAPAMAAVNLTLGFAGKTVLDQVsmgfparavTSLMGPTGSGKTTFLRTLNRMNDKVSGyRYSgdvLLGGRSIFNYR 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857580 89 D---FTTRIAFMPQTLGLYKtLSCRENleVFAGLRGFE----GEADGAAglERRIAELLSMTGLAGFEERQAGKLSGGMK 161
Cdd:PRK14271 95 DvleFRRRVGMLFQRPNPFP-MSIMDN--VLAGVRAHKlvprKEFRGVA--QARLTEVGLWDAVKDRLSDSPFRLSGGQQ 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857580 162 QKLALASALLRIPDLLLLDEPTVGVDPLSRRELWSVVRRmLADTPMTCVFSTAYLEEAEAADRVLLFESGRIIADENPQS 241
Cdd:PRK14271 170 QLLCLARTLAVNPEVLLLDEPTSALDPTTTEKIEEFIRS-LADRLTVIIVTHNLAQAARISDRAALFFDGRLVEEGPTEQ 248
|
....*.
gi 2553857580 242 FISRAK 247
Cdd:PRK14271 249 LFSSPK 254
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
36-190 |
6.72e-09 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 56.11 E-value: 6.72e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857580 36 LKAGGaeasdrLIALVGPDGAGKSTFMRLLCGLEAPDEGRLSVLGTTPDPDNEDFTTRIAFMPQTLGLYKTLSCRENleV 115
Cdd:PRK13540 24 LPAGG------LLHLKGSNGAGKTTLLKLIAGLLNPEKGEILFERQSIKKDLCTYQKQLCFVGHRSGINPYLTLREN--C 95
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2553857580 116 FAGLRgfegEADGAAGlerrIAELLSMTGLAGFEERQAGKLSGGMKQKLALASALLRIPDLLLLDEPTVGVDPLS 190
Cdd:PRK13540 96 LYDIH----FSPGAVG----ITELCRLFSLEHLIDYPCGLLSSGQKRQVALLRLWMSKAKLWLLDEPLVALDELS 162
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
29-244 |
7.92e-09 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 57.33 E-value: 7.92e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857580 29 RAVDGISLKAggaeASDRLIALVGPDGAGKSTFMRLLCGLEAPDEGRlSVLGTTPDPDNEDFTTRIAFMPQTLGL----- 103
Cdd:PRK13645 25 KALNNTSLTF----KKNKVTCVIGTTGSGKSTMIQLTNGLIISETGQ-TIVGDYAIPANLKKIKEVKRLRKEIGLvfqfp 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857580 104 -YKTLscRENLE---VFAGLRGFEGEADgaagLERRIAELLSMTGLA-GFEERQAGKLSGGMKQKLALASALLRIPDLLL 178
Cdd:PRK13645 100 eYQLF--QETIEkdiAFGPVNLGENKQE----AYKKVPELLKLVQLPeDYVKRSPFELSGGQKRRVALAGIIAMDGNTLV 173
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2553857580 179 LDEPTVGVDPLSRRELWSVVRRMLADTPMTCVFSTAYLEEA-EAADRVLLFESGRIIADENPQSFIS 244
Cdd:PRK13645 174 LDEPTGGLDPKGEEDFINLFERLNKEYKKRIIMVTHNMDQVlRIADEVIVMHEGKVISIGSPFEIFS 240
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
384-568 |
8.28e-09 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 58.89 E-value: 8.28e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857580 384 DTSFEVRRGEIFGLLGPNGAGKTTTFRMLCGLLVPSKGQIEVA-GYDLRTAKAGA-RARIGYVAQ-------------KF 448
Cdd:PTZ00265 403 DLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIIINdSHNLKDINLKWwRSKIGVVSQdpllfsnsiknniKY 482
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857580 449 SLYGKLSVE----------------QNLRYFGRS--YGFFGQALQ--------------------DRIDAS----LEDF- 485
Cdd:PTZ00265 483 SLYSLKDLEalsnyynedgndsqenKNKRNSCRAkcAGDLNDMSNttdsneliemrknyqtikdsEVVDVSkkvlIHDFv 562
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857580 486 -GLTDRRDTTAGS----LSFGAKQDLSMACGLIHSPEILFLDEATSGADLASRRAFWRRINALASAGTSV-VVTTHFLEE 559
Cdd:PTZ00265 563 sALPDKYETLVGSnaskLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQKTINNLKGNENRItIIIAHRLST 642
|
....*....
gi 2553857580 560 AEYCDRFLI 568
Cdd:PTZ00265 643 IRYANTIFV 651
|
|
| PRK13546 |
PRK13546 |
teichoic acids export ABC transporter ATP-binding subunit TagH; |
379-583 |
1.14e-08 |
|
teichoic acids export ABC transporter ATP-binding subunit TagH;
Pssm-ID: 184131 [Multi-domain] Cd Length: 264 Bit Score: 56.36 E-value: 1.14e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857580 379 FVAVADTSFEVRRGEIFGLLGPNGAGKTTTFRMLCGLLVPSKGQIEVAGydlrtakagaraRIGYVAQKFSLYGKLSVEQ 458
Cdd:PRK13546 37 FFALDDISLKAYEGDVIGLVGINGSGKSTLSNIIGGSLSPTVGKVDRNG------------EVSVIAISAGLSGQLTGIE 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857580 459 NLRYFGRSYGFFGQALQDRIDASLEDFGLTDRRDTTAGSLSFGAKQDLSMACGLIHSPEILFLDEATSGADLASRRAFWR 538
Cdd:PRK13546 105 NIEFKMLCMGFKRKEIKAMTPKIIEFSELGEFIYQPVKKYSSGMRAKLGFSINITVNPDILVIDEALSVGDQTFAQKCLD 184
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 2553857580 539 RINALASAGTSVVVTTHFLEEA-EYCDRFLIQDAGKVLALGTPREV 583
Cdd:PRK13546 185 KIYEFKEQNKTIFFVSHNLGQVrQFCTKIAWIEGGKLKDYGELDDV 230
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
29-234 |
1.60e-08 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 57.66 E-value: 1.60e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857580 29 RAVDGISLKAGGAEAsdrlIALVGPDGAGKSTFMRLLCGLEAPDEGRLSVLGTtpdpDNEDFTTR-----IAFMPQTLGL 103
Cdd:PRK13657 349 QGVEDVSFEAKPGQT----VAIVGPTGAGKSTLINLLQRVFDPQSGRILIDGT----DIRTVTRAslrrnIAVVFQDAGL 420
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857580 104 YKTlSCRENLEVfaglrGFEG--EADGAAGLERRIAELLSMTGLAGFE----ERqAGKLSGGMKQKLALASALLRIPDLL 177
Cdd:PRK13657 421 FNR-SIEDNIRV-----GRPDatDEEMRAAAERAQAHDFIERKPDGYDtvvgER-GRQLSGGERQRLAIARALLKDPPIL 493
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857580 178 LLDEPTVGVDPLSRRELWSVVrrmlaDTPMT--CVFSTAY-LEEAEAADRVLLFESGRII 234
Cdd:PRK13657 494 ILDEATSALDVETEAKVKAAL-----DELMKgrTTFIIAHrLSTVRNADRILVFDNGRVV 548
|
|
| PRK13541 |
PRK13541 |
cytochrome c biogenesis protein CcmA; Provisional |
399-555 |
1.84e-08 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184128 [Multi-domain] Cd Length: 195 Bit Score: 54.88 E-value: 1.84e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857580 399 GPNGAGKTTTFRMLCGLLVPSKGQIEVAGYDLRTAkagARARIGYVAQKFSLYGKLSVEQNLRYFGRSYGFfgqalQDRI 478
Cdd:PRK13541 33 GANGCGKSSLLRMIAGIMQPSSGNIYYKNCNINNI---AKPYCTYIGHNLGLKLEMTVFENLKFWSEIYNS-----AETL 104
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2553857580 479 DASLEDFGLTDRRDTTAGSLSFGAKQDLSMACGLIHSPEILFLDEATSGADLASRRAFWRRINALASAGTSVVVTTH 555
Cdd:PRK13541 105 YAAIHYFKLHDLLDEKCYSLSSGMQKIVAIARLIACQSDLWLLDEVETNLSKENRDLLNNLIVMKANSGGIVLLSSH 181
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
29-244 |
1.84e-08 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 55.99 E-value: 1.84e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857580 29 RAVDGISLKAggaeASDRLIALVGPDGAGKSTFMRLLCGLEAPDEGRLSVLG--TTPDPDNE---DFTTRIAFMPQtlgl 103
Cdd:PRK13641 21 KGLDNISFEL----EEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITIAGyhITPETGNKnlkKLRKKVSLVFQ---- 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857580 104 YKTLSCRENL---EVFAGLRGFegeadGAAGLERRIAELLSMTGLaGFEERQAGK----LSGGMKQKLALASALLRIPDL 176
Cdd:PRK13641 93 FPEAQLFENTvlkDVEFGPKNF-----GFSEDEAKEKALKWLKKV-GLSEDLISKspfeLSGGQMRRVAIAGVMAYEPEI 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2553857580 177 LLLDEPTVGVDPLSRRELWSVVRRMLADTPMTCVFSTAYLEEAEAADRVLLFESGRIIADENPQSFIS 244
Cdd:PRK13641 167 LCLDEPAAGLDPEGRKEMMQLFKDYQKAGHTVILVTHNMDDVAEYADDVLVLEHGKLIKHASPKEIFS 234
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
376-618 |
3.01e-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: 57.23 E-value: 3.01e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857580 376 FGNFV-----AVADTSFEVRRGEIFGLLGPNGAGKTTTFRMLCGLLVPSKGQIEVAGydlrtakagaraRIGYVAQkFSL 450
Cdd:TIGR01271 431 FSNFSlyvtpVLKNISFKLEKGQLLAVAGSTGSGKSSLLMMIMGELEPSEGKIKHSG------------RISFSPQ-TSW 497
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857580 451 YGKLSVEQNLrYFGRSYGFFgqALQDRIDASL--EDFGLTDRRDTT-----AGSLSFGAKQDLSMACGLIHSPEILFLDE 523
Cdd:TIGR01271 498 IMPGTIKDNI-IFGLSYDEY--RYTSVIKACQleEDIALFPEKDKTvlgegGITLSGGQRARISLARAVYKDADLYLLDS 574
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857580 524 ATSGADLASRRA-FWRRINALASAGTSVVVTTHfLEEAEYCDRFLIQDAGKVLALGTPREVKQRAAVLSAVSGQSLVVDR 602
Cdd:TIGR01271 575 PFTHLDVVTEKEiFESCLCKLMSNKTRILVTSK-LEHLKKADKILLLHEGVCYFYGTFSELQAKRPDFSSLLLGLEAFDN 653
|
250
....*....|....*.
gi 2553857580 603 MSIEDAFVAIVEAGRR 618
Cdd:TIGR01271 654 FSAERRNSILTETLRR 669
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
46-241 |
3.19e-08 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 55.16 E-value: 3.19e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857580 46 RLIALVGPDGAGKSTFMRLLCGLEAPDEGRLSVlgttpDPDNEDFTTR---------IAFMPQTLGLYKTLSCRENleVF 116
Cdd:PRK11831 34 KITAIMGPSGIGKTTLLRLIGGQIAPDHGEILF-----DGENIPAMSRsrlytvrkrMSMLFQSGALFTDMNVFDN--VA 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857580 117 AGLRgfEGEADGAAGLERRIAELLSMTGLAGFEERQAGKLSGGMKQKLALASALLRIPDLLLLDEPTVGVDPLSRRELWS 196
Cdd:PRK11831 107 YPLR--EHTQLPAPLLHSTVMMKLEAVGLRGAAKLMPSELSGGMARRAALARAIALEPDLIMFDEPFVGQDPITMGVLVK 184
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 2553857580 197 VVRRMLADTPMTC-VFSTAYLEEAEAADRVLLFESGRIIADENPQS 241
Cdd:PRK11831 185 LISELNSALGVTCvVVSHDVPEVLSIADHAYIVADKKIVAHGSAQA 230
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
377-574 |
3.89e-08 |
|
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: 54.86 E-value: 3.89e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857580 377 GNFVaVADTSFEVRRGEIFGLLGPNGAGKTTTFRMLCGLLvPSKGQIEVAGYDLRTAKAGA-RARIGYVAQK---FS--- 449
Cdd:cd03289 16 GNAV-LENISFSISPGQRVGLLGRTGSGKSTLLSAFLRLL-NTEGDIQIDGVSWNSVPLQKwRKAFGVIPQKvfiFSgtf 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857580 450 -----LYGKLSVEQNLRyFGRSYGFFGQALQ--DRIDASLEDFGLTdrrdttagsLSFGAKQDLSMACGLIHSPEILFLD 522
Cdd:cd03289 94 rknldPYGKWSDEEIWK-VAEEVGLKSVIEQfpGQLDFVLVDGGCV---------LSHGHKQLMCLARSVLSKAKILLLD 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 2553857580 523 EATSGADLASRRAFwRRINALASAGTSVVVTTHFLEEAEYCDRFLIQDAGKV 574
Cdd:cd03289 164 EPSAHLDPITYQVI-RKTLKQAFADCTVILSEHRIEAMLECQRFLVIEENKV 214
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
48-234 |
4.92e-08 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 56.01 E-value: 4.92e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857580 48 IALVGPDGAGKSTFMRLLCGLeAPDEGRLSVLGTT-PDPDNEDFTTRIAFMPQTLGLYK-TLscRENLEVfaglrgfege 125
Cdd:PRK11174 379 IALVGPSGAGKTSLLNALLGF-LPYQGSLKINGIElRELDPESWRKHLSWVGQNPQLPHgTL--RDNVLL---------- 445
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857580 126 ADGAAGlERRIAELLSMTGLAGFEER-----------QAGKLSGGMKQKLALASALLRIPDLLLLDEPTVGVDPLSRREL 194
Cdd:PRK11174 446 GNPDAS-DEQLQQALENAWVSEFLPLlpqgldtpigdQAAGLSVGQAQRLALARALLQPCQLLLLDEPTASLDAHSEQLV 524
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 2553857580 195 WSVVRRMLADTpmTCVFSTAYLEEAEAADRVLLFESGRII 234
Cdd:PRK11174 525 MQALNAASRRQ--TTLMVTHQLEDLAQWDQIWVMQDGQIV 562
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
9-99 |
5.44e-08 |
|
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: 52.07 E-value: 5.44e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857580 9 IRLEGVVKTFPNpldaaRPIraVDGISLKAggaEASDRlIALVGPDGAGKSTFMRLLCGLEAPDEGRLSVlgttpdpdne 88
Cdd:cd03221 1 IELENLSKTYGG-----KLL--LKDISLTI---NPGDR-IGLVGRNGAGKSTLLKLIAGELEPDEGIVTW---------- 59
|
90
....*....|.
gi 2553857580 89 DFTTRIAFMPQ 99
Cdd:cd03221 60 GSTVKIGYFEQ 70
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
367-560 |
6.75e-08 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 53.94 E-value: 6.75e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857580 367 IRADGIARKFGNFVAVADTSFEVRRGEIFGLLGPNGAGKTTTFRMLCGLLVPSKGQIEVAGydlrTAKAGARARIGYVAQ 446
Cdd:PRK11248 2 LQISHLYADYGGKPALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDG----KPVEGPGAERGVVFQ 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857580 447 KFSLYGKLSVEQNLRYFGRSYGFFGQALQDRIDASLEDFGLTDRRDTTAGSLSFGAKQDLSMACGLIHSPEILFLDEATS 526
Cdd:PRK11248 78 NEGLLPWRNVQDNVAFGLQLAGVEKMQRLEIAHQMLKKVGLEGAEKRYIWQLSGGQRQRVGIARALAANPQLLLLDEPFG 157
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 2553857580 527 GADLASRRAF-------WRRinalasAGTSVVVTTHFLEEA 560
Cdd:PRK11248 158 ALDAFTREQMqtlllklWQE------TGKQVLLITHDIEEA 192
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
392-569 |
7.91e-08 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 55.56 E-value: 7.91e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857580 392 GEIFGLLGPNGAGKTTTFRMLCGLLVPSKGQIEVAgydlrtakagARARIGYVA--------------QKFSLYGKLSVE 457
Cdd:PRK10636 338 GSRIGLLGRNGAGKSTLIKLLAGELAPVSGEIGLA----------KGIKLGYFAqhqleflradesplQHLARLAPQELE 407
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857580 458 QNLRYFGRSYGFFGqalqDRIDASLEDFgltdrrdttagslSFGAKQDLSMACGLIHSPEILFLDEATSGADLASRRAFw 537
Cdd:PRK10636 408 QKLRDYLGGFGFQG----DKVTEETRRF-------------SGGEKARLVLALIVWQRPNLLLLDEPTNHLDLDMRQAL- 469
|
170 180 190
....*....|....*....|....*....|..
gi 2553857580 538 rrINALASAGTSVVVTTHfleeaeycDRFLIQ 569
Cdd:PRK10636 470 --TEALIDFEGALVVVSH--------DRHLLR 491
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
389-578 |
7.94e-08 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 55.89 E-value: 7.94e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857580 389 VRRGEIFGLLGPNGAGKTTTFRMLCGLL---VPSKGQIEVAGYDLRTAKAgarARIGYVAQKFSLYGKLSVEQNLRY--F 463
Cdd:TIGR00956 786 VKPGTLTALMGASGAGKTTLLNVLAERVttgVITGGDRLVNGRPLDSSFQ---RSIGYVQQQDLHLPTSTVRESLRFsaY 862
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857580 464 GRSYGFFGQALQDR-IDASLEDFGLTDRRDTTAG----SLSFGAKQDLSMACGLIHSPE-ILFLDEATSGADLASRRAFW 537
Cdd:TIGR00956 863 LRQPKSVSKSEKMEyVEEVIKLLEMESYADAVVGvpgeGLNVEQRKRLTIGVELVAKPKlLLFLDEPTSGLDSQTAWSIC 942
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 2553857580 538 RRINALASAGTSVVVTTH-----FLEEAeycDRFL-IQDAGKVLALG 578
Cdd:TIGR00956 943 KLMRKLADHGQAILCTIHqpsaiLFEEF---DRLLlLQKGGQTVYFG 986
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
390-555 |
1.03e-07 |
|
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: 54.79 E-value: 1.03e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857580 390 RRGEIFGLLGPNGAGKTTTFRMLCGLLVPSKGQIEV-AGYDlrtakagararigYVAQKFS----------LY-GKLSVE 457
Cdd:COG1245 97 KKGKVTGILGPNGIGKSTALKILSGELKPNLGDYDEePSWD-------------EVLKRFRgtelqdyfkkLAnGEIKVA 163
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857580 458 ---QNLRYFGRSY-GFFGQALQ-----DRIDASLEDFGLTDRRDTTAGSLSFGAKQDLSMACGLIHSPEILFLDEATSGA 528
Cdd:COG1245 164 hkpQYVDLIPKVFkGTVRELLEkvderGKLDELAEKLGLENILDRDISELSGGELQRVAIAAALLRDADFYFFDEPSSYL 243
|
170 180
....*....|....*....|....*..
gi 2553857580 529 DLASRRAFWRRINALASAGTSVVVTTH 555
Cdd:COG1245 244 DIYQRLNVARLIRELAEEGKYVLVVEH 270
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
9-169 |
1.13e-07 |
|
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: 53.90 E-value: 1.13e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857580 9 IRLEGVVKTFPNPldaARPIRAVDGISL--KAGgaEAsdrlIALVGPDGAGKSTFMRLLCGLEAP---DEGRLSVLGTT- 82
Cdd:COG0444 2 LEVRNLKVYFPTR---RGVVKAVDGVSFdvRRG--ET----LGLVGESGSGKSTLARAILGLLPPpgiTSGEILFDGEDl 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857580 83 ---PDPDNEDF-TTRIAFMPQ----------TLGlyKTLscRENLEVFAGLRGfegeadgaAGLERRIAELLSMTGLAGF 148
Cdd:COG0444 73 lklSEKELRKIrGREIQMIFQdpmtslnpvmTVG--DQI--AEPLRIHGGLSK--------AEARERAIELLERVGLPDP 140
|
170 180
....*....|....*....|....*
gi 2553857580 149 EERqAGK----LSGGMKQKLALASA 169
Cdd:COG0444 141 ERR-LDRypheLSGGMRQRVMIARA 164
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
32-201 |
1.15e-07 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 54.81 E-value: 1.15e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857580 32 DGISLKAGGAEAS-DRLIALVGPDGAGKSTFMRLLCGLEAPDEGRLsvlgttpdpdneDFTTRIAFMPQtlglYktLSCR 110
Cdd:PRK13409 351 GDFSLEVEGGEIYeGEVIGIVGPNGIGKTTFAKLLAGVLKPDEGEV------------DPELKISYKPQ----Y--IKPD 412
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857580 111 ENLEVFAGLRGfEGEADGAAGLERRIAELLSMTGLAgfeERQAGKLSGGMKQKLALASALLRIPDLLLLDEPTVGVDPLS 190
Cdd:PRK13409 413 YDGTVEDLLRS-ITDDLGSSYYKSEIIKPLQLERLL---DKNVKDLSGGELQRVAIAACLSRDADLYLLDEPSAHLDVEQ 488
|
170
....*....|.
gi 2553857580 191 RRELWSVVRRM 201
Cdd:PRK13409 489 RLAVAKAIRRI 499
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
386-619 |
1.47e-07 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 54.78 E-value: 1.47e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857580 386 SFEVRRGEIFGLLGPNGAGKTT---TF-RML--CGllvpskGQIEVAG-----YDLRTAkagaRARIGYVAQKFSLYGKl 454
Cdd:PTZ00243 1330 SFRIAPREKVGIVGRTGSGKSTlllTFmRMVevCG------GEIRVNGreigaYGLREL----RRQFSMIPQDPVLFDG- 1398
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857580 455 SVEQNLRYFGrsygffgQALQDRIDASLEDFGLTDR----------RDTTAGS-LSFGAKQDLSMACGLIH--SPEILfL 521
Cdd:PTZ00243 1399 TVRQNVDPFL-------EASSAEVWAALELVGLRERvasesegidsRVLEGGSnYSVGQRQLMCMARALLKkgSGFIL-M 1470
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857580 522 DEATSGADLASRRAFWRRINALASAGTsVVVTTHFLEEAEYCDRFLIQDAGKVLALGTPREvkqraavlsavsgqsLVVD 601
Cdd:PTZ00243 1471 DEATANIDPALDRQIQATVMSAFSAYT-VITIAHRLHTVAQYDKIIVMDHGAVAEMGSPRE---------------LVMN 1534
|
250
....*....|....*...
gi 2553857580 602 RMSIedaFVAIVEAGRRS 619
Cdd:PTZ00243 1535 RQSI---FHSMVEALGRS 1549
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
27-239 |
1.53e-07 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 53.70 E-value: 1.53e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857580 27 PIRAVDGISLKAggaeASDRLIALVGPDGAGKSTFMRLLCGLEAPDEGRLSVLGTTPDPDNEDFTTRIAFMPQTLGLYKT 106
Cdd:PRK13631 38 ELVALNNISYTF----EKNKIYFIIGNSGSGKSTLVTHFNGLIKSKYGTIQVGDIYIGDKKNNHELITNPYSKKIKNFKE 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857580 107 LscRENLEV---FAGLRGFEG--EAD---GAAGL-------ERRIAELLSMTGL-AGFEERQAGKLSGGMKQKLALASAL 170
Cdd:PRK13631 114 L--RRRVSMvfqFPEYQLFKDtiEKDimfGPVALgvkkseaKKLAKFYLNKMGLdDSYLERSPFGLSGGQKRRVAIAGIL 191
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857580 171 LRIPDLLLLDEPTVGVDPLSRRELWSVVRRMLADTpMTCVFSTAYLEEA-EAADRVLLFESGRIIADENP 239
Cdd:PRK13631 192 AIQPEILIFDEPTAGLDPKGEHEMMQLILDAKANN-KTVFVITHTMEHVlEVADEVIVMDKGKILKTGTP 260
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
55-246 |
1.88e-07 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 54.15 E-value: 1.88e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857580 55 GAGKSTFMRLLCGLEAPDEGRLSVLGTTPDPDNEDFTTR--IAFMPQ---TLGLYKTLSCRENLEV--------FAGLRG 121
Cdd:PRK11288 289 GAGRSELMKLLYGATRRTAGQVYLDGKPIDIRSPRDAIRagIMLCPEdrkAEGIIPVHSVADNINIsarrhhlrAGCLIN 368
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857580 122 FEGEADGAaglERRIAELLSMTGLAgfeERQAGKLSGGMKQKLALASALLRIPDLLLLDEPTVGVDPLSRRELWSVVRRm 201
Cdd:PRK11288 369 NRWEAENA---DRFIRSLNIKTPSR---EQLIMNLSGGNQQKAILGRWLSEDMKVILLDEPTRGIDVGAKHEIYNVIYE- 441
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 2553857580 202 LADTPMTCVFSTAYLEEAEA-ADRVLLFESGRII-----ADENPQSFISRA 246
Cdd:PRK11288 442 LAAQGVAVLFVSSDLPEVLGvADRIVVMREGRIAgelarEQATERQALSLA 492
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
130-533 |
2.15e-07 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 54.09 E-value: 2.15e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857580 130 AGLERRIAELLSMTGLAGFEERQA------GKLSGGMKQKLALASALLRIPDLLLLDEPTVGVDPLSRRELWSVVRRMLA 203
Cdd:PRK10261 137 ASREEAMVEAKRMLDQVRIPEAQTilsrypHQLSGGMRQRVMIAMALSCRPAVLIADEPTTALDVTIQAQILQLIKVLQK 216
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857580 204 DTPMTCVFSTAYLE-EAEAADRVLLFESGRIIADENPQSfISRAKGRTYllplanraehdaqmlcrrlseetaaTRSdal 282
Cdd:PRK10261 217 EMSMGVIFITHDMGvVAEIADRVLVMYQGEAVETGSVEQ-IFHAPQHPY-------------------------TRA--- 267
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857580 283 FLDIVPRMGGAAATTLAPTLPVkdarvpsgfiprqPSLEDAYalltfPRAPKTANHLASPPSDASGAlaasaasaddtae 362
Cdd:PRK10261 268 LLAAVPQLGAMKGLDYPRRFPL-------------ISLEHPA-----KQEPPIEQDTVVDGEPILQV------------- 316
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857580 363 RPVVIR---ADGIARKFGNFV-AVADTSFEVRRGEIFGLLGPNGAGKTTTFRMLCGLLVPSKGQIEVAGYDLRTAKAGA- 437
Cdd:PRK10261 317 RNLVTRfplRSGLLNRVTREVhAVEKVSFDLWPGETLSLVGESGSGKSTTGRALLRLVESQGGEIIFNGQRIDTLSPGKl 396
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857580 438 ---RARIGYVAQK--FSLYGKLSVEQNLRYFGRSYGFF-GQALQDRIDASLEDFGLTDRRD-TTAGSLSFGAKQDLSMAC 510
Cdd:PRK10261 397 qalRRDIQFIFQDpyASLDPRQTVGDSIMEPLRVHGLLpGKAAAARVAWLLERVGLLPEHAwRYPHEFSGGQRQRICIAR 476
|
410 420
....*....|....*....|...
gi 2553857580 511 GLIHSPEILFLDEATSGADLASR 533
Cdd:PRK10261 477 ALALNPKVIIADEAVSALDVSIR 499
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
43-226 |
3.20e-07 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 51.33 E-value: 3.20e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857580 43 ASDRLIALVGPDGAGKSTFMRLLCGLEAPD---EGRLSVlgttpdpDNEDFTT------RIAFMPQTLGLYKTLSCRENL 113
Cdd:COG4136 25 APGEILTLMGPSGSGKSTLLAAIAGTLSPAfsaSGEVLL-------NGRRLTAlpaeqrRIGILFQDDLLFPHLSVGENL 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857580 114 eVFAGLRGFEGEADgaaglERRIAELLSMTGLAGFEERQAGKLSGGMKQKLALASALLRIPDLLLLDEPTVGVDPLSRRE 193
Cdd:COG4136 98 -AFALPPTIGRAQR-----RARVEQALEEAGLAGFADRDPATLSGGQRARVALLRALLAEPRALLLDEPFSKLDAALRAQ 171
|
170 180 190
....*....|....*....|....*....|...
gi 2553857580 194 LWSVVRRMLADTPMTCVFSTAYLEEAEAADRVL 226
Cdd:COG4136 172 FREFVFEQIRQRGIPALLVTHDEEDAPAAGRVL 204
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
4-183 |
3.44e-07 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 52.43 E-value: 3.44e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857580 4 ASAPAIRLEGVVKTFP---NPLDAARP-IRAVDGISL--KAGgaeasdRLIALVGPDGAGKSTFMRLLCGLEAPDEGRLS 77
Cdd:COG4608 3 MAEPLLEVRDLKKHFPvrgGLFGRTVGvVKAVDGVSFdiRRG------ETLGLVGESGCGKSTLGRLLLRLEEPTSGEIL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857580 78 VlgttpdpDNEDFTT--RIAFMPQTLGL-------YKTLSCR--------ENLEVFaglrgfeGEADGAAgLERRIAELL 140
Cdd:COG4608 77 F-------DGQDITGlsGRELRPLRRRMqmvfqdpYASLNPRmtvgdiiaEPLRIH-------GLASKAE-RRERVAELL 141
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 2553857580 141 SMTGL-AGFEERQAGKLSGGMKQKLALASALLRIPDLLLLDEPT 183
Cdd:COG4608 142 ELVGLrPEHADRYPHEFSGGQRQRIGIARALALNPKLIVCDEPV 185
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
389-557 |
3.64e-07 |
|
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: 51.98 E-value: 3.64e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857580 389 VRRGEIFGLLGPNGAGKTTTFRMLCGLLVPSKGQIEVAGY--DLRTAKAGARARIgYVAQkfSLYGKLSVEQNLRYFGR- 465
Cdd:cd03236 23 PREGQVLGLVGPNGIGKSTALKILAGKLKPNLGKFDDPPDwdEILDEFRGSELQN-YFTK--LLEGDVKVIVKPQYVDLi 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857580 466 SYGFFGQALQ--------DRIDASLEDFGLTDRRDTTAGSLSFGAKQDLSMACGLIHSPEILFLDEATSGADLASRRAFW 537
Cdd:cd03236 100 PKAVKGKVGEllkkkderGKLDELVDQLELRHVLDRNIDQLSGGELQRVAIAAALARDADFYFFDEPSSYLDIKQRLNAA 179
|
170 180
....*....|....*....|
gi 2553857580 538 RRINALASAGTSVVVTTHFL 557
Cdd:cd03236 180 RLIRELAEDDNYVLVVEHDL 199
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
49-234 |
3.65e-07 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 51.77 E-value: 3.65e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857580 49 ALVGPDGAGKSTFMRLLCGL-----EAPDEGRLSVLGT---TPDPDNEDFTTRIAFMPQTLGLYKTLSCRENLEVfaGLR 120
Cdd:PRK14267 34 ALMGPSGCGKSTLLRTFNRLlelneEARVEGEVRLFGRniySPDVDPIEVRREVGMVFQYPNPFPHLTIYDNVAI--GVK 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857580 121 gFEGEADGAAGLERRIAELLSMTGLagFEERQ------AGKLSGGMKQKLALASALLRIPDLLLLDEPTVGVDPLSRREL 194
Cdd:PRK14267 112 -LNGLVKSKKELDERVEWALKKAAL--WDEVKdrlndyPSNLSGGQRQRLVIARALAMKPKILLMDEPTANIDPVGTAKI 188
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 2553857580 195 WSVVRRMLADTPMTCVfSTAYLEEAEAADRVLLFESGRII 234
Cdd:PRK14267 189 EELLFELKKEYTIVLV-THSPAQAARVSDYVAFLYLGKLI 227
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
390-555 |
3.99e-07 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 53.31 E-value: 3.99e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857580 390 RRGEIFGLLGPNGAGKTTTFRMLCGLLVPS--KGQIEVAGYdlrTAKAGARARI-GYVAQKFSLYGKLSVEQNLRY--FG 464
Cdd:PLN03140 904 RPGVLTALMGVSGAGKTTLMDVLAGRKTGGyiEGDIRISGF---PKKQETFARIsGYCEQNDIHSPQVTVRESLIYsaFL 980
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857580 465 RSYGFFGQALQDR-IDASLEDFGLTDRRDTTAG-----SLSFGAKQDLSMACGLIHSPEILFLDEATSGADLASRRAFWR 538
Cdd:PLN03140 981 RLPKEVSKEEKMMfVDEVMELVELDNLKDAIVGlpgvtGLSTEQRKRLTIAVELVANPSIIFMDEPTSGLDARAAAIVMR 1060
|
170
....*....|....*..
gi 2553857580 539 RINALASAGTSVVVTTH 555
Cdd:PLN03140 1061 TVRNTVDTGRTVVCTIH 1077
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
373-594 |
4.25e-07 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 51.58 E-value: 4.25e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857580 373 ARKFGNFVAVADT-------SFEVRRGEIFGLLGPNGAGKTTTFRMLCGL-----LVPSKGQIEVAG---YDLRTAKAGA 437
Cdd:PRK14258 7 AIKVNNLSFYYDTqkilegvSMEIYQSKVTAIIGPSGCGKSTFLKCLNRMnelesEVRVEGRVEFFNqniYERRVNLNRL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857580 438 RARIGYVAQKFSLYgKLSVEQNLRYFGRSYGFFGQA-LQDRIDASLEDFGLTD----RRDTTAGSLSFGAKQDLSMACGL 512
Cdd:PRK14258 87 RRQVSMVHPKPNLF-PMSVYDNVAYGVKIVGWRPKLeIDDIVESALKDADLWDeikhKIHKSALDLSGGQQQRLCIARAL 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857580 513 IHSPEILFLDEATSGADLASRRAFWRRINALA-SAGTSVVVTTHFLEEAEYCDRFLI------QDAGKVLALGT------ 579
Cdd:PRK14258 166 AVKPKVLLMDEPCFGLDPIASMKVESLIQSLRlRSELTMVIVSHNLHQVSRLSDFTAffkgneNRIGQLVEFGLtkkifn 245
|
250
....*....|....*.
gi 2553857580 580 -PREVKQRAAVLSAVS 594
Cdd:PRK14258 246 sPHDSRTREYVLSRLG 261
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
376-584 |
7.12e-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: 51.40 E-value: 7.12e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857580 376 FGNFVAVA-----DTSFEVRRGEIFGLLGPNGAGKTTTFRMLCGLLVPSKGQIEVAGydlrtakagaraRIGYVAQkFSL 450
Cdd:cd03291 42 FSNLCLVGapvlkNINLKIEKGEMLAITGSTGSGKTSLLMLILGELEPSEGKIKHSG------------RISFSSQ-FSW 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857580 451 YGKLSVEQNLrYFGRSYGFFG-----QALQDRIDASledfGLTDRRDTTAG----SLSFGAKQDLSMACGLIHSPEILFL 521
Cdd:cd03291 109 IMPGTIKENI-IFGVSYDEYRyksvvKACQLEEDIT----KFPEKDNTVLGeggiTLSGGQRARISLARAVYKDADLYLL 183
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2553857580 522 DEATSGADLAS-RRAFWRRINALASAGTSVVVTTHfLEEAEYCDRFLIQDAGKVLALGTPREVK 584
Cdd:cd03291 184 DSPFGYLDVFTeKEIFESCVCKLMANKTRILVTSK-MEHLKKADKILILHEGSSYFYGTFSELQ 246
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
30-239 |
8.28e-07 |
|
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: 50.18 E-value: 8.28e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857580 30 AVDGISLKAGGAEAsdrlIALVGPDGAGKSTFMRLLCGLEAPDEGRLSVlgttpdpDNEDFTT--------RIAFMPQ-- 99
Cdd:cd03244 19 VLKNISFSIKPGEK----VGIVGRTGSGKSSLLLALFRLVELSSGSILI-------DGVDISKiglhdlrsRISIIPQdp 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857580 100 -----TLglyktlscRENLEVFaglrgfeGEADgaaglERRIAELLSMTGLAGFEERQAGKL-----------SGGMKQK 163
Cdd:cd03244 88 vlfsgTI--------RSNLDPF-------GEYS-----DEELWQALERVGLKEFVESLPGGLdtvveeggenlSVGQRQL 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2553857580 164 LALASALLRIPDLLLLDEPTVGVDPLSRRELWSVVRRMLADTpmTcVFSTAY-LEEAEAADRVLLFESGRIIADENP 239
Cdd:cd03244 148 LCLARALLRKSKILVLDEATASVDPETDALIQKTIREAFKDC--T-VLTIAHrLDTIIDSDRILVLDKGRVVEFDSP 221
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
384-590 |
9.41e-07 |
|
multi drug resistance-associated protein (MRP); This model describes multi drug resistance-associated protein (MRP) in eukaryotes. The multidrug resistance-associated protein is an integral membrane protein that causes multidrug resistance when overexpressed in mammalian cells. It belongs to ABC transporter superfamily. The protein topology and function was experimentally demonstrated by epitope tagging and immunofluorescence. Insertion of tags in the critical regions associated with drug efflux, abrogated its function. The C-terminal domain seem to highly conserved. [Transport and binding proteins, Other]
Pssm-ID: 188098 [Multi-domain] Cd Length: 1522 Bit Score: 52.26 E-value: 9.41e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857580 384 DTSFEVRRGEIFGLLGPNGAGKTTTFRMLCGLLVPSKGQIEVAGydLRTAKAGA---RARIGYVAQKFSLYGKlSVEQNL 460
Cdd:TIGR00957 1304 HINVTIHGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDG--LNIAKIGLhdlRFKITIIPQDPVLFSG-SLRMNL 1380
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857580 461 RYFGrSYG--------------FFGQALQDRIDASLEDFGltdrrdttaGSLSFGAKQDLSMACGLIHSPEILFLDEATS 526
Cdd:TIGR00957 1381 DPFS-QYSdeevwwalelahlkTFVSALPDKLDHECAEGG---------ENLSVGQRQLVCLARALLRKTKILVLDEATA 1450
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2553857580 527 GADLASRRAFWRRINALASAGTsVVVTTHFLEEAEYCDRFLIQDAGKVLALGTPREVKQRAAVL 590
Cdd:TIGR00957 1451 AVDLETDNLIQSTIRTQFEDCT-VLTIAHRLNTIMDYTRVIVLDKGEVAEFGAPSNLLQQRGIF 1513
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
7-78 |
1.07e-06 |
|
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: 50.13 E-value: 1.07e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2553857580 7 PAIRLEGVVKTFPNPLDAARPIRAVDGISLKAGGAEasdrLIALVGPDGAGKSTFMRLLCGLEAPDEGRLSV 78
Cdd:COG4778 3 TLLEVENLSKTFTLHLQGGKRLPVLDGVSFSVAAGE----CVALTGPSGAGKSTLLKCIYGNYLPDSGSILV 70
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
388-452 |
1.16e-06 |
|
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: 49.11 E-value: 1.16e-06
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2553857580 388 EVRRGEIFGLLGPNGAGKTTTFRMLCGLLVPSKGQIEVagydlrtakagARARIGYVAQKFSLYG 452
Cdd:cd03222 21 VVKEGEVIGIVGPNGTGKTTAVKILAGQLIPNGDNDEW-----------DGITPVYKPQYIDLSG 74
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
49-247 |
1.20e-06 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 50.55 E-value: 1.20e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857580 49 ALVGPDGAGKSTFMRLLCGLEAPDEGRLSVLGTTPDPDNEDFTTR-------IAFMPQTLGLYKTLSCREnleVFAGLRG 121
Cdd:PRK13646 37 AIVGQTGSGKSTLIQNINALLKPTTGTVTVDDITITHKTKDKYIRpvrkrigMVFQFPESQLFEDTVERE---IIFGPKN 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857580 122 FEGEADGAAglERRIAELLSMtglaGFE----ERQAGKLSGGMKQKLALASALLRIPDLLLLDEPTVGVDPLSRRELWSV 197
Cdd:PRK13646 114 FKMNLDEVK--NYAHRLLMDL----GFSrdvmSQSPFQMSGGQMRKIAIVSILAMNPDIIVLDEPTAGLDPQSKRQVMRL 187
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 2553857580 198 VRRMLADTPMTCVFSTAYLEE-AEAADRVLLFESGRIIADENPQSFISRAK 247
Cdd:PRK13646 188 LKSLQTDENKTIILVSHDMNEvARYADEVIVMKEGSIVSQTSPKELFKDKK 238
|
|
| 3a01203 |
TIGR00954 |
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ... |
380-526 |
1.34e-06 |
|
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 273360 [Multi-domain] Cd Length: 659 Bit Score: 51.29 E-value: 1.34e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857580 380 VAVADTSFEVRRGEIFGLLGPNGAGKTTTFRMLCGLLvPSKGqievagyDLRTAKagARARIGYVAQK--FSLyGKLSvE 457
Cdd:TIGR00954 466 VLIESLSFEVPSGNNLLICGPNGCGKSSLFRILGELW-PVYG-------GRLTKP--AKGKLFYVPQRpyMTL-GTLR-D 533
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2553857580 458 QNLrYFGRSYGFFGQALQDR-IDASLEDFGLTDRRDTTAG---------SLSFGAKQDLSMACGLIHSPEILFLDEATS 526
Cdd:TIGR00954 534 QII-YPDSSEDMKRRGLSDKdLEQILDNVQLTHILEREGGwsavqdwmdVLSGGEKQRIAMARLFYHKPQFAILDECTS 611
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
44-200 |
1.43e-06 |
|
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: 49.58 E-value: 1.43e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857580 44 SDRLIALVGPDGAGKSTFMRLLCGLEAPDE---GRLSVLGTTPDPDNedFTTRIAFMPQTLGLYKTLSCRENLEVFAGLR 120
Cdd:cd03234 32 SGQVMAILGSSGSGKTTLLDAISGRVEGGGttsGQILFNGQPRKPDQ--FQKCVAYVRQDDILLPGLTVRETLTYTAILR 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857580 121 GFEGEADGAaglERRIAELLSMTGLAgfEERQAGK----LSGGMKQKLALASALLRIPDLLLLDEPTVGVDPLSRRELWS 196
Cdd:cd03234 110 LPRKSSDAI---RKKRVEDVLLRDLA--LTRIGGNlvkgISGGERRRVSIAVQLLWDPKVLILDEPTSGLDSFTALNLVS 184
|
....
gi 2553857580 197 VVRR 200
Cdd:cd03234 185 TLSQ 188
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
394-583 |
1.50e-06 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 50.09 E-value: 1.50e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857580 394 IFGLLGPNGAGKTTTFRMLcgllvpSKGQIEVAGYDLR-TAKAGARA------------RIGYVAQKFSLYgKLSVEQNL 460
Cdd:PRK14271 49 VTSLMGPTGSGKTTFLRTL------NRMNDKVSGYRYSgDVLLGGRSifnyrdvlefrrRVGMLFQRPNPF-PMSIMDNV 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857580 461 RYFGRSYGFFG-QALQDRIDASLEDFGL----TDRRDTTAGSLSFGAKQDLSMACGLIHSPEILFLDEATSGADLASRRA 535
Cdd:PRK14271 122 LAGVRAHKLVPrKEFRGVAQARLTEVGLwdavKDRLSDSPFRLSGGQQQLLCLARTLAVNPEVLLLDEPTSALDPTTTEK 201
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 2553857580 536 FWRRINALASAGTSVVVTTHFLEEAEYCDRFLIQDAGKVLALGTPREV 583
Cdd:PRK14271 202 IEEFIRSLADRLTVIIVTHNLAQAARISDRAALFFDGRLVEEGPTEQL 249
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
389-585 |
1.63e-06 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 51.65 E-value: 1.63e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857580 389 VRRGEIFGLLGPNGAGKTTTFRMLCGLLVPSK----GQIEVAGYDLRTAKAGARARIGYVAQKFSLYGKLSVEQNLRYFG 464
Cdd:TIGR00956 84 IKPGELTVVLGRPGSGCSTLLKTIASNTDGFHigveGVITYDGITPEEIKKHYRGDVVYNAETDVHFPHLTVGETLDFAA 163
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857580 465 RSygffgQALQDRID--------ASLED-----FGLTDRRDTTAGS-----LSFGAKQDLSMACGLIHSPEILFLDEATS 526
Cdd:TIGR00956 164 RC-----KTPQNRPDgvsreeyaKHIADvymatYGLSHTRNTKVGNdfvrgVSGGERKRVSIAEASLGGAKIQCWDNATR 238
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2553857580 527 GADLASRRAFWRRINALAS-AGTSVVVTTHFLEEAEY--CDRFLIQDAGKVLALGTPREVKQ 585
Cdd:TIGR00956 239 GLDSATALEFIRALKTSANiLDTTPLVAIYQCSQDAYelFDKVIVLYEGYQIYFGPADKAKQ 300
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
24-187 |
1.67e-06 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 50.35 E-value: 1.67e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857580 24 AARPIRAVDGIS--LKAGgaeasdRLIALVGPDGAGKSTFMRLLCGLEAPDEGRLSVLG---TTPDPDNEDFTTR---IA 95
Cdd:PRK11308 24 PERLVKALDGVSftLERG------KTLAVVGESGCGKSTLARLLTMIETPTGGELYYQGqdlLKADPEAQKLLRQkiqIV 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857580 96 FM-PqtlglYKTLSCR--------ENLEVFAGLrgfegeadGAAGLERRIAELLSMTGL-AGFEERQAGKLSGGMKQKLA 165
Cdd:PRK11308 98 FQnP-----YGSLNPRkkvgqileEPLLINTSL--------SAAERREKALAMMAKVGLrPEHYDRYPHMFSGGQRQRIA 164
|
170 180
....*....|....*....|..
gi 2553857580 166 LASALLRIPDLLLLDEPTVGVD 187
Cdd:PRK11308 165 IARALMLDPDVVVADEPVSALD 186
|
|
| PvdE |
COG4615 |
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ... |
386-586 |
1.70e-06 |
|
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: 50.95 E-value: 1.70e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857580 386 SFEVRRGEIFGLLGPNGAGKTTTFRMLCGLLVPSKGQIEVAGydlrtaKAGARARIGYVAQKFSlygklSVEQNLRYFGR 465
Cdd:COG4615 352 DLTIRRGELVFIVGGNGSGKSTLAKLLTGLYRPESGEILLDG------QPVTADNREAYRQLFS-----AVFSDFHLFDR 420
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857580 466 SYGFFGQALQDRIDASLEDFGLTD-------RRDTTAgsLSFGAKQDLSMACGLIHSPEILFLDEATSGADLASRRAFWR 538
Cdd:COG4615 421 LLGLDGEADPARARELLERLELDHkvsvedgRFSTTD--LSQGQRKRLALLVALLEDRPILVFDEWAADQDPEFRRVFYT 498
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 2553857580 539 RI-NALASAGTSVVVTTH---FLEEAeycDRFLIQDAGKVLALGTPREVKQR 586
Cdd:COG4615 499 ELlPELKARGKTVIAISHddrYFDLA---DRVLKMDYGKLVELTGPAALAAS 547
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
381-529 |
2.01e-06 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 50.87 E-value: 2.01e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857580 381 AVADTSFEVRRGEIFGLLGPNGAGKTTTFRMLCGLLVPSKGQIEVAGYDLRTAKAGA-RARIGYVAQKFSLYGKlSVEQN 459
Cdd:PRK10789 330 ALENVNFTLKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGDIRFHDIPLTKLQLDSwRSRLAVVSQTPFLFSD-TVANN 408
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857580 460 LRyFGRSygffgQALQDRID-----ASLED--FGLTDRRDTTAGS----LSFGAKQDLSMACGLIHSPEILFLDEATSGA 528
Cdd:PRK10789 409 IA-LGRP-----DATQQEIEhvarlASVHDdiLRLPQGYDTEVGErgvmLSGGQKQRISIARALLLNAEILILDDALSAV 482
|
.
gi 2553857580 529 D 529
Cdd:PRK10789 483 D 483
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
384-574 |
2.91e-06 |
|
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: 50.68 E-value: 2.91e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857580 384 DTSFEVRRGEIFGLLGPNGAGKTTTFRMLCGLLvPSKGQIEVAG--YDLRTAKAGARArIGYVAQK-FSLYGKLSV---- 456
Cdd:TIGR01271 1237 DLSFSVEGGQRVGLLGRTGSGKSTLLSALLRLL-STEGEIQIDGvsWNSVTLQTWRKA-FGVIPQKvFIFSGTFRKnldp 1314
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857580 457 -----EQNLRYFGRSYGFFGQALQ--DRIDASLEDFGLTdrrdttagsLSFGAKQDLSMACGLIHSPEILFLDEATSGAD 529
Cdd:TIGR01271 1315 yeqwsDEEIWKVAEEVGLKSVIEQfpDKLDFVLVDGGYV---------LSNGHKQLMCLARSILSKAKILLLDEPSAHLD 1385
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 2553857580 530 LASRRAFwRRINALASAGTSVVVTTHFLEEAEYCDRFLIQDAGKV 574
Cdd:TIGR01271 1386 PVTLQII-RKTLKQSFSNCTVILSEHRVEALLECQQFLVIEGSSV 1429
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
397-579 |
2.96e-06 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 50.10 E-value: 2.96e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857580 397 LLGPNGAGKTTTFRMLCGLLVPSKGQIEVAGYDLRTAKAGA-RARIGYVAQKFSLYGKlSVEQNLRyFGRSYGffgqalQ 475
Cdd:PRK10790 372 LVGHTGSGKSTLASLLMGYYPLTEGEIRLDGRPLSSLSHSVlRQGVAMVQQDPVVLAD-TFLANVT-LGRDIS------E 443
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857580 476 DRIDASLEDFGLTD-RRDTTAG----------SLSFGAKQDLSMACGLIHSPEILFLDEATSGADLASRRAFWRRINALA 544
Cdd:PRK10790 444 EQVWQALETVQLAElARSLPDGlytplgeqgnNLSVGQKQLLALARVLVQTPQILILDEATANIDSGTEQAIQQALAAVR 523
|
170 180 190
....*....|....*....|....*....|....*
gi 2553857580 545 SAgTSVVVTTHFLEEAEYCDRFLIQDAGKVLALGT 579
Cdd:PRK10790 524 EH-TTLVVIAHRLSTIVEADTILVLHRGQAVEQGT 557
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
369-446 |
4.94e-06 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 49.51 E-value: 4.94e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2553857580 369 ADGIARKFGNFVAVADTSFEVRRGEIFGLLGPNGAGKTTTFRMLCGLLVPSKGQIevagydlrtaKAGARARIGYVAQ 446
Cdd:PRK15064 322 VENLTKGFDNGPLFKNLNLLLEAGERLAIIGENGVGKTTLLRTLVGELEPDSGTV----------KWSENANIGYYAQ 389
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
30-190 |
5.02e-06 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 48.62 E-value: 5.02e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857580 30 AVDGISLKAggaeASDRLIALVGPDGAGKSTFMR-------LLCGLEApdEGRLSVLGTT---PDPDNEDFTTRIAFMPQ 99
Cdd:PRK14243 25 AVKNVWLDI----PKNQITAFIGPSGCGKSTILRcfnrlndLIPGFRV--EGKVTFHGKNlyaPDVDPVEVRRRIGMVFQ 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857580 100 TLGLYKTlSCRENLEVFAGLRGFEGEADG-------AAGLERRIAELLSMTGLAgfeerqagkLSGGMKQKLALASALLR 172
Cdd:PRK14243 99 KPNPFPK-SIYDNIAYGARINGYKGDMDElverslrQAALWDEVKDKLKQSGLS---------LSGGQQQRLCIARAIAV 168
|
170
....*....|....*...
gi 2553857580 173 IPDLLLLDEPTVGVDPLS 190
Cdd:PRK14243 169 QPEVILMDEPCSALDPIS 186
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
9-187 |
6.43e-06 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 47.56 E-value: 6.43e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857580 9 IRLEGVVKTFpnpLDAARPIRAVDgISLKAGgaeasdRLIALVGPDGAGKSTFMRLLCGLEAPDEGR-------LSVLGT 81
Cdd:PRK10908 2 IRFEHVSKAY---LGGRQALQGVT-FHMRPG------EMAFLTGHSGAGKSTLLKLICGIERPSAGKiwfsghdITRLKN 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857580 82 TPDPdnedFTTR-IAFMPQTLGLYKTLSCRENLEVFAGLRGFEGEadgaaGLERRIAELLSMTGLAGFEERQAGKLSGGM 160
Cdd:PRK10908 72 REVP----FLRRqIGMIFQDHHLLMDRTVYDNVAIPLIIAGASGD-----DIRRRVSAALDKVGLLDKAKNFPIQLSGGE 142
|
170 180
....*....|....*....|....*..
gi 2553857580 161 KQKLALASALLRIPDLLLLDEPTVGVD 187
Cdd:PRK10908 143 QQRVGIARAVVNKPAVLLADEPTGNLD 169
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
47-187 |
6.86e-06 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 47.89 E-value: 6.86e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857580 47 LIALVGPDGAGKSTFMRLLCGLEAPDEGR-------LSVLGTTPDPDNEDftTRIAFMPQTLGLYKTLSCRENLEVFAGL 119
Cdd:PRK11629 37 MMAIVGSSGSGKSTLLHLLGGLDTPTSGDvifngqpMSKLSSAAKAELRN--QKLGFIYQFHHLLPDFTALENVAMPLLI 114
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2553857580 120 RGFEgeadgAAGLERRIAELLSMTGLAGFEERQAGKLSGGMKQKLALASALLRIPDLLLLDEPTVGVD 187
Cdd:PRK11629 115 GKKK-----PAEINSRALEMLAAVGLEHRANHRPSELSGGERQRVAIARALVNNPRLVLADEPTGNLD 177
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
384-553 |
7.39e-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: 47.26 E-value: 7.39e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857580 384 DTSFEVRRGEIFGLLGPNGAGKTTTFRMLCGLLVPS---KGQIEVAGYDLRTAKAGARARIGYVAQKFSLYGKLSVEQNL 460
Cdd:cd03233 25 DFSGVVKPGEMVLVLGRPGSGCSTLLKALANRTEGNvsvEGDIHYNGIPYKEFAEKYPGEIIYVSEEDVHFPTLTVRETL 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857580 461 ryfgrsygffgqalqdridasleDFGLTDRRDTTAGSLSFGAKQDLSMACGLIHSPEILFLDEATSGADLASRRAFWRRI 540
Cdd:cd03233 105 -----------------------DFALRCKGNEFVRGISGGERKRVSIAEALVSRASVLCWDNSTRGLDSSTALEILKCI 161
|
170
....*....|....
gi 2553857580 541 NALASA-GTSVVVT 553
Cdd:cd03233 162 RTMADVlKTTTFVS 175
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
29-239 |
7.54e-06 |
|
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type transporter 1). NFT1 belongs to the MRP (multidrug resistance-associated protein) family of ABC transporters. Some of the MRP members have five additional transmembrane segments in their N-terminus, but the function of these additional membrane-spanning domains is not clear. The MRP was found in the multidrug-resisting lung cancer cell in which p-glycoprotein was not overexpressed. MRP exports glutathione by drug stimulation, as well as, certain substrates in conjugated forms with anions such as glutathione, glucuronate, and sulfate.
Pssm-ID: 213269 [Multi-domain] Cd Length: 207 Bit Score: 47.41 E-value: 7.54e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857580 29 RAVDGISLKAGGAEAsdrlIALVGPDGAGKSTFMRLLCGLEAPDEGRLSVLGT-TPDPDNEDFTTRIAFMPQTLGLYKTl 107
Cdd:cd03369 22 PVLKNVSFKVKAGEK----IGIVGRTGAGKSTLILALFRFLEAEEGKIEIDGIdISTIPLEDLRSSLTIIPQDPTLFSG- 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857580 108 SCRENLEVFaglrgfeGEADgaaglERRIAELLSMTGlagfeerQAGKLSGGMKQKLALASALLRIPDLLLLDEPTVGVD 187
Cdd:cd03369 97 TIRSNLDPF-------DEYS-----DEEIYGALRVSE-------GGLNLSQGQRQLLCLARALLKRPRVLVLDEATASID 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 2553857580 188 PLSRRELWSVVRRMLADTpmTCVFSTAYLEEAEAADRVLLFESGRIIADENP 239
Cdd:cd03369 158 YATDALIQKTIREEFTNS--TILTIAHRLRTIIDYDKILVMDAGEVKEYDHP 207
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
28-261 |
7.77e-06 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 49.34 E-value: 7.77e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857580 28 IRAVDGIsLKAGgaeasdRLIALVGPDGAGKSTFMRLLC----GLEAPDEGRLSVLGTTPDPDNEDFTTRIAFMPQTLGL 103
Cdd:TIGR00956 77 LKPMDGL-IKPG------ELTVVLGRPGSGCSTLLKTIAsntdGFHIGVEGVITYDGITPEEIKKHYRGDVVYNAETDVH 149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857580 104 YKTLSCRENLEVFAGLRGFEGEADGAAGLERR--IAELLSMT-GLAGFEERQAGK-----LSGGMKQKLALASALLRIPD 175
Cdd:TIGR00956 150 FPHLTVGETLDFAARCKTPQNRPDGVSREEYAkhIADVYMATyGLSHTRNTKVGNdfvrgVSGGERKRVSIAEASLGGAK 229
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857580 176 LLLLDEPTVGVDPLSRRELWSVVRRMLADTPMTcVFSTAYL--EEA-EAADRVLLFESGRII----ADENPQSFI----- 243
Cdd:TIGR00956 230 IQCWDNATRGLDSATALEFIRALKTSANILDTT-PLVAIYQcsQDAyELFDKVIVLYEGYQIyfgpADKAKQYFEkmgfk 308
|
250 260
....*....|....*....|
gi 2553857580 244 --SRAKGRTYLLPLANRAEH 261
Cdd:TIGR00956 309 cpDRQTTADFLTSLTSPAER 328
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
2-205 |
8.03e-06 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 49.04 E-value: 8.03e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857580 2 TKASAPAIRLEGVVKTFPNpldaARPIRAVDGISLKAGgaeasDRLIaLVGPDGAGKSTFMRLLCGLEAPDEGRLSVlgt 81
Cdd:COG4178 356 ETSEDGALALEDLTLRTPD----GRPLLEDLSLSLKPG-----ERLL-ITGPSGSGKSTLLRAIAGLWPYGSGRIAR--- 422
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857580 82 tpdPDNEdfttRIAFMPQT----LGlykTLscRENLevfagLRGFEGEADGAAglerRIAELLSMTGLAGF------EER 151
Cdd:COG4178 423 ---PAGA----RVLFLPQRpylpLG---TL--REAL-----LYPATAEAFSDA----ELREALEAVGLGHLaerldeEAD 481
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 2553857580 152 QAGKLSGGMKQKLALASALLRIPDLLLLDEPTVGVDPLSRRELWSVVRRMLADT 205
Cdd:COG4178 482 WDQVLSLGEQQRLAFARLLLHKPDWLFLDEATSALDEENEAALYQLLREELPGT 535
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
48-233 |
8.06e-06 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 48.95 E-value: 8.06e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857580 48 IALVGPDGAGKSTFMRLLCGLEAPDEGRLSVLGT-TPDPDNEDFTTRIAFMPQTLGLYKTlSCRENleVFAGLRGFEGE- 125
Cdd:TIGR00958 510 VALVGPSGSGKSTVAALLQNLYQPTGGQVLLDGVpLVQYDHHYLHRQVALVGQEPVLFSG-SVREN--IAYGLTDTPDEe 586
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857580 126 ---ADGAAGLERRIAELlsMTGLAGFEERQAGKLSGGMKQKLALASALLRIPDLLLLDEPTVGVDPLSRRELWSvvRRML 202
Cdd:TIGR00958 587 imaAAKAANAHDFIMEF--PNGYDTEVGEKGSQLSGGQKQRIAIARALVRKPRVLILDEATSALDAECEQLLQE--SRSR 662
|
170 180 190
....*....|....*....|....*....|.
gi 2553857580 203 ADtpMTCVFSTAYLEEAEAADRVLLFESGRI 233
Cdd:TIGR00958 663 AS--RTVLLIAHRLSTVERADQILVLKKGSV 691
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
389-424 |
8.58e-06 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 48.65 E-value: 8.58e-06
10 20 30
....*....|....*....|....*....|....*.
gi 2553857580 389 VRRGEIFGLLGPNGAGKTTTFRMLCGLLVPSKGQIE 424
Cdd:PRK13409 96 PKEGKVTGILGPNGIGKTTAVKILSGELIPNLGDYE 131
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
49-235 |
8.76e-06 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 48.33 E-value: 8.76e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857580 49 ALVGPDGAGKSTFMRLLCGLEAPDEGRLSVLGTT-PDPDNEDFTT----RIAFMPQTLGLYKTLSCRENLEVfaglrgfe 123
Cdd:PRK11144 28 AIFGRSGAGKTSLINAISGLTRPQKGRIVLNGRVlFDAEKGICLPpekrRIGYVFQDARLFPHYKVRGNLRY-------- 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857580 124 GEADGAAGLERRIAELLSMTGLAgfeERQAGKLSGGMKQKLALASALLRIPDLLLLDEPTVGVDPLSRRELWSVVRRmLA 203
Cdd:PRK11144 100 GMAKSMVAQFDKIVALLGIEPLL---DRYPGSLSGGEKQRVAIGRALLTAPELLLMDEPLASLDLPRKRELLPYLER-LA 175
|
170 180 190
....*....|....*....|....*....|....*.
gi 2553857580 204 ---DTPMtcVFSTAYLEEA-EAADRVLLFESGRIIA 235
Cdd:PRK11144 176 reiNIPI--LYVSHSLDEIlRLADRVVVLEQGKVKA 209
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
28-234 |
8.99e-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: 46.87 E-value: 8.99e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857580 28 IRAVDGIsLKAGgaeasdRLIALVGPDGAGKSTFMRLLCGLEAPD---EGRLSVLGTTPDPDNEDFTTRIAFMPQTLGLY 104
Cdd:cd03233 23 LKDFSGV-VKPG------EMVLVLGRPGSGCSTLLKALANRTEGNvsvEGDIHYNGIPYKEFAEKYPGEIIYVSEEDVHF 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857580 105 KTLSCRENLEVFAGLRGfegeadgaaglerriAELLSmtglagfeerqagKLSGGMKQKLALASALLRIPDLLLLDEPTV 184
Cdd:cd03233 96 PTLTVRETLDFALRCKG---------------NEFVR-------------GISGGERKRVSIAEALVSRASVLCWDNSTR 147
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 2553857580 185 GVDPLSRRELWSVVRRMLADTPMTCVFST--AYLEEAEAADRVLLFESGRII 234
Cdd:cd03233 148 GLDSSTALEILKCIRTMADVLKTTTFVSLyqASDEIYDLFDKVLVLYEGRQI 199
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
396-577 |
9.53e-06 |
|
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of the ABC transporter ATP-binding cassette, but are found outside the common ABC transporter operon structure that features integral membrane permease proteins and substrate-binding proteins encoded next to the ATP-binding cassette (ABC domain) protein. The member protein ChvD from Agrobacterium tumefaciens was identified as both a candidate to interact with VirB8, based on yeast two-hybrid analysis, and as an apparent regulator of VirG. The general function of this protein family is unknown.
Pssm-ID: 274744 [Multi-domain] Cd Length: 552 Bit Score: 48.78 E-value: 9.53e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857580 396 GLLGPNGAGKTTTFRMLCGLLVPSKGQievagydlrtAKAGARARIGYVAQKFSLYGKLSVEQN-----------LRYFG 464
Cdd:TIGR03719 35 GVLGLNGAGKSTLLRIMAGVDKDFNGE----------ARPQPGIKVGYLPQEPQLDPTKTVRENveegvaeikdaLDRFN 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857580 465 RSYGFFG------------QA-LQDRIDASleDFGLTDRR-------------DTTAGSLSFGAKQDLSMACGLIHSPEI 518
Cdd:TIGR03719 105 EISAKYAepdadfdklaaeQAeLQEIIDAA--DAWDLDSQleiamdalrcppwDADVTKLSGGERRRVALCRLLLSKPDM 182
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857580 519 LFLDEATSGADLASrrAFWRRiNALASAGTSVVVTTHfleeaeycDR-FLIQDAGKVLAL 577
Cdd:TIGR03719 183 LLLDEPTNHLDAES--VAWLE-RHLQEYPGTVVAVTH--------DRyFLDNVAGWILEL 231
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
51-233 |
1.23e-05 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 47.72 E-value: 1.23e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857580 51 VGPDGAGKSTFMRLLCGLEAPDEGRLsVLGTTPDPDNEDFTTRIAFMPQTLGLYKTLSCRENLEVFAGLRGFEgeadgAA 130
Cdd:PRK11000 35 VGPSGCGKSTLLRMIAGLEDITSGDL-FIGEKRMNDVPPAERGVGMVFQSYALYPHLSVAENMSFGLKLAGAK-----KE 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857580 131 GLERRIAELLSMTGLAGFEERQAGKLSGGMKQKLALASALLRIPDLLLLDEPTVGVDPLSRRELWSVVRRMLADTPMTCV 210
Cdd:PRK11000 109 EINQRVNQVAEVLQLAHLLDRKPKALSGGQRQRVAIGRTLVAEPSVFLLDEPLSNLDAALRVQMRIEISRLHKRLGRTMI 188
|
170 180
....*....|....*....|....*.
gi 2553857580 211 FSTAylEEAEA---ADRVLLFESGRI 233
Cdd:PRK11000 189 YVTH--DQVEAmtlADKIVVLDAGRV 212
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
7-218 |
1.71e-05 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 46.95 E-value: 1.71e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857580 7 PAIRlegvVKTFPNPLDAARpirAVDGISLKAggaeASDRLIALVGPDGAGKSTFMRLLCGL-----EAPDEGRLSVLGT 81
Cdd:PRK14258 6 PAIK----VNNLSFYYDTQK---ILEGVSMEI----YQSKVTAIIGPSGCGKSTFLKCLNRMnelesEVRVEGRVEFFNQ 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857580 82 TPDPDNEDFTT---RIAFMPQTLGLYKtLSCRENLEVFAGLRGFEG--EADGAAGLERRIAELLSMtgLAGFEERQAGKL 156
Cdd:PRK14258 75 NIYERRVNLNRlrrQVSMVHPKPNLFP-MSVYDNVAYGVKIVGWRPklEIDDIVESALKDADLWDE--IKHKIHKSALDL 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2553857580 157 SGGMKQKLALASALLRIPDLLLLDEPTVGVDPLSRRELWSVVRRMLADTPMTCVFSTAYLEE 218
Cdd:PRK14258 152 SGGQQQRLCIARALAVKPKVLLMDEPCFGLDPIASMKVESLIQSLRLRSELTMVIVSHNLHQ 213
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
366-555 |
1.99e-05 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 46.10 E-value: 1.99e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857580 366 VIRADGIARKFGNFVAVADTSFEVRRGEIFGLLGPNGAGKTTTFRMLCGLLV--PSKGQIEVagydlrtakagararigy 443
Cdd:COG2401 30 VLEAFGVELRVVERYVLRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGALKgtPVAGCVDV------------------ 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857580 444 vaQKFSLYGKLSVEQNLryfgrsygffgqALQDRIDASLE---DFGLTD----RRdtTAGSLSFGAKQDLSMACGLIHSP 516
Cdd:COG2401 92 --PDNQFGREASLIDAI------------GRKGDFKDAVEllnAVGLSDavlwLR--RFKELSTGQKFRFRLALLLAERP 155
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 2553857580 517 EILFLDEATSGAD--LASRRAF-----WRRinalasAGTSVVVTTH 555
Cdd:COG2401 156 KLLVIDEFCSHLDrqTAKRVARnlqklARR------AGITLVVATH 195
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
47-183 |
2.22e-05 |
|
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: 47.24 E-value: 2.22e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857580 47 LIALVGPDGAGKSTFMRLLCGLEAPDEGRLSVlGTtpdpdnedfTTRIAFMPQTlglyktlscRENLEvfAGLRGFEGEA 126
Cdd:TIGR03719 350 IVGVIGPNGAGKSTLFRMITGQEQPDSGTIEI-GE---------TVKLAYVDQS---------RDALD--PNKTVWEEIS 408
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2553857580 127 DGAAGLERRIAELLSMTGLAGF------EERQAGKLSGGMKQKLALASALLRIPDLLLLDEPT 183
Cdd:TIGR03719 409 GGLDIIKLGKREIPSRAYVGRFnfkgsdQQKKVGQLSGGERNRVHLAKTLKSGGNVLLLDEPT 471
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
423-568 |
2.27e-05 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 47.72 E-value: 2.27e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857580 423 IEVAGYDLRTAkagaRARIGYVAQKFSLYgKLSVEQNLRyFGRSYGFFGQALQDRIDASLEDF--GLTDRRDTTAG---- 496
Cdd:PTZ00265 1284 VDICDYNLKDL----RNLFSIVSQEPMLF-NMSIYENIK-FGKEDATREDVKRACKFAAIDEFieSLPNKYDTNVGpygk 1357
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2553857580 497 SLSFGAKQDLSMACGLIHSPEILFLDEATSGADLASRRAFWRRINALASAGTSVVVT-THFLEEAEYCDRFLI 568
Cdd:PTZ00265 1358 SLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDIKDKADKTIITiAHRIASIKRSDKIVV 1430
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
47-232 |
3.17e-05 |
|
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: 45.15 E-value: 3.17e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857580 47 LIALVGPDGAGKSTFMRLLCGLEAPDEGRLSVLGttpdpdnedfttRIAFMPQTLGLYKTlSCRENLeVFaGLRgFEGE- 125
Cdd:cd03250 33 LVAIVGPVGSGKSSLLSALLGELEKLSGSVSVPG------------SIAYVSQEPWIQNG-TIRENI-LF-GKP-FDEEr 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857580 126 ---ADGAAGLERRIAEL----LSMTGlagfeERQAGkLSGGMKQKLALASALLRIPDLLLLDEPTVGVDPLSRRELW-SV 197
Cdd:cd03250 97 yekVIKACALEPDLEILpdgdLTEIG-----EKGIN-LSGGQKQRISLARAVYSDADIYLLDDPLSAVDAHVGRHIFeNC 170
|
170 180 190
....*....|....*....|....*....|....*
gi 2553857580 198 VRRMLADTpMTCVFSTAYLEEAEAADRVLLFESGR 232
Cdd:cd03250 171 ILGLLLNN-KTRILVTHQLQLLPHADQIVVLDNGR 204
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
382-529 |
4.05e-05 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 46.48 E-value: 4.05e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857580 382 VADTSFEVRRGEIFGLLGPNGAGKTTTFRMLCGLLVPSKGQI------EVAGYD-LRTAKAGARARIGYVAQkfslyGKL 454
Cdd:PRK11147 335 VKDFSAQVQRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRIhcgtklEVAYFDqHRAELDPEKTVMDNLAE-----GKQ 409
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2553857580 455 SVEQNlryfGRSYGFFGQalqdridasLEDFGLTDRRDTT-AGSLSFGAKQDLSMACGLIHSPEILFLDEATSGAD 529
Cdd:PRK11147 410 EVMVN----GRPRHVLGY---------LQDFLFHPKRAMTpVKALSGGERNRLLLARLFLKPSNLLILDEPTNDLD 472
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
9-253 |
4.10e-05 |
|
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: 45.22 E-value: 4.10e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857580 9 IRLEGVVKTFPNpldaaRP-IRAVDGISL--KAGgaeasdRLIALVGPDGAGKSTFMRLLCGLEAPDEGRLSVLGTtpdp 85
Cdd:cd03249 1 IEFKNVSFRYPS-----RPdVPILKGLSLtiPPG------KTVALVGSSGCGKSTVVSLLERFYDPTSGEILLDGV---- 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857580 86 DNEDFTTR-----IAFMPQTLGLYKTlSCRENLEvFAGLRGFEGEADGAAglerRIAELLS-MTGLA-GFEER---QAGK 155
Cdd:cd03249 66 DIRDLNLRwlrsqIGLVSQEPVLFDG-TIAENIR-YGKPDATDEEVEEAA----KKANIHDfIMSLPdGYDTLvgeRGSQ 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857580 156 LSGGMKQKLALASALLRIPDLLLLDEPTVGVDPLSRRELWSVVRRMLADtpMTCVFSTAYLEEAEAADRVLLFESGRIIA 235
Cdd:cd03249 140 LSGGQKQRIAIARALLRNPKILLLDEATSALDAESEKLVQEALDRAMKG--RTTIVIAHRLSTIRNADLIAVLQNGQVVE 217
|
250
....*....|....*...
gi 2553857580 236 DENPQSFISRaKGRTYLL 253
Cdd:cd03249 218 QGTHDELMAQ-KGVYAKL 234
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
377-583 |
4.83e-05 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 45.87 E-value: 4.83e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857580 377 GNFVAVADTSFEVRRGEIFGLLGPNGAGKTTTFRMLCGLLVpSKGQIE-VAGYDLR-----TAKAGARARIGYVAQKF-- 448
Cdd:PRK09473 27 GDVTAVNDLNFSLRAGETLGIVGESGSGKSQTAFALMGLLA-ANGRIGgSATFNGReilnlPEKELNKLRAEQISMIFqd 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857580 449 ---SL--YGKLSvEQNLRYFGRSYGFfgqalqDRIDASLEDFGLTD---------RRDTTAGSLSFGAKQDLSMACGLIH 514
Cdd:PRK09473 106 pmtSLnpYMRVG-EQLMEVLMLHKGM------SKAEAFEESVRMLDavkmpearkRMKMYPHEFSGGMRQRVMIAMALLC 178
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2553857580 515 SPEILFLDEATSGADLASRRAFWRRINALASA-GTSVVVTTHFLE-EAEYCDRFLIQDAGKVLALGTPREV 583
Cdd:PRK09473 179 RPKLLIADEPTTALDVTVQAQIMTLLNELKREfNTAIIMITHDLGvVAGICDKVLVMYAGRTMEYGNARDV 249
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
3-80 |
5.82e-05 |
|
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 444078 [Multi-domain] Cd Length: 605 Bit Score: 45.97 E-value: 5.82e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857580 3 KASAPAIRLEGVVKTFpnplDAARPIraVDGISL--KAGgaeasdRLIALVGPDGAGKSTFMRLLCGLEAPDEGRLSVLG 80
Cdd:COG5265 352 VVGGGEVRFENVSFGY----DPERPI--LKGVSFevPAG------KTVAIVGPSGAGKSTLARLLFRFYDVTSGRILIDG 419
|
|
| sufC |
PRK09580 |
cysteine desulfurase ATPase component; Reviewed |
388-562 |
5.85e-05 |
|
cysteine desulfurase ATPase component; Reviewed
Pssm-ID: 181965 [Multi-domain] Cd Length: 248 Bit Score: 45.17 E-value: 5.85e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857580 388 EVRRGEIFGLLGPNGAGKTTTFRMLCGL--LVPSKGQIEVAGYDLRTAKAGARA------------RIGYVAQKFSLYGK 453
Cdd:PRK09580 23 EVRPGEVHAIMGPNGSGKSTLSATLAGRedYEVTGGTVEFKGKDLLELSPEDRAgegifmafqypvEIPGVSNQFFLQTA 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857580 454 LSVEQNLRyfgrsygffGQALQDRIDasLEDFgLTDR------------RDTTAGsLSFGAKQD---LSMAcglIHSPEI 518
Cdd:PRK09580 103 LNAVRSYR---------GQEPLDRFD--FQDL-MEEKiallkmpedlltRSVNVG-FSGGEKKRndiLQMA---VLEPEL 166
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 2553857580 519 LFLDEATSGADLASRRAFWRRINALASAGTSVVVTTHFLEEAEY 562
Cdd:PRK09580 167 CILDESDSGLDIDALKIVADGVNSLRDGKRSFIIVTHYQRILDY 210
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
384-589 |
6.21e-05 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 45.20 E-value: 6.21e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857580 384 DTSFEVRRGEIFGLLGPNGAGKTTTFRMLCGLLVPS--------KGQIEVAGYDLRTAKAGARARIGYV-AQKFSLYGKL 454
Cdd:PRK13547 19 DLSLRIEPGRVTALLGRNGAGKSTLLKALAGDLTGGgaprgarvTGDVTLNGEPLAAIDAPRLARLRAVlPQAAQPAFAF 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857580 455 SVEQNL---RY-FGRSYGFFGQALQDRIDASLEDFGLT--DRRDTTAGSLSFGAKQDLSMACGLIH-------SPEILFL 521
Cdd:PRK13547 99 SAREIVllgRYpHARRAGALTHRDGEIAWQALALAGATalVGRDVTTLSGGELARVQFARVLAQLWpphdaaqPPRYLLL 178
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2553857580 522 DEATSGADLASRRAFWRRINALA---SAGTSVVVTTHFLeEAEYCDRFLIQDAGKVLALGTPREVKQRAAV 589
Cdd:PRK13547 179 DEPTAALDLAHQHRLLDTVRRLArdwNLGVLAIVHDPNL-AARHADRIAMLADGAIVAHGAPADVLTPAHI 248
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
9-233 |
6.33e-05 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 46.12 E-value: 6.33e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857580 9 IRLEGVVKTFPNPLDAARPIravdGISLKAGgaeasdRLIALVGPDGAGKSTFMRLLCGLEAPDEGRLSVLGTTPDPDN- 87
Cdd:PRK10522 323 LELRNVTFAYQDNGFSVGPI----NLTIKRG------ELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKPVTAEQp 392
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857580 88 EDFTTRIAfmpqtlglyktlSCRENLEVFAGLRGFEGE----ADGAAGLERriaelLSMTGLAGFEERQAG--KLSGGMK 161
Cdd:PRK10522 393 EDYRKLFS------------AVFTDFHLFDQLLGPEGKpanpALVEKWLER-----LKMAHKLELEDGRISnlKLSKGQK 455
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2553857580 162 QKLALASALLRIPDLLLLDEPTVGVDPLSRRELWSVVRRMLADTPMTcVFST----AYLEEaeaADRVLLFESGRI 233
Cdd:PRK10522 456 KRLALLLALAEERDILLLDEWAADQDPHFRREFYQVLLPLLQEMGKT-IFAIshddHYFIH---ADRLLEMRNGQL 527
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
42-183 |
6.38e-05 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 46.10 E-value: 6.38e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857580 42 EASDRlIALVGPDGAGKSTFMRLLCGLEAPDEGRL--------SVLGTTPdPDNE-----DFTTR-IAFMPQTLGLYKTL 107
Cdd:PRK11147 27 EDNER-VCLVGRNGAGKSTLMKILNGEVLLDDGRIiyeqdlivARLQQDP-PRNVegtvyDFVAEgIEEQAEYLKRYHDI 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857580 108 SCR-------ENLEVFAGLRGfEGEADGAAGLERRIAELLSMTGLAGfeERQAGKLSGGMKQKLALASALLRIPDLLLLD 180
Cdd:PRK11147 105 SHLvetdpseKNLNELAKLQE-QLDHHNLWQLENRINEVLAQLGLDP--DAALSSLSGGWLRKAALGRALVSNPDVLLLD 181
|
...
gi 2553857580 181 EPT 183
Cdd:PRK11147 182 EPT 184
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
381-591 |
6.71e-05 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 45.34 E-value: 6.71e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857580 381 AVADTSFEVRRGEIFGLLGPNGAGKTTTFRMLCGLLVPSKGQIEVAGYDL----RTAKAGARARIGYVAQkfSLYGKLSV 456
Cdd:PRK11308 30 ALDGVSFTLERGKTLAVVGESGCGKSTLARLLTMIETPTGGELYYQGQDLlkadPEAQKLLRQKIQIVFQ--NPYGSLNP 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857580 457 EQNLryfgrsygffGQALQD--RIDASLedfGLTDRRDTTAGSL-----------------SFGAKQDLSMACGLIHSPE 517
Cdd:PRK11308 108 RKKV----------GQILEEplLINTSL---SAAERREKALAMMakvglrpehydryphmfSGGQRQRIAIARALMLDPD 174
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2553857580 518 ILFLDEATSGADLaSRRAfwRRINALA----SAGTSVVVTTHFLEEAEYcdrflIQDAGKVLALGTPREVKQRAAVLS 591
Cdd:PRK11308 175 VVVADEPVSALDV-SVQA--QVLNLMMdlqqELGLSYVFISHDLSVVEH-----IADEVMVMYLGRCVEKGTKEQIFN 244
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
391-555 |
7.02e-05 |
|
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a variety of cellular activities. This profile/alignment only detects a fraction of this vast family. The poorly conserved N-terminal helix is missing from the alignment.
Pssm-ID: 214640 [Multi-domain] Cd Length: 148 Bit Score: 43.52 E-value: 7.02e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857580 391 RGEIFGLLGPNGAGKTTTFRMLCGLLVPSKGQIEVAGydlrtakagararigyvAQKFSLYGKLSVEQNLRYFGRSYGFF 470
Cdd:smart00382 1 PGEVILIVGPPGSGKTTLARALARELGPPGGGVIYID-----------------GEDILEEVLDQLLLIIVGGKKASGSG 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857580 471 GQALQDRIDAsledfgltdrrdttagslsfgAKQdlsmacgliHSPEILFLDEATSGADLASRRAFWR------RINALA 544
Cdd:smart00382 64 ELRLRLALAL---------------------ARK---------LKPDVLILDEITSLLDAEQEALLLLleelrlLLLLKS 113
|
170
....*....|.
gi 2553857580 545 SAGTSVVVTTH 555
Cdd:smart00382 114 EKNLTVILTTN 124
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
9-169 |
7.11e-05 |
|
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: 45.89 E-value: 7.11e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857580 9 IRLEGVVKTFPNpldAARPIraVDGISLKAGGAEAsdrlIALVGPDGAGKSTFMRLLCGLEAPDEGRLSVLGTTPDP-DN 87
Cdd:COG4618 331 LSVENLTVVPPG---SKRPI--LRGVSFSLEPGEV----LGVIGPSGSGKSTLARLLVGVWPPTAGSVRLDGADLSQwDR 401
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857580 88 EDFTTRIAFMPQTLGLYKTlSCRENLEVFaglrgfeGEADG--------AAGLERRIAEL-------LSMTGLAgfeerq 152
Cdd:COG4618 402 EELGRHIGYLPQDVELFDG-TIAENIARF-------GDADPekvvaaakLAGVHEMILRLpdgydtrIGEGGAR------ 467
|
170
....*....|....*..
gi 2553857580 153 agkLSGGMKQKLALASA 169
Cdd:COG4618 468 ---LSGGQRQRIGLARA 481
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
371-414 |
7.69e-05 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 45.55 E-value: 7.69e-05
10 20 30 40
....*....|....*....|....*....|....*....|....
gi 2553857580 371 GIARKFGNFVAVADTSFEVRRGEIFGLLGPNGAGKTTTFRMLCG 414
Cdd:NF040905 6 GITKTFPGVKALDDVNLSVREGEIHALCGENGAGKSTLMKVLSG 49
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
154-236 |
1.53e-04 |
|
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: 44.82 E-value: 1.53e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857580 154 GKLSGGMKQKLALASALLRIPDLLLLDEPTVGVDPLSRRELWSVVRRMLADTPMTCVFSTAYLEEAEAADRVLLFESGRI 233
Cdd:TIGR02633 402 GRLSGGNQQKAVLAKMLLTNPRVLILDEPTRGVDVGAKYEIYKLINQLAQEGVAIIVVSSELAEVLGLSDRVLVIGEGKL 481
|
...
gi 2553857580 234 IAD 236
Cdd:TIGR02633 482 KGD 484
|
|
| nickel_nikD |
TIGR02770 |
nickel import ATP-binding protein NikD; This family represents the NikD subunit of a ... |
30-234 |
1.58e-04 |
|
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: 43.51 E-value: 1.58e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857580 30 AVDGISL--KAGgaeasdRLIALVGPDGAGKSTFMRLLCGLEAPD----EGRLSVLGTTPDPD---NEDFTT-----RIA 95
Cdd:TIGR02770 1 LVQDLNLslKRG------EVLALVGESGSGKSLTCLAILGLLPPGltqtSGEILLDGRPLLPLsirGRHIATimqnpRTA 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857580 96 FMP-QTLGLYKTLSCRENLEVFAGLRGFEGEADGAAGLERrIAELLSMTGlagFEerqagkLSGGMKQKLALASALLRIP 174
Cdd:TIGR02770 75 FNPlFTMGNHAIETLRSLGKLSKQARALILEALEAVGLPD-PEEVLKKYP---FQ------LSGGMLQRVMIALALLLEP 144
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2553857580 175 DLLLLDEPTVGVDPLSRRELWSVVRRMLADTPMTCVFSTAYLEE-AEAADRVLLFESGRII 234
Cdd:TIGR02770 145 PFLIADEPTTDLDVVNQARVLKLLRELRQLFGTGILLITHDLGVvARIADEVAVMDDGRIV 205
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
45-81 |
1.70e-04 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 44.56 E-value: 1.70e-04
10 20 30
....*....|....*....|....*....|....*..
gi 2553857580 45 DRlIALVGPDGAGKSTFMRLLCGLEAPDEGRLSVlGT 81
Cdd:PRK11147 346 DK-IALIGPNGCGKTTLLKLMLGQLQADSGRIHC-GT 380
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
377-446 |
1.70e-04 |
|
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: 44.68 E-value: 1.70e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2553857580 377 GNFVAVADTSFEVRRGEIFGLLGPNGAGKTTTFRMLCGLLVPS----KGQIEVAGYDLRTAKAGAR-----ARIGYVAQ 446
Cdd:COG4172 21 GTVEAVKGVSFDIAAGETLALVGESGSGKSVTALSILRLLPDPaahpSGSILFDGQDLLGLSERELrrirgNRIAMIFQ 99
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
3-74 |
1.83e-04 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 44.50 E-value: 1.83e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2553857580 3 KASA---PAIRLEGVVKTFPNPLDAARPIRAVDGISLKAGG---AEASDRlIALVGPDGAGKSTFMRLLCGLEAPDEG 74
Cdd:PRK15064 298 KPSSrqnPFIRFEQDKKLHRNALEVENLTKGFDNGPLFKNLnllLEAGER-LAIIGENGVGKTTLLRTLVGELEPDSG 374
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
382-574 |
1.84e-04 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 44.40 E-value: 1.84e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857580 382 VADTSFEVRRGEIFGLLGPNGAGKTTTFRMLCGLLVPSK--GQIEVAG--YDLRTAKAGARARIGYVAQKFSLYGkLSVE 457
Cdd:NF040905 276 VDDVSLNVRRGEIVGIAGLMGAGRTELAMSVFGRSYGRNisGTVFKDGkeVDVSTVSDAIDAGLAYVTEDRKGYG-LNLI 354
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857580 458 QNLRY-------FGRSYGFFGQALQDRIDAslEDFgltdRR---------DTTAGSLSFGAKQDLSMACGLIHSPEILFL 521
Cdd:NF040905 355 DDIKRnitlanlGKVSRRGVIDENEEIKVA--EEY----RKkmniktpsvFQKVGNLSGGNQQKVVLSKWLFTDPDVLIL 428
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 2553857580 522 DEATSGADLASRRAFWRRINALASAGTSVVVTTHFLEEA-EYCDRFLIQDAGKV 574
Cdd:NF040905 429 DEPTRGIDVGAKYEIYTIINELAAEGKGVIVISSELPELlGMCDRIYVMNEGRI 482
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
7-214 |
2.09e-04 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 43.02 E-value: 2.09e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857580 7 PAIRLEGVVKTFPNPLDAARPIRAVdgisLKAGGAEASDR----------------LIALVGPDGAGKSTFMRLLCGLE- 69
Cdd:COG2401 6 PFFVLMRVTKVYSSVLDLSERVAIV----LEAFGVELRVVeryvlrdlnleiepgeIVLIVGASGSGKSTLLRLLAGALk 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857580 70 -APDEGRLSVLGTTPDPDnedfttriafmpqtlglyktLSCRENLevfaglrGFEGEADGAaglerriAELLSMTGL--A 146
Cdd:COG2401 82 gTPVAGCVDVPDNQFGRE--------------------ASLIDAI-------GRKGDFKDA-------VELLNAVGLsdA 127
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2553857580 147 GFEERQAGKLSGGMKQKLALASALLRIPDLLLLDEPTVGVDPLSRRELWSVVRRMLADTPMTCVFSTA 214
Cdd:COG2401 128 VLWLRRFKELSTGQKFRFRLALLLAERPKLLVIDEFCSHLDRQTAKRVARNLQKLARRAGITLVVATH 195
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
49-250 |
2.53e-04 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 43.23 E-value: 2.53e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857580 49 ALVGPDGAGKSTFMRLLCGL-----EAPDEGRLSVLGT---TPDPDNEDFTTRIAFMPQTLGLYKtLSCRENleVFAGLR 120
Cdd:PRK14239 35 ALIGPSGSGKSTLLRSINRMndlnpEVTITGSIVYNGHniySPRTDTVDLRKEIGMVFQQPNPFP-MSIYEN--VVYGLR 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857580 121 gFEGEADGA---AGLERriaellSMTGLAGFEERQ------AGKLSGGMKQKLALASALLRIPDLLLLDEPTVGVDPLSR 191
Cdd:PRK14239 112 -LKGIKDKQvldEAVEK------SLKGASIWDEVKdrlhdsALGLSGGQQQRVCIARVLATSPKIILLDEPTSALDPISA 184
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2553857580 192 RELWSVVRRMLADTPMTCVfsTAYLEEA-EAADRVLLFESGRIIA-DENPQSFISRAKGRT 250
Cdd:PRK14239 185 GKIEETLLGLKDDYTMLLV--TRSMQQAsRISDRTGFFLDGDLIEyNDTKQMFMNPKHKET 243
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
48-245 |
2.97e-04 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 44.20 E-value: 2.97e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857580 48 IALVGPDGAGKSTFMRLLCGLEAPDEGRLSV-------LGTTpdpdneDFTTRIAFMPQTLGLYKTlSCRENLEVFAGlr 120
Cdd:PLN03232 1265 VGVVGRTGAGKSSMLNALFRIVELEKGRIMIddcdvakFGLT------DLRRVLSIIPQSPVLFSG-TVRFNIDPFSE-- 1335
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857580 121 gfEGEADGAAGLER-RIAELLSMT--GLAGFEERQAGKLSGGMKQKLALASALLRIPDLLLLDEPTVGVDPLSRRELWSV 197
Cdd:PLN03232 1336 --HNDADLWEALERaHIKDVIDRNpfGLDAEVSEGGENFSVGQRQLLSLARALLRRSKILVLDEATASVDVRTDSLIQRT 1413
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 2553857580 198 VRRMLADTPMTCVfsTAYLEEAEAADRVLLFESGRIIADENPQSFISR 245
Cdd:PLN03232 1414 IREEFKSCTMLVI--AHRLNTIIDCDKILVLSSGQVLEYDSPQELLSR 1459
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
47-121 |
3.26e-04 |
|
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: 42.23 E-value: 3.26e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2553857580 47 LIALVGPDGAGKSTFMRLLCGLEAPD--EGRLSVLGTtpdPDNEDFTTRIAFMPQTLGLYKTLSCRENLEVFAGLRG 121
Cdd:cd03232 35 LTALMGESGAGKTTLLDVLAGRKTAGviTGEILINGR---PLDKNFQRSTGYVEQQDVHSPNLTVREALRFSALLRG 108
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
51-78 |
3.61e-04 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 43.57 E-value: 3.61e-04
10 20
....*....|....*....|....*...
gi 2553857580 51 VGPDGAGKSTFMRLLCGLEAPDEGRLSV 78
Cdd:PRK11819 356 IGPNGAGKSTLFKMITGQEQPDSGTIKI 383
|
|
| AAA_21 |
pfam13304 |
AAA domain, putative AbiEii toxin, Type IV TA system; Several members are annotated as being ... |
422-555 |
4.58e-04 |
|
AAA domain, putative AbiEii toxin, Type IV TA system; Several members are annotated as being of the abortive phage resistance system, in which case the family would be acting as the toxin for a type IV toxin-antitoxin resistance system.
Pssm-ID: 433102 [Multi-domain] Cd Length: 303 Bit Score: 42.76 E-value: 4.58e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857580 422 QIEVAGYDLRTAKAGARARIGYVAQKFSLYGKLSVEQNLRYFGRSYGFFGQALQDRIDASLEDFGL-----TDRRDTTAG 496
Cdd:pfam13304 156 LLDEGLLLEDWAVLDLAADLALFPDLKELLQRLVRGLKLADLNLSDLGEGIEKSLLVDDRLRERGLillenGGGGELPAF 235
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2553857580 497 SLSFGAKQdlsmACGLI-------HSPEILFLDEATSGADLASRRAFWRRINALASAGTSVVVTTH 555
Cdd:pfam13304 236 ELSDGTKR----LLALLaallsalPKGGLLLIDEPESGLHPKLLRRLLELLKELSRNGAQLILTTH 297
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
4-169 |
5.32e-04 |
|
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: 43.13 E-value: 5.32e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857580 4 ASAPAI-RLEGVVKTFPNP----LDAARPIRAVDGIS--LKAGgaeasdRLIALVGPDGAGKSTFMRLLCGLEaPDEGRL 76
Cdd:COG4172 270 PDAPPLlEARDLKVWFPIKrglfRRTVGHVKAVDGVSltLRRG------ETLGLVGESGSGKSTLGLALLRLI-PSEGEI 342
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857580 77 SVLGTTPD--PDNEDFTTR----IAFM-PqtlglYKTLSCRENLE--VFAGLRGFEGEADGAAgLERRIAELLSMTGL-A 146
Cdd:COG4172 343 RFDGQDLDglSRRALRPLRrrmqVVFQdP-----FGSLSPRMTVGqiIAEGLRVHGPGLSAAE-RRARVAEALEEVGLdP 416
|
170 180
....*....|....*....|...
gi 2553857580 147 GFEERQAGKLSGGMKQKLALASA 169
Cdd:COG4172 417 AARHRYPHEFSGGQRQRIAIARA 439
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
46-231 |
5.50e-04 |
|
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: 43.36 E-value: 5.50e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857580 46 RLIALVGPDGAGKSTFMRLLCGLEAPDEGRLSVLGttpdpdnedfttRIAFMPQTLGLYKTlSCRENLeVFaGLRGFE-- 123
Cdd:TIGR01271 453 QLLAVAGSTGSGKSSLLMMIMGELEPSEGKIKHSG------------RISFSPQTSWIMPG-TIKDNI-IF-GLSYDEyr 517
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857580 124 -GEADGAAGLERRIAELL----SMTGLAGFeerqagKLSGGMKQKLALASALLRIPDLLLLDEPTVGVDPLSRRELW-SV 197
Cdd:TIGR01271 518 yTSVIKACQLEEDIALFPekdkTVLGEGGI------TLSGGQRARISLARAVYKDADLYLLDSPFTHLDVVTEKEIFeSC 591
|
170 180 190
....*....|....*....|....*....|....
gi 2553857580 198 VRRMLADTpmTCVFSTAYLEEAEAADRVLLFESG 231
Cdd:TIGR01271 592 LCKLMSNK--TRILVTSKLEHLKKADKILLLHEG 623
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
381-593 |
9.78e-04 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 41.62 E-value: 9.78e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857580 381 AVADTSFEVRRGEIFGLLGPNGAGKTTTFRMLCGLLVPSKGQIEVAGYDLRTAKA----GARARIGYVAQK--FSLYGKL 454
Cdd:PRK15079 36 AVDGVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGEVAWLGKDLLGMKDdewrAVRSDIQMIFQDplASLNPRM 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857580 455 SVEQNLRYFGRSY--GFFGQALQDRIDASLEDFGL----TDRrdtTAGSLSFGAKQDLSMACGLIHSPEILFLDEATSGA 528
Cdd:PRK15079 116 TIGEIIAEPLRTYhpKLSRQEVKDRVKAMMLKVGLlpnlINR---YPHEFSGGQCQRIGIARALILEPKLIICDEPVSAL 192
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2553857580 529 DLaSRRAfwRRINALAS----AGTSVVVTTHFLEEAEY-CDRFLIQDAGKVLALGTPREVKQRA------AVLSAV 593
Cdd:PRK15079 193 DV-SIQA--QVVNLLQQlqreMGLSLIFIAHDLAVVKHiSDRVLVMYLGHAVELGTYDEVYHNPlhpytkALMSAV 265
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
397-555 |
1.01e-03 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 42.15 E-value: 1.01e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857580 397 LLGPNGAGKTTTFRMLCGLLVPSKGQIevagydLRTAKagarARIGYVAQKFSLYGKLSVEQnLRYFGRSYgffGQALQD 476
Cdd:PLN03073 540 MVGPNGIGKSTILKLISGELQPSSGTV------FRSAK----VRMAVFSQHHVDGLDLSSNP-LLYMMRCF---PGVPEQ 605
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857580 477 RIDASLEDFGLTDRRDTTAG-SLSFGAKQDLSMACGLIHSPEILFLDEATSGADLASRRAFwrrINALASAGTSVVVTTH 555
Cdd:PLN03073 606 KLRAHLGSFGVTGNLALQPMyTLSGGQKSRVAFAKITFKKPHILLLDEPSNHLDLDAVEAL---IQGLVLFQGGVLMVSH 682
|
|
| ABC_sbcCD |
cd03279 |
ATP-binding cassette domain of sbcCD; SbcCD and other Mre11/Rad50 (MR) complexes are ... |
374-555 |
1.10e-03 |
|
ATP-binding cassette domain of sbcCD; SbcCD and other Mre11/Rad50 (MR) complexes are implicated in the metabolism of DNA ends. They cleave ends sealed by hairpin structures and are thought to play a role in removing protein bound to DNA termini.
Pssm-ID: 213246 [Multi-domain] Cd Length: 213 Bit Score: 40.72 E-value: 1.10e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857580 374 RKFGNFVAVADTSFE-VRRGEIFGLLGPNGAGKTTTFRMLCGLL---VPSKGQIEVAGYDLRTAKAGARarigyVAQKFS 449
Cdd:cd03279 9 KNFGPFREEQVIDFTgLDNNGLFLICGPTGAGKSTILDAITYALygkTPRYGRQENLRSVFAPGEDTAE-----VSFTFQ 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857580 450 LYGKL-SVEqnlRYFGRSYGFFGQAL---QDRIDASLedfgltdRRDTTagSLSFG--AKQDLSMACGL---IHSP---- 516
Cdd:cd03279 84 LGGKKyRVE---RSRGLDYDQFTRIVllpQGEFDRFL-------ARPVS--TLSGGetFLASLSLALALsevLQNRggar 151
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 2553857580 517 -EILFLDEATSGADLASRRAFWRRINALASAGTSVVVTTH 555
Cdd:cd03279 152 lEALFIDEGFGTLDPEALEAVATALELIRTENRMVGVISH 191
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
25-226 |
1.33e-03 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 40.85 E-value: 1.33e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857580 25 ARPIRAVDGISLKAGGAEASD-----------RLIAlvGPDGAGKSTFMRLLCGLEAPDEGRLSVLG---TTPDPdnEDF 90
Cdd:PRK10247 4 NSPLLQLQNVGYLAGDAKILNnisfslragefKLIT--GPSGCGKSTLLKIVASLISPTSGTLLFEGediSTLKP--EIY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857580 91 TTRIAFMPQTLGLYKTlSCRENLEVFAGLRGFEGEadgaaglERRIAEllsmtGLAGFE------ERQAGKLSGGMKQKL 164
Cdd:PRK10247 80 RQQVSYCAQTPTLFGD-TVYDNLIFPWQIRNQQPD-------PAIFLD-----DLERFAlpdtilTKNIAELSGGEKQRI 146
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2553857580 165 ALASALLRIPDLLLLDEPTVGVDPLSRRELWSVVRRMLADTPMTCVFSTAYLEEAEAADRVL 226
Cdd:PRK10247 147 SLIRNLQFMPKVLLLDEITSALDESNKHNVNEIIHRYVREQNIAVLWVTHDKDEINHADKVI 208
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
11-67 |
1.40e-03 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 41.70 E-value: 1.40e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857580 11 LE--GVVKTFPnpldaarPIRAVDGISLKAGGAEasdrlI-ALVGPDGAGKSTFMRLLCG 67
Cdd:NF040905 2 LEmrGITKTFP-------GVKALDDVNLSVREGE-----IhALCGENGAGKSTLMKVLSG 49
|
|
| BtuD |
COG4138 |
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ... |
31-169 |
1.59e-03 |
|
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism];
Pssm-ID: 443313 [Multi-domain] Cd Length: 248 Bit Score: 40.59 E-value: 1.59e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857580 31 VDGISLKAGGAEasdrLIALVGPDGAGKSTFMRLLCGLeAPDEGRLSVLGTtpdpDNEDFTT-----RIAFMPQtlglyk 105
Cdd:COG4138 12 LGPISAQVNAGE----LIHLIGPNGAGKSTLLARMAGL-LPGQGEILLNGR----PLSDWSAaelarHRAYLSQ------ 76
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2553857580 106 TLSCRENLEVFAGLRGFEGEADGAAGLERRIAELLSMTGLAGFEERQAGKLSGGMKQKLALASA 169
Cdd:COG4138 77 QQSPPFAMPVFQYLALHQPAGASSEAVEQLLAQLAEALGLEDKLSRPLTQLSGGEWQRVRLAAV 140
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
47-231 |
1.94e-03 |
|
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: 40.61 E-value: 1.94e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857580 47 LIALVGPDGAGKSTFMRLLCGLEAPDEGRLSVLGttpdpdnedfttRIAFMPQTLGLYKTlSCRENleVFAGLRGFEGEA 126
Cdd:cd03291 65 MLAITGSTGSGKTSLLMLILGELEPSEGKIKHSG------------RISFSSQFSWIMPG-TIKEN--IIFGVSYDEYRY 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857580 127 DG---AAGLERRIAELL----SMTGLAGFeerqagKLSGGMKQKLALASALLRIPDLLLLDEPTVGVDPLSRRELW-SVV 198
Cdd:cd03291 130 KSvvkACQLEEDITKFPekdnTVLGEGGI------TLSGGQRARISLARAVYKDADLYLLDSPFGYLDVFTEKEIFeSCV 203
|
170 180 190
....*....|....*....|....*....|...
gi 2553857580 199 RRMLADTpmTCVFSTAYLEEAEAADRVLLFESG 231
Cdd:cd03291 204 CKLMANK--TRILVTSKMEHLKKADKILILHEG 234
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
28-80 |
2.01e-03 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 40.85 E-value: 2.01e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 2553857580 28 IRAVDGISLKAGGAEAsdrlIALVGPDGAGKSTFMRLLCGLEAPDEGRLSVLG 80
Cdd:PRK15079 34 LKAVDGVTLRLYEGET----LGVVGESGCGKSTFARAIIGLVKATDGEVAWLG 82
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
19-187 |
2.14e-03 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 41.02 E-value: 2.14e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857580 19 PNPLDAARPIRA---VDGISlkagGAEASDRLIALVGPDGAGKSTFMRLLCGLEAPDEGRLSVLGTTPDPDNEdFTTRIA 95
Cdd:PLN03211 69 PKISDETRQIQErtiLNGVT----GMASPGEILAVLGPSGSGKSTLLNALAGRIQGNNFTGTILANNRKPTKQ-ILKRTG 143
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857580 96 FMPQTLGLYKTLSCRENLeVFAGLRGFE---GEADGAAGLERRIAELlsmtGLAGFEERQAGK-----LSGGMKQKLALA 167
Cdd:PLN03211 144 FVTQDDILYPHLTVRETL-VFCSLLRLPkslTKQEKILVAESVISEL----GLTKCENTIIGNsfirgISGGERKRVSIA 218
|
170 180
....*....|....*....|
gi 2553857580 168 SALLRIPDLLLLDEPTVGVD 187
Cdd:PLN03211 219 HEMLINPSLLILDEPTSGLD 238
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
44-234 |
2.27e-03 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 40.42 E-value: 2.27e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857580 44 SDRLIALVGPDGAGKSTFMRLLCGLEAPDEGRLSVLGTTPDPDNEDFTTRIAFMPQTLGL-------YKTLSCRENLEVF 116
Cdd:PRK14246 35 NNSIFGIMGPSGSGKSTLLKVLNRLIEIYDSKIKVDGKVLYFGKDIFQIDAIKLRKEVGMvfqqpnpFPHLSIYDNIAYP 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857580 117 AGLRGFEGEADgaagLERRIAELLSMTGL-AGFEER---QAGKLSGGMKQKLALASALLRIPDLLLLDEPTVGVDPLSRR 192
Cdd:PRK14246 115 LKSHGIKEKRE----IKKIVEECLRKVGLwKEVYDRlnsPASQLSGGQQQRLTIARALALKPKVLLMDEPTSMIDIVNSQ 190
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 2553857580 193 ELWSVVRRMLADTPMTCVfSTAYLEEAEAADRVLLFESGRII 234
Cdd:PRK14246 191 AIEKLITELKNEIAIVIV-SHNPQQVARVADYVAFLYNGELV 231
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
382-583 |
2.35e-03 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 41.11 E-value: 2.35e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857580 382 VADTSFEVRRGEIFGLLGPNGAGKTTTFRMLCGLLVPSKgqievagydlrTAKAGARARIGYVAQKFSLYGKlSVEQNLr 461
Cdd:PLN03232 633 LSDINLEIPVGSLVAIVGGTGEGKTSLISAMLGELSHAE-----------TSSVVIRGSVAYVPQVSWIFNA-TVRENI- 699
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857580 462 YFGRSY--GFFGQALQdrIDASLEDFGLTDRRDTT-----AGSLSFGAKQDLSMACGLIHSPEILFLDEATSGADL-ASR 533
Cdd:PLN03232 700 LFGSDFesERYWRAID--VTALQHDLDLLPGRDLTeigerGVNISGGQKQRVSMARAVYSNSDIYIFDDPLSALDAhVAH 777
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 2553857580 534 RAFWRRINALASAGTSVVVTT--HFLEEAeycDRFLIQDAGKVLALGTPREV 583
Cdd:PLN03232 778 QVFDSCMKDELKGKTRVLVTNqlHFLPLM---DRIILVSEGMIKEEGTFAEL 826
|
|
| PRK15177 |
PRK15177 |
Vi polysaccharide ABC transporter ATP-binding protein VexC; |
48-74 |
2.40e-03 |
|
Vi polysaccharide ABC transporter ATP-binding protein VexC;
Pssm-ID: 185099 [Multi-domain] Cd Length: 213 Bit Score: 39.66 E-value: 2.40e-03
10 20
....*....|....*....|....*..
gi 2553857580 48 IALVGPDGAGKSTFMRLLCGLEAPDEG 74
Cdd:PRK15177 16 IGILAAPGSGKTTLTRLLCGLDAPDEG 42
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
47-83 |
2.54e-03 |
|
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI's are not transport proteins, and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLI's have an N-terminal Fe-S domain and two nucleotide-binding domains, which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213189 [Multi-domain] Cd Length: 177 Bit Score: 39.09 E-value: 2.54e-03
10 20 30
....*....|....*....|....*....|....*..
gi 2553857580 47 LIALVGPDGAGKSTFMRLLCGLEAPDEGRLSVLGTTP 83
Cdd:cd03222 27 VIGIVGPNGTGKTTAVKILAGQLIPNGDNDEWDGITP 63
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
372-423 |
2.96e-03 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 40.65 E-value: 2.96e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 2553857580 372 IARKFGNfvavadtsfevrrGEIFGLLGPNGAGKTTTFRMLCGLLVPSKGQI 423
Cdd:PRK15064 20 ISVKFGG-------------GNRYGLIGANGCGKSTFMKILGGDLEPSAGNV 58
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
47-187 |
2.98e-03 |
|
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: 40.70 E-value: 2.98e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857580 47 LIALVGPDGAGKSTFMRLLCGLEAPDEGRLSVLGTtpdpdnedfttrIAFMPQTLGLyKTLSCRENLevfagLRGFEGEA 126
Cdd:TIGR00957 666 LVAVVGQVGCGKSSLLSALLAEMDKVEGHVHMKGS------------VAYVPQQAWI-QNDSLRENI-----LFGKALNE 727
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2553857580 127 DGAAGLERRIAELLSMTGLAGFEERQAGK----LSGGMKQKLALASALLRIPDLLLLDEPTVGVD 187
Cdd:TIGR00957 728 KYYQQVLEACALLPDLEILPSGDRTEIGEkgvnLSGGQKQRVSLARAVYSNADIYLFDDPLSAVD 792
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
363-586 |
3.37e-03 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 39.68 E-value: 3.37e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857580 363 RPVVIRADGIaRKFGNFVAVADTSFEVRRGEIFGLLGPNGAGKTTTFRMLCGLLVP----SKGQIEVAGydLRTAKAGAR 438
Cdd:PRK10418 1 MPQQIELRNI-ALQAAQPLVHGVSLTLQRGRVLALVGGSGSGKSLTCAAALGILPAgvrqTAGRVLLDG--KPVAPCALR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857580 439 AR-IGYVAQK-FSLYGKL-SVEQNLRYFGRSYGffGQALQDRIDASLEDFGLTDRR---DTTAGSLSFGAKQDLSMACGL 512
Cdd:PRK10418 78 GRkIATIMQNpRSAFNPLhTMHTHARETCLALG--KPADDATLTAALEAVGLENAArvlKLYPFEMSGGMLQRMMIALAL 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2553857580 513 IHSPEILFLDEATSGADLASRRAFWRRINAL-ASAGTSVVVTTHFLE-EAEYCDRFLIQDAGKVLALGTPREVKQR 586
Cdd:PRK10418 156 LCEAPFIIADEPTTDLDVVAQARILDLLESIvQKRALGMLLVTHDMGvVARLADDVAVMSHGRIVEQGDVETLFNA 231
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
2-167 |
3.92e-03 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 40.01 E-value: 3.92e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857580 2 TKASAPAIRLEGVVktfpnpLDAARPIRAVDGISLKAGGAEasdrLIALVGPDGAGKSTFMRLLCGLEAPDEGRLSVLGT 81
Cdd:COG3845 251 AEPGEVVLEVENLS------VRDDRGVPALKDVSLEVRAGE----ILGIAGVAGNGQSELAEALAGLRPPASGSIRLDGE 320
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857580 82 tpDPDNEDFTTR----IAFMP---QTLGLYKTLSCRENLevfaGLRGFEGEADGAAGLERRiAELLSMTG--------LA 146
Cdd:COG3845 321 --DITGLSPRERrrlgVAYIPedrLGRGLVPDMSVAENL----ILGRYRRPPFSRGGFLDR-KAIRAFAEelieefdvRT 393
|
170 180
....*....|....*....|.
gi 2553857580 147 GFEERQAGKLSGGMKQKLALA 167
Cdd:COG3845 394 PGPDTPARSLSGGNQQKVILA 414
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
396-525 |
5.83e-03 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 39.72 E-value: 5.83e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857580 396 GLLGPNGAGKTTTFRMLCGLLVPSKGQievagydlrtAKAGARARIGYVAQKFSLYGKLSVEQN-----------LRYFG 464
Cdd:PRK11819 37 GVLGLNGAGKSTLLRIMAGVDKEFEGE----------ARPAPGIKVGYLPQEPQLDPEKTVRENveegvaevkaaLDRFN 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857580 465 RSYGFFG------------QA-LQDRIDASleDFGLTDRR-------------DTTAGSLSFGAKQDLSMACGLIHSPEI 518
Cdd:PRK11819 107 EIYAAYAepdadfdalaaeQGeLQEIIDAA--DAWDLDSQleiamdalrcppwDAKVTKLSGGERRRVALCRLLLEKPDM 184
|
....*..
gi 2553857580 519 LFLDEAT 525
Cdd:PRK11819 185 LLLDEPT 191
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
50-205 |
7.98e-03 |
|
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: 38.50 E-value: 7.98e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857580 50 LVGPDGAGKSTFMRLLCGLEAPDEGRLsvlGTTPDPDN----------EDFTTRI-------AFMPQTLGLY-KTL--SC 109
Cdd:cd03236 31 LVGPNGIGKSTALKILAGKLKPNLGKF---DDPPDWDEildefrgselQNYFTKLlegdvkvIVKPQYVDLIpKAVkgKV 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857580 110 RENLEvfaglrgfegEADGAAGLErriaELLSMTGLAGFEERQAGKLSGGMKQKLALASALLRIPDLLLLDEPTVGVDPL 189
Cdd:cd03236 108 GELLK----------KKDERGKLD----ELVDQLELRHVLDRNIDQLSGGELQRVAIAAALARDADFYFFDEPSSYLDIK 173
|
170
....*....|....*.
gi 2553857580 190 SRRELWSVVRRMLADT 205
Cdd:cd03236 174 QRLNAARLIRELAEDD 189
|
|
| CP_lyasePhnK |
TIGR02323 |
phosphonate C-P lyase system protein PhnK; Members of this family are the PhnK protein of C-P ... |
47-234 |
9.28e-03 |
|
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: 38.27 E-value: 9.28e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857580 47 LIALVGPDGAGKSTFMRLLCGLEAPDEGRLSV---------LGTTPDPDNEDFT-TRIAFMPQTL--GLYKTLSCRENLE 114
Cdd:TIGR02323 31 VLGIVGESGSGKSTLLGCLAGRLAPDHGTATYimrsgaeleLYQLSEAERRRLMrTEWGFVHQNPrdGLRMRVSAGANIG 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857580 115 ---VFAGLRGFeGEADGAAGLERRIAELLsmtglAGFEERQAGKLSGGMKQKLALASALLRIPDLLLLDEPTVGVDPLSR 191
Cdd:TIGR02323 111 erlMAIGARHY-GNIRATAQDWLEEVEID-----PTRIDDLPRAFSGGMQQRLQIARNLVTRPRLVFMDEPTGGLDVSVQ 184
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 2553857580 192 RELWSVVRRMLADTPMTCVFSTAYLEEAE-AADRVLLFESGRII 234
Cdd:TIGR02323 185 ARLLDLLRGLVRDLGLAVIIVTHDLGVARlLAQRLLVMQQGRVV 228
|
|
| |
