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Conserved domains on  [gi|1054819401|ref|WP_066582031|]
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ABC transporter ATP-binding protein [Cellulomonas timonensis]

Protein Classification

ABC transporter ATP-binding protein( domain architecture ID 11467437)

ABC transporter ATP-binding protein is the ATPase catalytic subunit of an ATP transporter complex responsible for coupling the energy of ATP hydrolysis to the import of one or more from a variety of substrates including Fe(3+) ions and polyamines such as spermidine and putrescine

CATH:  3.40.50.300
EC:  7.-.-.-
Gene Ontology:  GO:0042626|GO:0140359|GO:0005524|GO:0016887
PubMed:  25750732|24638992
SCOP:  4003976
TCDB:  3.A.1

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PotA COG3842
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ...
 20-368 0e+00

ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];


:

Pssm-ID: 443052 [Multi-domain]  Cd Length: 353  Bit Score: 511.57  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054819401  20 LELAAVTKRFGAFVAVDDLTLTVPSGSFFALLGPSGCGKTTTLRMVAGLEQPTDGTISIDGRDVTGTRAHRRPVNTVFQS 99
Cdd:COG3842     6 LELENVSKRYGDVTALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRILLDGRDVTGLPPEKRNVGMVFQD 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054819401 100 YALFPHLTVAENVAFGLRRRR--EADVEARVAEGLALVELGHLADRRPALLSGGQQQRVALARALVNRPALLLLDEPLGA 177
Cdd:COG3842    86 YALFPHLTVAENVAFGLRMRGvpKAEIRARVAELLELVGLEGLADRYPHQLSGGQQQRVALARALAPEPRVLLLDEPLSA 165

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054819401 178 LDLKLRRQMQLELKRIQTEVGLTFVHVTHDQEEAMTMADTVAVMNRGRIEQMGPPADLYEHPRTTFVANFLGRSNLVPGT 257
Cdd:COG3842   166 LDAKLREEMREELRRLQRELGITFIYVTHDQEEALALADRIAVMNDGRIEQVGTPEEIYERPATRFVADFIGEANLLPGT 245

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054819401 258 VVERLDGdllGVDVGGARVRVPASRAVRDTGDVLVGARPEKVRLladgeEPAPDENVVgPGTVTDVSFTGVSTQYEVRVP 337
Cdd:COG3842   246 VLGDEGG---GVRTGGRTLEVPADAGLAAGGPVTVAIRPEDIRL-----SPEGPENGL-PGTVEDVVFLGSHVRYRVRLG 316

                         330       340       350
                  ....*....|....*....|....*....|.
gi 1054819401 338 GLGVFGVFAQNlSGRAGAALGDQVRLAWAVD 368
Cdd:COG3842   317 DGQELVVRVPN-RAALPLEPGDRVGLSWDPE 346
 
Name Accession Description Interval E-value
PotA COG3842
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ...
 20-368 0e+00

ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];


Pssm-ID: 443052 [Multi-domain]  Cd Length: 353  Bit Score: 511.57  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054819401  20 LELAAVTKRFGAFVAVDDLTLTVPSGSFFALLGPSGCGKTTTLRMVAGLEQPTDGTISIDGRDVTGTRAHRRPVNTVFQS 99
Cdd:COG3842     6 LELENVSKRYGDVTALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRILLDGRDVTGLPPEKRNVGMVFQD 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054819401 100 YALFPHLTVAENVAFGLRRRR--EADVEARVAEGLALVELGHLADRRPALLSGGQQQRVALARALVNRPALLLLDEPLGA 177
Cdd:COG3842    86 YALFPHLTVAENVAFGLRMRGvpKAEIRARVAELLELVGLEGLADRYPHQLSGGQQQRVALARALAPEPRVLLLDEPLSA 165

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054819401 178 LDLKLRRQMQLELKRIQTEVGLTFVHVTHDQEEAMTMADTVAVMNRGRIEQMGPPADLYEHPRTTFVANFLGRSNLVPGT 257
Cdd:COG3842   166 LDAKLREEMREELRRLQRELGITFIYVTHDQEEALALADRIAVMNDGRIEQVGTPEEIYERPATRFVADFIGEANLLPGT 245

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054819401 258 VVERLDGdllGVDVGGARVRVPASRAVRDTGDVLVGARPEKVRLladgeEPAPDENVVgPGTVTDVSFTGVSTQYEVRVP 337
Cdd:COG3842   246 VLGDEGG---GVRTGGRTLEVPADAGLAAGGPVTVAIRPEDIRL-----SPEGPENGL-PGTVEDVVFLGSHVRYRVRLG 316

                         330       340       350
                  ....*....|....*....|....*....|.
gi 1054819401 338 GLGVFGVFAQNlSGRAGAALGDQVRLAWAVD 368
Cdd:COG3842   317 DGQELVVRVPN-RAALPLEPGDRVGLSWDPE 346
ABC_PotA_N cd03300
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ...
 20-249 6.66e-141

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: 400.07  E-value: 6.66e-141
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054819401  20 LELAAVTKRFGAFVAVDDLTLTVPSGSFFALLGPSGCGKTTTLRMVAGLEQPTDGTISIDGRDVTGTRAHRRPVNTVFQS 99
Cdd:cd03300     1 IELENVSKFYGGFVALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGKDITNLPPHKRPVNTVFQN 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054819401 100 YALFPHLTVAENVAFGLRRRR--EADVEARVAEGLALVELGHLADRRPALLSGGQQQRVALARALVNRPALLLLDEPLGA 177
Cdd:cd03300    81 YALFPHLTVFENIAFGLRLKKlpKAEIKERVAEALDLVQLEGYANRKPSQLSGGQQQRVAIARALVNEPKVLLLDEPLGA 160

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1054819401 178 LDLKLRRQMQLELKRIQTEVGLTFVHVTHDQEEAMTMADTVAVMNRGRIEQMGPPADLYEHPRTTFVANFLG 249
Cdd:cd03300   161 LDLKLRKDMQLELKRLQKELGITFVFVTHDQEEALTMSDRIAVMNKGKIQQIGTPEEIYEEPANRFVADFIG 232
potA PRK09452
spermidine/putrescine ABC transporter ATP-binding protein PotA;
20-311 9.85e-139

spermidine/putrescine ABC transporter ATP-binding protein PotA;


Pssm-ID: 236523 [Multi-domain]  Cd Length: 375  Bit Score: 400.09  E-value: 9.85e-139
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054819401  20 LELAAVTKRFGAFVAVDDLTLTVPSGSFFALLGPSGCGKTTTLRMVAGLEQPTDGTISIDGRDVTGTRAHRRPVNTVFQS 99
Cdd:PRK09452   15 VELRGISKSFDGKEVISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLDGQDITHVPAENRHVNTVFQS 94

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054819401 100 YALFPHLTVAENVAFGLR--RRREADVEARVAEGLALVELGHLADRRPALLSGGQQQRVALARALVNRPALLLLDEPLGA 177
Cdd:PRK09452   95 YALFPHMTVFENVAFGLRmqKTPAAEITPRVMEALRMVQLEEFAQRKPHQLSGGQQQRVAIARAVVNKPKVLLLDESLSA 174

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054819401 178 LDLKLRRQMQLELKRIQTEVGLTFVHVTHDQEEAMTMADTVAVMNRGRIEQMGPPADLYEHPRTTFVANFLGRSNLVPGT 257
Cdd:PRK09452  175 LDYKLRKQMQNELKALQRKLGITFVFVTHDQEEALTMSDRIVVMRDGRIEQDGTPREIYEEPKNLFVARFIGEINIFDAT 254

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1054819401 258 VVERLDGDLLGVDVGGARVRVPASRAVRdTGDVL-VGARPEKVRLLADGEEPAPD 311
Cdd:PRK09452  255 VIERLDEQRVRANVEGRECNIYVNFAVE-PGQKLhVLLRPEDLRVEEINDDEHAE 308
potA TIGR01187
spermidine/putrescine ABC transporter ATP-binding subunit; This model describes spermidine ...
 50-370 1.30e-119

spermidine/putrescine ABC transporter ATP-binding subunit; This model describes spermidine/putrescine ABC transporter, ATP binding subunit in bacteria and its equivalents in archaea. This transport system belong to the larger ATP-Binding Cassette (ABC) transporter superfamily. The characteristic feature of these transporter is the obligatory coupling of ATP hydrolysis to substrate translocation. The minimal configuration of bacterial ABC transport system: an ATPase or ATP binding subunit; An integral membrane protein; a hydrophilic polypetpide, which likely functions as substrate binding protein. Polyamines like spermidine and putrescine play vital role in cell proliferation, differentiation, and ion homeostasis. The concentration of polyamines within the cell are regulated by biosynthesis, degradation and transport (uptake and efflux included). [Transport and binding proteins, Amino acids, peptides and amines]


Pssm-ID: 162242 [Multi-domain]  Cd Length: 325  Bit Score: 349.87  E-value: 1.30e-119
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054819401  50 LLGPSGCGKTTTLRMVAGLEQPTDGTISIDGRDVTGTRAHRRPVNTVFQSYALFPHLTVAENVAFGLRRRRE--ADVEAR 127
Cdd:TIGR01187   1 LLGPSGCGKTTLLRLLAGFEQPDSGSIMLDGEDVTNVPPHLRHINMVFQSYALFPHMTVEENVAFGLKMRKVprAEIKPR 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054819401 128 VAEGLALVELGHLADRRPALLSGGQQQRVALARALVNRPALLLLDEPLGALDLKLRRQMQLELKRIQTEVGLTFVHVTHD 207
Cdd:TIGR01187  81 VLEALRLVQLEEFADRKPHQLSGGQQQRVALARALVFKPKILLLDEPLSALDKKLRDQMQLELKTIQEQLGITFVFVTHD 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054819401 208 QEEAMTMADTVAVMNRGRIEQMGPPADLYEHPRTTFVANFLGRSNLVPGTVVERLDGDLLGVDVGGARVRVPASRAVRDT 287
Cdd:TIGR01187 161 QEEAMTMSDRIAIMRKGKIAQIGTPEEIYEEPANLFVARFIGEINVFEATVIERKSEQVVLAGVEGRRCDIYTDVPVEKD 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054819401 288 GDVLVGARPEKVRLladgEEPAPDENVVG-PGTVTDVSFTGVSTQYEVRVPGLGVFGVFAQ-NLSGRAGA-ALGDQVRLA 364
Cdd:TIGR01187 241 QPLHVVLRPEKIVI----EEEDEANSSNAiIGHVIDITYLGMTLEVHVRLETGQKVLVSEFfNEDDPHMSpSIGDRVGLT 316


                  ....*.
gi 1054819401 365 WAVDFT 370
Cdd:TIGR01187 317 WHPGSE 322
tungstate_WtpC NF040840
tungstate ABC transporter ATP-binding protein WtpC;
20-301 3.29e-90

tungstate ABC transporter ATP-binding protein WtpC;


Pssm-ID: 468779 [Multi-domain]  Cd Length: 347  Bit Score: 275.42  E-value: 3.29e-90
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054819401  20 LELAAVTKRFGAFvAVDDLTLTVPSGSFFALLGPSGCGKTTTLRMVAGLEQPTDGTISIDGRDVTGTRAHRRPVNTVFQS 99
Cdd:NF040840    2 IRIENLSKDWKEF-KLRDISLEVKEGEYFIILGPSGAGKTVLLELIAGIWPPDSGKIYLDGKDITNLPPEKRGIAYVYQN 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054819401 100 YALFPHLTVAENVAFGLRRRR--EADVEARVAEGLALVELGHLADRRPALLSGGQQQRVALARALVNRPALLLLDEPLGA 177
Cdd:NF040840   81 YMLFPHKTVFENIAFGLKLRKvpKEEIERKVKEIMELLGISHLLHRKPRTLSGGEQQRVALARALIIEPKLLLLDEPLSA 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054819401 178 LDLKLRRQMQLELKRIQTEVGLTFVHVTHDQEEAMTMADTVAVMNRGRIEQMGPPADLYEHPRTTFVANFLGRSNLVPGT 257
Cdd:NF040840  161 LDVQTRDELIREMKRWHREFGFTAIHVTHNFEEALSLADRVGIMLNGRLSQVGDVREVFRRPKNEFVARFVGFENIIEGV 240

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....
gi 1054819401 258 VveRLDGDLLGVDVGGARVRVPASRavrdTGDVLVGARPEKVRL 301
Cdd:NF040840  241 A--EKGGEGTILDTGNIKIELPEEK----KGKVRIGIRPEDITI 278
ABC_tran pfam00005
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ...
 35-174 2.72e-47

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: 158.19  E-value: 2.72e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054819401  35 VDDLTLTVPSGSFFALLGPSGCGKTTTLRMVAGLEQPTDGTISIDGRDVTGT--RAHRRPVNTVFQSYALFPHLTVAENV 112
Cdd:pfam00005   1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDLTDDerKSLRKEIGYVFQDPQLFPRLTVRENL 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1054819401 113 AFGLR--RRREADVEARVAEGLALVELGHLADRR----PALLSGGQQQRVALARALVNRPALLLLDEP 174
Cdd:pfam00005  81 RLGLLlkGLSKREKDARAEEALEKLGLGDLADRPvgerPGTLSGGQRQRVAIARALLTKPKLLLLDEP 148
ABC_ATP_DarD NF038007
darobactin export ABC transporter ATP-binding protein;
34-226 1.87e-45

darobactin export ABC transporter ATP-binding protein;


Pssm-ID: 411600 [Multi-domain]  Cd Length: 218  Bit Score: 155.65  E-value: 1.87e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054819401  34 AVDDLTLTVPSGSFFALLGPSGCGKTTTLRMVAGLEQPTDGTISIDGRDVTGTR------AHRRPVNTVFQSYALFPHLT 107
Cdd:NF038007   20 VLNHLNFSVEKGDFVSIMGPSGSGKSTLLNIIGMFDSLDSGSLTLAGKEVTNLSysqkiiLRRELIGYIFQSFNLIPHLS 99

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054819401 108 VAENVAFGLRRRREADVE--ARVAEGLALVELGHLADRRPALLSGGQQQRVALARALVNRPALLLLDEPLGALDLKLRRQ 185
Cdd:NF038007  100 IFDNVALPLKYRGVAKKEriERVNQVLNLFGIDNRRNHKPMQLSGGQQQRVAIARAMVSNPALLLADEPTGNLDSKNARA 179

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 1054819401 186 MQLELKRIQtEVGLTFVHVTHdQEEAMTMADTVAVMNRGRI 226
Cdd:NF038007  180 VLQQLKYIN-QKGTTIIMVTH-SDEASTYGNRIINMKDGKL 218
AztA NF040873
zinc ABC transporter ATP-binding protein AztA;
28-212 2.03e-30

zinc ABC transporter ATP-binding protein AztA;


Pssm-ID: 468810 [Multi-domain]  Cd Length: 191  Bit Score: 115.02  E-value: 2.03e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054819401  28 RFGAFVAVDDLTLTVPSGSFFALLGPSGCGKTTTLRMVAGLEQPTDGTIsidgrdvtgTRAHRRPVNTVFQSYAL---FP 104
Cdd:NF040873    1 GYGGRPVLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTV---------RRAGGARVAYVPQRSEVpdsLP 71

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054819401 105 hLTVAENVAFGLRRRR------EADVEARVAEGLALVELGHLADRRPALLSGGQQQRVALARALVNRPALLLLDEPLGAL 178
Cdd:NF040873   72 -LTVRDLVAMGRWARRglwrrlTRDDRAAVDDALERVGLADLAGRQLGELSGGQRQRALLAQGLAQEADLLLLDEPTTGL 150

                         170       180       190
                  ....*....|....*....|....*....|....
gi 1054819401 179 DLKLRRQMQLELKRIQTEvGLTFVHVTHDQEEAM 212
Cdd:NF040873  151 DAESRERIIALLAEEHAR-GATVVVVTHDLELVR 183
ABC2_perm_RbbA NF033858
ribosome-associated ATPase/putative transporter RbbA;
26-235 3.12e-30

ribosome-associated ATPase/putative transporter RbbA;


Pssm-ID: 468210 [Multi-domain]  Cd Length: 907  Bit Score: 122.93  E-value: 3.12e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054819401  26 TKRFGAFVAVDDLTLTVPSGSFFALLGPSGCGKTTTLRMVAGLEQPTDGTISIDGRDVT-GTRAHRRPVNTVFQSYALFP 104
Cdd:NF033858  273 TMRFGDFTAVDHVSFRIRRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGEAWLFGQPVDaGDIATRRRVGYMSQAFSLYG 352

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054819401 105 HLTVAENVA-----FGLrrrREADVEARVAEGLALVELGHLADRRPALLSGGQQQRVALARALVNRPALLLLDEPLGALD 179
Cdd:NF033858  353 ELTVRQNLElharlFHL---PAAEIAARVAEMLERFDLADVADALPDSLPLGIRQRLSLAVAVIHKPELLILDEPTSGVD 429

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1054819401 180 LKLR----RQMqLELKRiqtEVGLT-FVHvTHDQEEAMTmADTVAVMNRGRIEQMGPPADL 235
Cdd:NF033858  430 PVARdmfwRLL-IELSR---EDGVTiFIS-THFMNEAER-CDRISLMHAGRVLASDTPAAL 484
ABC2_perm_RbbA NF033858
ribosome-associated ATPase/putative transporter RbbA;
21-245 7.20e-24

ribosome-associated ATPase/putative transporter RbbA;


Pssm-ID: 468210 [Multi-domain]  Cd Length: 907  Bit Score: 103.67  E-value: 7.20e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054819401  21 ELAAVTKRFGAFVAVDDLTLTVPSGSFFALLGPSGCGKTTTLRMVAGLEQPTDGTISIDGRDVtGTRAHRRPV------- 93
Cdd:NF033858    3 RLEGVSHRYGKTVALDDVSLDIPAGCMVGLIGPDGVGKSSLLSLIAGARKIQQGRVEVLGGDM-ADARHRRAVcpriaym 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054819401  94 ------NtvfqsyaLFPHLTVAENVAF-----GLRRrreADVEARVAEGLALVELGHLADRRPALLSGGQQQRVALARAL 162
Cdd:NF033858   82 pqglgkN-------LYPTLSVFENLDFfgrlfGQDA---AERRRRIDELLRATGLAPFADRPAGKLSGGMKQKLGLCCAL 151

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054819401 163 VNRPALLLLDEPLGALDLKLRRQM-QLeLKRIQTE-VGLTFVHVTHDQEEAMTMaDTVAVMNRGRIEQMGPPADLYEHPR 240
Cdd:NF033858  152 IHDPDLLILDEPTTGVDPLSRRQFwEL-IDRIRAErPGMSVLVATAYMEEAERF-DWLVAMDAGRVLATGTPAELLARTG 229

                         250
                  ....*....|
gi 1054819401 241 TT-----FVA 245
Cdd:NF033858  230 ADtleaaFIA 239
GguA NF040905
sugar ABC transporter ATP-binding protein;
20-229 2.54e-15

sugar ABC transporter ATP-binding protein;


Pssm-ID: 468840 [Multi-domain]  Cd Length: 500  Bit Score: 77.14  E-value: 2.54e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054819401  20 LELAAVTKRFGAFVAVDDLTLTVPSGSFFALLGPSGCGKTTTLRMVAGLeQPT---DGTISIDGRDVT--GTRA-HRRPV 93
Cdd:NF040905    2 LEMRGITKTFPGVKALDDVNLSVREGEIHALCGENGAGKSTLMKVLSGV-YPHgsyEGEILFDGEVCRfkDIRDsEALGI 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054819401  94 NTVFQSYALFPHLTVAENV-------AFGLRRRREADVEARvaEGLALVELGHLADRRPALLSGGQQQRVALARALVNRP 166
Cdd:NF040905   81 VIIHQELALIPYLSIAENIflgneraKRGVIDWNETNRRAR--ELLAKVGLDESPDTLVTDIGVGKQQLVEIAKALSKDV 158

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1054819401 167 ALLLLDEPLGALD-------LKLrrqmQLELKriqtEVGLTFVHVTHDQEEAMTMADTVAVMNRGR-IEQM 229
Cdd:NF040905  159 KLLILDEPTAALNeedsaalLDL----LLELK----AQGITSIIISHKLNEIRRVADSITVLRDGRtIETL 221
40850658_otr NF000106
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
20-226 8.48e-15

oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;


Pssm-ID: 411078 [Multi-domain]  Cd Length: 351  Bit Score: 74.77  E-value: 8.48e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054819401  20 LELAAVTKRFGAFVAVDDLTLTVPSGSFFALLGPSGCGKTTTlRMVAGLEQPTDG-------TISIDGRDVTGTRAHRRP 92
Cdd:NF000106   14 VEVRGLVKHFGEVKAVDGVDLDVREGTVLGVLGP*GAA**RG-ALPAHV*GPDAGrrpwrf*TWCANRRALRRTIG*HRP 92

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054819401  93 VNT-VFQSYALFPHLTVAENVaFGLRRRreaDVEARVAEGLALVELGHLADRRPALLSGGQQQRVALARALVNRPALLLL 171
Cdd:NF000106   93 VR*gRRESFSGRENLYMIGR*-LDLSRK---DARARADELLERFSLTEAAGRAAAKYSGGMRRRLDLAASMIGRPAVLYL 168

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1054819401 172 DEPLGALDLKLRRQMQLELKRIQTEvGLTFVHVTHDQEEAMTMADTVAVMNRGRI 226
Cdd:NF000106  169 DEPTTGLDPRTRNEVWDEVRSMVRD-GATVLLTTQYMEEAEQLAHELTVIDRGRV 222
AAA smart00382
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ...
 44-215 8.28e-10

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: 57.00  E-value: 8.28e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054819401   44 SGSFFALLGPSGCGKTTTLRMVAGLEQPTDGT-ISIDGRDVTgtrahrrpvntvfqsyalfphltvaenvafglrrrrea 122
Cdd:smart00382   1 PGEVILIVGPPGSGKTTLARALARELGPPGGGvIYIDGEDIL-------------------------------------- 42

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054819401  123 dvearvaEGLALVELGHLADRRPALLSGGQQQRVALARALVNRPALLLLDEPLGALDLKLRRQMQLE-----LKRIQTEV 197
Cdd:smart00382  43 -------EEVLDQLLLIIVGGKKASGSGELRLRLALALARKLKPDVLILDEITSLLDAEQEALLLLLeelrlLLLLKSEK 115

                          170
                   ....*....|....*...
gi 1054819401  198 GLTFVHVTHDQEEAMTMA 215
Cdd:smart00382 116 NLTVILTTNDEKDLGPAL 133
GguA NF040905
sugar ABC transporter ATP-binding protein;
148-174 3.44e-03

sugar ABC transporter ATP-binding protein;


Pssm-ID: 468840 [Multi-domain]  Cd Length: 500  Bit Score: 39.39  E-value: 3.44e-03
                          10        20
                  ....*....|....*....|....*..
gi 1054819401 148 LSGGQQQRVALARALVNRPALLLLDEP 174
Cdd:NF040905  405 LSGGNQQKVVLSKWLFTDPDVLILDEP 431
 
Name Accession Description Interval E-value
PotA COG3842
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ...
 20-368 0e+00

ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];


Pssm-ID: 443052 [Multi-domain]  Cd Length: 353  Bit Score: 511.57  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054819401  20 LELAAVTKRFGAFVAVDDLTLTVPSGSFFALLGPSGCGKTTTLRMVAGLEQPTDGTISIDGRDVTGTRAHRRPVNTVFQS 99
Cdd:COG3842     6 LELENVSKRYGDVTALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRILLDGRDVTGLPPEKRNVGMVFQD 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054819401 100 YALFPHLTVAENVAFGLRRRR--EADVEARVAEGLALVELGHLADRRPALLSGGQQQRVALARALVNRPALLLLDEPLGA 177
Cdd:COG3842    86 YALFPHLTVAENVAFGLRMRGvpKAEIRARVAELLELVGLEGLADRYPHQLSGGQQQRVALARALAPEPRVLLLDEPLSA 165

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054819401 178 LDLKLRRQMQLELKRIQTEVGLTFVHVTHDQEEAMTMADTVAVMNRGRIEQMGPPADLYEHPRTTFVANFLGRSNLVPGT 257
Cdd:COG3842   166 LDAKLREEMREELRRLQRELGITFIYVTHDQEEALALADRIAVMNDGRIEQVGTPEEIYERPATRFVADFIGEANLLPGT 245

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054819401 258 VVERLDGdllGVDVGGARVRVPASRAVRDTGDVLVGARPEKVRLladgeEPAPDENVVgPGTVTDVSFTGVSTQYEVRVP 337
Cdd:COG3842   246 VLGDEGG---GVRTGGRTLEVPADAGLAAGGPVTVAIRPEDIRL-----SPEGPENGL-PGTVEDVVFLGSHVRYRVRLG 316

                         330       340       350
                  ....*....|....*....|....*....|.
gi 1054819401 338 GLGVFGVFAQNlSGRAGAALGDQVRLAWAVD 368
Cdd:COG3842   317 DGQELVVRVPN-RAALPLEPGDRVGLSWDPE 346
MalK COG3839
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ...
 20-368 1.86e-152

ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];


Pssm-ID: 443050 [Multi-domain]  Cd Length: 352  Bit Score: 434.12  E-value: 1.86e-152
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054819401  20 LELAAVTKRFGAFVAVDDLTLTVPSGSFFALLGPSGCGKTTTLRMVAGLEQPTDGTISIDGRDVTGTRAHRRPVNTVFQS 99
Cdd:COG3839     4 LELENVSKSYGGVEALKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAGLEDPTSGEILIGGRDVTDLPPKDRNIAMVFQS 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054819401 100 YALFPHLTVAENVAFGLRRRR--EADVEARVAEGLALVELGHLADRRPALLSGGQQQRVALARALVNRPALLLLDEPLGA 177
Cdd:COG3839    84 YALYPHMTVYENIAFPLKLRKvpKAEIDRRVREAAELLGLEDLLDRKPKQLSGGQRQRVALGRALVREPKVFLLDEPLSN 163

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054819401 178 LDLKLRRQMQLELKRIQTEVGLTFVHVTHDQEEAMTMADTVAVMNRGRIEQMGPPADLYEHPRTTFVANFLGRS--NLVP 255
Cdd:COG3839   164 LDAKLRVEMRAEIKRLHRRLGTTTIYVTHDQVEAMTLADRIAVMNDGRIQQVGTPEELYDRPANLFVAGFIGSPpmNLLP 243

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054819401 256 GTVVERldgdllGVDVGGARVRVPASRAVRDTGDVLVGARPEKVRLladgeepAPDENVVGPGTVTDVSFTGVSTQYEVR 335
Cdd:COG3839   244 GTVEGG------GVRLGGVRLPLPAALAAAAGGEVTLGIRPEHLRL-------ADEGDGGLEATVEVVEPLGSETLVHVR 310

                         330       340       350
                  ....*....|....*....|....*....|...
gi 1054819401 336 VPGLGVFGVfaqnLSGRAGAALGDQVRLAWAVD 368
Cdd:COG3839   311 LGGQELVAR----VPGDTRLRPGDTVRLAFDPE 339
ABC_PotA_N cd03300
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ...
 20-249 6.66e-141

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: 400.07  E-value: 6.66e-141
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054819401  20 LELAAVTKRFGAFVAVDDLTLTVPSGSFFALLGPSGCGKTTTLRMVAGLEQPTDGTISIDGRDVTGTRAHRRPVNTVFQS 99
Cdd:cd03300     1 IELENVSKFYGGFVALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGKDITNLPPHKRPVNTVFQN 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054819401 100 YALFPHLTVAENVAFGLRRRR--EADVEARVAEGLALVELGHLADRRPALLSGGQQQRVALARALVNRPALLLLDEPLGA 177
Cdd:cd03300    81 YALFPHLTVFENIAFGLRLKKlpKAEIKERVAEALDLVQLEGYANRKPSQLSGGQQQRVAIARALVNEPKVLLLDEPLGA 160

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1054819401 178 LDLKLRRQMQLELKRIQTEVGLTFVHVTHDQEEAMTMADTVAVMNRGRIEQMGPPADLYEHPRTTFVANFLG 249
Cdd:cd03300   161 LDLKLRKDMQLELKRLQKELGITFVFVTHDQEEALTMSDRIAVMNKGKIQQIGTPEEIYEEPANRFVADFIG 232
potA PRK09452
spermidine/putrescine ABC transporter ATP-binding protein PotA;
20-311 9.85e-139

spermidine/putrescine ABC transporter ATP-binding protein PotA;


Pssm-ID: 236523 [Multi-domain]  Cd Length: 375  Bit Score: 400.09  E-value: 9.85e-139
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054819401  20 LELAAVTKRFGAFVAVDDLTLTVPSGSFFALLGPSGCGKTTTLRMVAGLEQPTDGTISIDGRDVTGTRAHRRPVNTVFQS 99
Cdd:PRK09452   15 VELRGISKSFDGKEVISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLDGQDITHVPAENRHVNTVFQS 94

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054819401 100 YALFPHLTVAENVAFGLR--RRREADVEARVAEGLALVELGHLADRRPALLSGGQQQRVALARALVNRPALLLLDEPLGA 177
Cdd:PRK09452   95 YALFPHMTVFENVAFGLRmqKTPAAEITPRVMEALRMVQLEEFAQRKPHQLSGGQQQRVAIARAVVNKPKVLLLDESLSA 174

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054819401 178 LDLKLRRQMQLELKRIQTEVGLTFVHVTHDQEEAMTMADTVAVMNRGRIEQMGPPADLYEHPRTTFVANFLGRSNLVPGT 257
Cdd:PRK09452  175 LDYKLRKQMQNELKALQRKLGITFVFVTHDQEEALTMSDRIVVMRDGRIEQDGTPREIYEEPKNLFVARFIGEINIFDAT 254

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1054819401 258 VVERLDGDLLGVDVGGARVRVPASRAVRdTGDVL-VGARPEKVRLLADGEEPAPD 311
Cdd:PRK09452  255 VIERLDEQRVRANVEGRECNIYVNFAVE-PGQKLhVLLRPEDLRVEEINDDEHAE 308
CysA COG1118
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ...
 20-365 1.92e-129

ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];


Pssm-ID: 440735 [Multi-domain]  Cd Length: 348  Bit Score: 375.64  E-value: 1.92e-129
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054819401  20 LELAAVTKRFGAFVAVDDLTLTVPSGSFFALLGPSGCGKTTTLRMVAGLEQPTDGTISIDGRDV-TGTRAHRRPVNTVFQ 98
Cdd:COG1118     3 IEVRNISKRFGSFTLLDDVSLEIASGELVALLGPSGSGKTTLLRIIAGLETPDSGRIVLNGRDLfTNLPPRERRVGFVFQ 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054819401  99 SYALFPHLTVAENVAFGLRRRR--EADVEARVAEGLALVELGHLADRRPALLSGGQQQRVALARALVNRPALLLLDEPLG 176
Cdd:COG1118    83 HYALFPHMTVAENIAFGLRVRPpsKAEIRARVEELLELVQLEGLADRYPSQLSGGQRQRVALARALAVEPEVLLLDEPFG 162

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054819401 177 ALDLKLRRQMQLELKRIQTEVGLTFVHVTHDQEEAMTMADTVAVMNRGRIEQMGPPADLYEHPRTTFVANFLGRSNLVPG 256
Cdd:COG1118   163 ALDAKVRKELRRWLRRLHDELGGTTVFVTHDQEEALELADRVVVMNQGRIEQVGTPDEVYDRPATPFVARFLGCVNVLRG 242

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054819401 257 TVverLDGDLLgvdVGGarVRVPASRAVRDtGDVLVGARPEKVRLLADGEEpapdENVVgPGTVTDVSFTGVSTQYEVRV 336
Cdd:COG1118   243 RV---IGGQLE---ADG--LTLPVAEPLPD-GPAVAGVRPHDIEVSREPEG----ENTF-PATVARVSELGPEVRVELKL 308

                         330       340       350
                  ....*....|....*....|....*....|...
gi 1054819401 337 PGLGVFGVFAQnLSGRAGAAL----GDQVRLAW 365
Cdd:COG1118   309 EDGEGQPLEAE-VTKEAWAELglapGDPVYLRP 340
potA TIGR01187
spermidine/putrescine ABC transporter ATP-binding subunit; This model describes spermidine ...
 50-370 1.30e-119

spermidine/putrescine ABC transporter ATP-binding subunit; This model describes spermidine/putrescine ABC transporter, ATP binding subunit in bacteria and its equivalents in archaea. This transport system belong to the larger ATP-Binding Cassette (ABC) transporter superfamily. The characteristic feature of these transporter is the obligatory coupling of ATP hydrolysis to substrate translocation. The minimal configuration of bacterial ABC transport system: an ATPase or ATP binding subunit; An integral membrane protein; a hydrophilic polypetpide, which likely functions as substrate binding protein. Polyamines like spermidine and putrescine play vital role in cell proliferation, differentiation, and ion homeostasis. The concentration of polyamines within the cell are regulated by biosynthesis, degradation and transport (uptake and efflux included). [Transport and binding proteins, Amino acids, peptides and amines]


Pssm-ID: 162242 [Multi-domain]  Cd Length: 325  Bit Score: 349.87  E-value: 1.30e-119
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054819401  50 LLGPSGCGKTTTLRMVAGLEQPTDGTISIDGRDVTGTRAHRRPVNTVFQSYALFPHLTVAENVAFGLRRRRE--ADVEAR 127
Cdd:TIGR01187   1 LLGPSGCGKTTLLRLLAGFEQPDSGSIMLDGEDVTNVPPHLRHINMVFQSYALFPHMTVEENVAFGLKMRKVprAEIKPR 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054819401 128 VAEGLALVELGHLADRRPALLSGGQQQRVALARALVNRPALLLLDEPLGALDLKLRRQMQLELKRIQTEVGLTFVHVTHD 207
Cdd:TIGR01187  81 VLEALRLVQLEEFADRKPHQLSGGQQQRVALARALVFKPKILLLDEPLSALDKKLRDQMQLELKTIQEQLGITFVFVTHD 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054819401 208 QEEAMTMADTVAVMNRGRIEQMGPPADLYEHPRTTFVANFLGRSNLVPGTVVERLDGDLLGVDVGGARVRVPASRAVRDT 287
Cdd:TIGR01187 161 QEEAMTMSDRIAIMRKGKIAQIGTPEEIYEEPANLFVARFIGEINVFEATVIERKSEQVVLAGVEGRRCDIYTDVPVEKD 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054819401 288 GDVLVGARPEKVRLladgEEPAPDENVVG-PGTVTDVSFTGVSTQYEVRVPGLGVFGVFAQ-NLSGRAGA-ALGDQVRLA 364
Cdd:TIGR01187 241 QPLHVVLRPEKIVI----EEEDEANSSNAiIGHVIDITYLGMTLEVHVRLETGQKVLVSEFfNEDDPHMSpSIGDRVGLT 316


                  ....*.
gi 1054819401 365 WAVDFT 370
Cdd:TIGR01187 317 WHPGSE 322
potG PRK11607
putrescine ABC transporter ATP-binding subunit PotG;
20-368 1.14e-115

putrescine ABC transporter ATP-binding subunit PotG;


Pssm-ID: 183226 [Multi-domain]  Cd Length: 377  Bit Score: 341.82  E-value: 1.14e-115
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054819401  20 LELAAVTKRFGAFVAVDDLTLTVPSGSFFALLGPSGCGKTTTLRMVAGLEQPTDGTISIDGRDVTGTRAHRRPVNTVFQS 99
Cdd:PRK11607   20 LEIRNLTKSFDGQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVDLSHVPPYQRPINMMFQS 99

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054819401 100 YALFPHLTVAENVAFGLRRRR--EADVEARVAEGLALVELGHLADRRPALLSGGQQQRVALARALVNRPALLLLDEPLGA 177
Cdd:PRK11607  100 YALFPHMTVEQNIAFGLKQDKlpKAEIASRVNEMLGLVHMQEFAKRKPHQLSGGQRQRVALARSLAKRPKLLLLDEPMGA 179

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054819401 178 LDLKLRRQMQLELKRIQTEVGLTFVHVTHDQEEAMTMADTVAVMNRGRIEQMGPPADLYEHPRTTFVANFLGRSNLVPGT 257
Cdd:PRK11607  180 LDKKLRDRMQLEVVDILERVGVTCVMVTHDQEEAMTMAGRIAIMNRGKFVQIGEPEEIYEHPTTRYSAEFIGSVNVFEGV 259

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054819401 258 VVERLDgDLLGVDVGGAR--VRVPASRAVRDTGDVLVGARPEKVRLLadgEEPAPDENVVGPGTVTDVSFTGVSTQYEVR 335
Cdd:PRK11607  260 LKERQE-DGLVIDSPGLVhpLKVDADASVVDNVPVHVALRPEKIMLC---EEPPADGCNFAVGEVIHIAYLGDLSIYHVR 335

                         330       340       350
                  ....*....|....*....|....*....|....*
gi 1054819401 336 VPGLGVFGVFAQNLSG-RAGA-ALGDQVRLAWAVD 368
Cdd:PRK11607  336 LKSGQMISAQLQNAHRyRKGLpTWGDEVRLCWEAD 370
fbpC PRK11432
ferric ABC transporter ATP-binding protein;
20-336 2.44e-115

ferric ABC transporter ATP-binding protein;


Pssm-ID: 183133 [Multi-domain]  Cd Length: 351  Bit Score: 339.77  E-value: 2.44e-115
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054819401  20 LELAAVTKRFGAFVAVDDLTLTVPSGSFFALLGPSGCGKTTTLRMVAGLEQPTDGTISIDGRDVTGTRAHRRPVNTVFQS 99
Cdd:PRK11432    7 VVLKNITKRFGSNTVIDNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIFIDGEDVTHRSIQQRDICMVFQS 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054819401 100 YALFPHLTVAENVAFGLR--RRREADVEARVAEGLALVELGHLADRRPALLSGGQQQRVALARALVNRPALLLLDEPLGA 177
Cdd:PRK11432   87 YALFPHMSLGENVGYGLKmlGVPKEERKQRVKEALELVDLAGFEDRYVDQISGGQQQRVALARALILKPKVLLFDEPLSN 166

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054819401 178 LDLKLRRQMQLELKRIQTEVGLTFVHVTHDQEEAMTMADTVAVMNRGRIEQMGPPADLYEHPRTTFVANFLGRSNLVPGT 257
Cdd:PRK11432  167 LDANLRRSMREKIRELQQQFNITSLYVTHDQSEAFAVSDTVIVMNKGKIMQIGSPQELYRQPASRFMASFMGDANIFPAT 246

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054819401 258 vverLDGDLlgVDVGGARVRVPASRAVRDT-GDVLVGARPEKVRLLADGEEPApdenvvgPGTVTDVSFTGvsTQYEVRV 336
Cdd:PRK11432  247 ----LSGDY--VDIYGYRLPRPAAFAFNLPdGECTVGVRPEAITLSEQGEESQ-------RCTIKHVAYMG--PQYEVTV 311
ABC_Carb_Solutes_like cd03259
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ...
 20-230 2.41e-114

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: 332.18  E-value: 2.41e-114
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054819401  20 LELAAVTKRFGAFVAVDDLTLTVPSGSFFALLGPSGCGKTTTLRMVAGLEQPTDGTISIDGRDVTGTRAHRRPVNTVFQS 99
Cdd:cd03259     1 LELKGLSKTYGSVRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDGRDVTGVPPERRNIGMVFQD 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054819401 100 YALFPHLTVAENVAFGLRRRR--EADVEARVAEGLALVELGHLADRRPALLSGGQQQRVALARALVNRPALLLLDEPLGA 177
Cdd:cd03259    81 YALFPHLTVAENIAFGLKLRGvpKAEIRARVRELLELVGLEGLLNRYPHELSGGQQQRVALARALAREPSLLLLDEPLSA 160

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1054819401 178 LDLKLRRQMQLELKRIQTEVGLTFVHVTHDQEEAMTMADTVAVMNRGRIEQMG 230
Cdd:cd03259   161 LDAKLREELREELKELQRELGITTIYVTHDQEEALALADRIAVMNEGRIVQVG 213
PhnT2 TIGR03265
putative 2-aminoethylphosphonate ABC transporter, ATP-binding protein; This ABC transporter ...
 20-364 1.75e-112

putative 2-aminoethylphosphonate ABC transporter, ATP-binding protein; This ABC transporter ATP-binding protein is found in a number of genomes in operon-like contexts strongly suggesting a substrate specificity for 2-aminoethylphosphonate (2-AEP). The characterized PhnSTUV system is absent in the genomes in which this system is found. These genomes encode systems for the catabolism of 2-AEP, making the need for a 2-AEP-specific transporter likely. [Transport and binding proteins, Amino acids, peptides and amines]


Pssm-ID: 274496 [Multi-domain]  Cd Length: 353  Bit Score: 332.77  E-value: 1.75e-112
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054819401  20 LELAAVTKRFGAFVAVDDLTLTVPSGSFFALLGPSGCGKTTTLRMVAGLEQPTDGTISIDGRDVTGTRAHRRPVNTVFQS 99
Cdd:TIGR03265   5 LSIDNIRKRFGAFTALKDISLSVKKGEFVCLLGPSGCGKTTLLRIIAGLERQTAGTIYQGGRDITRLPPQKRDYGIVFQS 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054819401 100 YALFPHLTVAENVAFGL--RRRREADVEARVAEGLALVELGHLADRRPALLSGGQQQRVALARALVNRPALLLLDEPLGA 177
Cdd:TIGR03265  85 YALFPNLTVADNIAYGLknRGMGRAEVAERVAELLDLVGLPGSERKYPGQLSGGQQQRVALARALATSPGLLLLDEPLSA 164

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054819401 178 LDLKLRRQMQLELKRIQTEVGLTFVHVTHDQEEAMTMADTVAVMNRGRIEQMGPPADLYEHPRTTFVANFLGRSNLVPGT 257
Cdd:TIGR03265 165 LDARVREHLRTEIRQLQRRLGVTTIMVTHDQEEALSMADRIVVMNHGVIEQVGTPQEIYRHPATPFVADFVGEVNWLPGT 244

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054819401 258 VverldGDLLGVDVGGARVRVPASRAVRDTGDVLVgARPEKVRLladgeEPAPDENVVGPGTVTDVSFTGVSTQYEVRVP 337
Cdd:TIGR03265 245 R-----GGGSRARVGGLTLACAPGLAQPGASVRLA-VRPEDIRV-----SPAGNAANLLLARVEDMEFLGAFYRLRLRLE 313

                         330       340       350
                  ....*....|....*....|....*....|
gi 1054819401 338 GLG---VFGVFAQNLSGRAGAALGDQVRLA 364
Cdd:TIGR03265 314 GLPgqaLVADVSASEVERLGIRAGQPIWIE 343
ABC_CysA_sulfate_importer cd03296
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ...
 20-249 8.01e-106

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: 311.58  E-value: 8.01e-106
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054819401  20 LELAAVTKRFGAFVAVDDLTLTVPSGSFFALLGPSGCGKTTTLRMVAGLEQPTDGTISIDGRDVTGTRAHRRPVNTVFQS 99
Cdd:cd03296     3 IEVRNVSKRFGDFVALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGGEDATDVPVQERNVGFVFQH 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054819401 100 YALFPHLTVAENVAFGLRRRR------EADVEARVAEGLALVELGHLADRRPALLSGGQQQRVALARALVNRPALLLLDE 173
Cdd:cd03296    83 YALFRHMTVFDNVAFGLRVKPrserppEAEIRAKVHELLKLVQLDWLADRYPAQLSGGQRQRVALARALAVEPKVLLLDE 162

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1054819401 174 PLGALDLKLRRQMQLELKRIQTEVGLTFVHVTHDQEEAMTMADTVAVMNRGRIEQMGPPADLYEHPRTTFVANFLG 249
Cdd:cd03296   163 PFGALDAKVRKELRRWLRRLHDELHVTTVFVTHDQEEALEVADRVVVMNKGRIEQVGTPDEVYDHPASPFVYSFLG 238
ugpC PRK11650
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
20-305 1.38e-103

sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;


Pssm-ID: 236947 [Multi-domain]  Cd Length: 356  Bit Score: 309.85  E-value: 1.38e-103
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054819401  20 LELAAVTKRF-GAFVAVDDLTLTVPSGSFFALLGPSGCGKTTTLRMVAGLEQPTDGTISIDGRDVTGTRAHRRPVNTVFQ 98
Cdd:PRK11650    4 LKLQAVRKSYdGKTQVIKGIDLDVADGEFIVLVGPSGCGKSTLLRMVAGLERITSGEIWIGGRVVNELEPADRDIAMVFQ 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054819401  99 SYALFPHLTVAENVAFGLRRRR--EADVEARVAEGLALVELGHLADRRPALLSGGQQQRVALARALVNRPALLLLDEPLG 176
Cdd:PRK11650   84 NYALYPHMSVRENMAYGLKIRGmpKAEIEERVAEAARILELEPLLDRKPRELSGGQRQRVAMGRAIVREPAVFLFDEPLS 163

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054819401 177 ALDLKLRRQMQLELKRIQTEVGLTFVHVTHDQEEAMTMADTVAVMNRGRIEQMGPPADLYEHPRTTFVANFLGRS--NLV 254
Cdd:PRK11650  164 NLDAKLRVQMRLEIQRLHRRLKTTSLYVTHDQVEAMTLADRVVVMNGGVAEQIGTPVEVYEKPASTFVASFIGSPamNLL 243

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1054819401 255 PGTVveRLDGDLLGVDvGGARVRVPASRAVRDTGDVLVGARPEKVRLLADG 305
Cdd:PRK11650  244 DGRV--SADGAAFELA-GGIALPLGGGYRQYAGRKLTLGIRPEHIALSSAE 291
ABC_MalK_N cd03301
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ...
 20-230 1.39e-103

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: 304.56  E-value: 1.39e-103
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054819401  20 LELAAVTKRFGAFVAVDDLTLTVPSGSFFALLGPSGCGKTTTLRMVAGLEQPTDGTISIDGRDVTGTRAHRRPVNTVFQS 99
Cdd:cd03301     1 VELENVTKRFGNVTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGRDVTDLPPKDRDIAMVFQN 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054819401 100 YALFPHLTVAENVAFGLRRR--READVEARVAEGLALVELGHLADRRPALLSGGQQQRVALARALVNRPALLLLDEPLGA 177
Cdd:cd03301    81 YALYPHMTVYDNIAFGLKLRkvPKDEIDERVREVAELLQIEHLLDRKPKQLSGGQRQRVALGRAIVREPKVFLMDEPLSN 160

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1054819401 178 LDLKLRRQMQLELKRIQTEVGLTFVHVTHDQEEAMTMADTVAVMNRGRIEQMG 230
Cdd:cd03301   161 LDAKLRVQMRAELKRLQQRLGTTTIYVTHDQVEAMTMADRIAVMNDGQIQQIG 213
3a0106s01 TIGR00968
sulfate ABC transporter, ATP-binding protein; [Transport and binding proteins, Anions]
 20-252 2.06e-100

sulfate ABC transporter, ATP-binding protein; [Transport and binding proteins, Anions]


Pssm-ID: 130041 [Multi-domain]  Cd Length: 237  Bit Score: 297.48  E-value: 2.06e-100
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054819401  20 LELAAVTKRFGAFVAVDDLTLTVPSGSFFALLGPSGCGKTTTLRMVAGLEQPTDGTISIDGRDVTGTRAHRRPVNTVFQS 99
Cdd:TIGR00968   1 IEIANISKRFGSFQALDDVNLEVPTGSLVALLGPSGSGKSTLLRIIAGLEQPDSGRIRLNGQDATRVHARDRKIGFVFQH 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054819401 100 YALFPHLTVAENVAFGL--RRRREADVEARVAEGLALVELGHLADRRPALLSGGQQQRVALARALVNRPALLLLDEPLGA 177
Cdd:TIGR00968  81 YALFKHLTVRDNIAFGLeiRKHPKAKIKARVEELLELVQLEGLGDRYPNQLSGGQRQRVALARALAVEPQVLLLDEPFGA 160

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1054819401 178 LDLKLRRQMQLELKRIQTEVGLTFVHVTHDQEEAMTMADTVAVMNRGRIEQMGPPADLYEHPRTTFVANFLGRSN 252
Cdd:TIGR00968 161 LDAKVRKELRSWLRKLHDEVHVTTVFVTHDQEEAMEVADRIVVMSNGKIEQIGSPDEVYDHPANPFVMSFLGEVN 235
OpuBA COG1125
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and ...
 21-251 6.08e-94

ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and metabolism];


Pssm-ID: 440742 [Multi-domain]  Cd Length: 306  Bit Score: 283.52  E-value: 6.08e-94
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054819401  21 ELAAVTKRF-GAFVAVDDLTLTVPSGSFFALLGPSGCGKTTTLRMVAGLEQPTDGTISIDGRDVTGTRAH--RRPVNTVF 97
Cdd:COG1125     3 EFENVTKRYpDGTVAVDDLSLTIPAGEFTVLVGPSGCGKTTTLRMINRLIEPTSGRILIDGEDIRDLDPVelRRRIGYVI 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054819401  98 QSYALFPHLTVAENVAF--GLRRRREADVEARVAEGLALVEL--GHLADRRPALLSGGQQQRVALARALVNRPALLLLDE 173
Cdd:COG1125    83 QQIGLFPHMTVAENIATvpRLLGWDKERIRARVDELLELVGLdpEEYRDRYPHELSGGQQQRVGVARALAADPPILLMDE 162

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1054819401 174 PLGALDLKLRRQMQLELKRIQTEVGLTFVHVTHDQEEAMTMADTVAVMNRGRIEQMGPPADLYEHPRTTFVANFLGRS 251
Cdd:COG1125   163 PFGALDPITREQLQDELLRLQRELGKTIVFVTHDIDEALKLGDRIAVMREGRIVQYDTPEEILANPANDFVADFVGAD 240
PRK10851 PRK10851
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
20-334 8.74e-92

sulfate/thiosulfate ABC transporter ATP-binding protein CysA;


Pssm-ID: 182778 [Multi-domain]  Cd Length: 353  Bit Score: 279.66  E-value: 8.74e-92
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054819401  20 LELAAVTKRFGAFVAVDDLTLTVPSGSFFALLGPSGCGKTTTLRMVAGLEQPTDGTISIDGRDVTGTRAHRRPVNTVFQS 99
Cdd:PRK10851    3 IEIANIKKSFGRTQVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFHGTDVSRLHARDRKVGFVFQH 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054819401 100 YALFPHLTVAENVAFGL----RRRR--EADVEARVAEGLALVELGHLADRRPALLSGGQQQRVALARALVNRPALLLLDE 173
Cdd:PRK10851   83 YALFRHMTVFDNIAFGLtvlpRRERpnAAAIKAKVTQLLEMVQLAHLADRYPAQLSGGQKQRVALARALAVEPQILLLDE 162

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054819401 174 PLGALDLKLRRQMQLELKRIQTEVGLTFVHVTHDQEEAMTMADTVAVMNRGRIEQMGPPADLYEHPRTTFVANFLGRSNl 253
Cdd:PRK10851  163 PFGALDAQVRKELRRWLRQLHEELKFTSVFVTHDQEEAMEVADRVVVMSQGNIEQAGTPDQVWREPATRFVLEFMGEVN- 241

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054819401 254 vpgtvveRLDGDLLGVD--VGGARVRVPASRAVRdtGDVLVGARPEKVRLladGEEPAPDENVvgPGTVTDVSFTGVSTQ 331
Cdd:PRK10851  242 -------RLQGTIRGGQfhVGAHRWPLGYTPAYQ--GPVDLFLRPWEVDI---SRRTSLDSPL--PVQVLEVSPKGHYWQ 307


                  ...
gi 1054819401 332 YEV 334
Cdd:PRK10851  308 LVV 310
tungstate_WtpC NF040840
tungstate ABC transporter ATP-binding protein WtpC;
20-301 3.29e-90

tungstate ABC transporter ATP-binding protein WtpC;


Pssm-ID: 468779 [Multi-domain]  Cd Length: 347  Bit Score: 275.42  E-value: 3.29e-90
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054819401  20 LELAAVTKRFGAFvAVDDLTLTVPSGSFFALLGPSGCGKTTTLRMVAGLEQPTDGTISIDGRDVTGTRAHRRPVNTVFQS 99
Cdd:NF040840    2 IRIENLSKDWKEF-KLRDISLEVKEGEYFIILGPSGAGKTVLLELIAGIWPPDSGKIYLDGKDITNLPPEKRGIAYVYQN 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054819401 100 YALFPHLTVAENVAFGLRRRR--EADVEARVAEGLALVELGHLADRRPALLSGGQQQRVALARALVNRPALLLLDEPLGA 177
Cdd:NF040840   81 YMLFPHKTVFENIAFGLKLRKvpKEEIERKVKEIMELLGISHLLHRKPRTLSGGEQQRVALARALIIEPKLLLLDEPLSA 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054819401 178 LDLKLRRQMQLELKRIQTEVGLTFVHVTHDQEEAMTMADTVAVMNRGRIEQMGPPADLYEHPRTTFVANFLGRSNLVPGT 257
Cdd:NF040840  161 LDVQTRDELIREMKRWHREFGFTAIHVTHNFEEALSLADRVGIMLNGRLSQVGDVREVFRRPKNEFVARFVGFENIIEGV 240

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....
gi 1054819401 258 VveRLDGDLLGVDVGGARVRVPASRavrdTGDVLVGARPEKVRL 301
Cdd:NF040840  241 A--EKGGEGTILDTGNIKIELPEEK----KGKVRIGIRPEDITI 278
TauB COG1116
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ...
 1-226 1.39e-89

ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];


Pssm-ID: 440733 [Multi-domain]  Cd Length: 260  Bit Score: 270.81  E-value: 1.39e-89
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054819401   1 MTTTAPAhpgaasasagaaLELAAVTKRF----GAFVAVDDLTLTVPSGSFFALLGPSGCGKTTTLRMVAGLEQPTDGTI 76
Cdd:COG1116     1 MSAAAPA------------LELRGVSKRFptggGGVTALDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPTSGEV 68

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054819401  77 SIDGRDVTGTRAHRRpvnTVFQSYALFPHLTVAENVAFGLRRRRE--ADVEARVAEGLALVELGHLADRRPALLSGGQQQ 154
Cdd:COG1116    69 LVDGKPVTGPGPDRG---VVFQEPALLPWLTVLDNVALGLELRGVpkAERRERARELLELVGLAGFEDAYPHQLSGGMRQ 145

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1054819401 155 RVALARALVNRPALLLLDEPLGALDLKLRRQMQLELKRIQTEVGLTFVHVTHDQEEAMTMADTVAVMNR--GRI 226
Cdd:COG1116   146 RVAIARALANDPEVLLMDEPFGALDALTRERLQDELLRLWQETGKTVLFVTHDVDEAVFLADRVVVLSArpGRI 219
ABC_ModC_like cd03299
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ...
 20-253 7.96e-86

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: 260.35  E-value: 7.96e-86
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054819401  20 LELAAVTKRFGAFVaVDDLTLTVPSGSFFALLGPSGCGKTTTLRMVAGLEQPTDGTISIDGRDVTGTRAHRRPVNTVFQS 99
Cdd:cd03299     1 LKVENLSKDWKEFK-LKNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNGKDITNLPPEKRDISYVPQN 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054819401 100 YALFPHLTVAENVAFGLRRRRE--ADVEARVAEGLALVELGHLADRRPALLSGGQQQRVALARALVNRPALLLLDEPLGA 177
Cdd:cd03299    80 YALFPHMTVYKNIAYGLKKRKVdkKEIERKVLEIAEMLGIDHLLNRKPETLSGGEQQRVAIARALVVNPKILLLDEPFSA 159

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1054819401 178 LDLKLRRQMQLELKRIQTEVGLTFVHVTHDQEEAMTMADTVAVMNRGRIEQMGPPADLYEHPRTTFVANFLGRSNL 253
Cdd:cd03299   160 LDVRTKEKLREELKKIRKEFGVTVLHVTHDFEEAWALADKVAIMLNGKLIQVGKPEEVFKKPKNEFVAEFLGFNNI 235
ABC_NrtD_SsuB_transporters cd03293
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ...
 20-226 7.19e-85

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: 257.40  E-value: 7.19e-85
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054819401  20 LELAAVTKRFG----AFVAVDDLTLTVPSGSFFALLGPSGCGKTTTLRMVAGLEQPTDGTISIDGRDVTGTRAHRRpvnT 95
Cdd:cd03293     1 LEVRNVSKTYGggggAVTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVDGEPVTGPGPDRG---Y 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054819401  96 VFQSYALFPHLTVAENVAFGLRRRR--EADVEARVAEGLALVELGHLADRRPALLSGGQQQRVALARALVNRPALLLLDE 173
Cdd:cd03293    78 VFQQDALLPWLTVLDNVALGLELQGvpKAEARERAEELLELVGLSGFENAYPHQLSGGMRQRVALARALAVDPDVLLLDE 157

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1054819401 174 PLGALDLKLRRQMQLELKRIQTEVGLTFVHVTHDQEEAMTMADTVAVMNR--GRI 226
Cdd:cd03293   158 PFSALDALTREQLQEELLDIWRETGKTVLLVTHDIDEAVFLADRVVVLSArpGRI 212
PRK11000 PRK11000
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
22-339 4.83e-84

maltose/maltodextrin ABC transporter ATP-binding protein MalK;


Pssm-ID: 182893 [Multi-domain]  Cd Length: 369  Bit Score: 260.35  E-value: 4.83e-84
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054819401  22 LAAVTKRFGAFVAVDDLTLTVPSGSFFALLGPSGCGKTTTLRMVAGLEQPTDGTISIDGRDVTGTRAHRRPVNTVFQSYA 101
Cdd:PRK11000    6 LRNVTKAYGDVVISKDINLDIHEGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLFIGEKRMNDVPPAERGVGMVFQSYA 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054819401 102 LFPHLTVAENVAFGLR--RRREADVEARVAEGLALVELGHLADRRPALLSGGQQQRVALARALVNRPALLLLDEPLGALD 179
Cdd:PRK11000   86 LYPHLSVAENMSFGLKlaGAKKEEINQRVNQVAEVLQLAHLLDRKPKALSGGQRQRVAIGRTLVAEPSVFLLDEPLSNLD 165

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054819401 180 LKLRRQMQLELKRIQTEVGLTFVHVTHDQEEAMTMADTVAVMNRGRIEQMGPPADLYEHPRTTFVANFLG--RSNLVPGT 257
Cdd:PRK11000  166 AALRVQMRIEISRLHKRLGRTMIYVTHDQVEAMTLADKIVVLDAGRVAQVGKPLELYHYPANRFVAGFIGspKMNFLPVK 245

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054819401 258 VVERLDGdllGVDV---GGARVRVPASRAVRDTGDVL-VGARPEkvRLLadgeePAPDENVVGPGTVTDVSFTGVSTQYE 333
Cdd:PRK11000  246 VTATAIE---QVQVelpNRQQVWLPVEGRGVQVGANMsLGIRPE--HLL-----PSDIADVTLEGEVQVVEQLGNETQIH 315


                  ....*.
gi 1054819401 334 VRVPGL 339
Cdd:PRK11000  316 IQIPAI 321
ABC_OpuCA_Osmoprotection cd03295
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ...
 20-253 2.74e-83

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: 254.15  E-value: 2.74e-83
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054819401  20 LELAAVTKRFGA-FVAVDDLTLTVPSGSFFALLGPSGCGKTTTLRMVAGLEQPTDGTISIDGRDVTGTRAH--RRPVNTV 96
Cdd:cd03295     1 IEFENVTKRYGGgKKAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGEDIREQDPVelRRKIGYV 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054819401  97 FQSYALFPHLTVAENVAF--GLRRRREADVEARVAEGLALVEL--GHLADRRPALLSGGQQQRVALARALVNRPALLLLD 172
Cdd:cd03295    81 IQQIGLFPHMTVEENIALvpKLLKWPKEKIRERADELLALVGLdpAEFADRYPHELSGGQQQRVGVARALAADPPLLLMD 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054819401 173 EPLGALDLKLRRQMQLELKRIQTEVGLTFVHVTHDQEEAMTMADTVAVMNRGRIEQMGPPADLYEHPRTTFVANFLGRSN 252
Cdd:cd03295   161 EPFGALDPITRDQLQEEFKRLQQELGKTIVFVTHDIDEAFRLADRIAIMKNGEIVQVGTPDEILRSPANDFVAEFVGADR 240


                  .
gi 1054819401 253 L 253
Cdd:cd03295   241 L 241
ModC COG4148
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ...
 23-283 5.90e-78

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: 244.24  E-value: 5.90e-78
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054819401  23 AAVTKRFGAF-VAVDdltLTVPSGSFFALLGPSGCGKTTTLRMVAGLEQPTDGTISIDGRDVTGTRA------HRRPVNT 95
Cdd:COG4148     5 VDFRLRRGGFtLDVD---FTLPGRGVTALFGPSGSGKTTLLRAIAGLERPDSGRIRLGGEVLQDSARgiflppHRRRIGY 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054819401  96 VFQSYALFPHLTVAENVAFGLRRRREADVEARVAEGLALVELGHLADRRPALLSGGQQQRVALARALVNRPALLLLDEPL 175
Cdd:COG4148    82 VFQEARLFPHLSVRGNLLYGRKRAPRAERRISFDEVVELLGIGHLLDRRPATLSGGERQRVAIGRALLSSPRLLLMDEPL 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054819401 176 GALDLKLRRQMQLELKRIQTEVGLTFVHVTHDQEEAMTMADTVAVMNRGRIEQMGPPADLYEHPRTTFVANFLGRSNLVP 255
Cdd:COG4148   162 AALDLARKAEILPYLERLRDELDIPILYVSHSLDEVARLADHVVLLEQGRVVASGPLAEVLSRPDLLPLAGGEEAGSVLE 241

                         250       260
                  ....*....|....*....|....*....
gi 1054819401 256 GTVVERLDGD-LLGVDVGGARVRVPASRA 283
Cdd:COG4148   242 ATVAAHDPDYgLTRLALGGGRLWVPRLDL 270
ABC_Class3 cd03229
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ...
 20-225 2.17e-75

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: 231.69  E-value: 2.17e-75
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054819401  20 LELAAVTKRFGAFVAVDDLTLTVPSGSFFALLGPSGCGKTTTLRMVAGLEQPTDGTISIDGRDVTG----TRAHRRPVNT 95
Cdd:cd03229     1 LELKNVSKRYGQKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGEDLTDledeLPPLRRRIGM 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054819401  96 VFQSYALFPHLTVAENVAFGLrrrreadvearvaeglalvelghladrrpallSGGQQQRVALARALVNRPALLLLDEPL 175
Cdd:cd03229    81 VFQDFALFPHLTVLENIALGL--------------------------------SGGQQQRVALARALAMDPDVLLLDEPT 128

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 1054819401 176 GALDLKLRRQMQLELKRIQTEVGLTFVHVTHDQEEAMTMADTVAVMNRGR 225
Cdd:cd03229   129 SALDPITRREVRALLKSLQAQLGITVVLVTHDLDEAARLADRVVVLRDGK 178
MlaF COG1127
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ...
 20-248 9.81e-74

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: 229.48  E-value: 9.81e-74
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054819401  20 LELAAVTKRFGAFVAVDDLTLTVPSGSFFALLGPSGCGKTTTLRMVAGLEQPTDGTISIDGRDVTGT-----RAHRRPVN 94
Cdd:COG1127     6 IEVRNLTKSFGDRVVLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEILVDGQDITGLsekelYELRRRIG 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054819401  95 TVFQSYALFPHLTVAENVAFGLRRRR---EADVEARVAEGLALVELGHLADRRPALLSGGQQQRVALARALVNRPALLLL 171
Cdd:COG1127    86 MLFQGGALFDSLTVFENVAFPLREHTdlsEAEIRELVLEKLELVGLPGAADKMPSELSGGMRKRVALARALALDPEILLY 165

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054819401 172 DEPLGALD-LKLRRQMQLeLKRIQTEVGLTFVHVTHDQEEAMTMADTVAVMNRGRIEQMGPPADLY--EHPrttFVANFL 248
Cdd:COG1127   166 DEPTAGLDpITSAVIDEL-IRELRDELGLTSVVVTHDLDSAFAIADRVAVLADGKIIAEGTPEELLasDDP---WVRQFL 241
ThiQ COG3840
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
20-250 9.90e-74

ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];


Pssm-ID: 443051 [Multi-domain]  Cd Length: 232  Bit Score: 229.26  E-value: 9.90e-74
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054819401  20 LELAAVTKRFGAFVAvdDLTLTVPSGSFFALLGPSGCGKTTTLRMVAGLEQPTDGTISIDGRDVTGTRAHRRPVNTVFQS 99
Cdd:COG3840     2 LRLDDLTYRYGDFPL--RFDLTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILWNGQDLTALPPAERPVSMLFQE 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054819401 100 YALFPHLTVAENVAFGLR--RRREADVEARVAEGLALVELGHLADRRPALLSGGQQQRVALARALV-NRPaLLLLDEPLG 176
Cdd:COG3840    80 NNLFPHLTVAQNIGLGLRpgLKLTAEQRAQVEQALERVGLAGLLDRLPGQLSGGQRQRVALARCLVrKRP-ILLLDEPFS 158

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1054819401 177 ALDLKLRRQMQLELKRIQTEVGLTFVHVTHDQEEAMTMADTVAVMNRGRIEQMGPPADLYEHPRTTFVANFLGR 250
Cdd:COG3840   159 ALDPALRQEMLDLVDELCRERGLTVLMVTHDPEDAARIADRVLLVADGRIAADGPTAALLDGEPPPALAAYLGI 232
CcmA COG1131
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
20-235 2.88e-73

ABC-type multidrug transport system, ATPase component [Defense mechanisms];


Pssm-ID: 440746 [Multi-domain]  Cd Length: 236  Bit Score: 228.02  E-value: 2.88e-73
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054819401  20 LELAAVTKRFGAFVAVDDLTLTVPSGSFFALLGPSGCGKTTTLRMVAGLEQPTDGTISIDGRDV-TGTRAHRRPVNTVFQ 98
Cdd:COG1131     1 IEVRGLTKRYGDKTALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRVLGEDVaRDPAEVRRRIGYVPQ 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054819401  99 SYALFPHLTVAENVAF--GLRRRREADVEARVAEGLALVELGHLADRRPALLSGGQQQRVALARALVNRPALLLLDEPLG 176
Cdd:COG1131    81 EPALYPDLTVRENLRFfaRLYGLPRKEARERIDELLELFGLTDAADRKVGTLSGGMKQRLGLALALLHDPELLILDEPTS 160

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1054819401 177 ALDLKLRRQMQLELKRIQTEvGLTFVHVTHDQEEAMTMADTVAVMNRGRIEQMGPPADL 235
Cdd:COG1131   161 GLDPEARRELWELLRELAAE-GKTVLLSTHYLEEAERLCDRVAIIDKGRIVADGTPDEL 218
ABC_Pro_Gly_Betaine cd03294
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ...
 23-247 7.28e-73

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: 228.30  E-value: 7.28e-73
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054819401  23 AAVTKRFGAFVAVDDLTLTVPSGSFFALLGPSGCGKTTTLRMVAGLEQPTDGTISIDGRDVTGTRA------HRRPVNTV 96
Cdd:cd03294    28 EEILKKTGQTVGVNDVSLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGKVLIDGQDIAAMSRkelrelRRKKISMV 107

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054819401  97 FQSYALFPHLTVAENVAFGL--RRRREADVEARVAEGLALVELGHLADRRPALLSGGQQQRVALARALVNRPALLLLDEP 174
Cdd:cd03294   108 FQSFALLPHRTVLENVAFGLevQGVPRAEREERAAEALELVGLEGWEHKYPDELSGGMQQRVGLARALAVDPDILLMDEA 187

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1054819401 175 LGALDLKLRRQMQLELKRIQTEVGLTFVHVTHDQEEAMTMADTVAVMNRGRIEQMGPPADLYEHPRTTFVANF 247
Cdd:cd03294   188 FSALDPLIRREMQDELLRLQAELQKTIVFITHDLDEALRLGDRIAIMKDGRLVQVGTPEEILTNPANDYVREF 260
ABC_ModC_molybdenum_transporter cd03297
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ...
 27-230 1.96e-72

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: 225.25  E-value: 1.96e-72
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054819401  27 KRFGAFVAVDDLTLtvpSGSFFALLGPSGCGKTTTLRMVAGLEQPTDGTISIDGRDVTGTR------AHRRPVNTVFQSY 100
Cdd:cd03297     8 KRLPDFTLKIDFDL---NEEVTGIFGASGAGKSTLLRCIAGLEKPDGGTIVLNGTVLFDSRkkinlpPQQRKIGLVFQQY 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054819401 101 ALFPHLTVAENVAFGLRRRREADVEARVAEGLALVELGHLADRRPALLSGGQQQRVALARALVNRPALLLLDEPLGALDL 180
Cdd:cd03297    85 ALFPHLNVRENLAFGLKRKRNREDRISVDELLDLLGLDHLLNRYPAQLSGGEKQRVALARALAAQPELLLLDEPFSALDR 164

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 1054819401 181 KLRRQMQLELKRIQTEVGLTFVHVTHDQEEAMTMADTVAVMNRGRIEQMG 230
Cdd:cd03297   165 ALRLQLLPELKQIKKNLNIPVIFVTHDLSEAEYLADRIVVMEDGRLQYIG 214
GlnQ COG1126
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ...
 20-250 9.19e-72

ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism];


Pssm-ID: 440743 [Multi-domain]  Cd Length: 239  Bit Score: 224.49  E-value: 9.19e-72
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054819401  20 LELAAVTKRFGAFVAVDDLTLTVPSGSFFALLGPSGCGKTTTLRMVAGLEQPTDGTISIDGRDVTGTRAH----RRPVNT 95
Cdd:COG1126     2 IEIENLHKSFGDLEVLKGISLDVEKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTITVDGEDLTDSKKDinklRRKVGM 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054819401  96 VFQSYALFPHLTVAENVAFGL---RRRREADVEARVAEGLALVELGHLADRRPALLSGGQQQRVALARALVNRPALLLLD 172
Cdd:COG1126    82 VFQQFNLFPHLTVLENVTLAPikvKKMSKAEAEERAMELLERVGLADKADAYPAQLSGGQQQRVAIARALAMEPKVMLFD 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054819401 173 EPLGALD-------LKLRRQMQLElkriqtevGLTFVHVTHDQEEAMTMADTVAVMNRGRIEQMGPPADLYEHPRTTFVA 245
Cdd:COG1126   162 EPTSALDpelvgevLDVMRDLAKE--------GMTMVVVTHEMGFAREVADRVVFMDGGRIVEEGPPEEFFENPQHERTR 233


                  ....*
gi 1054819401 246 NFLGR 250
Cdd:COG1126   234 AFLSK 238
AbcC COG1135
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
20-288 3.67e-71

ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];


Pssm-ID: 440750 [Multi-domain]  Cd Length: 339  Bit Score: 226.11  E-value: 3.67e-71
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054819401  20 LELAAVTKRF----GAFVAVDDLTLTVPSGSFFALLGPSGCGKTTTLRMVAGLEQPTDGTISIDGRDVTG-----TRAHR 90
Cdd:COG1135     2 IELENLSKTFptkgGPVTALDDVSLTIEKGEIFGIIGYSGAGKSTLIRCINLLERPTSGSVLVDGVDLTAlsereLRAAR 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054819401  91 RPVNTVFQSYALFPHLTVAENVAFGLR--RRREADVEARVAEGLALVELGHLADRRPALLSGGQQQRVALARALVNRPAL 168
Cdd:COG1135    82 RKIGMIFQHFNLLSSRTVAENVALPLEiaGVPKAEIRKRVAELLELVGLSDKADAYPSQLSGGQKQRVGIARALANNPKV 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054819401 169 LLLDEPLGALD-------LKLrrqmqleLKRIQTEVGLTFVHVTHDQEEAMTMADTVAVMNRGRIEQMGPPADLYEHPRT 241
Cdd:COG1135   162 LLCDEATSALDpettrsiLDL-------LKDINRELGLTIVLITHEMDVVRRICDRVAVLENGRIVEQGPVLDVFANPQS 234

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1054819401 242 TFVANFLGRS--NLVPGTVVERL-----DGDLLGVDVGGARVRVPA-SRAVRDTG 288
Cdd:COG1135   235 ELTRRFLPTVlnDELPEELLARLreaagGGRLVRLTFVGESADEPLlSELARRFG 289
ProV COG4175
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and ...
 23-247 5.70e-71

ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and metabolism];


Pssm-ID: 443334 [Multi-domain]  Cd Length: 389  Bit Score: 227.29  E-value: 5.70e-71
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054819401  23 AAVTKRFGAFVAVDDLTLTVPSGSFFALLGPSGCGKTTTLRMVAGLEQPTDGTISIDGRDVTG--------TRAHRrpVN 94
Cdd:COG4175    31 DEILEKTGQTVGVNDASFDVEEGEIFVIMGLSGSGKSTLVRCLNRLIEPTAGEVLIDGEDITKlskkelreLRRKK--MS 108

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054819401  95 TVFQSYALFPHLTVAENVAFGL--RRRREADVEARVAEGLALVELGHLADRRPALLSGGQQQRVALARALVNRPALLLLD 172
Cdd:COG4175   109 MVFQHFALLPHRTVLENVAFGLeiQGVPKAERRERAREALELVGLAGWEDSYPDELSGGMQQRVGLARALATDPDILLMD 188

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1054819401 173 EPLGALDLKLRRQMQLELKRIQTEVGLTFVHVTHDQEEAMTMADTVAVMNRGRIEQMGPPADLYEHPRTTFVANF 247
Cdd:COG4175   189 EAFSALDPLIRREMQDELLELQAKLKKTIVFITHDLDEALRLGDRIAIMKDGRIVQIGTPEEILTNPANDYVADF 263
LolD COG1136
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
20-227 8.44e-71

ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 440751 [Multi-domain]  Cd Length: 227  Bit Score: 221.46  E-value: 8.44e-71
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054819401  20 LELAAVTKRFG----AFVAVDDLTLTVPSGSFFALLGPSGCGKTTTLRMVAGLEQPTDGTISIDGRDVTG------TRAH 89
Cdd:COG1136     5 LELRNLTKSYGtgegEVTALRGVSLSIEAGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVLIDGQDISSlserelARLR 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054819401  90 RRPVNTVFQSYALFPHLTVAENVAFGLR--RRREADVEARVAEGLALVELGHLADRRPALLSGGQQQRVALARALVNRPA 167
Cdd:COG1136    85 RRHIGFVFQFFNLLPELTALENVALPLLlaGVSRKERRERARELLERVGLGDRLDHRPSQLSGGQQQRVAIARALVNRPK 164

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1054819401 168 LLLLDEPLGALDLKLRRQ-MQLeLKRIQTEVGLTFVHVTHDqEEAMTMADTVAVMNRGRIE 227
Cdd:COG1136   165 LILADEPTGNLDSKTGEEvLEL-LRELNRELGTTIVMVTHD-PELAARADRVIRLRDGRIV 223
GsiA COG1123
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ...
 20-240 2.35e-70

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: 229.40  E-value: 2.35e-70
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054819401  20 LELAAVTKRF-----GAFVAVDDLTLTVPSGSFFALLGPSGCGKTTTLRMVAGLEQPTDGTISIDGRDVTG-----TRAH 89
Cdd:COG1123   261 LEVRNLSKRYpvrgkGGVRAVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRPTSGSILFDGKDLTKlsrrsLREL 340

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054819401  90 RRPVNTVFQ--SYALFPHLTVAENVAFGLRRRR---EADVEARVAEGLALVELG-HLADRRPALLSGGQQQRVALARALV 163
Cdd:COG1123   341 RRRVQMVFQdpYSSLNPRMTVGDIIAEPLRLHGllsRAERRERVAELLERVGLPpDLADRYPHELSGGQRQRVAIARALA 420

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1054819401 164 NRPALLLLDEPLGALDLKLRRQMQLELKRIQTEVGLTFVHVTHDQEEAMTMADTVAVMNRGRIEQMGPPADLYEHPR 240
Cdd:COG1123   421 LEPKLLILDEPTSALDVSVQAQILNLLRDLQRELGLTYLFISHDLAVVRYIADRVAVMYDGRIVEDGPTEEVFANPQ 497
ABC_MJ0796_LolCDE_FtsE cd03255
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ...
 20-226 5.59e-69

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: 216.59  E-value: 5.59e-69
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054819401  20 LELAAVTKRFGA----FVAVDDLTLTVPSGSFFALLGPSGCGKTTTLRMVAGLEQPTDGTISIDGRDVTG------TRAH 89
Cdd:cd03255     1 IELKNLSKTYGGggekVQALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRVDGTDISKlsekelAAFR 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054819401  90 RRPVNTVFQSYALFPHLTVAENVAFGLR--RRREADVEARVAEGLALVELGHLADRRPALLSGGQQQRVALARALVNRPA 167
Cdd:cd03255    81 RRHIGFVFQSFNLLPDLTALENVELPLLlaGVPKKERRERAEELLERVGLGDRLNHYPSELSGGQQQRVAIARALANDPK 160

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054819401 168 LLLLDEPLGALDLKLRRQ-MQLeLKRIQTEVGLTFVHVTHDQEEAMtMADTVAVMNRGRI 226
Cdd:cd03255   161 IILADEPTGNLDSETGKEvMEL-LRELNKEAGTTIVVVTHDPELAE-YADRIIELRDGKI 218
EcfA2 COG1122
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ...
 20-241 5.65e-67

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: 211.81  E-value: 5.65e-67
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054819401  20 LELAAVTKRF-GAFVAVDDLTLTVPSGSFFALLGPSGCGKTTTLRMVAGLEQPTDGTISIDGRDVT--GTRAHRRPVNTV 96
Cdd:COG1122     1 IELENLSFSYpGGTPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVDGKDITkkNLRELRRKVGLV 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054819401  97 FQS--YALFpHLTVAENVAFGLRRRR--EADVEARVAEGLALVELGHLADRRPALLSGGQQQRVALARALVNRPALLLLD 172
Cdd:COG1122    81 FQNpdDQLF-APTVEEDVAFGPENLGlpREEIRERVEEALELVGLEHLADRPPHELSGGQKQRVAIAGVLAMEPEVLVLD 159

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1054819401 173 EPLGALDLKLRRQMQLELKRIQTEvGLTFVHVTHDQEEAMTMADTVAVMNRGRIEQMGPPADLYEHPRT 241
Cdd:COG1122   160 EPTAGLDPRGRRELLELLKRLNKE-GKTVIIVTHDLDLVAELADRVIVLDDGRIVADGTPREVFSDYEL 227
DppF COG1124
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ...
 20-251 7.32e-67

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: 211.97  E-value: 7.32e-67
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054819401  20 LELAAVTKRFGA----FVAVDDLTLTVPSGSFFALLGPSGCGKTTTLRMVAGLEQPTDGTISIDGRDVTG--TRAHRRPV 93
Cdd:COG1124     2 LEVRNLSVSYGQggrrVPVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVTFDGRPVTRrrRKAFRRRV 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054819401  94 NTVFQSY--ALFPHLTVAENVAFGLRRRREADVEARVAEGLALVELG-HLADRRPALLSGGQQQRVALARALVNRPALLL 170
Cdd:COG1124    82 QMVFQDPyaSLHPRHTVDRILAEPLRIHGLPDREERIAELLEQVGLPpSFLDRYPHQLSGGQRQRVAIARALILEPELLL 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054819401 171 LDEPLGALDLKLRRQMQLELKRIQTEVGLTFVHVTHDQEEAMTMADTVAVMNRGRIEQMGPPADLYEHPRTTFVANFLGR 250
Cdd:COG1124   162 LDEPTSALDVSVQAEILNLLKDLREERGLTYLFVSHDLAVVAHLCDRVAVMQNGRIVEELTVADLLAGPKHPYTRELLAA 241


                  .
gi 1054819401 251 S 251
Cdd:COG1124   242 S 242
ABC_MetN_methionine_transporter cd03258
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ...
 20-240 1.49e-66

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: 210.90  E-value: 1.49e-66
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054819401  20 LELAAVTKRFG----AFVAVDDLTLTVPSGSFFALLGPSGCGKTTTLRMVAGLEQPTDGTISIDGRDVTGT-----RAHR 90
Cdd:cd03258     2 IELKNVSKVFGdtggKVTALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGSVLVDGTDLTLLsgkelRKAR 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054819401  91 RPVNTVFQSYALFPHLTVAENVAFGLR--RRREADVEARVAEGLALVELGHLADRRPALLSGGQQQRVALARALVNRPAL 168
Cdd:cd03258    82 RRIGMIFQHFNLLSSRTVFENVALPLEiaGVPKAEIEERVLELLELVGLEDKADAYPAQLSGGQKQRVGIARALANNPKV 161

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1054819401 169 LLLDEPLGALDLKLRRQMQLELKRIQTEVGLTFVHVTHDQEEAMTMADTVAVMNRGRIEQMGPPADLYEHPR 240
Cdd:cd03258   162 LLCDEATSALDPETTQSILALLRDINRELGLTIVLITHEMEVVKRICDRVAVMEKGEVVEEGTVEEVFANPQ 233
ABC_Org_Solvent_Resistant cd03261
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ...
 20-235 1.98e-64

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: 205.43  E-value: 1.98e-64
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054819401  20 LELAAVTKRFGAFVAVDDLTLTVPSGSFFALLGPSGCGKTTTLRMVAGLEQPTDGTISIDGRDVTG-----TRAHRRPVN 94
Cdd:cd03261     1 IELRGLTKSFGGRTVLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGEDISGlseaeLYRLRRRMG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054819401  95 TVFQSYALFPHLTVAENVAFGLRRRR---EADVEARVAEGLALVELGHLADRRPALLSGGQQQRVALARALVNRPALLLL 171
Cdd:cd03261    81 MLFQSGALFDSLTVFENVAFPLREHTrlsEEEIREIVLEKLEAVGLRGAEDLYPAELSGGMKKRVALARALALDPELLLY 160

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1054819401 172 DEPLGALDLKLRRQMQLELKRIQTEVGLTFVHVTHDQEEAMTMADTVAVMNRGRIEQMGPPADL 235
Cdd:cd03261   161 DEPTAGLDPIASGVIDDLIRSLKKELGLTSIMVTHDLDTAFAIADRIAVLYDGKIVAEGTPEEL 224
LivG COG0411
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ...
 20-240 2.12e-64

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: 206.04  E-value: 2.12e-64
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054819401  20 LELAAVTKRFGAFVAVDDLTLTVPSGSFFALLGPSGCGKTTTLRMVAGLEQPTDGTISIDGRDVTGTRAHRRP----VNT 95
Cdd:COG0411     5 LEVRGLTKRFGGLVAVDDVSLEVERGEIVGLIGPNGAGKTTLFNLITGFYRPTSGRILFDGRDITGLPPHRIArlgiART 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054819401  96 vFQSYALFPHLTVAENVAFGL-----------------RRRREADVEARVAEGLALVELGHLADRRPALLSGGQQQRVAL 158
Cdd:COG0411    85 -FQNPRLFPELTVLENVLVAAharlgrgllaallrlprARREEREARERAEELLERVGLADRADEPAGNLSYGQQRRLEI 163

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054819401 159 ARALVNRPALLLLDEPLGALDLKLRRQMQLELKRIQTEVGLTFVHVTHDQEEAMTMADTVAVMNRGRIEQMGPPADLYEH 238
Cdd:COG0411   164 ARALATEPKLLLLDEPAAGLNPEETEELAELIRRLRDERGITILLIEHDMDLVMGLADRIVVLDFGRVIAEGTPAEVRAD 243


                  ..
gi 1054819401 239 PR 240
Cdd:COG0411   244 PR 245
FtsE COG2884
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
20-226 8.48e-64

Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 442130 [Multi-domain]  Cd Length: 223  Bit Score: 203.36  E-value: 8.48e-64
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054819401  20 LELAAVTKRF-GAFVAVDDLTLTVPSGSFFALLGPSGCGKTTTLRMVAGLEQPTDGTISIDGRDVTGTRA-----HRRPV 93
Cdd:COG2884     2 IRFENVSKRYpGGREALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLVNGQDLSRLKRreipyLRRRI 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054819401  94 NTVFQSYALFPHLTVAENVAFGLR--RRREADVEARVAEGLALVELGHLADRRPALLSGGQQQRVALARALVNRPALLLL 171
Cdd:COG2884    82 GVVFQDFRLLPDRTVYENVALPLRvtGKSRKEIRRRVREVLDLVGLSDKAKALPHELSGGEQQRVAIARALVNRPELLLA 161

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1054819401 172 DEPLGALDLKLRRQ-MQLeLKRIQtEVGLTFVHVTHDQEEAMTMADTVAVMNRGRI 226
Cdd:COG2884   162 DEPTGNLDPETSWEiMEL-LEEIN-RRGTTVLIATHDLELVDRMPKRVLELEDGRL 215
TauB COG4525
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
34-226 2.29e-61

ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];


Pssm-ID: 443596 [Multi-domain]  Cd Length: 262  Bit Score: 198.55  E-value: 2.29e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054819401  34 AVDDLTLTVPSGSFFALLGPSGCGKTTTLRMVAGLEQPTDGTISIDGRDVTGTRAHRrpvNTVFQSYALFPHLTVAENVA 113
Cdd:COG4525    22 ALQDVSLTIESGEFVVALGASGCGKTTLLNLIAGFLAPSSGEITLDGVPVTGPGADR---GVVFQKDALLPWLNVLDNVA 98

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054819401 114 FGLRRRR--EADVEARVAEGLALVELGHLADRRPALLSGGQQQRVALARALVNRPALLLLDEPLGALDLKLRRQMQLELK 191
Cdd:COG4525    99 FGLRLRGvpKAERRARAEELLALVGLADFARRRIWQLSGGMRQRVGIARALAADPRFLLMDEPFGALDALTREQMQELLL 178

                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 1054819401 192 RIQTEVGLTFVHVTHDQEEAMTMADTVAVM--NRGRI 226
Cdd:COG4525   179 DVWQRTGKGVFLITHSVEEALFLATRLVVMspGPGRI 215
PhnC COG3638
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and ...
 20-235 4.02e-61

ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and metabolism];


Pssm-ID: 442855 [Multi-domain]  Cd Length: 249  Bit Score: 197.20  E-value: 4.02e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054819401  20 LELAAVTKRF-GAFVAVDDLTLTVPSGSFFALLGPSGCGKTTTLRMVAGLEQPTDGTISIDGRDVTG-----TRAHRRPV 93
Cdd:COG3638     3 LELRNLSKRYpGGTPALDDVSLEIERGEFVALIGPSGAGKSTLLRCLNGLVEPTSGEILVDGQDVTAlrgraLRRLRRRI 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054819401  94 NTVFQSYALFPHLTVAENVAFG-----------LRRRREADVEaRVAEGLALVELGHLADRRPALLSGGQQQRVALARAL 162
Cdd:COG3638    83 GMIFQQFNLVPRLSVLTNVLAGrlgrtstwrslLGLFPPEDRE-RALEALERVGLADKAYQRADQLSGGQQQRVAIARAL 161

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1054819401 163 VNRPALLLLDEPLGALDLKLRRQ-MQLeLKRIQTEVGLTFVHVTHDQEEAMTMADTVAVMNRGRIEQMGPPADL 235
Cdd:COG3638   162 VQEPKLILADEPVASLDPKTARQvMDL-LRRIAREDGITVVVNLHQVDLARRYADRIIGLRDGRVVFDGPPAEL 234
ABC_Mj1267_LivG_branched cd03219
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ...
 20-240 7.42e-61

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: 196.12  E-value: 7.42e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054819401  20 LELAAVTKRFGAFVAVDDLTLTVPSGSFFALLGPSGCGKTTTLRMVAGLEQPTDGTISIDGRDVTGTRAHRRP---VNTV 96
Cdd:cd03219     1 LEVRGLTKRFGGLVALDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFDGEDITGLPPHEIArlgIGRT 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054819401  97 FQSYALFPHLTVAENVA------------FGLRRRREADVEARVAEGLALVELGHLADRRPALLSGGQQQRVALARALVN 164
Cdd:cd03219    81 FQIPRLFPELTVLENVMvaaqartgsgllLARARREEREARERAEELLERVGLADLADRPAGELSYGQQRRLEIARALAT 160

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1054819401 165 RPALLLLDEPLGALDLKLRRQMQLELKRIQTEvGLTFVHVTHDQEEAMTMADTVAVMNRGRIEQMGPPADLYEHPR 240
Cdd:cd03219   161 DPKLLLLDEPAAGLNPEETEELAELIRELRER-GITVLLVEHDMDVVMSLADRVTVLDQGRVIAEGTPDEVRNNPR 235
ABC_NikE_OppD_transporters cd03257
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ...
 20-226 1.82e-60

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: 195.03  E-value: 1.82e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054819401  20 LELAAVTKRF----GAFVAVDDLTLTVPSGSFFALLGPSGCGKTTTLRMVAGLEQPTDGTISIDGRDVTG-----TRAHR 90
Cdd:cd03257     2 LEVKNLSVSFptggGSVKALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGKDLLKlsrrlRKIRR 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054819401  91 RPVNTVFQSY--ALFPHLTVAENVAFGLRRRREADVEA--RVAEGLALVELG---HLADRRPALLSGGQQQRVALARALV 163
Cdd:cd03257    82 KEIQMVFQDPmsSLNPRMTIGEQIAEPLRIHGKLSKKEarKEAVLLLLVGVGlpeEVLNRYPHELSGGQRQRVAIARALA 161

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1054819401 164 NRPALLLLDEPLGALDLKLRRQMQLELKRIQTEVGLTFVHVTHDQEEAMTMADTVAVMNRGRI 226
Cdd:cd03257   162 LNPKLLIADEPTSALDVSVQAQILDLLKKLQEELGLTLLFITHDLGVVAKIADRVAVMYAGKI 224
ABC_HisP_GlnQ cd03262
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ...
 20-226 1.78e-59

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: 191.97  E-value: 1.78e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054819401  20 LELAAVTKRFGAFVAVDDLTLTVPSGSFFALLGPSGCGKTTTLRMVAGLEQPTDGTISIDGRDVTGTRAH----RRPVNT 95
Cdd:cd03262     1 IEIKNLHKSFGDFHVLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIDGLKLTDDKKNinelRQKVGM 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054819401  96 VFQSYALFPHLTVAENVAFGLRRRR---EADVEARVAEGLALVELGHLADRRPALLSGGQQQRVALARALVNRPALLLLD 172
Cdd:cd03262    81 VFQQFNLFPHLTVLENITLAPIKVKgmsKAEAEERALELLEKVGLADKADAYPAQLSGGQQQRVAIARALAMNPKVMLFD 160

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1054819401 173 EPLGALDLKLRRQMqLELKRIQTEVGLTFVHVTHDQEEAMTMADTVAVMNRGRI 226
Cdd:cd03262   161 EPTSALDPELVGEV-LDVMKDLAEEGMTMVVVTHEMGFAREVADRVIFMDDGRI 213
ABC_cobalt_CbiO_domain1 cd03225
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ...
 30-225 3.70e-59

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: 191.14  E-value: 3.70e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054819401  30 GAFVAVDDLTLTVPSGSFFALLGPSGCGKTTTLRMVAGLEQPTDGTISIDGRDVTGTRAH--RRPVNTVFQsyalFP--- 104
Cdd:cd03225    12 GARPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDLTKLSLKelRRKVGLVFQ----NPddq 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054819401 105 --HLTVAENVAFGLRRR--READVEARVAEGLALVELGHLADRRPALLSGGQQQRVALARALVNRPALLLLDEPLGALDL 180
Cdd:cd03225    88 ffGPTVEEEVAFGLENLglPEEEIEERVEEALELVGLEGLRDRSPFTLSGGQKQRVAIAGVLAMDPDILLLDEPTAGLDP 167

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 1054819401 181 KLRRQMQLELKRIQTEvGLTFVHVTHDQEEAMTMADTVAVMNRGR 225
Cdd:cd03225   168 AGRRELLELLKKLKAE-GKTIIIVTHDLDLLLELADRVIVLEDGK 211
glnQ PRK09493
glutamine ABC transporter ATP-binding protein GlnQ;
20-248 5.74e-59

glutamine ABC transporter ATP-binding protein GlnQ;


Pssm-ID: 181906 [Multi-domain]  Cd Length: 240  Bit Score: 191.46  E-value: 5.74e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054819401  20 LELAAVTKRFGAFVAVDDLTLTVPSGSFFALLGPSGCGKTTTLRMVAGLEQPTDGTISIDGRDVTGTRAH----RRPVNT 95
Cdd:PRK09493    2 IEFKNVSKHFGPTQVLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGLKVNDPKVDerliRQEAGM 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054819401  96 VFQSYALFPHLTVAENVAFGLRRRR---EADVEARVAEGLALVELGHLADRRPALLSGGQQQRVALARALVNRPALLLLD 172
Cdd:PRK09493   82 VFQQFYLFPHLTALENVMFGPLRVRgasKEEAEKQARELLAKVGLAERAHHYPSELSGGQQQRVAIARALAVKPKLMLFD 161

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1054819401 173 EPLGALDLKLRRQMqLELKRIQTEVGLTFVHVTHDQEEAMTMADTVAVMNRGRIEQMGPPADLYEHPRTTFVANFL 248
Cdd:PRK09493  162 EPTSALDPELRHEV-LKVMQDLAEEGMTMVIVTHEIGFAEKVASRLIFIDKGRIAEDGDPQVLIKNPPSQRLQEFL 236
metN PRK11153
DL-methionine transporter ATP-binding subunit; Provisional
 21-241 6.36e-59

DL-methionine transporter ATP-binding subunit; Provisional


Pssm-ID: 236863 [Multi-domain]  Cd Length: 343  Bit Score: 194.63  E-value: 6.36e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054819401  21 ELAAVTKRF----GAFVAVDDLTLTVPSGSFFALLGPSGCGKTTTLRMVAGLEQPTDGTISIDGRDVT-----GTRAHRR 91
Cdd:PRK11153    3 ELKNISKVFpqggRTIHALNNVSLHIPAGEIFGVIGASGAGKSTLIRCINLLERPTSGRVLVDGQDLTalsekELRKARR 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054819401  92 PVNTVFQSYALFPHLTVAENVAFGLR--RRREADVEARVAEGLALVELGHLADRRPALLSGGQQQRVALARALVNRPALL 169
Cdd:PRK11153   83 QIGMIFQHFNLLSSRTVFDNVALPLElaGTPKAEIKARVTELLELVGLSDKADRYPAQLSGGQKQRVAIARALASNPKVL 162

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1054819401 170 LLDEPLGALDLKLRRQ-MQLeLKRIQTEVGLTFVHVTHDQEEAMTMADTVAVMNRGRIEQMGPPADLYEHPRT 241
Cdd:PRK11153  163 LCDEATSALDPATTRSiLEL-LKDINRELGLTIVLITHEMDVVKRICDRVAVIDAGRLVEQGTVSEVFSHPKH 234
modC_ABC TIGR02142
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ...
 27-283 1.09e-58

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: 194.56  E-value: 1.09e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054819401  27 KRFGAFVAvdDLTLTVPSGSFFALLGPSGCGKTTTLRMVAGLEQPTDGTISIDGRDVTGTR------AHRRPVNTVFQSY 100
Cdd:TIGR02142   7 KRLGDFSL--DADFTLPGQGVTAIFGRSGSGKTTLIRLIAGLTRPDEGEIVLNGRTLFDSRkgiflpPEKRRIGYVFQEA 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054819401 101 ALFPHLTVAENVAFGLRRRREADVEARVAEGLALVELGHLADRRPALLSGGQQQRVALARALVNRPALLLLDEPLGALDL 180
Cdd:TIGR02142  85 RLFPHLSVRGNLRYGMKRARPSERRISFERVIELLGIGHLLGRLPGRLSGGEKQRVAIGRALLSSPRLLLMDEPLAALDD 164

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054819401 181 KLRRQMQLELKRIQTEVGLTFVHVTHDQEEAMTMADTVAVMNRGRIEQMGPPADLYEHPRTTFVAnFLGRSNLVPGTVVE 260
Cdd:TIGR02142 165 PRKYEILPYLERLHAEFGIPILYVSHSLQEVLRLADRVVVLEDGRVAAAGPIAEVWASPDLPWLA-REDQGSLIEGVVAE 243

                         250       260
                  ....*....|....*....|....
gi 1054819401 261 RLDGD-LLGVDVGGARVRVPASRA 283
Cdd:TIGR02142 244 HDQHYgLTALRLGGGHLWVPENLG 267
ntrCD TIGR01184
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ...
 35-240 1.08e-57

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: 188.06  E-value: 1.08e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054819401  35 VDDLTLTVPSGSFFALLGPSGCGKTTTLRMVAGLEQPTDGTISIDGRDVTGTRAHRRpvnTVFQSYALFPHLTVAENVAF 114
Cdd:TIGR01184   1 LKGVNLTIQQGEFISLIGHSGCGKSTLLNLISGLAQPTSGGVILEGKQITEPGPDRM---VVFQNYSLLPWLTVRENIAL 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054819401 115 G----LRRRREADVEARVAEGLALVELGHLADRRPALLSGGQQQRVALARALVNRPALLLLDEPLGALDLKLRRQMQLEL 190
Cdd:TIGR01184  78 AvdrvLPDLSKSERRAIVEEHIALVGLTEAADKRPGQLSGGMKQRVAIARALSIRPKVLLLDEPFGALDALTRGNLQEEL 157

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1054819401 191 KRIQTEVGLTFVHVTHDQEEAMTMADTVAVMNRGRIEQMGPPADL-YEHPR 240
Cdd:TIGR01184 158 MQIWEEHRVTVLMVTHDVDEALLLSDRVVMLTNGPAANIGQILEVpFPRPR 208
ABC_PstB_phosphate_transporter cd03260
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ...
 20-232 1.57e-56

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: 184.69  E-value: 1.57e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054819401  20 LELAAVTKRFGAFVAVDDLTLTVPSGSFFALLGPSGCGKTTTLRMVAGL-----EQPTDGTISIDGRDVTGTR----AHR 90
Cdd:cd03260     1 IELRDLNVYYGDKHALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRLndlipGAPDEGEVLLDGKDIYDLDvdvlELR 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054819401  91 RPVNTVFQSYALFPhLTVAENVAFGLR---RRREADVEARVAEGLALVEL-GHLADRRPAL-LSGGQQQRVALARALVNR 165
Cdd:cd03260    81 RRVGMVFQKPNPFP-GSIYDNVAYGLRlhgIKLKEELDERVEEALRKAALwDEVKDRLHALgLSGGQQQRLCLARALANE 159

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1054819401 166 PALLLLDEPLGALDLKLRRQMQLELKRIQTEVglTFVHVTHDQEEAMTMADTVAVMNRGRIEQMGPP 232
Cdd:cd03260   160 PEVLLLDEPTSALDPISTAKIEELIAELKKEY--TIVIVTHNMQQAARVADRTAFLLNGRLVEFGPT 224
FepC COG1120
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ...
 20-235 2.21e-56

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: 185.25  E-value: 2.21e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054819401  20 LELAAVTKRFGAFVAVDDLTLTVPSGSFFALLGPSGCGKTTTLRMVAGLEQPTDGTISIDGRDVTG--TRAHRRPVNTVF 97
Cdd:COG1120     2 LEAENLSVGYGGRPVLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDGRDLASlsRRELARRIAYVP 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054819401  98 QSYALFPHLTVAENVAFG-------LRRRREADvEARVAEGLALVELGHLADRRPALLSGGQQQRVALARALVNRPALLL 170
Cdd:COG1120    82 QEPPAPFGLTVRELVALGryphlglFGRPSAED-REAVEEALERTGLEHLADRPVDELSGGERQRVLIARALAQEPPLLL 160

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1054819401 171 LDEPLGALDlkLRRQMQL--ELKRIQTEVGLTFVHVTHDQEEAMTMADTVAVMNRGRIEQMGPPADL 235
Cdd:COG1120   161 LDEPTSHLD--LAHQLEVleLLRRLARERGRTVVMVLHDLNLAARYADRLVLLKDGRIVAQGPPEEV 225
ABC_DR_subfamily_A cd03230
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ...
 20-226 2.59e-56

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: 182.21  E-value: 2.59e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054819401  20 LELAAVTKRFGAFVAVDDLTLTVPSGSFFALLGPSGCGKTTTLRMVAGLEQPTDGTISIDGRDV-TGTRAHRRPVNTVFQ 98
Cdd:cd03230     1 IEVRNLSKRYGKKTALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVLGKDIkKEPEEVKRRIGYLPE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054819401  99 SYALFPHLTVAENVafglrrrreadvearvaeglalvelghladrrpaLLSGGQQQRVALARALVNRPALLLLDEPLGAL 178
Cdd:cd03230    81 EPSLYENLTVRENL----------------------------------KLSGGMKQRLALAQALLHDPELLILDEPTSGL 126

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 1054819401 179 DLKLRRQMQLELKRIQTEvGLTFVHVTHDQEEAMTMADTVAVMNRGRI 226
Cdd:cd03230   127 DPESRREFWELLRELKKE-GKTILLSSHILEEAERLCDRVAILNNGRI 173
NatA COG4555
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ...
 20-237 3.59e-56

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: 184.29  E-value: 3.59e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054819401  20 LELAAVTKRFGAFVAVDDLTLTVPSGSFFALLGPSGCGKTTTLRMVAGLEQPTDGTISIDGRDVT-GTRAHRRPVNTVFQ 98
Cdd:COG4555     2 IEVENLSKKYGKVPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIDGEDVRkEPREARRQIGVLPD 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054819401  99 SYALFPHLTVAENVAF--GLRRRREADVEARVAEGLALVELGHLADRRPALLSGGQQQRVALARALVNRPALLLLDEPLG 176
Cdd:COG4555    82 ERGLYDRLTVRENIRYfaELYGLFDEELKKRIEELIELLGLEEFLDRRVGELSTGMKKKVALARALVHDPKVLLLDEPTN 161

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1054819401 177 ALDLKLRRQMQLELKRIQTEvGLTFVHVTHDQEEAMTMADTVAVMNRGRIEQMGPPADLYE 237
Cdd:COG4555   162 GLDVMARRLLREILRALKKE-GKTVLFSSHIMQEVEALCDRVVILHKGKVVAQGSLDELRE 221
ECF_ATPase_2 TIGR04521
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ...
 31-239 1.57e-55

energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette (ABC) proteins by homology, but belong to energy coupling factor (ECF) transport systems. The architecture in general is two ATPase subunits (or a double-length fusion protein), a T component, and a substrate capture (S) component that is highly variable, and may be interchangeable in genomes with only one T component. This model identifies many but not examples of the downstream member of the pair of ECF ATPases in Firmicutes and Mollicutes. [Transport and binding proteins, Unknown substrate]


Pssm-ID: 275314 [Multi-domain]  Cd Length: 277  Bit Score: 183.81  E-value: 1.57e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054819401  31 AFVAVDDLTLTVPSGSFFALLGPSGCGKTTTLRMVAGLEQPTDGTISIDGRDVTGT-----RAHRRPVNTVFQ--SYALF 103
Cdd:TIGR04521  17 EKKALDDVSLTIEDGEFVAIIGHTGSGKSTLIQHLNGLLKPTSGTVTIDGRDITAKkkkklKDLRKKVGLVFQfpEHQLF 96

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054819401 104 pHLTVAENVAFGLRR--RREADVEARVAEGLALVELGH-LADRRPALLSGGQQQRVALARALVNRPALLLLDEPLGALDL 180
Cdd:TIGR04521  97 -EETVYKDIAFGPKNlgLSEEEAEERVKEALELVGLDEeYLERSPFELSGGQMRRVAIAGVLAMEPEVLILDEPTAGLDP 175

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1054819401 181 KLRRQMQLELKRIQTEVGLTFVHVTHDQEEAMTMADTVAVMNRGRIEQMGPPADLYEHP 239
Cdd:TIGR04521 176 KGRKEILDLFKRLHKEKGLTVILVTHSMEDVAEYADRVIVMHKGKIVLDGTPREVFSDV 234
YbbA COG4181
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ...
 20-233 7.29e-54

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: 178.01  E-value: 7.29e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054819401  20 LELAAVTKRF----GAFVAVDDLTLTVPSGSFFALLGPSGCGKTTTLRMVAGLEQPTDGTISIDGRDVTG----TRAHRR 91
Cdd:COG4181     9 IELRGLTKTVgtgaGELTILKGISLEVEAGESVAIVGASGSGKSTLLGLLAGLDRPTSGTVRLAGQDLFAldedARARLR 88

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054819401  92 P--VNTVFQSYALFPHLTVAENVAFGLRRRREADVEARVAEGLALVELGHLADRRPALLSGGQQQRVALARALVNRPALL 169
Cdd:COG4181    89 ArhVGFVFQSFQLLPTLTALENVMLPLELAGRRDARARARALLERVGLGHRLDHYPAQLSGGEQQRVALARAFATEPAIL 168

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1054819401 170 LLDEPLGALDLKLRRQMQLELKRIQTEVGLTFVHVTHDQEEAmTMADTVAVMNRGRIEQMGPPA 233
Cdd:COG4181   169 FADEPTGNLDAATGEQIIDLLFELNRERGTTLVLVTHDPALA-ARCDRVLRLRAGRLVEDTAAT 231
GsiA COG1123
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ...
 25-240 4.09e-53

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: 183.95  E-value: 4.09e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054819401  25 VTKRFGAFVAVDDLTLTVPSGSFFALLGPSGCGKTTTLRMVAGLEQPT---DGTISIDGRDVTGTRAHRRP--VNTVFQS 99
Cdd:COG1123    12 VRYPGGDVPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGLLPHGgriSGEVLLDGRDLLELSEALRGrrIGMVFQD 91

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054819401 100 --YALFPhLTVAENVAFGLRRRR--EADVEARVAEGLALVELGHLADRRPALLSGGQQQRVALARALVNRPALLLLDEPL 175
Cdd:COG1123    92 pmTQLNP-VTVGDQIAEALENLGlsRAEARARVLELLEAVGLERRLDRYPHQLSGGQRQRVAIAMALALDPDLLIADEPT 170

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1054819401 176 GALDLKLRRQMQLELKRIQTEVGLTFVHVTHDQEEAMTMADTVAVMNRGRIEQMGPPADLYEHPR 240
Cdd:COG1123   171 TALDVTTQAEILDLLRELQRERGTTVLLITHDLGVVAEIADRVVVMDDGRIVEDGPPEEILAAPQ 235
AppF COG4608
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ...
 34-240 4.15e-53

ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];


Pssm-ID: 443658 [Multi-domain]  Cd Length: 329  Bit Score: 179.16  E-value: 4.15e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054819401  34 AVDDLTLTVPSGSFFALLGPSGCGKTTTLRMVAGLEQPTDGTISIDGRDVTGT-----RAHRRPVNTVFQ-SYA-LFPHL 106
Cdd:COG4608    33 AVDGVSFDIRRGETLGLVGESGCGKSTLGRLLLRLEEPTSGEILFDGQDITGLsgrelRPLRRRMQMVFQdPYAsLNPRM 112

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054819401 107 TVAENVAFGLR---RRREADVEARVAEGLALVELG-HLADRRPALLSGGQQQRVALARALVNRPALLLLDEPLGALDLKL 182
Cdd:COG4608   113 TVGDIIAEPLRihgLASKAERRERVAELLELVGLRpEHADRYPHEFSGGQRQRIGIARALALNPKLIVCDEPVSALDVSI 192

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1054819401 183 RRQ-MQLeLKRIQTEVGLTFVHVTHDQEEAMTMADTVAVMNRGRIEQMGPPADLYEHPR 240
Cdd:COG4608   193 QAQvLNL-LEDLQDELGLTYLFISHDLSVVRHISDRVAVMYLGKIVEIAPRDELYARPL 250
ABC_DrrA cd03265
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ...
 25-235 1.51e-52

Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein component of a bacterial exporter complex that confers resistance to the antibiotics daunorubicin and doxorubicin. In addition to DrrA, the complex includes an integral membrane protein called DrrB. DrrA belongs to the ABC family of transporters and shares sequence and functional similarities with a protein found in cancer cells called P-glycoprotein. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region in addition to the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.


Pssm-ID: 213232 [Multi-domain]  Cd Length: 220  Bit Score: 174.48  E-value: 1.51e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054819401  25 VTKRFGAFVAVDDLTLTVPSGSFFALLGPSGCGKTTTLRMVAGLEQPTDGTISIDGRDVTG-TRAHRRPVNTVFQSYALF 103
Cdd:cd03265     6 LVKKYGDFEAVRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATVAGHDVVRePREVRRRIGIVFQDLSVD 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054819401 104 PHLTVAENVA-----FGLRRRREADveaRVAEGLALVELGHLADRRPALLSGGQQQRVALARALVNRPALLLLDEPLGAL 178
Cdd:cd03265    86 DELTGWENLYiharlYGVPGAERRE---RIDELLDFVGLLEAADRLVKTYSGGMRRRLEIARSLVHRPEVLFLDEPTIGL 162

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1054819401 179 DLKLRRQMQLELKRIQTEVGLTFVHVTHDQEEAMTMADTVAVMNRGRIEQMGPPADL 235
Cdd:cd03265   163 DPQTRAHVWEYIEKLKEEFGMTILLTTHYMEEAEQLCDRVAIIDHGRIIAEGTPEEL 219
ABC_subfamily_A cd03263
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ...
 20-235 2.33e-52

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: 173.85  E-value: 2.33e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054819401  20 LELAAVTKRFG--AFVAVDDLTLTVPSGSFFALLGPSGCGKTTTLRMVAGLEQPTDGTISIDGRDV-TGTRAHRRPVNTV 96
Cdd:cd03263     1 LQIRNLTKTYKkgTKPAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYINGYSIrTDRKAARQSLGYC 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054819401  97 FQSYALFPHLTVAENVAF--GLRRRREADVEARVAEGLALVELGHLADRRPALLSGGQQQRVALARALVNRPALLLLDEP 174
Cdd:cd03263    81 PQFDALFDELTVREHLRFyaRLKGLPKSEIKEEVELLLRVLGLTDKANKRARTLSGGMKRKLSLAIALIGGPSVLLLDEP 160

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1054819401 175 LGALDLKLRRQMQLELKRIQTevGLTFVHVTHDQEEAMTMADTVAVMNRGRIEQMGPPADL 235
Cdd:cd03263   161 TSGLDPASRRAIWDLILEVRK--GRSIILTTHSMDEAEALCDRIAIMSDGKLRCIGSPQEL 219
ABC_PhnC_transporter cd03256
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ...
 20-238 2.87e-52

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: 174.29  E-value: 2.87e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054819401  20 LELAAVTKRFGA-FVAVDDLTLTVPSGSFFALLGPSGCGKTTTLRMVAGLEQPTDGTISIDGRDVTG-----TRAHRRPV 93
Cdd:cd03256     1 IEVENLSKTYPNgKKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGTDINKlkgkaLRQLRRQI 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054819401  94 NTVFQSYALFPHLTVAENVAFG-----------LRRRREADVEaRVAEGLALVELGHLADRRPALLSGGQQQRVALARAL 162
Cdd:cd03256    81 GMIFQQFNLIERLSVLENVLSGrlgrrstwrslFGLFPKEEKQ-RALAALERVGLLDKAYQRADQLSGGQQQRVAIARAL 159

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1054819401 163 VNRPALLLLDEPLGALDLKLRRQ-MQLeLKRIQTEVGLTFVHVTHDQEEAMTMADTVAVMNRGRIEQMGPPADLYEH 238
Cdd:cd03256   160 MQQPKLILADEPVASLDPASSRQvMDL-LKRINREEGITVIVSLHQVDLAREYADRIVGLKDGRIVFDGPPAELTDE 235
ZnuC COG1121
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ...
 20-234 1.82e-51

ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];


Pssm-ID: 440738 [Multi-domain]  Cd Length: 245  Bit Score: 172.20  E-value: 1.82e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054819401  20 LELAAVTKRFGAFVAVDDLTLTVPSGSFFALLGPSGCGKTTTLRMVAGLEQPTDGTISIDGRDVTGTRAH------RRPV 93
Cdd:COG1121     7 IELENLTVSYGGRPVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLFGKPPRRARRRigyvpqRAEV 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054819401  94 NtvfqsyALFPhLTVAENVAFGL-------RRRREADvEARVAEGLALVELGHLADRRPALLSGGQQQRVALARALVNRP 166
Cdd:COG1121    87 D------WDFP-ITVRDVVLMGRygrrglfRRPSRAD-REAVDEALERVGLEDLADRPIGELSGGQQQRVLLARALAQDP 158

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1054819401 167 ALLLLDEPLGALDLKLRRQ-MQLeLKRIQTEvGLTFVHVTHDQEEAMTMADTVAVMNRGRIEQmGPPAD 234
Cdd:COG1121   159 DLLLLDEPFAGVDAATEEAlYEL-LRELRRE-GKTILVVTHDLGAVREYFDRVLLLNRGLVAH-GPPEE 224
FetA COG4619
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
20-226 1.94e-51

ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];


Pssm-ID: 443661 [Multi-domain]  Cd Length: 209  Bit Score: 171.15  E-value: 1.94e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054819401  20 LELAAVTKRFGAFVAVDDLTLTVPSGSFFALLGPSGCGKTTTLRMVAGLEQPTDGTISIDGRDVTGTRAH--RRPVNTVF 97
Cdd:COG4619     1 LELEGLSFRVGGKPILSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIYLDGKPLSAMPPPewRRQVAYVP 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054819401  98 QSYALFPHlTVAENVAFGLRRRREADVEARVAEGLALVELGH-LADRRPALLSGGQQQRVALARALVNRPALLLLDEPLG 176
Cdd:COG4619    81 QEPALWGG-TVRDNLPFPFQLRERKFDRERALELLERLGLPPdILDKPVERLSGGERQRLALIRALLLQPDVLLLDEPTS 159

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 1054819401 177 ALDLKLRRQMQLELKRIQTEVGLTFVHVTHDQEEAMTMADTVAVMNRGRI 226
Cdd:COG4619   160 ALDPENTRRVEELLREYLAEEGRAVLWVSHDPEQIERVADRVLTLEAGRL 209
artP PRK11124
arginine transporter ATP-binding subunit; Provisional
 20-248 1.46e-50

arginine transporter ATP-binding subunit; Provisional


Pssm-ID: 182980 [Multi-domain]  Cd Length: 242  Bit Score: 169.81  E-value: 1.46e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054819401  20 LELAAVTKRFGAFVAVDDLTLTVPSGSFFALLGPSGCGKTTTLRMVAGLEQPTDGTISIDGR--DVTGT------RAHRR 91
Cdd:PRK11124    3 IQLNGINCFYGAHQALFDITLDCPQGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLNIAGNhfDFSKTpsdkaiRELRR 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054819401  92 PVNTVFQSYALFPHLTVAENV------AFGLRrrrEADVEARVAEGLALVELGHLADRRPALLSGGQQQRVALARALVNR 165
Cdd:PRK11124   83 NVGMVFQQYNLWPHLTVQQNLieapcrVLGLS---KDQALARAEKLLERLRLKPYADRFPLHLSGGQQQRVAIARALMME 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054819401 166 PALLLLDEPLGALDLKLRRQMQLELKRIQtEVGLTFVHVTHDQEEAMTMADTVAVMNRGRIEQMGpPADLYEHPRTTFVA 245
Cdd:PRK11124  160 PQVLLFDEPTAALDPEITAQIVSIIRELA-ETGITQVIVTHEVEVARKTASRVVYMENGHIVEQG-DASCFTQPQTEAFK 237


                  ...
gi 1054819401 246 NFL 248
Cdd:PRK11124  238 NYL 240
ArtP COG4161
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
20-248 3.19e-50

ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];


Pssm-ID: 443326 [Multi-domain]  Cd Length: 242  Bit Score: 169.04  E-value: 3.19e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054819401  20 LELAAVTKRFGAFVAVDDLTLTVPSGSFFALLGPSGCGKTTTLRMVAGLEQPTDGTISIDGR--------DVTGTRAHRR 91
Cdd:COG4161     3 IQLKNINCFYGSHQALFDINLECPSGETLVLLGPSGAGKSSLLRVLNLLETPDSGQLNIAGHqfdfsqkpSEKAIRLLRQ 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054819401  92 PVNTVFQSYALFPHLTVAENV------AFGLRRrreADVEARVAEGLALVELGHLADRRPALLSGGQQQRVALARALVNR 165
Cdd:COG4161    83 KVGMVFQQYNLWPHLTVMENLieapckVLGLSK---EQAREKAMKLLARLRLTDKADRFPLHLSGGQQQRVAIARALMME 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054819401 166 PALLLLDEPLGALDLKLRRQMqLELKRIQTEVGLTFVHVTHDQEEAMTMADTVAVMNRGRIEQMGpPADLYEHPRTTFVA 245
Cdd:COG4161   160 PQVLLFDEPTAALDPEITAQV-VEIIRELSQTGITQVIVTHEVEFARKVASQVVYMEKGRIIEQG-DASHFTQPQTEAFA 237


                  ...
gi 1054819401 246 NFL 248
Cdd:COG4161   238 HYL 240
ECF_ATPase_1 TIGR04520
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ...
 34-238 5.77e-50

energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette (ABC) proteins by homology, but belong to energy coupling factor (ECF) transport systems. The architecture in general is two ATPase subunits (or a double-length fusion protein), a T component, and a substrate capture (S) component that is highly variable, and may be interchangeable in genomes with only one T component. This model identifies many but not examples of the upstream member of the pair of ECF ATPases in Firmicutes and Mollicutes. [Transport and binding proteins, Unknown substrate]


Pssm-ID: 275313 [Multi-domain]  Cd Length: 268  Bit Score: 169.15  E-value: 5.77e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054819401  34 AVDDLTLTVPSGSFFALLGPSGCGKTTTLRMVAGLEQPTDGTISIDGRDvTGTRAH----RRPVNTVFQSyalfPH---- 105
Cdd:TIGR04520  17 ALKNVSLSIEKGEFVAIIGHNGSGKSTLAKLLNGLLLPTSGKVTVDGLD-TLDEENlweiRKKVGMVFQN----PDnqfv 91

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054819401 106 -LTVAENVAFGLRRR---REaDVEARVAEGLALVELGHLADRRPALLSGGQQQRVALARALVNRPALLLLDEPLGALDLK 181
Cdd:TIGR04520  92 gATVEDDVAFGLENLgvpRE-EMRKRVDEALKLVGMEDFRDREPHLLSGGQKQRVAIAGVLAMRPDIIILDEATSMLDPK 170

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1054819401 182 LRRQMQLELKRIQTEVGLTFVHVTHDQEEAmTMADTVAVMNRGRIEQMGPPADLYEH 238
Cdd:TIGR04520 171 GRKEVLETIRKLNKEEGITVISITHDMEEA-VLADRVIVMNKGKIVAEGTPREIFSQ 226
ssuB PRK11247
aliphatic sulfonates transport ATP-binding subunit; Provisional
 20-226 6.60e-50

aliphatic sulfonates transport ATP-binding subunit; Provisional


Pssm-ID: 183055 [Multi-domain]  Cd Length: 257  Bit Score: 168.70  E-value: 6.60e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054819401  20 LELAAVTKRFGAFVAVDDLTLTVPSGSFFALLGPSGCGKTTTLRMVAGLEQPTDGTIsIDGRdvTGTRAHRRPVNTVFQS 99
Cdd:PRK11247   13 LLLNAVSKRYGERTVLNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAGEL-LAGT--APLAEAREDTRLMFQD 89

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054819401 100 YALFPHLTVAENVAFGLRrrreADVEARVAEGLALVELGHLADRRPALLSGGQQQRVALARALVNRPALLLLDEPLGALD 179
Cdd:PRK11247   90 ARLLPWKKVIDNVGLGLK----GQWRDAALQALAAVGLADRANEWPAALSGGQKQRVALARALIHRPGLLLLDEPLGALD 165

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 1054819401 180 LKLRRQMQLELKRIQTEVGLTFVHVTHDQEEAMTMADTVAVMNRGRI 226
Cdd:PRK11247  166 ALTRIEMQDLIESLWQQHGFTVLLVTHDVSEAVAMADRVLLIEEGKI 212
thiQ TIGR01277
thiamine ABC transporter, ATP-binding protein; This model describes the energy-transducing ...
 40-230 1.10e-49

thiamine ABC transporter, ATP-binding protein; This model describes the energy-transducing ATPase subunit ThiQ of the ThiBPQ thiamine (and thiamine pyrophosphate) ABC transporter in several Proteobacteria. This protein is found so far only in Proteobacteria, and is found in complete genomes only if the ThiB and ThiP subunits are also found. [Transport and binding proteins, Other]


Pssm-ID: 130344 [Multi-domain]  Cd Length: 213  Bit Score: 166.58  E-value: 1.10e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054819401  40 LTVPSGSFFALLGPSGCGKTTTLRMVAGLEQPTDGTISIDGRDVTGTRAHRRPVNTVFQSYALFPHLTVAENVAFGLRR- 118
Cdd:TIGR01277  19 LNVADGEIVAIMGPSGAGKSTLLNLIAGFIEPASGSIKVNDQSHTGLAPYQRPVSMLFQENNLFAHLTVRQNIGLGLHPg 98

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054819401 119 -RREADVEARVAEGLALVELGHLADRRPALLSGGQQQRVALARALVNRPALLLLDEPLGALDLKLRRQMQLELKRIQTEV 197
Cdd:TIGR01277  99 lKLNAEQQEKVVDAAQQVGIADYLDRLPEQLSGGQRQRVALARCLVRPNPILLLDEPFSALDPLLREEMLALVKQLCSER 178

                         170       180       190
                  ....*....|....*....|....*....|...
gi 1054819401 198 GLTFVHVTHDQEEAMTMADTVAVMNRGRIEQMG 230
Cdd:TIGR01277 179 QRTLLMVTHHLSDARAIASQIAVVSQGKIKVVS 211
ABC_ThiQ_thiamine_transporter cd03298
ATP-binding cassette domain of the thiamine transport system; Part of the ...
 37-226 1.14e-49

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: 166.51  E-value: 1.14e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054819401  37 DLTLTVPSGSFFALLGPSGCGKTTTLRMVAGLEQPTDGTISIDGRDVTGTRAHRRPVNTVFQSYALFPHLTVAENVAFGL 116
Cdd:cd03298    16 HFDLTFAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLINGVDVTAAPPADRPVSMLFQENNLFAHLTVEQNVGLGL 95

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054819401 117 --RRRREADVEARVAEGLALVELGHLADRRPALLSGGQQQRVALARALVNRPALLLLDEPLGALDLKLRRQMQLELKRIQ 194
Cdd:cd03298    96 spGLKLTAEDRQAIEVALARVGLAGLEKRLPGELSGGERQRVALARVLVRDKPVLLLDEPFAALDPALRAEMLDLVLDLH 175

                         170       180       190
                  ....*....|....*....|....*....|..
gi 1054819401 195 TEVGLTFVHVTHDQEEAMTMADTVAVMNRGRI 226
Cdd:cd03298   176 AETKMTVLMVTHQPEDAKRLAQRVVFLDNGRI 207
FtsE TIGR02673
cell division ATP-binding protein FtsE; This model describes FtsE, a member of the ABC ...
 20-225 1.21e-49

cell division ATP-binding protein FtsE; This model describes FtsE, a member of the ABC transporter ATP-binding protein family. This protein, and its permease partner FtsX, localize to the division site. In a number of species, the ftsEX gene pair is located next to FtsY, the signal recognition particle-docking protein. [Cellular processes, Cell division]


Pssm-ID: 131721 [Multi-domain]  Cd Length: 214  Bit Score: 166.65  E-value: 1.21e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054819401  20 LELAAVTKRF-GAFVAVDDLTLTVPSGSFFALLGPSGCGKTTTLRMVAGLEQPTDGTISIDGRDVTGTRAH-----RRPV 93
Cdd:TIGR02673   2 IEFHNVSKAYpGGVAALHDVSLHIRKGEFLFLTGPSGAGKTTLLKLLYGALTPSRGQVRIAGEDVNRLRGRqlpllRRRI 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054819401  94 NTVFQSYALFPHLTVAENVAFGL--RRRREADVEARVAEGLALVELGHLADRRPALLSGGQQQRVALARALVNRPALLLL 171
Cdd:TIGR02673  82 GVVFQDFRLLPDRTVYENVALPLevRGKKEREIQRRVGAALRQVGLEHKADAFPEQLSGGEQQRVAIARAIVNSPPLLLA 161

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1054819401 172 DEPLGALDLKLRRQMQLELKRIQtEVGLTFVHVTHDQEEAMTMADTVAVMNRGR 225
Cdd:TIGR02673 162 DEPTGNLDPDLSERILDLLKRLN-KRGTTVIVATHDLSLVDRVAHRVIILDDGR 214
ABC_phnC TIGR02315
phosphonate ABC transporter, ATP-binding protein; Phosphonates are a class of ...
 20-238 2.93e-49

phosphonate ABC transporter, ATP-binding protein; Phosphonates are a class of phosphorus-containing organic compound with a stable direct C-P bond rather than a C-O-P linkage. A number of bacterial species have operons, typically about 14 genes in size, with genes for ATP-dependent transport of phosphonates, degradation, and regulation of the expression of the system. Members of this protein family are the ATP-binding cassette component of tripartite ABC transporters of phosphonates. [Transport and binding proteins, Anions]


Pssm-ID: 131368 [Multi-domain]  Cd Length: 243  Bit Score: 166.32  E-value: 2.93e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054819401  20 LELAAVTKRFG-AFVAVDDLTLTVPSGSFFALLGPSGCGKTTTLRMVAGLEQPTDGTISIDGRDVTGTRAH-----RRPV 93
Cdd:TIGR02315   2 LEVENLSKVYPnGKQALKNINLNINPGEFVAIIGPSGAGKSTLLRCINRLVEPSSGSILLEGTDITKLRGKklrklRRRI 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054819401  94 NTVFQSYALFPHLTVAENVAFG-----------LRRRREADVEaRVAEGLALVELGHLADRRPALLSGGQQQRVALARAL 162
Cdd:TIGR02315  82 GMIFQHYNLIERLTVLENVLHGrlgykptwrslLGRFSEEDKE-RALSALERVGLADKAYQRADQLSGGQQQRVAIARAL 160

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1054819401 163 VNRPALLLLDEPLGALDLKLRRQMQLELKRIQTEVGLTFVHVTHDQEEAMTMADTVAVMNRGRIEQMGPPADLYEH 238
Cdd:TIGR02315 161 AQQPDLILADEPIASLDPKTSKQVMDYLKRINKEDGITVIINLHQVDLAKKYADRIVGLKAGEIVFDGAPSELDDE 236
ABC_FtsE cd03292
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ...
 20-226 3.15e-49

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: 165.66  E-value: 3.15e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054819401  20 LELAAVTKRFGA-FVAVDDLTLTVPSGSFFALLGPSGCGKTTTLRMVAGLEQPTDGTISIDGRDVTGTRAH-----RRPV 93
Cdd:cd03292     1 IEFINVTKTYPNgTAALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQDVSDLRGRaipylRRKI 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054819401  94 NTVFQSYALFPHLTVAENVAFGLRRRREA--DVEARVAEGLALVELGHLADRRPALLSGGQQQRVALARALVNRPALLLL 171
Cdd:cd03292    81 GVVFQDFRLLPDRNVYENVAFALEVTGVPprEIRKRVPAALELVGLSHKHRALPAELSGGEQQRVAIARAIVNSPTILIA 160

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1054819401 172 DEPLGALDLKLRRQMQLELKRIQtEVGLTFVHVTHDQEEAMTMADTVAVMNRGRI 226
Cdd:cd03292   161 DEPTGNLDPDTTWEIMNLLKKIN-KAGTTVVVATHAKELVDTTRHRVIALERGKL 214
DppD COG0444
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ...
 20-240 1.62e-48

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: 166.77  E-value: 1.62e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054819401  20 LELAAVTKRF----GAFVAVDDLTLTVPSGSFFALLGPSGCGKTTTLRMVAGLEQP---TDGTISIDGRDVTG-TRAHRR 91
Cdd:COG0444     2 LEVRNLKVYFptrrGVVKAVDGVSFDVRRGETLGLVGESGSGKSTLARAILGLLPPpgiTSGEILFDGEDLLKlSEKELR 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054819401  92 PVNT-----VFQ-SY-ALFPHLTVAENVAFGLRRRR---EADVEARVAEGLALVEL---GHLADRRPALLSGGQQQRVAL 158
Cdd:COG0444    82 KIRGreiqmIFQdPMtSLNPVMTVGDQIAEPLRIHGglsKAEARERAIELLERVGLpdpERRLDRYPHELSGGMRQRVMI 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054819401 159 ARALVNRPALLLLDEPLGALDLKLRRQ-MQLeLKRIQTEVGLTFVHVTHDQEEAMTMADTVAVMNRGRIEQMGPPADLYE 237
Cdd:COG0444   162 ARALALEPKLLIADEPTTALDVTIQAQiLNL-LKDLQRELGLAILFITHDLGVVAEIADRVAVMYAGRIVEEGPVEELFE 240


                  ...
gi 1054819401 238 HPR 240
Cdd:COG0444   241 NPR 243
ABC_TM1139_LivF_branched cd03224
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ...
 20-235 1.94e-48

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: 163.76  E-value: 1.94e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054819401  20 LELAAVTKRFGAFVAVDDLTLTVPSGSFFALLGPSGCGKTTTLRMVAGLEQPTDGTISIDGRDVTGTRAHRRP---VNTV 96
Cdd:cd03224     1 LEVENLNAGYGKSQILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDGRDITGLPPHERAragIGYV 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054819401  97 FQSYALFPHLTVAENVAFGLRRRREADVEARVAEGLALV-ELGHLADRRPALLSGGQQQRVALARALVNRPALLLLDEPL 175
Cdd:cd03224    81 PEGRRIFPELTVEENLLLGAYARRRAKRKARLERVYELFpRLKERRKQLAGTLSGGEQQMLAIARALMSRPKLLLLDEPS 160

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054819401 176 GALDLKLRRQMQLELKRIQTEvGLTFVHVTHDQEEAMTMADTVAVMNRGRIEQMGPPADL 235
Cdd:cd03224   161 EGLAPKIVEEIFEAIRELRDE-GVTILLVEQNARFALEIADRAYVLERGRVVLEGTAAEL 219
thiQ PRK10771
thiamine ABC transporter ATP-binding protein ThiQ;
39-235 5.55e-48

thiamine ABC transporter ATP-binding protein ThiQ;


Pssm-ID: 182716 [Multi-domain]  Cd Length: 232  Bit Score: 162.83  E-value: 5.55e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054819401  39 TLTVPSGSFFALLGPSGCGKTTTLRMVAGLEQPTDGTISIDGRDVTGTRAHRRPVNTVFQSYALFPHLTVAENVAFGLRR 118
Cdd:PRK10771   19 DLTVERGERVAILGPSGAGKSTLLNLIAGFLTPASGSLTLNGQDHTTTPPSRRPVSMLFQENNLFSHLTVAQNIGLGLNP 98

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054819401 119 --RREADVEARVAEGLALVELGHLADRRPALLSGGQQQRVALARALVNRPALLLLDEPLGALDLKLRRQMQLELKRIQTE 196
Cdd:PRK10771   99 glKLNAAQREKLHAIARQMGIEDLLARLPGQLSGGQRQRVALARCLVREQPILLLDEPFSALDPALRQEMLTLVSQVCQE 178

                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 1054819401 197 VGLTFVHVTHDQEEAMTMADTVAVMNRGRIEQMGPPADL 235
Cdd:PRK10771  179 RQLTLLMVSHSLEDAARIAPRSLVVADGRIAWDGPTDEL 217
ABC_tran pfam00005
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ...
 35-174 2.72e-47

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: 158.19  E-value: 2.72e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054819401  35 VDDLTLTVPSGSFFALLGPSGCGKTTTLRMVAGLEQPTDGTISIDGRDVTGT--RAHRRPVNTVFQSYALFPHLTVAENV 112
Cdd:pfam00005   1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDLTDDerKSLRKEIGYVFQDPQLFPRLTVRENL 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1054819401 113 AFGLR--RRREADVEARVAEGLALVELGHLADRR----PALLSGGQQQRVALARALVNRPALLLLDEP 174
Cdd:pfam00005  81 RLGLLlkGLSKREKDARAEEALEKLGLGDLADRPvgerPGTLSGGQRQRVAIARALLTKPKLLLLDEP 148
tauB PRK11248
taurine ABC transporter ATP-binding subunit;
20-226 1.06e-46

taurine ABC transporter ATP-binding subunit;


Pssm-ID: 183056 [Multi-domain]  Cd Length: 255  Bit Score: 160.25  E-value: 1.06e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054819401  20 LELAAVTKRFGAFVAVDDLTLTVPSGSFFALLGPSGCGKTTTLRMVAGLEQPTDGTISIDGRDVTGTRAHRrpvNTVFQS 99
Cdd:PRK11248    2 LQISHLYADYGGKPALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDGKPVEGPGAER---GVVFQN 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054819401 100 YALFPHLTVAENVAFGLRRR--READVEARVAEGLALVELGHLADRRPALLSGGQQQRVALARALVNRPALLLLDEPLGA 177
Cdd:PRK11248   79 EGLLPWRNVQDNVAFGLQLAgvEKMQRLEIAHQMLKKVGLEGAEKRYIWQLSGGQRQRVGIARALAANPQLLLLDEPFGA 158

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1054819401 178 LDLKLRRQMQLELKRIQTEVGLTFVHVTHDQEEAMTMADTVAVM--NRGRI 226
Cdd:PRK11248  159 LDAFTREQMQTLLLKLWQETGKQVLLITHDIEEAVFMATELVLLspGPGRV 209
YnjD COG4136
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ...
 20-211 1.19e-46

ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];


Pssm-ID: 443311 [Multi-domain]  Cd Length: 211  Bit Score: 158.80  E-value: 1.19e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054819401  20 LELAAVTKRFGAFVAVDDLTLTVPSGSFFALLGPSGCGKTTTLRMVAGLEQP---TDGTISIDGRDVTGTRAHRRPVNTV 96
Cdd:COG4136     2 LSLENLTITLGGRPLLAPLSLTVAPGEILTLMGPSGSGKSTLLAAIAGTLSPafsASGEVLLNGRRLTALPAEQRRIGIL 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054819401  97 FQSYALFPHLTVAENVAFGLRRR-READVEARVAEGLALVELGHLADRRPALLSGGQQQRVALARALVNRPALLLLDEPL 175
Cdd:COG4136    82 FQDDLLFPHLSVGENLAFALPPTiGRAQRRARVEQALEEAGLAGFADRDPATLSGGQRARVALLRALLAEPRALLLDEPF 161

                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 1054819401 176 GALDLKLRRQM-QLELKRIQTEvGLTFVHVTHDQEEA 211
Cdd:COG4136   162 SKLDAALRAQFrEFVFEQIRQR-GIPALLVTHDEEDA 197
YejF COG4172
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ...
 27-241 2.10e-46

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: 166.40  E-value: 2.10e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054819401  27 KRFGAFVAVDDLTLTVPSGSFFALLGPSGCGKTTTLRMVAGLeQPTDGTISIDGRDVTGT-----RAHRRPVNTVFQS-Y 100
Cdd:COG4172   294 RTVGHVKAVDGVSLTLRRGETLGLVGESGSGKSTLGLALLRL-IPSEGEIRFDGQDLDGLsrralRPLRRRMQVVFQDpF 372

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054819401 101 A-LFPHLTVAENVAFGLR----RRREADVEARVAEGLALVEL-GHLADRRPALLSGGQQQRVALARALVNRPALLLLDEP 174
Cdd:COG4172   373 GsLSPRMTVGQIIAEGLRvhgpGLSAAERRARVAEALEEVGLdPAARHRYPHEFSGGQRQRIAIARALILEPKLLVLDEP 452

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1054819401 175 LGALDLKLRRQMqLEL-KRIQTEVGLTFVHVTHDQEEAMTMADTVAVMNRGRIEQMGPPADLYEHPRT 241
Cdd:COG4172   453 TSALDVSVQAQI-LDLlRDLQREHGLAYLFISHDLAVVRALAHRVMVMKDGKVVEQGPTEQVFDAPQH 519
ABC_NatA_sodium_exporter cd03266
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ...
 20-226 3.64e-46

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: 157.53  E-value: 3.64e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054819401  20 LELAAVTKRFGA----FVAVDDLTLTVPSGSFFALLGPSGCGKTTTLRMVAGLEQPTDGTISIDGRDV-TGTRAHRRPVN 94
Cdd:cd03266     2 ITADALTKRFRDvkktVQAVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDGFDVvKEPAEARRRLG 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054819401  95 TVFQSYALFPHLTVAENVAF-----GLRRRreaDVEARVAEGLALVELGHLADRRPALLSGGQQQRVALARALVNRPALL 169
Cdd:cd03266    82 FVSDSTGLYDRLTARENLEYfaglyGLKGD---ELTARLEELADRLGMEELLDRRVGGFSTGMRQKVAIARALVHDPPVL 158

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1054819401 170 LLDEPLGALDLKLRRQMqLELKRIQTEVGLTFVHVTHDQEEAMTMADTVAVMNRGRI 226
Cdd:cd03266   159 LLDEPTTGLDVMATRAL-REFIRQLRALGKCILFSTHIMQEVERLCDRVVVLHRGRV 214
ABC_Metallic_Cations cd03235
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ...
 21-224 6.17e-46

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: 156.92  E-value: 6.17e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054819401  21 ELAAVTKRFGAFVAVDDLTLTVPSGSFFALLGPSGCGKTTTLRMVAGLEQPTDGTISIDGRDVTGTRAHrrpVNTVFQSY 100
Cdd:cd03235     1 EVEDLTVSYGGHPVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFGKPLEKERKR---IGYVPQRR 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054819401 101 AL---FPhLTVAENVAFGLRRRRE------ADVEARVAEGLALVELGHLADRRPALLSGGQQQRVALARALVNRPALLLL 171
Cdd:cd03235    78 SIdrdFP-ISVRDVVLMGLYGHKGlfrrlsKADKAKVDEALERVGLSELADRQIGELSGGQQQRVLLARALVQDPDLLLL 156

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1054819401 172 DEPLGALDLKLRRQMQLELKRIQTEvGLTFVHVTHDQEEAMTMADTVAVMNRG 224
Cdd:cd03235   157 DEPFAGVDPKTQEDIYELLRELRRE-GMTILVVTHDLGLVLEYFDRVLLLNRT 208
LivF COG0410
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ...
 20-240 9.90e-46

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: 157.07  E-value: 9.90e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054819401  20 LELAAVTKRFGAFVAVDDLTLTVPSGSFFALLGPSGCGKTTTLRMVAGLEQPTDGTISIDGRDVTGTRAHRRP---VNTV 96
Cdd:COG0410     4 LEVENLHAGYGGIHVLHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRSGSIRFDGEDITGLPPHRIArlgIGYV 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054819401  97 FQSYALFPHLTVAENVAFGLRRRR-EADVEARVAEGLALV-ELGHLADRRPALLSGGQQQRVALARALVNRPALLLLDEP 174
Cdd:COG0410    84 PEGRRIFPSLTVEENLLLGAYARRdRAEVRADLERVYELFpRLKERRRQRAGTLSGGEQQMLAIGRALMSRPKLLLLDEP 163

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1054819401 175 LGALDLKLRRQMQLELKRIQTEvGLTFVHVTHDQEEAMTMADTVAVMNRGRIEQMGPPADLYEHPR 240
Cdd:COG0410   164 SLGLAPLIVEEIFEIIRRLNRE-GVTILLVEQNARFALEIADRAYVLERGRIVLEGTAAELLADPE 228
ABC_ATP_DarD NF038007
darobactin export ABC transporter ATP-binding protein;
34-226 1.87e-45

darobactin export ABC transporter ATP-binding protein;


Pssm-ID: 411600 [Multi-domain]  Cd Length: 218  Bit Score: 155.65  E-value: 1.87e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054819401  34 AVDDLTLTVPSGSFFALLGPSGCGKTTTLRMVAGLEQPTDGTISIDGRDVTGTR------AHRRPVNTVFQSYALFPHLT 107
Cdd:NF038007   20 VLNHLNFSVEKGDFVSIMGPSGSGKSTLLNIIGMFDSLDSGSLTLAGKEVTNLSysqkiiLRRELIGYIFQSFNLIPHLS 99

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054819401 108 VAENVAFGLRRRREADVE--ARVAEGLALVELGHLADRRPALLSGGQQQRVALARALVNRPALLLLDEPLGALDLKLRRQ 185
Cdd:NF038007  100 IFDNVALPLKYRGVAKKEriERVNQVLNLFGIDNRRNHKPMQLSGGQQQRVAIARAMVSNPALLLADEPTGNLDSKNARA 179

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 1054819401 186 MQLELKRIQtEVGLTFVHVTHdQEEAMTMADTVAVMNRGRI 226
Cdd:NF038007  180 VLQQLKYIN-QKGTTIIMVTH-SDEASTYGNRIINMKDGKL 218
cbiO PRK13637
energy-coupling factor transporter ATPase;
33-236 4.80e-45

energy-coupling factor transporter ATPase;


Pssm-ID: 237455 [Multi-domain]  Cd Length: 287  Bit Score: 156.75  E-value: 4.80e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054819401  33 VAVDDLTLTVPSGSFFALLGPSGCGKTTTLRMVAGLEQPTDGTISIDGRDVTGTRAH----RRPVNTVFQ--SYALFPHl 106
Cdd:PRK13637   21 KALDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDGVDITDKKVKlsdiRKKVGLVFQypEYQLFEE- 99

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054819401 107 TVAENVAFGLRRR--READVEARVAEGLALVELGH--LADRRPALLSGGQQQRVALARALVNRPALLLLDEPLGALDLKL 182
Cdd:PRK13637  100 TIEKDIAFGPINLglSEEEIENRVKRAMNIVGLDYedYKDKSPFELSGGQKRRVAIAGVVAMEPKILILDEPTAGLDPKG 179

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1054819401 183 RRQMQLELKRIQTEVGLTFVHVTHDQEEAMTMADTVAVMNRGRIEQMGPPADLY 236
Cdd:PRK13637  180 RDEILNKIKELHKEYNMTIILVSHSMEDVAKLADRIIVMNKGKCELQGTPREVF 233
ABC_Iron-Siderophores_B12_Hemin cd03214
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ...
 21-226 2.36e-44

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: 151.43  E-value: 2.36e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054819401  21 ELAAVTKRFGAFVAVDDLTLTVPSGSFFALLGPSGCGKTTTLRMVAGLEQPTDGTISIDGRDVtgtrahrrpvntvfqsy 100
Cdd:cd03214     1 EVENLSVGYGGRTVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDGKDL----------------- 63

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054819401 101 ALFPHLTVAENVAFglrrrreadvearVAEGLALVELGHLADRRPALLSGGQQQRVALARALVNRPALLLLDEPLGALDL 180
Cdd:cd03214    64 ASLSPKELARKIAY-------------VPQALELLGLAHLADRPFNELSGGERQRVLLARALAQEPPILLLDEPTSHLDI 130

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 1054819401 181 KlrRQMQL--ELKRIQTEVGLTFVHVTHDQEEAMTMADTVAVMNRGRI 226
Cdd:cd03214   131 A--HQIELleLLRRLARERGKTVVMVLHDLNLAARYADRVILLKDGRI 176
CcmA COG4133
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ...
 20-179 2.49e-44

ABC-type transport system involved in cytochrome c biogenesis, ATPase component [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 443308 [Multi-domain]  Cd Length: 206  Bit Score: 152.25  E-value: 2.49e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054819401  20 LELAAVTKRFGAFVAVDDLTLTVPSGSFFALLGPSGCGKTTTLRMVAGLEQPTDGTISIDGRDVTGTR-AHRRPVNTVFQ 98
Cdd:COG4133     3 LEAENLSCRRGERLLFSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWNGEPIRDAReDYRRRLAYLGH 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054819401  99 SYALFPHLTVAENVAFGLRRRREADVEARVAEGLALVELGHLADRRPALLSGGQQQRVALARALVNRPALLLLDEPLGAL 178
Cdd:COG4133    83 ADGLKPELTVRENLRFWAALYGLRADREAIDEALEAVGLAGLADLPVRQLSAGQKRRVALARLLLSPAPLWLLDEPFTAL 162


                  .
gi 1054819401 179 D 179
Cdd:COG4133   163 D 163
ABC_ATPase cd00267
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ...
 25-225 3.60e-44

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: 150.47  E-value: 3.60e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054819401  25 VTKRFGAFVAVDDLTLTVPSGSFFALLGPSGCGKTTTLRMVAGLEQPTDGTISIDGRDVT--GTRAHRRPVNTVFQsyal 102
Cdd:cd00267     5 LSFRYGGRTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGKDIAklPLEELRRRIGYVPQ---- 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054819401 103 fphltvaenvafglrrrreadvearvaeglalvelghladrrpalLSGGQQQRVALARALVNRPALLLLDEPLGALDLKL 182
Cdd:cd00267    81 ---------------------------------------------LSGGQRQRVALARALLLNPDLLLLDEPTSGLDPAS 115

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 1054819401 183 RRQMQLELKRIQTEvGLTFVHVTHDQEEAMTMADTVAVMNRGR 225
Cdd:cd00267   116 RERLLELLRELAEE-GRTVIIVTHDPELAELAADRVIVLKDGK 157
SunT COG2274
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ...
 34-238 5.08e-44

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: 162.31  E-value: 5.08e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054819401  34 AVDDLTLTVPSGSFFALLGPSGCGKTTTLRMVAGLEQPTDGTISIDGRDVT--GTRAHRRPVNTVFQSYALFpHLTVAEN 111
Cdd:COG2274   490 VLDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEPTSGRILIDGIDLRqiDPASLRRQIGVVLQDVFLF-SGTIREN 568

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054819401 112 VAFGlrrRREADVEaRVAEGLALVELGHLADRRP-----------ALLSGGQQQRVALARALVNRPALLLLDEPLGALDL 180
Cdd:COG2274   569 ITLG---DPDATDE-EIIEAARLAGLHDFIEALPmgydtvvgeggSNLSGGQRQRLAIARALLRNPRILILDEATSALDA 644

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1054819401 181 KLRRQMQLELKRIqtEVGLTFVHVTHDqEEAMTMADTVAVMNRGRIEQMGPPADLYEH 238
Cdd:COG2274   645 ETEAIILENLRRL--LKGRTVIIIAHR-LSTIRLADRIIVLDKGRIVEDGTHEELLAR 699
YhaQ COG4152
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ...
 20-290 8.46e-44

ABC-type uncharacterized transport system, ATPase component [General function prediction only];


Pssm-ID: 443322 [Multi-domain]  Cd Length: 298  Bit Score: 153.73  E-value: 8.46e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054819401  20 LELAAVTKRFGAFVAVDDLTLTVPSGSFFALLGPSGCGKTTTLRMVAGLEQPTDGTISIDGRDVtgTRAHRRPVntvfqS 99
Cdd:COG4152     2 LELKGLTKRFGDKTAVDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDSGEVLWDGEPL--DPEDRRRI-----G 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054819401 100 Y-----ALFPHLTVAENVAF-----GLRRrreADVEARVAEGLALVELGHLADRRPALLSGGQQQRVALARALVNRPALL 169
Cdd:COG4152    75 YlpeerGLYPKMKVGEQLVYlarlkGLSK---AEAKRRADEWLERLGLGDRANKKVEELSKGNQQKVQLIAALLHDPELL 151

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054819401 170 LLDEPLGALD------LKlrrQMQLELKRiqteVGLTFVHVTHDQEEAMTMADTVAVMNRGRIEQMGPPADLYE-HPRTT 242
Cdd:COG4152   152 ILDEPFSGLDpvnvelLK---DVIRELAA----KGTTVIFSSHQMELVEELCDRIVIINKGRKVLSGSVDEIRRqFGRNT 224

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1054819401 243 F---VANFLGRSNLVPGTVVERLDGDllgvdvgGARVRVPAS-------RAVRDTGDV 290
Cdd:COG4152   225 LrleADGDAGWLRALPGVTVVEEDGD-------GAELKLEDGadaqellRALLARGPV 275
ABC_BcrA_bacitracin_resist cd03268
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ...
 20-226 1.29e-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: 150.45  E-value: 1.29e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054819401  20 LELAAVTKRFGAFVAVDDLTLTVPSGSFFALLGPSGCGKTTTLRMVAGLEQPTDGTISIDGRDVTGTRAHRRPVNTVFQS 99
Cdd:cd03268     1 LKTNDLTKTYGKKRVLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEITFDGKSYQKNIEALRRIGALIEA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054819401 100 YALFPHLTVAENV---AFGLRRRreadvEARVAEGLALVELGHLADRRPALLSGGQQQRVALARALVNRPALLLLDEPLG 176
Cdd:cd03268    81 PGFYPNLTARENLrllARLLGIR-----KKRIDEVLDVVGLKDSAKKKVKGFSLGMKQRLGIALALLGNPDLLILDEPTN 155

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 1054819401 177 ALDLKLRRQMQlELKRIQTEVGLTFVHVTHDQEEAMTMADTVAVMNRGRI 226
Cdd:cd03268   156 GLDPDGIKELR-ELILSLRDQGITVLISSHLLSEIQKVADRIGIINKGKL 204
HisP COG4598
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism];
1-251 2.09e-43

ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism];


Pssm-ID: 443652 [Multi-domain]  Cd Length: 259  Bit Score: 151.49  E-value: 2.09e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054819401   1 MTTTAPAhpgaasasagaALELAAVTKRFGAFVAVDDLTLTVPSGSFFALLGPSGCGKTTTLRMVAGLEQPTDGTISIDG 80
Cdd:COG4598     1 MTDTAPP-----------ALEVRDLHKSFGDLEVLKGVSLTARKGDVISIIGSSGSGKSTFLRCINLLETPDSGEIRVGG 69

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054819401  81 ---RDVTGTRAHRRPVNT------------VFQSYALFPHLTVAENVAFG----LRRRReADVEARVAEGLALVELGHLA 141
Cdd:COG4598    70 eeiRLKPDRDGELVPADRrqlqrirtrlgmVFQSFNLWSHMTVLENVIEApvhvLGRPK-AEAIERAEALLAKVGLADKR 148

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054819401 142 DRRPALLSGGQQQRVALARALVNRPALLLLDEPLGALD-------LKLRRQMQLElkriqtevGLTFVHVTHDQEEAMTM 214
Cdd:COG4598   149 DAYPAHLSGGQQQRAAIARALAMEPEVMLFDEPTSALDpelvgevLKVMRDLAEE--------GRTMLVVTHEMGFARDV 220

                         250       260       270
                  ....*....|....*....|....*....|....*..
gi 1054819401 215 ADTVAVMNRGRIEQMGPPADLYEHPRTTFVANFLGRS 251
Cdd:COG4598   221 SSHVVFLHQGRIEEQGPPAEVFGNPKSERLRQFLSSS 257
ABC_putative_ATPase cd03269
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ...
 20-226 2.38e-43

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: 150.12  E-value: 2.38e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054819401  20 LELAAVTKRFGAFVAVDDLTLTVPSGSFFALLGPSGCGKTTTLRMVAGLEQPTDGTISIDGRDVtgTRAHRRPVNTVFQS 99
Cdd:cd03269     1 LEVENVTKRFGRVTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDGKPL--DIAARNRIGYLPEE 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054819401 100 YALFPHLTVAENVAF-----GLRRRreaDVEARVAEGLALVELGHLADRRPALLSGGQQQRVALARALVNRPALLLLDEP 174
Cdd:cd03269    79 RGLYPKMKVIDQLVYlaqlkGLKKE---EARRRIDEWLERLELSEYANKRVEELSKGNQQKVQFIAAVIHDPELLILDEP 155

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1054819401 175 LGALD---LKLRRQMQLELKRiqteVGLTFVHVTHDQEEAMTMADTVAVMNRGRI 226
Cdd:cd03269   156 FSGLDpvnVELLKDVIRELAR----AGKTVILSTHQMELVEELCDRVLLLNKGRA 206
nikE PRK10419
nickel ABC transporter ATP-binding protein NikE;
35-239 5.02e-43

nickel ABC transporter ATP-binding protein NikE;


Pssm-ID: 236689 [Multi-domain]  Cd Length: 268  Bit Score: 150.99  E-value: 5.02e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054819401  35 VDDLTLTVPSGSFFALLGPSGCGKTTTLRMVAGLEQPTDGTISIDGRDVT-----GTRAHRRPVNTVFQSY--ALFPHLT 107
Cdd:PRK10419   28 LNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWRGEPLAklnraQRKAFRRDIQMVFQDSisAVNPRKT 107

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054819401 108 VAENVAFGLR---RRREADVEARVAEGLALVELG-HLADRRPALLSGGQQQRVALARALVNRPALLLLDEPLGALDLKLR 183
Cdd:PRK10419  108 VREIIREPLRhllSLDKAERLARASEMLRAVDLDdSVLDKRPPQLSGGQLQRVCLARALAVEPKLLILDEAVSNLDLVLQ 187

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1054819401 184 RQMQLELKRIQTEVGLTFVHVTHDQEEAMTMADTVAVMNRGRI--EQMGPPADLYEHP 239
Cdd:PRK10419  188 AGVIRLLKKLQQQFGTACLFITHDLRLVERFCQRVMVMDNGQIveTQPVGDKLTFSSP 245
ABC_drug_resistance_like cd03264
ABC-type multidrug transport system, ATPase component; The biological function of this family ...
 20-230 5.28e-43

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: 149.27  E-value: 5.28e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054819401  20 LELAAVTKRFGAFVAVDDLTLTVPSGsFFALLGPSGCGKTTTLRMVAGLEQPTDGTISIDGRDVTGTR-AHRRPVNTVFQ 98
Cdd:cd03264     1 LQLENLTKRYGKKRALDGVSLTLGPG-MYGLLGPNGAGKTTLMRILATLTPPSSGTIRIDGQDVLKQPqKLRRRIGYLPQ 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054819401  99 SYALFPHLTVAENVAF--GLRRRREADVEARVAEGLALVELGHLADRRPALLSGGQQQRVALARALVNRPALLLLDEPLG 176
Cdd:cd03264    80 EFGVYPNFTVREFLDYiaWLKGIPSKEVKARVDEVLELVNLGDRAKKKIGSLSGGMRRRVGIAQALVGDPSILIVDEPTA 159

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1054819401 177 ALDLKLRRQMQLELKRIQTEVglTFVHVTHDQEEAMTMADTVAVMNRGRIEQMG 230
Cdd:cd03264   160 GLDPEERIRFRNLLSELGEDR--IVILSTHIVEDVESLCNQVAVLNKGKLVFEG 211
PRK11264 PRK11264
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
 20-249 5.35e-43

putative amino-acid ABC transporter ATP-binding protein YecC; Provisional


Pssm-ID: 183063 [Multi-domain]  Cd Length: 250  Bit Score: 150.29  E-value: 5.35e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054819401  20 LELAAVTKRFGAFVAVDDLTLTVPSGSFFALLGPSGCGKTTTLRMVAGLEQPTDGTI-----SIDGRDVTG-----TRAH 89
Cdd:PRK11264    4 IEVKNLVKKFHGQTVLHGIDLEVKPGEVVAIIGPSGSGKTTLLRCINLLEQPEAGTIrvgdiTIDTARSLSqqkglIRQL 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054819401  90 RRPVNTVFQSYALFPHLTVAENVAFG---LRRRREADVEARVAEGLALVELGHLADRRPALLSGGQQQRVALARALVNRP 166
Cdd:PRK11264   84 RQHVGFVFQNFNLFPHRTVLENIIEGpviVKGEPKEEATARARELLAKVGLAGKETSYPRRLSGGQQQRVAIARALAMRP 163

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054819401 167 ALLLLDEPLGALDLKLRRQMqLELKRIQTEVGLTFVHVTHDQEEAMTMADTVAVMNRGRIEQMGPPADLY---EHPRT-T 242
Cdd:PRK11264  164 EVILFDEPTSALDPELVGEV-LNTIRQLAQEKRTMVIVTHEMSFARDVADRAIFMDQGRIVEQGPAKALFadpQQPRTrQ 242


                  ....*..
gi 1054819401 243 FVANFLG 249
Cdd:PRK11264  243 FLEKFLL 249
PstB COG1117
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ...
 29-240 8.91e-43

ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];


Pssm-ID: 440734 [Multi-domain]  Cd Length: 258  Bit Score: 149.80  E-value: 8.91e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054819401  29 FGAFVAVDDLTLTVPSGSFFALLGPSGCGKTTTLR-------MVAGLEqpTDGTISIDGRDVTGTR----AHRRPVNTVF 97
Cdd:COG1117    21 YGDKQALKDINLDIPENKVTALIGPSGCGKSTLLRclnrmndLIPGAR--VEGEILLDGEDIYDPDvdvvELRRRVGMVF 98

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054819401  98 QSYALFPHlTVAENVAFGLR---RRREADVEARVAEGLALVEL-GHLADR--RPAL-LSGGQQQRVALARALVNRPALLL 170
Cdd:COG1117    99 QKPNPFPK-SIYDNVAYGLRlhgIKSKSELDEIVEESLRKAALwDEVKDRlkKSALgLSGGQQQRLCIARALAVEPEVLL 177

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1054819401 171 LDEPLGALD----LKLRRQMQlELKRiqtevGLTFVHVTHDQEEAMTMADTVAVMNRGRIEQMGPPADLYEHPR 240
Cdd:COG1117   178 MDEPTSALDpistAKIEELIL-ELKK-----DYTIVIVTHNMQQAARVSDYTAFFYLGELVEFGPTEQIFTNPK 245
CeuD COG4604
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ...
 21-235 9.55e-43

ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];


Pssm-ID: 443654 [Multi-domain]  Cd Length: 252  Bit Score: 149.85  E-value: 9.55e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054819401  21 ELAAVTKRFGAFVAVDDLTLTVPSGSFFALLGPSGCGKTTTLRMVAGLEQPTDGTISIDGRDVTGTR----AHRrpVNTV 96
Cdd:COG4604     3 EIKNVSKRYGGKVVLDDVSLTIPKGGITALIGPNGAGKSTLLSMISRLLPPDSGEVLVDGLDVATTPsrelAKR--LAIL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054819401  97 FQSYALFPHLTVAENVAFGlR------RRREADvEARVAEGLALVELGHLADRRPALLSGGQQQRVALARALVNRPALLL 170
Cdd:COG4604    81 RQENHINSRLTVRELVAFG-RfpyskgRLTAED-REIIDEAIAYLDLEDLADRYLDELSGGQRQRAFIAMVLAQDTDYVL 158

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1054819401 171 LDEPLGALDLKLRRQMQLELKRIQTEVGLTFVHVTHDQEEAMTMADTVAVMNRGRIEQMGPPADL 235
Cdd:COG4604   159 LDEPLNNLDMKHSVQMMKLLRRLADELGKTVVIVLHDINFASCYADHIVAMKDGRVVAQGTPEEI 223
3a0107s01c2 TIGR00972
phosphate ABC transporter, ATP-binding protein; This model represents the ATP-binding protein ...
 25-240 2.99e-42

phosphate ABC transporter, ATP-binding protein; This model represents the ATP-binding protein of a family of ABC transporters for inorganic phosphate. In the model species Escherichia coli, a constitutive transporter for inorganic phosphate, with low affinity, is also present. The high affinity transporter that includes this polypeptide is induced when extracellular phosphate concentrations are low. The proteins most similar to the members of this family but not included appear to be amino acid transporters. [Transport and binding proteins, Anions]


Pssm-ID: 273372 [Multi-domain]  Cd Length: 247  Bit Score: 148.21  E-value: 2.99e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054819401  25 VTKRFGAFVAVDDLTLTVPSGSFFALLGPSGCGKTTTLR----MVAGLE-QPTDGTISIDGRDVTGTR----AHRRPVNT 95
Cdd:TIGR00972   7 LNLFYGEKEALKNINLDIPKNQVTALIGPSGCGKSTLLRslnrMNDLVPgVRIEGKVLFDGQDIYDKKidvvELRRRVGM 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054819401  96 VFQSYALFPhLTVAENVAFGLR---RRREADVEARVAEGLALVEL-GHLADR--RPAL-LSGGQQQRVALARALVNRPAL 168
Cdd:TIGR00972  87 VFQKPNPFP-MSIYDNIAYGPRlhgIKDKKELDEIVEESLKKAALwDEVKDRlhDSALgLSGGQQQRLCIARALAVEPEV 165

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1054819401 169 LLLDEPLGALD----LKLRRQMQlELKRiqtevGLTFVHVTHDQEEAMTMADTVAVMNRGRIEQMGPPADLYEHPR 240
Cdd:TIGR00972 166 LLLDEPTSALDpiatGKIEELIQ-ELKK-----KYTIVIVTHNMQQAARISDRTAFFYDGELVEYGPTEQIFTNPK 235
nickel_nikE TIGR02769
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a ...
 35-239 4.72e-42

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: 148.41  E-value: 4.72e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054819401  35 VDDLTLTVPSGSFFALLGPSGCGKTTTLRMVAGLEQPTDGTISIDGRDVT-----GTRAHRRPVNTVFQ-SYALF-PHLT 107
Cdd:TIGR02769  27 LTNVSLSIEEGETVGLLGRSGCGKSTLARLLLGLEKPAQGTVSFRGQDLYqldrkQRRAFRRDVQLVFQdSPSAVnPRMT 106

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054819401 108 VAENVAFGLR---RRREADVEARVAEGLALVEL-GHLADRRPALLSGGQQQRVALARALVNRPALLLLDEPLGALDLKLR 183
Cdd:TIGR02769 107 VRQIIGEPLRhltSLDESEQKARIAELLDMVGLrSEDADKLPRQLSGGQLQRINIARALAVKPKLIVLDEAVSNLDMVLQ 186

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1054819401 184 RQMQLELKRIQTEVGLTFVHVTHDQEEAMTMADTVAVMNRGRIEQMGPPADL--YEHP 239
Cdd:TIGR02769 187 AVILELLRKLQQAFGTAYLFITHDLRLVQSFCQRVAVMDKGQIVEECDVAQLlsFKHP 244
PhnK COG1101
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ...
 20-226 2.31e-41

ABC-type uncharacterized transport system, ATPase component [General function prediction only];


Pssm-ID: 440718 [Multi-domain]  Cd Length: 264  Bit Score: 146.38  E-value: 2.31e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054819401  20 LELAAVTKRFGA-----FVAVDDLTLTVPSGSFFALLGPSGCGKTTTLRMVAGLEQPTDGTISIDGRDVTGTRAHRRP-- 92
Cdd:COG1101     2 LELKNLSKTFNPgtvneKRALDGLNLTIEEGDFVTVIGSNGAGKSTLLNAIAGSLPPDSGSILIDGKDVTKLPEYKRAky 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054819401  93 VNTVFQSYAL--FPHLTVAENVA--------FGLRRRREADVEARVAEGLALVELGhLADR---RPALLSGGQQQRVALA 159
Cdd:COG1101    82 IGRVFQDPMMgtAPSMTIEENLAlayrrgkrRGLRRGLTKKRRELFRELLATLGLG-LENRldtKVGLLSGGQRQALSLL 160

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1054819401 160 RALVNRPALLLLDEPLGALDLKlRRQMQLEL-KRIQTEVGLTFVHVTHDQEEAMTMADTVAVMNRGRI 226
Cdd:COG1101   161 MATLTKPKLLLLDEHTAALDPK-TAALVLELtEKIVEENNLTTLMVTHNMEQALDYGNRLIMMHEGRI 227
cbiO PRK13634
cobalt transporter ATP-binding subunit; Provisional
 34-239 1.07e-40

cobalt transporter ATP-binding subunit; Provisional


Pssm-ID: 237454 [Multi-domain]  Cd Length: 290  Bit Score: 145.55  E-value: 1.07e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054819401  34 AVDDLTLTVPSGSFFALLGPSGCGKTTTLRMVAGLEQPTDGTISIDGRDVTGT------RAHRRPVNTVFQ--SYALFPH 105
Cdd:PRK13634   22 ALYDVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVTIGERVITAGkknkklKPLRKKVGIVFQfpEHQLFEE 101

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054819401 106 lTVAENVAFGLRR--RREADVEARVAEGLALVELGH-LADRRPALLSGGQQQRVALARALVNRPALLLLDEPLGALDLKL 182
Cdd:PRK13634  102 -TVEKDICFGPMNfgVSEEDAKQKAREMIELVGLPEeLLARSPFELSGGQMRRVAIAGVLAMEPEVLVLDEPTAGLDPKG 180

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1054819401 183 RRQMQLELKRIQTEVGLTFVHVTHDQEEAMTMADTVAVMNRGRIEQMGPPADLYEHP 239
Cdd:PRK13634  181 RKEMMEMFYKLHKEKGLTTVLVTHSMEDAARYADQIVVMHKGTVFLQGTPREIFADP 237
PRK10070 PRK10070
proline/glycine betaine ABC transporter ATP-binding protein ProV;
8-248 1.63e-40

proline/glycine betaine ABC transporter ATP-binding protein ProV;


Pssm-ID: 182221 [Multi-domain]  Cd Length: 400  Bit Score: 147.87  E-value: 1.63e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054819401   8 HPGAASASAGAALELAAVTKRFGAFVAVDDLTLTVPSGSFFALLGPSGCGKTTTLRMVAGLEQPTDGTISIDGRDVTGT- 86
Cdd:PRK10070   17 HPQRAFKYIEQGLSKEQILEKTGLSLGVKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAKIs 96

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054819401  87 -----RAHRRPVNTVFQSYALFPHLTVAENVAFGLRRRREADVEAR--VAEGLALVELGHLADRRPALLSGGQQQRVALA 159
Cdd:PRK10070   97 daelrEVRRKKIAMVFQSFALMPHMTVLDNTAFGMELAGINAEERRekALDALRQVGLENYAHSYPDELSGGMRQRVGLA 176

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054819401 160 RALVNRPALLLLDEPLGALDLKLRRQMQLELKRIQTEVGLTFVHVTHDQEEAMTMADTVAVMNRGRIEQMGPPADLYEHP 239
Cdd:PRK10070  177 RALAINPDILLMDEAFSALDPLIRTEMQDELVKLQAKHQRTIVFISHDLDEAMRIGDRIAIMQNGEVVQVGTPDEILNNP 256


                  ....*....
gi 1054819401 240 RTTFVANFL 248
Cdd:PRK10070  257 ANDYVRTFF 265
urea_trans_UrtE TIGR03410
urea ABC transporter, ATP-binding protein UrtE; Members of this protein family are ABC ...
 20-235 2.05e-40

urea ABC transporter, ATP-binding protein UrtE; Members of this protein family are ABC transporter ATP-binding subunits associated with urea transport and metabolism. This protein is found in a conserved five-gene transport operon typically found adjacent to urease genes. It was shown in Cyanobacteria that disruption leads to the loss of high-affinity urea transport activity. [Transport and binding proteins, Amino acids, peptides and amines]


Pssm-ID: 274567 [Multi-domain]  Cd Length: 230  Bit Score: 143.05  E-value: 2.05e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054819401  20 LELAAVTKRFGAFVAVDDLTLTVPSGSFFALLGPSGCGKTTTLRMVAGLEQPTDGTISIDGRDVTGTRAHRRP---VNTV 96
Cdd:TIGR03410   1 LEVSNLNVYYGQSHILRGVSLEVPKGEVTCVLGRNGVGKTTLLKTLMGLLPVKSGSIRLDGEDITKLPPHERAragIAYV 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054819401  97 FQSYALFPHLTVAENVAFGL--RRRREADVEARVAEgLALVeLGHLADRRPALLSGGQQQRVALARALVNRPALLLLDEP 174
Cdd:TIGR03410  81 PQGREIFPRLTVEENLLTGLaaLPRRSRKIPDEIYE-LFPV-LKEMLGRRGGDLSGGQQQQLAIARALVTRPKLLLLDEP 158

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1054819401 175 LGALDLKLRRQMQLELKRIQTEVGLTFVHVTHDQEEAMTMADTVAVMNRGRIEQMGPPADL 235
Cdd:TIGR03410 159 TEGIQPSIIKDIGRVIRRLRAEGGMAILLVEQYLDFARELADRYYVMERGRVVASGAGDEL 219
cbiO PRK13635
energy-coupling factor ABC transporter ATP-binding protein;
34-238 2.99e-40

energy-coupling factor ABC transporter ATP-binding protein;


Pssm-ID: 184195 [Multi-domain]  Cd Length: 279  Bit Score: 144.00  E-value: 2.99e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054819401  34 AVDDLTLTVPSGSFFALLGPSGCGKTTTLRMVAGLEQPTDGTISIDGRDVTGTRAH--RRPVNTVFQSY-ALFPHLTVAE 110
Cdd:PRK13635   22 ALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGGMVLSEETVWdvRRQVGMVFQNPdNQFVGATVQD 101

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054819401 111 NVAFGLRRR---READVEaRVAEGLALVELGHLADRRPALLSGGQQQRVALARALVNRPALLLLDEPLGALDLKLRRQMQ 187
Cdd:PRK13635  102 DVAFGLENIgvpREEMVE-RVDQALRQVGMEDFLNREPHRLSGGQKQRVAIAGVLALQPDIIILDEATSMLDPRGRREVL 180

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1054819401 188 LELKRIQTEVGLTFVHVTHDQEEAMTmADTVAVMNRGRIEQMGPPADLYEH 238
Cdd:PRK13635  181 ETVRQLKEQKGITVLSITHDLDEAAQ-ADRVIVMNKGEILEEGTPEEIFKS 230
modC PRK11144
molybdenum ABC transporter ATP-binding protein ModC;
20-239 4.42e-40

molybdenum ABC transporter ATP-binding protein ModC;


Pssm-ID: 182993 [Multi-domain]  Cd Length: 352  Bit Score: 145.40  E-value: 4.42e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054819401  20 LELAaVTKRFGafvavdDLTLTV----PSGSFFALLGPSGCGKTTTLRMVAGLEQPTDGTISIDGRDVTGTR------AH 89
Cdd:PRK11144    2 LELN-FKQQLG------DLCLTVnltlPAQGITAIFGRSGAGKTSLINAISGLTRPQKGRIVLNGRVLFDAEkgiclpPE 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054819401  90 RRPVNTVFQSYALFPHLTVAENVAFGLRRRREADVEARVAeglaLVELGHLADRRPALLSGGQQQRVALARALVNRPALL 169
Cdd:PRK11144   75 KRRIGYVFQDARLFPHYKVRGNLRYGMAKSMVAQFDKIVA----LLGIEPLLDRYPGSLSGGEKQRVAIGRALLTAPELL 150

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054819401 170 LLDEPLGALDLKLRRQMQLELKRIQTEVGLTFVHVTHDQEEAMTMADTVAVMNRGRIEQMGPPADLYEHP 239
Cdd:PRK11144  151 LMDEPLASLDLPRKRELLPYLERLAREINIPILYVSHSLDEILRLADRVVVLEQGKVKAFGPLEEVWASS 220
ABCC_MRP_Like cd03228
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ...
 34-225 5.95e-40

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: 139.83  E-value: 5.95e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054819401  34 AVDDLTLTVPSGSFFALLGPSGCGKTTTLRMVAGLEQPTDGTISIDGRDVTG--TRAHRRPVNTVFQSYALFpHLTVAEN 111
Cdd:cd03228    17 VLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGVDLRDldLESLRKNIAYVPQDPFLF-SGTIREN 95

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054819401 112 vafglrrrreadvearvaeglalvelghladrrpaLLSGGQQQRVALARALVNRPALLLLDEPLGALDLKLRRQMQLELK 191
Cdd:cd03228    96 -----------------------------------ILSGGQRQRIAIARALLRDPPILILDEATSALDPETEALILEALR 140

                         170       180       190
                  ....*....|....*....|....*....|....
gi 1054819401 192 RIQteVGLTFVHVTHDqEEAMTMADTVAVMNRGR 225
Cdd:cd03228   141 ALA--KGKTVIVIAHR-LSTIRDADRIIVLDDGR 171
COG4559 COG4559
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism];
35-234 1.90e-39

ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism];


Pssm-ID: 443620 [Multi-domain]  Cd Length: 258  Bit Score: 141.02  E-value: 1.90e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054819401  35 VDDLTLTVPSGSFFALLGPSGCGKTTTLRMVAGLEQPTDGTISIDGRDVTGT----RAHRRPVntVFQSYAL-FPhLTVA 109
Cdd:COG4559    17 LDDVSLTLRPGELTAIIGPNGAGKSTLLKLLTGELTPSSGEVRLNGRPLAAWspweLARRRAV--LPQHSSLaFP-FTVE 93

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054819401 110 ENVAFGL--RRRREADVEARVAEGLALVELGHLADRRPALLSGGQQQRVALARALV-------NRPALLLLDEPLGALDL 180
Cdd:COG4559    94 EVVALGRapHGSSAAQDRQIVREALALVGLAHLAGRSYQTLSGGEQQRVQLARVLAqlwepvdGGPRWLFLDEPTSALDL 173

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1054819401 181 KLRRQMqLELKRIQTEVGLTFVHVTHDQEEAMTMADTVAVMNRGRIEQMGPPAD 234
Cdd:COG4559   174 AHQHAV-LRLARQLARRGGGVVAVLHDLNLAAQYADRILLLHQGRLVAQGTPEE 226
hmuV PRK13548
hemin importer ATP-binding subunit; Provisional
 20-234 7.95e-39

hemin importer ATP-binding subunit; Provisional


Pssm-ID: 237422 [Multi-domain]  Cd Length: 258  Bit Score: 139.52  E-value: 7.95e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054819401  20 LELAAVTKRFGAFVAVDDLTLTVPSGSFFALLGPSGCGKTTTLRMVAGLEQPTDGTISIDGRDVTGT----RAHRRPVnt 95
Cdd:PRK13548    3 LEARNLSVRLGGRTLLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLNGRPLADWspaeLARRRAV-- 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054819401  96 VFQSYAL-FPhLTVAENVAFGL--RRRREADVEARVAEGLALVELGHLADRRPALLSGGQQQRVALARALV------NRP 166
Cdd:PRK13548   81 LPQHSSLsFP-FTVEEVVAMGRapHGLSRAEDDALVAAALAQVDLAHLAGRDYPQLSGGEQQRVQLARVLAqlwepdGPP 159

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1054819401 167 ALLLLDEPLGALDlkLRRQ---MQLeLKRIQTEVGLTFVHVTHDQEEAMTMADTVAVMNRGRIEQMGPPAD 234
Cdd:PRK13548  160 RWLLLDEPTSALD--LAHQhhvLRL-ARQLAHERGLAVIVVLHDLNLAARYADRIVLLHQGRLVADGTPAE 227
cbiO PRK13650
energy-coupling factor transporter ATPase;
35-236 1.02e-38

energy-coupling factor transporter ATPase;


Pssm-ID: 184209 [Multi-domain]  Cd Length: 279  Bit Score: 139.87  E-value: 1.02e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054819401  35 VDDLTLTVPSGSFFALLGPSGCGKTTTLRMVAGLEQPTDGTISIDGRDVTGTRAH--RRPVNTVFQSY-ALFPHLTVAEN 111
Cdd:PRK13650   23 LNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIIDGDLLTEENVWdiRHKIGMVFQNPdNQFVGATVEDD 102

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054819401 112 VAFGLRRR--READVEARVAEGLALVELGHLADRRPALLSGGQQQRVALARALVNRPALLLLDEPLGALDLKLRRQMQLE 189
Cdd:PRK13650  103 VAFGLENKgiPHEEMKERVNEALELVGMQDFKEREPARLSGGQKQRVAIAGAVAMRPKIIILDEATSMLDPEGRLELIKT 182

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 1054819401 190 LKRIQTEVGLTFVHVTHDQEEaMTMADTVAVMNRGRIEQMGPPADLY 236
Cdd:PRK13650  183 IKGIRDDYQMTVISITHDLDE-VALSDRVLVMKNGQVESTSTPRELF 228
L_ocin_972_ABC TIGR03608
putative bacteriocin export ABC transporter, lactococcin 972 group; A gene pair with a fairly ...
 25-218 1.19e-38

putative bacteriocin export ABC transporter, lactococcin 972 group; A gene pair with a fairly wide distribution consists of a polypeptide related to the lactococcin 972 (see TIGR01653) and multiple-membrane-spanning putative immunity protein (see TIGR01654). This model represents a small clade within the ABC transporters that regularly are found adjacent to these bacteriocin system gene pairs and are likely serve as export proteins. [Cellular processes, Toxin production and resistance, Transport and binding proteins, Unknown substrate]


Pssm-ID: 188353 [Multi-domain]  Cd Length: 206  Bit Score: 137.36  E-value: 1.19e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054819401  25 VTKRFGAFVAVDDLTLTVPSGSFFALLGPSGCGKTTTLRMVAGLEQPTDGTISIDGRD---VTGTRAH---RRPVNTVFQ 98
Cdd:TIGR03608   4 ISKKFGDKVILDDLNLTIEKGKMYAIIGESGSGKSTLLNIIGLLEKFDSGQVYLNGQEtppLNSKKASkfrREKLGYLFQ 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054819401  99 SYALFPHLTVAEN--VAFGLRRRREADVEARVAEGLALVELGHLADRRPALLSGGQQQRVALARALVNRPALLLLDEPLG 176
Cdd:TIGR03608  84 NFALIENETVEENldLGLKYKKLSKKEKREKKKEALEKVGLNLKLKQKIYELSGGEQQRVALARAILKPPPLILADEPTG 163

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 1054819401 177 ALDLKlRRQMQLELKRIQTEVGLTFVHVTHDQEEAmTMADTV 218
Cdd:TIGR03608 164 SLDPK-NRDEVLDLLLELNDEGKTIIIVTHDPEVA-KQADRV 203
CydD COG4988
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ...
 20-238 1.33e-38

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: 145.29  E-value: 1.33e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054819401  20 LELAAVTKRF-GAFVAVDDLTLTVPSGSFFALLGPSGCGKTTTLRMVAGLEQPTDGTISIDGRDVTGTRAH--RRPVNTV 96
Cdd:COG4988   337 IELEDVSFSYpGGRPALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPPYSGSILINGVDLSDLDPAswRRQIAWV 416

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054819401  97 FQSYALFpHLTVAENVAFGlrrRREADvEARVAEGLALVELGHLADRRP-----------ALLSGGQQQRVALARALVNR 165
Cdd:COG4988   417 PQNPYLF-AGTIRENLRLG---RPDAS-DEELEAALEAAGLDEFVAALPdgldtplgeggRGLSGGQAQRLALARALLRD 491

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1054819401 166 PALLLLDEPLGALDLKLRRQMQLELKRIQTevGLTFVHVTHDqEEAMTMADTVAVMNRGRIEQMGPPADLYEH 238
Cdd:COG4988   492 APLLLLDEPTAHLDAETEAEILQALRRLAK--GRTVILITHR-LALLAQADRILVLDDGRIVEQGTHEELLAK 561
ABC_Carb_Monos_I cd03216
First domain of the ATP-binding cassette component of monosaccharide transport system; This ...
 20-226 2.49e-38

First domain of the ATP-binding cassette component of monosaccharide transport system; This family represents the domain I of the carbohydrate uptake proteins that transport only monosaccharides (Monos). The Carb_Monos family is involved in the uptake of monosaccharides, such as pentoses (such as xylose, arabinose, and ribose) and hexoses (such as xylose, arabinose, and ribose), that cannot be broken down to simple sugars by hydrolysis. Pentoses include xylose, arabinose, and ribose. Important hexoses include glucose, galactose, and fructose. In members of the Carb_monos family, the single hydrophobic gene product forms a homodimer while the ABC protein represents a fusion of two nucleotide-binding domains. However, it is assumed that two copies of the ABC domains are present in the assembled transporter.


Pssm-ID: 213183 [Multi-domain]  Cd Length: 163  Bit Score: 135.25  E-value: 2.49e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054819401  20 LELAAVTKRFGAFVAVDDLTLTVPSGSFFALLGPSGCGKTTTLRMVAGLEQPTDGTISIDGRDVTG---TRAHRRPVNTV 96
Cdd:cd03216     1 LELRGITKRFGGVKALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVDGKEVSFaspRDARRAGIAMV 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054819401  97 FQsyalfphltvaenvafglrrrreadvearvaeglalvelghladrrpalLSGGQQQRVALARALVNRPALLLLDEPLG 176
Cdd:cd03216    81 YQ-------------------------------------------------LSVGERQMVEIARALARNARLLILDEPTA 111

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 1054819401 177 ALDLKLRRQMQLELKRIQTEvGLTFVHVTHDQEEAMTMADTVAVMNRGRI 226
Cdd:cd03216   112 ALTPAEVERLFKVIRRLRAQ-GVAVIFISHRLDEVFEIADRVTVLRDGRV 160
dppF PRK11308
dipeptide transporter ATP-binding subunit; Provisional
 34-240 2.68e-38

dipeptide transporter ATP-binding subunit; Provisional


Pssm-ID: 236898 [Multi-domain]  Cd Length: 327  Bit Score: 140.10  E-value: 2.68e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054819401  34 AVDDLTLTVPSGSFFALLGPSGCGKTTTLRMVAGLEQPTDGTISIDGRDVTGT-----RAHRRPVNTVFQS-YA-LFPHL 106
Cdd:PRK11308   30 ALDGVSFTLERGKTLAVVGESGCGKSTLARLLTMIETPTGGELYYQGQDLLKAdpeaqKLLRQKIQIVFQNpYGsLNPRK 109

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054819401 107 TVAE--------NVAFGLRRRREadveaRVAEGLALVELG--HlADRRPALLSGGQQQRVALARALVNRPALLLLDEPLG 176
Cdd:PRK11308  110 KVGQileeplliNTSLSAAERRE-----KALAMMAKVGLRpeH-YDRYPHMFSGGQRQRIAIARALMLDPDVVVADEPVS 183

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1054819401 177 ALDLKLRRQMQLELKRIQTEVGLTFVHVTHDQEEAMTMADTVAVMNRGRIEQMGPPADLYEHPR 240
Cdd:PRK11308  184 ALDVSVQAQVLNLMMDLQQELGLSYVFISHDLSVVEHIADEVMVMYLGRCVEKGTKEQIFNNPR 247
NupO COG3845
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ...
 20-225 3.41e-38

ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];


Pssm-ID: 443055 [Multi-domain]  Cd Length: 504  Bit Score: 143.63  E-value: 3.41e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054819401  20 LELAAVTKRFGAFVAVDDLTLTVPSGSFFALLGPSGCGKTTTLRMVAGLEQPTDGTISIDGRDVTGT---RAHRRPVNTV 96
Cdd:COG3845     6 LELRGITKRFGGVVANDDVSLTVRPGEIHALLGENGAGKSTLMKILYGLYQPDSGEILIDGKPVRIRsprDAIALGIGMV 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054819401  97 FQSYALFPHLTVAENVAFGLRRRRE-----ADVEARVAE-----GLAlVELghlaDRRPALLSGGQQQRVALARALVNRP 166
Cdd:COG3845    86 HQHFMLVPNLTVAENIVLGLEPTKGgrldrKAARARIRElseryGLD-VDP----DAKVEDLSVGEQQRVEILKALYRGA 160

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054819401 167 ALLLLDEPLGAL------DL-----KLRRQmqlelkriqtevGLTFVHVTHDQEEAMTMADTVAVMNRGR 225
Cdd:COG3845   161 RILILDEPTAVLtpqeadELfeilrRLAAE------------GKSIIFITHKLREVMAIADRVTVLRRGK 218
livG PRK11300
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
 20-240 1.67e-37

leucine/isoleucine/valine transporter ATP-binding subunit; Provisional


Pssm-ID: 183080 [Multi-domain]  Cd Length: 255  Bit Score: 135.89  E-value: 1.67e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054819401  20 LELAAVTKRFGAFVAVDDLTLTVPSGSFFALLGPSGCGKTTTLRMVAGLEQPTDGTISIDGRDVTGTRAH---RRPVNTV 96
Cdd:PRK11300    6 LSVSGLMMRFGGLLAVNNVNLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTILLRGQHIEGLPGHqiaRMGVVRT 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054819401  97 FQSYALFPHLTVAEN--VA----------FGL-----RRRREADVEARVAEGLALVELGHLADRRPALLSGGQQQRVALA 159
Cdd:PRK11300   86 FQHVRLFREMTVIENllVAqhqqlktglfSGLlktpaFRRAESEALDRAATWLERVGLLEHANRQAGNLAYGQQRRLEIA 165

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054819401 160 RALVNRPALLLLDEPLGALDLKLRRQMQLELKRIQTEVGLTFVHVTHDQEEAMTMADTVAVMNRGRIEQMGPPADLYEHP 239
Cdd:PRK11300  166 RCMVTQPEILMLDEPAAGLNPKETKELDELIAELRNEHNVTVLLIEHDMKLVMGISDRIYVVNQGTPLANGTPEEIRNNP 245


                  .
gi 1054819401 240 R 240
Cdd:PRK11300  246 D 246
heterocyst_DevA TIGR02982
ABC exporter ATP-binding subunit, DevA family; Members of this protein family are found mostly ...
 37-226 1.87e-37

ABC exporter ATP-binding subunit, DevA family; Members of this protein family are found mostly in the Cyanobacteria, but also in the Planctomycetes. Cyanobacterial examples are involved in heterocyst formation, by which some fraction of members of the colony undergo a developmental change and become capable of nitrogen fixation. The DevBCA proteins are thought export of either heterocyst-specific glycolipids or an enzyme essential for formation of the laminated layer found in heterocysts.


Pssm-ID: 274374 [Multi-domain]  Cd Length: 220  Bit Score: 134.76  E-value: 1.87e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054819401  37 DLTLTVPSGSFFALLGPSGCGKTTTLRMVAGLEQPTDGTISIDGRDVTGTRAH-----RRPVNTVFQSYALFPHLTVAEN 111
Cdd:TIGR02982  23 DINLEINPGEIVILTGPSGSGKTTLLTLIGGLRSVQEGSLKVLGQELHGASKKqlvqlRRRIGYIFQAHNLLGFLTARQN 102

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054819401 112 VAFGLRRRRE---ADVEARVAEGLALVELGHLADRRPALLSGGQQQRVALARALVNRPALLLLDEPLGALDLKLRRQMQL 188
Cdd:TIGR02982 103 VQMALELQPNlsyQEARERARAMLEAVGLGDHLNYYPHNLSGGQKQRVAIARALVHHPKLVLADEPTAALDSKSGRDVVE 182

                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 1054819401 189 ELKRIQTEVGLTFVHVTHDQeEAMTMADTVAVMNRGRI 226
Cdd:TIGR02982 183 LMQKLAKEQGCTILMVTHDN-RILDVADRILQMEDGKL 219
PRK10619 PRK10619
histidine ABC transporter ATP-binding protein HisP;
20-248 2.94e-37

histidine ABC transporter ATP-binding protein HisP;


Pssm-ID: 182592 [Multi-domain]  Cd Length: 257  Bit Score: 135.48  E-value: 2.94e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054819401  20 LELAAVTKRFGAFVAVDDLTLTVPSGSFFALLGPSGCGKTTTLRMVAGLEQPTDGTISIDGRDVTGTRAH---------- 89
Cdd:PRK10619    6 LNVIDLHKRYGEHEVLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNGQTINLVRDKdgqlkvadkn 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054819401  90 -----RRPVNTVFQSYALFPHLTVAENV------AFGLRRrreADVEARVAEGLALVELGHLA-DRRPALLSGGQQQRVA 157
Cdd:PRK10619   86 qlrllRTRLTMVFQHFNLWSHMTVLENVmeapiqVLGLSK---QEARERAVKYLAKVGIDERAqGKYPVHLSGGQQQRVS 162

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054819401 158 LARALVNRPALLLLDEPLGALDLKLRRQMqLELKRIQTEVGLTFVHVTHDQEEAMTMADTVAVMNRGRIEQMGPPADLYE 237
Cdd:PRK10619  163 IARALAMEPEVLLFDEPTSALDPELVGEV-LRIMQQLAEEGKTMVVVTHEMGFARHVSSHVIFLHQGKIEEEGAPEQLFG 241

                         250
                  ....*....|.
gi 1054819401 238 HPRTTFVANFL 248
Cdd:PRK10619  242 NPQSPRLQQFL 252
MglA COG1129
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
20-235 3.04e-37

ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];


Pssm-ID: 440745 [Multi-domain]  Cd Length: 497  Bit Score: 140.54  E-value: 3.04e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054819401  20 LELAAVTKRFGAFVAVDDLTLTVPSGSFFALLGPSGCGKTTTLRMVAGLEQPTDGTISIDGRDVTGT---RAHRRPVNTV 96
Cdd:COG1129     5 LEMRGISKSFGGVKALDGVSLELRPGEVHALLGENGAGKSTLMKILSGVYQPDSGEILLDGEPVRFRsprDAQAAGIAII 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054819401  97 FQSYALFPHLTVAENVAFG--LRRR---READVEARVAEGLALVELGHLADRRPALLSGGQQQRVALARALVNRPALLLL 171
Cdd:COG1129    85 HQELNLVPNLSVAENIFLGrePRRGgliDWRAMRRRARELLARLGLDIDPDTPVGDLSVAQQQLVEIARALSRDARVLIL 164

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1054819401 172 DEPLGALDLK----LRRQMQlELKriqtEVGLTFVHVTHDQEEAMTMADTVAVMNRGRIEQMGPPADL 235
Cdd:COG1129   165 DEPTASLTEReverLFRIIR-RLK----AQGVAIIYISHRLDEVFEIADRVTVLRDGRLVGTGPVAEL 227
ModF COG1119
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ...
 20-235 4.07e-37

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: 134.83  E-value: 4.07e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054819401  20 LELAAVTKRFGAFVAVDDLTLTVPSGSFFALLGPSGCGKTTTLRMVAGLEQPTDG-TISIDGRDVTGT--RAHRRP---V 93
Cdd:COG1119     4 LELRNVTVRRGGKTILDDISWTVKPGEHWAILGPNGAGKSTLLSLITGDLPPTYGnDVRLFGERRGGEdvWELRKRiglV 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054819401  94 NTVFQSYaLFPHLTVAENVA------FGLRRRREADVEARVAEGLALVELGHLADRRPALLSGGQQQRVALARALVNRPA 167
Cdd:COG1119    84 SPALQLR-FPRDETVLDVVLsgffdsIGLYREPTDEQRERARELLELLGLAHLADRPFGTLSQGEQRRVLIARALVKDPE 162

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1054819401 168 LLLLDEPLGALDLKLRRQMQLELKRIQTEVGLTFVHVTHDQEEAMTMADTVAVMNRGRIEQMGPPADL 235
Cdd:COG1119   163 LLILDEPTAGLDLGARELLLALLDKLAAEGAPTLVLVTHHVEEIPPGITHVLLLKDGRVVAAGPKEEV 230
PRK13536 PRK13536
nodulation factor ABC transporter ATP-binding protein NodI;
20-237 1.87e-36

nodulation factor ABC transporter ATP-binding protein NodI;


Pssm-ID: 237419 [Multi-domain]  Cd Length: 340  Bit Score: 135.73  E-value: 1.87e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054819401  20 LELAAVTKRFGAFVAVDDLTLTVPSGSFFALLGPSGCGKTTTLRMVAGLEQPTDGTISIDGRDVTG-TRAHRRPVNTVFQ 98
Cdd:PRK13536   42 IDLAGVSKSYGDKAVVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKITVLGVPVPArARLARARIGVVPQ 121

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054819401  99 SYALFPHLTVAENVA-----FGLRRRreaDVEARVAEGLALVELGHLADRRPALLSGGQQQRVALARALVNRPALLLLDE 173
Cdd:PRK13536  122 FDNLDLEFTVRENLLvfgryFGMSTR---EIEAVIPSLLEFARLESKADARVSDLSGGMKRRLTLARALINDPQLLILDE 198

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1054819401 174 PLGALDLKLRRQMQLELKRIQTEvGLTFVHVTHDQEEAMTMADTVAVMNRGRIEQMGPPADLYE 237
Cdd:PRK13536  199 PTTGLDPHARHLIWERLRSLLAR-GKTILLTTHFMEEAERLCDRLCVLEAGRKIAEGRPHALID 261
ABC_YhbG cd03218
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ...
 20-239 4.11e-36

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: 131.51  E-value: 4.11e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054819401  20 LELAAVTKRFGAFVAVDDLTLTVPSGSFFALLGPSGCGKTTTLRMVAGLEQPTDGTISIDGRDVTGTRAHRR-------- 91
Cdd:cd03218     1 LRAENLSKRYGKRKVVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDGQDITKLPMHKRarlgigyl 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054819401  92 PvntvfQSYALFPHLTVAENVAFGLRRRREADVEA--RVAEGLALVELGHLADRRPALLSGGQQQRVALARALVNRPALL 169
Cdd:cd03218    81 P-----QEASIFRKLTVEENILAVLEIRGLSKKEReeKLEELLEEFHITHLRKSKASSLSGGERRRVEIARALATNPKFL 155

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054819401 170 LLDEPLGALDLKLRRQMQlELKRIQTEVGLTFVHVTHDQEEAMTMADTVAVMNRGRIEQMGPPADLYEHP 239
Cdd:cd03218   156 LLDEPFAGVDPIAVQDIQ-KIIKILKDRGIGVLITDHNVRETLSITDRAYIIYEGKVLAEGTPEEIAANE 224
ABC_cobalt_CbiO_domain2 cd03226
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ...
 35-226 9.89e-36

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: 129.68  E-value: 9.89e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054819401  35 VDDLTLTVPSGSFFALLGPSGCGKTTTLRMVAGLEQPTDGTISIDGRDVtGTRAHRRPVNTVFQS--YALFPHlTVAENV 112
Cdd:cd03226    16 LDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLNGKPI-KAKERRKSIGYVMQDvdYQLFTD-SVREEL 93

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054819401 113 AFGLRRRreADVEARVAEGLALVELGHLADRRPALLSGGQQQRVALARALVNRPALLLLDEPLGALDlklRRQMQL--EL 190
Cdd:cd03226    94 LLGLKEL--DAGNEQAETVLKDLDLYALKERHPLSLSGGQKQRLAIAAALLSGKDLLIFDEPTSGLD---YKNMERvgEL 168

                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 1054819401 191 KRIQTEVGLTFVHVTHDQEEAMTMADTVAVMNRGRI 226
Cdd:cd03226   169 IRELAAQGKAVIVITHDYEFLAKVCDRVLLLANGAI 204
PRK13537 PRK13537
nodulation factor ABC transporter ATP-binding protein NodI;
20-238 1.45e-35

nodulation factor ABC transporter ATP-binding protein NodI;


Pssm-ID: 237420 [Multi-domain]  Cd Length: 306  Bit Score: 132.24  E-value: 1.45e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054819401  20 LELAAVTKRFGAFVAVDDLTLTVPSGSFFALLGPSGCGKTTTLRMVAGLEQPTDGTISIDGRDVTGtRAH--RRPVNTVF 97
Cdd:PRK13537    8 IDFRNVEKRYGDKLVVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCGEPVPS-RARhaRQRVGVVP 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054819401  98 QSYALFPHLTVAENVA-----FGLrrrREADVEARVAEGLALVELGHLADRRPALLSGGQQQRVALARALVNRPALLLLD 172
Cdd:PRK13537   87 QFDNLDPDFTVRENLLvfgryFGL---SAAAARALVPPLLEFAKLENKADAKVGELSGGMKRRLTLARALVNDPDVLVLD 163

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1054819401 173 EPLGALDLKLRRQMQLELKRIQTEvGLTFVHVTHDQEEAMTMADTVAVMNRGRIEQMGPPADLYEH 238
Cdd:PRK13537  164 EPTTGLDPQARHLMWERLRSLLAR-GKTILLTTHFMEEAERLCDRLCVIEEGRKIAEGAPHALIES 228
ABC_MTABC3_MDL1_MDL2 cd03249
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ...
 36-237 2.40e-35

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: 129.58  E-value: 2.40e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054819401  36 DDLTLTVPSGSFFALLGPSGCGKTTTLRMVAGLEQPTDGTISIDGRDVT--GTRAHRRPVNTVFQSYALFPhLTVAENVA 113
Cdd:cd03249    20 KGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEILLDGVDIRdlNLRWLRSQIGLVSQEPVLFD-GTIAENIR 98

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054819401 114 FGLRRRREADVE--ARVAEGLALVELghLADR-------RPALLSGGQQQRVALARALVNRPALLLLDEPLGALDLKLRR 184
Cdd:cd03249    99 YGKPDATDEEVEeaAKKANIHDFIMS--LPDGydtlvgeRGSQLSGGQKQRIAIARALLRNPKILLLDEATSALDAESEK 176

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1054819401 185 QMQLELKRIQteVGLTFVHVTHdQEEAMTMADTVAVMNRGRIEQMGPPADLYE 237
Cdd:cd03249   177 LVQEALDRAM--KGRTTIVIAH-RLSTIRNADLIAVLQNGQVVEQGTHDELMA 226
SapF COG4167
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms];
20-241 2.66e-35

ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms];


Pssm-ID: 443328 [Multi-domain]  Cd Length: 265  Bit Score: 130.34  E-value: 2.66e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054819401  20 LELAAVTKRF---------GAFVAVDDLTLTVPSGSFFALLGPSGCGKTTTLRMVAGLEQPTDGTISIDGRDVT-GTRAH 89
Cdd:COG4167     5 LEVRNLSKTFkyrtglfrrQQFEAVKPVSFTLEAGQTLAIIGENGSGKSTLAKMLAGIIEPTSGEILINGHKLEyGDYKY 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054819401  90 R-RPVNTVFQ--SYALFPHLTVAENVAFGLRRRREADVEAR---VAEGLALVEL--GHlADRRPALLSGGQQQRVALARA 161
Cdd:COG4167    85 RcKHIRMIFQdpNTSLNPRLNIGQILEEPLRLNTDLTAEEReerIFATLRLVGLlpEH-ANFYPHMLSSGQKQRVALARA 163

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054819401 162 LVNRPALLLLDEPLGALDLKLRRQM---QLELkriQTEVGLTFVHVTHDQEEAMTMADTVAVMNRGRIEQMGPPADLYEH 238
Cdd:COG4167   164 LILQPKIIIADEALAALDMSVRSQIinlMLEL---QEKLGISYIYVSQHLGIVKHISDKVLVMHQGEVVEYGKTAEVFAN 240


                  ...
gi 1054819401 239 PRT 241
Cdd:COG4167   241 PQH 243
MdlB COG1132
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
34-235 4.82e-35

ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];


Pssm-ID: 440747 [Multi-domain]  Cd Length: 579  Bit Score: 135.68  E-value: 4.82e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054819401  34 AVDDLTLTVPSGSFFALLGPSGCGKTTTLRMVAGLEQPTDGTISIDGRDVT--GTRAHRRPVNTVFQSYALFpHLTVAEN 111
Cdd:COG1132   355 VLKDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYDPTSGRILIDGVDIRdlTLESLRRQIGVVPQDTFLF-SGTIREN 433

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054819401 112 VAFGlrrRREADvEARVAEGLALVELGHLADRRP-----------ALLSGGQQQRVALARALVNRPALLLLDEPLGALDL 180
Cdd:COG1132   434 IRYG---RPDAT-DEEVEEAAKAAQAHEFIEALPdgydtvvgergVNLSGGQRQRIAIARALLKDPPILILDEATSALDT 509

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1054819401 181 KLRRQMQLELKRIQTevGLTFVHVTH------DqeeamtmADTVAVMNRGRIEQMGPPADL 235
Cdd:COG1132   510 ETEALIQEALERLMK--GRTTIVIAHrlstirN-------ADRILVLDDGRIVEQGTHEEL 561
LptB COG1137
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ...
 20-240 7.92e-35

ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 440752 [Multi-domain]  Cd Length: 240  Bit Score: 128.22  E-value: 7.92e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054819401  20 LELAAVTKRFGAFVAVDDLTLTVPSGSFFALLGPSGCGKTTTLRMVAGLEQPTDGTISIDGRDVTGTRAHRR-------- 91
Cdd:COG1137     4 LEAENLVKSYGKRTVVKDVSLEVNQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGRIFLDGEDITHLPMHKRarlgigyl 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054819401  92 PvntvfQSYALFPHLTVAENV--AFGLRRRREADVEARVAEGLALVELGHLADRRPALLSGGQQQRVALARALVNRPALL 169
Cdd:COG1137    84 P-----QEASIFRKLTVEDNIlaVLELRKLSKKEREERLEELLEEFGITHLRKSKAYSLSGGERRRVEIARALATNPKFI 158

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1054819401 170 LLDE------PLGALDLKlrrQMQLELKriQTEVGltfVHVT-HDQEEAMTMADTVAVMNRGRIEQMGPPADLYEHPR 240
Cdd:COG1137   159 LLDEpfagvdPIAVADIQ---KIIRHLK--ERGIG---VLITdHNVRETLGICDRAYIISEGKVLAEGTPEEILNNPL 228
fecE PRK11231
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
35-234 8.23e-35

Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;


Pssm-ID: 183044 [Multi-domain]  Cd Length: 255  Bit Score: 128.98  E-value: 8.23e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054819401  35 VDDLTLTVPSGSFFALLGPSGCGKTTTLRMVAGLEQPTDGTISIDGRDVTGTRAHRrpvntVFQSYALFP--HLT----- 107
Cdd:PRK11231   18 LNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDKPISMLSSRQ-----LARRLALLPqhHLTpegit 92

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054819401 108 VAENVAFG------LRRRREADVEARVAEGLALVELGHLADRRPALLSGGQQQRVALARALVNRPALLLLDEPLGALDL- 180
Cdd:PRK11231   93 VRELVAYGrspwlsLWGRLSAEDNARVNQAMEQTRINHLADRRLTDLSGGQRQRAFLAMVLAQDTPVVLLDEPTTYLDIn 172

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054819401 181 ------KLRRQMQLElkriqtevGLTFVHVTHDQEEAMTMADTVAVMNRGRIEQMGPPAD 234
Cdd:PRK11231  173 hqvelmRLMRELNTQ--------GKTVVTVLHDLNQASRYCDHLVVLANGHVMAQGTPEE 224
cbiO PRK13640
energy-coupling factor transporter ATPase;
34-239 1.68e-34

energy-coupling factor transporter ATPase;


Pssm-ID: 184200 [Multi-domain]  Cd Length: 282  Bit Score: 128.76  E-value: 1.68e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054819401  34 AVDDLTLTVPSGSFFALLGPSGCGKTTTLRMVAGLEQPTD---GTISIDGRDVTGTRAH--RRPVNTVFQSY-ALFPHLT 107
Cdd:PRK13640   22 ALNDISFSIPRGSWTALIGHNGSGKSTISKLINGLLLPDDnpnSKITVDGITLTAKTVWdiREKVGIVFQNPdNQFVGAT 101

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054819401 108 VAENVAFGLRRRREADVEAR--VAEGLALVELGHLADRRPALLSGGQQQRVALARALVNRPALLLLDEPLGALDLKLRRQ 185
Cdd:PRK13640  102 VGDDVAFGLENRAVPRPEMIkiVRDVLADVGMLDYIDSEPANLSGGQKQRVAIAGILAVEPKIIILDESTSMLDPAGKEQ 181

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1054819401 186 MQLELKRIQTEVGLTFVHVTHDQEEAmTMADTVAVMNRGRIEQMGPPADLYEHP 239
Cdd:PRK13640  182 ILKLIRKLKKKNNLTVISITHDIDEA-NMADQVLVLDDGKLLAQGSPVEIFSKV 234
PRK14247 PRK14247
phosphate ABC transporter ATP-binding protein; Provisional
 29-240 2.19e-34

phosphate ABC transporter ATP-binding protein; Provisional


Pssm-ID: 172735 [Multi-domain]  Cd Length: 250  Bit Score: 127.72  E-value: 2.19e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054819401  29 FGAFVAVDDLTLTVPSGSFFALLGPSGCGKTTTLRMVAGL-----EQPTDGTISIDGRDV--TGTRAHRRPVNTVFQSYA 101
Cdd:PRK14247   13 FGQVEVLDGVNLEIPDNTITALMGPSGSGKSTLLRVFNRLielypEARVSGEVYLDGQDIfkMDVIELRRRVQMVFQIPN 92

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054819401 102 LFPHLTVAENVAFGLRRRR----EADVEARVAEGLALVELGHLADRR---PA-LLSGGQQQRVALARALVNRPALLLLDE 173
Cdd:PRK14247   93 PIPNLSIFENVALGLKLNRlvksKKELQERVRWALEKAQLWDEVKDRldaPAgKLSGGQQQRLCIARALAFQPEVLLADE 172

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054819401 174 PLGALDLKLRRQMQ---LELKRiqtevGLTFVHVTHDQEEAMTMADTVAVMNRGRIEQMGPPADLYEHPR 240
Cdd:PRK14247  173 PTANLDPENTAKIEslfLELKK-----DMTIVLVTHFPQQAARISDYVAFLYKGQIVEWGPTREVFTNPR 237
cbiO PRK13649
energy-coupling factor transporter ATPase;
34-238 2.61e-34

energy-coupling factor transporter ATPase;


Pssm-ID: 184208 [Multi-domain]  Cd Length: 280  Bit Score: 128.32  E-value: 2.61e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054819401  34 AVDDLTLTVPSGSFFALLGPSGCGKTTTLRMVAGLEQPTDGTISIDGRDVTGT------RAHRRPVNTVFQsyalFPHL- 106
Cdd:PRK13649   22 ALFDVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDDTLITSTsknkdiKQIRKKVGLVFQ----FPESq 97

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054819401 107 ----TVAENVAFGLRR----RREADVEARvaEGLALVELGH-LADRRPALLSGGQQQRVALARALVNRPALLLLDEPLGA 177
Cdd:PRK13649   98 lfeeTVLKDVAFGPQNfgvsQEEAEALAR--EKLALVGISEsLFEKNPFELSGGQMRRVAIAGILAMEPKILVLDEPTAG 175

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1054819401 178 LDLKLRRQMQLELKRIQtEVGLTFVHVTHDQEEAMTMADTVAVMNRGRIEQMGPPADLYEH 238
Cdd:PRK13649  176 LDPKGRKELMTLFKKLH-QSGMTIVLVTHLMDDVANYADFVYVLEKGKLVLSGKPKDIFQD 235
cbiO PRK13648
cobalt transporter ATP-binding subunit; Provisional
 34-238 2.73e-34

cobalt transporter ATP-binding subunit; Provisional


Pssm-ID: 184207 [Multi-domain]  Cd Length: 269  Bit Score: 127.95  E-value: 2.73e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054819401  34 AVDDLTLTVPSGSFFALLGPSGCGKTTTLRMVAGLEQPTDGTI-----SIDGRDVTGTRAHrrpVNTVFQS-YALFPHLT 107
Cdd:PRK13648   24 TLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIfynnqAITDDNFEKLRKH---IGIVFQNpDNQFVGSI 100

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054819401 108 VAENVAFGLRRRR--EADVEARVAEGLALVELGHLADRRPALLSGGQQQRVALARALVNRPALLLLDEPLGALDLKLRRQ 185
Cdd:PRK13648  101 VKYDVAFGLENHAvpYDEMHRRVSEALKQVDMLERADYEPNALSGGQKQRVAIAGVLALNPSVIILDEATSMLDPDARQN 180

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1054819401 186 MQLELKRIQTEVGLTFVHVTHDQEEAMTmADTVAVMNRGRIEQMGPPADLYEH 238
Cdd:PRK13648  181 LLDLVRKVKSEHNITIISITHDLSEAME-ADHVIVMNKGTVYKEGTPTEIFDH 232
PRK15079 PRK15079
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
 34-240 3.68e-34

oligopeptide ABC transporter ATP-binding protein OppF; Provisional


Pssm-ID: 185037 [Multi-domain]  Cd Length: 331  Bit Score: 129.06  E-value: 3.68e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054819401  34 AVDDLTLTVPSGSFFALLGPSGCGKTTTLRMVAGLEQPTDGTISIDGRDVTGT-----RAHRRPVNTVFQS--YALFPHL 106
Cdd:PRK15079   36 AVDGVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGEVAWLGKDLLGMkddewRAVRSDIQMIFQDplASLNPRM 115

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054819401 107 TVAENVAFGLR----RRREADVEARVAEGLALVEL-GHLADRRPALLSGGQQQRVALARALVNRPALLLLDEPLGALDLK 181
Cdd:PRK15079  116 TIGEIIAEPLRtyhpKLSRQEVKDRVKAMMLKVGLlPNLINRYPHEFSGGQCQRIGIARALILEPKLIICDEPVSALDVS 195

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1054819401 182 LRRQMQLELKRIQTEVGLTFVHVTHDQEEAMTMADTVAVMNRGRIEQMGPPADLYEHPR 240
Cdd:PRK15079  196 IQAQVVNLLQQLQREMGLSLIFIAHDLAVVKHISDRVLVMYLGHAVELGTYDEVYHNPL 254
LPS_export_lptB TIGR04406
LPS export ABC transporter ATP-binding protein; Members of this fmaily are LptB, the ...
 27-251 4.75e-34

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: 126.23  E-value: 4.75e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054819401  27 KRFGAFVAVDDLTLTVPSGSFFALLGPSGCGKTTTLRMVAGLEQPTDGTISIDGRDVTGTRAHRRP---VNTVFQSYALF 103
Cdd:TIGR04406   9 KSYKKRKVVNDVSLSVKSGEIVGLLGPNGAGKTTSFYMIVGLVRPDAGKILIDGQDITHLPMHERArlgIGYLPQEASIF 88

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054819401 104 PHLTVAENVAFGLRRRREADVEARVAEGLALVE---LGHLADRRPALLSGGQQQRVALARALVNRPALLLLDEPLGALDL 180
Cdd:TIGR04406  89 RKLTVEENIMAVLEIRKDLDRAEREERLEALLEefqISHLRDNKAMSLSGGERRRVEIARALATNPKFILLDEPFAGVDP 168

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1054819401 181 KLRRQMQlELKRIQTEVGLTFVHVTHDQEEAMTMADTVAVMNRGRIEQMGPPADLYEHPRTTFVanFLGRS 251
Cdd:TIGR04406 169 IAVGDIK-KIIKHLKERGIGVLITDHNVRETLDICDRAYIISDGKVLAEGTPAEIVANEKVRRV--YLGEQ 236
CydC COG4987
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ...
 3-239 5.10e-34

ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease components [Energy production and conversion, Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 444011 [Multi-domain]  Cd Length: 569  Bit Score: 132.58  E-value: 5.10e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054819401   3 TTAPAHPGAASASAGaaLELAAVTKRF--GAFVAVDDLTLTVPSGSFFALLGPSGCGKTTTLRMVAGLEQPTDGTISIDG 80
Cdd:COG4987   319 VTEPAEPAPAPGGPS--LELEDVSFRYpgAGRPVLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFLDPQSGSITLGG 396

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054819401  81 RDVTGTRAH--RRPVNTVFQSYALFpHLTVAENVAFGlrrRREADvEARVAEGLALVELGHLADRRP-----------AL 147
Cdd:COG4987   397 VDLRDLDEDdlRRRIAVVPQRPHLF-DTTLRENLRLA---RPDAT-DEELWAALERVGLGDWLAALPdgldtwlgeggRR 471

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054819401 148 LSGGQQQRVALARALVNRPALLLLDEPLGALDLKLRRQMqleLKRIQTEV-GLTFVHVTHDqEEAMTMADTVAVMNRGRI 226
Cdd:COG4987   472 LSGGERRRLALARALLRDAPILLLDEPTEGLDAATEQAL---LADLLEALaGRTVLLITHR-LAGLERMDRILVLEDGRI 547

                         250
                  ....*....|...
gi 1054819401 227 EQMGPPADLYEHP 239
Cdd:COG4987   548 VEQGTHEELLAQN 560
PRK10247 PRK10247
putative ABC transporter ATP-binding protein YbbL; Provisional
 20-218 1.91e-33

putative ABC transporter ATP-binding protein YbbL; Provisional


Pssm-ID: 182331 [Multi-domain]  Cd Length: 225  Bit Score: 124.44  E-value: 1.91e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054819401  20 LELAAVTKRFGAFVAVDDLTLTVPSGSFFALLGPSGCGKTTTLRMVAGLEQPTDGTISIDGRDVT--GTRAHRRPVNTVF 97
Cdd:PRK10247    8 LQLQNVGYLAGDAKILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFEGEDIStlKPEIYRQQVSYCA 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054819401  98 QSYALFPHlTVAENVAFGLRRRREADVEARVAEGLALVELG-HLADRRPALLSGGQQQRVALARALVNRPALLLLDEPLG 176
Cdd:PRK10247   88 QTPTLFGD-TVYDNLIFPWQIRNQQPDPAIFLDDLERFALPdTILTKNIAELSGGEKQRISLIRNLQFMPKVLLLDEITS 166

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 1054819401 177 ALDLKLRRQMQLELKRIQTEVGLTFVHVTHDQEEaMTMADTV 218
Cdd:PRK10247  167 ALDESNKHNVNEIIHRYVREQNIAVLWVTHDKDE-INHADKV 207
YejF COG4172
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ...
 30-240 1.75e-32

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: 127.88  E-value: 1.75e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054819401  30 GAFVAVDDLTLTVPSGSFFALLGPSGCGKTTT----LRMVAGLEQPTDGTISIDGRDVTGT-----RAHR-RPVNTVFQ- 98
Cdd:COG4172    21 GTVEAVKGVSFDIAAGETLALVGESGSGKSVTalsiLRLLPDPAAHPSGSILFDGQDLLGLserelRRIRgNRIAMIFQe 100

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054819401  99 -SYALFPHLTVAENVAFGLR-----RRREAdvEARVAEGLALVEL---GHLADRRPALLSGGQQQRVALARALVNRPALL 169
Cdd:COG4172   101 pMTSLNPLHTIGKQIAEVLRlhrglSGAAA--RARALELLERVGIpdpERRLDAYPHQLSGGQRQRVMIAMALANEPDLL 178

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1054819401 170 LLDEPLGALDLKLRRQMqLEL-KRIQTEVGLTFVHVTHDqeeaMT----MADTVAVMNRGRIEQMGPPADLYEHPR 240
Cdd:COG4172   179 IADEPTTALDVTVQAQI-LDLlKDLQRELGMALLLITHD----LGvvrrFADRVAVMRQGEIVEQGPTAELFAAPQ 249
PRK14267 PRK14267
phosphate ABC transporter ATP-binding protein; Provisional
 29-240 2.20e-32

phosphate ABC transporter ATP-binding protein; Provisional


Pssm-ID: 184596 [Multi-domain]  Cd Length: 253  Bit Score: 122.26  E-value: 2.20e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054819401  29 FGAFVAVDDLTLTVPSGSFFALLGPSGCGKTTTLRMVAGL-----EQPTDGTISIDGRDVTGTRAH----RRPVNTVFQS 99
Cdd:PRK14267   14 YGSNHVIKGVDLKIPQNGVFALMGPSGCGKSTLLRTFNRLlelneEARVEGEVRLFGRNIYSPDVDpievRREVGMVFQY 93

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054819401 100 YALFPHLTVAENVAFGLRR----RREADVEARVAEGLALVEL-GHLADR---RPALLSGGQQQRVALARALVNRPALLLL 171
Cdd:PRK14267   94 PNPFPHLTIYDNVAIGVKLnglvKSKKELDERVEWALKKAALwDEVKDRlndYPSNLSGGQRQRLVIARALAMKPKILLM 173

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1054819401 172 DEPLGALDLKLRRQMQLELKRIQTEvgLTFVHVTHDQEEAMTMADTVAVMNRGRIEQMGPPADLYEHPR 240
Cdd:PRK14267  174 DEPTANIDPVGTAKIEELLFELKKE--YTIVLVTHSPAQAARVSDYVAFLYLGKLIEVGPTRKVFENPE 240
btuD PRK09536
corrinoid ABC transporter ATPase; Reviewed
 20-297 4.16e-32

corrinoid ABC transporter ATPase; Reviewed


Pssm-ID: 236554 [Multi-domain]  Cd Length: 402  Bit Score: 124.95  E-value: 4.16e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054819401  20 LELAAVTKRFGAFVAVDDLTLTVPSGSFFALLGPSGCGKTTTLRMVAGLEQPTDGTISIDGRDV--TGTRAHRRPVNTVF 97
Cdd:PRK09536    4 IDVSDLSVEFGDTTVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGDDVeaLSARAASRRVASVP 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054819401  98 QSYALFPHLTVAENVAFG-------LRRRREADvEARVAEGLALVELGHLADRRPALLSGGQQQRVALARALVNRPALLL 170
Cdd:PRK09536   84 QDTSLSFEFDVRQVVEMGrtphrsrFDTWTETD-RAAVERAMERTGVAQFADRPVTSLSGGERQRVLLARALAQATPVLL 162

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054819401 171 LDEPLGALDLKlrRQMQ-LELKRIQTEVGLTFVHVTHDQEEAMTMADTVAVMNRGRIEQMGPPADLYEHP--RTTFVANF 247
Cdd:PRK09536  163 LDEPTASLDIN--HQVRtLELVRRLVDDGKTAVAAIHDLDLAARYCDELVLLADGRVRAAGPPADVLTADtlRAAFDART 240

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054819401 248 LGRSNLVPGTV-VERLDGDLLGVDVGGARVRV-----PASRAVRDTG----DVLVGARPE 297
Cdd:PRK09536  241 AVGTDPATGAPtVTPLPDPDRTEAAADTRVHVvgggqPAARAVSRLVaagaSVSVGPVPE 300
ABCC_Protease_Secretion cd03246
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ...
 35-226 5.68e-32

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: 118.86  E-value: 5.68e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054819401  35 VDDLTLTVPSGSFFALLGPSGCGKTTTLRMVAGLEQPTDGTISIDGRDVT--GTRAHRRPVNTVFQSYALFPHlTVAENV 112
Cdd:cd03246    18 LRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDGADISqwDPNELGDHVGYLPQDDELFSG-SIAENI 96

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054819401 113 afglrrrreadvearvaeglalvelghladrrpalLSGGQQQRVALARALVNRPALLLLDEPLGALDLKLRRQMQLELKR 192
Cdd:cd03246    97 -----------------------------------LSGGQRQRLGLARALYGNPRILVLDEPNSHLDVEGERALNQAIAA 141

                         170       180       190
                  ....*....|....*....|....*....|....
gi 1054819401 193 IQtEVGLTFVHVTHdQEEAMTMADTVAVMNRGRI 226
Cdd:cd03246   142 LK-AAGATRIVIAH-RPETLASADRILVLEDGRV 173
met_CoM_red_A2 TIGR03269
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ...
 20-237 9.13e-32

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: 125.69  E-value: 9.13e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054819401  20 LELAAVTKRF-----GAFVAVDDLTLTVPSGSFFALLGPSGCGKTTTLRMVAGLEQPTDGTISI----DGRDVTGTRAHR 90
Cdd:TIGR03269 280 IKVRNVSKRYisvdrGVVKAVDNVSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGEVNVrvgdEWVDMTKPGPDG 359

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054819401  91 RP-----VNTVFQSYALFPHLTVAENV--AFGLR-----RRREAdVEARVAEGLALVELGHLADRRPALLSGGQQQRVAL 158
Cdd:TIGR03269 360 RGrakryIGILHQEYDLYPHRTVLDNLteAIGLElpdelARMKA-VITLKMVGFDEEKAEEILDKYPDELSEGERHRVAL 438

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1054819401 159 ARALVNRPALLLLDEPLGALDLKLRRQMQLELKRIQTEVGLTFVHVTHDQEEAMTMADTVAVMNRGRIEQMGPPADLYE 237
Cdd:TIGR03269 439 AQVLIKEPRIVILDEPTGTMDPITKVDVTHSILKAREEMEQTFIIVSHDMDFVLDVCDRAALMRDGKIVKIGDPEEIVE 517
cbiO PRK13632
cobalt transporter ATP-binding subunit; Provisional
 34-237 1.10e-31

cobalt transporter ATP-binding subunit; Provisional


Pssm-ID: 237452 [Multi-domain]  Cd Length: 271  Bit Score: 120.87  E-value: 1.10e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054819401  34 AVDDLTLTVPSGSFFALLGPSGCGKTTTLRMVAGLEQPTDGTISIDGRDVT--GTRAHRRPVNTVFQSY-ALFPHLTVAE 110
Cdd:PRK13632   24 ALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIDGITISkeNLKEIRKKIGIIFQNPdNQFIGATVED 103

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054819401 111 NVAFGLRRRRE--ADVEARVAEGLALVELGHLADRRPALLSGGQQQRVALARALVNRPALLLLDEPLGALDLKLRRQMQL 188
Cdd:PRK13632  104 DIAFGLENKKVppKKMKDIIDDLAKKVGMEDYLDKEPQNLSGGQKQRVAIASVLALNPEIIIFDESTSMLDPKGKREIKK 183

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 1054819401 189 ELKRIQTEVGLTFVHVTHDQEEAmTMADTVAVMNRGRIEQMGPPADLYE 237
Cdd:PRK13632  184 IMVDLRKTRKKTLISITHDMDEA-ILADKVIVFSEGKLIAQGKPKEILN 231
ABCC_MsbA cd03251
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ...
 34-237 2.38e-31

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: 118.87  E-value: 2.38e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054819401  34 AVDDLTLTVPSGSFFALLGPSGCGKTTTLRMVAGLEQPTDGTISIDGRDVTGTRAH--RRPVNTVFQSYALFpHLTVAEN 111
Cdd:cd03251    17 VLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDGHDVRDYTLAslRRQIGLVSQDVFLF-NDTVAEN 95

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054819401 112 VAFGLRRRREADVE--ARVAEGLALVE-----LGHLADRRPALLSGGQQQRVALARALVNRPALLLLDEPLGALDLKLRR 184
Cdd:cd03251    96 IAYGRPGATREEVEeaARAANAHEFIMelpegYDTVIGERGVKLSGGQRQRIAIARALLKDPPILILDEATSALDTESER 175

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1054819401 185 QMQLELKRIQteVGLTFVHVTHdQEEAMTMADTVAVMNRGRIEQMGPPADLYE 237
Cdd:cd03251   176 LVQAALERLM--KNRTTFVIAH-RLSTIENADRIVVLEDGKIVERGTHEELLA 225
PRK11831 PRK11831
phospholipid ABC transporter ATP-binding protein MlaF;
20-239 4.34e-31

phospholipid ABC transporter ATP-binding protein MlaF;


Pssm-ID: 236997 [Multi-domain]  Cd Length: 269  Bit Score: 119.48  E-value: 4.34e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054819401  20 LELAAVTKRFGAFVAVDDLTLTVPSGSFFALLGPSGCGKTTTLRMVAGLEQPTDGTISIDGRDV-TGTRAH----RRPVN 94
Cdd:PRK11831    8 VDMRGVSFTRGNRCIFDNISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEILFDGENIpAMSRSRlytvRKRMS 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054819401  95 TVFQSYALFPHLTVAENVAFGLR---RRREADVEARVAEGLALVELGHLADRRPALLSGGQQQRVALARALVNRPALLLL 171
Cdd:PRK11831   88 MLFQSGALFTDMNVFDNVAYPLRehtQLPAPLLHSTVMMKLEAVGLRGAAKLMPSELSGGMARRAALARAIALEPDLIMF 167

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1054819401 172 DEPLGALD-------LKLrrqmqleLKRIQTEVGLTFVHVTHDQEEAMTMADTVAVMNRGRIEQMGPPADLYEHP 239
Cdd:PRK11831  168 DEPFVGQDpitmgvlVKL-------ISELNSALGVTCVVVSHDVPEVLSIADHAYIVADKKIVAHGSAQALQANP 235
PRK14246 PRK14246
phosphate ABC transporter ATP-binding protein; Provisional
 37-250 1.45e-30

phosphate ABC transporter ATP-binding protein; Provisional


Pssm-ID: 172734 [Multi-domain]  Cd Length: 257  Bit Score: 117.46  E-value: 1.45e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054819401  37 DLTLTVPSGSFFALLGPSGCGKTTTLRMVAGLEQPTDGTISIDGR------DVTGTRA--HRRPVNTVFQSYALFPHLTV 108
Cdd:PRK14246   28 DITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLIEIYDSKIKVDGKvlyfgkDIFQIDAikLRKEVGMVFQQPNPFPHLSI 107

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054819401 109 AENVAF-----GLRRRREadVEARVAEGLALVEL-GHLADR--RPA-LLSGGQQQRVALARALVNRPALLLLDEPLGALD 179
Cdd:PRK14246  108 YDNIAYplkshGIKEKRE--IKKIVEECLRKVGLwKEVYDRlnSPAsQLSGGQQQRLTIARALALKPKVLLMDEPTSMID 185

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1054819401 180 LKLRRQMQLELKRIQTEvgLTFVHVTHDQEEAMTMADTVAVMNRGRIEQMGPPADLYEHPRTTFVANF-LGR 250
Cdd:PRK14246  186 IVNSQAIEKLITELKNE--IAIVIVSHNPQQVARVADYVAFLYNGELVEWGSSNEIFTSPKNELTEKYvIGR 255
ABCC_Glucan_exporter_like cd03254
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ...
 34-237 1.91e-30

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: 116.56  E-value: 1.91e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054819401  34 AVDDLTLTVPSGSFFALLGPSGCGKTTTLRMVAGLEQPTDGTISIDGRDVTGTRAH--RRPVNTVFQSYALFPHlTVAEN 111
Cdd:cd03254    18 VLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGIDIRDISRKslRSMIGVVLQDTFLFSG-TIMEN 96

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054819401 112 VAFGlrrRREADVEaRVAEGLALVELGHLADRRP-----------ALLSGGQQQRVALARALVNRPALLLLDEPLGALDL 180
Cdd:cd03254    97 IRLG---RPNATDE-EVIEAAKEAGAHDFIMKLPngydtvlgengGNLSQGERQLLAIARAMLRDPKILILDEATSNIDT 172

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1054819401 181 KLRRQMQLELKRIQteVGLTFVHVTHdQEEAMTMADTVAVMNRGRIEQMGPPADLYE 237
Cdd:cd03254   173 ETEKLIQEALEKLM--KGRTSIIIAH-RLSTIKNADKILVLDDGKIIEEGTHDELLA 226
AztA NF040873
zinc ABC transporter ATP-binding protein AztA;
28-212 2.03e-30

zinc ABC transporter ATP-binding protein AztA;


Pssm-ID: 468810 [Multi-domain]  Cd Length: 191  Bit Score: 115.02  E-value: 2.03e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054819401  28 RFGAFVAVDDLTLTVPSGSFFALLGPSGCGKTTTLRMVAGLEQPTDGTIsidgrdvtgTRAHRRPVNTVFQSYAL---FP 104
Cdd:NF040873    1 GYGGRPVLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTV---------RRAGGARVAYVPQRSEVpdsLP 71

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054819401 105 hLTVAENVAFGLRRRR------EADVEARVAEGLALVELGHLADRRPALLSGGQQQRVALARALVNRPALLLLDEPLGAL 178
Cdd:NF040873   72 -LTVRDLVAMGRWARRglwrrlTRDDRAAVDDALERVGLADLAGRQLGELSGGQRQRALLAQGLAQEADLLLLDEPTTGL 150

                         170       180       190
                  ....*....|....*....|....*....|....
gi 1054819401 179 DLKLRRQMQLELKRIQTEvGLTFVHVTHDQEEAM 212
Cdd:NF040873  151 DAESRERIIALLAEEHAR-GATVVVVTHDLELVR 183
PRK13633 PRK13633
energy-coupling factor transporter ATPase;
33-236 2.43e-30

energy-coupling factor transporter ATPase;


Pssm-ID: 237453 [Multi-domain]  Cd Length: 280  Bit Score: 117.50  E-value: 2.43e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054819401  33 VAVDDLTLTVPSGSFFALLGPSGCGKTTTLRMVAGLEQPTDGTISIDGRDvTGTRAH----RRPVNTVFQSyalfPH--- 105
Cdd:PRK13633   24 LALDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVYVDGLD-TSDEENlwdiRNKAGMVFQN----PDnqi 98

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054819401 106 --LTVAENVAFGLRRR--READVEARVAEGLALVELGHLADRRPALLSGGQQQRVALARALVNRPALLLLDEPLGALDLK 181
Cdd:PRK13633   99 vaTIVEEDVAFGPENLgiPPEEIRERVDESLKKVGMYEYRRHAPHLLSGGQKQRVAIAGILAMRPECIIFDEPTAMLDPS 178

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1054819401 182 LRRQMQLELKRIQTEVGLTFVHVTHDQEEAMTmADTVAVMNRGRIEQMGPPADLY 236
Cdd:PRK13633  179 GRREVVNTIKELNKKYGITIILITHYMEEAVE-ADRIIVMDSGKVVMEGTPKEIF 232
cbiO PRK13641
energy-coupling factor transporter ATPase;
35-239 2.59e-30

energy-coupling factor transporter ATPase;


Pssm-ID: 237456 [Multi-domain]  Cd Length: 287  Bit Score: 117.62  E-value: 2.59e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054819401  35 VDDLTLTVPSGSFFALLGPSGCGKTTTLRMVAGLEQPTDGTISIDGRDVT------GTRAHRRPVNTVFQsyalFPHL-- 106
Cdd:PRK13641   23 LDNISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITIAGYHITpetgnkNLKKLRKKVSLVFQ----FPEAql 98

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054819401 107 ---TVAENVAFGLRRRREADVEARVAEGLALVELG---HLADRRPALLSGGQQQRVALARALVNRPALLLLDEPLGALDL 180
Cdd:PRK13641   99 fenTVLKDVEFGPKNFGFSEDEAKEKALKWLKKVGlseDLISKSPFELSGGQMRRVAIAGVMAYEPEILCLDEPAAGLDP 178

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1054819401 181 KLRRQMQLELKRIQTEvGLTFVHVTHDQEEAMTMADTVAVMNRGRIEQMGPPADLYEHP 239
Cdd:PRK13641  179 EGRKEMMQLFKDYQKA-GHTVILVTHNMDDVAEYADDVLVLEHGKLIKHASPKEIFSDK 236
type_I_sec_LssB TIGR03375
type I secretion system ATPase, LssB family; Type I protein secretion is a system in some ...
 34-233 2.60e-30

type I secretion system ATPase, LssB family; Type I protein secretion is a system in some Gram-negative bacteria to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type I secretion apparatus. Targeted proteins are not cleaved at the N-terminus, but rather carry signals located toward the extreme C-terminus to direct type I secretion. This model is related to models TIGR01842 and TIGR01846, and to bacteriocin ABC transporters that cleave their substrates during export. [Protein fate, Protein and peptide secretion and trafficking, Cellular processes, Pathogenesis]


Pssm-ID: 274550 [Multi-domain]  Cd Length: 694  Bit Score: 122.67  E-value: 2.60e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054819401  34 AVDDLTLTVPSGSFFALLGPSGCGKTTTLRMVAGLEQPTDGTISIDGRDVTGTRAH--RRPVNTVFQSYALFpHLTVAEN 111
Cdd:TIGR03375 480 ALDNVSLTIRPGEKVAIIGRIGSGKSTLLKLLLGLYQPTEGSVLLDGVDIRQIDPAdlRRNIGYVPQDPRLF-YGTLRDN 558

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054819401 112 VAFGlrrRREADvEARVAEGLALVELGHLADRRP-----------ALLSGGQQQRVALARALVNRPALLLLDEPLGALDL 180
Cdd:TIGR03375 559 IALG---APYAD-DEEILRAAELAGVTEFVRRHPdgldmqigergRSLSGGQRQAVALARALLRDPPILLLDEPTSAMDN 634

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1054819401 181 KLRRQMQLELKRIQteVGLTFVHVTHDQeEAMTMADTVAVMNRGRIEQMGPPA 233
Cdd:TIGR03375 635 RSEERFKDRLKRWL--AGKTLVLVTHRT-SLLDLVDRIIVMDNGRIVADGPKD 684
ABC2_perm_RbbA NF033858
ribosome-associated ATPase/putative transporter RbbA;
26-235 3.12e-30

ribosome-associated ATPase/putative transporter RbbA;


Pssm-ID: 468210 [Multi-domain]  Cd Length: 907  Bit Score: 122.93  E-value: 3.12e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054819401  26 TKRFGAFVAVDDLTLTVPSGSFFALLGPSGCGKTTTLRMVAGLEQPTDGTISIDGRDVT-GTRAHRRPVNTVFQSYALFP 104
Cdd:NF033858  273 TMRFGDFTAVDHVSFRIRRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGEAWLFGQPVDaGDIATRRRVGYMSQAFSLYG 352

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054819401 105 HLTVAENVA-----FGLrrrREADVEARVAEGLALVELGHLADRRPALLSGGQQQRVALARALVNRPALLLLDEPLGALD 179
Cdd:NF033858  353 ELTVRQNLElharlFHL---PAAEIAARVAEMLERFDLADVADALPDSLPLGIRQRLSLAVAVIHKPELLILDEPTSGVD 429

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1054819401 180 LKLR----RQMqLELKRiqtEVGLT-FVHvTHDQEEAMTmADTVAVMNRGRIEQMGPPADL 235
Cdd:NF033858  430 PVARdmfwRLL-IELSR---EDGVTiFIS-THFMNEAER-CDRISLMHAGRVLASDTPAAL 484
cbiO PRK13652
cobalt transporter ATP-binding subunit; Provisional
 34-239 3.17e-30

cobalt transporter ATP-binding subunit; Provisional


Pssm-ID: 172200 [Multi-domain]  Cd Length: 277  Bit Score: 117.21  E-value: 3.17e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054819401  34 AVDDLTLTVPSGSFFALLGPSGCGKTTTLRMVAGLEQPTDGTISIDGRDVTGTRAH--RRPVNTVFQSY--ALFPHlTVA 109
Cdd:PRK13652   19 ALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIRGEPITKENIRevRKFVGLVFQNPddQIFSP-TVE 97

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054819401 110 ENVAFGLRRR--READVEARVAEGLALVELGHLADRRPALLSGGQQQRVALARALVNRPALLLLDEPLGALDLKLRRQMQ 187
Cdd:PRK13652   98 QDIAFGPINLglDEETVAHRVSSALHMLGLEELRDRVPHHLSGGEKKRVAIAGVIAMEPQVLVLDEPTAGLDPQGVKELI 177

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1054819401 188 LELKRIQTEVGLTFVHVTHDQEEAMTMADTVAVMNRGRIEQMGPPADLYEHP 239
Cdd:PRK13652  178 DFLNDLPETYGMTVIFSTHQLDLVPEMADYIYVMDKGRIVAYGTVEEIFLQP 229
nickel_nikD TIGR02770
nickel import ATP-binding protein NikD; This family represents the NikD subunit of a ...
 34-250 4.81e-30

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: 115.54  E-value: 4.81e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054819401  34 AVDDLTLTVPSGSFFALLGPSGCGKTTTLRMVAGLEQP----TDGTISIDGRDVTGTRAHRRPVNTVFQS--YALFPHLT 107
Cdd:TIGR02770   1 LVQDLNLSLKRGEVLALVGESGSGKSLTCLAILGLLPPgltqTSGEILLDGRPLLPLSIRGRHIATIMQNprTAFNPLFT 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054819401 108 VAENVAFGLRRRR--EADVEARVAEGLALVELGH---LADRRPALLSGGQQQRVALARALVNRPALLLLDEPLGALDLKL 182
Cdd:TIGR02770  81 MGNHAIETLRSLGklSKQARALILEALEAVGLPDpeeVLKKYPFQLSGGMLQRVMIALALLLEPPFLIADEPTTDLDVVN 160

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1054819401 183 RRQMQLELKRIQTEVGLTFVHVTHDQEEAMTMADTVAVMNRGRIEQMGPPADLYEHPRTTFVANFLGR 250
Cdd:TIGR02770 161 QARVLKLLRELRQLFGTGILLITHDLGVVARIADEVAVMDDGRIVERGTVKEIFYNPKHETTRKLLSA 228
CydD TIGR02857
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ...
 20-221 6.68e-30

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: 120.47  E-value: 6.68e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054819401  20 LELAAVTKRF-GAFVAVDDLTLTVPSGSFFALLGPSGCGKTTTLRMVAGLEQPTDGTISIDGRDVTGTRAH--RRPVNTV 96
Cdd:TIGR02857 322 LEFSGVSVAYpGRRPALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSIAVNGVPLADADADswRDQIAWV 401

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054819401  97 FQSYALFPHlTVAENVAFGlrrRREADvEARVAEGLALVELGHL-----------ADRRPALLSGGQQQRVALARALVNR 165
Cdd:TIGR02857 402 PQHPFLFAG-TIAENIRLA---RPDAS-DAEIREALERAGLDEFvaalpqgldtpIGEGGAGLSGGQAQRLALARAFLRD 476

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1054819401 166 PALLLLDEPLGALDLKLRRQMQLELKRIQTevGLTFVHVTHDqEEAMTMADTVAVM 221
Cdd:TIGR02857 477 APLLLLDEPTAHLDAETEAEVLEALRALAQ--GRTVLLVTHR-LALAALADRIVVL 529
lolD PRK11629
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
37-228 1.29e-29

lipoprotein-releasing ABC transporter ATP-binding protein LolD;


Pssm-ID: 183244 [Multi-domain]  Cd Length: 233  Bit Score: 114.53  E-value: 1.29e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054819401  37 DLTLTVPSGSFFALLGPSGCGKTTTLRMVAGLEQPTDGTISIDGRDV----TGTRA--HRRPVNTVFQSYALFPHLTVAE 110
Cdd:PRK11629   27 NVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPMsklsSAAKAelRNQKLGFIYQFHHLLPDFTALE 106

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054819401 111 NVAF----GLRRRREADVEARvaEGLALVELGHLADRRPALLSGGQQQRVALARALVNRPALLLLDEPLGALDLKLRR-- 184
Cdd:PRK11629  107 NVAMplliGKKKPAEINSRAL--EMLAAVGLEHRANHRPSELSGGERQRVAIARALVNNPRLVLADEPTGNLDARNADsi 184

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 1054819401 185 -QMQLELKRIQtevGLTFVHVTHDQEEAMTMADTVAvMNRGRIEQ 228
Cdd:PRK11629  185 fQLLGELNRLQ---GTAFLVVTHDLQLAKRMSRQLE-MRDGRLTA 225
ABCC_bacteriocin_exporters cd03245
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ...
 34-226 1.61e-29

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: 113.84  E-value: 1.61e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054819401  34 AVDDLTLTVPSGSFFALLGPSGCGKTTTLRMVAGLEQPTDGTISIDGRDVT--GTRAHRRPVNTVFQSYALFpHLTVAEN 111
Cdd:cd03245    19 ALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGTDIRqlDPADLRRNIGYVPQDVTLF-YGTLRDN 97

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054819401 112 VAFGlrrRREADvEARVAEGLALVELGHLADRRP-----------ALLSGGQQQRVALARALVNRPALLLLDEPLGALDL 180
Cdd:cd03245    98 ITLG---APLAD-DERILRAAELAGVTDFVNKHPngldlqigergRGLSGGQRQAVALARALLNDPPILLLDEPTSAMDM 173

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 1054819401 181 KLRRQMQLELKriQTEVGLTFVHVTHDQeEAMTMADTVAVMNRGRI 226
Cdd:cd03245   174 NSEERLKERLR--QLLGDKTLIIITHRP-SLLDLVDRIIVMDSGRI 216
ABCC_ATM1_transporter cd03253
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ...
 36-235 1.78e-29

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: 113.86  E-value: 1.78e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054819401  36 DDLTLTVPSGSFFALLGPSGCGKTTTLRMVAGLEQPTDGTISIDGRDVTGTRAH--RRPVNTVFQSYALFpHLTVAENVA 113
Cdd:cd03253    18 KDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDGQDIREVTLDslRRAIGVVPQDTVLF-NDTIGYNIR 96

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054819401 114 FGLRRRREADVE--ARVAeglalvelgHLADR--------------RPALLSGGQQQRVALARALVNRPALLLLDEPLGA 177
Cdd:cd03253    97 YGRPDATDEEVIeaAKAA---------QIHDKimrfpdgydtivgeRGLKLSGGEKQRVAIARAILKNPPILLLDEATSA 167

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1054819401 178 LDLKLRRQMQLELKRIQTevGLTFVHVTHDQEEAMTmADTVAVMNRGRIEQMGPPADL 235
Cdd:cd03253   168 LDTHTEREIQAALRDVSK--GRTTIVIAHRLSTIVN-ADKIIVLKDGRIVERGTHEEL 222
cbiO PRK13643
energy-coupling factor transporter ATPase;
34-237 3.40e-29

energy-coupling factor transporter ATPase;


Pssm-ID: 184203 [Multi-domain]  Cd Length: 288  Bit Score: 114.83  E-value: 3.40e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054819401  34 AVDDLTLTVPSGSFFALLGPSGCGKTTTLRMVAGLEQPTDGTISIDGRDVTGTRAH------RRPVNTVFQ--SYALFPH 105
Cdd:PRK13643   21 ALFDIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVTVGDIVVSSTSKQkeikpvRKKVGVVFQfpESQLFEE 100

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054819401 106 lTVAENVAFGLRRR--READVEARVAEGLALVELG-HLADRRPALLSGGQQQRVALARALVNRPALLLLDEPLGALDLKL 182
Cdd:PRK13643  101 -TVLKDVAFGPQNFgiPKEKAEKIAAEKLEMVGLAdEFWEKSPFELSGGQMRRVAIAGILAMEPEVLVLDEPTAGLDPKA 179

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1054819401 183 RRQMQLELKRIQtEVGLTFVHVTHDQEEAMTMADTVAVMNRGRIEQMGPPADLYE 237
Cdd:PRK13643  180 RIEMMQLFESIH-QSGQTVVLVTHLMDDVADYADYVYLLEKGHIISCGTPSDVFQ 233
cbiO PRK13646
energy-coupling factor transporter ATPase;
32-236 8.32e-29

energy-coupling factor transporter ATPase;


Pssm-ID: 184205 [Multi-domain]  Cd Length: 286  Bit Score: 113.72  E-value: 8.32e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054819401  32 FVAVDDLTLTVPSGSFFALLGPSGCGKTTTLRMVAGLEQPTDGTISIDGRDVTGT------RAHRRPVNTVFQsyalFPH 105
Cdd:PRK13646   20 HQAIHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVDDITITHKtkdkyiRPVRKRIGMVFQ----FPE 95

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054819401 106 L-----TVAENVAFGLRRRREADVEARVAEGLALVELGHLAD---RRPALLSGGQQQRVALARALVNRPALLLLDEPLGA 177
Cdd:PRK13646   96 SqlfedTVEREIIFGPKNFKMNLDEVKNYAHRLLMDLGFSRDvmsQSPFQMSGGQMRKIAIVSILAMNPDIIVLDEPTAG 175

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1054819401 178 LDLKLRRQMQLELKRIQTEVGLTFVHVTHDQEEAMTMADTVAVMNRGRIEQMGPPADLY 236
Cdd:PRK13646  176 LDPQSKRQVMRLLKSLQTDENKTIILVSHDMNEVARYADEVIVMKEGSIVSQTSPKELF 234
cbiO PRK13639
cobalt transporter ATP-binding subunit; Provisional
 33-246 9.15e-29

cobalt transporter ATP-binding subunit; Provisional


Pssm-ID: 184199 [Multi-domain]  Cd Length: 275  Bit Score: 113.25  E-value: 9.15e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054819401  33 VAVDDLTLTVPSGSFFALLGPSGCGKTTTLRMVAGLEQPTDGTISIDGR----DVTGTRAHRRPVNTVFQSY--ALF-Ph 105
Cdd:PRK13639   16 EALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIKGEpikyDKKSLLEVRKTVGIVFQNPddQLFaP- 94

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054819401 106 lTVAENVAFG---LRRRREaDVEARVAEGLALVELGHLADRRPALLSGGQQQRVALARALVNRPALLLLDEPLGALDLKL 182
Cdd:PRK13639   95 -TVEEDVAFGplnLGLSKE-EVEKRVKEALKAVGMEGFENKPPHHLSGGQKKRVAIAGILAMKPEIIVLDEPTSGLDPMG 172

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1054819401 183 RRQMQLELKRIQTEvGLTFVHVTHDQEEAMTMADTVAVMNRGRIEQMGPPADLYEHPRTTFVAN 246
Cdd:PRK13639  173 ASQIMKLLYDLNKE-GITIIISTHDVDLVPVYADKVYVMSDGKIIKEGTPKEVFSDIETIRKAN 235
PRK10535 PRK10535
macrolide ABC transporter ATP-binding protein/permease MacB;
20-226 1.39e-28

macrolide ABC transporter ATP-binding protein/permease MacB;


Pssm-ID: 182528 [Multi-domain]  Cd Length: 648  Bit Score: 117.52  E-value: 1.39e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054819401  20 LELAAVTKRF----GAFVAVDDLTLTVPSGSFFALLGPSGCGKTTTLRMVAGLEQPTDGTISIDGRDVTG------TRAH 89
Cdd:PRK10535    5 LELKDIRRSYpsgeEQVEVLKGISLDIYAGEMVAIVGASGSGKSTLMNILGCLDKPTSGTYRVAGQDVATldadalAQLR 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054819401  90 RRPVNTVFQSYALFPHLTVAENVAF-----GLRRRREadvEARVAEGLALVELGHLADRRPALLSGGQQQRVALARALVN 164
Cdd:PRK10535   85 REHFGFIFQRYHLLSHLTAAQNVEVpavyaGLERKQR---LLRAQELLQRLGLEDRVEYQPSQLSGGQQQRVSIARALMN 161

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1054819401 165 RPALLLLDEPLGALDLKLRRQMQLELKRIQtEVGLTFVHVTHDQEEAmTMADTVAVMNRGRI 226
Cdd:PRK10535  162 GGQVILADEPTGALDSHSGEEVMAILHQLR-DRGHTVIIVTHDPQVA-AQAERVIEIRDGEI 221
ABC_NatA_like cd03267
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ...
 33-226 1.56e-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: 111.66  E-value: 1.56e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054819401  33 VAVDDLTLTVPSGSFFALLGPSGCGKTTTLRMVAGLEQPTDGTISIDGRdVTGTR--AHRRPVNTVF-QSYALFPHLTVA 109
Cdd:cd03267    35 EALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRVAGL-VPWKRrkKFLRRIGVVFgQKTQLWWDLPVI 113

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054819401 110 ENVAFGLRRRREADVEA--RVAEGLALVELGHLADRRPALLSGGQQQRVALARALVNRPALLLLDEPLGALDLKLRRQMQ 187
Cdd:cd03267   114 DSFYLLAAIYDLPPARFkkRLDELSELLDLEELLDTPVRQLSLGQRMRAEIAAALLHEPEILFLDEPTIGLDVVAQENIR 193

                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 1054819401 188 LELKRIQTEVGLTFVHVTHDQEEAMTMADTVAVMNRGRI 226
Cdd:cd03267   194 NFLKEYNRERGTTVLLTSHYMKDIEALARRVLVIDKGRL 232
MsbA_lipidA TIGR02203
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ...
 20-238 2.48e-28

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: 116.35  E-value: 2.48e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054819401  20 LELAAVTKRFGA--FVAVDDLTLTVPSGSFFALLGPSGCGKTTTLRMVAGLEQPTDGTISIDGRDVTG--TRAHRRPVNT 95
Cdd:TIGR02203 331 VEFRNVTFRYPGrdRPALDSISLVIEPGETVALVGRSGSGKSTLVNLIPRFYEPDSGQILLDGHDLADytLASLRRQVAL 410

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054819401  96 VFQSYALFPHlTVAENVAFGlrRRREADvEARVAEGLALVELGHLADRRP-----------ALLSGGQQQRVALARALVN 164
Cdd:TIGR02203 411 VSQDVVLFND-TIANNIAYG--RTEQAD-RAEIERALAAAYAQDFVDKLPlgldtpigengVLLSGGQRQRLAIARALLK 486

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1054819401 165 RPALLLLDEPLGALDLKLRRQMQLELKRIQTE-VGLTFVHVTHDQEEamtmADTVAVMNRGRIEQMGPPADLYEH 238
Cdd:TIGR02203 487 DAPILILDEATSALDNESERLVQAALERLMQGrTTLVIAHRLSTIEK----ADRIVVMDDGRIVERGTHNELLAR 557
cbiO PRK13642
energy-coupling factor transporter ATPase;
35-236 2.50e-28

energy-coupling factor transporter ATPase;


Pssm-ID: 184202 [Multi-domain]  Cd Length: 277  Bit Score: 112.11  E-value: 2.50e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054819401  35 VDDLTLTVPSGSFFALLGPSGCGKTTTLRMVAGLEQPTDGTISIDGRDVTGTRAH--RRPVNTVFQSY-ALFPHLTVAEN 111
Cdd:PRK13642   23 LNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDGELLTAENVWnlRRKIGMVFQNPdNQFVGATVEDD 102

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054819401 112 VAFGLRRR---READVEaRVAEGLALVELGHLADRRPALLSGGQQQRVALARALVNRPALLLLDEPLGALDLKLRRQMQL 188
Cdd:PRK13642  103 VAFGMENQgipREEMIK-RVDEALLAVNMLDFKTREPARLSGGQKQRVAVAGIIALRPEIIILDESTSMLDPTGRQEIMR 181

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 1054819401 189 ELKRIQTEVGLTFVHVTHDQEEAMTmADTVAVMNRGRIEQMGPPADLY 236
Cdd:PRK13642  182 VIHEIKEKYQLTVLSITHDLDEAAS-SDRILVMKAGEIIKEAAPSELF 228
PRK10584 PRK10584
putative ABC transporter ATP-binding protein YbbA; Provisional
 40-211 2.52e-28

putative ABC transporter ATP-binding protein YbbA; Provisional


Pssm-ID: 182569 [Multi-domain]  Cd Length: 228  Bit Score: 110.64  E-value: 2.52e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054819401  40 LTVPSGSFFALLGPSGCGKTTTLRMVAGLEQPTDGTISIDGRDVTG----TRAHRRPVNT--VFQSYALFPHLTVAENVA 113
Cdd:PRK10584   31 LVVKRGETIALIGESGSGKSTLLAILAGLDDGSSGEVSLVGQPLHQmdeeARAKLRAKHVgfVFQSFMLIPTLNALENVE 110

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054819401 114 FG--LRRRREADVEARVAEGLALVELGHLADRRPALLSGGQQQRVALARALVNRPALLLLDEPLGALDLKLRRQMQLELK 191
Cdd:PRK10584  111 LPalLRGESSRQSRNGAKALLEQLGLGKRLDHLPAQLSGGEQQRVALARAFNGRPDVLFADEPTGNLDRQTGDKIADLLF 190

                         170       180
                  ....*....|....*....|
gi 1054819401 192 RIQTEVGLTFVHVTHDQEEA 211
Cdd:PRK10584  191 SLNREHGTTLILVTHDLQLA 210
3a01208 TIGR00958
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
 37-239 2.62e-28

Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]


Pssm-ID: 273363 [Multi-domain]  Cd Length: 711  Bit Score: 116.75  E-value: 2.62e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054819401  37 DLTLTVPSGSFFALLGPSGCGKTTTLRMVAGLEQPTDGTISIDGRDVTGTRAH--RRPVNTVFQSYALFPHlTVAENVAF 114
Cdd:TIGR00958 499 GLTFTLHPGEVVALVGPSGSGKSTVAALLQNLYQPTGGQVLLDGVPLVQYDHHylHRQVALVGQEPVLFSG-SVRENIAY 577

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054819401 115 GLRRRREADVEARVAEGLA---LVELGHLAD----RRPALLSGGQQQRVALARALVNRPALLLLDEPLGALDLKLRRQMQ 187
Cdd:TIGR00958 578 GLTDTPDEEIMAAAKAANAhdfIMEFPNGYDtevgEKGSQLSGGQKQRIAIARALVRKPRVLILDEATSALDAECEQLLQ 657

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1054819401 188 LELKRiqteVGLTFVHVTHdQEEAMTMADTVAVMNRGRIEQMGPPADLYEHP 239
Cdd:TIGR00958 658 ESRSR----ASRTVLLIAH-RLSTVERADQILVLKKGSVVEMGTHKQLMEDQ 704
cbiO PRK13647
cobalt transporter ATP-binding subunit; Provisional
 34-235 4.08e-28

cobalt transporter ATP-binding subunit; Provisional


Pssm-ID: 237457 [Multi-domain]  Cd Length: 274  Bit Score: 111.37  E-value: 4.08e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054819401  34 AVDDLTLTVPSGSFFALLGPSGCGKTTTLRMVAGLEQPTDGTISIDGRDVTGT--RAHRRPVNTVFQSY--ALFPhLTVA 109
Cdd:PRK13647   20 ALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGREVNAEneKWVRSKVGLVFQDPddQVFS-STVW 98

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054819401 110 ENVAFGLR--RRREADVEARVAEGLALVELGHLADRRPALLSGGQQQRVALARALVNRPALLLLDEPLGALDLKLRRQMQ 187
Cdd:PRK13647   99 DDVAFGPVnmGLDKDEVERRVEEALKAVRMWDFRDKPPYHLSYGQKKRVAIAGVLAMDPDVIVLDEPMAYLDPRGQETLM 178

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 1054819401 188 LELKRIQTEvGLTFVHVTHDQEEAMTMADTVAVMNRGRIEQMGPPADL 235
Cdd:PRK13647  179 EILDRLHNQ-GKTVIVATHDVDLAAEWADQVIVLKEGRVLAEGDKSLL 225
ABC_KpsT_Wzt cd03220
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ...
 27-230 2.78e-27

ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC transporter subfamily is involved in extracellular polysaccharide export. Among the variety of membrane-linked or extracellular polysaccharides excreted by bacteria, only capsular polysaccharides, lipopolysaccharides, and teichoic acids have been shown to be exported by ABC transporters. A typical system is made of a conserved integral membrane and an ABC. In addition to these proteins, capsular polysaccharide exporter systems require two 'accessory' proteins to perform their function: a periplasmic (E.coli) or a lipid-anchored outer membrane protein called OMA (Neisseria meningitidis and Haemophilus influenza) and a cytoplasmic membrane protein MPA2.


Pssm-ID: 213187 [Multi-domain]  Cd Length: 224  Bit Score: 107.62  E-value: 2.78e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054819401  27 KRFGAFVAVDDLTLTVPSGSFFALLGPSGCGKTTTLRMVAGLEQPTDGTISIDGRDVTGTRahrrpVNTVFQsyalfPHL 106
Cdd:cd03220    30 GEVGEFWALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVTVRGRVSSLLG-----LGGGFN-----PEL 99

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054819401 107 TVAENVAFGLR--RRREADVEARVAEGLALVELGHLADRRPALLSGGQQQRVALARALVNRPALLLLDEPLGALDLKLRR 184
Cdd:cd03220   100 TGRENIYLNGRllGLSRKEIDEKIDEIIEFSELGDFIDLPVKTYSSGMKARLAFAIATALEPDILLIDEVLAVGDAAFQE 179

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 1054819401 185 QMQlelKRIQTEV--GLTFVHVTHDQEEAMTMADTVAVMNRGRIEQMG 230
Cdd:cd03220   180 KCQ---RRLRELLkqGKTVILVSHDPSSIKRLCDRALVLEKGKIRFDG 224
TagH COG1134
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ...
 27-238 4.47e-27

ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];


Pssm-ID: 440749 [Multi-domain]  Cd Length: 245  Bit Score: 107.86  E-value: 4.47e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054819401  27 KRFGAFVAVDDLTLTVPSGSFFALLGPSGCGKTTTLRMVAGLEQPTDGTISIDGRdVTGtrahrrP--VNTVFQsyalfP 104
Cdd:COG1134    34 TRREEFWALKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTSGRVEVNGR-VSA------LleLGAGFH-----P 101

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054819401 105 HLTVAENVAF-----GLRRrreADVEARVAEGLALVELGHLADRRPALLSGGQQQRVALARALVNRPALLLLDEPLGALD 179
Cdd:COG1134   102 ELTGRENIYLngrllGLSR---KEIDEKFDEIVEFAELGDFIDQPVKTYSSGMRARLAFAVATAVDPDILLVDEVLAVGD 178

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1054819401 180 LKLRRQMQLELKRIQTEvGLTFVHVTHDQEEAMTMADTVAVMNRGRIEQMGPPADLYEH 238
Cdd:COG1134   179 AAFQKKCLARIRELRES-GRTVIFVSHSMGAVRRLCDRAIWLEKGRLVMDGDPEEVIAA 236
PRK09984 PRK09984
phosphonate ABC transporter ATP-binding protein;
25-226 6.54e-27

phosphonate ABC transporter ATP-binding protein;


Pssm-ID: 182182 [Multi-domain]  Cd Length: 262  Bit Score: 107.79  E-value: 6.54e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054819401  25 VTKRFGAFVAVDDLTLTVPSGSFFALLGPSGCGKTTTLRMVAGL---EQPTDGTISIDG----------RDVTGTRAHrr 91
Cdd:PRK09984   10 LAKTFNQHQALHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGLitgDKSAGSHIELLGrtvqregrlaRDIRKSRAN-- 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054819401  92 pVNTVFQSYALFPHLTVAENVAFGLR----------RRREADVEARVAEGLALVELGHLADRRPALLSGGQQQRVALARA 161
Cdd:PRK09984   88 -TGYIFQQFNLVNRLSVLENVLIGALgstpfwrtcfSWFTREQKQRALQALTRVGMVHFAHQRVSTLSGGQQQRVAIARA 166

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1054819401 162 LVNRPALLLLDEPLGALDLKLRRQMQLELKRIQTEVGLTFVHVTHDQEEAMTMADTVAVMNRGRI 226
Cdd:PRK09984  167 LMQQAKVILADEPIASLDPESARIVMDTLRDINQNDGITVVVTLHQVDYALRYCERIVALRQGHV 231
ccmA TIGR01189
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ...
 20-179 1.44e-26

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: 105.13  E-value: 1.44e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054819401  20 LELAAVTKRFGAFVAVDDLTLTVPSGSFFALLGPSGCGKTTTLRMVAGLEQPTDGTISIDGRDVTGTRAHR-RPVNTVFQ 98
Cdd:TIGR01189   1 LAARNLACSRGERMLFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRWNGTPLAEQRDEPhENILYLGH 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054819401  99 SYALFPHLTVAENVAFGLRRRREADVEarVAEGLALVELGHLADRRPALLSGGQQQRVALARALVNRPALLLLDEPLGAL 178
Cdd:TIGR01189  81 LPGLKPELSALENLHFWAAIHGGAQRT--IEDALAAVGLTGFEDLPAAQLSAGQQRRLALARLWLSRRPLWILDEPTTAL 158


                  .
gi 1054819401 179 D 179
Cdd:TIGR01189 159 D 159
cbiO PRK13636
cobalt transporter ATP-binding subunit; Provisional
 34-236 1.48e-26

cobalt transporter ATP-binding subunit; Provisional


Pssm-ID: 184196 [Multi-domain]  Cd Length: 283  Bit Score: 107.24  E-value: 1.48e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054819401  34 AVDDLTLTVPSGSFFALLGPSGCGKTTTLRMVAGLEQPTDGTISIDGRDVTGTRAH----RRPVNTVFQS--YALFPhLT 107
Cdd:PRK13636   21 ALKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGKPIDYSRKGlmklRESVGMVFQDpdNQLFS-AS 99

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054819401 108 VAENVAFGLRRRR--EADVEARVAEGLALVELGHLADRRPALLSGGQQQRVALARALVNRPALLLLDEPLGALDLKLRRQ 185
Cdd:PRK13636  100 VYQDVSFGAVNLKlpEDEVRKRVDNALKRTGIEHLKDKPTHCLSFGQKKRVAIAGVLVMEPKVLVLDEPTAGLDPMGVSE 179

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1054819401 186 MQLELKRIQTEVGLTFVHVTHDQEEAMTMADTVAVMNRGRIEQMGPPADLY 236
Cdd:PRK13636  180 IMKLLVEMQKELGLTIIIATHDIDIVPLYCDNVFVMKEGRVILQGNPKEVF 230
YddA COG4178
ABC-type uncharacterized transport system, permease and ATPase components [General function ...
 35-206 1.62e-26

ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];


Pssm-ID: 443337 [Multi-domain]  Cd Length: 571  Bit Score: 111.05  E-value: 1.62e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054819401  35 VDDLTLTVPSGSffALL--GPSGCGKTTTLRMVAGLEQPTDGTIsidgrdvtgtrahRRP--VNTVF---QSYalFPHLT 107
Cdd:COG4178   379 LEDLSLSLKPGE--RLLitGPSGSGKSTLLRAIAGLWPYGSGRI-------------ARPagARVLFlpqRPY--LPLGT 441

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054819401 108 VAENVAFGLRRRREADveARVAEGLALVELGHLADR------RPALLSGGQQQRVALARALVNRPALLLLDEPLGALDLK 181
Cdd:COG4178   442 LREALLYPATAEAFSD--AELREALEAVGLGHLAERldeeadWDQVLSLGEQQRLAFARLLLHKPDWLFLDEATSALDEE 519

                         170       180
                  ....*....|....*....|....*.
gi 1054819401 182 LRRQMqleLKRIQTEV-GLTFVHVTH 206
Cdd:COG4178   520 NEAAL---YQLLREELpGTTVISVGH 542
PRK13539 PRK13539
cytochrome c biogenesis protein CcmA; Provisional
 37-179 1.66e-26

cytochrome c biogenesis protein CcmA; Provisional


Pssm-ID: 237421 [Multi-domain]  Cd Length: 207  Bit Score: 104.96  E-value: 1.66e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054819401  37 DLTLTVPSGSFFALLGPSGCGKTTTLRMVAGLEQPTDGTISIDGRDVTGTRaHRRPVNTVFQSYALFPHLTVAENVAF-- 114
Cdd:PRK13539   20 GLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDGGDIDDPD-VAEACHYLGHRNAMKPALTVAENLEFwa 98

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1054819401 115 GLRRRREADVEArvaeGLALVELGHLADRRPALLSGGQQQRVALARALV-NRPaLLLLDEPLGALD 179
Cdd:PRK13539   99 AFLGGEELDIAA----ALEAVGLAPLAHLPFGYLSAGQKRRVALARLLVsNRP-IWILDEPTAALD 159
PRK15112 PRK15112
peptide ABC transporter ATP-binding protein SapF;
34-239 1.80e-26

peptide ABC transporter ATP-binding protein SapF;


Pssm-ID: 185067 [Multi-domain]  Cd Length: 267  Bit Score: 106.80  E-value: 1.80e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054819401  34 AVDDLTLTVPSGSFFALLGPSGCGKTTTLRMVAGLEQPTDGTISIDGRDVT----GTRAHRrpVNTVFQ--SYALFPHLT 107
Cdd:PRK15112   28 AVKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDHPLHfgdySYRSQR--IRMIFQdpSTSLNPRQR 105

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054819401 108 VAENVAFGLRRRREADVEARVAE-GLALVELGHLADRR---PALLSGGQQQRVALARALVNRPALLLLDEPLGALDLKLR 183
Cdd:PRK15112  106 ISQILDFPLRLNTDLEPEQREKQiIETLRQVGLLPDHAsyyPHMLAPGQKQRLGLARALILRPKVIIADEALASLDMSMR 185

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1054819401 184 RQ---MQLELkriQTEVGLTFVHVThdQEEAMT--MADTVAVMNRGRIEQMGPPADLYEHP 239
Cdd:PRK15112  186 SQlinLMLEL---QEKQGISYIYVT--QHLGMMkhISDQVLVMHQGEVVERGSTADVLASP 241
PRK10253 PRK10253
iron-enterobactin ABC transporter ATP-binding protein;
25-235 3.21e-26

iron-enterobactin ABC transporter ATP-binding protein;


Pssm-ID: 182336 [Multi-domain]  Cd Length: 265  Bit Score: 105.84  E-value: 3.21e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054819401  25 VTKRFGAFVAVDDLTLTVPSGSFFALLGPSGCGKTTTLRMVAGLEQPTDGTISIDGRDVT--GTRAHRRPVNTVFQSYAL 102
Cdd:PRK10253   13 LTLGYGKYTVAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIQhyASKEVARRIGLLAQNATT 92

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054819401 103 FPHLTVAENVAFG-------LRRRREADVEArVAEGLALVELGHLADRRPALLSGGQQQRVALARALVNRPALLLLDEPL 175
Cdd:PRK10253   93 PGDITVQELVARGryphqplFTRWRKEDEEA-VTKAMQATGITHLADQSVDTLSGGQRQRAWIAMVLAQETAIMLLDEPT 171

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054819401 176 GALDLKLRRQMQLELKRIQTEVGLTFVHVTHDQEEAMTMADTVAVMNRGRIEQMGPPADL 235
Cdd:PRK10253  172 TWLDISHQIDLLELLSELNREKGYTLAAVLHDLNQACRYASHLIALREGKIVAQGAPKEI 231
rim_protein TIGR01257
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ...
 34-232 5.09e-26

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: 110.49  E-value: 5.09e-26
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054819401   34 AVDDLTLTVPSGSFFALLGPSGCGKTTTLRMVAGLEQPTDGTISIDGRDV-TGTRAHRRPVNTVFQSYALFPHLTVAENV 112
Cdd:TIGR01257  945 AVDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGKDIeTNLDAVRQSLGMCPQHNILFHHLTVAEHI 1024

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054819401  113 AFGLRRRREADVEARVaEGLALVE---LGHLADRRPALLSGGQQQRVALARALVNRPALLLLDEPLGALDLKLRRQMQLE 189
Cdd:TIGR01257 1025 LFYAQLKGRSWEEAQL-EMEAMLEdtgLHHKRNEEAQDLSGGMQRKLSVAIAFVGDAKVVVLDEPTSGVDPYSRRSIWDL 1103

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|...
gi 1054819401  190 LKRIQTevGLTFVHVTHDQEEAMTMADTVAVMNRGRIEQMGPP 232
Cdd:TIGR01257 1104 LLKYRS--GRTIIMSTHHMDEADLLGDRIAIISQGRLYCSGTP 1144
PRK10908 PRK10908
cell division ATP-binding protein FtsE;
29-226 5.81e-26

cell division ATP-binding protein FtsE;


Pssm-ID: 182829 [Multi-domain]  Cd Length: 222  Bit Score: 104.19  E-value: 5.81e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054819401  29 FGAFVAVDDLTLTVPSGSFFALLGPSGCGKTTTLRMVAGLEQPTDGTISIDGRDVTGTRAH-----RRPVNTVFQSYALF 103
Cdd:PRK10908   12 LGGRQALQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDITRLKNRevpflRRQIGMIFQDHHLL 91

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054819401 104 PHLTVAENVAFGL--RRRREADVEARVAEGLALVELGHLADRRPALLSGGQQQRVALARALVNRPALLLLDEPLGALDLK 181
Cdd:PRK10908   92 MDRTVYDNVAIPLiiAGASGDDIRRRVSAALDKVGLLDKAKNFPIQLSGGEQQRVGIARAVVNKPAVLLADEPTGNLDDA 171

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 1054819401 182 LRRQMqLELKRIQTEVGLTFVHVTHDQEEAMTMADTVAVMNRGRI 226
Cdd:PRK10908  172 LSEGI-LRLFEEFNRVGVTVLMATHDIGLISRRSYRMLTLSDGHL 215
ArpD COG4618
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ...
 33-234 6.68e-26

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: 109.07  E-value: 6.68e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054819401  33 VAVDDLTLTVPSGSFFALLGPSGCGKTTTLRMVAGLEQPTDGTISIDGRDVTG-TRAHRRP-VNTVFQSYALFPHlTVAE 110
Cdd:COG4618   346 PILRGVSFSLEPGEVLGVIGPSGSGKSTLARLLVGVWPPTAGSVRLDGADLSQwDREELGRhIGYLPQDVELFDG-TIAE 424

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054819401 111 NVAfglrRRREADVEARV-AEGLALV-EL-GHLAD-------RRPALLSGGQQQRVALARALVNRPALLLLDEPLGALD- 179
Cdd:COG4618   425 NIA----RFGDADPEKVVaAAKLAGVhEMiLRLPDgydtrigEGGARLSGGQRQRIGLARALYGDPRLVVLDEPNSNLDd 500

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1054819401 180 ---LKLRRQMQlELKriqtEVGLTFVHVTHDQeEAMTMADTVAVMNRGRIEQMGPPAD 234
Cdd:COG4618   501 egeAALAAAIR-ALK----ARGATVVVITHRP-SLLAAVDKLLVLRDGRVQAFGPRDE 552
PRK14243 PRK14243
phosphate transporter ATP-binding protein; Provisional
 20-246 9.55e-26

phosphate transporter ATP-binding protein; Provisional


Pssm-ID: 184588 [Multi-domain]  Cd Length: 264  Bit Score: 104.48  E-value: 9.55e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054819401  20 LELAAVTKRFGAFVAVDDLTLTVPSGSFFALLGPSGCGKTTTLR-------MVAGLEqpTDGTISIDGRDVTGTRAH--- 89
Cdd:PRK14243   11 LRTENLNVYYGSFLAVKNVWLDIPKNQITAFIGPSGCGKSTILRcfnrlndLIPGFR--VEGKVTFHGKNLYAPDVDpve 88

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054819401  90 -RRPVNTVFQSYALFPHlTVAENVAFGLR-RRREADVEARVAEGLALVEL-GHLAD--RRPAL-LSGGQQQRVALARALV 163
Cdd:PRK14243   89 vRRRIGMVFQKPNPFPK-SIYDNIAYGARiNGYKGDMDELVERSLRQAALwDEVKDklKQSGLsLSGGQQQRLCIARAIA 167

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054819401 164 NRPALLLLDEPLGALD----LKLRRQMQlELKRiqtevGLTFVHVTHDQEEAMTMADTVAVMNRGRIEQMGPPADLYEHP 239
Cdd:PRK14243  168 VQPEVILMDEPCSALDpistLRIEELMH-ELKE-----QYTIIIVTHNMQQAARVSDMTAFFNVELTEGGGRYGYLVEFD 241


                  ....*..
gi 1054819401 240 RTTFVAN 246
Cdd:PRK14243  242 RTEKIFN 248
ABCC_Hemolysin cd03252
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ...
 20-230 9.76e-26

ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a central component of the secretion machinery that translocates the toxin, hemolysin A, in a Sec-independent fashion across both membranes of E. coli. The hemolysin A (HlyA) transport machinery is composed of the ATP-binding cassette (ABC) transporter HlyB located in the inner membrane, hemolysin D (HlyD), also anchored in the inner membrane, and TolC, which resides in the outer membrane. HlyD apparently forms a continuous channel that bridges the entire periplasm, interacting with TolC and HlyB. This arrangement prevents the appearance of periplasmic intermediates of HlyA during substrate transport. Little is known about the molecular details of HlyA transport, but it is evident that ATP-hydrolysis by the ABC-transporter HlyB is a necessary source of energy.


Pssm-ID: 213219 [Multi-domain]  Cd Length: 237  Bit Score: 104.11  E-value: 9.76e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054819401  20 LELAAVTKRFGA--FVAVDDLTLTVPSGSFFALLGPSGCGKTTTLRMVAGLEQPTDGTISIDGRDV--TGTRAHRRPVNT 95
Cdd:cd03252     1 ITFEHVRFRYKPdgPVILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGHDLalADPAWLRRQVGV 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054819401  96 VFQSYALFpHLTVAENVAFG-----LRRRREAdveARVAEGLALV-EL----GHLADRRPALLSGGQQQRVALARALVNR 165
Cdd:cd03252    81 VLQENVLF-NRSIRDNIALAdpgmsMERVIEA---AKLAGAHDFIsELpegyDTIVGEQGAGLSGGQRQRIAIARALIHN 156

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1054819401 166 PALLLLDEPLGALDLKLRRQMQLELKRIQTevGLTFVHVTHDQEEAMTmADTVAVMNRGRIEQMG 230
Cdd:cd03252   157 PRILIFDEATSALDYESEHAIMRNMHDICA--GRTVIIIAHRLSTVKN-ADRIIVMEKGRIVEQG 218
cbiO PRK13638
energy-coupling factor ABC transporter ATP-binding protein;
38-236 1.03e-25

energy-coupling factor ABC transporter ATP-binding protein;


Pssm-ID: 184198 [Multi-domain]  Cd Length: 271  Bit Score: 104.70  E-value: 1.03e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054819401  38 LTLTVPSGSFFALLGPSGCGKTTTLRMVAGLEQPTDGTISIDGRDVT----GTRAHRRPVNTVFQ--SYALFpHLTVAEN 111
Cdd:PRK13638   20 LNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLRPQKGAVLWQGKPLDyskrGLLALRQQVATVFQdpEQQIF-YTDIDSD 98

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054819401 112 VAFGLRRR--READVEARVAEGLALVELGHLADRRPALLSGGQQQRVALARALVNRPALLLLDEPLGALDLKLRRQMQLE 189
Cdd:PRK13638   99 IAFSLRNLgvPEAEITRRVDEALTLVDAQHFRHQPIQCLSHGQKKRVAIAGALVLQARYLLLDEPTAGLDPAGRTQMIAI 178

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 1054819401 190 LKRIQTEvGLTFVHVTHDQEEAMTMADTVAVMNRGRIEQMGPPADLY 236
Cdd:PRK13638  179 IRRIVAQ-GNHVIISSHDIDLIYEISDAVYVLRQGQILTHGAPGEVF 224
ABC_Carb_Monos_II cd03215
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ...
 34-226 1.13e-25

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: 102.13  E-value: 1.13e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054819401  34 AVDDLTLTVPSGSFFALLGPSGCGKTTTLRMVAGLEQPTDGTISIDGRDVTGTRAHRRPVNTVF------QSYALFPHLT 107
Cdd:cd03215    15 AVRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITLDGKPVTRRSPRDAIRAGIAyvpedrKREGLVLDLS 94

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054819401 108 VAENVAFglrrrreadvearvaeglalvelghladrrPALLSGGQQQRVALARALVNRPALLLLDEPLGALDLKLRRQMq 187
Cdd:cd03215    95 VAENIAL------------------------------SSLLSGGNQQKVVLARWLARDPRVLILDEPTRGVDVGAKAEI- 143

                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 1054819401 188 LELKRIQTEVGLTFVHVTHDQEEAMTMADTVAVMNRGRI 226
Cdd:cd03215   144 YRLIRELADAGKAVLLISSELDELLGLCDRILVMYEGRI 182
Uup COG0488
ATPase components of ABC transporters with duplicated ATPase domains [General function ...
 25-174 1.33e-25

ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];


Pssm-ID: 440254 [Multi-domain]  Cd Length: 520  Bit Score: 108.23  E-value: 1.33e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054819401  25 VTKRFGAFVAVDDLTLTVPSGSFFALLGPSGCGKTTTLRMVAGLEQPTDGTISIDGrdvtGTRahrrpVNTVFQSYALFP 104
Cdd:COG0488     4 LSKSFGGRPLLDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEVSIPK----GLR-----IGYLPQEPPLDD 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054819401 105 HLTVAENVAFGLRRRREA----------------------------------DVEARVAEglALVELG---HLADRRPAL 147
Cdd:COG0488    75 DLTVLDTVLDGDAELRALeaeleeleaklaepdedlerlaelqeefealggwEAEARAEE--ILSGLGfpeEDLDRPVSE 152

                         170       180
                  ....*....|....*....|....*..
gi 1054819401 148 LSGGQQQRVALARALVNRPALLLLDEP 174
Cdd:COG0488   153 LSGGWRRRVALARALLSEPDLLLLDEP 179
PRK10261 PRK10261
glutathione transporter ATP-binding protein; Provisional
 34-240 1.60e-25

glutathione transporter ATP-binding protein; Provisional


Pssm-ID: 182342 [Multi-domain]  Cd Length: 623  Bit Score: 108.40  E-value: 1.60e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054819401  34 AVDDLTLTVPSGSFFALLGPSGCGKTTTLRMVAGLEQPTDGTISIDGRDV-----TGTRAHRRPVNTVFQS-YA-LFPHL 106
Cdd:PRK10261  339 AVEKVSFDLWPGETLSLVGESGSGKSTTGRALLRLVESQGGEIIFNGQRIdtlspGKLQALRRDIQFIFQDpYAsLDPRQ 418

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054819401 107 TVAENVAFGLRRRREADVEA---RVAEGLALVEL-GHLADRRPALLSGGQQQRVALARALVNRPALLLLDEPLGALDLKL 182
Cdd:PRK10261  419 TVGDSIMEPLRVHGLLPGKAaaaRVAWLLERVGLlPEHAWRYPHEFSGGQRQRICIARALALNPKVIIADEAVSALDVSI 498

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1054819401 183 RRQMQLELKRIQTEVGLTFVHVTHDQEEAMTMADTVAVMNRGRIEQMGPPADLYEHPR 240
Cdd:PRK10261  499 RGQIINLLLDLQRDFGIAYLFISHDMAVVERISHRVAVMYLGQIVEIGPRRAVFENPQ 556
cbiO PRK13644
energy-coupling factor transporter ATPase;
34-239 3.64e-25

energy-coupling factor transporter ATPase;


Pssm-ID: 106587 [Multi-domain]  Cd Length: 274  Bit Score: 103.14  E-value: 3.64e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054819401  34 AVDDLTLTVPSGSFFALLGPSGCGKTTTLRMVAGLEQPTDGTI---SIDGRDVTGTRAHRRPVNTVFQS-YALFPHLTVA 109
Cdd:PRK13644   17 ALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVlvsGIDTGDFSKLQGIRKLVGIVFQNpETQFVGRTVE 96

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054819401 110 ENVAFGLRRR--READVEARVAEGLALVELGHLADRRPALLSGGQQQRVALARALVNRPALLLLDEPLGALDLKLRRQMQ 187
Cdd:PRK13644   97 EDLAFGPENLclPPIEIRKRVDRALAEIGLEKYRHRSPKTLSGGQGQCVALAGILTMEPECLIFDEVTSMLDPDSGIAVL 176

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1054819401 188 LELKRIQtEVGLTFVHVTHDQEEaMTMADTVAVMNRGRIEQMGPPADLYEHP 239
Cdd:PRK13644  177 ERIKKLH-EKGKTIVYITHNLEE-LHDADRIIVMDRGKIVLEGEPENVLSDV 226
PRK10895 PRK10895
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
 35-235 4.06e-25

lipopolysaccharide ABC transporter ATP-binding protein; Provisional


Pssm-ID: 182817 [Multi-domain]  Cd Length: 241  Bit Score: 102.28  E-value: 4.06e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054819401  35 VDDLTLTVPSGSFFALLGPSGCGKTTTLRMVAGLEQPTDGTISIDGRDVTGTRAH---RRPVNTVFQSYALFPHLTVAEN 111
Cdd:PRK10895   19 VEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEDISLLPLHaraRRGIGYLPQEASIFRRLSVYDN 98

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054819401 112 VAFGLRRRREADVEARVAEGLALVELGHLADRRPAL---LSGGQQQRVALARALVNRPALLLLDEPLGALDlklrRQMQL 188
Cdd:PRK10895   99 LMAVLQIRDDLSAEQREDRANELMEEFHIEHLRDSMgqsLSGGERRRVEIARALAANPKFILLDEPFAGVD----PISVI 174

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 1054819401 189 ELKRIQTEV---GLTFVHVTHDQEEAMTMADTVAVMNRGRIEQMGPPADL 235
Cdd:PRK10895  175 DIKRIIEHLrdsGLGVLITDHNVRETLAVCERAYIVSQGHLIAHGTPTEI 224
PRK15439 PRK15439
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
 20-235 5.42e-25

autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional


Pssm-ID: 185336 [Multi-domain]  Cd Length: 510  Bit Score: 106.29  E-value: 5.42e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054819401  20 LELAAVTKRFGAFVAVDDLTLTVPSGSFFALLGPSGCGKTTTLRMVAGLEQPTDGTISIDGRDVTG---TRAHRRPVNTV 96
Cdd:PRK15439   12 LCARSISKQYSGVEVLKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIGGNPCARltpAKAHQLGIYLV 91

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054819401  97 FQSYALFPHLTVAENVAFGLRRRREAdvEARVAEGLAlvELG-HLA-DRRPALLSGGQQQRVALARALVNRPALLLLDEP 174
Cdd:PRK15439   92 PQEPLLFPNLSVKENILFGLPKRQAS--MQKMKQLLA--ALGcQLDlDSSAGSLEVADRQIVEILRGLMRDSRILILDEP 167

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1054819401 175 LGALD----LKLRRQMQLELkriQTEVGLTFvhVTHDQEEAMTMADTVAVMNRGRIEQMGPPADL 235
Cdd:PRK15439  168 TASLTpaetERLFSRIRELL---AQGVGIVF--ISHKLPEIRQLADRISVMRDGTIALSGKTADL 227
ABCG_White cd03234
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ...
 37-226 1.34e-24

White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ABC transporters homologous to the Drosophila white gene, which acts as a dimeric importer for eye pigment precursors. The eye pigmentation of Drosophila is developed from the synthesis and deposition in the cells of red pigments, which are synthesized from guanine, and brown pigments, which are synthesized from tryptophan. The pigment precursors are encoded by the white, brown, and scarlet genes, respectively. Evidence from genetic and biochemical studies suggest that the White and Brown proteins function as heterodimers to import guanine, while the White and Scarlet proteins function to import tryptophan. However, a recent study also suggests that White may be involved in the transport of a metabolite, such as 3-hydroxykynurenine, across intracellular membranes. Mammalian ABC transporters belonging to the White subfamily (ABCG1, ABCG5, and ABCG8) have been shown to be involved in the regulation of lipid-trafficking mechanisms in macrophages, hepatocytes, and intestinal mucosa cells. ABCG1 (ABC8), the human homolog of the Drosophila white gene is induced in monocyte-derived macrophages during cholesterol influx mediated by acetylated low-density lipoprotein. It is possible that human ABCG1 forms heterodimers with several heterologous partners.


Pssm-ID: 213201 [Multi-domain]  Cd Length: 226  Bit Score: 100.42  E-value: 1.34e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054819401  37 DLTLTVPSGSFFALLGPSGCGKTTTLRMVAGLEQP---TDGTISIDGRDVtgtRAH--RRPVNTVFQSYALFPHLTVAEN 111
Cdd:cd03234    25 DVSLHVESGQVMAILGSSGSGKTTLLDAISGRVEGggtTSGQILFNGQPR---KPDqfQKCVAYVRQDDILLPGLTVRET 101

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054819401 112 VAFGL-----RRRREADVEARVA-EGLALVELGHLADRRPALLSGGQQQRVALARALVNRPALLLLDEPLGALDLKLRRQ 185
Cdd:cd03234   102 LTYTAilrlpRKSSDAIRKKRVEdVLLRDLALTRIGGNLVKGISGGERRRVSIAVQLLWDPKVLILDEPTSGLDSFTALN 181

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 1054819401 186 MQLELKRIQTEVGLTFVHVTHDQEEAMTMADTVAVMNRGRI 226
Cdd:cd03234   182 LVSTLSQLARRNRIVILTIHQPRSDLFRLFDRILLLSSGEI 222
PRK15134 PRK15134
microcin C ABC transporter ATP-binding protein YejF; Provisional
 33-240 3.18e-24

microcin C ABC transporter ATP-binding protein YejF; Provisional


Pssm-ID: 237917 [Multi-domain]  Cd Length: 529  Bit Score: 104.02  E-value: 3.18e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054819401  33 VAVDDLTLTVPSGSFFALLGPSGCGKTTT----LRMVAgleqpTDGTISIDGRDVTGTRAH-----RRPVNTVFQ--SYA 101
Cdd:PRK15134  300 VVVKNISFTLRPGETLGLVGESGSGKSTTglalLRLIN-----SQGEIWFDGQPLHNLNRRqllpvRHRIQVVFQdpNSS 374

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054819401 102 LFPHLTVAENVAFGLRRRRE----ADVEARVAEglALVELGHLADRR---PALLSGGQQQRVALARALVNRPALLLLDEP 174
Cdd:PRK15134  375 LNPRLNVLQIIEEGLRVHQPtlsaAQREQQVIA--VMEEVGLDPETRhryPAEFSGGQRQRIAIARALILKPSLIILDEP 452

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1054819401 175 LGALDLKLRRQMQLELKRIQTEVGLTFVHVTHDQEEAMTMADTVAVMNRGRIEQMGPPADLYEHPR 240
Cdd:PRK15134  453 TSSLDKTVQAQILALLKSLQQKHQLAYLFISHDLHVVRALCHQVIVLRQGEVVEQGDCERVFAAPQ 518
PRK13538 PRK13538
cytochrome c biogenesis heme-transporting ATPase CcmA;
36-179 4.07e-24

cytochrome c biogenesis heme-transporting ATPase CcmA;


Pssm-ID: 184125 [Multi-domain]  Cd Length: 204  Bit Score: 98.72  E-value: 4.07e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054819401  36 DDLTLTVPSGSFFALLGPSGCGKTTTLRMVAGLEQPTDGTISIDGRDVTGTRAHrrpvntvFQSYALF--------PHLT 107
Cdd:PRK13538   18 SGLSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVLWQGEPIRRQRDE-------YHQDLLYlghqpgikTELT 90

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1054819401 108 VAENVAFGLRRRREADvEARVAEGLALVELGHLADRRPALLSGGQQQRVALARALVNRPALLLLDEPLGALD 179
Cdd:PRK13538   91 ALENLRFYQRLHGPGD-DEALWEALAQVGLAGFEDVPVRQLSAGQQRRVALARLWLTRAPLWILDEPFTAID 161
ABC2_perm_RbbA NF033858
ribosome-associated ATPase/putative transporter RbbA;
21-245 7.20e-24

ribosome-associated ATPase/putative transporter RbbA;


Pssm-ID: 468210 [Multi-domain]  Cd Length: 907  Bit Score: 103.67  E-value: 7.20e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054819401  21 ELAAVTKRFGAFVAVDDLTLTVPSGSFFALLGPSGCGKTTTLRMVAGLEQPTDGTISIDGRDVtGTRAHRRPV------- 93
Cdd:NF033858    3 RLEGVSHRYGKTVALDDVSLDIPAGCMVGLIGPDGVGKSSLLSLIAGARKIQQGRVEVLGGDM-ADARHRRAVcpriaym 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054819401  94 ------NtvfqsyaLFPHLTVAENVAF-----GLRRrreADVEARVAEGLALVELGHLADRRPALLSGGQQQRVALARAL 162
Cdd:NF033858   82 pqglgkN-------LYPTLSVFENLDFfgrlfGQDA---AERRRRIDELLRATGLAPFADRPAGKLSGGMKQKLGLCCAL 151

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054819401 163 VNRPALLLLDEPLGALDLKLRRQM-QLeLKRIQTE-VGLTFVHVTHDQEEAMTMaDTVAVMNRGRIEQMGPPADLYEHPR 240
Cdd:NF033858  152 IHDPDLLILDEPTTGVDPLSRRQFwEL-IDRIRAErPGMSVLVATAYMEEAERF-DWLVAMDAGRVLATGTPAELLARTG 229

                         250
                  ....*....|
gi 1054819401 241 TT-----FVA 245
Cdd:NF033858  230 ADtleaaFIA 239
PRK14239 PRK14239
phosphate transporter ATP-binding protein; Provisional
 34-239 1.04e-23

phosphate transporter ATP-binding protein; Provisional


Pssm-ID: 184585 [Multi-domain]  Cd Length: 252  Bit Score: 98.69  E-value: 1.04e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054819401  34 AVDDLTLTVPSGSFFALLGPSGCGKTTTLRMVAGL-----EQPTDGTISIDGRDVTGTRAH----RRPVNTVFQSYALFP 104
Cdd:PRK14239   20 ALNSVSLDFYPNEITALIGPSGSGKSTLLRSINRMndlnpEVTITGSIVYNGHNIYSPRTDtvdlRKEIGMVFQQPNPFP 99

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054819401 105 hLTVAENVAFGLRRRREAD---VEARVAEGLALVEL-GHLADR--RPAL-LSGGQQQRVALARALVNRPALLLLDEPLGA 177
Cdd:PRK14239  100 -MSIYENVVYGLRLKGIKDkqvLDEAVEKSLKGASIwDEVKDRlhDSALgLSGGQQQRVCIARVLATSPKIILLDEPTSA 178

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1054819401 178 LDLKLRRQMQLELKRIQTEvgLTFVHVTHDQEEAMTMADTVAVMNRGRIEQMGPPADLYEHP 239
Cdd:PRK14239  179 LDPISAGKIEETLLGLKDD--YTMLLVTRSMQQASRISDRTGFFLDGDLIEYNDTKQMFMNP 238
type_I_sec_PrtD TIGR01842
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in ...
 30-231 1.28e-23

type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in some Gram-negative bacteria to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type I secretion apparatus. Targeted proteins are not cleaved at the N-terminus, but rather carry signals located toward the extreme C-terminus to direct type I secretion. [Protein fate, Protein and peptide secretion and trafficking]


Pssm-ID: 200134 [Multi-domain]  Cd Length: 544  Bit Score: 102.43  E-value: 1.28e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054819401  30 GAFVAVDDLTLTVPSGSFFALLGPSGCGKTTTLRMVAGLEQPTDGTISIDGRDVT--GTRAHRRPVNTVFQSYALFPHlT 107
Cdd:TIGR01842 329 GKKPTLRGISFSLQAGEALAIIGPSGSGKSTLARLIVGIWPPTSGSVRLDGADLKqwDRETFGKHIGYLPQDVELFPG-T 407

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054819401 108 VAENVA-FGLRRRREADVEARVAEGLALVELG-------HLADRrPALLSGGQQQRVALARALVNRPALLLLDEPLGALD 179
Cdd:TIGR01842 408 VAENIArFGENADPEKIIEAAKLAGVHELILRlpdgydtVIGPG-GATLSGGQRQRIALARALYGDPKLVVLDEPNSNLD 486

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1054819401 180 LKLRRQMQLELKRIQTEvGLTFVHVTHdQEEAMTMADTVAVMNRGRIEQMGP 231
Cdd:TIGR01842 487 EEGEQALANAIKALKAR-GITVVVITH-RPSLLGCVDKILVLQDGRIARFGE 536
COG4586 COG4586
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ...
 34-226 1.34e-23

ABC-type uncharacterized transport system, ATPase component [General function prediction only];


Pssm-ID: 443643 [Multi-domain]  Cd Length: 323  Bit Score: 99.78  E-value: 1.34e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054819401  34 AVDDLTLTVPSGSFFALLGPSGCGKTTTLRMVAGLEQPTDGTISIDGRD-VTGTRAHRRPVNTVF-QSYALFPHLTVAEN 111
Cdd:COG4586    37 AVDDISFTIEPGEIVGFIGPNGAGKSTTIKMLTGILVPTSGEVRVLGYVpFKRRKEFARRIGVVFgQRSQLWWDLPAIDS 116

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054819401 112 vaFGLRRR----READVEARVAEGLALVELGHLADRRPALLSGGQQQRVALARALVNRPALLLLDEP-LGaLDLKLRRQM 186
Cdd:COG4586   117 --FRLLKAiyriPDAEYKKRLDELVELLDLGELLDTPVRQLSLGQRMRCELAAALLHRPKILFLDEPtIG-LDVVSKEAI 193

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 1054819401 187 QLELKRIQTEVGLTFVHVTHDQEEAMTMADTVAVMNRGRI 226
Cdd:COG4586   194 REFLKEYNRERGTTILLTSHDMDDIEALCDRVIVIDHGRI 233
ABCC_TAP cd03248
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ...
 37-187 1.71e-23

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: 97.54  E-value: 1.71e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054819401  37 DLTLTVPSGSFFALLGPSGCGKTTTLRMVAGLEQPTDGTISIDGRDVTG--TRAHRRPVNTVFQSYALFPHlTVAENVAF 114
Cdd:cd03248    32 DVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDGKPISQyeHKYLHSKVSLVGQEPVLFAR-SLQDNIAY 110

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054819401 115 GLR-----RRREADVEARVAEGLALVELGHL--ADRRPALLSGGQQQRVALARALVNRPALLLLDEPLGALDLKLRRQMQ 187
Cdd:cd03248   111 GLQscsfeCVKEAAQKAHAHSFISELASGYDteVGEKGSQLSGGQKQRVAIARALIRNPQVLILDEATSALDAESEQQVQ 190
cbiO PRK13645
energy-coupling factor transporter ATPase;
32-238 1.75e-23

energy-coupling factor transporter ATPase;


Pssm-ID: 184204 [Multi-domain]  Cd Length: 289  Bit Score: 98.93  E-value: 1.75e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054819401  32 FVAVDDLTLTVPSGSFFALLGPSGCGKTTTLRMVAGL-----EQPTDGTISIDG--RDVTGTRAHRRPVNTVFQ--SYAL 102
Cdd:PRK13645   24 FKALNNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGLiisetGQTIVGDYAIPAnlKKIKEVKRLRKEIGLVFQfpEYQL 103

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054819401 103 FPHlTVAENVAFGLRRRREADVEA--RVAEGLALVELGH-LADRRPALLSGGQQQRVALARALVNRPALLLLDEPLGALD 179
Cdd:PRK13645  104 FQE-TIEKDIAFGPVNLGENKQEAykKVPELLKLVQLPEdYVKRSPFELSGGQKRRVALAGIIAMDGNTLVLDEPTGGLD 182

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1054819401 180 LKLRRQMQLELKRIQTEVGLTFVHVTHDQEEAMTMADTVAVMNRGRIEQMGPPADLYEH 238
Cdd:PRK13645  183 PKGEEDFINLFERLNKEYKKRIIMVTHNMDQVLRIADEVIVMHEGKVISIGSPFEIFSN 241
PRK14271 PRK14271
phosphate ABC transporter ATP-binding protein; Provisional
 22-249 3.52e-23

phosphate ABC transporter ATP-binding protein; Provisional


Pssm-ID: 172759 [Multi-domain]  Cd Length: 276  Bit Score: 97.86  E-value: 3.52e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054819401  22 LAAV--TKRFGAFVAVDDLTLTVPSGSFFALLGPSGCGKTTTLRMVAGLEQPTDG-----TISIDGRDVTGTR---AHRR 91
Cdd:PRK14271   22 MAAVnlTLGFAGKTVLDQVSMGFPARAVTSLMGPTGSGKTTFLRTLNRMNDKVSGyrysgDVLLGGRSIFNYRdvlEFRR 101

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054819401  92 PVNTVFQSYALFPhLTVAENVAFGLRR-----RRE--ADVEARVAE-GLALVELGHLADRrPALLSGGQQQRVALARALV 163
Cdd:PRK14271  102 RVGMLFQRPNPFP-MSIMDNVLAGVRAhklvpRKEfrGVAQARLTEvGLWDAVKDRLSDS-PFRLSGGQQQLLCLARTLA 179

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054819401 164 NRPALLLLDEPLGALDLKLRRQMQLELKRIQTEvgLTFVHVTHDQEEAMTMADTVAVMNRGRIEQMGPPADLYEHPRTTF 243
Cdd:PRK14271  180 VNPEVLLLDEPTSALDPTTTEKIEEFIRSLADR--LTVIIVTHNLAQAARISDRAALFFDGRLVEEGPTEQLFSSPKHAE 257


                  ....*.
gi 1054819401 244 VANFLG 249
Cdd:PRK14271  258 TARYVA 263
cbiO PRK13631
cobalt transporter ATP-binding subunit; Provisional
 32-239 5.63e-23

cobalt transporter ATP-binding subunit; Provisional


Pssm-ID: 237451 [Multi-domain]  Cd Length: 320  Bit Score: 98.00  E-value: 5.63e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054819401  32 FVAVDDLTLTVPSGSFFALLGPSGCGKTTTLRMVAGLEQPTDGTISID----GRDVTGTRAH--------------RRPV 93
Cdd:PRK13631   39 LVALNNISYTFEKNKIYFIIGNSGSGKSTLVTHFNGLIKSKYGTIQVGdiyiGDKKNNHELItnpyskkiknfkelRRRV 118

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054819401  94 NTVFQ--SYALFPHlTVAENVAFGLRRRREADVEARVAEGLALVELG---HLADRRPALLSGGQQQRVALARALVNRPAL 168
Cdd:PRK13631  119 SMVFQfpEYQLFKD-TIEKDIMFGPVALGVKKSEAKKLAKFYLNKMGlddSYLERSPFGLSGGQKRRVAIAGILAIQPEI 197

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1054819401 169 LLLDEPLGALDLKLRRQMqLELKRIQTEVGLTFVHVTHDQEEAMTMADTVAVMNRGRIEQMGPPADLYEHP 239
Cdd:PRK13631  198 LIFDEPTAGLDPKGEHEM-MQLILDAKANNKTVFVITHTMEHVLEVADEVIVMDKGKILKTGTPYEIFTDQ 267
znuC PRK09544
high-affinity zinc transporter ATPase; Reviewed
 22-247 5.90e-23

high-affinity zinc transporter ATPase; Reviewed


Pssm-ID: 181939 [Multi-domain]  Cd Length: 251  Bit Score: 96.72  E-value: 5.90e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054819401  22 LAAVTKRFGAFVAVDDLTLTVPSGSFFALLGPSGCGKTTTLRMVAGLEQPTDGTISidgrdvtgtRAHRRPVNTVFQSYA 101
Cdd:PRK09544    7 LENVSVSFGQRRVLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIK---------RNGKLRIGYVPQKLY 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054819401 102 LFPH--LTVAEnvafgLRRRREADVEARVAEGLALVELGHLADRRPALLSGGQQQRVALARALVNRPALLLLDEPLGALD 179
Cdd:PRK09544   78 LDTTlpLTVNR-----FLRLRPGTKKEDILPALKRVQAGHLIDAPMQKLSGGETQRVLLARALLNRPQLLVLDEPTQGVD 152

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1054819401 180 LKLRRQMQLELKRIQTEVGLTFVHVTHDQEEAMTMADTVAVMNRgRIEQMGPPADLYEHPRttFVANF 247
Cdd:PRK09544  153 VNGQVALYDLIDQLRRELDCAVLMVSHDLHLVMAKTDEVLCLNH-HICCSGTPEVVSLHPE--FISMF 217
PRK14258 PRK14258
phosphate ABC transporter ATP-binding protein; Provisional
 35-229 6.60e-23

phosphate ABC transporter ATP-binding protein; Provisional


Pssm-ID: 184593 [Multi-domain]  Cd Length: 261  Bit Score: 96.64  E-value: 6.60e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054819401  35 VDDLTLTVPSGSFFALLGPSGCGKTTTLRMVAGL-----EQPTDGTISIDGRDVTGTRAH----RRPVNTVFQSYALFPh 105
Cdd:PRK14258   23 LEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLNRMnelesEVRVEGRVEFFNQNIYERRVNlnrlRRQVSMVHPKPNLFP- 101

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054819401 106 LTVAENVAFGL-----RRRREAD--VEARVAEGLALVELGHLADRRPALLSGGQQQRVALARALVNRPALLLLDEPLGAL 178
Cdd:PRK14258  102 MSVYDNVAYGVkivgwRPKLEIDdiVESALKDADLWDEIKHKIHKSALDLSGGQQQRLCIARALAVKPKVLLMDEPCFGL 181

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1054819401 179 DLKLRRQMQLELKRIQTEVGLTFVHVTHDQEEAMTMADTVAVM--NRGRIEQM 229
Cdd:PRK14258  182 DPIASMKVESLIQSLRLRSELTMVIVSHNLHQVSRLSDFTAFFkgNENRIGQL 234
livF PRK11614
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
20-226 7.74e-23

high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;


Pssm-ID: 183231 [Multi-domain]  Cd Length: 237  Bit Score: 96.10  E-value: 7.74e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054819401  20 LELAAVTKRFGAFVAVDDLTLTVPSGSFFALLGPSGCGKTTTLRMVAGLEQPTDGTISIDGRDVTG---TRAHRRPVNTV 96
Cdd:PRK11614    6 LSFDKVSAHYGKIQALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDGKDITDwqtAKIMREAVAIV 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054819401  97 FQSYALFPHLTVAENVAFGLRRRREADVEARVAEGLALV-ELGHLADRRPALLSGGQQQRVALARALVNRPALLLLDEPL 175
Cdd:PRK11614   86 PEGRRVFSRMTVEENLAMGGFFAERDQFQERIKWVYELFpRLHERRIQRAGTMSGGEQQMLAIGRALMSQPRLLLLDEPS 165

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1054819401 176 GALDLKLRRQMQLELKRIQTEvGLTFVHVTHDQEEAMTMADTVAVMNRGRI 226
Cdd:PRK11614  166 LGLAPIIIQQIFDTIEQLREQ-GMTIFLVEQNANQALKLADRGYVLENGHV 215
PRK11160 PRK11160
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
 34-235 1.27e-22

cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed


Pssm-ID: 236865 [Multi-domain]  Cd Length: 574  Bit Score: 99.51  E-value: 1.27e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054819401  34 AVDDLTLTVPSGSFFALLGPSGCGKTTTLRMVAGLEQPTDGTISIDGRDVTG--TRAHRRPVNTVFQSYALFPHlTVAEN 111
Cdd:PRK11160  355 VLKGLSLQIKAGEKVALLGRTGCGKSTLLQLLTRAWDPQQGEILLNGQPIADysEAALRQAISVVSQRVHLFSA-TLRDN 433

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054819401 112 VAFGLrrrREADvEARVAEGLALVELGHLADRRPAL----------LSGGQQQRVALARALVNRPALLLLDEPLGALDLK 181
Cdd:PRK11160  434 LLLAA---PNAS-DEALIEVLQQVGLEKLLEDDKGLnawlgeggrqLSGGEQRRLGIARALLHDAPLLLLDEPTEGLDAE 509

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1054819401 182 LRRQ-MQLELKRIQtevGLTFVHVTHdQEEAMTMADTVAVMNRGRIEQMGPPADL 235
Cdd:PRK11160  510 TERQiLELLAEHAQ---NKTVLMITH-RLTGLEQFDRICVMDNGQIIEQGTHQEL 560
PRK10575 PRK10575
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
38-235 1.68e-22

Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;


Pssm-ID: 182561 [Multi-domain]  Cd Length: 265  Bit Score: 95.62  E-value: 1.68e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054819401  38 LTLTVPSGSFFALLGPSGCGKTTTLRMVAGLEQPTDGTISIDGRDVTG--TRAHRRPVNTVFQSYALFPHLTVAENVAFG 115
Cdd:PRK10575   30 LSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPLESwsSKAFARKVAYLPQQLPAAEGMTVRELVAIG 109

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054819401 116 -------LRRRREADVEaRVAEGLALVELGHLADRRPALLSGGQQQRVALARALVNRPALLLLDEPLGALDLKLRRQMQL 188
Cdd:PRK10575  110 rypwhgaLGRFGAADRE-KVEEAISLVGLKPLAHRLVDSLSGGERQRAWIAMLVAQDSRCLLLDEPTSALDIAHQVDVLA 188

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 1054819401 189 ELKRIQTEVGLTFVHVTHDQEEAMTMADTVAVMNRGRIEQMGPPADL 235
Cdd:PRK10575  189 LVHRLSQERGLTVIAVLHDINMAARYCDYLVALRGGEMIAQGTPAEL 235
PRK13657 PRK13657
glucan ABC transporter ATP-binding protein/ permease;
34-230 1.87e-22

glucan ABC transporter ATP-binding protein/ permease;


Pssm-ID: 184214 [Multi-domain]  Cd Length: 588  Bit Score: 99.27  E-value: 1.87e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054819401  34 AVDDLTLTVPSGSFFALLGPSGCGKTTTLRMVAGLEQPTDGTISIDGRDVTG-TRAH-RRPVNTVFQSYALFpHLTVAEN 111
Cdd:PRK13657  350 GVEDVSFEAKPGQTVAIVGPTGAGKSTLINLLQRVFDPQSGRILIDGTDIRTvTRASlRRNIAVVFQDAGLF-NRSIEDN 428

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054819401 112 VAFGLRRRREADVE--ARVAEGLALVE-----LGHLADRRPALLSGGQQQRVALARALVNRPALLLLDEPLGALDLKLRR 184
Cdd:PRK13657  429 IRVGRPDATDEEMRaaAERAQAHDFIErkpdgYDTVVGERGRQLSGGERQRLAIARALLKDPPILILDEATSALDVETEA 508

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 1054819401 185 QMQLELKRIqTEVGLTFVhVTHdQEEAMTMADTVAVMNRGRIEQMG 230
Cdd:PRK13657  509 KVKAALDEL-MKGRTTFI-IAH-RLSTVRNADRILVFDNGRVVESG 551
CydC TIGR02868
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ...
 20-207 3.35e-22

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: 98.20  E-value: 3.35e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054819401  20 LELAAVTKRF-GAFVAVDDLTLTVPSGSFFALLGPSGCGKTTTLRMVAGLEQPTDGTISIDGRDVTGTR--AHRRPVNTV 96
Cdd:TIGR02868 335 LELRDLSAGYpGAPPVLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPLQGEVTLDGVPVSSLDqdEVRRRVSVC 414

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054819401  97 FQSYALFpHLTVAENVAFGlrrRREADvEARVAEGLALVELGHLADRRP-----------ALLSGGQQQRVALARALVNR 165
Cdd:TIGR02868 415 AQDAHLF-DTTVRENLRLA---RPDAT-DEELWAALERVGLADWLRALPdgldtvlgeggARLSGGERQRLALARALLAD 489

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 1054819401 166 PALLLLDEPLGALDLKLRRQMQLELkrIQTEVGLTFVHVTHD 207
Cdd:TIGR02868 490 APILLLDEPTEHLDAETADELLEDL--LAALSGRTVVLITHH 529
araG PRK11288
L-arabinose ABC transporter ATP-binding protein AraG;
20-302 3.61e-22

L-arabinose ABC transporter ATP-binding protein AraG;


Pssm-ID: 183077 [Multi-domain]  Cd Length: 501  Bit Score: 98.06  E-value: 3.61e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054819401  20 LELAAVTKRFGAFVAVDDLTLTVPSGSFFALLGPSGCGKTTTLRMVAGLEQPTDGTISIDGRDV--TGTR-AHRRPVNTV 96
Cdd:PRK11288    5 LSFDGIGKTFPGVKALDDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSILIDGQEMrfASTTaALAAGVAII 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054819401  97 FQSYALFPHLTVAENV-------AFGLRRRREADVEARvaegLALVELGHLADRRPAL--LSGGQQQRVALARALVNRPA 167
Cdd:PRK11288   85 YQELHLVPEMTVAENLylgqlphKGGIVNRRLLNYEAR----EQLEHLGVDIDPDTPLkyLSIGQRQMVEIAKALARNAR 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054819401 168 LLLLDEPLGALDLKLRRQmqleLKRIQTEV---GLTFVHVTHDQEEAMTMADTVAVMNRGRIEQMGPpaDLYEHPRTTFV 244
Cdd:PRK11288  161 VIAFDEPTSSLSAREIEQ----LFRVIRELraeGRVILYVSHRMEEIFALCDAITVFKDGRYVATFD--DMAQVDRDQLV 234

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1054819401 245 ANFLGRS-----NLVP---GTVVERLDGdllgvdVGGARVRVPASRAVRdTGDV-----LVGA-RPEKVRLL 302
Cdd:PRK11288  235 QAMVGREigdiyGYRPrplGEVRLRLDG------LKGPGLREPISFSVR-AGEIvglfgLVGAgRSELMKLL 299
PhnL COG4778
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ...
 20-225 3.94e-22

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: 93.65  E-value: 3.94e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054819401  20 LELAAVTKRF------GA-FVAVDDLTLTVPSGSFFALLGPSGCGKTTTLRMVAGLEQPTDGTISI--DGRDVTGTRA-- 88
Cdd:COG4778     5 LEVENLSKTFtlhlqgGKrLPVLDGVSFSVAAGECVALTGPSGAGKSTLLKCIYGNYLPDSGSILVrhDGGWVDLAQAsp 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054819401  89 ------HRRPVNTVFQSYALFPHLTVAENVAFGLRRRREADVEARVAEGLALVELG---HLADRRPALLSGGQQQRVALA 159
Cdd:COG4778    85 reilalRRRTIGYVSQFLRVIPRVSALDVVAEPLLERGVDREEARARARELLARLNlpeRLWDLPPATFSGGEQQRVNIA 164

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054819401 160 RALVNRPALLLLDEPLGALDLKLR---RQMQLELKRiqteVGLTFVHVTHDqEEAM-TMADTVAVMNRGR 225
Cdd:COG4778   165 RGFIADPPLLLLDEPTASLDAANRavvVELIEEAKA----RGTAIIGIFHD-EEVReAVADRVVDVTPFS 229
ABCC_cytochrome_bd cd03247
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ...
 33-230 4.01e-22

ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome bd biogenesis. The CydC and CydD proteins are important for the formation of cytochrome bd terminal oxidase of E. coli and it has been proposed that they were necessary for biosynthesis of the cytochrome bd quinol oxidase and for periplasmic c-type cytochromes. CydCD were proposed to determine a heterooligomeric complex important for heme export into the periplasm or to be involved in the maintenance of the proper redox state of the periplasmic space. In Bacillus subtilis, the absence of CydCD does not affect the presence of halo-cytochrome c in the membrane and this observation suggests that CydCD proteins are not involved in the export of heme in this organism.


Pssm-ID: 213214 [Multi-domain]  Cd Length: 178  Bit Score: 92.38  E-value: 4.01e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054819401  33 VAVDDLTLTVPSGSFFALLGPSGCGKTTTLRMVAGLEQPTDGTISIDGRDVTGTRAHRRPVNTVFQSYalfPHL---TVA 109
Cdd:cd03247    16 QVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDGVPVSDLEKALSSLISVLNQR---PYLfdtTLR 92

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054819401 110 ENVafGLRrrreadvearvaeglalvelghladrrpalLSGGQQQRVALARALVNRPALLLLDEPLGALDLKLRRQMqLE 189
Cdd:cd03247    93 NNL--GRR------------------------------FSGGERQRLALARILLQDAPIVLLDEPTVGLDPITERQL-LS 139

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 1054819401 190 LKRIQTEvGLTFVHVTHdQEEAMTMADTVAVMNRGRIEQMG 230
Cdd:cd03247   140 LIFEVLK-DKTLIWITH-HLTGIEHMDKILFLENGKIIMQG 178
PRK13651 PRK13651
cobalt transporter ATP-binding subunit; Provisional
 31-255 8.10e-22

cobalt transporter ATP-binding subunit; Provisional


Pssm-ID: 184210 [Multi-domain]  Cd Length: 305  Bit Score: 94.77  E-value: 8.10e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054819401  31 AFVAVDDLTLTVPSGSFFALLGPSGCGKTTTLRMVAGLEQPTDGTISIDGRD--------------------------VT 84
Cdd:PRK13651   19 ELKALDNVSVEINQGEFIAIIGQTGSGKTTFIEHLNALLLPDTGTIEWIFKDeknkkktkekekvleklviqktrfkkIK 98

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054819401  85 GTRAHRRPVNTVFQ--SYALFPHlTVAENVAFGLR----RRREAdvEARVAEGLALVELG-HLADRRPALLSGGQQQRVA 157
Cdd:PRK13651   99 KIKEIRRRVGVVFQfaEYQLFEQ-TIEKDIIFGPVsmgvSKEEA--KKRAAKYIELVGLDeSYLQRSPFELSGGQKRRVA 175

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054819401 158 LARALVNRPALLLLDEPLGALDLKLRRQMQLELKRIQTEvGLTFVHVTHDQEEAMTMADTVAVMNRGRIEQMGppaDLYE 237
Cdd:PRK13651  176 LAGILAMEPDFLVFDEPTAGLDPQGVKEILEIFDNLNKQ-GKTIILVTHDLDNVLEWTKRTIFFKDGKIIKDG---DTYD 251

                         250
                  ....*....|....*...
gi 1054819401 238 HPRTTfvaNFLGRSNLVP 255
Cdd:PRK13651  252 ILSDN---KFLIENNMEP 266
met_CoM_red_A2 TIGR03269
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ...
 20-232 1.79e-21

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: 96.02  E-value: 1.79e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054819401  20 LELAAVTKRFGAFVAVDDLTLTVPSGSFFALLGPSGCGKTTTLRMVAGLEQ--PTDGTI----------------SIDGR 81
Cdd:TIGR03269   1 IEVKNLTKKFDGKEVLKNISFTIEEGEVLGILGRSGAGKSVLMHVLRGMDQyePTSGRIiyhvalcekcgyverpSKVGE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054819401  82 -------------------DVTGTRAHRRPVNTVFQ-SYALFPHLTVAENVafgLRRRREADVEARVAEGLA--LVELGH 139
Cdd:TIGR03269  81 pcpvcggtlepeevdfwnlSDKLRRRIRKRIAIMLQrTFALYGDDTVLDNV---LEALEEIGYEGKEAVGRAvdLIEMVQ 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054819401 140 LADRRPAL---LSGGQQQRVALARALVNRPALLLLDEPLGALDLKLRRQMQLELKRIQTEVGLTFVHVTHDQEEAMTMAD 216
Cdd:TIGR03269 158 LSHRITHIardLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALEEAVKASGISMVLTSHWPEVIEDLSD 237

                         250
                  ....*....|....*.
gi 1054819401 217 TVAVMNRGRIEQMGPP 232
Cdd:TIGR03269 238 KAIWLENGEIKEEGTP 253
ABCG_EPDR cd03213
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ...
 35-226 1.83e-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: 91.07  E-value: 1.83e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054819401  35 VDDLTLTVPSGSFFALLGPSGCGKTTTLRMVAGL--EQPTDGTISIDGRDVTgTRAHRRPVNTVFQSYALFPHLTVAENV 112
Cdd:cd03213    25 LKNVSGKAKPGELTAIMGPSGAGKSTLLNALAGRrtGLGVSGEVLINGRPLD-KRSFRKIIGYVPQDDILHPTLTVRETL 103

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054819401 113 AFGLRRRReadvearvaeglalvelghladrrpalLSGGQQQRVALARALVNRPALLLLDEPLGALDLKLRRQMQLELKR 192
Cdd:cd03213   104 MFAAKLRG---------------------------LSGGERKRVSIALELVSNPSLLFLDEPTSGLDSSSALQVMSLLRR 156

                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 1054819401 193 I-QTevGLTFVHVTHD-QEEAMTMADTVAVMNRGRI 226
Cdd:cd03213   157 LaDT--GRTIICSIHQpSSEIFELFDKLLLLSQGRV 190
phnK PRK11701
phosphonate C-P lyase system protein PhnK; Provisional
 20-230 2.41e-21

phosphonate C-P lyase system protein PhnK; Provisional


Pssm-ID: 183280 [Multi-domain]  Cd Length: 258  Bit Score: 92.30  E-value: 2.41e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054819401  20 LELAAVTKRFGAFVAVDDLTLTVPSGSFFALLGPSGCGKTTTLRMVAGLEQPTDGTISIDGRD------VTGTRAHRRpv 93
Cdd:PRK11701    7 LSVRGLTKLYGPRKGCRDVSFDLYPGEVLGIVGESGSGKTTLLNALSARLAPDAGEVHYRMRDgqlrdlYALSEAERR-- 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054819401  94 nTVFQSYALFPHltvaENVAFGLRR-----------------RREADVEARVAEGLALVELGhlADR---RPALLSGGQQ 153
Cdd:PRK11701   85 -RLLRTEWGFVH----QHPRDGLRMqvsaggnigerlmavgaRHYGDIRATAGDWLERVEID--AARiddLPTTFSGGMQ 157

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1054819401 154 QRVALARALVNRPALLLLDEPLGALDLKLRRQMQLELKRIQTEVGLTFVHVTHDQEEAMTMADTVAVMNRGRIEQMG 230
Cdd:PRK11701  158 QRLQIARNLVTHPRLVFMDEPTGGLDVSVQARLLDLLRGLVRELGLAVVIVTHDLAVARLLAHRLLVMKQGRVVESG 234
PRK11174 PRK11174
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
 33-235 3.04e-21

cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed


Pssm-ID: 236870 [Multi-domain]  Cd Length: 588  Bit Score: 95.30  E-value: 3.04e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054819401  33 VAVDDLTLTVPSGSFFALLGPSGCGKTTTLRMVAGLeQPTDGTISIDG---RDVTGTrAHRRPVNTVFQSYALFpHLTVA 109
Cdd:PRK11174  364 TLAGPLNFTLPAGQRIALVGPSGAGKTSLLNALLGF-LPYQGSLKINGielRELDPE-SWRKHLSWVGQNPQLP-HGTLR 440

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054819401 110 ENVAFGLRRRREADVE-----ARVAEGLALVELG--HLADRRPALLSGGQQQRVALARALVNRPALLLLDEPLGALDLKL 182
Cdd:PRK11174  441 DNVLLGNPDASDEQLQqalenAWVSEFLPLLPQGldTPIGDQAAGLSVGQAQRLALARALLQPCQLLLLDEPTASLDAHS 520

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1054819401 183 RRQMQLELKRIQTevGLTFVHVTHdQEEAMTMADTVAVMNRGRIEQMGPPADL 235
Cdd:PRK11174  521 EQLVMQALNAASR--RQTTLMVTH-QLEDLAQWDQIWVMQDGQIVQQGDYAEL 570
CP_lyasePhnK TIGR02323
phosphonate C-P lyase system protein PhnK; Members of this family are the PhnK protein of C-P ...
 20-230 4.88e-21

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: 91.43  E-value: 4.88e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054819401  20 LELAAVTKRFGAFVAVDDLTLTVPSGSFFALLGPSGCGKTTTLRMVAGLEQPTDGTISIDGRD------VTGTRAHRRPV 93
Cdd:TIGR02323   4 LQVSGLSKSYGGGKGCRDVSFDLYPGEVLGIVGESGSGKSTLLGCLAGRLAPDHGTATYIMRSgaelelYQLSEAERRRL 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054819401  94 NTVFQSYalfphltVAENVAFGLRRRREADveARVAEGLALVELGHLADRR--------------------PALLSGGQQ 153
Cdd:TIGR02323  84 MRTEWGF-------VHQNPRDGLRMRVSAG--ANIGERLMAIGARHYGNIRataqdwleeveidptriddlPRAFSGGMQ 154

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1054819401 154 QRVALARALVNRPALLLLDEPLGALDLKLRRQMQLELKRIQTEVGLTFVHVTHDQEEAMTMADTVAVMNRGRIEQMG 230
Cdd:TIGR02323 155 QRLQIARNLVTRPRLVFMDEPTGGLDVSVQARLLDLLRGLVRDLGLAVIIVTHDLGVARLLAQRLLVMQQGRVVESG 231
nikD PRK10418
nickel transporter ATP-binding protein NikD; Provisional
 35-240 2.24e-20

nickel transporter ATP-binding protein NikD; Provisional


Pssm-ID: 236688 [Multi-domain]  Cd Length: 254  Bit Score: 89.37  E-value: 2.24e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054819401  35 VDDLTLTVPSGSFFALLGPSGCGKTTTLRMVAGLEQP----TDGTISIDGRDVTGTRAHRRPVNTVFQS--YALFPHLTV 108
Cdd:PRK10418   19 VHGVSLTLQRGRVLALVGGSGSGKSLTCAAALGILPAgvrqTAGRVLLDGKPVAPCALRGRKIATIMQNprSAFNPLHTM 98

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054819401 109 AENVAFGLRRRREADVEARVAEGLALVELGH---LADRRPALLSGGQQQRVALARALVNRPALLLLDEPLGALDLKLRRQ 185
Cdd:PRK10418   99 HTHARETCLALGKPADDATLTAALEAVGLENaarVLKLYPFEMSGGMLQRMMIALALLCEAPFIIADEPTTDLDVVAQAR 178

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1054819401 186 MQLELKRIQTEVGLTFVHVTHDQEEAMTMADTVAVMNRGRIEQMGPPADLYEHPR 240
Cdd:PRK10418  179 ILDLLESIVQKRALGMLLVTHDMGVVARLADDVAVMSHGRIVEQGDVETLFNAPK 233
ABCF_EF-3 cd03221
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ...
 20-209 2.26e-20

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: 86.35  E-value: 2.26e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054819401  20 LELAAVTKRFGAFVAVDDLTLTVPSGSFFALLGPSGCGKTTTLRMVAGLEQPTDGTISIDGRdvtgtrahrrpvntvfqs 99
Cdd:cd03221     1 IELENLSKTYGGKLLLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIVTWGST------------------ 62

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054819401 100 yalfphltvaenvafglrrrreadvearvaeglalVELGHLAdrrpaLLSGGQQQRVALARALVNRPALLLLDEPLGALD 179
Cdd:cd03221    63 -----------------------------------VKIGYFE-----QLSGGEKMRLALAKLLLENPNLLLLDEPTNHLD 102

                         170       180       190
                  ....*....|....*....|....*....|
gi 1054819401 180 LKLRRQMQLELKRIQTevglTFVHVTHDQE 209
Cdd:cd03221   103 LESIEALEEALKEYPG----TVILVSHDRY 128
PRK11176 PRK11176
lipid A ABC transporter ATP-binding protein/permease MsbA;
34-238 5.95e-20

lipid A ABC transporter ATP-binding protein/permease MsbA;


Pssm-ID: 183016 [Multi-domain]  Cd Length: 582  Bit Score: 91.62  E-value: 5.95e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054819401  34 AVDDLTLTVPSGSFFALLGPSGCGKTTTLRMVAGLEQPTDGTISIDGRDVTGTR--AHRRPVNTVFQSYALFpHLTVAEN 111
Cdd:PRK11176  358 ALRNINFKIPAGKTVALVGRSGSGKSTIANLLTRFYDIDEGEILLDGHDLRDYTlaSLRNQVALVSQNVHLF-NDTIANN 436

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054819401 112 VAFGLRRR--REaDVE--ARVAEGLALVE-----LGHLADRRPALLSGGQQQRVALARALVNRPALLLLDEPLGALDLKL 182
Cdd:PRK11176  437 IAYARTEQysRE-QIEeaARMAYAMDFINkmdngLDTVIGENGVLLSGGQRQRIAIARALLRDSPILILDEATSALDTES 515

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1054819401 183 RRQMQLELKRIQTE-VGLTFVHVTHDQEEamtmADTVAVMNRGRIEQMGPPADLYEH 238
Cdd:PRK11176  516 ERAIQAALDELQKNrTSLVIAHRLSTIEK----ADEILVVEDGEIVERGTHAELLAQ 568
ATM1 COG5265
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ...
 36-228 7.03e-20

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: 91.42  E-value: 7.03e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054819401  36 DDLTLTVPSGSFFALLGPSGCGKTTTLRMVAGLEQPTDGTISIDGRDVTGTRAH--RRPVNTVFQSYALFpHLTVAENVA 113
Cdd:COG5265   375 KGVSFEVPAGKTVAIVGPSGAGKSTLARLLFRFYDVTSGRILIDGQDIRDVTQAslRAAIGIVPQDTVLF-NDTIAYNIA 453

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054819401 114 FGlrrRREADvEARVAEGLALVELGHLADRRP----------AL-LSGGQQQRVALARALVNRPALLLLDEPLGALDLKL 182
Cdd:COG5265   454 YG---RPDAS-EEEVEAAARAAQIHDFIESLPdgydtrvgerGLkLSGGEKQRVAIARTLLKNPPILIFDEATSALDSRT 529

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1054819401 183 RRQMQLELKRI-QTEVGLTFVH----VTHdqeeamtmADTVAVMNRGRI-EQ 228
Cdd:COG5265   530 ERAIQAALREVaRGRTTLVIAHrlstIVD--------ADEILVLEAGRIvER 573
PRK13549 PRK13549
xylose transporter ATP-binding subunit; Provisional
 20-225 1.14e-19

xylose transporter ATP-binding subunit; Provisional


Pssm-ID: 184134 [Multi-domain]  Cd Length: 506  Bit Score: 90.37  E-value: 1.14e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054819401  20 LELAAVTKRFGAFVAVDDLTLTVPSGSFFALLGPSGCGKTTTLRMVAGLeQPT---DGTISIDGRDVtgtRAH------R 90
Cdd:PRK13549    6 LEMKNITKTFGGVKALDNVSLKVRAGEIVSLCGENGAGKSTLMKVLSGV-YPHgtyEGEIIFEGEEL---QASnirdteR 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054819401  91 RPVNTVFQSYALFPHLTVAENVAFGlrrrRE---------ADVEARVAEGLALVELGHLADRRPALLSGGQQQRVALARA 161
Cdd:PRK13549   82 AGIAIIHQELALVKELSVLENIFLG----NEitpggimdyDAMYLRAQKLLAQLKLDINPATPVGNLGLGQQQLVEIAKA 157

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1054819401 162 LVNRPALLLLDEPLGALDLKLRRQMqLELKRIQTEVGLTFVHVTHDQEEAMTMADTVAVMNRGR 225
Cdd:PRK13549  158 LNKQARLLILDEPTASLTESETAVL-LDIIRDLKAHGIACIYISHKLNEVKAISDTICVIRDGR 220
PRK13540 PRK13540
cytochrome c biogenesis protein CcmA; Provisional
 35-194 1.28e-19

cytochrome c biogenesis protein CcmA; Provisional


Pssm-ID: 184127 [Multi-domain]  Cd Length: 200  Bit Score: 86.16  E-value: 1.28e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054819401  35 VDDLTLTVPSGSFFALLGPSGCGKTTTLRMVAGLEQPTDGTISIDGRDVTGTR-AHRRPVNTVFQSYALFPHLTVAENVA 113
Cdd:PRK13540   17 LQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEILFERQSIKKDLcTYQKQLCFVGHRSGINPYLTLRENCL 96

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054819401 114 FGLRRRREAdveARVAEGLALVELGHLADRRPALLSGGQQQRVALARALVNRPALLLLDEPLGALDlklRRQMQLELKRI 193
Cdd:PRK13540   97 YDIHFSPGA---VGITELCRLFSLEHLIDYPCGLLSSGQKRQVALLRLWMSKAKLWLLDEPLVALD---ELSLLTIITKI 170


                  .
gi 1054819401 194 Q 194
Cdd:PRK13540  171 Q 171
xylG TIGR02633
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ...
 20-225 1.38e-19

D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose isomerase and xylulokinase enzymes for xylose utilization. Members of this protein family are the ATP-binding cassette (ABC) subunit of the known or predicted high-affinity xylose ABC transporter for xylose import. These genes, which closely resemble other sugar transport ABC transporter genes, typically are encoded near xylose utilization enzymes and regulatory proteins. Note that this form of the transporter contains two copies of the ABC transporter domain (pfam00005). [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]


Pssm-ID: 131681 [Multi-domain]  Cd Length: 500  Bit Score: 90.27  E-value: 1.38e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054819401  20 LELAAVTKRFGAFVAVDDLTLTVPSGSFFALLGPSGCGKTTTLRMVAGL--EQPTDGTISIDGRDVTGTR---AHRRPVN 94
Cdd:TIGR02633   2 LEMKGIVKTFGGVKALDGIDLEVRPGECVGLCGENGAGKSTLMKILSGVypHGTWDGEIYWSGSPLKASNirdTERAGIV 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054819401  95 TVFQSYALFPHLTVAENVAFG----LRRRREADVEA--RVAEGLALVELGHLADRRPAL-LSGGQQQRVALARALVNRPA 167
Cdd:TIGR02633  82 IIHQELTLVPELSVAENIFLGneitLPGGRMAYNAMylRAKNLLRELQLDADNVTRPVGdYGGGQQQLVEIAKALNKQAR 161

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1054819401 168 LLLLDEPLGALDLKlRRQMQLELKRIQTEVGLTFVHVTHDQEEAMTMADTVAVMNRGR 225
Cdd:TIGR02633 162 LLILDEPSSSLTEK-ETEILLDIIRDLKAHGVACVYISHKLNEVKAVCDTICVIRDGQ 218
bacteriocin_ABC TIGR01193
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ...
 34-235 1.43e-19

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: 90.57  E-value: 1.43e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054819401  34 AVDDLTLTVPSGSFFALLGPSGCGKTTTLRMVAGLEQPTDGTISIDGRDVTGTRAH--RRPVNTVFQSYALFPHlTVAEN 111
Cdd:TIGR01193 489 ILSDISLTIKMNSKTTIVGMSGSGKSTLAKLLVGFFQARSGEILLNGFSLKDIDRHtlRQFINYLPQEPYIFSG-SILEN 567

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054819401 112 VAFGLRRRREADveaRVAEGLALVELGHLADRRP-----------ALLSGGQQQRVALARALVNRPALLLLDEPLGALDL 180
Cdd:TIGR01193 568 LLLGAKENVSQD---EIWAACEIAEIKDDIENMPlgyqtelseegSSISGGQKQRIALARALLTDSKVLILDESTSNLDT 644

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1054819401 181 KLRRQMQLELKRIQTEvglTFVHVTHDQEEAmTMADTVAVMNRGRIEQMGPPADL 235
Cdd:TIGR01193 645 ITEKKIVNNLLNLQDK---TIIFVAHRLSVA-KQSDKIIVLDHGKIIEQGSHDEL 695
Uup COG0488
ATPase components of ABC transporters with duplicated ATPase domains [General function ...
 20-227 1.81e-19

ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];


Pssm-ID: 440254 [Multi-domain]  Cd Length: 520  Bit Score: 89.74  E-value: 1.81e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054819401  20 LELAAVTKRFGAFVAVDDLTLTVPSGSFFALLGPSGCGKTTTLRMVAGLEQPTDGTISIdgrdvtGTrahrrpvnTVFQS 99
Cdd:COG0488   316 LELEGLSKSYGDKTLLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPDSGTVKL------GE--------TVKIG 381

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054819401 100 Y------ALFPHLTVAENVAFGLRRRREADVEARvaeglalveLGHL------ADRRPALLSGGQQQRVALARALVNRPA 167
Cdd:COG0488   382 YfdqhqeELDPDKTVLDELRDGAPGGTEQEVRGY---------LGRFlfsgddAFKPVGVLSGGEKARLALAKLLLSPPN 452

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1054819401 168 LLLLDEPLGALDLKLRRQMqlelkriqtEVGL-----TFVHVTHDQEEAMTMADTVAVMNRGRIE 227
Cdd:COG0488   453 VLLLDEPTNHLDIETLEAL---------EEALddfpgTVLLVSHDRYFLDRVATRILEFEDGGVR 508
PRK09700 PRK09700
D-allose ABC transporter ATP-binding protein AlsA;
20-224 2.16e-19

D-allose ABC transporter ATP-binding protein AlsA;


Pssm-ID: 182036 [Multi-domain]  Cd Length: 510  Bit Score: 89.84  E-value: 2.16e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054819401  20 LELAAVTKRFGAFVAVDDLTLTVPSGSFFALLGPSGCGKTTTLRMVAGLEQPTDGTISIDGRD---VTGTRAHRRPVNTV 96
Cdd:PRK09700    6 ISMAGIGKSFGPVHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNINynkLDHKLAAQLGIGII 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054819401  97 FQSYALFPHLTVAENVAFGLRRRRE---------ADVEARVAEGLALVELGHLADRRPALLSGGQQQRVALARALVNRPA 167
Cdd:PRK09700   86 YQELSVIDELTVLENLYIGRHLTKKvcgvniidwREMRVRAAMMLLRVGLKVDLDEKVANLSISHKQMLEIAKTLMLDAK 165

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1054819401 168 LLLLDEPLGALDLKLRRQMQLELKRIQTEvGLTFVHVTHDQEEAMTMADTVAVMNRG 224
Cdd:PRK09700  166 VIIMDEPTSSLTNKEVDYLFLIMNQLRKE-GTAIVYISHKLAEIRRICDRYTVMKDG 221
MglA COG1129
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
34-226 3.33e-19

ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];


Pssm-ID: 440745 [Multi-domain]  Cd Length: 497  Bit Score: 88.92  E-value: 3.33e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054819401  34 AVDDLTLTVPSGSFFALLGPSGCGKTTTLRMVAGLEQPTDGTISIDGRDVTGTRAH-------------RRpvntvfqSY 100
Cdd:COG1129   267 VVRDVSFSVRAGEILGIAGLVGAGRTELARALFGADPADSGEIRLDGKPVRIRSPRdairagiayvpedRK-------GE 339

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054819401 101 ALFPHLTVAENVAFG----------LRRRREADVEARVAEGLAlVELGHLaDRRPALLSGGQQQRVALARALVNRPALLL 170
Cdd:COG1129   340 GLVLDLSIRENITLAsldrlsrgglLDRRRERALAEEYIKRLR-IKTPSP-EQPVGNLSGGNQQKVVLAKWLATDPKVLI 417

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1054819401 171 LDEP-----LGA----LDL--KLRRQmqlelkriqtevGLTFVHVTHDQEEAMTMADTVAVMNRGRI 226
Cdd:COG1129   418 LDEPtrgidVGAkaeiYRLirELAAE------------GKAVIVISSELPELLGLSDRILVMREGRI 472
ABCC_MRP_domain1 cd03250
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ...
 37-225 5.95e-19

ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This subfamily is also known as MRP (multidrug resistance-associated protein). Some of the MRP members have five additional transmembrane segments in their N-terminus, but the function of these additional membrane-spanning domains is not clear. The MRP was found in the multidrug-resisting lung cancer cell in which p-glycoprotein was not overexpressed. MRP exports glutathione by drug stimulation, as well as, certain substrates in conjugated forms with anions, such as glutathione, glucuronate, and sulfate.


Pssm-ID: 213217 [Multi-domain]  Cd Length: 204  Bit Score: 84.06  E-value: 5.95e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054819401  37 DLTLTVPSGSFFALLGPSGCGKTTTLRMVAGLEQPTDGTISIDGRDvtgtrahrrpvntvfqSY-ALFPHL---TVAENV 112
Cdd:cd03250    23 DINLEVPKGELVAIVGPVGSGKSSLLSALLGELEKLSGSVSVPGSI----------------AYvSQEPWIqngTIRENI 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054819401 113 AFGLR---RRREADVEA--------RVAEGLaLVELGhladRRPALLSGGQQQRVALARALVNRPALLLLDEPLGALDLK 181
Cdd:cd03250    87 LFGKPfdeERYEKVIKAcalepdleILPDGD-LTEIG----EKGINLSGGQKQRISLARAVYSDADIYLLDDPLSAVDAH 161

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1054819401 182 LRRQM-------QLELKRiqtevglTFVHVTHdQEEAMTMADTVAVMNRGR 225
Cdd:cd03250   162 VGRHIfencilgLLLNNK-------TRILVTH-QLQLLPHADQIVVLDNGR 204
PRK15134 PRK15134
microcin C ABC transporter ATP-binding protein YejF; Provisional
 35-228 7.24e-19

microcin C ABC transporter ATP-binding protein YejF; Provisional


Pssm-ID: 237917 [Multi-domain]  Cd Length: 529  Bit Score: 88.22  E-value: 7.24e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054819401  35 VDDLTLTVPSGSFFALLGPSGCGKT-TTLRMVAGLEQP----TDGTISIDGRDV--------TGTRAHRrpVNTVFQS-- 99
Cdd:PRK15134   25 VNDVSLQIEAGETLALVGESGSGKSvTALSILRLLPSPpvvyPSGDIRFHGESLlhaseqtlRGVRGNK--IAMIFQEpm 102

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054819401 100 YALFPHLTVAENVA--FGLRR--RREAdVEARVAEGLALVELGHLADRR---PALLSGGQQQRVALARALVNRPALLLLD 172
Cdd:PRK15134  103 VSLNPLHTLEKQLYevLSLHRgmRREA-ARGEILNCLDRVGIRQAAKRLtdyPHQLSGGERQRVMIAMALLTRPELLIAD 181

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1054819401 173 EPLGALDLKLRRQMQLELKRIQTEVGLTFVHVTHDQEEAMTMADTVAVMNRGR-IEQ 228
Cdd:PRK15134  182 EPTTALDVSVQAQILQLLRELQQELNMGLLFITHNLSIVRKLADRVAVMQNGRcVEQ 238
ABC_CcmA_heme_exporter cd03231
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ...
 38-179 1.18e-18

Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the bacterial CcmAB transporter. The CCM family is involved in bacterial cytochrome c biogenesis. Cytochrome c maturation in E. coli requires the ccm operon, which encodes eight membrane proteins (CcmABCDEFGH). CcmE is a periplasmic heme chaperon that binds heme covalently and transfers it onto apocytochrome c in the presence of CcmF, CcmG, and CcmH. The CcmAB proteins represent an ABC transporter and the CcmCD proteins participate in heme transfer to CcmE.


Pssm-ID: 213198 [Multi-domain]  Cd Length: 201  Bit Score: 83.31  E-value: 1.18e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054819401  38 LTLTVPSGSFFALLGPSGCGKTTTLRMVAGLEQPTDGTISIDGRDVTGTR-AHRRPVNTVFQSYALFPHLTVAENVAFGL 116
Cdd:cd03231    19 LSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNGGPLDFQRdSIARGLLYLGHAPGIKTTLSVLENLRFWH 98

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1054819401 117 RRRREADVEarvaEGLALVELGHLADRRPALLSGGQQQRVALARALVNRPALLLLDEPLGALD 179
Cdd:cd03231    99 ADHSDEQVE----EALARVGLNGFEDRPVAQLSAGQQRRVALARLLLSGRPLWILDEPTTALD 157
PRK10261 PRK10261
glutathione transporter ATP-binding protein; Provisional
 34-241 2.91e-18

glutathione transporter ATP-binding protein; Provisional


Pssm-ID: 182342 [Multi-domain]  Cd Length: 623  Bit Score: 86.45  E-value: 2.91e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054819401  34 AVDDLTLTVPSGSFFALLGPSGCGKTTTLRMVAGLEQPTDGTISIDG-------RDV----TGTRAHRRPVN-----TVF 97
Cdd:PRK10261   31 AVRNLSFSLQRGETLAIVGESGSGKSVTALALMRLLEQAGGLVQCDKmllrrrsRQVielsEQSAAQMRHVRgadmaMIF 110

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054819401  98 QS--YALFPHLTVAENVAFGLR-----RRREADVEA-RVAEGLALVELGHLADRRPALLSGGQQQRVALARALVNRPALL 169
Cdd:PRK10261  111 QEpmTSLNPVFTVGEQIAESIRlhqgaSREEAMVEAkRMLDQVRIPEAQTILSRYPHQLSGGMRQRVMIAMALSCRPAVL 190

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1054819401 170 LLDEPLGALDLKLRRQMQLELKRIQTEVGLTFVHVTHDQEEAMTMADTVAVMNRGRIEQMGPPADLY---EHPRT 241
Cdd:PRK10261  191 IADEPTTALDVTIQAQILQLIKVLQKEMSMGVIFITHDMGVVAEIADRVLVMYQGEAVETGSVEQIFhapQHPYT 265
PRK15056 PRK15056
manganese/iron ABC transporter ATP-binding protein;
25-251 4.55e-18

manganese/iron ABC transporter ATP-binding protein;


Pssm-ID: 185016 [Multi-domain]  Cd Length: 272  Bit Score: 83.39  E-value: 4.55e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054819401  25 VTKRFGaFVAVDDLTLTVPSGSFFALLGPSGCGKTTTLRMVAGLEQPTDGTISIDGRDVTgtRAHRRP-VNTVFQSYAL- 102
Cdd:PRK15056   14 VTWRNG-HTALRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKISILGQPTR--QALQKNlVAYVPQSEEVd 90

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054819401 103 --FPHLTvaENVAF-------GLRRRREADVEARVAEGLALVELGHLADRRPALLSGGQQQRVALARALVNRPALLLLDE 173
Cdd:PRK15056   91 wsFPVLV--EDVVMmgryghmGWLRRAKKRDRQIVTAALARVDMVEFRHRQIGELSGGQKKRVFLARAIAQQGQVILLDE 168

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1054819401 174 PLGALDLKLRRQMQLELKRIQTEvGLTFVHVTHDQEEAMTMADtVAVMNRGRIEQMGPpadlyehPRTTFVANFLGRS 251
Cdd:PRK15056  169 PFTGVDVKTEARIISLLRELRDE-GKTMLVSTHNLGSVTEFCD-YTVMVKGTVLASGP-------TETTFTAENLELA 237
oppD PRK09473
oligopeptide transporter ATP-binding component; Provisional
 30-265 8.33e-18

oligopeptide transporter ATP-binding component; Provisional


Pssm-ID: 181888 [Multi-domain]  Cd Length: 330  Bit Score: 83.62  E-value: 8.33e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054819401  30 GAFVAVDDLTLTVPSGSFFALLGPSGCGKTTTLRMVAGLEQP---TDGTISIDGRDVTGTRAHR------RPVNTVFQS- 99
Cdd:PRK09473   27 GDVTAVNDLNFSLRAGETLGIVGESGSGKSQTAFALMGLLAAngrIGGSATFNGREILNLPEKElnklraEQISMIFQDp 106

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054819401 100 -YALFPHLTVAENVAFGLR-----RRREADVEA-RVAEGLALVElghlADRR----PALLSGGQQQRVALARALVNRPAL 168
Cdd:PRK09473  107 mTSLNPYMRVGEQLMEVLMlhkgmSKAEAFEESvRMLDAVKMPE----ARKRmkmyPHEFSGGMRQRVMIAMALLCRPKL 182

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054819401 169 LLLDEPLGALDLKLRRQ-MQL--ELKRiqtEVGLTFVHVTHDQEEAMTMADTVAVMNRGRIEQMGPPADLYEHPRTTFVA 245
Cdd:PRK09473  183 LIADEPTTALDVTVQAQiMTLlnELKR---EFNTAIIMITHDLGVVAGICDKVLVMYAGRTMEYGNARDVFYQPSHPYSI 259

                         250       260
                  ....*....|....*....|
gi 1054819401 246 NFLgrsNLVPgtvveRLDGD 265
Cdd:PRK09473  260 GLL---NAVP-----RLDAE 271
rim_protein TIGR01257
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ...
 34-230 9.69e-18

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: 85.45  E-value: 9.69e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054819401   34 AVDDLTLTVPSGSFFALLGPSGCGKTTTLRMVAGLEQPTDGTISIDGRDVTGTrahrrpVNTVFQSYALFPHLTVAENVA 113
Cdd:TIGR01257 1954 AVDRLCVGVRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAGKSILTN------ISDVHQNMGYCPQFDAIDDLL 2027

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054819401  114 FG---------LRRRREADVEARVAEGLALVELGHLADRRPALLSGGQQQRVALARALVNRPALLLLDEPLGALDLKLRR 184
Cdd:TIGR01257 2028 TGrehlylyarLRGVPAEEIEKVANWSIQSLGLSLYADRLAGTYSGGNKRKLSTAIALIGCPPLVLLDEPTTGMDPQARR 2107

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*.
gi 1054819401  185 QMQLELKRIQTEvGLTFVHVTHDQEEAMTMADTVAVMNRGRIEQMG 230
Cdd:TIGR01257 2108 MLWNTIVSIIRE-GRAVVLTSHSMEECEALCTRLAIMVKGAFQCLG 2152
ABCD_peroxisomal_ALDP cd03223
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ...
 35-206 1.18e-17

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: 79.51  E-value: 1.18e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054819401  35 VDDLTLTVPSGSFFALLGPSGCGKTTTLRMVAGLEQPTDGTISIDGRDvtgtrahrrpvNTVF---QSYalFPHLTVAEN 111
Cdd:cd03223    17 LKDLSFEIKPGDRLLITGPSGTGKSSLFRALAGLWPWGSGRIGMPEGE-----------DLLFlpqRPY--LPLGTLREQ 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054819401 112 VAFGLRRRreadvearvaeglalvelghladrrpalLSGGQQQRVALARALVNRPALLLLDEPLGALDLklrrQMQLELK 191
Cdd:cd03223    84 LIYPWDDV----------------------------LSGGEQQRLAFARLLLHKPKFVFLDEATSALDE----ESEDRLY 131

                         170
                  ....*....|....*
gi 1054819401 192 RIQTEVGLTFVHVTH 206
Cdd:cd03223   132 QLLKELGITVISVGH 146
PRK10790 PRK10790
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
37-230 1.39e-17

SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;


Pssm-ID: 182733 [Multi-domain]  Cd Length: 592  Bit Score: 84.38  E-value: 1.39e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054819401  37 DLTLTVPSGSFFALLGPSGCGKTTTLRMVAGLEQPTDGTISIDGRDVTGT--RAHRRPVNTVFQSYALFPHlTVAENVAF 114
Cdd:PRK10790  359 NINLSVPSRGFVALVGHTGSGKSTLASLLMGYYPLTEGEIRLDGRPLSSLshSVLRQGVAMVQQDPVVLAD-TFLANVTL 437

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054819401 115 GlrrrREADvEARVAEGLALVELGHLADRRPA-----------LLSGGQQQRVALARALVNRPALLLLDEPLGALDLKLR 183
Cdd:PRK10790  438 G----RDIS-EEQVWQALETVQLAELARSLPDglytplgeqgnNLSVGQKQLLALARVLVQTPQILILDEATANIDSGTE 512

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 1054819401 184 RQMQ--LELKRIQTevglTFVHVTHdQEEAMTMADTVAVMNRGRIEQMG 230
Cdd:PRK10790  513 QAIQqaLAAVREHT----TLVVIAH-RLSTIVEADTILVLHRGQAVEQG 556
NupO COG3845
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ...
 33-226 1.45e-17

ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];


Pssm-ID: 443055 [Multi-domain]  Cd Length: 504  Bit Score: 83.92  E-value: 1.45e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054819401  33 VAVDDLTLTVPSGSFFALLGPSGCGKTTTLRMVAGLEQPTDGTISIDGRDVTGTRAHRRPVNTVF------QSYALFPHL 106
Cdd:COG3845   272 PALKDVSLEVRAGEILGIAGVAGNGQSELAEALAGLRPPASGSIRLDGEDITGLSPRERRRLGVAyipedrLGRGLVPDM 351

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054819401 107 TVAENVAFGLRRRREA------DVEARVAEGLALVE----LGHLADRRPALLSGGQQQRVALARALVNRPALLLLDEPLG 176
Cdd:COG3845   352 SVAENLILGRYRRPPFsrggflDRKAIRAFAEELIEefdvRTPGPDTPARSLSGGNQQKVILARELSRDPKLLIAAQPTR 431

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1054819401 177 ALDLK----LRRQMqLELKriqtEVGLTFVHVTHDQEEAMTMADTVAVMNRGRI 226
Cdd:COG3845   432 GLDVGaiefIHQRL-LELR----DAGAAVLLISEDLDEILALSDRIAVMYEGRI 480
PLN03211 PLN03211
ABC transporter G-25; Provisional
 45-225 4.77e-17

ABC transporter G-25; Provisional


Pssm-ID: 215634 [Multi-domain]  Cd Length: 659  Bit Score: 83.01  E-value: 4.77e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054819401  45 GSFFALLGPSGCGKTTTLRMVAGLEQPTD--GTISIDGRDVTGTRAHRrpVNTVFQSYALFPHLTVAENVAF----GLRR 118
Cdd:PLN03211   94 GEILAVLGPSGSGKSTLLNALAGRIQGNNftGTILANNRKPTKQILKR--TGFVTQDDILYPHLTVRETLVFcsllRLPK 171

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054819401 119 RREADVEARVAE------GLALVELGHLADRRPALLSGGQQQRVALARALVNRPALLLLDEPLGALDLKLRRQMQLELKR 192
Cdd:PLN03211  172 SLTKQEKILVAEsviselGLTKCENTIIGNSFIRGISGGERKRVSIAHEMLINPSLLILDEPTSGLDATAAYRLVLTLGS 251

                         170       180       190
                  ....*....|....*....|....*....|....
gi 1054819401 193 IQTEvGLTFVHVTHD-QEEAMTMADTVAVMNRGR 225
Cdd:PLN03211  252 LAQK-GKTIVTSMHQpSSRVYQMFDSVLVLSEGR 284
PRK10522 PRK10522
multidrug transporter membrane component/ATP-binding component; Provisional
 20-226 1.73e-16

multidrug transporter membrane component/ATP-binding component; Provisional


Pssm-ID: 236707 [Multi-domain]  Cd Length: 547  Bit Score: 80.79  E-value: 1.73e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054819401  20 LELAAVTKRFG--AFvAVDDLTLTVPSGSFFALLGPSGCGKTTTLRMVAGLEQPTDGTISIDGRDVTGT--RAHRRPVNT 95
Cdd:PRK10522  323 LELRNVTFAYQdnGF-SVGPINLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKPVTAEqpEDYRKLFSA 401

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054819401  96 VFQSYALFPHLTVAENvafglrrrREADVEArVAEGLALVELGH---LADRRPAL--LSGGQQQRVALARALVNRPALLL 170
Cdd:PRK10522  402 VFTDFHLFDQLLGPEG--------KPANPAL-VEKWLERLKMAHkleLEDGRISNlkLSKGQKKRLALLLALAEERDILL 472

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1054819401 171 LDEPLGALDLKLRRQMQLELKRIQTEVGLTFVHVTHDqEEAMTMADTVAVMNRGRI 226
Cdd:PRK10522  473 LDEWAADQDPHFRREFYQVLLPLLQEMGKTIFAISHD-DHYFIHADRLLEMRNGQL 527
BtuD COG4138
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ...
 20-234 2.85e-16

ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism];


Pssm-ID: 443313 [Multi-domain]  Cd Length: 248  Bit Score: 77.57  E-value: 2.85e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054819401  20 LELAAVTKRFGAFvavddlTLTVPSGSFFALLGPSGCGKTTTLRMVAGLeQPTDGTISIDGRDVTGTR----AHRR---- 91
Cdd:COG4138     3 LNDVAVAGRLGPI------SAQVNAGELIHLIGPNGAGKSTLLARMAGL-LPGQGEILLNGRPLSDWSaaelARHRayls 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054819401  92 ------PVNTVFQSYALFPHLTVaenvafglrrrREADVEARVAEGLALVELGHLADRRPALLSGGQQQRVALARAL--- 162
Cdd:COG4138    76 qqqsppFAMPVFQYLALHQPAGA-----------SSEAVEQLLAQLAEALGLEDKLSRPLTQLSGGEWQRVRLAAVLlqv 144

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054819401 163 ---VN-RPALLLLDEPLGALD-------LKLRRQMqlelkriqTEVGLTFVHVTHDQEEAMTMADTVAVMNRGRIEQMGP 231
Cdd:COG4138   145 wptINpEGQLLLLDEPMNSLDvaqqaalDRLLREL--------CQQGITVVMSSHDLNHTLRHADRVWLLKQGKLVASGE 216


                  ...
gi 1054819401 232 PAD 234
Cdd:COG4138   217 TAE 219
ABC_ABC_ChvD TIGR03719
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ...
 20-179 6.47e-16

ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of the ABC transporter ATP-binding cassette, but are found outside the common ABC transporter operon structure that features integral membrane permease proteins and substrate-binding proteins encoded next to the ATP-binding cassette (ABC domain) protein. The member protein ChvD from Agrobacterium tumefaciens was identified as both a candidate to interact with VirB8, based on yeast two-hybrid analysis, and as an apparent regulator of VirG. The general function of this protein family is unknown.


Pssm-ID: 274744 [Multi-domain]  Cd Length: 552  Bit Score: 79.21  E-value: 6.47e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054819401  20 LELAAVTKRFGAFVAVDDLTLTVPSGSFFALLGPSGCGKTTTLRMVAGLEQPTDGTISIdGRDVT-----GTRAHRRPVN 94
Cdd:TIGR03719 323 IEAENLTKAFGDKLLIDDLSFKLPPGGIVGVIGPNGAGKSTLFRMITGQEQPDSGTIEI-GETVKlayvdQSRDALDPNK 401

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054819401  95 TVFQSyalfphltvaenvafglrrrreadvearVAEGLALVELGHL---------------AD--RRPALLSGGQQQRVA 157
Cdd:TIGR03719 402 TVWEE----------------------------ISGGLDIIKLGKReipsrayvgrfnfkgSDqqKKVGQLSGGERNRVH 453

                         170       180
                  ....*....|....*....|..
gi 1054819401 158 LARALVNRPALLLLDEPLGALD 179
Cdd:TIGR03719 454 LAKTLKSGGNVLLLDEPTNDLD 475
MK0520 COG2401
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ...
 20-209 8.54e-16

ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];


Pssm-ID: 441957 [Multi-domain]  Cd Length: 222  Bit Score: 75.77  E-value: 8.54e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054819401  20 LELAAVTKRFGAFVAVDDLTLTVPSGSFFALLGPSGCGKTTTLRMVAGLEQPTDGTISIDGRDVTgtrahrrpvntvfqs 99
Cdd:COG2401    31 LEAFGVELRVVERYVLRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGALKGTPVAGCVDVPDNQ--------------- 95

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054819401 100 yaLFPHLTVAENVAfglrrrREADVEArVAEGLALVELG--HLADRRPALLSGGQQQRVALARALVNRPALLLLDEPLGA 177
Cdd:COG2401    96 --FGREASLIDAIG------RKGDFKD-AVELLNAVGLSdaVLWLRRFKELSTGQKFRFRLALLLAERPKLLVIDEFCSH 166

                         170       180       190
                  ....*....|....*....|....*....|..
gi 1054819401 178 LDLKLRRQMQLELKRIQTEVGLTFVHVTHDQE 209
Cdd:COG2401   167 LDRQTAKRVARNLQKLARRAGITLVVATHHYD 198
3a01204 TIGR00955
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ...
 44-232 1.07e-15

The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]


Pssm-ID: 273361 [Multi-domain]  Cd Length: 617  Bit Score: 78.55  E-value: 1.07e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054819401  44 SGSFFALLGPSGCGKTTTLRMVAGLEQP---TDGTISIDGRDVTGTRAHRRPVnTVFQSYALFPHLTVAENVAFGLRRRR 120
Cdd:TIGR00955  50 PGELLAVMGSSGAGKTTLMNALAFRSPKgvkGSGSVLLNGMPIDAKEMRAISA-YVQQDDLFIPTLTVREHLMFQAHLRM 128

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054819401 121 EADVE-----ARVAEGLALVELGHLADRR---PAL---LSGGQQQRVALARALVNRPALLLLDEPLGALDLKLRRQMQLE 189
Cdd:TIGR00955 129 PRRVTkkekrERVDEVLQALGLRKCANTRigvPGRvkgLSGGERKRLAFASELLTDPPLLFCDEPTSGLDSFMAYSVVQV 208

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 1054819401 190 LKRIQTEvGLTFVHVTHD-QEEAMTMADTVAVMNRGRIEQMGPP 232
Cdd:TIGR00955 209 LKGLAQK-GKTIICTIHQpSSELFELFDKIILMAEGRVAYLGSP 251
MRP_assoc_pro TIGR00957
multi drug resistance-associated protein (MRP); This model describes multi drug ...
 24-248 1.33e-15

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: 78.83  E-value: 1.33e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054819401   24 AVTKRFGAFV-------AVDDLTLTVPSGSFFALLGPSGCGKTTTLRMVAGLEQPTDGTISIDGRdvtgtrahrrpVNTV 96
Cdd:TIGR00957  636 SITVHNATFTwardlppTLNGITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVHMKGS-----------VAYV 704

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054819401   97 FQSyALFPHLTVAENVAFGLR---RRREADVEArvAEGLALVELGHLADR-----RPALLSGGQQQRVALARALVNRPAL 168
Cdd:TIGR00957  705 PQQ-AWIQNDSLRENILFGKAlneKYYQQVLEA--CALLPDLEILPSGDRteigeKGVNLSGGQKQRVSLARAVYSNADI 781

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054819401  169 LLLDEPLGALDLKLRRQMqleLKRIQTEVGL----TFVHVTHDQeEAMTMADTVAVMNRGRIEQMGPPADLYEhpRTTFV 244
Cdd:TIGR00957  782 YLFDDPLSAVDAHVGKHI---FEHVIGPEGVlknkTRILVTHGI-SYLPQVDVIIVMSGGKISEMGSYQELLQ--RDGAF 855


                   ....
gi 1054819401  245 ANFL 248
Cdd:TIGR00957  856 AEFL 859
GguA NF040905
sugar ABC transporter ATP-binding protein;
20-229 2.54e-15

sugar ABC transporter ATP-binding protein;


Pssm-ID: 468840 [Multi-domain]  Cd Length: 500  Bit Score: 77.14  E-value: 2.54e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054819401  20 LELAAVTKRFGAFVAVDDLTLTVPSGSFFALLGPSGCGKTTTLRMVAGLeQPT---DGTISIDGRDVT--GTRA-HRRPV 93
Cdd:NF040905    2 LEMRGITKTFPGVKALDDVNLSVREGEIHALCGENGAGKSTLMKVLSGV-YPHgsyEGEILFDGEVCRfkDIRDsEALGI 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054819401  94 NTVFQSYALFPHLTVAENV-------AFGLRRRREADVEARvaEGLALVELGHLADRRPALLSGGQQQRVALARALVNRP 166
Cdd:NF040905   81 VIIHQELALIPYLSIAENIflgneraKRGVIDWNETNRRAR--ELLAKVGLDESPDTLVTDIGVGKQQLVEIAKALSKDV 158

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1054819401 167 ALLLLDEPLGALD-------LKLrrqmQLELKriqtEVGLTFVHVTHDQEEAMTMADTVAVMNRGR-IEQM 229
Cdd:NF040905  159 KLLILDEPTAALNeedsaalLDL----LLELK----AQGITSIIISHKLNEIRRVADSITVLRDGRtIETL 221
ABCC_MRP_domain2 cd03244
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ...
 34-232 2.71e-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: 74.45  E-value: 2.71e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054819401  34 AVDDLTLTVPSGSFFALLGPSGCGKTTT----LRMVagleQPTDGTISIDGRDVTGTRAH--RRPVNTVFQSYALFPHlT 107
Cdd:cd03244    19 VLKNISFSIKPGEKVGIVGRTGSGKSSLllalFRLV----ELSSGSILIDGVDISKIGLHdlRSRISIIPQDPVLFSG-T 93

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054819401 108 VAENVA-FGlrrrrEADvEARVAEGLALVEL-GHLADRRPAL----------LSGGQQQRVALARALVNRPALLLLDEPL 175
Cdd:cd03244    94 IRSNLDpFG-----EYS-DEELWQALERVGLkEFVESLPGGLdtvveeggenLSVGQRQLLCLARALLRKSKILVLDEAT 167

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1054819401 176 GALDLKLRRQMQlelKRIQTEvgltFVHVThdqeeAMTMA---------DTVAVMNRGRIEQMGPP 232
Cdd:cd03244   168 ASVDPETDALIQ---KTIREA----FKDCT-----VLTIAhrldtiidsDRILVLDKGRVVEFDSP 221
PRK10789 PRK10789
SmdA family multidrug ABC transporter permease/ATP-binding protein;
34-239 2.91e-15

SmdA family multidrug ABC transporter permease/ATP-binding protein;


Pssm-ID: 182732 [Multi-domain]  Cd Length: 569  Bit Score: 77.45  E-value: 2.91e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054819401  34 AVDDLTLTVPSGSFFALLGPSGCGKTTTLRMVAGLEQPTDGTISIDGRDVTGTRAH--RRPVNTVFQSYALFPHlTVAEN 111
Cdd:PRK10789  330 ALENVNFTLKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGDIRFHDIPLTKLQLDswRSRLAVVSQTPFLFSD-TVANN 408

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054819401 112 VAFGLRRRREADVE-----ARVAEGLALVELGHLAD--RRPALLSGGQQQRVALARALVNRPALLLLDEPLGALDLKLRR 184
Cdd:PRK10789  409 IALGRPDATQQEIEhvarlASVHDDILRLPQGYDTEvgERGVMLSGGQKQRISIARALLLNAEILILDDALSAVDGRTEH 488

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1054819401 185 QMQLELKriQTEVGLTFVHVTHdQEEAMTMADTVAVMNRGRIEQMGPPADLYEHP 239
Cdd:PRK10789  489 QILHNLR--QWGEGRTVIISAH-RLSALTEASEILVMQHGHIAQRGNHDQLAQQS 540
ABCC_SUR1_N cd03290
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ...
 35-224 3.14e-15

ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The sulfonylurea receptor SUR is an ATP transporter of the ABCC/MRP family with tandem ATPase binding domains. Unlike other ABC proteins, it has no intrinsic transport function, neither active nor passive, but associates with the potassium channel proteins Kir6.1 or Kir6.2 to form the ATP-sensitive potassium (K(ATP)) channel. Within the channel complex, SUR serves as a regulatory subunit that fine-tunes the gating of Kir6.x in response to alterations in cellular metabolism. It constitutes a major pharmaceutical target as it binds numerous drugs, K(ATP) channel openers and blockers, capable of up- or down-regulating channel activity.


Pssm-ID: 213257 [Multi-domain]  Cd Length: 218  Bit Score: 74.29  E-value: 3.14e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054819401  35 VDDLTLTVPSGSFFALLGPSGCGKTTTLRMVAGLEQPTDGTI-----SIDGRDVTGTRAHRR-PVNTVFQSYALFpHLTV 108
Cdd:cd03290    17 LSNINIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVhwsnkNESEPSFEATRSRNRySVAYAAQKPWLL-NATV 95

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054819401 109 AENVAFGL---RRRREADVEA-RVAEGLALVELGHLAD--RRPALLSGGQQQRVALARALVNRPALLLLDEPLGALDLKL 182
Cdd:cd03290    96 EENITFGSpfnKQRYKAVTDAcSLQPDIDLLPFGDQTEigERGINLSGGQRQRICVARALYQNTNIVFLDDPFSALDIHL 175

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 1054819401 183 RRQ-MQLELKRIQTEVGLTFVHVTHdQEEAMTMADTVAVMNRG 224
Cdd:cd03290   176 SDHlMQEGILKFLQDDKRTLVLVTH-KLQYLPHADWIIAMKDG 217
PRK10762 PRK10762
D-ribose transporter ATP binding protein; Provisional
 20-237 8.15e-15

D-ribose transporter ATP binding protein; Provisional


Pssm-ID: 236755 [Multi-domain]  Cd Length: 501  Bit Score: 75.81  E-value: 8.15e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054819401  20 LELAAVTKRFGAFVAVDDLTLTVPSGSFFALLGPSGCGKTTTLRMVAGLEQPTDGTISIDGRDVT--GTRAHRRP-VNTV 96
Cdd:PRK10762    5 LQLKGIDKAFPGVKALSGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSILYLGKEVTfnGPKSSQEAgIGII 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054819401  97 FQSYALFPHLTVAENV--------AFGL----RRRREADVEarvaegLALVELGHLADRRPALLSGGQQQRVALARALVN 164
Cdd:PRK10762   85 HQELNLIPQLTIAENIflgrefvnRFGRidwkKMYAEADKL------LARLNLRFSSDKLVGELSIGEQQMVEIAKVLSF 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054819401 165 RPALLLLDEPLGALD-------LKLRRqmqlELKriqtEVGLTFVHVTHDQEEAMTMADTVAVMNRGRIEQMGPPADLYE 237
Cdd:PRK10762  159 ESKVIIMDEPTDALTdteteslFRVIR----ELK----SQGRGIVYISHRLKEIFEICDDVTVFRDGQFIAEREVADLTE 230
40850658_otr NF000106
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
20-226 8.48e-15

oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;


Pssm-ID: 411078 [Multi-domain]  Cd Length: 351  Bit Score: 74.77  E-value: 8.48e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054819401  20 LELAAVTKRFGAFVAVDDLTLTVPSGSFFALLGPSGCGKTTTlRMVAGLEQPTDG-------TISIDGRDVTGTRAHRRP 92
Cdd:NF000106   14 VEVRGLVKHFGEVKAVDGVDLDVREGTVLGVLGP*GAA**RG-ALPAHV*GPDAGrrpwrf*TWCANRRALRRTIG*HRP 92

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054819401  93 VNT-VFQSYALFPHLTVAENVaFGLRRRreaDVEARVAEGLALVELGHLADRRPALLSGGQQQRVALARALVNRPALLLL 171
Cdd:NF000106   93 VR*gRRESFSGRENLYMIGR*-LDLSRK---DARARADELLERFSLTEAAGRAAAKYSGGMRRRLDLAASMIGRPAVLYL 168

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1054819401 172 DEPLGALDLKLRRQMQLELKRIQTEvGLTFVHVTHDQEEAMTMADTVAVMNRGRI 226
Cdd:NF000106  169 DEPTTGLDPRTRNEVWDEVRSMVRD-GATVLLTTQYMEEAEQLAHELTVIDRGRV 222
dppD PRK11022
dipeptide transporter ATP-binding subunit; Provisional
 32-240 1.18e-14

dipeptide transporter ATP-binding subunit; Provisional


Pssm-ID: 182906 [Multi-domain]  Cd Length: 326  Bit Score: 74.01  E-value: 1.18e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054819401  32 FVAVDDLTLTVPSGSFFALLGPSGCGKTTTLRMVAGL-EQP---TDGTISIDGRDVTGTRAHRR------PVNTVFQS-- 99
Cdd:PRK11022   20 FRAVDRISYSVKQGEVVGIVGESGSGKSVSSLAIMGLiDYPgrvMAEKLEFNGQDLQRISEKERrnlvgaEVAMIFQDpm 99

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054819401 100 YALFPHLTVAENVAFGL--------RRRREadveaRVAEGLALVELGHLADR---RPALLSGGQQQRVALARALVNRPAL 168
Cdd:PRK11022  100 TSLNPCYTVGFQIMEAIkvhqggnkKTRRQ-----RAIDLLNQVGIPDPASRldvYPHQLSGGMSQRVMIAMAIACRPKL 174

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1054819401 169 LLLDEPLGALDLKLRRQMQLELKRIQTEVGLTFVHVTHDQEEAMTMADTVAVMNRGRIEQMGPPADLYEHPR 240
Cdd:PRK11022  175 LIADEPTTALDVTIQAQIIELLLELQQKENMALVLITHDLALVAEAAHKIIVMYAGQVVETGKAHDIFRAPR 246
PLN03232 PLN03232
ABC transporter C family member; Provisional
 37-237 1.34e-14

ABC transporter C family member; Provisional


Pssm-ID: 215640 [Multi-domain]  Cd Length: 1495  Bit Score: 75.78  E-value: 1.34e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054819401   37 DLTLTVPSGSFFALLGPSGCGKTTTLRMVAGlEQPTDGTISIDGRdvtGTRAHRRPVNTVFQSyalfphlTVAENVAFGL 116
Cdd:PLN03232   635 DINLEIPVGSLVAIVGGTGEGKTSLISAMLG-ELSHAETSSVVIR---GSVAYVPQVSWIFNA-------TVRENILFGS 703

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054819401  117 -----RRRREADVEA-----RVAEGLALVELGHladrRPALLSGGQQQRVALARALVNRPALLLLDEPLGALDLKLRRQ- 185
Cdd:PLN03232   704 dfeseRYWRAIDVTAlqhdlDLLPGRDLTEIGE----RGVNISGGQKQRVSMARAVYSNSDIYIFDDPLSALDAHVAHQv 779

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1054819401  186 ----MQLELKriqtevGLTFVHVThDQEEAMTMADTVAVMNRGRIEQMGPPADLYE 237
Cdd:PLN03232   780 fdscMKDELK------GKTRVLVT-NQLHFLPLMDRIILVSEGMIKEEGTFAELSK 828
hmuV PRK13547
heme ABC transporter ATP-binding protein;
33-235 1.84e-14

heme ABC transporter ATP-binding protein;


Pssm-ID: 184132 [Multi-domain]  Cd Length: 272  Bit Score: 72.94  E-value: 1.84e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054819401  33 VAVDDLTLTVPSGSFFALLGPSGCGKTTTLRMVAG-LEQPTD-------GTISIDGRD---VTGTRAHRRPVNTVFQSYA 101
Cdd:PRK13547   15 AILRDLSLRIEPGRVTALLGRNGAGKSTLLKALAGdLTGGGAprgarvtGDVTLNGEPlaaIDAPRLARLRAVLPQAAQP 94

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054819401 102 LFPhLTVAENVAFG----LRRRREADVEAR--VAEGLALVELGHLADRRPALLSGGQQQRVALARALVN---------RP 166
Cdd:PRK13547   95 AFA-FSAREIVLLGryphARRAGALTHRDGeiAWQALALAGATALVGRDVTTLSGGELARVQFARVLAQlwpphdaaqPP 173

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1054819401 167 ALLLLDEPLGALDLKLRRQMQLELKRIQTEVGLTFVHVTHDQEEAMTMADTVAVMNRGRIEQMGPPADL 235
Cdd:PRK13547  174 RYLLLDEPTAALDLAHQHRLLDTVRRLARDWNLGVLAIVHDPNLAARHADRIAMLADGAIVAHGAPADV 242
ABC_RNaseL_inhibitor_domain2 cd03237
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ...
 36-219 2.29e-14

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: 72.06  E-value: 2.29e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054819401  36 DDLTLTVPSGSF-----FALLGPSGCGKTTTLRMVAGLEQPTDGTISIDGRDVTGTRAHRRPVNTVFQSYALFPHLTVAE 110
Cdd:cd03237    11 GEFTLEVEGGSIsesevIGILGPNGIGKTTFIKMLAGVLKPDEGDIEIELDTVSYKPQYIKADYEGTVRDLLSSITKDFY 90

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054819401 111 NVAFglrrrreadVEARVAEGLALVElghLADRRPALLSGGQQQRVALARALVNRPALLLLDEPLGALDLKLRRQMQLEL 190
Cdd:cd03237    91 THPY---------FKTEIAKPLQIEQ---ILDREVPELSGGELQRVAIAACLSKDADIYLLDEPSAYLDVEQRLMASKVI 158

                         170       180
                  ....*....|....*....|....*....
gi 1054819401 191 KRIQTEVGLTFVHVTHDqeeaMTMADTVA 219
Cdd:cd03237   159 RRFAENNEKTAFVVEHD----IIMIDYLA 183
ABC_FeS_Assembly cd03217
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ...
 35-238 3.82e-14

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: 70.63  E-value: 3.82e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054819401  35 VDDLTLTVPSGSFFALLGPSGCGKTTTLRMVAGLE--QPTDGTISIDGRDVTG----TRAhRRPVNTVFQSYALFPHLTV 108
Cdd:cd03217    16 LKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMGHPkyEVTEGEILFKGEDITDlppeERA-RLGIFLAFQYPPEIPGVKN 94

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054819401 109 AEnvaFgLRrrreadveaRVAEGlalvelghladrrpalLSGGQQQRVALARALVNRPALLLLDEPLGALDLKLRRQMQL 188
Cdd:cd03217    95 AD---F-LR---------YVNEG----------------FSGGEKKRNEILQLLLLEPDLAILDEPDSGLDIDALRLVAE 145

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1054819401 189 ELKRIQTEvGLTFVHVTHDQEEAMTM-ADTVAVMNRGRIEQMGPPA---DLYEH 238
Cdd:cd03217   146 VINKLREE-GKSVLIITHYQRLLDYIkPDRVHVLYDGRIVKSGDKElalEIEKK 198
PRK15439 PRK15439
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
 37-226 7.94e-14

autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional


Pssm-ID: 185336 [Multi-domain]  Cd Length: 510  Bit Score: 72.78  E-value: 7.94e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054819401  37 DLTLTVPSGSFFALLGPSGCGKTTTLRMVAGLEQPTDGTISIDGRDVTG-TRAHRRPVNTVF-----QSYALFPHLTVAE 110
Cdd:PRK15439  281 NISLEVRAGEILGLAGVVGAGRTELAETLYGLRPARGGRIMLNGKEINAlSTAQRLARGLVYlpedrQSSGLYLDAPLAW 360

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054819401 111 NV--------AFGLRRRREADVEARVAEGLAlVELGHlADRRPALLSGGQQQRVALARALVNRPALLLLDEPLGALDLKL 182
Cdd:PRK15439  361 NVcalthnrrGFWIKPARENAVLERYRRALN-IKFNH-AEQAARTLSGGNQQKVLIAKCLEASPQLLIVDEPTRGVDVSA 438

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 1054819401 183 RRQMQLELKRI-QTEVGLTFvhVTHDQEEAMTMADTVAVMNRGRI 226
Cdd:PRK15439  439 RNDIYQLIRSIaAQNVAVLF--ISSDLEEIEQMADRVLVMHQGEI 481
PRK10762 PRK10762
D-ribose transporter ATP binding protein; Provisional
 35-226 2.35e-13

D-ribose transporter ATP binding protein; Provisional


Pssm-ID: 236755 [Multi-domain]  Cd Length: 501  Bit Score: 71.19  E-value: 2.35e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054819401  35 VDDLTLTVPSGSFFALLGPSGCGKTTTLRMVAGLEQPTDGTISIDGRDVTGTRAHRRPVN-TVFQSY-----ALFPHLTV 108
Cdd:PRK10762  268 VNDVSFTLRKGEILGVSGLMGAGRTELMKVLYGALPRTSGYVTLDGHEVVTRSPQDGLANgIVYISEdrkrdGLVLGMSV 347

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054819401 109 AENVA---------FGLRRRREADVEArVAEGLALVELGHLA-DRRPALLSGGQQQRVALARALVNRPALLLLDEPLGAL 178
Cdd:PRK10762  348 KENMSltalryfsrAGGSLKHADEQQA-VSDFIRLFNIKTPSmEQAIGLLSGGNQQKVAIARGLMTRPKVLILDEPTRGV 426

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 1054819401 179 DLKLRRQM-QLeLKRIQTEvGLTFVHVTHDQEEAMTMADTVAVMNRGRI 226
Cdd:PRK10762  427 DVGAKKEIyQL-INQFKAE-GLSIILVSSEMPEVLGMSDRILVMHEGRI 473
PRK13543 PRK13543
heme ABC exporter ATP-binding protein CcmA;
38-180 4.21e-13

heme ABC exporter ATP-binding protein CcmA;


Pssm-ID: 184129 [Multi-domain]  Cd Length: 214  Bit Score: 67.95  E-value: 4.21e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054819401  38 LTLTVPSGSFFALLGPSGCGKTTTLRMVAGLEQPTDGTISIDGRDVTgtRAHR-RPVNTVFQSYALFPHLTVAENVAF-- 114
Cdd:PRK13543   30 LDFHVDAGEALLVQGDNGAGKTTLLRVLAGLLHVESGQIQIDGKTAT--RGDRsRFMAYLGHLPGLKADLSTLENLHFlc 107

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1054819401 115 GLRRRREADVEArvaEGLALVELGHLADRRPALLSGGQQQRVALARALVNRPALLLLDEPLGALDL 180
Cdd:PRK13543  108 GLHGRRAKQMPG---SALAIVGLAGYEDTLVRQLSAGQKKRLALARLWLSPAPLWLLDEPYANLDL 170
PRK11819 PRK11819
putative ABC transporter ATP-binding protein; Reviewed
 20-179 5.08e-13

putative ABC transporter ATP-binding protein; Reviewed


Pssm-ID: 236992 [Multi-domain]  Cd Length: 556  Bit Score: 70.15  E-value: 5.08e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054819401  20 LELAAVTKRFGAFVAVDDLTLTVPSGSFFALLGPSGCGKTTTLRMVAGLEQPTDGTISIdGRDVT-----GTRAHRRPVN 94
Cdd:PRK11819  325 IEAENLSKSFGDRLLIDDLSFSLPPGGIVGIIGPNGAGKSTLFKMITGQEQPDSGTIKI-GETVKlayvdQSRDALDPNK 403

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054819401  95 TVFQSyalfphltvaenvafglrrrreadvearVAEGLALVELGHL---------------AD--RRPALLSGGQQQRVA 157
Cdd:PRK11819  404 TVWEE----------------------------ISGGLDIIKVGNReipsrayvgrfnfkgGDqqKKVGVLSGGERNRLH 455

                         170       180
                  ....*....|....*....|..
gi 1054819401 158 LARALVNRPALLLLDEPLGALD 179
Cdd:PRK11819  456 LAKTLKQGGNVLLLDEPTNDLD 477
ABCC_NFT1 cd03369
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ...
 34-232 5.95e-13

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: 67.44  E-value: 5.95e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054819401  34 AVDDLTLTVPSGSFFALLGPSGCGKTTTLRMVAGLEQPTDGTISIDGRDVT--GTRAHRRPVNTVFQSYALFPHlTVAEN 111
Cdd:cd03369    23 VLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDGIDIStiPLEDLRSSLTIIPQDPTLFSG-TIRSN 101

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054819401 112 V-AFGLRRRREADVEARVAEGlalvelghladrrPALLSGGQQQRVALARALVNRPALLLLDEPLGALDLKLRRQMQlel 190
Cdd:cd03369   102 LdPFDEYSDEEIYGALRVSEG-------------GLNLSQGQRQLLCLARALLKRPRVLVLDEATASIDYATDALIQ--- 165

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 1054819401 191 KRIQTEV-GLTFVHVTHdqeEAMTMA--DTVAVMNRGRIEQMGPP 232
Cdd:cd03369   166 KTIREEFtNSTILTIAH---RLRTIIdyDKILVMDAGEVKEYDHP 207
PLN03130 PLN03130
ABC transporter C family member; Provisional
 37-235 8.33e-13

ABC transporter C family member; Provisional


Pssm-ID: 215595 [Multi-domain]  Cd Length: 1622  Bit Score: 70.15  E-value: 8.33e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054819401   37 DLTLTVPSGSFFALLGPSGCGKTTTLRMVAGlEQPT--DGTISIdgrdvTGTRAHRRPVNTVFQSyalfphlTVAENVAF 114
Cdd:PLN03130   635 NINLDVPVGSLVAIVGSTGEGKTSLISAMLG-ELPPrsDASVVI-----RGTVAYVPQVSWIFNA-------TVRDNILF 701

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054819401  115 GL-----RRRREADVEArVAEGLALVELGHLAD--RRPALLSGGQQQRVALARALVNRPALLLLDEPLGALDLKLRRQ-- 185
Cdd:PLN03130   702 GSpfdpeRYERAIDVTA-LQHDLDLLPGGDLTEigERGVNISGGQKQRVSMARAVYSNSDVYIFDDPLSALDAHVGRQvf 780

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|...
gi 1054819401  186 ---MQLELKriqtevGLTFVHVThDQEEAMTMADTVAVMNRGRIEQMGPPADL 235
Cdd:PLN03130   781 dkcIKDELR------GKTRVLVT-NQLHFLSQVDRIILVHEGMIKEEGTYEEL 826
3a01203 TIGR00954
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ...
 33-206 1.14e-12

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: 69.39  E-value: 1.14e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054819401  33 VAVDDLTLTVPSGSFFALLGPSGCGKTTTLRMVAGLEQPTDGTISIDgRDVTGTRAHRRPVNTV--FQSYALFPhltvae 110
Cdd:TIGR00954 466 VLIESLSFEVPSGNNLLICGPNGCGKSSLFRILGELWPVYGGRLTKP-AKGKLFYVPQRPYMTLgtLRDQIIYP------ 538

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054819401 111 NVAFGLRRR--READVEARvaegLALVELGHLADRRPA---------LLSGGQQQRVALARALVNRPALLLLDEPLGALD 179
Cdd:TIGR00954 539 DSSEDMKRRglSDKDLEQI----LDNVQLTHILEREGGwsavqdwmdVLSGGEKQRIAMARLFYHKPQFAILDECTSAVS 614

                         170       180
                  ....*....|....*....|....*..
gi 1054819401 180 LKLRRQMQLELKriqtEVGLTFVHVTH 206
Cdd:TIGR00954 615 VDVEGYMYRLCR----EFGITLFSVSH 637
ABC_ABC_ChvD TIGR03719
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ...
 36-207 1.30e-12

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: 69.19  E-value: 1.30e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054819401  36 DDLTLTVPSGSFFALLGPSGCGKTTTLRMVAGLEQPTDGtisidgrdvtgtRAHRRPVNTV---FQSYALFPHLTVAENV 112
Cdd:TIGR03719  22 KDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKDFNG------------EARPQPGIKVgylPQEPQLDPTKTVRENV 89

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054819401 113 AFGLRRRRE----------------ADVEARVAEGLALVEL-----GHLADRR----------P------ALLSGGQQQR 155
Cdd:TIGR03719  90 EEGVAEIKDaldrfneisakyaepdADFDKLAAEQAELQEIidaadAWDLDSQleiamdalrcPpwdadvTKLSGGERRR 169

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1054819401 156 VALARALVNRPALLLLDEPLGALDLKLRRQMQLELKRIQTevglTFVHVTHD 207
Cdd:TIGR03719 170 VALCRLLLSKPDMLLLDEPTNHLDAESVAWLERHLQEYPG----TVVAVTHD 217
SufC COG0396
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, ...
 33-232 1.47e-12

Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 440165 [Multi-domain]  Cd Length: 245  Bit Score: 66.63  E-value: 1.47e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054819401  33 VAVDD------LTLTVPSGSFFALLGPSGCGKTTTLRMVAGLE--QPTDGTISIDGRDVTG----TRAhRRPVNTVFQSY 100
Cdd:COG0396     8 VSVEGkeilkgVNLTIKPGEVHAIMGPNGSGKSTLAKVLMGHPkyEVTSGSILLDGEDILElspdERA-RAGIFLAFQYP 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054819401 101 ALFPHLTVAE--NVAFGLRRRREADVEA---RVAEGLALVELGH-LADRrpAL---LSGGQQQRVALARALVNRPALLLL 171
Cdd:COG0396    87 VEIPGVSVSNflRTALNARRGEELSAREflkLLKEKMKELGLDEdFLDR--YVnegFSGGEKKRNEILQMLLLEPKLAIL 164

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1054819401 172 DEPLGALDLKLRRQMQLELKRIQTEvGLTFVHVTHDQE--EAMTmADTVAVMNRGRIEQMGPP 232
Cdd:COG0396   165 DETDSGLDIDALRIVAEGVNKLRSP-DRGILIITHYQRilDYIK-PDFVHVLVDGRIVKSGGK 225
PRK11147 PRK11147
ABC transporter ATPase component; Reviewed
 35-209 1.88e-12

ABC transporter ATPase component; Reviewed


Pssm-ID: 236861 [Multi-domain]  Cd Length: 635  Bit Score: 68.82  E-value: 1.88e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054819401  35 VDDLTLTVPSGSFFALLGPSGCGKTTTLRMVAGLEQPTDGTISIdgrdvtGTR---AHrrpvntvFQSY--ALFPHLTVA 109
Cdd:PRK11147  335 VKDFSAQVQRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRIHC------GTKlevAY-------FDQHraELDPEKTVM 401

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054819401 110 ENVAFGlrrRREADVEAR---VaeglalveLGHLAD--------RRPA-LLSGGQQQRVALARALVnRPA-LLLLDEPLG 176
Cdd:PRK11147  402 DNLAEG---KQEVMVNGRprhV--------LGYLQDflfhpkraMTPVkALSGGERNRLLLARLFL-KPSnLLILDEPTN 469

                         170       180       190
                  ....*....|....*....|....*....|....
gi 1054819401 177 ALDLKlrrqmQLE-LKRIQTEVGLTFVHVTHDQE 209
Cdd:PRK11147  470 DLDVE-----TLElLEELLDSYQGTVLLVSHDRQ 498
ABCG_PDR_domain1 cd03233
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ...
 27-226 4.08e-12

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: 64.59  E-value: 4.08e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054819401  27 KRFGAFVAVDDLTLTVPSGSFFALLGPSGCGKTTTLRMVAGLEQPT---DGTISIDGRDVTGT-RAHRRPVNTVFQSYAL 102
Cdd:cd03233    15 KGRSKIPILKDFSGVVKPGEMVLVLGRPGSGCSTLLKALANRTEGNvsvEGDIHYNGIPYKEFaEKYPGEIIYVSEEDVH 94

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054819401 103 FPHLTVAENVAFGLRRRREADVeaRVaeglalvelghladrrpalLSGGQQQRVALARALVNRPALLLLDEPLGALD--- 179
Cdd:cd03233    95 FPTLTVRETLDFALRCKGNEFV--RG-------------------ISGGERKRVSIAEALVSRASVLCWDNSTRGLDsst 153

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1054819401 180 ----LKLRRQMQLELKriqtevGLTFVHVTHDQEEAMTMADTVAVMNRGRI 226
Cdd:cd03233   154 aleiLKCIRTMADVLK------TTTFVSLYQASDEIYDLFDKVLVLYEGRQ 198
PRK03695 PRK03695
vitamin B12-transporter ATPase; Provisional
 33-234 1.41e-11

vitamin B12-transporter ATPase; Provisional


Pssm-ID: 235150 [Multi-domain]  Cd Length: 248  Bit Score: 64.18  E-value: 1.41e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054819401  33 VAVDD----LTLTVPSGSFFALLGPSGCGKTTTLRMVAGLeQPTDGTISIDGRDV----TGTRAHRR---------PVNT 95
Cdd:PRK03695    6 VAVSTrlgpLSAEVRAGEILHLVGPNGAGKSTLLARMAGL-LPGSGSIQFAGQPLeawsAAELARHRaylsqqqtpPFAM 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054819401  96 -VFQSYALfpHLTVaenvafglrRRREADVEARVAEGLALVELGHLADRRPALLSGGQQQRVALARAL-----VNRPA-- 167
Cdd:PRK03695   85 pVFQYLTL--HQPD---------KTRTEAVASALNEVAEALGLDDKLGRSVNQLSGGEWQRVRLAAVVlqvwpDINPAgq 153

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1054819401 168 LLLLDEPLGALDLKLRRQMQLELKRIqTEVGLTFVHVTHDQEEAMTMADTVAVMNRGRIEQMGPPAD 234
Cdd:PRK03695  154 LLLLDEPMNSLDVAQQAALDRLLSEL-CQQGIAVVMSSHDLNHTLRHADRVWLLKQGKLLASGRRDE 219
PRK09700 PRK09700
D-allose ABC transporter ATP-binding protein AlsA;
35-229 1.60e-11

D-allose ABC transporter ATP-binding protein AlsA;


Pssm-ID: 182036 [Multi-domain]  Cd Length: 510  Bit Score: 65.58  E-value: 1.60e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054819401  35 VDDLTLTVPSGSFFALLGPSGCGKTTTLRMVAGLEQPTDGTISIDGRDVTgtraHRRPVNTVFQSYAL----------FP 104
Cdd:PRK09700  279 VRDISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEIRLNGKDIS----PRSPLDAVKKGMAYitesrrdngfFP 354

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054819401 105 HLTVAENVA-------------FGLRRRREadvEARVAEGL-ALVELG-HLADRRPALLSGGQQQRVALARALVNRPALL 169
Cdd:PRK09700  355 NFSIAQNMAisrslkdggykgaMGLFHEVD---EQRTAENQrELLALKcHSVNQNITELSGGNQQKVLISKWLCCCPEVI 431

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054819401 170 LLDEPLGALDLKLRRQMqLELKRIQTEVGLTFVHVTHDQEEAMTMADTVAVMNRGRIEQM 229
Cdd:PRK09700  432 IFDEPTRGIDVGAKAEI-YKVMRQLADDGKVILMVSSELPEIITVCDRIAVFCEGRLTQI 490
araG PRK11288
L-arabinose ABC transporter ATP-binding protein AraG;
39-226 2.06e-11

L-arabinose ABC transporter ATP-binding protein AraG;


Pssm-ID: 183077 [Multi-domain]  Cd Length: 501  Bit Score: 65.32  E-value: 2.06e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054819401  39 TLTVPSGSFFALLGPSGCGKTTTLRMVAGLEQPTDGTISIDGRDVtgtrAHRRPVNTVFQSYAL----------FPHLTV 108
Cdd:PRK11288  273 SFSVRAGEIVGLFGLVGAGRSELMKLLYGATRRTAGQVYLDGKPI----DIRSPRDAIRAGIMLcpedrkaegiIPVHSV 348

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054819401 109 AENVAFGLRR-----------RREADVEARVAEGLALVELGhlADRRPALLSGGQQQRVALARALVNRPALLLLDEPLGA 177
Cdd:PRK11288  349 ADNINISARRhhlragclinnRWEAENADRFIRSLNIKTPS--REQLIMNLSGGNQQKAILGRWLSEDMKVILLDEPTRG 426

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1054819401 178 LDLKLRR---QMQLELkriqTEVGLTFVHVTHDQEEAMTMADTVAVMNRGRI 226
Cdd:PRK11288  427 IDVGAKHeiyNVIYEL----AAQGVAVLFVSSDLPEVLGVADRIVVMREGRI 474
PvdE COG4615
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ...
 40-173 2.61e-11

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: 64.82  E-value: 2.61e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054819401  40 LTVPSGSFFALLGPSGCGKTTTLRMVAGLEQPTDGTISIDGRDVTGTR--AHRRPVNTVFQSYALFPHLtvaenvaFGLr 117
Cdd:COG4615   353 LTIRRGELVFIVGGNGSGKSTLAKLLTGLYRPESGEILLDGQPVTADNreAYRQLFSAVFSDFHLFDRL-------LGL- 424

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1054819401 118 rrREADVEARVAEGLALVELGH--------LADRRpalLSGGQQQRVALARALV-NRPaLLLLDE 173
Cdd:COG4615   425 --DGEADPARARELLERLELDHkvsvedgrFSTTD---LSQGQRKRLALLVALLeDRP-ILVFDE 483
Rli1 COG1245
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ...
 8-219 2.58e-10

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: 62.11  E-value: 2.58e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054819401   8 HPGAASASAGAALELAAVTKRFGAFvavddlTLTVPSGSFF-----ALLGPSGCGKTTTLRMVAGLEQPTDGTISIDGR- 81
Cdd:COG1245   330 HAPRREKEEETLVEYPDLTKSYGGF------SLEVEGGEIRegevlGIVGPNGIGKTTFAKILAGVLKPDEGEVDEDLKi 403

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054819401  82 ---------DVTGTrahrrpvntvfqsyalfphltvaenVAFGLRRRREADV-----EARVAEGLAlveLGHLADRRPAL 147
Cdd:COG1245   404 sykpqyispDYDGT-------------------------VEEFLRSANTDDFgssyyKTEIIKPLG---LEKLLDKNVKD 455

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1054819401 148 LSGGQQQRVALARALVnRPA-LLLLDEPLGALDLKLRRQMQLELKRIQTEVGLTFVHVTHDqeeaMTMADTVA 219
Cdd:COG1245   456 LSGGELQRVAIAACLS-RDAdLYLLDEPSAHLDVEQRLAVAKAIRRFAENRGKTAMVVDHD----IYLIDYIS 523
PLN03073 PLN03073
ABC transporter F family; Provisional
 46-226 3.25e-10

ABC transporter F family; Provisional


Pssm-ID: 215558 [Multi-domain]  Cd Length: 718  Bit Score: 61.80  E-value: 3.25e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054819401  46 SFFALLGPSGCGKTTTLRMVAGLEQPTDGTI--------------SIDGRDVTGTrahrrPVNTVFQSYALFPHLTVAEN 111
Cdd:PLN03073  536 SRIAMVGPNGIGKSTILKLISGELQPSSGTVfrsakvrmavfsqhHVDGLDLSSN-----PLLYMMRCFPGVPEQKLRAH 610

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054819401 112 V-AFGLRrrreadvearvaeglalvelGHLADRRPALLSGGQQQRVALARALVNRPALLLLDEPLGALDLKLRRQMQLEL 190
Cdd:PLN03073  611 LgSFGVT--------------------GNLALQPMYTLSGGQKSRVAFAKITFKKPHILLLDEPSNHLDLDAVEALIQGL 670

                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 1054819401 191 KRIQTEVgltfVHVTHDQEEAMTMADTVAVMNRGRI 226
Cdd:PLN03073  671 VLFQGGV----LMVSHDEHLISGSVDELWVVSEGKV 702
xylG TIGR02633
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ...
 35-241 3.59e-10

D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose isomerase and xylulokinase enzymes for xylose utilization. Members of this protein family are the ATP-binding cassette (ABC) subunit of the known or predicted high-affinity xylose ABC transporter for xylose import. These genes, which closely resemble other sugar transport ABC transporter genes, typically are encoded near xylose utilization enzymes and regulatory proteins. Note that this form of the transporter contains two copies of the ABC transporter domain (pfam00005). [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]


Pssm-ID: 131681 [Multi-domain]  Cd Length: 500  Bit Score: 61.38  E-value: 3.59e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054819401  35 VDDLTLTVPSGSFFALLGPSGCGKTTTLRMVAGL-EQPTDGTISIDGRDVtgtrAHRRPVNTVFQSYALFPH-------- 105
Cdd:TIGR02633 276 VDDVSFSLRRGEILGVAGLVGAGRTELVQALFGAyPGKFEGNVFINGKPV----DIRNPAQAIRAGIAMVPEdrkrhgiv 351

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054819401 106 --LTVAENVAFG-LRR---RREADVEARVAEGLALVELGHLADRRPAL----LSGGQQQRVALARALVNRPALLLLDEPL 175
Cdd:TIGR02633 352 piLGVGKNITLSvLKSfcfKMRIDAAAELQIIGSAIQRLKVKTASPFLpigrLSGGNQQKAVLAKMLLTNPRVLILDEPT 431

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1054819401 176 GALDLKLRRQMQLELKRIQTEvGLTFVHVTHDQEEAMTMADTVAVMNRGRIEqmgppADLYEHPRT 241
Cdd:TIGR02633 432 RGVDVGAKYEIYKLINQLAQE-GVAIIVVSSELAEVLGLSDRVLVIGEGKLK-----GDFVNHALT 491
CFTR_protein TIGR01271
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ...
 37-180 3.91e-10

cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis fibrosis transmembrane conductor regulator (CFTR) in eukaryotes. The principal role of this protein is chloride ion conductance. The protein is predicted to consist of 12 transmembrane domains. Mutations or lesions in the genetic loci have been linked to the aetiology of asthma, bronchiectasis, chronic obstructive pulmonary disease etc. Disease-causing mutations have been studied by 36Cl efflux assays in vitro cell cultures and electrophysiology, all of which point to the impairment of chloride channel stability and not the biosynthetic processing per se. [Transport and binding proteins, Anions]


Pssm-ID: 273530 [Multi-domain]  Cd Length: 1490  Bit Score: 61.85  E-value: 3.91e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054819401   37 DLTLTVPSGSFFALLGPSGCGKTTTLRMVAGLEQPTDGTISIDGRdvtgtrahrrpVNTVFQSYALFPHlTVAENVAFGL 116
Cdd:TIGR01271  444 NISFKLEKGQLLAVAGSTGSGKSSLLMMIMGELEPSEGKIKHSGR-----------ISFSPQTSWIMPG-TIKDNIIFGL 511

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1054819401  117 R----RRREADVEARVAEGLALVELghlADRRPAL-----LSGGQQQRVALARALVNRPALLLLDEPLGALDL 180
Cdd:TIGR01271  512 SydeyRYTSVIKACQLEEDIALFPE---KDKTVLGeggitLSGGQRARISLARAVYKDADLYLLDSPFTHLDV 581
PRK11819 PRK11819
putative ABC transporter ATP-binding protein; Reviewed
 36-179 3.97e-10

putative ABC transporter ATP-binding protein; Reviewed


Pssm-ID: 236992 [Multi-domain]  Cd Length: 556  Bit Score: 61.29  E-value: 3.97e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054819401  36 DDLTLtvpsgSFF-----ALLGPSGCGKTTTLRMVAGLEQPTDGtisiDGRDVTGTRahrrpVNTVFQSYALFPHLTVAE 110
Cdd:PRK11819   24 KDISL-----SFFpgakiGVLGLNGAGKSTLLRIMAGVDKEFEG----EARPAPGIK-----VGYLPQEPQLDPEKTVRE 89

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054819401 111 NVAFGLRRRRE----------------ADVEARVAEGLALVEL-----GHLADRR-----PAL-----------LSGGQQ 153
Cdd:PRK11819   90 NVEEGVAEVKAaldrfneiyaayaepdADFDALAAEQGELQEIidaadAWDLDSQleiamDALrcppwdakvtkLSGGER 169

                         170       180
                  ....*....|....*....|....*.
gi 1054819401 154 QRVALARALVNRPALLLLDEPLGALD 179
Cdd:PRK11819  170 RRVALCRLLLEKPDMLLLDEPTNHLD 195
PTZ00265 PTZ00265
multidrug resistance protein (mdr1); Provisional
 37-225 5.48e-10

multidrug resistance protein (mdr1); Provisional


Pssm-ID: 240339 [Multi-domain]  Cd Length: 1466  Bit Score: 61.20  E-value: 5.48e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054819401   37 DLTLTVPSGSFFALLGPSGCGKTTTLRMVAGLEQPTDGTISIDG----RDVTgTRAHRRPVNTVFQSYALFPHlTVAENV 112
Cdd:PTZ00265   403 DLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIIINDshnlKDIN-LKWWRSKIGVVSQDPLLFSN-SIKNNI 480

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054819401  113 AFGLRRRREADV----------------------EARVAEGLALV-------ELGH------------------------ 139
Cdd:PTZ00265   481 KYSLYSLKDLEAlsnyynedgndsqenknkrnscRAKCAGDLNDMsnttdsnELIEmrknyqtikdsevvdvskkvlihd 560

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054819401  140 ----LADRRPAL-------LSGGQQQRVALARALVNRPALLLLDEPLGALDLKLRRQMQLELKRIQTEVGLTFVHVTHdQ 208
Cdd:PTZ00265   561 fvsaLPDKYETLvgsnaskLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQKTINNLKGNENRITIIIAH-R 639

                          250
                   ....*....|....*...
gi 1054819401  209 EEAMTMADTVAVM-NRGR 225
Cdd:PTZ00265   640 LSTIRYANTIFVLsNRER 657
ABCC_CFTR1 cd03291
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ...
 37-186 6.23e-10

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: 59.49  E-value: 6.23e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054819401  37 DLTLTVPSGSFFALLGPSGCGKTTTLRMVAGLEQPTDGTISIDGRdvtgtrahrrpVNTVFQSYALFPHlTVAENVAFGL 116
Cdd:cd03291    55 NINLKIEKGEMLAITGSTGSGKTSLLMLILGELEPSEGKIKHSGR-----------ISFSSQFSWIMPG-TIKENIIFGV 122

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054819401 117 ---RRRREADVEARVAEGlalvELGHLADRRPAL-------LSGGQQQRVALARALVNRPALLLLDEPLGALDLKLRRQM 186
Cdd:cd03291   123 sydEYRYKSVVKACQLEE----DITKFPEKDNTVlgeggitLSGGQRARISLARAVYKDADLYLLDSPFGYLDVFTEKEI 198
MRP_assoc_pro TIGR00957
multi drug resistance-associated protein (MRP); This model describes multi drug ...
 37-235 6.85e-10

multi drug resistance-associated protein (MRP); This model describes multi drug resistance-associated protein (MRP) in eukaryotes. The multidrug resistance-associated protein is an integral membrane protein that causes multidrug resistance when overexpressed in mammalian cells. It belongs to ABC transporter superfamily. The protein topology and function was experimentally demonstrated by epitope tagging and immunofluorescence. Insertion of tags in the critical regions associated with drug efflux, abrogated its function. The C-terminal domain seem to highly conserved. [Transport and binding proteins, Other]


Pssm-ID: 188098 [Multi-domain]  Cd Length: 1522  Bit Score: 61.11  E-value: 6.85e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054819401   37 DLTLTVPSGSFFALLGPSGCGKTTTLRMVAGLEQPTDGTISIDGRDVTGTRAH--RRPVNTVFQSYALFPHlTVAENV-A 113
Cdd:TIGR00957 1304 HINVTIHGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGLNIAKIGLHdlRFKITIIPQDPVLFSG-SLRMNLdP 1382

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054819401  114 FGlrrrREADVEARVAeglalVELGHLADRRPAL--------------LSGGQQQRVALARALVNRPALLLLDEPLGALD 179
Cdd:TIGR00957 1383 FS----QYSDEEVWWA-----LELAHLKTFVSALpdkldhecaeggenLSVGQRQLVCLARALLRKTKILVLDEATAAVD 1453

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1054819401  180 LKLRRQMQLELkRIQTEvGLTFVHVTHDQEEAMTMAdTVAVMNRGRIEQMGPPADL 235
Cdd:TIGR00957 1454 LETDNLIQSTI-RTQFE-DCTVLTIAHRLNTIMDYT-RVIVLDKGEVAEFGAPSNL 1506
AAA smart00382
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ...
 44-215 8.28e-10

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: 57.00  E-value: 8.28e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054819401   44 SGSFFALLGPSGCGKTTTLRMVAGLEQPTDGT-ISIDGRDVTgtrahrrpvntvfqsyalfphltvaenvafglrrrrea 122
Cdd:smart00382   1 PGEVILIVGPPGSGKTTLARALARELGPPGGGvIYIDGEDIL-------------------------------------- 42

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054819401  123 dvearvaEGLALVELGHLADRRPALLSGGQQQRVALARALVNRPALLLLDEPLGALDLKLRRQMQLE-----LKRIQTEV 197
Cdd:smart00382  43 -------EEVLDQLLLIIVGGKKASGSGELRLRLALALARKLKPDVLILDEITSLLDAEQEALLLLLeelrlLLLLKSEK 115

                          170
                   ....*....|....*...
gi 1054819401  198 GLTFVHVTHDQEEAMTMA 215
Cdd:smart00382 116 NLTVILTTNDEKDLGPAL 133
PRK10982 PRK10982
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
 22-225 9.69e-10

galactose/methyl galaxtoside transporter ATP-binding protein; Provisional


Pssm-ID: 182880 [Multi-domain]  Cd Length: 491  Bit Score: 60.13  E-value: 9.69e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054819401  22 LAAVTKRFGAFVAVDDLTLTVPSGSFFALLGPSGCGKTTTLRMVAGLEQPTDGTISIDGRDV---TGTRAHRRPVNTVFQ 98
Cdd:PRK10982    1 MSNISKSFPGVKALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEIdfkSSKEALENGISMVHQ 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054819401  99 SYALFPHLTVAENVAFGLRRRRE--ADVEARVAEGLALV-ELGHLADRRP--ALLSGGQQQRVALARALVNRPALLLLDE 173
Cdd:PRK10982   81 ELNLVLQRSVMDNMWLGRYPTKGmfVDQDKMYRDTKAIFdELDIDIDPRAkvATLSVSQMQMIEIAKAFSYNAKIVIMDE 160

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1054819401 174 PLGALDLKLRRQMQLELKRIQtEVGLTFVHVTHDQEEAMTMADTVAVMNRGR 225
Cdd:PRK10982  161 PTSSLTEKEVNHLFTIIRKLK-ERGCGIVYISHKMEEIFQLCDEITILRDGQ 211
PRK13541 PRK13541
cytochrome c biogenesis protein CcmA; Provisional
 37-173 1.29e-09

cytochrome c biogenesis protein CcmA; Provisional


Pssm-ID: 184128 [Multi-domain]  Cd Length: 195  Bit Score: 57.19  E-value: 1.29e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054819401  37 DLTLTVPSGSFFALLGPSGCGKTTTLRMVAGLEQPTDGTISIdgRDVTGTRAHRRPVNTVFQSYALFPHLTVAENVAFGL 116
Cdd:PRK13541   18 DLSITFLPSAITYIKGANGCGKSSLLRMIAGIMQPSSGNIYY--KNCNINNIAKPYCTYIGHNLGLKLEMTVFENLKFWS 95

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1054819401 117 RRRREADVearVAEGLALVELGHLADRRPALLSGGQQQRVALARALVNRPALLLLDE 173
Cdd:PRK13541   96 EIYNSAET---LYAAIHYFKLHDLLDEKCYSLSSGMQKIVAIARLIACQSDLWLLDE 149
ABCG_PDR_domain2 cd03232
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ...
 36-179 1.33e-09

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: 57.25  E-value: 1.33e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054819401  36 DDLTLTVPSGSFFALLGPSGCGKTTTLRMVAGLEqpTDGTIS----IDGRDVTGTraHRRPVNTVFQSYALFPHLTVAEN 111
Cdd:cd03232    24 NNISGYVKPGTLTALMGESGAGKTTLLDVLAGRK--TAGVITgeilINGRPLDKN--FQRSTGYVEQQDVHSPNLTVREA 99

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054819401 112 VAFG--LRrrreadvearvaeGLALvelghladrrpallsgGQQQRVALARALVNRPALLLLDEPLGALD 179
Cdd:cd03232   100 LRFSalLR-------------GLSV----------------EQRKRLTIGVELAAKPSILFLDEPTSGLD 140
PRK13409 PRK13409
ribosome biogenesis/translation initiation ATPase RLI;
8-207 1.98e-09

ribosome biogenesis/translation initiation ATPase RLI;


Pssm-ID: 184037 [Multi-domain]  Cd Length: 590  Bit Score: 59.05  E-value: 1.98e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054819401   8 HPGAASASAGAALELAAVTKRFGAFvavddlTLTVPSGSFFA-----LLGPSGCGKTTTLRMVAGLEQPTDGTISID--- 79
Cdd:PRK13409  329 RPPRDESERETLVEYPDLTKKLGDF------SLEVEGGEIYEgevigIVGPNGIGKTTFAKLLAGVLKPDEGEVDPElki 402

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054819401  80 -------GRDVTGT-RAHRRPVNTVF-QSYalfphltvaenvafglrrrreadVEARVAEGLAlveLGHLADRRPALLSG 150
Cdd:PRK13409  403 sykpqyiKPDYDGTvEDLLRSITDDLgSSY-----------------------YKSEIIKPLQ---LERLLDKNVKDLSG 456

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1054819401 151 GQQQRVALARALvNRPA-LLLLDEPLGALDLKLRRQMQLELKRIQTEVGLTFVHVTHD 207
Cdd:PRK13409  457 GELQRVAIAACL-SRDAdLYLLDEPSAHLDVEQRLAVAKAIRRIAEEREATALVVDHD 513
PRK11147 PRK11147
ABC transporter ATPase component; Reviewed
 50-179 2.02e-09

ABC transporter ATPase component; Reviewed


Pssm-ID: 236861 [Multi-domain]  Cd Length: 635  Bit Score: 59.19  E-value: 2.02e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054819401  50 LLGPSGCGKTTTLRMVAGlEQPTD-GTISIDgRDVTGTRAHRRPVN----TVFqSYalfphltVAENVA---------FG 115
Cdd:PRK11147   34 LVGRNGAGKSTLMKILNG-EVLLDdGRIIYE-QDLIVARLQQDPPRnvegTVY-DF-------VAEGIEeqaeylkryHD 103

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054819401 116 LRRRREAD-----------------------VEARVAEGLALVELGhlADRRPALLSGGQQQRVALARALVNRPALLLLD 172
Cdd:PRK11147  104 ISHLVETDpseknlnelaklqeqldhhnlwqLENRINEVLAQLGLD--PDAALSSLSGGWLRKAALGRALVSNPDVLLLD 181


                  ....*..
gi 1054819401 173 EPLGALD 179
Cdd:PRK11147  182 EPTNHLD 188
PTZ00265 PTZ00265
multidrug resistance protein (mdr1); Provisional
 73-222 2.81e-09

multidrug resistance protein (mdr1); Provisional


Pssm-ID: 240339 [Multi-domain]  Cd Length: 1466  Bit Score: 59.27  E-value: 2.81e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054819401   73 DGTISIDGRDVT--GTRAHRRPVNTVFQSYALFpHLTVAENVAFGLRRRREADVEaRVAEGLALVE-LGHLADRRPA--- 146
Cdd:PTZ00265  1276 SGKILLDGVDICdyNLKDLRNLFSIVSQEPMLF-NMSIYENIKFGKEDATREDVK-RACKFAAIDEfIESLPNKYDTnvg 1353

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054819401  147 ----LLSGGQQQRVALARALVNRPALLLLDEPLGALDLKLRRQMQLELKRIQTEVGLTFVHVTHdQEEAMTMADTVAVMN 222
Cdd:PTZ00265  1354 pygkSLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDIKDKADKTIITIAH-RIASIKRSDKIVVFN 1432
PTZ00243 PTZ00243
ABC transporter; Provisional
 37-239 2.98e-09

ABC transporter; Provisional


Pssm-ID: 240327 [Multi-domain]  Cd Length: 1560  Bit Score: 59.02  E-value: 2.98e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054819401   37 DLTLTVPSGSFFALLGPSGCGKTTTLRMVAGLEQPTDGTISIDgRDVTGTRAHRRPVNTVFQSYALFPHLTVAENVAFGL 116
Cdd:PTZ00243   678 DVSVSVPRGKLTVVLGATGSGKSTLLQSLLSQFEISEGRVWAE-RSIAYVPQQAWIMNATVRGNILFFDEEDAARLADAV 756

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054819401  117 R-RRREADVeARVAEGLAlVELGHladrRPALLSGGQQQRVALARALVNRPALLLLDEPLGALDLKLRrqmqlelKRIQT 195
Cdd:PTZ00243   757 RvSQLEADL-AQLGGGLE-TEIGE----KGVNLSGGQKARVSLARAVYANRDVYLLDDPLSALDAHVG-------ERVVE 823

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|
gi 1054819401  196 EV------GLTFVHVTHdQEEAMTMADTVAVMNRGRIEQMGPPADLYEHP 239
Cdd:PTZ00243   824 ECflgalaGKTRVLATH-QVHVVPRADYVVALGDGRVEFSGSSADFMRTS 872
PRK15093 PRK15093
peptide ABC transporter ATP-binding protein SapD;
30-241 3.73e-09

peptide ABC transporter ATP-binding protein SapD;


Pssm-ID: 185049 [Multi-domain]  Cd Length: 330  Bit Score: 57.50  E-value: 3.73e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054819401  30 GAFVAVDDLTLTVPSGSFFALLGPSGCGKTTTLRMVAGLEQP----TDGTISIDGRDVT--GTRAHRR----PVNTVFQS 99
Cdd:PRK15093   18 GWVKAVDRVSMTLTEGEIRGLVGESGSGKSLIAKAICGVTKDnwrvTADRMRFDDIDLLrlSPRERRKlvghNVSMIFQE 97

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054819401 100 yalfPH--LTVAENVA-------------------FGLRRRREADVEARVAeglalvelghLADRR------PALLSGGQ 152
Cdd:PRK15093   98 ----PQscLDPSERVGrqlmqnipgwtykgrwwqrFGWRKRRAIELLHRVG----------IKDHKdamrsfPYELTEGE 163

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054819401 153 QQRVALARALVNRPALLLLDEPLGALDLKLRRQMQLELKRIQTEVGLTFVHVTHDQEEAMTMADTVAVMNRGRIEQMGPP 232
Cdd:PRK15093  164 CQKVMIAIALANQPRLLIADEPTNAMEPTTQAQIFRLLTRLNQNNNTTILLISHDLQMLSQWADKINVLYCGQTVETAPS 243

                         250
                  ....*....|..
gi 1054819401 233 ADLY---EHPRT 241
Cdd:PRK15093  244 KELVttpHHPYT 255
PTZ00243 PTZ00243
ABC transporter; Provisional
 50-251 4.27e-09

ABC transporter; Provisional


Pssm-ID: 240327 [Multi-domain]  Cd Length: 1560  Bit Score: 58.64  E-value: 4.27e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054819401   50 LLGPSGCGKTTTL----RMVagleQPTDGTISIDGRDVT--GTRAHRRPVNTVFQSYALFPHlTVAENVafglrrrrEAD 123
Cdd:PTZ00243  1341 IVGRTGSGKSTLLltfmRMV----EVCGGEIRVNGREIGayGLRELRRQFSMIPQDPVLFDG-TVRQNV--------DPF 1407

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054819401  124 VEARVAEGLALVELGHLADRRPA--------LLSGG------QQQRVALARALVNR-PALLLLDEPLGALDLKLRRQMQL 188
Cdd:PTZ00243  1408 LEASSAEVWAALELVGLRERVASesegidsrVLEGGsnysvgQRQLMCMARALLKKgSGFILMDEATANIDPALDRQIQA 1487

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1054819401  189 E-LKRIQTEVGLTFVHVTHdqeeamTMA--DTVAVMNRGRIEQMGPPADLYEHPRTTF--VANFLGRS 251
Cdd:PTZ00243  1488 TvMSAFSAYTVITIAHRLH------TVAqyDKIIVMDHGAVAEMGSPRELVMNRQSIFhsMVEALGRS 1549
PRK10938 PRK10938
putative molybdenum transport ATP-binding protein ModF; Provisional
 121-235 7.24e-09

putative molybdenum transport ATP-binding protein ModF; Provisional


Pssm-ID: 182852 [Multi-domain]  Cd Length: 490  Bit Score: 57.33  E-value: 7.24e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054819401 121 EADVEARVAEGLALVELGHLADRRPALLSGGQQQRVALARALVNRPALLLLDEPLGALDLKLRRQMQLELKRIQTEvGLT 200
Cdd:PRK10938  109 EVKDPARCEQLAQQFGITALLDRRFKYLSTGETRKTLLCQALMSEPDLLILDEPFDGLDVASRQQLAELLASLHQS-GIT 187

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 1054819401 201 FVHVTHDQEEAMTMADTVAVMNRGRIEQMGPPADL 235
Cdd:PRK10938  188 LVLVLNRFDEIPDFVQFAGVLADCTLAETGEREEI 222
3a01205 TIGR00956
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
 42-179 1.01e-08

Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]


Pssm-ID: 273362 [Multi-domain]  Cd Length: 1394  Bit Score: 57.43  E-value: 1.01e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054819401   42 VPSGSFFALLGPSGCGKTTTLRMVAglEQPTDGTISIDGRDVTGtrahrRPVNTVFQSYALF--------PHLTVAENVA 113
Cdd:TIGR00956  786 VKPGTLTALMGASGAGKTTLLNVLA--ERVTTGVITGGDRLVNG-----RPLDSSFQRSIGYvqqqdlhlPTSTVRESLR 858

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1054819401  114 FGLRRRREADVEAR-----VAEGLALVELGHLADrrpAL-------LSGGQQQRVALARALVNRPALLL-LDEPLGALD 179
Cdd:TIGR00956  859 FSAYLRQPKSVSKSekmeyVEEVIKLLEMESYAD---AVvgvpgegLNVEQRKRLTIGVELVAKPKLLLfLDEPTSGLD 934
PLN03232 PLN03232
ABC transporter C family member; Provisional
 38-243 1.14e-08

ABC transporter C family member; Provisional


Pssm-ID: 215640 [Multi-domain]  Cd Length: 1495  Bit Score: 57.29  E-value: 1.14e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054819401   38 LTLTVPSGSFFALLGPSGCGKTTTLRMVAGLEQPTDGTISIDGRDVT--GTRAHRRPVNTVFQSYALFphltvAENVAFG 115
Cdd:PLN03232  1255 LSFFVSPSEKVGVVGRTGAGKSSMLNALFRIVELEKGRIMIDDCDVAkfGLTDLRRVLSIIPQSPVLF-----SGTVRFN 1329

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054819401  116 LRRRREADvEARVAEGLALVELGHLADRRPALL-----------SGGQQQRVALARALVNRPALLLLDEPLGALDLKLRR 184
Cdd:PLN03232  1330 IDPFSEHN-DADLWEALERAHIKDVIDRNPFGLdaevseggenfSVGQRQLLSLARALLRRSKILVLDEATASVDVRTDS 1408

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 1054819401  185 QMQlelKRIQTEVGLTFVHVTHDQEEAMTMADTVAVMNRGRIEQMGPPADLYEHPRTTF 243
Cdd:PLN03232  1409 LIQ---RTIREEFKSCTMLVIAHRLNTIIDCDKILVLSSGQVLEYDSPQELLSRDTSAF 1464
PRK13546 PRK13546
teichoic acids export ABC transporter ATP-binding subunit TagH;
32-251 1.58e-08

teichoic acids export ABC transporter ATP-binding subunit TagH;


Pssm-ID: 184131 [Multi-domain]  Cd Length: 264  Bit Score: 55.21  E-value: 1.58e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054819401  32 FVAVDDLTLTVPSGSFFALLGPSGCGKTTTLRMVAGLEQPTDGTISIDGRdvtgtrahrrpVNTVFQSYALFPHLTVAEN 111
Cdd:PRK13546   37 FFALDDISLKAYEGDVIGLVGINGSGKSTLSNIIGGSLSPTVGKVDRNGE-----------VSVIAISAGLSGQLTGIEN 105

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054819401 112 VAF-----GLRRRreaDVEARVAEGLALVELGHLADRRPALLSGGQQQRVALARALVNRPALLLLDEPLGALDLKLrrqM 186
Cdd:PRK13546  106 IEFkmlcmGFKRK---EIKAMTPKIIEFSELGEFIYQPVKKYSSGMRAKLGFSINITVNPDILVIDEALSVGDQTF---A 179

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1054819401 187 QLELKRIQ--TEVGLTFVHVTHDQEEAMTMADTVAVMNRGRIEQMGPPADLYEHpRTTFVANFLGRS 251
Cdd:PRK13546  180 QKCLDKIYefKEQNKTIFFVSHNLGQVRQFCTKIAWIEGGKLKDYGELDDVLPK-YEAFLNDFKKKS 245
PRK10636 PRK10636
putative ABC transporter ATP-binding protein; Provisional
 20-227 2.30e-08

putative ABC transporter ATP-binding protein; Provisional


Pssm-ID: 236729 [Multi-domain]  Cd Length: 638  Bit Score: 55.95  E-value: 2.30e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054819401  20 LELAAVTKRFGAFVAVDDLTLTVPSGSFFALLGPSGCGKTTTLRMVAGLEQPTDGTISIDGRDVTGTRAHR-----RPVN 94
Cdd:PRK10636  313 LKMEKVSAGYGDRIILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELAPVSGEIGLAKGIKLGYFAQHqleflRADE 392

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054819401  95 TVFQsyalfpHLT-VAENVA----------FGLRRRREADVEARvaeglalvelghladrrpalLSGGQQQRVALARALV 163
Cdd:PRK10636  393 SPLQ------HLArLAPQELeqklrdylggFGFQGDKVTEETRR--------------------FSGGEKARLVLALIVW 446

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1054819401 164 NRPALLLLDEPLGALDLKLRRQMQLELkrIQTEVGLtfVHVTHDQEEAMTMADTVAVMNRGRIE 227
Cdd:PRK10636  447 QRPNLLLLDEPTNHLDLDMRQALTEAL--IDFEGAL--VVVSHDRHLLRSTTDDLYLVHDGKVE 506
PRK15064 PRK15064
ABC transporter ATP-binding protein; Provisional
 20-209 2.44e-08

ABC transporter ATP-binding protein; Provisional


Pssm-ID: 237894 [Multi-domain]  Cd Length: 530  Bit Score: 55.67  E-value: 2.44e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054819401  20 LELAAVTKRFGAFVAVDDLTLTVPSGSFFALLGPSGCGKTTTLRMVAGLEQPTDGTISIdgrdvtgtrahrrpvntvfqs 99
Cdd:PRK15064  320 LEVENLTKGFDNGPLFKNLNLLLEAGERLAIIGENGVGKTTLLRTLVGELEPDSGTVKW--------------------- 378

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054819401 100 yalfphltvAENVAFGLRRRreaDVEARVAEGLALVE------------------LGHL------ADRRPALLSGGQQQR 155
Cdd:PRK15064  379 ---------SENANIGYYAQ---DHAYDFENDLTLFDwmsqwrqegddeqavrgtLGRLlfsqddIKKSVKVLSGGEKGR 446

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1054819401 156 VALARALVNRPALLLLDEPLGALDLKLRRQMQLELKRIQTevglTFVHVTHDQE 209
Cdd:PRK15064  447 MLFGKLMMQKPNVLVMDEPTNHMDMESIESLNMALEKYEG----TLIFVSHDRE 496
ABC_RNaseL_inhibitor cd03222
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ...
 24-220 2.51e-08

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: 53.34  E-value: 2.51e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054819401  24 AVTKRFGAFVAVDDLTlTVPSGSFFALLGPSGCGKTTTLRMVAGLEQPTDGTISIDGrdvtgtrahrrpvntvfqsyalf 103
Cdd:cd03222     5 DCVKRYGVFFLLVELG-VVKEGEVIGIVGPNGTGKTTAVKILAGQLIPNGDNDEWDG----------------------- 60

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054819401 104 phltvaenvafglrrrreadveARVAEGLALVELghladrrpallSGGQQQRVALARALVNRPALLLLDEPLGALDLKLR 183
Cdd:cd03222    61 ----------------------ITPVYKPQYIDL-----------SGGELQRVAIAAALLRNATFYLFDEPSAYLDIEQR 107

                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 1054819401 184 RQMQLELKRIQTEVGLTFVHVTHDQEEAMTMADTVAV 220
Cdd:cd03222   108 LNAARAIRRLSEEGKKTALVVEHDLAVLDYLSDRIHV 144
ABC_RNaseL_inhibitor_domain1 cd03236
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ...
 40-207 2.72e-08

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: 54.29  E-value: 2.72e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054819401  40 LTVP-SGSFFALLGPSGCGKTTTLRMVAGLEQPTDGTIS--IDGRDVT----GT--------------RAHRRPvntvfQ 98
Cdd:cd03236    20 LPVPrEGQVLGLVGPNGIGKSTALKILAGKLKPNLGKFDdpPDWDEILdefrGSelqnyftkllegdvKVIVKP-----Q 94

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054819401  99 SYALFPHlTVAENVAFGLRRRREADVEARVAEGLalvELGHLADRRPALLSGGQQQRVALARALVNRPALLLLDEPLGAL 178
Cdd:cd03236    95 YVDLIPK-AVKGKVGELLKKKDERGKLDELVDQL---ELRHVLDRNIDQLSGGELQRVAIAAALARDADFYFFDEPSSYL 170

                         170       180
                  ....*....|....*....|....*....
gi 1054819401 179 DLKLRRQMQLELKRIQTEVGLTFVhVTHD 207
Cdd:cd03236   171 DIKQRLNAARLIRELAEDDNYVLV-VEHD 198
3a01205 TIGR00956
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
 50-231 3.85e-08

Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]


Pssm-ID: 273362 [Multi-domain]  Cd Length: 1394  Bit Score: 55.50  E-value: 3.85e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054819401   50 LLGPSGCGKTTTLRMVAG-LEQ---PTDGTISIDGRDVTGTRAHRR-PVNTVFQSYALFPHLTVAENVAFGLRRR----- 119
Cdd:TIGR00956   92 VLGRPGSGCSTLLKTIASnTDGfhiGVEGVITYDGITPEEIKKHYRgDVVYNAETDVHFPHLTVGETLDFAARCKtpqnr 171

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054819401  120 -----READVEARVAEGLALVELGHLADRRPAL-----LSGGQQQRVALARALVNRPALLLLDEPLGALDLKLRRQMQLE 189
Cdd:TIGR00956  172 pdgvsREEYAKHIADVYMATYGLSHTRNTKVGNdfvrgVSGGERKRVSIAEASLGGAKIQCWDNATRGLDSATALEFIRA 251

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|...
gi 1054819401  190 LKRIQTEVGLT-FVHVTHDQEEAMTMADTVAVMNRGRIEQMGP 231
Cdd:TIGR00956  252 LKTSANILDTTpLVAIYQCSQDAYELFDKVIVLYEGYQIYFGP 294
PRK10938 PRK10938
putative molybdenum transport ATP-binding protein ModF; Provisional
 36-211 6.85e-08

putative molybdenum transport ATP-binding protein ModF; Provisional


Pssm-ID: 182852 [Multi-domain]  Cd Length: 490  Bit Score: 54.25  E-value: 6.85e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054819401  36 DDLTLTVPSGSFFALLGPSGCGKTTTLRMVAGlEQPTDGTisidgRDVT--GTRahRRPVNTVFQ--------SYALfpH 105
Cdd:PRK10938  277 HNLSWQVNPGEHWQIVGPNGAGKSTLLSLITG-DHPQGYS-----NDLTlfGRR--RGSGETIWDikkhigyvSSSL--H 346

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054819401 106 L-----TVAENV-------AFGL------RRRREADvearvaEGLALVEL-GHLADRRPALLSGGQQQRVALARALVNRP 166
Cdd:PRK10938  347 LdyrvsTSVRNVilsgffdSIGIyqavsdRQQKLAQ------QWLDILGIdKRTADAPFHSLSWGQQRLALIVRALVKHP 420

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 1054819401 167 ALLLLDEPLGALDlKLRRQMQLELKRI---QTEVGLTFvhVTHDQEEA 211
Cdd:PRK10938  421 TLLILDEPLQGLD-PLNRQLVRRFVDVlisEGETQLLF--VSHHAEDA 465
PLN03140 PLN03140
ABC transporter G family member; Provisional
 37-224 8.11e-08

ABC transporter G family member; Provisional


Pssm-ID: 215599 [Multi-domain]  Cd Length: 1470  Bit Score: 54.47  E-value: 8.11e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054819401   37 DLTLTVPSGSFFALLGPSGCGKTTTLRMVAGleQPTDGTISIDGRdVTG----TRAHRRPVNTVFQSYALFPHLTVAENV 112
Cdd:PLN03140   898 EVTGAFRPGVLTALMGVSGAGKTTLMDVLAG--RKTGGYIEGDIR-ISGfpkkQETFARISGYCEQNDIHSPQVTVRESL 974

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054819401  113 AFG--LRRRREADVEAR---VAEGLALVELGHLADRRPAL-----LSGGQQQRVALARALVNRPALLLLDEPLGALDlkl 182
Cdd:PLN03140   975 IYSafLRLPKEVSKEEKmmfVDEVMELVELDNLKDAIVGLpgvtgLSTEQRKRLTIAVELVANPSIIFMDEPTSGLD--- 1051

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*...
gi 1054819401  183 RRQMQLELKRIQTEV--GLTFVHVTH----DQEEAMtmaDTVAVMNRG 224
Cdd:PLN03140  1052 ARAAAIVMRTVRNTVdtGRTVVCTIHqpsiDIFEAF---DELLLMKRG 1096
PRK13549 PRK13549
xylose transporter ATP-binding subunit; Provisional
 35-226 9.93e-08

xylose transporter ATP-binding subunit; Provisional


Pssm-ID: 184134 [Multi-domain]  Cd Length: 506  Bit Score: 53.78  E-value: 9.93e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054819401  35 VDDLTLTVPSGSFFALLGPSGCGKTTTLRMVAGLEQ-PTDGTISIDGRDVTgtraHRRPVNTVFQSYALFPH-------- 105
Cdd:PRK13549  278 VDDVSFSLRRGEILGIAGLVGAGRTELVQCLFGAYPgRWEGEIFIDGKPVK----IRNPQQAIAQGIAMVPEdrkrdgiv 353

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054819401 106 --LTVAENVA------FGLRRRREADVEARVAEglalVELGHLADRRP------ALLSGGQQQRVALARALVNRPALLLL 171
Cdd:PRK13549  354 pvMGVGKNITlaaldrFTGGSRIDDAAELKTIL----ESIQRLKVKTAspelaiARLSGGNQQKAVLAKCLLLNPKILIL 429

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1054819401 172 DEPLGALDL-------KLRRQMqlelkriqTEVGLTFVHVTHDQEEAMTMADTVAVMNRGRI 226
Cdd:PRK13549  430 DEPTRGIDVgakyeiyKLINQL--------VQQGVAIIVISSELPEVLGLSDRVLVMHEGKL 483
SapD COG4170
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms];
30-239 2.29e-07

ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms];


Pssm-ID: 443330 [Multi-domain]  Cd Length: 331  Bit Score: 52.22  E-value: 2.29e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054819401  30 GAFVAVDDLTLTVPSGSFFALLGPSGCGKTTTLRMVAGLeQPTDGTISID-----GRDVTGTRAH------RRPVNTVFQ 98
Cdd:COG4170    18 GRVKAVDRVSLTLNEGEIRGLVGESGSGKSLIAKAICGI-TKDNWHVTADrfrwnGIDLLKLSPRerrkiiGREIAMIFQ 96

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054819401  99 --SYALFPHLTVAENVA---------------FGLRRRReadvearvaeglaLVELGH---LADRR------PALLSGGQ 152
Cdd:COG4170    97 epSSCLDPSAKIGDQLIeaipswtfkgkwwqrFKWRKKR-------------AIELLHrvgIKDHKdimnsyPHELTEGE 163

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054819401 153 QQRVALARALVNRPALLLLDEPLGALDLKLRRQMQLELKRIQTEVGLTFVHVTHDQEEAMTMADTVAVMNRGRIEQMGPP 232
Cdd:COG4170   164 CQKVMIAMAIANQPRLLIADEPTNAMESTTQAQIFRLLARLNQLQGTSILLISHDLESISQWADTITVLYCGQTVESGPT 243


                  ....*..
gi 1054819401 233 ADLYEHP 239
Cdd:COG4170   244 EQILKSP 250
PLN03130 PLN03130
ABC transporter C family member; Provisional
 50-243 2.50e-07

ABC transporter C family member; Provisional


Pssm-ID: 215595 [Multi-domain]  Cd Length: 1622  Bit Score: 52.82  E-value: 2.50e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054819401   50 LLGPSGCGKTTTLRMVAGLEQPTDGTISIDGRDVT--GTRAHRRPVNTVFQSYALFphltvAENVAFGLRRRREADvEAR 127
Cdd:PLN03130  1270 IVGRTGAGKSSMLNALFRIVELERGRILIDGCDISkfGLMDLRKVLGIIPQAPVLF-----SGTVRFNLDPFNEHN-DAD 1343

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054819401  128 VAEGLalvELGHLAD--RRPAL------------LSGGQQQRVALARALVNRPALLLLDEPLGALDLKLRRQMQlelKRI 193
Cdd:PLN03130  1344 LWESL---ERAHLKDviRRNSLgldaevseagenFSVGQRQLLSLARALLRRSKILVLDEATAAVDVRTDALIQ---KTI 1417

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|.
gi 1054819401  194 QTEV-GLTFVHVTHdQEEAMTMADTVAVMNRGRIEQMGPPADLYEHPRTTF 243
Cdd:PLN03130  1418 REEFkSCTMLIIAH-RLNTIIDCDRILVLDAGRVVEFDTPENLLSNEGSAF 1467
ABCC_SUR2 cd03288
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The ...
 45-243 5.20e-07

ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The sulfonylurea receptor SUR is an ATP binding cassette (ABC) protein of the ABCC/MRP family. Unlike other ABC proteins, it has no intrinsic transport function, neither active nor passive, but associates with the potassium channel proteins Kir6.1 or Kir6.2 to form the ATP-sensitive potassium (K(ATP)) channel. Within the channel complex, SUR serves as a regulatory subunit that fine-tunes the gating of Kir6.x in response to alterations in cellular metabolism. It constitutes a major pharmaceutical target as it binds numerous drugs, K(ATP) channel openers and blockers, capable of up- or down-regulating channel activity.


Pssm-ID: 213255 [Multi-domain]  Cd Length: 257  Bit Score: 50.68  E-value: 5.20e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054819401  45 GSFFALLGPSGCGKTTT----LRMVAGLeqptDGTISIDGRDVTGTRAH--RRPVNTVFQSYALFphltvAENVAFGLRR 118
Cdd:cd03288    47 GQKVGICGRTGSGKSSLslafFRMVDIF----DGKIVIDGIDISKLPLHtlRSRLSIILQDPILF-----SGSIRFNLDP 117

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054819401 119 RREAdVEARVAEGLALVELGHLADRRPALL-----------SGGQQQRVALARALVNRPALLLLDEPLGALDLKLRRQMQ 187
Cdd:cd03288   118 ECKC-TDDRLWEALEIAQLKNMVKSLPGGLdavvteggenfSVGQRQLFCLARAFVRKSSILIMDEATASIDMATENILQ 196

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1054819401 188 lelKRIQTEVG-LTFVHVTHDQEEAMTmADTVAVMNRGRIEQMGPPADLYEHPRTTF 243
Cdd:cd03288   197 ---KVVMTAFAdRTVVTIAHRVSTILD-ADLVLVLSRGILVECDTPENLLAQEDGVF 249
TOBE_2 pfam08402
TOBE domain; The TOBE domain (Transport-associated OB) always occurs as a dimer as the ...
 292-368 6.26e-07

TOBE domain; The TOBE domain (Transport-associated OB) always occurs as a dimer as the C-terminal strand of each domain is supplied by the partner. Probably involved in the recognition of small ligands such as molybdenum and sulphate. Found in ABC transporters immediately after the ATPase domain. In this family a strong RPE motif is found at the presumed N-terminus of the domain.


Pssm-ID: 462465 [Multi-domain]  Cd Length: 73  Bit Score: 46.46  E-value: 6.26e-07
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1054819401 292 VGARPEKVRLLADGEepapdenvVGPGTVTDVSFTGVSTQYEVRVPGLGVFGVFAQNlSGRAGAALGDQVRLAWAVD 368
Cdd:pfam08402   1 LAIRPEKIRLAAAAN--------GLSGTVTDVEYLGDHTRYHVELAGGEELVVRVPN-AHARPPAPGDRVGLGWDPE 68
Rli1 COG1245
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ...
 40-221 1.84e-06

Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ribosomal structure and biogenesis];


Pssm-ID: 440858 [Multi-domain]  Cd Length: 592  Bit Score: 49.78  E-value: 1.84e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054819401  40 LTVP-SGSFFALLGPSGCGKTTTLRMVAGLEQPTDGTISidgRDVTGTRAHRRpvntvFQSYALFPHLT-VAEN------ 111
Cdd:COG1245    93 LPVPkKGKVTGILGPNGIGKSTALKILSGELKPNLGDYD---EEPSWDEVLKR-----FRGTELQDYFKkLANGeikvah 164

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054819401 112 ----------VAFG-----LRRRREADVEARVAEGLalvELGHLADRRPALLSGGQQQRVALARALVNRPALLLLDEPLG 176
Cdd:COG1245   165 kpqyvdlipkVFKGtvrelLEKVDERGKLDELAEKL---GLENILDRDISELSGGELQRVAIAAALLRDADFYFFDEPSS 241

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 1054819401 177 ALDLKLRRQMQLELKRIqTEVGLTFVHVTHDQeeAM--TMADTVAVM 221
Cdd:COG1245   242 YLDIYQRLNVARLIREL-AEEGKYVLVVEHDL--AIldYLADYVHIL 285
ABC_UvrA cd03238
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ...
 37-236 7.10e-06

ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins, and UvrB having one ATP binding site that is structurally related to that of helicases.


Pssm-ID: 213205 [Multi-domain]  Cd Length: 176  Bit Score: 46.16  E-value: 7.10e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054819401  37 DLTLTVPSGSFFALLGPSGCGKTTTlrmvagleqptdgtisidgrdvtgtrahrrpVNTVFQsyalfphlTVAENVAFGL 116
Cdd:cd03238    13 NLDVSIPLNVLVVVTGVSGSGKSTL-------------------------------VNEGLY--------ASGKARLISF 53

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054819401 117 RRRREADVEARVAEGLALVE--LGHLA-DRRPALLSGGQQQRVALARALVNRP--ALLLLDEPLGALDLKLRRQMQLELK 191
Cdd:cd03238    54 LPKFSRNKLIFIDQLQFLIDvgLGYLTlGQKLSTLSGGELQRVKLASELFSEPpgTLFILDEPSTGLHQQDINQLLEVIK 133

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 1054819401 192 RIQTEvGLTFVHVTHDqEEAMTMADtvavmnrgRIEQMGPPADLY 236
Cdd:cd03238   134 GLIDL-GNTVILIEHN-LDVLSSAD--------WIIDFGPGSGKS 168
PLN03073 PLN03073
ABC transporter F family; Provisional
 125-209 1.02e-05

ABC transporter F family; Provisional


Pssm-ID: 215558 [Multi-domain]  Cd Length: 718  Bit Score: 47.55  E-value: 1.02e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054819401 125 EARVAEGLA-LVELGHLADRRPALLSGGQQQRVALARALVNRPALLLLDEPLGALDLklrrQMQLELKRIQTEVGLTFVH 203
Cdd:PLN03073  321 EARAASILAgLSFTPEMQVKATKTFSGGWRMRIALARALFIEPDLLLLDEPTNHLDL----HAVLWLETYLLKWPKTFIV 396


                  ....*.
gi 1054819401 204 VTHDQE 209
Cdd:PLN03073  397 VSHARE 402
sufC PRK09580
cysteine desulfurase ATPase component; Reviewed
 38-230 1.24e-05

cysteine desulfurase ATPase component; Reviewed


Pssm-ID: 181965 [Multi-domain]  Cd Length: 248  Bit Score: 46.32  E-value: 1.24e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054819401  38 LTLTVPSGSFFALLGPSGCGKTTTLRMVAGLE--QPTDGTISIDGRDVTGTRAHRRPVNTVFQSYAlFPHLTVAENVAFG 115
Cdd:PRK09580   20 LNLEVRPGEVHAIMGPNGSGKSTLSATLAGREdyEVTGGTVEFKGKDLLELSPEDRAGEGIFMAFQ-YPVEIPGVSNQFF 98

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054819401 116 LRRRREADVEARVAEGLALVELGHLADRRPALL---------------SGGQQQRVALARALVNRPALLLLDEPLGALDL 180
Cdd:PRK09580   99 LQTALNAVRSYRGQEPLDRFDFQDLMEEKIALLkmpedlltrsvnvgfSGGEKKRNDILQMAVLEPELCILDESDSGLDI 178

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1054819401 181 KLRRQMQLELKRIQTEvGLTFVHVTHDQE-EAMTMADTVAVMNRGRIEQMG 230
Cdd:PRK09580  179 DALKIVADGVNSLRDG-KRSFIIVTHYQRiLDYIKPDYVHVLYQGRIVKSG 228
PRK10982 PRK10982
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
 34-226 1.29e-05

galactose/methyl galaxtoside transporter ATP-binding protein; Provisional


Pssm-ID: 182880 [Multi-domain]  Cd Length: 491  Bit Score: 47.03  E-value: 1.29e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054819401  34 AVDDLTLTVPSGSFFALLGPSGCGKTTTLRMVAGLEQPTDGTISIDGRDVTGTRAHRrPVNTVF-------QSYALFPHL 106
Cdd:PRK10982  263 SIRDVSFDLHKGEILGIAGLVGAKRTDIVETLFGIREKSAGTITLHGKKINNHNANE-AINHGFalvteerRSTGIYAYL 341

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054819401 107 TVAENV----------AFGL--RRRREADVEArVAEGLALVELGHLAdrRPALLSGGQQQRVALARALVNRPALLLLDEP 174
Cdd:PRK10982  342 DIGFNSlisnirnyknKVGLldNSRMKSDTQW-VIDSMRVKTPGHRT--QIGSLSGGNQQKVIIGRWLLTQPEILMLDEP 418

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1054819401 175 LGALDLKLRRQM-QLELKRIQTEVGLtfVHVTHDQEEAMTMADTVAVMNRGRI 226
Cdd:PRK10982  419 TRGIDVGAKFEIyQLIAELAKKDKGI--IIISSEMPELLGITDRILVMSNGLV 469
PRK10636 PRK10636
putative ABC transporter ATP-binding protein; Provisional
 28-209 1.34e-05

putative ABC transporter ATP-binding protein; Provisional


Pssm-ID: 236729 [Multi-domain]  Cd Length: 638  Bit Score: 47.09  E-value: 1.34e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054819401  28 RFGAFVAVDDLTLTVPSGSFFALLGPSGCGKTTTLRMVagleqptDGTISIDGRDVTgtrahrrpvntVFQSYAL----- 102
Cdd:PRK10636   10 RRGVRVLLDNATATINPGQKVGLVGKNGCGKSTLLALL-------KNEISADGGSYT-----------FPGNWQLawvnq 71

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054819401 103 -FPHLTVA--ENVAFGLRRRREADVEARVA----EGLALVELGHLAD---------RRPALL-----------------S 149
Cdd:PRK10636   72 eTPALPQPalEYVIDGDREYRQLEAQLHDAnernDGHAIATIHGKLDaidawtirsRAASLLhglgfsneqlerpvsdfS 151

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054819401 150 GGQQQRVALARALVNRPALLLLDEPLGALDLKLRRQMQLELKRIQTevglTFVHVTHDQE 209
Cdd:PRK10636  152 GGWRMRLNLAQALICRSDLLLLDEPTNHLDLDAVIWLEKWLKSYQG----TLILISHDRD 207
ABC_Rad50 cd03240
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ...
 47-218 2.42e-05

ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ATP-binding cassette of ABC transporters, but are not associated with membrane-spanning domains. The conserved ATP-binding motifs common to Rad50 and the ABC transporter family include the Walker A and Walker B motifs, the Q loop, a histidine residue in the switch region, a D-loop, and a conserved LSGG sequence. This conserved sequence, LSGG, is the most specific and characteristic motif of this family and is thus known as the ABC signature sequence.


Pssm-ID: 213207 [Multi-domain]  Cd Length: 204  Bit Score: 44.91  E-value: 2.42e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054819401  47 FFALLGPSGCGKTTT---LRMVAGLEQPTDGTISIDGRDVTGTRAHRRPVNTVFQS-----YALFPHLTVAENVAFglrr 118
Cdd:cd03240    24 LTLIVGQNGAGKTTIieaLKYALTGELPPNSKGGAHDPKLIREGEVRAQVKLAFENangkkYTITRSLAILENVIF---- 99

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054819401 119 rreadvearVAEGlalvELGHLADRRPALLSGGQQQ------RVALARALVNRPALLLLDEPLGALDlKLRRQMQLE--L 190
Cdd:cd03240   100 ---------CHQG----ESNWPLLDMRGRCSGGEKVlasliiRLALAETFGSNCGILALDEPTTNLD-EENIEESLAeiI 165

                         170       180
                  ....*....|....*....|....*...
gi 1054819401 191 KRIQTEVGLTFVHVTHDqEEAMTMADTV 218
Cdd:cd03240   166 EERKSQKNFQLIVITHD-EELVDAADHI 192
tagH PRK13545
teichoic acids export protein ATP-binding subunit; Provisional
 34-179 2.91e-05

teichoic acids export protein ATP-binding subunit; Provisional


Pssm-ID: 184130 [Multi-domain]  Cd Length: 549  Bit Score: 46.04  E-value: 2.91e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054819401  34 AVDDLTLTVPSGSFFALLGPSGCGKTTTLRMVAGLEQPTDGTISIDGRdvtgtrahrrpVNTVFQSYALFPHLTVAENVA 113
Cdd:PRK13545   39 ALNNISFEVPEGEIVGIIGLNGSGKSTLSNLIAGVTMPNKGTVDIKGS-----------AALIAISSGLNGQLTGIENIE 107

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1054819401 114 F-----GLRRRREADVEARVAEglaLVELGHLADRRPALLSGGQQQRVALARALVNRPALLLLDEPLGALD 179
Cdd:PRK13545  108 LkglmmGLTKEKIKEIIPEIIE---FADIGKFIYQPVKTYSSGMKSRLGFAISVHINPDILVIDEALSVGD 175
PRK13409 PRK13409
ribosome biogenesis/translation initiation ATPase RLI;
40-183 4.25e-05

ribosome biogenesis/translation initiation ATPase RLI;


Pssm-ID: 184037 [Multi-domain]  Cd Length: 590  Bit Score: 45.57  E-value: 4.25e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054819401  40 LTVPS-GSFFALLGPSGCGKTTTLRMVAGLEQP----TDGTISIDgrDVTgtRAHRRpvnTVFQSYalFPHL-----TVA 109
Cdd:PRK13409   93 LPIPKeGKVTGILGPNGIGKTTAVKILSGELIPnlgdYEEEPSWD--EVL--KRFRG---TELQNY--FKKLyngeiKVV 163

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054819401 110 E--------------NVAFGLRRRREADVEARVAEGLalvELGHLADRRPALLSGGQQQRVALARALVNRPALLLLDEPL 175
Cdd:PRK13409  164 HkpqyvdlipkvfkgKVRELLKKVDERGKLDEVVERL---GLENILDRDISELSGGELQRVAIAAALLRDADFYFFDEPT 240


                  ....*...
gi 1054819401 176 GALDLKLR 183
Cdd:PRK13409  241 SYLDIRQR 248
ABC_UvrA_I cd03270
ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair ...
 37-218 5.88e-05

ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins, and UvrB having one ATP binding site that is structurally related to that of helicases.


Pssm-ID: 213237 [Multi-domain]  Cd Length: 226  Bit Score: 43.79  E-value: 5.88e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054819401  37 DLTLTVPSGSFFALLGPSGCGKTT----------------TLRMVA-----GLEQP----TDG---TISIDGRdvTGTRA 88
Cdd:cd03270    13 NVDVDIPRNKLVVITGVSGSGKSSlafdtiyaegqrryveSLSAYArqflgQMDKPdvdsIEGlspAIAIDQK--TTSRN 90

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054819401  89 HRRPVNTVFQSYALFPHLTVAEnvafGLRRRREADVEarvaeglalVELGHLA-DRRPALLSGGQQQRVALARALVNR-- 165
Cdd:cd03270    91 PRSTVGTVTEIYDYLRLLFARV----GIRERLGFLVD---------VGLGYLTlSRSAPTLSGGEAQRIRLATQIGSGlt 157

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1054819401 166 PALLLLDEPLGALDLKLRRQMQLELKRIQtEVGLTFVHVTHDqEEAMTMADTV 218
Cdd:cd03270   158 GVLYVLDEPSIGLHPRDNDRLIETLKRLR-DLGNTVLVVEHD-EDTIRAADHV 208
uvra TIGR00630
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ...
 135-316 6.59e-05

excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of proteins of which all members for which functions are known except the UvrA proteins are involved in the transport of material through membranes. UvrA orthologs are involved in the recognition of DNA damage as a step in nucleotide excision repair. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]


Pssm-ID: 273184 [Multi-domain]  Cd Length: 925  Bit Score: 45.00  E-value: 6.59e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054819401 135 VELGHLA-DRRPALLSGGQQQRVALAR----ALVNrpALLLLDEPlgALDLKLRRQMQL--ELKRIQtEVGLTFVHVTHD 207
Cdd:TIGR00630 475 VGLDYLSlSRAAGTLSGGEAQRIRLATqigsGLTG--VLYVLDEP--SIGLHQRDNRRLinTLKRLR-DLGNTLIVVEHD 549

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054819401 208 qEEAMTMADTV------AVMNRGRIEQMGPPADLYEHPRTTFVANFLGRSNL-VPGtvvERLDGDLLGVDVGGAR----- 275
Cdd:TIGR00630 550 -EDTIRAADYVidigpgAGEHGGEVVASGTPEEILANPDSLTGQYLSGRKKIeVPA---ERRPGNGKFLTLKGARennlk 625

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1054819401 276 ---VRVPASRAVRDTG-----------DVLVGARPEkvRLLADGEEPAPDENVVG 316
Cdd:TIGR00630 626 nitVSIPLGLFTCITGvsgsgkstlinDTLYPALAN--RLNGAKTVPGRYTSIEG 678
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
148-218 2.30e-03

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 40.05  E-value: 2.30e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054819401 148 LSGGQqqRVALARA--------LVNRPALLLLDEPLGALDLKLRRQ----MQLELKRI-QTEVgltfvhVTHDqEEAMTM 214
Cdd:PRK03918  789 LSGGE--RIALGLAfrlalslyLAGNIPLLILDEPTPFLDEERRRKlvdiMERYLRKIpQVII------VSHD-EELKDA 859


                  ....
gi 1054819401 215 ADTV 218
Cdd:PRK03918  860 ADYV 863
ABC_Class2 cd03227
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ...
 36-221 2.49e-03

ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems involved in cellular processes other than transport. These families are characterized by the fact that the ABC subunit is made up of duplicated, fused ABC modules (ABC2). No known transmembrane proteins or domains are associated with these proteins.


Pssm-ID: 213194 [Multi-domain]  Cd Length: 162  Bit Score: 38.49  E-value: 2.49e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054819401  36 DDLTLTVPSGSFFALLGPSGCGKTTTLRMVAgleqptdgtisidgrdvtgtrahrrpvntvfqsYALFPHLTVAENVAFG 115
Cdd:cd03227    12 VPNDVTFGEGSLTIITGPNGSGKSTILDAIG---------------------------------LALGGAQSATRRRSGV 58

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054819401 116 LRRRREADVEARvaegLALVELGhladrrpalLSGGQQQRVALARAL----VNRPALLLLDEPLGALDLKlRRQMQLELK 191
Cdd:cd03227    59 KAGCIVAAVSAE----LIFTRLQ---------LSGGEKELSALALILalasLKPRPLYILDEIDRGLDPR-DGQALAEAI 124

                         170       180       190
                  ....*....|....*....|....*....|
gi 1054819401 192 RIQTEVGLTFVHVTHDqEEAMTMADTVAVM 221
Cdd:cd03227   125 LEHLVKGAQVIVITHL-PELAELADKLIHI 153
GguA NF040905
sugar ABC transporter ATP-binding protein;
148-174 3.44e-03

sugar ABC transporter ATP-binding protein;


Pssm-ID: 468840 [Multi-domain]  Cd Length: 500  Bit Score: 39.39  E-value: 3.44e-03
                          10        20
                  ....*....|....*....|....*..
gi 1054819401 148 LSGGQQQRVALARALVNRPALLLLDEP 174
Cdd:NF040905  405 LSGGNQQKVVLSKWLFTDPDVLILDEP 431
uvra TIGR00630
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ...
 131-174 8.89e-03

excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of proteins of which all members for which functions are known except the UvrA proteins are involved in the transport of material through membranes. UvrA orthologs are involved in the recognition of DNA damage as a step in nucleotide excision repair. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]


Pssm-ID: 273184 [Multi-domain]  Cd Length: 925  Bit Score: 38.46  E-value: 8.89e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 1054819401 131 GLALVELGhladrRPAL-LSGGQQQRVALARALVNR---PALLLLDEP 174
Cdd:TIGR00630 817 GLGYIRLG-----QPATtLSGGEAQRIKLAKELSKRstgRTLYILDEP 859
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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