NCBI Conserved Domain Search

Conserved domains on [gi|521099586|ref|WP_020430478|]

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ABC transporter ATP-binding protein [Vibrio fluvialis]

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 ...

1-343

1.49e-165

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

Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 465.34 E-value: 1.49e-165

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099586   1 MSCALSIQNLTCQYDTQTVLESLSLNVEHGEIVCLLGASGCGKTTLLKAIAGLLPLSSGIMSLNGMTIDDgkhwLAPEQR 80
Cdd:COG3842    2 AMPALELENVSKRYGDVTALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRILLDGRDVTG----LPPEKR 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099586  81 NIGMIFQDYALFPHLTVAENIAFGLRQ--MAAEERHLQVQQMLELVHLSGFGDRYPHQLSGGQQQRVAIARSLAYKPDLL 158
Cdd:COG3842   78 NVGMVFQDYALFPHLTVAENVAFGLRMrgVPKAEIRARVAELLELVGLEGLADRYPHQLSGGQQQRVALARALAPEPRVL 157

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099586 159 LLDEPFSNIDTQVRHDLIGEIRKIFKKQGVTAIFVTHSREEAFAFADKMAVMNHGVIEQYGTASELYYRPSSKFVADFLG 238
Cdd:COG3842  158 LLDEPLSALDAKLREEMREELRRLQRELGITFIYVTHDQEEALALADRIAVMNDGRIEQVGTPEEIYERPATRFVADFIG 237

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099586 239 GGSYLPATRLAEHQY--QTPLGVVDAYAQQSIAQGSQCELLLRPQQISIYADEES---SVTVLEQQFMGDHCRYVID-AH 312
Cdd:COG3842  238 EANLLPGTVLGDEGGgvRTGGRTLEVPADAGLAAGGPVTVAIRPEDIRLSPEGPEnglPGTVEDVVFLGSHVRYRVRlGD 317

                        330       340       350
                 ....*....|....*....|....*....|....*
gi 521099586 313 GSKLLA----TSSRGLAVGQTVAVSIDTQGVLAFA 343
Cdd:COG3842  318 GQELVVrvpnRAALPLEPGDRVGLSWDPEDVVVLP 352

Name

Accession

Description

Interval

E-value

PotA

COG3842

ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ...

1-343

1.49e-165

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

Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 465.34 E-value: 1.49e-165

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099586   1 MSCALSIQNLTCQYDTQTVLESLSLNVEHGEIVCLLGASGCGKTTLLKAIAGLLPLSSGIMSLNGMTIDDgkhwLAPEQR 80
Cdd:COG3842    2 AMPALELENVSKRYGDVTALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRILLDGRDVTG----LPPEKR 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099586  81 NIGMIFQDYALFPHLTVAENIAFGLRQ--MAAEERHLQVQQMLELVHLSGFGDRYPHQLSGGQQQRVAIARSLAYKPDLL 158
Cdd:COG3842   78 NVGMVFQDYALFPHLTVAENVAFGLRMrgVPKAEIRARVAELLELVGLEGLADRYPHQLSGGQQQRVALARALAPEPRVL 157

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099586 159 LLDEPFSNIDTQVRHDLIGEIRKIFKKQGVTAIFVTHSREEAFAFADKMAVMNHGVIEQYGTASELYYRPSSKFVADFLG 238
Cdd:COG3842  158 LLDEPLSALDAKLREEMREELRRLQRELGITFIYVTHDQEEALALADRIAVMNDGRIEQVGTPEEIYERPATRFVADFIG 237

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099586 239 GGSYLPATRLAEHQY--QTPLGVVDAYAQQSIAQGSQCELLLRPQQISIYADEES---SVTVLEQQFMGDHCRYVID-AH 312
Cdd:COG3842  238 EANLLPGTVLGDEGGgvRTGGRTLEVPADAGLAAGGPVTVAIRPEDIRLSPEGPEnglPGTVEDVVFLGSHVRYRVRlGD 317

                        330       340       350
                 ....*....|....*....|....*....|....*
gi 521099586 313 GSKLLA----TSSRGLAVGQTVAVSIDTQGVLAFA 343
Cdd:COG3842  318 GQELVVrvpnRAALPLEPGDRVGLSWDPEDVVVLP 352

PhnT2

TIGR03265

putative 2-aminoethylphosphonate ABC transporter, ATP-binding protein; This ABC transporter ...

1-343

6.14e-119

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: 347.41 E-value: 6.14e-119

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099586    1 MSCALSIQNLTCQYDTQTVLESLSLNVEHGEIVCLLGASGCGKTTLLKAIAGLLPLSSGIMSLNGMTIDDgkhwLAPEQR 80
Cdd:TIGR03265   1 SSPYLSIDNIRKRFGAFTALKDISLSVKKGEFVCLLGPSGCGKTTLLRIIAGLERQTAGTIYQGGRDITR----LPPQKR 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099586   81 NIGMIFQDYALFPHLTVAENIAFGL--RQMAAEERHLQVQQMLELVHLSGFGDRYPHQLSGGQQQRVAIARSLAYKPDLL 158
Cdd:TIGR03265  77 DYGIVFQSYALFPNLTVADNIAYGLknRGMGRAEVAERVAELLDLVGLPGSERKYPGQLSGGQQQRVALARALATSPGLL 156

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099586  159 LLDEPFSNIDTQVRHDLIGEIRKIFKKQGVTAIFVTHSREEAFAFADKMAVMNHGVIEQYGTASELYYRPSSKFVADFLG 238
Cdd:TIGR03265 157 LLDEPLSALDARVREHLRTEIRQLQRRLGVTTIMVTHDQEEALSMADRIVVMNHGVIEQVGTPQEIYRHPATPFVADFVG 236

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099586  239 GGSYLPATRLAEHQYQTPlGVVDAYAQQSIAQGSQCELLLRPQQISIYADEES----SVTVLEQQFMGDHCRY---VIDA 311
Cdd:TIGR03265 237 EVNWLPGTRGGGSRARVG-GLTLACAPGLAQPGASVRLAVRPEDIRVSPAGNAanllLARVEDMEFLGAFYRLrlrLEGL 315

                         330       340       350
                  ....*....|....*....|....*....|....*...
gi 521099586  312 HGSKLLATSSR------GLAVGQTVAVSIDTQGVLAFA 343
Cdd:TIGR03265 316 PGQALVADVSAseverlGIRAGQPIWIELPAERLRAFA 353

ABC_Carb_Solutes_like

cd03259

ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ...

5-219

3.16e-106

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: 309.45 E-value: 3.16e-106

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099586   5 LSIQNLTCQYDTQTVLESLSLNVEHGEIVCLLGASGCGKTTLLKAIAGLLPLSSGIMSLNGMTIDDgkhwLAPEQRNIGM 84
Cdd:cd03259    1 LELKGLSKTYGSVRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDGRDVTG----VPPERRNIGM 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099586  85 IFQDYALFPHLTVAENIAFGLRQ--MAAEERHLQVQQMLELVHLSGFGDRYPHQLSGGQQQRVAIARSLAYKPDLLLLDE 162
Cdd:cd03259   77 VFQDYALFPHLTVAENIAFGLKLrgVPKAEIRARVRELLELVGLEGLLNRYPHELSGGQQQRVALARALAREPSLLLLDE 156

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 521099586 163 PFSNIDTQVRHDLIGEIRKIFKKQGVTAIFVTHSREEAFAFADKMAVMNHGVIEQYG 219
Cdd:cd03259  157 PLSALDAKLREELREELKELQRELGITTIYVTHDQEEALALADRIAVMNEGRIVQVG 213

potA

PRK09452

spermidine/putrescine ABC transporter ATP-binding protein PotA;

2-292

9.48e-100

spermidine/putrescine ABC transporter ATP-binding protein PotA;

Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 299.17 E-value: 9.48e-100

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099586   2 SCALSIQNLTCQYDTQTVLESLSLNVEHGEIVCLLGASGCGKTTLLKAIAGLLPLSSGIMSLNGMTIDDgkhwLAPEQRN 81
Cdd:PRK09452  12 SPLVELRGISKSFDGKEVISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLDGQDITH----VPAENRH 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099586  82 IGMIFQDYALFPHLTVAENIAFGLR--QMAAEERHLQVQQMLELVHLSGFGDRYPHQLSGGQQQRVAIARSLAYKPDLLL 159
Cdd:PRK09452  88 VNTVFQSYALFPHMTVFENVAFGLRmqKTPAAEITPRVMEALRMVQLEEFAQRKPHQLSGGQQQRVAIARAVVNKPKVLL 167

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099586 160 LDEPFSNIDTQVRHDLIGEIRKIFKKQGVTAIFVTHSREEAFAFADKMAVMNHGVIEQYGTASELYYRPSSKFVADFLGG 239
Cdd:PRK09452 168 LDESLSALDYKLRKQMQNELKALQRKLGITFVFVTHDQEEALTMSDRIVVMRDGRIEQDGTPREIYEEPKNLFVARFIGE 247

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 521099586 240 GSYLPAT---RLAEHQYQTPL-GVV-DAYAQQSIAQGSQCELLLRPQQISIYADEESS 292
Cdd:PRK09452 248 INIFDATvieRLDEQRVRANVeGREcNIYVNFAVEPGQKLHVLLRPEDLRVEEINDDE 305

tungstate_WtpC

NF040840

tungstate ABC transporter ATP-binding protein WtpC;

20-238

1.19e-82

tungstate ABC transporter ATP-binding protein WtpC;

Pssm-ID: 468779 [Multi-domain] Cd Length: 347 Bit Score: 254.62 E-value: 1.19e-82

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099586  20 LESLSLNVEHGEIVCLLGASGCGKTTLLKAIAGLLPLSSGIMSLNGMTIDDgkhwLAPEQRNIGMIFQDYALFPHLTVAE 99
Cdd:NF040840  16 LRDISLEVKEGEYFIILGPSGAGKTVLLELIAGIWPPDSGKIYLDGKDITN----LPPEKRGIAYVYQNYMLFPHKTVFE 91

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099586 100 NIAFGL--RQMAAEERHLQVQQMLELVHLSGFGDRYPHQLSGGQQQRVAIARSLAYKPDLLLLDEPFSNIDTQVRHDLIG 177
Cdd:NF040840  92 NIAFGLklRKVPKEEIERKVKEIMELLGISHLLHRKPRTLSGGEQQRVALARALIIEPKLLLLDEPLSALDVQTRDELIR 171

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 521099586 178 EIRKIFKKQGVTAIFVTHSREEAFAFADKMAVMNHGVIEQYGTASELYYRPSSKFVADFLG 238
Cdd:NF040840 172 EMKRWHREFGFTAIHVTHNFEEALSLADRVGIMLNGRLSQVGDVREVFRRPKNEFVARFVG 232

ABC_ATP_DarD

NF038007

darobactin export ABC transporter ATP-binding protein;

5-213

8.28e-51

darobactin export ABC transporter ATP-binding protein;

Pssm-ID: 411600 [Multi-domain] Cd Length: 218 Bit Score: 168.36 E-value: 8.28e-51

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099586   5 LSIQNLTCQYDTQT----VLESLSLNVEHGEIVCLLGASGCGKTTLLKAIAGLLPLSSGIMSLNGMTIDDGKHW--LAPE 78
Cdd:NF038007   2 LNMQNAEKCYITKTiktkVLNHLNFSVEKGDFVSIMGPSGSGKSTLLNIIGMFDSLDSGSLTLAGKEVTNLSYSqkIILR 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099586  79 QRNIGMIFQDYALFPHLTVAENIAFGL--RQMAAEERHLQVQQMLELVHLSGFGDRYPHQLSGGQQQRVAIARSLAYKPD 156
Cdd:NF038007  82 RELIGYIFQSFNLIPHLSIFDNVALPLkyRGVAKKERIERVNQVLNLFGIDNRRNHKPMQLSGGQQQRVAIARAMVSNPA 161

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 521099586 157 LLLLDEPFSNIDTQVRHDLIGEIRKIfKKQGVTAIFVTHSrEEAFAFADKMAVMNHG 213
Cdd:NF038007 162 LLLADEPTGNLDSKNARAVLQQLKYI-NQKGTTIIMVTHS-DEASTYGNRIINMKDG 216

ABC_tran

pfam00005

ABC transporter; ABC transporters for a large family of proteins responsible for translocation ...

20-165

6.88e-49

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: 160.89 E-value: 6.88e-49

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099586   20 LESLSLNVEHGEIVCLLGASGCGKTTLLKAIAGLLPLSSGIMSLNGMTIDDGkhWLAPEQRNIGMIFQDYALFPHLTVAE 99
Cdd:pfam00005   1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDLTDD--ERKSLRKEIGYVFQDPQLFPRLTVRE 78

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 521099586  100 NIAFGLRQMAAEERHL--QVQQMLELVHLSGFGDR----YPHQLSGGQQQRVAIARSLAYKPDLLLLDEPFS 165
Cdd:pfam00005  79 NLRLGLLLKGLSKREKdaRAEEALEKLGLGDLADRpvgeRPGTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150

AztA

NF040873

zinc ABC transporter ATP-binding protein AztA;

14-200

1.31e-30

zinc ABC transporter ATP-binding protein AztA;

Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 114.64 E-value: 1.31e-30

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099586  14 YDTQTVLESLSLNVEHGEIVCLLGASGCGKTTLLKAIAGLLPLSSGIMSLNGmtiddgkhwlapeQRNIGMIFQDYAL-- 91
Cdd:NF040873   2 YGGRPVLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTVRRAG-------------GARVAYVPQRSEVpd 68

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099586  92 -FPhLTVAENIAFG-------LRQMAAEERhLQVQQMLELVHLSGFGDRYPHQLSGGQQQRVAIARSLAYKPDLLLLDEP 163
Cdd:NF040873  69 sLP-LTVRDLVAMGrwarrglWRRLTRDDR-AAVDDALERVGLADLAGRQLGELSGGQRQRALLAQGLAQEADLLLLDEP 146

                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 521099586 164 FSNIDTQVRHDLIGEIRKIfKKQGVTAIFVTHSREEA 200
Cdd:NF040873 147 TTGLDAESRERIIALLAEE-HARGATVVVVTHDLELV 182

ABC2_perm_RbbA

NF033858

ribosome-associated ATPase/putative transporter RbbA;

8-222

1.37e-22

ribosome-associated ATPase/putative transporter RbbA;

Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 99.04 E-value: 1.37e-22

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099586   8 QNLTCQYDTQTVLESLSLNVEHGEIVCLLGASGCGKTTLLKAIAGLLPLSSGIMSLNGMTIDDGKhwLAPEQRnIGMIFQ 87
Cdd:NF033858 270 RGLTMRFGDFTAVDHVSFRIRRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGEAWLFGQPVDAGD--IATRRR-VGYMSQ 346

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099586  88 DYALFPHLTVAENIAFGLR--QMAAEERHLQVQQMLELVHLSGFGDRYPHQLSGGQQQRVAIARSLAYKPDLLLLDEPFS 165
Cdd:NF033858 347 AFSLYGELTVRQNLELHARlfHLPAAEIAARVAEMLERFDLADVADALPDSLPLGIRQRLSLAVAVIHKPELLILDEPTS 426

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 521099586 166 NIDTQVR----HDLIGEIRkifkKQGVTaIFV-THSREEAfAFADKMAVMNHG----------VIEQYGTAS 222
Cdd:NF033858 427 GVDPVARdmfwRLLIELSR----EDGVT-IFIsTHFMNEA-ERCDRISLMHAGrvlasdtpaaLVAARGAAT 492

GguA

NF040905

sugar ABC transporter ATP-binding protein;

20-213

4.94e-20

sugar ABC transporter ATP-binding protein;

Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 90.62 E-value: 4.94e-20

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099586  20 LESLSLNVEHGEIVCLLGASGCGKTTLLKAIAGLLPLSS--GIMSLNGMT-----IDDGkhwlapEQRNIGMIFQDYALF 92
Cdd:NF040905  17 LDDVNLSVREGEIHALCGENGAGKSTLMKVLSGVYPHGSyeGEILFDGEVcrfkdIRDS------EALGIVIIHQELALI 90

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099586  93 PHLTVAENIAFGLRQMAA-----EERHLQVQQMLELVHLsgfgDRYPHQLSG----GQQQRVAIARSLAYKPDLLLLDEP 163
Cdd:NF040905  91 PYLSIAENIFLGNERAKRgvidwNETNRRARELLAKVGL----DESPDTLVTdigvGKQQLVEIAKALSKDVKLLILDEP 166

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 521099586 164 ---FSNIDTQVRHDLIGEirkiFKKQGVTAIFVTHSREEAFAFADKMAVMNHG 213
Cdd:NF040905 167 taaLNEEDSAALLDLLLE----LKAQGITSIIISHKLNEIRRVADSITVLRDG 215

ABC2_perm_RbbA

NF033858

ribosome-associated ATPase/putative transporter RbbA;

4-252

1.70e-19

ribosome-associated ATPase/putative transporter RbbA;

Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 89.80 E-value: 1.70e-19

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099586   4 ALSIQNLTCQYDTQTVLESLSLNVEHGEIVCLLGASGCGKTTLLKAIAGLLPLSSG-IMSLNGmTIDDGKH--WLAPE-- 78
Cdd:NF033858   1 VARLEGVSHRYGKTVALDDVSLDIPAGCMVGLIGPDGVGKSSLLSLIAGARKIQQGrVEVLGG-DMADARHrrAVCPRia 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099586  79 ---Q---RNigmifqdyaLFPHLTVAENIAF-----GLrqmAAEERHLQVQQMLELVHLSGFGDRYPHQLSGGQQQRVAI 147
Cdd:NF033858  80 ympQglgKN---------LYPTLSVFENLDFfgrlfGQ---DAAERRRRIDELLRATGLAPFADRPAGKLSGGMKQKLGL 147

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099586 148 ARSLAYKPDLLLLDEPFSNIDTQVRH---DLIGEIRKifKKQGVTAIFVTHSREEAFAFaDKMAVMNHGVIEQYGTASEL 224
Cdd:NF033858 148 CCALIHDPDLLILDEPTTGVDPLSRRqfwELIDRIRA--ERPGMSVLVATAYMEEAERF-DWLVAMDAGRVLATGTPAEL 224

                        250       260       270
                 ....*....|....*....|....*....|...
gi 521099586 225 YYRPSSK-----FVAdflgggsYLPATRLAEHQ 252
Cdd:NF033858 225 LARTGADtleaaFIA-------LLPEEKRRGHQ 250

AAA

smart00382

ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ...

29-199

5.42e-11

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: 60.08 E-value: 5.42e-11

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099586    29 HGEIVCLLGASGCGKTTLLKAIAGLL-PLSSGIMSLNGMTIDDGKHWLAPEQRnigmifqdyalfphltvaeniafglrq 107
Cdd:smart00382   1 PGEVILIVGPPGSGKTTLARALARELgPPGGGVIYIDGEDILEEVLDQLLLII--------------------------- 53

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099586   108 maaeerhlqvqqmlelvhlsgfGDRYPHQLSGGQQQRVAIARSLAYKPDLLLLDEPFSNIDTQVRHDLIGEIRKIFKKQ- 186
Cdd:smart00382  54 ----------------------VGGKKASGSGELRLRLALALARKLKPDVLILDEITSLLDAEQEALLLLLEELRLLLLl 111

                          170
                   ....*....|....*..
gi 521099586   187 ----GVTAIFVTHSREE 199
Cdd:smart00382 112 ksekNLTVILTTNDEKD 128

40850658_otr

NF000106

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

108-224

5.70e-10

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

Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 59.75 E-value: 5.70e-10

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099586 108 MAAEERHLQVQQMLELVHLSGFGDRYPHQLSGGQQQRVAIARSLAYKPDLLLLDEPFSNIDTQVRHDLIGEIRKIFkKQG 187
Cdd:NF000106 116 LSRKDARARADELLERFSLTEAAGRAAAKYSGGMRRRLDLAASMIGRPAVLYLDEPTTGLDPRTRNEVWDEVRSMV-RDG 194

                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 521099586 188 VTAIFVTHSREEAFAFADKMAVMNHGVIEQYGTASEL 224
Cdd:NF000106 195 ATVLLTTQYMEEAEQLAHELTVIDRGRVIADGKVDEL 231

GguA

NF040905

sugar ABC transporter ATP-binding protein;

4-168

2.69e-04

sugar ABC transporter ATP-binding protein;

Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 42.47 E-value: 2.69e-04

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099586   4 ALSIQNLTCQYDTQT---VLESLSLNVEHGEIVCLLGASGCGKTTLLKAIAGLlplS-----SGIMSLNGMTIDDG---- 71
Cdd:NF040905 257 VFEVKNWTVYHPLHPerkVVDDVSLNVRRGEIVGIAGLMGAGRTELAMSVFGR---SygrniSGTVFKDGKEVDVStvsd 333

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099586  72 --KHWLA--PEQR-NIGMIFQDyalfphlTVAENI-AFGLRQMAaeeRHLQVQQMLELVHLSGFGD----RYPH------ 135
Cdd:NF040905 334 aiDAGLAyvTEDRkGYGLNLID-------DIKRNItLANLGKVS---RRGVIDENEEIKVAEEYRKkmniKTPSvfqkvg 403

                        170       180       190
                 ....*....|....*....|....*....|...
gi 521099586 136 QLSGGQQQRVAIARSLAYKPDLLLLDEPFSNID 168
Cdd:NF040905 404 NLSGGNQQKVVLSKWLFTDPDVLILDEPTRGID 436

Name

Accession

Description

Interval

E-value

PotA

COG3842

ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ...

1-343

1.49e-165

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

Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 465.34 E-value: 1.49e-165

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099586   1 MSCALSIQNLTCQYDTQTVLESLSLNVEHGEIVCLLGASGCGKTTLLKAIAGLLPLSSGIMSLNGMTIDDgkhwLAPEQR 80
Cdd:COG3842    2 AMPALELENVSKRYGDVTALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRILLDGRDVTG----LPPEKR 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099586  81 NIGMIFQDYALFPHLTVAENIAFGLRQ--MAAEERHLQVQQMLELVHLSGFGDRYPHQLSGGQQQRVAIARSLAYKPDLL 158
Cdd:COG3842   78 NVGMVFQDYALFPHLTVAENVAFGLRMrgVPKAEIRARVAELLELVGLEGLADRYPHQLSGGQQQRVALARALAPEPRVL 157

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099586 159 LLDEPFSNIDTQVRHDLIGEIRKIFKKQGVTAIFVTHSREEAFAFADKMAVMNHGVIEQYGTASELYYRPSSKFVADFLG 238
Cdd:COG3842  158 LLDEPLSALDAKLREEMREELRRLQRELGITFIYVTHDQEEALALADRIAVMNDGRIEQVGTPEEIYERPATRFVADFIG 237

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099586 239 GGSYLPATRLAEHQY--QTPLGVVDAYAQQSIAQGSQCELLLRPQQISIYADEES---SVTVLEQQFMGDHCRYVID-AH 312
Cdd:COG3842  238 EANLLPGTVLGDEGGgvRTGGRTLEVPADAGLAAGGPVTVAIRPEDIRLSPEGPEnglPGTVEDVVFLGSHVRYRVRlGD 317

                        330       340       350
                 ....*....|....*....|....*....|....*
gi 521099586 313 GSKLLA----TSSRGLAVGQTVAVSIDTQGVLAFA 343
Cdd:COG3842  318 GQELVVrvpnRAALPLEPGDRVGLSWDPEDVVVLP 352

MalK

COG3839

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

1-342

3.26e-124

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

Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 360.54 E-value: 3.26e-124

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099586   1 MScALSIQNLTCQYDTQTVLESLSLNVEHGEIVCLLGASGCGKTTLLKAIAGLLPLSSGIMSLNGMTIDDgkhwLAPEQR 80
Cdd:COG3839    1 MA-SLELENVSKSYGGVEALKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAGLEDPTSGEILIGGRDVTD----LPPKDR 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099586  81 NIGMIFQDYALFPHLTVAENIAFGLRQ--MAAEERHLQVQQMLELVHLSGFGDRYPHQLSGGQQQRVAIARSLAYKPDLL 158
Cdd:COG3839   76 NIAMVFQSYALYPHMTVYENIAFPLKLrkVPKAEIDRRVREAAELLGLEDLLDRKPKQLSGGQRQRVALGRALVREPKVF 155

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099586 159 LLDEPFSNIDTQVRHDLIGEIRKIFKKQGVTAIFVTHSREEAFAFADKMAVMNHGVIEQYGTASELYYRPSSKFVADFLG 238
Cdd:COG3839  156 LLDEPLSNLDAKLRVEMRAEIKRLHRRLGTTTIYVTHDQVEAMTLADRIAVMNDGRIQQVGTPEELYDRPANLFVAGFIG 235

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099586 239 GGS--YLPATrLAEHQYQTPLGVVDAYAQQSIAQGSQCELLLRPQQISIYADEES--SVTVLEQQFMGDHCRYVIDAHGS 314
Cdd:COG3839  236 SPPmnLLPGT-VEGGGVRLGGVRLPLPAALAAAAGGEVTLGIRPEHLRLADEGDGglEATVEVVEPLGSETLVHVRLGGQ 314

                        330       340       350
                 ....*....|....*....|....*....|
gi 521099586 315 KLLA--TSSRGLAVGQTVAVSIDTQGVLAF 342
Cdd:COG3839  315 ELVArvPGDTRLRPGDTVRLAFDPERLHLF 344

CysA

COG1118

ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ...

1-335

1.01e-120

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

Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 351.37 E-value: 1.01e-120

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099586   1 MScaLSIQNLTCQYDTQTVLESLSLNVEHGEIVCLLGASGCGKTTLLKAIAGLLPLSSGIMSLNGmtiDDGKHWLAPEQR 80
Cdd:COG1118    1 MS--IEVRNISKRFGSFTLLDDVSLEIASGELVALLGPSGSGKTTLLRIIAGLETPDSGRIVLNG---RDLFTNLPPRER 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099586  81 NIGMIFQDYALFPHLTVAENIAFGLRQM--AAEERHLQVQQMLELVHLSGFGDRYPHQLSGGQQQRVAIARSLAYKPDLL 158
Cdd:COG1118   76 RVGFVFQHYALFPHMTVAENIAFGLRVRppSKAEIRARVEELLELVQLEGLADRYPSQLSGGQRQRVALARALAVEPEVL 155

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099586 159 LLDEPFSNIDTQVRHDLIGEIRKIFKKQGVTAIFVTHSREEAFAFADKMAVMNHGVIEQYGTASELYYRPSSKFVADFLG 238
Cdd:COG1118  156 LLDEPFGALDAKVRKELRRWLRRLHDELGGTTVFVTHDQEEALELADRVVVMNQGRIEQVGTPDEVYDRPATPFVARFLG 235

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099586 239 GGSYLPATRLAEHQYqtpLGVVDAYAQQSIAQGsQCELLLRPQQISIYADEESS----VTVLEQQFMGDHCRY---VIDA 311
Cdd:COG1118  236 CVNVLRGRVIGGQLE---ADGLTLPVAEPLPDG-PAVAGVRPHDIEVSREPEGEntfpATVARVSELGPEVRVelkLEDG 311

                        330       340       350
                 ....*....|....*....|....*....|
gi 521099586 312 HGSKLLATSSR------GLAVGQTVAVSID 335
Cdd:COG1118  312 EGQPLEAEVTKeawaelGLAPGDPVYLRPR 341

PhnT2

TIGR03265

putative 2-aminoethylphosphonate ABC transporter, ATP-binding protein; This ABC transporter ...

1-343

6.14e-119

Pssm-ID: 274496 [Multi-domain] Cd Length: 353 Bit Score: 347.41 E-value: 6.14e-119

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099586    1 MSCALSIQNLTCQYDTQTVLESLSLNVEHGEIVCLLGASGCGKTTLLKAIAGLLPLSSGIMSLNGMTIDDgkhwLAPEQR 80
Cdd:TIGR03265   1 SSPYLSIDNIRKRFGAFTALKDISLSVKKGEFVCLLGPSGCGKTTLLRIIAGLERQTAGTIYQGGRDITR----LPPQKR 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099586   81 NIGMIFQDYALFPHLTVAENIAFGL--RQMAAEERHLQVQQMLELVHLSGFGDRYPHQLSGGQQQRVAIARSLAYKPDLL 158
Cdd:TIGR03265  77 DYGIVFQSYALFPNLTVADNIAYGLknRGMGRAEVAERVAELLDLVGLPGSERKYPGQLSGGQQQRVALARALATSPGLL 156

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099586  159 LLDEPFSNIDTQVRHDLIGEIRKIFKKQGVTAIFVTHSREEAFAFADKMAVMNHGVIEQYGTASELYYRPSSKFVADFLG 238
Cdd:TIGR03265 157 LLDEPLSALDARVREHLRTEIRQLQRRLGVTTIMVTHDQEEALSMADRIVVMNHGVIEQVGTPQEIYRHPATPFVADFVG 236

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099586  239 GGSYLPATRLAEHQYQTPlGVVDAYAQQSIAQGSQCELLLRPQQISIYADEES----SVTVLEQQFMGDHCRY---VIDA 311
Cdd:TIGR03265 237 EVNWLPGTRGGGSRARVG-GLTLACAPGLAQPGASVRLAVRPEDIRVSPAGNAanllLARVEDMEFLGAFYRLrlrLEGL 315

                         330       340       350
                  ....*....|....*....|....*....|....*...
gi 521099586  312 HGSKLLATSSR------GLAVGQTVAVSIDTQGVLAFA 343
Cdd:TIGR03265 316 PGQALVADVSAseverlGIRAGQPIWIELPAERLRAFA 353

ABC_Carb_Solutes_like

cd03259

ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ...

5-219

3.16e-106

Pssm-ID: 213226 [Multi-domain] Cd Length: 213 Bit Score: 309.45 E-value: 3.16e-106

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099586   5 LSIQNLTCQYDTQTVLESLSLNVEHGEIVCLLGASGCGKTTLLKAIAGLLPLSSGIMSLNGMTIDDgkhwLAPEQRNIGM 84
Cdd:cd03259    1 LELKGLSKTYGSVRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDGRDVTG----VPPERRNIGM 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099586  85 IFQDYALFPHLTVAENIAFGLRQ--MAAEERHLQVQQMLELVHLSGFGDRYPHQLSGGQQQRVAIARSLAYKPDLLLLDE 162
Cdd:cd03259   77 VFQDYALFPHLTVAENIAFGLKLrgVPKAEIRARVRELLELVGLEGLLNRYPHELSGGQQQRVALARALAREPSLLLLDE 156

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 521099586 163 PFSNIDTQVRHDLIGEIRKIFKKQGVTAIFVTHSREEAFAFADKMAVMNHGVIEQYG 219
Cdd:cd03259  157 PLSALDAKLREELREELKELQRELGITTIYVTHDQEEALALADRIAVMNEGRIVQVG 213

potA

PRK09452

spermidine/putrescine ABC transporter ATP-binding protein PotA;

2-292

9.48e-100

spermidine/putrescine ABC transporter ATP-binding protein PotA;

Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 299.17 E-value: 9.48e-100

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099586   2 SCALSIQNLTCQYDTQTVLESLSLNVEHGEIVCLLGASGCGKTTLLKAIAGLLPLSSGIMSLNGMTIDDgkhwLAPEQRN 81
Cdd:PRK09452  12 SPLVELRGISKSFDGKEVISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLDGQDITH----VPAENRH 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099586  82 IGMIFQDYALFPHLTVAENIAFGLR--QMAAEERHLQVQQMLELVHLSGFGDRYPHQLSGGQQQRVAIARSLAYKPDLLL 159
Cdd:PRK09452  88 VNTVFQSYALFPHMTVFENVAFGLRmqKTPAAEITPRVMEALRMVQLEEFAQRKPHQLSGGQQQRVAIARAVVNKPKVLL 167

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099586 160 LDEPFSNIDTQVRHDLIGEIRKIFKKQGVTAIFVTHSREEAFAFADKMAVMNHGVIEQYGTASELYYRPSSKFVADFLGG 239
Cdd:PRK09452 168 LDESLSALDYKLRKQMQNELKALQRKLGITFVFVTHDQEEALTMSDRIVVMRDGRIEQDGTPREIYEEPKNLFVARFIGE 247

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 521099586 240 GSYLPAT---RLAEHQYQTPL-GVV-DAYAQQSIAQGSQCELLLRPQQISIYADEESS 292
Cdd:PRK09452 248 INIFDATvieRLDEQRVRANVeGREcNIYVNFAVEPGQKLHVLLRPEDLRVEEINDDE 305

ABC_PotA_N

cd03300

ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ...

5-238

1.39e-96

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: 286.06 E-value: 1.39e-96

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099586   5 LSIQNLTCQYDTQTVLESLSLNVEHGEIVCLLGASGCGKTTLLKAIAGLLPLSSGIMSLNGMTIddgkHWLAPEQRNIGM 84
Cdd:cd03300    1 IELENVSKFYGGFVALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGKDI----TNLPPHKRPVNT 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099586  85 IFQDYALFPHLTVAENIAFGLR--QMAAEERHLQVQQMLELVHLSGFGDRYPHQLSGGQQQRVAIARSLAYKPDLLLLDE 162
Cdd:cd03300   77 VFQNYALFPHLTVFENIAFGLRlkKLPKAEIKERVAEALDLVQLEGYANRKPSQLSGGQQQRVAIARALVNEPKVLLLDE 156

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 521099586 163 PFSNIDTQVRHDLIGEIRKIFKKQGVTAIFVTHSREEAFAFADKMAVMNHGVIEQYGTASELYYRPSSKFVADFLG 238
Cdd:cd03300  157 PLGALDLKLRKDMQLELKRLQKELGITFVFVTHDQEEALTMSDRIAVMNKGKIQQIGTPEEIYEEPANRFVADFIG 232

TauB

COG1116

ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ...

4-210

6.71e-95

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

Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 282.75 E-value: 6.71e-95

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099586   4 ALSIQNLTCQYDT----QTVLESLSLNVEHGEIVCLLGASGCGKTTLLKAIAGLLPLSSGIMSLNGMTIDdgkhwlAPEQ 79
Cdd:COG1116    7 ALELRGVSKRFPTggggVTALDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPTSGEVLVDGKPVT------GPGP 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099586  80 RnIGMIFQDYALFPHLTVAENIAFGLRQ--MAAEERHLQVQQMLELVHLSGFGDRYPHQLSGGQQQRVAIARSLAYKPDL 157
Cdd:COG1116   81 D-RGVVFQEPALLPWLTVLDNVALGLELrgVPKAERRERARELLELVGLAGFEDAYPHQLSGGMRQRVAIARALANDPEV 159

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 521099586 158 LLLDEPFSNIDTQVRHDLIGEIRKIFKKQGVTAIFVTHSREEAFAFADKMAVM 210
Cdd:COG1116  160 LLMDEPFGALDALTRERLQDELLRLWQETGKTVLFVTHDVDEAVFLADRVVVL 212

fbpC

PRK11432

ferric ABC transporter ATP-binding protein;

5-317

3.55e-92

ferric ABC transporter ATP-binding protein;

Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 278.91 E-value: 3.55e-92

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099586   5 LSIQNLTCQYDTQTVLESLSLNVEHGEIVCLLGASGCGKTTLLKAIAGLLPLSSGIMSLNGMTIDDGkhwlAPEQRNIGM 84
Cdd:PRK11432   7 VVLKNITKRFGSNTVIDNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIFIDGEDVTHR----SIQQRDICM 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099586  85 IFQDYALFPHLTVAENIAFGLRQM--AAEERHLQVQQMLELVHLSGFGDRYPHQLSGGQQQRVAIARSLAYKPDLLLLDE 162
Cdd:PRK11432  83 VFQSYALFPHMSLGENVGYGLKMLgvPKEERKQRVKEALELVDLAGFEDRYVDQISGGQQQRVALARALILKPKVLLFDE 162

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099586 163 PFSNIDTQVRHDLIGEIRKIFKKQGVTAIFVTHSREEAFAFADKMAVMNHGVIEQYGTASELYYRPSSKFVADFLGGGSY 242
Cdd:PRK11432 163 PLSNLDANLRRSMREKIRELQQQFNITSLYVTHDQSEAFAVSDTVIVMNKGKIMQIGSPQELYRQPASRFMASFMGDANI 242

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099586 243 LPATRLAE----HQYQTPLgvvDAYAQQSIAQGSqCELLLRPQQISIYADEESS--VTVLEQQFMGDHCRYVIDAHGSKL 316
Cdd:PRK11432 243 FPATLSGDyvdiYGYRLPR---PAAFAFNLPDGE-CTVGVRPEAITLSEQGEESqrCTIKHVAYMGPQYEVTVDWHGQEL 318


                 .
gi 521099586 317 L 317
Cdd:PRK11432 319 L 319

ABC_CysA_sulfate_importer

cd03296

ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ...

7-238

1.00e-90

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: 271.13 E-value: 1.00e-90

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099586   7 IQNLTCQYDTQTVLESLSLNVEHGEIVCLLGASGCGKTTLLKAIAGLLPLSSGIMSLNGMTIDDgkhwLAPEQRNIGMIF 86
Cdd:cd03296    5 VRNVSKRFGDFVALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGGEDATD----VPVQERNVGFVF 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099586  87 QDYALFPHLTVAENIAFGLRQMAAEER------HLQVQQMLELVHLSGFGDRYPHQLSGGQQQRVAIARSLAYKPDLLLL 160
Cdd:cd03296   81 QHYALFRHMTVFDNVAFGLRVKPRSERppeaeiRAKVHELLKLVQLDWLADRYPAQLSGGQRQRVALARALAVEPKVLLL 160

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 521099586 161 DEPFSNIDTQVRHDLIGEIRKIFKKQGVTAIFVTHSREEAFAFADKMAVMNHGVIEQYGTASELYYRPSSKFVADFLG 238
Cdd:cd03296  161 DEPFGALDAKVRKELRRWLRRLHDELHVTTVFVTHDQEEALEVADRVVVMNKGRIEQVGTPDEVYDHPASPFVYSFLG 238

potA

TIGR01187

spermidine/putrescine ABC transporter ATP-binding subunit; This model describes spermidine ...

35-332

4.85e-89

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: 270.13 E-value: 4.85e-89

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099586   35 LLGASGCGKTTLLKAIAGLLPLSSGIMSLNGMTIDDgkhwLAPEQRNIGMIFQDYALFPHLTVAENIAFGLRQ--MAAEE 112
Cdd:TIGR01187   1 LLGPSGCGKTTLLRLLAGFEQPDSGSIMLDGEDVTN----VPPHLRHINMVFQSYALFPHMTVEENVAFGLKMrkVPRAE 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099586  113 RHLQVQQMLELVHLSGFGDRYPHQLSGGQQQRVAIARSLAYKPDLLLLDEPFSNIDTQVRHDLIGEIRKIFKKQGVTAIF 192
Cdd:TIGR01187  77 IKPRVLEALRLVQLEEFADRKPHQLSGGQQQRVALARALVFKPKILLLDEPLSALDKKLRDQMQLELKTIQEQLGITFVF 156

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099586  193 VTHSREEAFAFADKMAVMNHGVIEQYGTASELYYRPSSKFVADFLGGGSYLPATRLAEHQYQTPLGVV-----DAYAQQS 267
Cdd:TIGR01187 157 VTHDQEEAMTMSDRIAIMRKGKIAQIGTPEEIYEEPANLFVARFIGEINVFEATVIERKSEQVVLAGVegrrcDIYTDVP 236

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 521099586  268 IAQGSQCELLLRPQQISIYADEESS------VTVLEQQFMGDHCRYV--IDAHGSKLLAT------SSRGLAVGQTVAV 332
Cdd:TIGR01187 237 VEKDQPLHVVLRPEKIVIEEEDEANssnaiiGHVIDITYLGMTLEVHvrLETGQKVLVSEffneddPHMSPSIGDRVGL 315

ABC_NrtD_SsuB_transporters

cd03293

ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ...

5-211

1.68e-88

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: 264.72 E-value: 1.68e-88

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099586   5 LSIQNLTCQYDT----QTVLESLSLNVEHGEIVCLLGASGCGKTTLLKAIAGLLPLSSGIMSLNGMTIddgkhwlAPEQR 80
Cdd:cd03293    1 LEVRNVSKTYGGgggaVTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVDGEPV-------TGPGP 73

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099586  81 NIGMIFQDYALFPHLTVAENIAFGLRQ--MAAEERHLQVQQMLELVHLSGFGDRYPHQLSGGQQQRVAIARSLAYKPDLL 158
Cdd:cd03293   74 DRGYVFQQDALLPWLTVLDNVALGLELqgVPKAEARERAEELLELVGLSGFENAYPHQLSGGMRQRVALARALAVDPDVL 153

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 521099586 159 LLDEPFSNIDTQVRHDLIGEIRKIFKKQGVTAIFVTHSREEAFAFADKMAVMN 211
Cdd:cd03293  154 LLDEPFSALDALTREQLQEELLDIWRETGKTVLLVTHDIDEAVFLADRVVVLS 206

PRK10851

sulfate/thiosulfate ABC transporter ATP-binding protein CysA;

1-285

2.34e-84

sulfate/thiosulfate ABC transporter ATP-binding protein CysA;

Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 259.25 E-value: 2.34e-84

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099586   1 MScaLSIQNLTCQYDTQTVLESLSLNVEHGEIVCLLGASGCGKTTLLKAIAGLLPLSSGIMSLNGMTIDDgkhwLAPEQR 80
Cdd:PRK10851   1 MS--IEIANIKKSFGRTQVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFHGTDVSR----LHARDR 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099586  81 NIGMIFQDYALFPHLTVAENIAFGLRQMAAEER------HLQVQQMLELVHLSGFGDRYPHQLSGGQQQRVAIARSLAYK 154
Cdd:PRK10851  75 KVGFVFQHYALFRHMTVFDNIAFGLTVLPRRERpnaaaiKAKVTQLLEMVQLAHLADRYPAQLSGGQKQRVALARALAVE 154

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099586 155 PDLLLLDEPFSNIDTQVRHDLIGEIRKIFKKQGVTAIFVTHSREEAFAFADKMAVMNHGVIEQYGTASELYYRPSSKFVA 234
Cdd:PRK10851 155 PQILLLDEPFGALDAQVRKELRRWLRQLHEELKFTSVFVTHDQEEAMEVADRVVVMSQGNIEQAGTPDQVWREPATRFVL 234

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 521099586 235 DFLGGGSYLPAT----RLAEHQYQTPLGVVDAYaqqsiaQGsQCELLLRPQQISI 285
Cdd:PRK10851 235 EFMGEVNRLQGTirggQFHVGAHRWPLGYTPAY------QG-PVDLFLRPWEVDI 282

OpuBA

COG1125

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

7-255

3.19e-84

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

Pssm-ID: 440742 [Multi-domain] Cd Length: 306 Bit Score: 256.94 E-value: 3.19e-84

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099586   7 IQNLTCQY-DTQTVLESLSLNVEHGEIVCLLGASGCGKTTLLKAIAGLLPLSSGIMSLNGMTIDDgkhwLAPEQ--RNIG 83
Cdd:COG1125    4 FENVTKRYpDGTVAVDDLSLTIPAGEFTVLVGPSGCGKTTTLRMINRLIEPTSGRILIDGEDIRD----LDPVElrRRIG 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099586  84 MIFQDYALFPHLTVAENIAF--GLRQMAAEERHLQVQQMLELVHL--SGFGDRYPHQLSGGQQQRVAIARSLAYKPDLLL 159
Cdd:COG1125   80 YVIQQIGLFPHMTVAENIATvpRLLGWDKERIRARVDELLELVGLdpEEYRDRYPHELSGGQQQRVGVARALAADPPILL 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099586 160 LDEPFSNIDTQVRHDLIGEIRKIFKKQGVTAIFVTHSREEAFAFADKMAVMNHGVIEQYGTASELYYRPSSKFVADFLGG 239
Cdd:COG1125  160 MDEPFGALDPITREQLQDELLRLQRELGKTIVFVTHDIDEALKLGDRIAVMREGRIVQYDTPEEILANPANDFVADFVGA 239

                        250       260
                 ....*....|....*....|..
gi 521099586 240 G------SYLPATRLAEHQYQT 255
Cdd:COG1125  240 DrglrrlSLLRVEDLMLPEPPT 261

3a0106s01

TIGR00968

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

7-238

2.77e-83

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

Pssm-ID: 130041 [Multi-domain] Cd Length: 237 Bit Score: 252.41 E-value: 2.77e-83

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099586    7 IQNLTCQYDTQTVLESLSLNVEHGEIVCLLGASGCGKTTLLKAIAGLLPLSSGIMSLNGMtidDGKHwLAPEQRNIGMIF 86
Cdd:TIGR00968   3 IANISKRFGSFQALDDVNLEVPTGSLVALLGPSGSGKSTLLRIIAGLEQPDSGRIRLNGQ---DATR-VHARDRKIGFVF 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099586   87 QDYALFPHLTVAENIAFGL--RQMAAEERHLQVQQMLELVHLSGFGDRYPHQLSGGQQQRVAIARSLAYKPDLLLLDEPF 164
Cdd:TIGR00968  79 QHYALFKHLTVRDNIAFGLeiRKHPKAKIKARVEELLELVQLEGLGDRYPNQLSGGQRQRVALARALAVEPQVLLLDEPF 158

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 521099586  165 SNIDTQVRHDLIGEIRKIFKKQGVTAIFVTHSREEAFAFADKMAVMNHGVIEQYGTASELYYRPSSKFVADFLG 238
Cdd:TIGR00968 159 GALDAKVRKELRSWLRKLHDEVHVTTVFVTHDQEEAMEVADRIVVMSNGKIEQIGSPDEVYDHPANPFVMSFLG 232

ABC_ModC_like

cd03299

ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ...

5-238

5.98e-83

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: 251.10 E-value: 5.98e-83

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099586   5 LSIQNLtCQYDTQTVLESLSLNVEHGEIVCLLGASGCGKTTLLKAIAGLLPLSSGIMSLNGMTIDDgkhwLAPEQRNIGM 84
Cdd:cd03299    1 LKVENL-SKDWKEFKLKNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNGKDITN----LPPEKRDISY 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099586  85 IFQDYALFPHLTVAENIAFGLRQMAAE--ERHLQVQQMLELVHLSGFGDRYPHQLSGGQQQRVAIARSLAYKPDLLLLDE 162
Cdd:cd03299   76 VPQNYALFPHMTVYKNIAYGLKKRKVDkkEIERKVLEIAEMLGIDHLLNRKPETLSGGEQQRVAIARALVVNPKILLLDE 155

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 521099586 163 PFSNIDTQVRHDLIGEIRKIFKKQGVTAIFVTHSREEAFAFADKMAVMNHGVIEQYGTASELYYRPSSKFVADFLG 238
Cdd:cd03299  156 PFSALDVRTKEKLREELKKIRKEFGVTVLHVTHDFEEAWALADKVAIMLNGKLIQVGKPEEVFKKPKNEFVAEFLG 231

ABC_MalK_N

cd03301

The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ...

5-219

1.14e-82

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: 249.86 E-value: 1.14e-82

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099586   5 LSIQNLTCQYDTQTVLESLSLNVEHGEIVCLLGASGCGKTTLLKAIAGLLPLSSGIMSLNGMTIDDgkhwLAPEQRNIGM 84
Cdd:cd03301    1 VELENVTKRFGNVTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGRDVTD----LPPKDRDIAM 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099586  85 IFQDYALFPHLTVAENIAFGLR-----QMAAEERHLQVQQMLELVHLSgfgDRYPHQLSGGQQQRVAIARSLAYKPDLLL 159
Cdd:cd03301   77 VFQNYALYPHMTVYDNIAFGLKlrkvpKDEIDERVREVAELLQIEHLL---DRKPKQLSGGQRQRVALGRAIVREPKVFL 153

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099586 160 LDEPFSNIDTQVRHDLIGEIRKIFKKQGVTAIFVTHSREEAFAFADKMAVMNHGVIEQYG 219
Cdd:cd03301  154 MDEPLSNLDAKLRVQMRAELKRLQQRLGTTTIYVTHDQVEAMTMADRIAVMNDGQIQQIG 213

tungstate_WtpC

NF040840

tungstate ABC transporter ATP-binding protein WtpC;

20-238

1.19e-82

tungstate ABC transporter ATP-binding protein WtpC;

Pssm-ID: 468779 [Multi-domain] Cd Length: 347 Bit Score: 254.62 E-value: 1.19e-82

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099586  20 LESLSLNVEHGEIVCLLGASGCGKTTLLKAIAGLLPLSSGIMSLNGMTIDDgkhwLAPEQRNIGMIFQDYALFPHLTVAE 99
Cdd:NF040840  16 LRDISLEVKEGEYFIILGPSGAGKTVLLELIAGIWPPDSGKIYLDGKDITN----LPPEKRGIAYVYQNYMLFPHKTVFE 91

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099586 100 NIAFGL--RQMAAEERHLQVQQMLELVHLSGFGDRYPHQLSGGQQQRVAIARSLAYKPDLLLLDEPFSNIDTQVRHDLIG 177
Cdd:NF040840  92 NIAFGLklRKVPKEEIERKVKEIMELLGISHLLHRKPRTLSGGEQQRVALARALIIEPKLLLLDEPLSALDVQTRDELIR 171

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 521099586 178 EIRKIFKKQGVTAIFVTHSREEAFAFADKMAVMNHGVIEQYGTASELYYRPSSKFVADFLG 238
Cdd:NF040840 172 EMKRWHREFGFTAIHVTHNFEEALSLADRVGIMLNGRLSQVGDVREVFRRPKNEFVARFVG 232

potG

PRK11607

putrescine ABC transporter ATP-binding subunit PotG;

5-283

5.54e-80

putrescine ABC transporter ATP-binding subunit PotG;

Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 248.60 E-value: 5.54e-80

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099586   5 LSIQNLTCQYDTQTVLESLSLNVEHGEIVCLLGASGCGKTTLLKAIAGLLPLSSGIMSLNGMTIDDgkhwLAPEQRNIGM 84
Cdd:PRK11607  20 LEIRNLTKSFDGQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVDLSH----VPPYQRPINM 95

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099586  85 IFQDYALFPHLTVAENIAFGLRQ--MAAEERHLQVQQMLELVHLSGFGDRYPHQLSGGQQQRVAIARSLAYKPDLLLLDE 162
Cdd:PRK11607  96 MFQSYALFPHMTVEQNIAFGLKQdkLPKAEIASRVNEMLGLVHMQEFAKRKPHQLSGGQRQRVALARSLAKRPKLLLLDE 175

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099586 163 PFSNIDTQVRHDLIGEIRKIFKKQGVTAIFVTHSREEAFAFADKMAVMNHGVIEQYGTASELYYRPSSKFVADFLGGGSY 242
Cdd:PRK11607 176 PMGALDKKLRDRMQLEVVDILERVGVTCVMVTHDQEEAMTMAGRIAIMNRGKFVQIGEPEEIYEHPTTRYSAEFIGSVNV 255

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|
gi 521099586 243 LPATrLAEHQ-----YQTPLGV----VDAYAqqSIAQGSQCELLLRPQQI 283
Cdd:PRK11607 256 FEGV-LKERQedglvIDSPGLVhplkVDADA--SVVDNVPVHVALRPEKI 302

GlnQ

COG1126

ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ...

5-238

7.67e-77

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

Pssm-ID: 440743 [Multi-domain] Cd Length: 239 Bit Score: 235.66 E-value: 7.67e-77

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099586   5 LSIQNLTCQYDTQTVLESLSLNVEHGEIVCLLGASGCGKTTLLKAIAGLLPLSSGIMSLNGMTIDDGKHWLAPEQRNIGM 84
Cdd:COG1126    2 IEIENLHKSFGDLEVLKGISLDVEKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTITVDGEDLTDSKKDINKLRRKVGM 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099586  85 IFQDYALFPHLTVAENIAFGLRQ---MAAEERHLQVQQMLELVHLSGFGDRYPHQLSGGQQQRVAIARSLAYKPDLLLLD 161
Cdd:COG1126   82 VFQQFNLFPHLTVLENVTLAPIKvkkMSKAEAEERAMELLERVGLADKADAYPAQLSGGQQQRVAIARALAMEPKVMLFD 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099586 162 EPFSNIDTQvrhdLIGEIRKIFK---KQGVTAIFVTHsrEEAFAF--ADKMAVMNHGVIEQYGTASELYYRPSSKFVADF 236
Cdd:COG1126  162 EPTSALDPE----LVGEVLDVMRdlaKEGMTMVVVTH--EMGFARevADRVVFMDGGRIVEEGPPEEFFENPQHERTRAF 235


                 ..
gi 521099586 237 LG 238
Cdd:COG1126  236 LS 237

ABC_OpuCA_Osmoprotection

cd03295

ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ...

5-238

2.51e-76

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: 234.50 E-value: 2.51e-76

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099586   5 LSIQNLTCQY-DTQTVLESLSLNVEHGEIVCLLGASGCGKTTLLKAIAGLLPLSSGIMSLNGMTIDDgkhwLAPEQ--RN 81
Cdd:cd03295    1 IEFENVTKRYgGGKKAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGEDIRE----QDPVElrRK 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099586  82 IGMIFQDYALFPHLTVAENIAF--GLRQMAAEERHLQVQQMLELVHL--SGFGDRYPHQLSGGQQQRVAIARSLAYKPDL 157
Cdd:cd03295   77 IGYVIQQIGLFPHMTVEENIALvpKLLKWPKEKIRERADELLALVGLdpAEFADRYPHELSGGQQQRVGVARALAADPPL 156

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099586 158 LLLDEPFSNIDTQVRHDLIGEIRKIFKKQGVTAIFVTHSREEAFAFADKMAVMNHGVIEQYGTASELYYRPSSKFVADFL 237
Cdd:cd03295  157 LLMDEPFGALDPITRDQLQEEFKRLQQELGKTIVFVTHDIDEAFRLADRIAIMKNGEIVQVGTPDEILRSPANDFVAEFV 236


                 .
gi 521099586 238 G 238
Cdd:cd03295  237 G 237

ugpC

PRK11650

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

4-337

9.10e-76

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

Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 237.05 E-value: 9.10e-76

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099586   4 ALSIQNLTCQYDTQT-VLESLSLNVEHGEIVCLLGASGCGKTTLLKAIAGLLPLSSGIMSLNGMTIDDgkhwLAPEQRNI 82
Cdd:PRK11650   3 GLKLQAVRKSYDGKTqVIKGIDLDVADGEFIVLVGPSGCGKSTLLRMVAGLERITSGEIWIGGRVVNE----LEPADRDI 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099586  83 GMIFQDYALFPHLTVAENIAFGL--RQMAAEERHLQVQQMLELVHLSGFGDRYPHQLSGGQQQRVAIARSLAYKPDLLLL 160
Cdd:PRK11650  79 AMVFQNYALYPHMSVRENMAYGLkiRGMPKAEIEERVAEAARILELEPLLDRKPRELSGGQRQRVAMGRAIVREPAVFLF 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099586 161 DEPFSNIDTQVRHDLIGEIRKIFKKQGVTAIFVTHSREEAFAFADKMAVMNHGVIEQYGTASELYYRPSSKFVADFLGGG 240
Cdd:PRK11650 159 DEPLSNLDAKLRVQMRLEIQRLHRRLKTTSLYVTHDQVEAMTLADRVVVMNGGVAEQIGTPVEVYEKPASTFVASFIGSP 238

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099586 241 S--YLPATRLAEH-QYQTPLGV-VDAYAQQSIAQGSQCELLLRPQQISIYADEESSVTVLEqqfmgdhcryVIDAHGSKL 316
Cdd:PRK11650 239 AmnLLDGRVSADGaAFELAGGIaLPLGGGYRQYAGRKLTLGIRPEHIALSSAEGGVPLTVD----------TVELLGADN 308

                        330       340
                 ....*....|....*....|.
gi 521099586 317 LATSSRGlavGQTVAVSIDTQ 337
Cdd:PRK11650 309 LAHGRWG---GQPLVVRLPHQ 326

MlaF

COG1127

ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ...

1-237

1.37e-75

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: 232.56 E-value: 1.37e-75

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099586   1 MSCALSIQNLTCQYDTQTVLESLSLNVEHGEIVCLLGASGCGKTTLLKAIAGLLPLSSGIMSLNGMTIDD-GKHWLAPEQ 79
Cdd:COG1127    2 SEPMIEVRNLTKSFGDRVVLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEILVDGQDITGlSEKELYELR 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099586  80 RNIGMIFQDYALFPHLTVAENIAFGLRQ---MAAEERHLQVQQMLELVHLSGFGDRYPHQLSGGQQQRVAIARSLAYKPD 156
Cdd:COG1127   82 RRIGMLFQGGALFDSLTVFENVAFPLREhtdLSEAEIRELVLEKLELVGLPGAADKMPSELSGGMRKRVALARALALDPE 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099586 157 LLLLDEPFSNID---TQVRHDLIGEIRkifKKQGVTAIFVTHSREEAFAFADKMAVMNHGVIEQYGTASELyYRPSSKFV 233
Cdd:COG1127  162 ILLYDEPTAGLDpitSAVIDELIRELR---DELGLTSVVVTHDLDSAFAIADRVAVLADGKIIAEGTPEEL-LASDDPWV 237


                 ....
gi 521099586 234 ADFL 237
Cdd:COG1127  238 RQFL 241

PhnT

TIGR03258

2-aminoethylphosphonate ABC transport system, ATP-binding component PhnT; This ATP-binding ...

7-285

3.73e-75

2-aminoethylphosphonate ABC transport system, ATP-binding component PhnT; This ATP-binding component of an ABC transport system is found in Salmonella and Burkholderia lineages in the vicinity of enzymes for the breakdown of 2-aminoethylphosphonate.

Pssm-ID: 132302 [Multi-domain] Cd Length: 362 Bit Score: 235.66 E-value: 3.73e-75

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099586    7 IQNLTCQYDTQTVLESLSLNVEHGEIVCLLGASGCGKTTLLKAIAGLLPlSSGIMSLNGMTIDDGKHwLAPEQRNIGMIF 86
Cdd:TIGR03258   8 IDHLRVAYGANTVLDDLSLEIEAGELLALIGKSGCGKTTLLRAIAGFVK-AAGLTGRIAIADRDLTH-APPHKRGLALLF 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099586   87 QDYALFPHLTVAENIAFGLR--QMAAEERHLQVQQMLELVHLSGFGDRYPHQLSGGQQQRVAIARSLAYKPDLLLLDEPF 164
Cdd:TIGR03258  86 QNYALFPHLKVEDNVAFGLRaqKMPKADIAERVADALKLVGLGDAAAHLPAQLSGGMQQRIAIARAIAIEPDVLLLDEPL 165

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099586  165 SNIDTQVRHDLIGEIRKIFKK-QGVTAIFVTHSREEAFAFADKMAVMNHGVIEQYGTASELYYRPSSKFVADFLGGGSYL 243
Cdd:TIGR03258 166 SALDANIRANMREEIAALHEElPELTILCVTHDQDDALTLADKAGIMKDGRLAAHGEPQALYDAPADGFAAEFLGAANIL 245

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*...
gi 521099586  244 PATRLAEHQYQTPL------GVVDAYAQQSiAQGSQCELLLRPQQISI 285
Cdd:TIGR03258 246 PAIALGITEAPGLVdvscggAVIFAFGDGR-HDGRDKLACIRPEHLAL 292

ABC_ModC_molybdenum_transporter

cd03297

ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ...

20-219

1.10e-74

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: 229.49 E-value: 1.10e-74

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099586  20 LESLSLNVE---HGEIVCLLGASGCGKTTLLKAIAGLLPLSSGIMSLNGMTIDDG--KHWLAPEQRNIGMIFQDYALFPH 94
Cdd:cd03297   10 LPDFTLKIDfdlNEEVTGIFGASGAGKSTLLRCIAGLEKPDGGTIVLNGTVLFDSrkKINLPPQQRKIGLVFQQYALFPH 89

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099586  95 LTVAENIAFGLRQMAAEERHLQVQQMLELVHLSGFGDRYPHQLSGGQQQRVAIARSLAYKPDLLLLDEPFSNIDTQVRHD 174
Cdd:cd03297   90 LNVRENLAFGLKRKRNREDRISVDELLDLLGLDHLLNRYPAQLSGGEKQRVALARALAAQPELLLLDEPFSALDRALRLQ 169

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*
gi 521099586 175 LIGEIRKIFKKQGVTAIFVTHSREEAFAFADKMAVMNHGVIEQYG 219
Cdd:cd03297  170 LLPELKQIKKNLNIPVIFVTHDLSEAEYLADRIVVMEDGRLQYIG 214

EcfA2

COG1122

Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ...

5-228

5.03e-73

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: 225.67 E-value: 5.03e-73

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099586   5 LSIQNLTCQY-DTQTVLESLSLNVEHGEIVCLLGASGCGKTTLLKAIAGLLPLSSGIMSLNGMTIDDGKHWLAPeqRNIG 83
Cdd:COG1122    1 IELENLSFSYpGGTPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVDGKDITKKNLRELR--RKVG 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099586  84 MIFQ--DYALFpHLTVAENIAFGLRQM--AAEERHLQVQQMLELVHLSGFGDRYPHQLSGGQQQRVAIARSLAYKPDLLL 159
Cdd:COG1122   79 LVFQnpDDQLF-APTVEEDVAFGPENLglPREEIRERVEEALELVGLEHLADRPPHELSGGQKQRVAIAGVLAMEPEVLV 157

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 521099586 160 LDEPFSNIDTQVRHDLIGEIRKIfKKQGVTAIFVTHSREEAFAFADKMAVMNHGVIEQYGTASELYYRP 228
Cdd:COG1122  158 LDEPTAGLDPRGRRELLELLKRL-NKEGKTVIIVTHDLDLVAELADRVIVLDDGRIVADGTPREVFSDY 225

ThiQ

COG3840

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

5-238

7.49e-73

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

Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 225.40 E-value: 7.49e-73

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099586   5 LSIQNLTCQYDTQTVleSLSLNVEHGEIVCLLGASGCGKTTLLKAIAGLLPLSSGIMSLNGMTIDDgkhwLAPEQRNIGM 84
Cdd:COG3840    2 LRLDDLTYRYGDFPL--RFDLTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILWNGQDLTA----LPPAERPVSM 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099586  85 IFQDYALFPHLTVAENIAFGLR---QMAAEERHlQVQQMLELVHLSGFGDRYPHQLSGGQQQRVAIARSLAYKPDLLLLD 161
Cdd:COG3840   76 LFQENNLFPHLTVAQNIGLGLRpglKLTAEQRA-QVEQALERVGLAGLLDRLPGQLSGGQRQRVALARCLVRKRPILLLD 154

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 521099586 162 EPFSNIDTQVRHDLIGEIRKIFKKQGVTAIFVTHSREEAFAFADKMAVMNHGVIEQYGTASELYYRPSSKFVADFLG 238
Cdd:COG3840  155 EPFSALDPALRQEMLDLVDELCRERGLTVLMVTHDPEDAARIADRVLLVADGRIAADGPTAALLDGEPPPALAAYLG 231

ModC

COG4148

ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ...

24-335

7.45e-72

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: 226.91 E-value: 7.45e-72

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099586  24 SLNVEHGEIVCLLGASGCGKTTLLKAIAGLLPLSSGIMSLNGMTIDDG--KHWLAPEQRNIGMIFQDYALFPHLTVAENI 101
Cdd:COG4148   19 DFTLPGRGVTALFGPSGSGKTTLLRAIAGLERPDSGRIRLGGEVLQDSarGIFLPPHRRRIGYVFQEARLFPHLSVRGNL 98

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099586 102 AFGLRQMAAEERHLQVQQMLELVHLSGFGDRYPHQLSGGQQQRVAIARSLAYKPDLLLLDEPFSNIDTQVRHDLIGEIRK 181
Cdd:COG4148   99 LYGRKRAPRAERRISFDEVVELLGIGHLLDRRPATLSGGERQRVAIGRALLSSPRLLLMDEPLAALDLARKAEILPYLER 178

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099586 182 IFKKQGVTAIFVTHSREEAFAFADKMAVMNHGVIEQYGTASELYYRPSSKFVADFLGGGSYLPAtRLAEHQYQTPLGVVD 261
Cdd:COG4148  179 LRDELDIPILYVSHSLDEVARLADHVVLLEQGRVVASGPLAEVLSRPDLLPLAGGEEAGSVLEA-TVAAHDPDYGLTRLA 257

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099586 262 AYAQQ------SIAQGSQCEL----------LLRPQQISI-----------YADEESSVTVleqqfmgdhcryVIDAHGS 314
Cdd:COG4148  258 LGGGRlwvprlDLPPGTRVRVrirardvslaLEPPEGSSIlnilpgrvveiEPADGGQVLV------------RLDLGGQ 325

                        330       340       350
                 ....*....|....*....|....*....|..
gi 521099586 315 KLLATSSR------GLAVGQTV-----AVSID 335
Cdd:COG4148  326 TLLARITRrsadelGLAPGQTVyaqikSVALL 357

PRK11000

maltose/maltodextrin ABC transporter ATP-binding protein MalK;

6-238

4.21e-71

maltose/maltodextrin ABC transporter ATP-binding protein MalK;

Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 225.68 E-value: 4.21e-71

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099586   6 SIQNLTCQYDTQTVLESLSLNVEHGEIVCLLGASGCGKTTLLKAIAGLLPLSSGIMSLNGMTIDDgkhwLAPEQRNIGMI 85
Cdd:PRK11000   5 TLRNVTKAYGDVVISKDINLDIHEGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLFIGEKRMND----VPPAERGVGMV 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099586  86 FQDYALFPHLTVAENIAFGLRQMAAE--ERHLQVQQMLELVHLSGFGDRYPHQLSGGQQQRVAIARSLAYKPDLLLLDEP 163
Cdd:PRK11000  81 FQSYALYPHLSVAENMSFGLKLAGAKkeEINQRVNQVAEVLQLAHLLDRKPKALSGGQRQRVAIGRTLVAEPSVFLLDEP 160

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 521099586 164 FSNIDTQVRHDLIGEIRKIFKKQGVTAIFVTHSREEAFAFADKMAVMNHGVIEQYGTASELYYRPSSKFVADFLG 238
Cdd:PRK11000 161 LSNLDAALRVQMRIEISRLHKRLGRTMIYVTHDQVEAMTLADKIVVLDAGRVAQVGKPLELYHYPANRFVAGFIG 235

GsiA

COG1123

ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ...

5-228

1.08e-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: 228.63 E-value: 1.08e-70

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099586   5 LSIQNLTCQY-----DTQTVLESLSLNVEHGEIVCLLGASGCGKTTLLKAIAGLLPLSSGIMSLNGMTIDDGKHW-LAPE 78
Cdd:COG1123  261 LEVRNLSKRYpvrgkGGVRAVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRPTSGSILFDGKDLTKLSRRsLREL 340

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099586  79 QRNIGMIFQD--YALFPHLTVAENIAFGLRQ---MAAEERHLQVQQMLELVHLS-GFGDRYPHQLSGGQQQRVAIARSLA 152
Cdd:COG1123  341 RRRVQMVFQDpySSLNPRMTVGDIIAEPLRLhglLSRAERRERVAELLERVGLPpDLADRYPHELSGGQRQRVAIARALA 420

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 521099586 153 YKPDLLLLDEPFSNIDTQVRHDLIGEIRKIFKKQGVTAIFVTHSREEAFAFADKMAVMNHGVIEQYGTASELYYRP 228
Cdd:COG1123  421 LEPKLLILDEPTSALDVSVQAQILNLLRDLQRELGLTYLFISHDLAVVRYIADRVAVMYDGRIVEDGPTEEVFANP 496

ABC_Pro_Gly_Betaine

cd03294

ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ...

24-236

2.64e-70

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: 220.21 E-value: 2.64e-70

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099586  24 SLNVEHGEIVCLLGASGCGKTTLLKAIAGLLPLSSGIMSLNGMTID--DGKHWLAPEQRNIGMIFQDYALFPHLTVAENI 101
Cdd:cd03294   44 SLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGKVLIDGQDIAamSRKELRELRRKKISMVFQSFALLPHRTVLENV 123

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099586 102 AFGL--RQMAAEERHLQVQQMLELVHLSGFGDRYPHQLSGGQQQRVAIARSLAYKPDLLLLDEPFSNIDTQVRHDLIGEI 179
Cdd:cd03294  124 AFGLevQGVPRAEREERAAEALELVGLEGWEHKYPDELSGGMQQRVGLARALAVDPDILLMDEAFSALDPLIRREMQDEL 203

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 521099586 180 RKIFKKQGVTAIFVTHSREEAFAFADKMAVMNHGVIEQYGTASELYYRPSSKFVADF 236
Cdd:cd03294  204 LRLQAELQKTIVFITHDLDEALRLGDRIAIMKDGRLVQVGTPEEILTNPANDYVREF 260

ABC_Class3

cd03229

ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ...

5-213

4.07e-69

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: 213.97 E-value: 4.07e-69

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099586   5 LSIQNLTCQYDTQTVLESLSLNVEHGEIVCLLGASGCGKTTLLKAIAGLLPLSSGIMSLNGMTIDDGKHWLAPEQRNIGM 84
Cdd:cd03229    1 LELKNVSKRYGQKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGEDLTDLEDELPPLRRRIGM 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099586  85 IFQDYALFPHLTVAENIAFGlrqmaaeerhlqvqqmlelvhlsgfgdryphqLSGGQQQRVAIARSLAYKPDLLLLDEPF 164
Cdd:cd03229   81 VFQDFALFPHLTVLENIALG--------------------------------LSGGQQQRVALARALAMDPDVLLLDEPT 128

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 521099586 165 SNIDTQVRHDLIGEIRKIFKKQGVTAIFVTHSREEAFAFADKMAVMNHG 213
Cdd:cd03229  129 SALDPITRREVRALLKSLQAQLGITVVLVTHDLDEAARLADRVVVLRDG 177

CcmA

COG1131

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

5-224

5.94e-69

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

Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 215.31 E-value: 5.94e-69

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099586   5 LSIQNLTCQYDTQTVLESLSLNVEHGEIVCLLGASGCGKTTLLKAIAGLLPLSSGIMSLNGMTI-DDGKHWLapeqRNIG 83
Cdd:COG1131    1 IEVRGLTKRYGDKTALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRVLGEDVaRDPAEVR----RRIG 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099586  84 MIFQDYALFPHLTVAENIAF--GLRQMAAEERHLQVQQMLELVHLSGFGDRYPHQLSGGQQQRVAIARSLAYKPDLLLLD 161
Cdd:COG1131   77 YVPQEPALYPDLTVRENLRFfaRLYGLPRKEARERIDELLELFGLTDAADRKVGTLSGGMKQRLGLALALLHDPELLILD 156

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 521099586 162 EPFSNIDTQVRHDLIGEIRKIfKKQGVTAIFVTHSREEAFAFADKMAVMNHGVIEQYGTASEL 224
Cdd:COG1131  157 EPTSGLDPEARRELWELLREL-AAEGKTVLLSTHYLEEAERLCDRVAIIDKGRIVADGTPDEL 218

LolD

COG1136

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

1-216

6.46e-69

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

Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 214.91 E-value: 6.46e-69

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099586   1 MSCALSIQNLTCQYDT----QTVLESLSLNVEHGEIVCLLGASGCGKTTLLKAIAGLLPLSSGIMSLNGMTIDDgkhwLA 76
Cdd:COG1136    1 MSPLLELRNLTKSYGTgegeVTALRGVSLSIEAGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVLIDGQDISS----LS 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099586  77 PEQR------NIGMIFQDYALFPHLTVAENIAFGLR--QMAAEERHLQVQQMLELVHLSGFGDRYPHQLSGGQQQRVAIA 148
Cdd:COG1136   77 ERELarlrrrHIGFVFQFFNLLPELTALENVALPLLlaGVSRKERRERARELLERVGLGDRLDHRPSQLSGGQQQRVAIA 156

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 521099586 149 RSLAYKPDLLLLDEPFSNIDTQVRHDLIGEIRKIFKKQGVTAIFVTHSrEEAFAFADKMAVMNHGVIE 216
Cdd:COG1136  157 RALVNRPKLILADEPTGNLDSKTGEEVLELLRELNRELGTTIVMVTHD-PELAARADRVIRLRDGRIV 223

ABC_Org_Solvent_Resistant

cd03261

ATP-binding cassette transport system involved in resistance to organic solvents; ABC ...

5-224

9.22e-69

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: 215.06 E-value: 9.22e-69

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099586   5 LSIQNLTCQYDTQTVLESLSLNVEHGEIVCLLGASGCGKTTLLKAIAGLLPLSSGIMSLNGMTIDD-GKHWLAPEQRNIG 83
Cdd:cd03261    1 IELRGLTKSFGGRTVLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGEDISGlSEAELYRLRRRMG 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099586  84 MIFQDYALFPHLTVAENIAFGLRQMAAEERHL---QVQQMLELVHLSGFGDRYPHQLSGGQQQRVAIARSLAYKPDLLLL 160
Cdd:cd03261   81 MLFQSGALFDSLTVFENVAFPLREHTRLSEEEireIVLEKLEAVGLRGAEDLYPAELSGGMKKRVALARALALDPELLLY 160

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 521099586 161 DEPFSNID---TQVRHDLigeIRKIFKKQGVTAIFVTHSREEAFAFADKMAVMNHGVIEQYGTASEL 224
Cdd:cd03261  161 DEPTAGLDpiaSGVIDDL---IRSLKKELGLTSIMVTHDLDTAFAIADRIAVLYDGKIVAEGTPEEL 224

DppF

COG1124

ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ...

4-238

2.85e-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: 211.59 E-value: 2.85e-67

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099586   4 ALSIQNLTCQYDT----QTVLESLSLNVEHGEIVCLLGASGCGKTTLLKAIAGLLPLSSGIMSLNGMTIddGKHWLAPEQ 79
Cdd:COG1124    1 MLEVRNLSVSYGQggrrVPVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVTFDGRPV--TRRRRKAFR 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099586  80 RNIGMIFQDY--ALFPHLTVAENIAFGLRQMAAEERHLQVQQMLELVHL-SGFGDRYPHQLSGGQQQRVAIARSLAYKPD 156
Cdd:COG1124   79 RRVQMVFQDPyaSLHPRHTVDRILAEPLRIHGLPDREERIAELLEQVGLpPSFLDRYPHQLSGGQRQRVAIARALILEPE 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099586 157 LLLLDEPFSNIDTQVRHDLIGEIRKIFKKQGVTAIFVTHSREEAFAFADKMAVMNHGVIEQYGTASELYYRPSSKFVADF 236
Cdd:COG1124  159 LLLLDEPTSALDVSVQAEILNLLKDLREERGLTYLFVSHDLAVVAHLCDRVAVMQNGRIVEELTVADLLAGPKHPYTREL 238


                 ..
gi 521099586 237 LG 238
Cdd:COG1124  239 LA 240

YnjD

COG4136

ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ...

5-200

1.57e-66

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

Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 208.49 E-value: 1.57e-66

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099586   5 LSIQNLTCQYDTQTVLESLSLNVEHGEIVCLLGASGCGKTTLLKAIAGLLPL---SSGIMSLNGMTIDDgkhwLAPEQRN 81
Cdd:COG4136    2 LSLENLTITLGGRPLLAPLSLTVAPGEILTLMGPSGSGKSTLLAAIAGTLSPafsASGEVLLNGRRLTA----LPAEQRR 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099586  82 IGMIFQDYALFPHLTVAENIAFGL-RQMAAEERHLQVQQMLELVHLSGFGDRYPHQLSGGQQQRVAIARSLAYKPDLLLL 160
Cdd:COG4136   78 IGILFQDDLLFPHLSVGENLAFALpPTIGRAQRRARVEQALEEAGLAGFADRDPATLSGGQRARVALLRALLAEPRALLL 157

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....
gi 521099586 161 DEPFSNIDT----QVRHDLIGEIRkifkKQGVTAIFVTHSREEA 200
Cdd:COG4136  158 DEPFSKLDAalraQFREFVFEQIR----QRGIPALLVTHDEEDA 197

ABC_MJ0796_LolCDE_FtsE

cd03255

ATP-binding cassette domain of the transporters involved in export of lipoprotein and ...

5-215

1.14e-65

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: 206.57 E-value: 1.14e-65

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099586   5 LSIQNLTCQYDTQ----TVLESLSLNVEHGEIVCLLGASGCGKTTLLKAIAGLLPLSSGIMSLNGMTI---DDGKhwLAP 77
Cdd:cd03255    1 IELKNLSKTYGGGgekvQALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRVDGTDIsklSEKE--LAA 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099586  78 EQR-NIGMIFQDYALFPHLTVAENIAFGLR--QMAAEERHLQVQQMLELVHLSGFGDRYPHQLSGGQQQRVAIARSLAYK 154
Cdd:cd03255   79 FRRrHIGFVFQSFNLLPDLTALENVELPLLlaGVPKKERRERAEELLERVGLGDRLNHYPSELSGGQQQRVAIARALAND 158

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 521099586 155 PDLLLLDEPFSNIDTQVRHDLIGEIRKIFKKQGVTAIFVTHSREEAfAFADKMAVMNHGVI 215
Cdd:cd03255  159 PKIILADEPTGNLDSETGKEVMELLRELNKEAGTTIVVVTHDPELA-EYADRIIELRDGKI 218

ABC_cobalt_CbiO_domain1

cd03225

First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ...

6-213

2.21e-64

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: 203.08 E-value: 2.21e-64

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099586   6 SIQNLTCQYDTQT--VLESLSLNVEHGEIVCLLGASGCGKTTLLKAIAGLLPLSSGIMSLNGMTIDDGKhwLAPEQRNIG 83
Cdd:cd03225    1 ELKNLSFSYPDGArpALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDLTKLS--LKELRRKVG 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099586  84 MIFQ--DYALFpHLTVAENIAFGLRQM--AAEERHLQVQQMLELVHLSGFGDRYPHQLSGGQQQRVAIARSLAYKPDLLL 159
Cdd:cd03225   79 LVFQnpDDQFF-GPTVEEEVAFGLENLglPEEEIEERVEEALELVGLEGLRDRSPFTLSGGQKQRVAIAGVLAMDPDILL 157

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 521099586 160 LDEPFSNIDTQVRHDLIGEIRKIfKKQGVTAIFVTHSREEAFAFADKMAVMNHG 213
Cdd:cd03225  158 LDEPTAGLDPAGRRELLELLKKL-KAEGKTIIIVTHDLDLLLELADRVIVLEDG 210

ABC_HisP_GlnQ

cd03262

ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ...

5-215

2.65e-64

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: 202.76 E-value: 2.65e-64

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099586   5 LSIQNLTCQYDTQTVLESLSLNVEHGEIVCLLGASGCGKTTLLKAIAGLLPLSSGIMSLNGMTIDDGKHWLAPEQRNIGM 84
Cdd:cd03262    1 IEIKNLHKSFGDFHVLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIDGLKLTDDKKNINELRQKVGM 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099586  85 IFQDYALFPHLTVAENIAFGLRQM------AAEERHLqvqQMLELVHLSGFGDRYPHQLSGGQQQRVAIARSLAYKPDLL 158
Cdd:cd03262   81 VFQQFNLFPHLTVLENITLAPIKVkgmskaEAEERAL---ELLEKVGLADKADAYPAQLSGGQQQRVAIARALAMNPKVM 157

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 521099586 159 LLDEPFSNIDTQvrhdLIGEIRKIFK---KQGVTAIFVTHsrEEAFA--FADKMAVMNHGVI 215
Cdd:cd03262  158 LFDEPTSALDPE----LVGEVLDVMKdlaEEGMTMVVVTH--EMGFAreVADRVIFMDDGRI 213

FtsE

COG2884

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

5-198

6.30e-64

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

Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 202.20 E-value: 6.30e-64

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099586   5 LSIQNLTCQYDT-QTVLESLSLNVEHGEIVCLLGASGCGKTTLLKAIAGLLPLSSGIMSLNGMTIDDGKHW-LAPEQRNI 82
Cdd:COG2884    2 IRFENVSKRYPGgREALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLVNGQDLSRLKRReIPYLRRRI 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099586  83 GMIFQDYALFPHLTVAENIAFGLRQMAAEERHLQ--VQQMLELVHLSGFGDRYPHQLSGGQQQRVAIARSLAYKPDLLLL 160
Cdd:COG2884   82 GVVFQDFRLLPDRTVYENVALPLRVTGKSRKEIRrrVREVLDLVGLSDKAKALPHELSGGEQQRVAIARALVNRPELLLA 161

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 521099586 161 DEPFSNIDtqvrHDLIGEIRKIFK---KQGVTAIFVTHSRE 198
Cdd:COG2884  162 DEPTGNLD----PETSWEIMELLEeinRRGTTVLIATHDLE 198

GsiA

COG1123

ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ...

1-228

1.42e-63

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: 210.14 E-value: 1.42e-63

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099586   1 MSCALSIQNLTCQY--DTQTVLESLSLNVEHGEIVCLLGASGCGKTTLLKAIAGLLPLS---SGIMSLNGMTIDDGKHWL 75
Cdd:COG1123    1 MTPLLEVRDLSVRYpgGDVPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGLLPHGgriSGEVLLDGRDLLELSEAL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099586  76 ApeQRNIGMIFQD--YALFPhLTVAENIAFGLR--QMAAEERHLQVQQMLELVHLSGFGDRYPHQLSGGQQQRVAIARSL 151
Cdd:COG1123   81 R--GRRIGMVFQDpmTQLNP-VTVGDQIAEALEnlGLSRAEARARVLELLEAVGLERRLDRYPHQLSGGQRQRVAIAMAL 157

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 521099586 152 AYKPDLLLLDEPFSNIDTQVRHDLIGEIRKIFKKQGVTAIFVTHSREEAFAFADKMAVMNHGVIEQYGTASELYYRP 228
Cdd:COG1123  158 ALDPDLLIADEPTTALDVTTQAEILDLLRELQRERGTTVLLITHDLGVVAEIADRVVVMDDGRIVEDGPPEEILAAP 234

ABC_NikE_OppD_transporters

cd03257

ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ...

5-217

4.18e-63

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: 200.42 E-value: 4.18e-63

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099586   5 LSIQNLTCQYDTQ----TVLESLSLNVEHGEIVCLLGASGCGKTTLLKAIAGLLPLSSGIMSLNGMTIDD-GKHWLAPEQ 79
Cdd:cd03257    2 LEVKNLSVSFPTGggsvKALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGKDLLKlSRRLRKIRR 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099586  80 RNIGMIFQDY--ALFPHLTVAENIAFGLR----QMAAEERHLQVQQMLELVHLS-GFGDRYPHQLSGGQQQRVAIARSLA 152
Cdd:cd03257   82 KEIQMVFQDPmsSLNPRMTIGEQIAEPLRihgkLSKKEARKEAVLLLLVGVGLPeEVLNRYPHELSGGQRQRVAIARALA 161

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 521099586 153 YKPDLLLLDEPFSNIDTQVRHDLIGEIRKIFKKQGVTAIFVTHSREEAFAFADKMAVMNHG-VIEQ 217
Cdd:cd03257  162 LNPKLLIADEPTSALDVSVQAQILDLLKKLQEELGLTLLFITHDLGVVAKIADRVAVMYAGkIVEE 227

proV

TIGR01186

glycine betaine/L-proline transport ATP binding subunit; This model describes the glycine ...

22-295

5.32e-63

glycine betaine/L-proline transport ATP binding subunit; This model describes the glycine betaine/L-proline ATP binding subunit in bacteria and its equivalents in archaea. This transport system belong to the larger ATP-Binding Cassette (ABC) transporter superfamily. The characteristic feature of these transporter is the obligatory coupling of ATP hydrolysis to substrate translocation. The minimal configuration of bacterial ABC transport system: an ATPase or ATP binding subunit; An integral membrane protein; a hydrophilic polypetpide, which likely functions as substrate binding protein. Functionally, this transport system is involved in osmoregulation. Under conditions of stress, the organism recruits these transport system to accumulate glycine betaine and other solutes which offer osmo-protection. It has been demonstrated that glycine betaine uptake is accompanied by symport with sodium ions. The locus has been named variously as proU or opuA. A gene library from L.lactis functionally complements an E.coli proU mutant. The comlementing locus is similar to a opuA locus in B.sutlis. This clarifies the differences in nomenclature. [Transport and binding proteins, Amino acids, peptides and amines]

Pssm-ID: 130254 [Multi-domain] Cd Length: 363 Bit Score: 204.32 E-value: 5.32e-63

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099586   22 SLSLNVEHGEIVCLLGASGCGKTTLLKAIAGLLPLSSGIMSLNG---MTIDDGKhWLAPEQRNIGMIFQDYALFPHLTVA 98
Cdd:TIGR01186  11 DADLAIAKGEIFVIMGLSGSGKSTTVRMLNRLIEPTAGQIFIDGeniMKQSPVE-LREVRRKKIGMVFQQFALFPHMTIL 89

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099586   99 ENIAFG--LRQMAAEERHLQVQQMLELVHLSGFGDRYPHQLSGGQQQRVAIARSLAYKPDLLLLDEPFSNIDTQVRHDLI 176
Cdd:TIGR01186  90 QNTSLGpeLLGWPEQERKEKALELLKLVGLEEYEHRYPDELSGGMQQRVGLARALAAEPDILLMDEAFSALDPLIRDSMQ 169

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099586  177 GEIRKIFKKQGVTAIFVTHSREEAFAFADKMAVMNHGVIEQYGTASELYYRPSSKFVADFLGGGSyLPATRLAEHQYQ-T 255
Cdd:TIGR01186 170 DELKKLQATLQKTIVFITHDLDEAIRIGDRIVIMKAGEIVQVGTPDEILRNPANEYVEEFIGKVD-LSQVFDAERIAQrM 248

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|.
gi 521099586  256 PLGVVDAYAQQSIAQGSQcelLLRPQQI-SIYADEESSVTV 295
Cdd:TIGR01186 249 NTGPITKTADKGPRSALQ---LMRDERVdSLYVVDRQNKLV 286

TauB

COG4525

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

1-210

8.25e-63

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

Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 200.86 E-value: 8.25e-63

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099586   1 MScALSIQNLTCQYD----TQTVLESLSLNVEHGEIVCLLGASGCGKTTLLKAIAGLLPLSSGIMSLNGMTIDdgkhwlA 76
Cdd:COG4525    1 MS-MLTVRHVSVRYPgggqPQPALQDVSLTIESGEFVVALGASGCGKTTLLNLIAGFLAPSSGEITLDGVPVT------G 73

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099586  77 PEQRNiGMIFQDYALFPHLTVAENIAFGLR--QMAAEERHLQVQQMLELVHLSGFGDRYPHQLSGGQQQRVAIARSLAYK 154
Cdd:COG4525   74 PGADR-GVVFQKDALLPWLNVLDNVAFGLRlrGVPKAERRARAEELLALVGLADFARRRIWQLSGGMRQRVGIARALAAD 152

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 521099586 155 PDLLLLDEPFSNIDTQVRHDLIGEIRKIFKKQGVTAIFVTHSREEAFAFADKMAVM 210
Cdd:COG4525  153 PRFLLMDEPFGALDALTREQMQELLLDVWQRTGKGVFLITHSVEEALFLATRLVVM 208

FepC

COG1120

ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ...

4-224

5.72e-62

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: 198.34 E-value: 5.72e-62

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099586   4 ALSIQNLTCQYDTQTVLESLSLNVEHGEIVCLLGASGCGKTTLLKAIAGLLPLSSGIMSLNGMTIDDgkhwLAPEQ--RN 81
Cdd:COG1120    1 MLEAENLSVGYGGRPVLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDGRDLAS----LSRRElaRR 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099586  82 IGMIFQDYALFPHLTVAENIAFG-------LRQMAAEERHLqVQQMLELVHLSGFGDRYPHQLSGGQQQRVAIARSLAYK 154
Cdd:COG1120   77 IAYVPQEPPAPFGLTVRELVALGryphlglFGRPSAEDREA-VEEALERTGLEHLADRPVDELSGGERQRVLIARALAQE 155

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099586 155 PDLLLLDEPFSNIDTQVRHDLIGEIRKIFKKQGVTAIFVTHSREEAFAFADKMAVMNHGVIEQYGTASEL 224
Cdd:COG1120  156 PPLLLLDEPTSHLDLAHQLEVLELLRRLARERGRTVVMVLHDLNLAARYADRLVLLKDGRIVAQGPPEEV 225

ZnuC

COG1121

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

1-223

5.67e-61

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

Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 195.31 E-value: 5.67e-61

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099586   1 MSCALSIQNLTCQYDTQTVLESLSLNVEHGEIVCLLGASGCGKTTLLKAIAGLLPLSSGIMSLNGMTIDDGKHWLA--PE 78
Cdd:COG1121    3 MMPAIELENLTVSYGGRPVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLFGKPPRRARRRIGyvPQ 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099586  79 QRNIGmifqdyALFPhLTVAENIA------FGLRQMAAEERHLQVQQMLELVHLSGFGDRYPHQLSGGQQQRVAIARSLA 152
Cdd:COG1121   83 RAEVD------WDFP-ITVRDVVLmgrygrRGLFRRPSRADREAVDEALERVGLEDLADRPIGELSGGQQQRVLLARALA 155

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 521099586 153 YKPDLLLLDEPFSNIDTQVRHDLIGEIRKIfKKQGVTAIFVTHSREEAFAFADKMAVMNHGVIEqYGTASE 223
Cdd:COG1121  156 QDPDLLLLDEPFAGVDAATEEALYELLREL-RREGKTILVVTHDLGAVREYFDRVLLLNRGLVA-HGPPEE 224

ABC_MetN_methionine_transporter

cd03258

ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ...

5-229

6.62e-60

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: 192.41 E-value: 6.62e-60

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099586   5 LSIQNLTCQYDTQ----TVLESLSLNVEHGEIVCLLGASGCGKTTLLKAIAGLLPLSSGIMSLNGMTIDD-GKHWLAPEQ 79
Cdd:cd03258    2 IELKNVSKVFGDTggkvTALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGSVLVDGTDLTLlSGKELRKAR 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099586  80 RNIGMIFQDYALFPHLTVAENIAFGLR--QMAAEERHLQVQQMLELVHLSGFGDRYPHQLSGGQQQRVAIARSLAYKPDL 157
Cdd:cd03258   82 RRIGMIFQHFNLLSSRTVFENVALPLEiaGVPKAEIEERVLELLELVGLEDKADAYPAQLSGGQKQRVGIARALANNPKV 161

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 521099586 158 LLLDEPFSNIDTQVRHDLIGEIRKIFKKQGVTAIFVTHSREEAFAFADKMAVMNHGVIEQYGTASELYYRPS 229
Cdd:cd03258  162 LLCDEATSALDPETTQSILALLRDINRELGLTIVLITHEMEVVKRICDRVAVMEKGEVVEEGTVEEVFANPQ 233

glnQ

PRK09493

glutamine ABC transporter ATP-binding protein GlnQ;

8-237

1.09e-58

glutamine ABC transporter ATP-binding protein GlnQ;

Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 189.53 E-value: 1.09e-58

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099586   8 QNLTCQYDTQTVLESLSLNVEHGEIVCLLGASGCGKTTLLKAIAGLLPLSSGIMSLNGMTIDDGKhwlaPEQRNI----G 83
Cdd:PRK09493   5 KNVSKHFGPTQVLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGLKVNDPK----VDERLIrqeaG 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099586  84 MIFQDYALFPHLTVAENIAFG---LRQMAAEERHLQVQQMLELVHLSGFGDRYPHQLSGGQQQRVAIARSLAYKPDLLLL 160
Cdd:PRK09493  81 MVFQQFYLFPHLTALENVMFGplrVRGASKEEAEKQARELLAKVGLAERAHHYPSELSGGQQQRVAIARALAVKPKLMLF 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099586 161 DEPFSNIDTQVRHdligEIRKIFK---KQGVTAIFVTHsrEEAFA--FADKMAVMNHGVIEQYGTASELYYRPSSKFVAD 235
Cdd:PRK09493 161 DEPTSALDPELRH----EVLKVMQdlaEEGMTMVIVTH--EIGFAekVASRLIFIDKGRIAEDGDPQVLIKNPPSQRLQE 234


                 ..
gi 521099586 236 FL 237
Cdd:PRK09493 235 FL 236

ECF_ATPase_1

TIGR04520

energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ...

5-229

3.02e-58

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: 189.18 E-value: 3.02e-58

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099586    5 LSIQNLTCQYDTQT--VLESLSLNVEHGEIVCLLGASGCGKTTLLKAIAGLLPLSSGIMSLNGM-TIDDGKHWLApeQRN 81
Cdd:TIGR04520   1 IEVENVSFSYPESEkpALKNVSLSIEKGEFVAIIGHNGSGKSTLAKLLNGLLLPTSGKVTVDGLdTLDEENLWEI--RKK 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099586   82 IGMIFQDyalfPH-----LTVAENIAFGL--RQMAAEERHLQVQQMLELVHLSGFGDRYPHQLSGGQQQRVAIARSLAYK 154
Cdd:TIGR04520  79 VGMVFQN----PDnqfvgATVEDDVAFGLenLGVPREEMRKRVDEALKLVGMEDFRDREPHLLSGGQKQRVAIAGVLAMR 154

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 521099586  155 PDLLLLDEPFSNIDTQVRHDLIGEIRKIFKKQGVTAIFVTHSREEAfAFADKMAVMNHGVIEQYGTASELYYRPS 229
Cdd:TIGR04520 155 PDIIILDEATSMLDPKGRKEVLETIRKLNKEEGITVISITHDMEEA-VLADRVIVMNKGKIVAEGTPREIFSQVE 228

ECF_ATPase_2

TIGR04521

energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ...

5-225

2.30e-57

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: 187.27 E-value: 2.30e-57

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099586    5 LSIQNLTCQYDTQT-----VLESLSLNVEHGEIVCLLGASGCGKTTLLKAIAGLLPLSSGIMSLNGMTIDDGKHW-LAPE 78
Cdd:TIGR04521   1 IKLKNVSYIYQPGTpfekkALDDVSLTIEDGEFVAIIGHTGSGKSTLIQHLNGLLKPTSGTVTIDGRDITAKKKKkLKDL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099586   79 QRNIGMIFQ--DYALFpHLTVAENIAFGLRQM--AAEERHLQVQQMLELVHLS-GFGDRYPHQLSGGQQQRVAIARSLAY 153
Cdd:TIGR04521  81 RKKVGLVFQfpEHQLF-EETVYKDIAFGPKNLglSEEEAEERVKEALELVGLDeEYLERSPFELSGGQMRRVAIAGVLAM 159

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 521099586  154 KPDLLLLDEPFSNIDTQVRHDLIGEIRKIFKKQGVTAIFVTHSREEAFAFADKMAVMNHGVIEQYGTASELY 225
Cdd:TIGR04521 160 EPEVLILDEPTAGLDPKGRKEILDLFKRLHKEKGLTVILVTHSMEDVAEYADRVIVMHKGKIVLDGTPREVF 231

NatA

COG4555

ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ...

5-224

6.55e-57

ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, Inorganic ion transport and metabolism];

Pssm-ID: 443618 [Multi-domain] Cd Length: 243 Bit Score: 184.68 E-value: 6.55e-57

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099586   5 LSIQNLTCQYDTQTVLESLSLNVEHGEIVCLLGASGCGKTTLLKAIAGLLPLSSGIMSLNGmtiDDGKHWLAPEQRNIGM 84
Cdd:COG4555    2 IEVENLSKKYGKVPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIDG---EDVRKEPREARRQIGV 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099586  85 IFQDYALFPHLTVAENIAF--GLRQMAAEERHLQVQQMLELVHLSGFGDRYPHQLSGGQQQRVAIARSLAYKPDLLLLDE 162
Cdd:COG4555   79 LPDERGLYDRLTVRENIRYfaELYGLFDEELKKRIEELIELLGLEEFLDRRVGELSTGMKKKVALARALVHDPKVLLLDE 158

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 521099586 163 PFSNIDTQVRHDLIGEIRKiFKKQGVTAIFVTHSREEAFAFADKMAVMNHGVIEQYGTASEL 224
Cdd:COG4555  159 PTNGLDVMARRLLREILRA-LKKEGKTVLFSSHIMQEVEALCDRVVILHKGKVVAQGSLDEL 219

AbcC

COG1135

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

5-238

2.71e-56

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

Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 186.44 E-value: 2.71e-56

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099586   5 LSIQNLTCQYDTQ----TVLESLSLNVEHGEIVCLLGASGCGKTTLLKAIAGLLPLSSGIMSLNGMTIDD-GKHWLAPEQ 79
Cdd:COG1135    2 IELENLSKTFPTKggpvTALDDVSLTIEKGEIFGIIGYSGAGKSTLIRCINLLERPTSGSVLVDGVDLTAlSERELRAAR 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099586  80 RNIGMIFQDYALFPHLTVAENIAFGLRQ--MAAEERHLQVQQMLELVHLSGFGDRYPHQLSGGQQQRVAIARSLAYKPDL 157
Cdd:COG1135   82 RKIGMIFQHFNLLSSRTVAENVALPLEIagVPKAEIRKRVAELLELVGLSDKADAYPSQLSGGQKQRVGIARALANNPKV 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099586 158 LLLDEPFSNIDTQVRHDLIGEIRKIFKKQGVTAIFVTHSREEAFAFADKMAVMNHGVIEQYGTASELYYRPSSKFVADFL 237
Cdd:COG1135  162 LLCDEATSALDPETTRSILDLLKDINRELGLTIVLITHEMDVVRRICDRVAVLENGRIVEQGPVLDVFANPQSELTRRFL 241


                 .
gi 521099586 238 G 238
Cdd:COG1135  242 P 242

ABC_DR_subfamily_A

cd03230

ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ...

5-215

2.04e-55

ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily A; This family of ATP-binding proteins belongs to a multi-subunit transporter involved in drug resistance (BcrA and DrrA), nodulation, lipid transport, and lantibiotic immunity. In bacteria and archaea, these transporters usually include an ATP-binding protein and one or two integral membrane proteins. Eukaryotic systems of the ABCA subfamily display ABC domains that are quite similar to this family. The ATP-binding domain shows the highest similarity between all members of the ABC transporter family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.

Pssm-ID: 213197 [Multi-domain] Cd Length: 173 Bit Score: 178.75 E-value: 2.04e-55

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099586   5 LSIQNLTCQYDTQTVLESLSLNVEHGEIVCLLGASGCGKTTLLKAIAGLLPLSSGIMSLNGMTIDDGKHWLapeQRNIGM 84
Cdd:cd03230    1 IEVRNLSKRYGKKTALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVLGKDIKKEPEEV---KRRIGY 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099586  85 IFQDYALFPHLTVAENIafglrqmaaeerhlqvqqmlelvhlsgfgdryphQLSGGQQQRVAIARSLAYKPDLLLLDEPF 164
Cdd:cd03230   78 LPEEPSLYENLTVRENL----------------------------------KLSGGMKQRLALAQALLHDPELLILDEPT 123

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 521099586 165 SNIDTQVRHDLIGEIRKIfKKQGVTAIFVTHSREEAFAFADKMAVMNHGVI 215
Cdd:cd03230  124 SGLDPESRREFWELLREL-KKEGKTILLSSHILEEAERLCDRVAILNNGRI 173

CcmA

COG4133

ABC-type transport system involved in cytochrome c biogenesis, ATPase component ...

5-200

2.19e-55

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: 179.60 E-value: 2.19e-55

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099586   5 LSIQNLTCQYDTQTVLESLSLNVEHGEIVCLLGASGCGKTTLLKAIAGLLPLSSGIMSLNGMTIDDGKhwlAPEQRNIGM 84
Cdd:COG4133    3 LEAENLSCRRGERLLFSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWNGEPIRDAR---EDYRRRLAY 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099586  85 IFQDYALFPHLTVAENIAFGLRQMAAEERHLQVQQMLELVHLSGFGDRYPHQLSGGQQQRVAIARSLAYKPDLLLLDEPF 164
Cdd:COG4133   80 LGHADGLKPELTVRENLRFWAALYGLRADREAIDEALEAVGLAGLADLPVRQLSAGQKRRVALARLLLSPAPLWLLDEPF 159

                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 521099586 165 SNIDTQVRHDLIGEIRKiFKKQGVTAIFVTHSREEA 200
Cdd:COG4133  160 TALDAAGVALLAELIAA-HLARGGAVLLTTHQPLEL 194

ABC_PstB_phosphate_transporter

cd03260

ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ...

5-224

5.70e-55

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: 179.30 E-value: 5.70e-55

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099586   5 LSIQNLTCQYDTQTVLESLSLNVEHGEIVCLLGASGCGKTTLLKAIAGLLPL-----SSGIMSLNGMTIDDGKHWLAPEQ 79
Cdd:cd03260    1 IELRDLNVYYGDKHALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRLNDLipgapDEGEVLLDGKDIYDLDVDVLELR 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099586  80 RNIGMIFQDYALFPhLTVAENIAFGLRQMA---AEERHLQVQQMLELVHLSG-FGDR-YPHQLSGGQQQRVAIARSLAYK 154
Cdd:cd03260   81 RRVGMVFQKPNPFP-GSIYDNVAYGLRLHGiklKEELDERVEEALRKAALWDeVKDRlHALGLSGGQQQRLCLARALANE 159

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 521099586 155 PDLLLLDEPFSNID---TQVRHDLIGEIRKifkkqGVTAIFVTHSREEAFAFADKMAVMNHGVIEQYGTASEL 224
Cdd:cd03260  160 PEVLLLDEPTSALDpisTAKIEELIAELKK-----EYTIVIVTHNMQQAARVADRTAFLLNGRLVEFGPTEQI 227

DppD

COG0444

ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ...

5-228

7.69e-55

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: 181.79 E-value: 7.69e-55

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099586   5 LSIQNLTCQYDTQ----TVLESLSLNVEHGEIVCLLGASGCGKTTLLKAIAGLLP---LSSGIMSLNGMTIDDgkhwLAP 77
Cdd:COG0444    2 LEVRNLKVYFPTRrgvvKAVDGVSFDVRRGETLGLVGESGSGKSTLARAILGLLPppgITSGEILFDGEDLLK----LSE 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099586  78 EQ------RNIGMIFQD-Y-ALFPHLTVAENIAFGLRQ---MAAEERHLQVQQMLELVHLSG---FGDRYPHQLSGGQQQ 143
Cdd:COG0444   78 KElrkirgREIQMIFQDpMtSLNPVMTVGDQIAEPLRIhggLSKAEARERAIELLERVGLPDperRLDRYPHELSGGMRQ 157

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099586 144 RVAIARSLAYKPDLLLLDEPFSNIDTQVRHDLIGEIRKIFKKQGVTAIFVTHSREEAFAFADKMAVMNHGVIEQYGTASE 223
Cdd:COG0444  158 RVMIARALALEPKLLIADEPTTALDVTIQAQILNLLKDLQRELGLAILFITHDLGVVAEIADRVAVMYAGRIVEEGPVEE 237


                 ....*
gi 521099586 224 LYYRP 228
Cdd:COG0444  238 LFENP 242

PhnC

COG3638

ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and ...

4-224

8.32e-55

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

Pssm-ID: 442855 [Multi-domain] Cd Length: 249 Bit Score: 179.48 E-value: 8.32e-55

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099586   4 ALSIQNLTCQYDTQT-VLESLSLNVEHGEIVCLLGASGCGKTTLLKAIAGLLPLSSGIMSLNGMTIDDGKH-WLAPEQRN 81
Cdd:COG3638    2 MLELRNLSKRYPGGTpALDDVSLEIERGEFVALIGPSGAGKSTLLRCLNGLVEPTSGEILVDGQDVTALRGrALRRLRRR 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099586  82 IGMIFQDYALFPHLTVAENIAFG-----------LRQMAAEERHlQVQQMLELVHLSGFGDRYPHQLSGGQQQRVAIARS 150
Cdd:COG3638   82 IGMIFQQFNLVPRLSVLTNVLAGrlgrtstwrslLGLFPPEDRE-RALEALERVGLADKAYQRADQLSGGQQQRVAIARA 160

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 521099586 151 LAYKPDLLLLDEPFSNIDTQVRHDLIGEIRKIFKKQGVTAIFVTHSREEAFAFADKMAVMNHGVIEQYGTASEL 224
Cdd:COG3638  161 LVQEPKLILADEPVASLDPKTARQVMDLLRRIAREDGITVVVNLHQVDLARRYADRIIGLRDGRVVFDGPPAEL 234

FetA

COG4619

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

5-215

5.75e-54

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

Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 176.16 E-value: 5.75e-54

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099586   5 LSIQNLTCQYDTQTVLESLSLNVEHGEIVCLLGASGCGKTTLLKAIAGLLPLSSGIMSLNGMTIDDgkhwLAPEQ--RNI 82
Cdd:COG4619    1 LELEGLSFRVGGKPILSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIYLDGKPLSA----MPPPEwrRQV 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099586  83 GMIFQDYALFPHlTVAENIAFGLRQMAAEERHLQVQQMLELVHLS-GFGDRYPHQLSGGQQQRVAIARSLAYKPDLLLLD 161
Cdd:COG4619   77 AYVPQEPALWGG-TVRDNLPFPFQLRERKFDRERALELLERLGLPpDILDKPVERLSGGERQRLALIRALLLQPDVLLLD 155

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 521099586 162 EPFSNIDTQVRHDLIGEIRKIFKKQGVTAIFVTHSREEAFAFADKMAVMNHGVI 215
Cdd:COG4619  156 EPTSALDPENTRRVEELLREYLAEEGRAVLWVSHDPEQIERVADRVLTLEAGRL 209

ntrCD

TIGR01184

nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ...

20-228

1.26e-53

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: 176.12 E-value: 1.26e-53

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099586   20 LESLSLNVEHGEIVCLLGASGCGKTTLLKAIAGLLPLSSGIMSLNGMTIDDGkhwlAPEQRnigMIFQDYALFPHLTVAE 99
Cdd:TIGR01184   1 LKGVNLTIQQGEFISLIGHSGCGKSTLLNLISGLAQPTSGGVILEGKQITEP----GPDRM---VVFQNYSLLPWLTVRE 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099586  100 NIAFG----LRQMAAEERHLQVQQMLELVHLSGFGDRYPHQLSGGQQQRVAIARSLAYKPDLLLLDEPFSNIDTQVRHDL 175
Cdd:TIGR01184  74 NIALAvdrvLPDLSKSERRAIVEEHIALVGLTEAADKRPGQLSGGMKQRVAIARALSIRPKVLLLDEPFGALDALTRGNL 153

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 521099586  176 IGEIRKIFKKQGVTAIFVTHSREEAFAFADKMAVMNHGVIEQYGTASEL-YYRP 228
Cdd:TIGR01184 154 QEELMQIWEEHRVTVLMVTHDVDEALLLSDRVVMLTNGPAANIGQILEVpFPRP 207

modC_ABC

TIGR02142

molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ...

23-334

1.02e-52

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: 177.61 E-value: 1.02e-52

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099586   23 LSLNVEHGEIVCLLGASGCGKTTLLKAIAGLLPLSSGIMSLNGMTIDDG--KHWLAPEQRNIGMIFQDYALFPHLTVAEN 100
Cdd:TIGR02142  16 ADFTLPGQGVTAIFGRSGSGKTTLIRLIAGLTRPDEGEIVLNGRTLFDSrkGIFLPPEKRRIGYVFQEARLFPHLSVRGN 95

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099586  101 IAFGLRQMAAEERHLQVQQMLELVHLSGFGDRYPHQLSGGQQQRVAIARSLAYKPDLLLLDEPFSNIDTQVRHDLIGEIR 180
Cdd:TIGR02142  96 LRYGMKRARPSERRISFERVIELLGIGHLLGRLPGRLSGGEKQRVAIGRALLSSPRLLLMDEPLAALDDPRKYEILPYLE 175

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099586  181 KIFKKQGVTAIFVTHSREEAFAFADKMAVMNHGVIEQYGTASELYYRPSSKFVAdFLGGGSYLPATRLAEHQ----YQTP 256
Cdd:TIGR02142 176 RLHAEFGIPILYVSHSLQEVLRLADRVVVLEDGRVAAAGPIAEVWASPDLPWLA-REDQGSLIEGVVAEHDQhyglTALR 254

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099586  257 LGVVDAYAQQSIAQ-GSQCELLL----------RPQQISIYADEESSVTVLEQQFMGdHCRYVIDAHGSKLLATSSR--- 322
Cdd:TIGR02142 255 LGGGHLWVPENLGPtGARLRLRVpardvslalqKPEATSIRNILPARVVEIEDSDIG-RVGVVLESGGKTLWARITRwar 333

                         330
                  ....*....|....*
gi 521099586  323 ---GLAVGQTVAVSI 334
Cdd:TIGR02142 334 delGIAPGTPVFAQI 348

cbiO

PRK13635

energy-coupling factor ABC transporter ATP-binding protein;

5-225

2.38e-52

energy-coupling factor ABC transporter ATP-binding protein;

Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 174.43 E-value: 2.38e-52

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099586   5 LSIQNLTCQYDTQT--VLESLSLNVEHGEIVCLLGASGCGKTTLLKAIAGLLPLSSGIMSLNGMTIDDGKHWLApeQRNI 82
Cdd:PRK13635   6 IRVEHISFRYPDAAtyALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGGMVLSEETVWDV--RRQV 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099586  83 GMIFQDY-ALFPHLTVAENIAFGL--RQMAAEERHLQVQQMLELVHLSGFGDRYPHQLSGGQQQRVAIARSLAYKPDLLL 159
Cdd:PRK13635  84 GMVFQNPdNQFVGATVQDDVAFGLenIGVPREEMVERVDQALRQVGMEDFLNREPHRLSGGQKQRVAIAGVLALQPDIII 163

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 521099586 160 LDEPFSNIDTQVRHDLIGEIRKIFKKQGVTAIFVTHSREEAfAFADKMAVMNHGVIEQYGTASELY 225
Cdd:PRK13635 164 LDEATSMLDPRGRREVLETVRQLKEQKGITVLSITHDLDEA-AQADRVIVMNKGEILEEGTPEEIF 228

ABC_Metallic_Cations

cd03235

ATP-binding cassette domain of the metal-type transporters; This family includes transporters ...

6-215

3.52e-52

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: 171.56 E-value: 3.52e-52

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099586   6 SIQNLTCQYDTQTVLESLSLNVEHGEIVCLLGASGCGKTTLLKAIAGLLPLSSGIMSLNGMTIDDGKHWLA--PEQRNIg 83
Cdd:cd03235    1 EVEDLTVSYGGHPVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFGKPLEKERKRIGyvPQRRSI- 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099586  84 mifqDYAlFPhLTVAENIAFGL-------RQMAAEERHLqVQQMLELVHLSGFGDRYPHQLSGGQQQRVAIARSLAYKPD 156
Cdd:cd03235   80 ----DRD-FP-ISVRDVVLMGLyghkglfRRLSKADKAK-VDEALERVGLSELADRQIGELSGGQQQRVLLARALVQDPD 152

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 521099586 157 LLLLDEPFSNIDTQVRHDLIGEIRKIfKKQGVTAIFVTHSREEAFAFADKMAVMNHGVI 215
Cdd:cd03235  153 LLLLDEPFAGVDPKTQEDIYELLREL-RREGMTILVVTHDLGLVLEYFDRVLLLNRTVV 210

ABC_TM1139_LivF_branched

cd03224

ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ...

5-224

3.38e-51

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: 169.54 E-value: 3.38e-51

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099586   5 LSIQNLTCQYDTQTVLESLSLNVEHGEIVCLLGASGCGKTTLLKAIAGLLPLSSGIMSLNGMTIDDgkhwLAPEQRN--- 81
Cdd:cd03224    1 LEVENLNAGYGKSQILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDGRDITG----LPPHERArag 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099586  82 IGMIFQDYALFPHLTVAENIAFGLRQMAAEERHLQVQQMLELV-HLSGFGDRYPHQLSGGQQQRVAIARSLAYKPDLLLL 160
Cdd:cd03224   77 IGYVPEGRRIFPELTVEENLLLGAYARRRAKRKARLERVYELFpRLKERRKQLAGTLSGGEQQMLAIARALMSRPKLLLL 156

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 521099586 161 DEPFSNIDTQVRHDLIGEIRKIfKKQGVTAIFVTHSREEAFAFADKMAVMNHGVIEQYGTASEL 224
Cdd:cd03224  157 DEPSEGLAPKIVEEIFEAIREL-RDEGVTILLVEQNARFALEIADRAYVLERGRVVLEGTAAEL 219

ABC_Iron-Siderophores_B12_Hemin

cd03214

ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ...

6-219

3.88e-51

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: 167.61 E-value: 3.88e-51

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099586   6 SIQNLTCQYDTQTVLESLSLNVEHGEIVCLLGASGCGKTTLLKAIAGLLPLSSGIMSLNGmtiddgkhwlapeqrnigmi 85
Cdd:cd03214    1 EVENLSVGYGGRTVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDG-------------------- 60

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099586  86 fQDYALFPHLTVAENIAFglrqmaaeerhlqVQQMLELVHLSGFGDRYPHQLSGGQQQRVAIARSLAYKPDLLLLDEPFS 165
Cdd:cd03214   61 -KDLASLSPKELARKIAY-------------VPQALELLGLAHLADRPFNELSGGERQRVLLARALAQEPPILLLDEPTS 126

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 521099586 166 NIDTQVRHDLIGEIRKIFKKQGVTAIFVTHSREEAFAFADKMAVMNHGVIEQYG 219
Cdd:cd03214  127 HLDIAHQIELLELLRRLARERGKTVVMVLHDLNLAARYADRVILLKDGRIVAQG 180

PRK11264

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

1-239

4.62e-51

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

Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 169.93 E-value: 4.62e-51

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099586   1 MScALSIQNLTCQYDTQTVLESLSLNVEHGEIVCLLGASGCGKTTLLKAIAGLLPLSSGIMSLNGMTIDDGKHwLAPEQR 80
Cdd:PRK11264   1 MS-AIEVKNLVKKFHGQTVLHGIDLEVKPGEVVAIIGPSGSGKTTLLRCINLLEQPEAGTIRVGDITIDTARS-LSQQKG 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099586  81 NI-------GMIFQDYALFPHLTVAENIAFG---LRQMAAEERHLQVQQMLELVHLSGFGDRYPHQLSGGQQQRVAIARS 150
Cdd:PRK11264  79 LIrqlrqhvGFVFQNFNLFPHRTVLENIIEGpviVKGEPKEEATARARELLAKVGLAGKETSYPRRLSGGQQQRVAIARA 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099586 151 LAYKPDLLLLDEPFSNIDTQVRHDLIGEIRKIFKKQGvTAIFVTHsrEEAFA--FADKMAVMNHGVIEQYGTASELYYRP 228
Cdd:PRK11264 159 LAMRPEVILFDEPTSALDPELVGEVLNTIRQLAQEKR-TMVIVTH--EMSFArdVADRAIFMDQGRIVEQGPAKALFADP 235

                        250
                 ....*....|....*
gi 521099586 229 ----SSKFVADFLGG 239
Cdd:PRK11264 236 qqprTRQFLEKFLLQ 250

ABC_ATP_DarD

NF038007

darobactin export ABC transporter ATP-binding protein;

5-213

8.28e-51

darobactin export ABC transporter ATP-binding protein;

Pssm-ID: 411600 [Multi-domain] Cd Length: 218 Bit Score: 168.36 E-value: 8.28e-51

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099586   5 LSIQNLTCQYDTQT----VLESLSLNVEHGEIVCLLGASGCGKTTLLKAIAGLLPLSSGIMSLNGMTIDDGKHW--LAPE 78
Cdd:NF038007   2 LNMQNAEKCYITKTiktkVLNHLNFSVEKGDFVSIMGPSGSGKSTLLNIIGMFDSLDSGSLTLAGKEVTNLSYSqkIILR 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099586  79 QRNIGMIFQDYALFPHLTVAENIAFGL--RQMAAEERHLQVQQMLELVHLSGFGDRYPHQLSGGQQQRVAIARSLAYKPD 156
Cdd:NF038007  82 RELIGYIFQSFNLIPHLSIFDNVALPLkyRGVAKKERIERVNQVLNLFGIDNRRNHKPMQLSGGQQQRVAIARAMVSNPA 161

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 521099586 157 LLLLDEPFSNIDTQVRHDLIGEIRKIfKKQGVTAIFVTHSrEEAFAFADKMAVMNHG 213
Cdd:NF038007 162 LLLADEPTGNLDSKNARAVLQQLKYI-NQKGTTIIMVTHS-DEASTYGNRIINMKDG 216

ABC_PhnC_transporter

cd03256

ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ...

5-224

1.72e-50

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: 168.13 E-value: 1.72e-50

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099586   5 LSIQNLTCQY-DTQTVLESLSLNVEHGEIVCLLGASGCGKTTLLKAIAGLLPLSSGIMSLNGMTIDDGKHWLAPEQR-NI 82
Cdd:cd03256    1 IEVENLSKTYpNGKKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGTDINKLKGKALRQLRrQI 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099586  83 GMIFQDYALFPHLTVAENIAFG----------LRQMAAEERHLQVQQMLELVHLSGFGDRYPHQLSGGQQQRVAIARSLA 152
Cdd:cd03256   81 GMIFQQFNLIERLSVLENVLSGrlgrrstwrsLFGLFPKEEKQRALAALERVGLLDKAYQRADQLSGGQQQRVAIARALM 160

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 521099586 153 YKPDLLLLDEPFSNIDTQVRHDLIGEIRKIFKKQGVTAIFVTHSREEAFAFADKMAVMNHGVIEQYGTASEL 224
Cdd:cd03256  161 QQPKLILADEPVASLDPASSRQVMDLLKRINREEGITVIVSLHQVDLAREYADRIVGLKDGRIVFDGPPAEL 232

ABC_phnC

TIGR02315

phosphonate ABC transporter, ATP-binding protein; Phosphonates are a class of ...

5-225

2.10e-50

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: 168.25 E-value: 2.10e-50

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099586    5 LSIQNLTCQYDTQT-VLESLSLNVEHGEIVCLLGASGCGKTTLLKAIAGLLPLSSGIMSLNGMTI-DDGKHWLAPEQRNI 82
Cdd:TIGR02315   2 LEVENLSKVYPNGKqALKNINLNINPGEFVAIIGPSGAGKSTLLRCINRLVEPSSGSILLEGTDItKLRGKKLRKLRRRI 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099586   83 GMIFQDYALFPHLTVAENIAFG-----------LRQMAAEERHLQVQqMLELVHLSGFGDRYPHQLSGGQQQRVAIARSL 151
Cdd:TIGR02315  82 GMIFQHYNLIERLTVLENVLHGrlgykptwrslLGRFSEEDKERALS-ALERVGLADKAYQRADQLSGGQQQRVAIARAL 160

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 521099586  152 AYKPDLLLLDEPFSNID----TQVRHDLigeiRKIFKKQGVTAIFVTHSREEAFAFADKMAVMNHGVIEQYGTASELY 225
Cdd:TIGR02315 161 AQQPDLILADEPIASLDpktsKQVMDYL----KRINKEDGITVIINLHQVDLAKKYADRIVGLKAGEIVFDGAPSELD 234

cbiO

PRK13637

energy-coupling factor transporter ATPase;

1-225

3.13e-50

energy-coupling factor transporter ATPase;

Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 169.07 E-value: 3.13e-50

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099586   1 MScaLSIQNLTCQYDTQTVLESLSLN-----VEHGEIVCLLGASGCGKTTLLKAIAGLLPLSSGIMSLNGMTIDDGKHWL 75
Cdd:PRK13637   1 MS--IKIENLTHIYMEGTPFEKKALDnvnieIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDGVDITDKKVKL 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099586  76 APEQRNIGMIFQ--DYALFPHlTVAENIAFGLRQM--AAEERHLQVQQMLELVHLS--GFGDRYPHQLSGGQQQRVAIAR 149
Cdd:PRK13637  79 SDIRKKVGLVFQypEYQLFEE-TIEKDIAFGPINLglSEEEIENRVKRAMNIVGLDyeDYKDKSPFELSGGQKRRVAIAG 157

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 521099586 150 SLAYKPDLLLLDEPFSNIDTQVRHDLIGEIRKIFKKQGVTAIFVTHSREEAFAFADKMAVMNHGVIEQYGTASELY 225
Cdd:PRK13637 158 VVAMEPKILILDEPTAGLDPKGRDEILNKIKELHKEYNMTIILVSHSMEDVAKLADRIIVMNKGKCELQGTPREVF 233

thiQ

PRK10771

thiamine ABC transporter ATP-binding protein ThiQ;

5-224

1.20e-49

thiamine ABC transporter ATP-binding protein ThiQ;

Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 165.91 E-value: 1.20e-49

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099586   5 LSIQNLTCQYDTQTVleSLSLNVEHGEIVCLLGASGCGKTTLLKAIAGLLPLSSGIMSLNGmtiDDGKHwLAPEQRNIGM 84
Cdd:PRK10771   2 LKLTDITWLYHHLPM--RFDLTVERGERVAILGPSGAGKSTLLNLIAGFLTPASGSLTLNG---QDHTT-TPPSRRPVSM 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099586  85 IFQDYALFPHLTVAENIAFGLR---QMAAEERHlQVQQMLELVHLSGFGDRYPHQLSGGQQQRVAIARSLAYKPDLLLLD 161
Cdd:PRK10771  76 LFQENNLFSHLTVAQNIGLGLNpglKLNAAQRE-KLHAIARQMGIEDLLARLPGQLSGGQRQRVALARCLVREQPILLLD 154

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 521099586 162 EPFSNIDTQVRHDLIGEIRKIFKKQGVTAIFVTHSREEAFAFADKMAVMNHGVIEQYGTASEL 224
Cdd:PRK10771 155 EPFSALDPALRQEMLTLVSQVCQERQLTLLMVSHSLEDAARIAPRSLVVADGRIAWDGPTDEL 217

ABC_subfamily_A

cd03263

ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ...

5-224

1.59e-49

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: 164.99 E-value: 1.59e-49

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099586   5 LSIQNLTCQY--DTQTVLESLSLNVEHGEIVCLLGASGCGKTTLLKAIAGLLPLSSGIMSLNGMTIDDGKHWLapeQRNI 82
Cdd:cd03263    1 LQIRNLTKTYkkGTKPAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYINGYSIRTDRKAA---RQSL 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099586  83 GMIFQDYALFPHLTVAENIAF--GLRQMAAEERHLQVQQMLELVHLSGFGDRYPHQLSGGQQQRVAIARSLAYKPDLLLL 160
Cdd:cd03263   78 GYCPQFDALFDELTVREHLRFyaRLKGLPKSEIKEEVELLLRVLGLTDKANKRARTLSGGMKRKLSLAIALIGGPSVLLL 157

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 521099586 161 DEPFSNIDTQVRHDLIGEIRKIfkKQGVTAIFVTHSREEAFAFADKMAVMNHGVIEQYGTASEL 224
Cdd:cd03263  158 DEPTSGLDPASRRAIWDLILEV--RKGRSIILTTHSMDEAEALCDRIAIMSDGKLRCIGSPQEL 219

tauB

PRK11248

taurine ABC transporter ATP-binding subunit;

4-213

3.22e-49

taurine ABC transporter ATP-binding subunit;

Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 165.26 E-value: 3.22e-49

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099586   4 ALSIQNLTCQYDTQTVLESLSLNVEHGEIVCLLGASGCGKTTLLKAIAGLLPLSSGIMSLNGMTIDDgkhwlAPEQRniG 83
Cdd:PRK11248   1 MLQISHLYADYGGKPALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDGKPVEG-----PGAER--G 73

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099586  84 MIFQDYALFPHLTVAENIAFGLR--QMAAEERHLQVQQMLELVHLSGFGDRYPHQLSGGQQQRVAIARSLAYKPDLLLLD 161
Cdd:PRK11248  74 VVFQNEGLLPWRNVQDNVAFGLQlaGVEKMQRLEIAHQMLKKVGLEGAEKRYIWQLSGGQRQRVGIARALAANPQLLLLD 153

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 521099586 162 EPFSNIDTQVRHDLIGEIRKIFKKQGVTAIFVTHSREEAFAFADKMAVMNHG 213
Cdd:PRK11248 154 EPFGALDAFTREQMQTLLLKLWQETGKQVLLITHDIEEAVFMATELVLLSPG 205

ABC_tran

pfam00005

ABC transporter; ABC transporters for a large family of proteins responsible for translocation ...

20-165

6.88e-49

Pssm-ID: 394964 [Multi-domain] Cd Length: 150 Bit Score: 160.89 E-value: 6.88e-49

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099586   20 LESLSLNVEHGEIVCLLGASGCGKTTLLKAIAGLLPLSSGIMSLNGMTIDDGkhWLAPEQRNIGMIFQDYALFPHLTVAE 99
Cdd:pfam00005   1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDLTDD--ERKSLRKEIGYVFQDPQLFPRLTVRE 78

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 521099586  100 NIAFGLRQMAAEERHL--QVQQMLELVHLSGFGDR----YPHQLSGGQQQRVAIARSLAYKPDLLLLDEPFS 165
Cdd:pfam00005  79 NLRLGLLLKGLSKREKdaRAEEALEKLGLGDLADRpvgeRPGTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150

LivG

COG0411

ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ...

1-223

2.14e-48

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: 163.29 E-value: 2.14e-48

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099586   1 MSCALSIQNLTCQYDTQTVLESLSLNVEHGEIVCLLGASGCGKTTLLKAIAGLLPLSSGIMSLNGMTIDDgkhwLAPEQR 80
Cdd:COG0411    1 SDPLLEVRGLTKRFGGLVAVDDVSLEVERGEIVGLIGPNGAGKTTLFNLITGFYRPTSGRILFDGRDITG----LPPHRI 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099586  81 N---IGMIFQDYALFPHLTVAENIA---------------FGLRQMAAEERHL--QVQQMLELVHLSGFGDRYPHQLSGG 140
Cdd:COG0411   77 ArlgIARTFQNPRLFPELTVLENVLvaaharlgrgllaalLRLPRARREEREAreRAEELLERVGLADRADEPAGNLSYG 156

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099586 141 QQQRVAIARSLAYKPDLLLLDEPFSNIDTQVRHDLIGEIRKIFKKQGVTAIFVTHSREEAFAFADKMAVMNHG-VIEQyG 219
Cdd:COG0411  157 QQRRLEIARALATEPKLLLLDEPAAGLNPEETEELAELIRRLRDERGITILLIEHDMDLVMGLADRIVVLDFGrVIAE-G 235


                 ....
gi 521099586 220 TASE 223
Cdd:COG0411  236 TPAE 239

ArtP

COG4161

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

1-237

2.54e-48

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

Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 162.49 E-value: 2.54e-48

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099586   1 MScaLSIQNLTCQYDTQTVLESLSLNVEHGEIVCLLGASGCGKTTLLKAIAGLLPLSSGIMSLNGMTIDDGKHWLAPE-- 78
Cdd:COG4161    1 MS--IQLKNINCFYGSHQALFDINLECPSGETLVLLGPSGAGKSSLLRVLNLLETPDSGQLNIAGHQFDFSQKPSEKAir 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099586  79 --QRNIGMIFQDYALFPHLTVAENI------AFGLRQMAAEERhlqVQQMLELVHLSGFGDRYPHQLSGGQQQRVAIARS 150
Cdd:COG4161   79 llRQKVGMVFQQYNLWPHLTVMENLieapckVLGLSKEQAREK---AMKLLARLRLTDKADRFPLHLSGGQQQRVAIARA 155

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099586 151 LAYKPDLLLLDEPFSNIDTQVRHDlIGEIRKIFKKQGVTAIFVTHSREEAFAFADKMAVMNHGVIEQYGTASeLYYRPSS 230
Cdd:COG4161  156 LMMEPQVLLFDEPTAALDPEITAQ-VVEIIRELSQTGITQVIVTHEVEFARKVASQVVYMEKGRIIEQGDAS-HFTQPQT 233


                 ....*..
gi 521099586 231 KFVADFL 237
Cdd:COG4161  234 EAFAHYL 240

YejF

COG4172

ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ...

5-228

4.32e-48

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: 169.48 E-value: 4.32e-48

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099586   5 LSIQNLTCQYDTQ-----------TVLESLSLNVEHGEIVCLLGASGCGKTTLLKAIAGLLPlSSGIMSLNGMTIDDGKH 73
Cdd:COG4172  276 LEARDLKVWFPIKrglfrrtvghvKAVDGVSLTLRRGETLGLVGESGSGKSTLGLALLRLIP-SEGEIRFDGQDLDGLSR 354

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099586  74 W-LAPEQRNIGMIFQD-YA-LFPHLTVAENIAFGLR----QMAAEERHLQVQQMLELVHLS-GFGDRYPHQLSGGQQQRV 145
Cdd:COG4172  355 RaLRPLRRRMQVVFQDpFGsLSPRMTVGQIIAEGLRvhgpGLSAAERRARVAEALEEVGLDpAARHRYPHEFSGGQRQRI 434

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099586 146 AIARSLAYKPDLLLLDEPFSNIDTQVRHDLIGEIRKIFKKQGVTAIFVTHS----ReeafAFADKMAVMNHG-VIEQyGT 220
Cdd:COG4172  435 AIARALILEPKLLVLDEPTSALDVSVQAQILDLLRDLQREHGLAYLFISHDlavvR----ALAHRVMVMKDGkVVEQ-GP 509


                 ....*...
gi 521099586 221 ASELYYRP 228
Cdd:COG4172  510 TEQVFDAP 517

LivF

COG0410

ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ...

5-224

2.02e-47

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: 160.15 E-value: 2.02e-47

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099586   5 LSIQNLTCQYDTQTVLESLSLNVEHGEIVCLLGASGCGKTTLLKAIAGLLPLSSGIMSLNGMTIDDgkhwLAPEQRN--- 81
Cdd:COG0410    4 LEVENLHAGYGGIHVLHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRSGSIRFDGEDITG----LPPHRIArlg 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099586  82 IGMIFQDYALFPHLTVAENIAFGLRQMAAEERhlqVQQMLELVHlsgfgDRYP------HQ----LSGGQQQRVAIARSL 151
Cdd:COG0410   80 IGYVPEGRRIFPSLTVEENLLLGAYARRDRAE---VRADLERVY-----ELFPrlkerrRQragtLSGGEQQMLAIGRAL 151

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 521099586 152 AYKPDLLLLDEPFSNIDTQVRHDLIGEIRKIfKKQGVTAIFVTHSREEAFAFADKMAVMNHGVIEQYGTASEL 224
Cdd:COG0410  152 MSRPKLLLLDEPSLGLAPLIVEEIFEIIRRL-NREGVTILLVEQNARFALEIADRAYVLERGRIVLEGTAAEL 223

ABC_ATPase

cd00267

ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ...

6-213

3.17e-47

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: 157.02 E-value: 3.17e-47

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099586   6 SIQNLTCQYDTQTVLESLSLNVEHGEIVCLLGASGCGKTTLLKAIAGLLPLSSGIMSLNGmtIDDGKHWLAPEQRNIGMI 85
Cdd:cd00267    1 EIENLSFRYGGRTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDG--KDIAKLPLEELRRRIGYV 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099586  86 FQdyalfphltvaeniafglrqmaaeerhlqvqqmlelvhlsgfgdryphqLSGGQQQRVAIARSLAYKPDLLLLDEPFS 165
Cdd:cd00267   79 PQ-------------------------------------------------LSGGQRQRVALARALLLNPDLLLLDEPTS 109

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*...
gi 521099586 166 NIDTQVRHDLIGEIRKIfKKQGVTAIFVTHSREEAFAFADKMAVMNHG 213
Cdd:cd00267  110 GLDPASRERLLELLREL-AEEGRTVIIVTHDPELAELAADRVIVLKDG 156

artP

PRK11124

arginine transporter ATP-binding subunit; Provisional

4-237

4.08e-47

arginine transporter ATP-binding subunit; Provisional

Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 159.41 E-value: 4.08e-47

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099586   4 ALSIQNLTCQYDTQTVLESLSLNVEHGEIVCLLGASGCGKTTLLKAIAGLLPLSSGIMSLNGMTIDDGKHWLAPE----Q 79
Cdd:PRK11124   2 SIQLNGINCFYGAHQALFDITLDCPQGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLNIAGNHFDFSKTPSDKAirelR 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099586  80 RNIGMIFQDYALFPHLTVAENI---AFGLRQMAAEERHLQVQQMLELVHLSGFGDRYPHQLSGGQQQRVAIARSLAYKPD 156
Cdd:PRK11124  82 RNVGMVFQQYNLWPHLTVQQNLieaPCRVLGLSKDQALARAEKLLERLRLKPYADRFPLHLSGGQQQRVAIARALMMEPQ 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099586 157 LLLLDEPFSNIDTQVRHDLIGEIRKIfKKQGVTAIFVTHSREEAFAFADKMAVMNHGVIEQYGTASElYYRPSSKFVADF 236
Cdd:PRK11124 162 VLLFDEPTAALDPEITAQIVSIIREL-AETGITQVIVTHEVEVARKTASRVVYMENGHIVEQGDASC-FTQPQTEAFKNY 239


                 .
gi 521099586 237 L 237
Cdd:PRK11124 240 L 240

thiQ

TIGR01277

thiamine ABC transporter, ATP-binding protein; This model describes the energy-transducing ...

5-219

7.56e-47

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: 158.10 E-value: 7.56e-47

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099586    5 LSIQNLTCQYDTQTVleSLSLNVEHGEIVCLLGASGCGKTTLLKAIAGLLPLSSGimslnGMTIDDGKHW-LAPEQRNIG 83
Cdd:TIGR01277   1 LALDKVRYEYEHLPM--EFDLNVADGEIVAIMGPSGAGKSTLLNLIAGFIEPASG-----SIKVNDQSHTgLAPYQRPVS 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099586   84 MIFQDYALFPHLTVAENIAFGLR---QMAAEERHlQVQQMLELVHLSGFGDRYPHQLSGGQQQRVAIARSLAYKPDLLLL 160
Cdd:TIGR01277  74 MLFQENNLFAHLTVRQNIGLGLHpglKLNAEQQE-KVVDAAQQVGIADYLDRLPEQLSGGQRQRVALARCLVRPNPILLL 152

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 521099586  161 DEPFSNIDTQVRHDLIGEIRKIFKKQGVTAIFVTHSREEAFAFADKMAVMNHGVIEQYG 219
Cdd:TIGR01277 153 DEPFSALDPLLREEMLALVKQLCSERQRTLLMVTHHLSDARAIASQIAVVSQGKIKVVS 211

SunT

COG2274

ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ...

4-224

8.51e-47

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: 168.47 E-value: 8.51e-47

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099586   4 ALSIQNLTCQY--DTQTVLESLSLNVEHGEIVCLLGASGCGKTTLLKAIAGLLPLSSGIMSLNGMTIDD-GKHWLApeqR 80
Cdd:COG2274  473 DIELENVSFRYpgDSPPVLDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEPTSGRILIDGIDLRQiDPASLR---R 549

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099586  81 NIGMIFQDYALFpHLTVAENIAFGlRQMAAEERhlqVQQMLELVHLSGFGDRYPH-----------QLSGGQQQRVAIAR 149
Cdd:COG2274  550 QIGVVLQDVFLF-SGTIRENITLG-DPDATDEE---IIEAARLAGLHDFIEALPMgydtvvgeggsNLSGGQRQRLAIAR 624

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 521099586 150 SLAYKPDLLLLDEPFSNIDTQVRHDLIGEIRKIFkkQGVTAIFVTHsREEAFAFADKMAVMNHGVIEQYGTASEL 224
Cdd:COG2274  625 ALLRNPRILILDEATSALDAETEAIILENLRRLL--KGRTVIIIAH-RLSTIRLADRIIVLDKGRIVEDGTHEEL 696

FtsE

TIGR02673

cell division ATP-binding protein FtsE; This model describes FtsE, a member of the ABC ...

7-213

9.61e-47

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: 157.80 E-value: 9.61e-47

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099586    7 IQNLTCQYDTQT-VLESLSLNVEHGEIVCLLGASGCGKTTLLKAIAGLLPLSSGIMSLNGMTIDDGKH-WLAPEQRNIGM 84
Cdd:TIGR02673   4 FHNVSKAYPGGVaALHDVSLHIRKGEFLFLTGPSGAGKTTLLKLLYGALTPSRGQVRIAGEDVNRLRGrQLPLLRRRIGV 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099586   85 IFQDYALFPHLTVAENIAFGLRQMAAEER--HLQVQQMLELVHLSGFGDRYPHQLSGGQQQRVAIARSLAYKPDLLLLDE 162
Cdd:TIGR02673  84 VFQDFRLLPDRTVYENVALPLEVRGKKEReiQRRVGAALRQVGLEHKADAFPEQLSGGEQQRVAIARAIVNSPPLLLADE 163

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 521099586  163 PFSNIDTqvrhDLIGEIRKIFK---KQGVTAIFVTHSREEAFAFADKMAVMNHG 213
Cdd:TIGR02673 164 PTGNLDP----DLSERILDLLKrlnKRGTTVIVATHDLSLVDRVAHRVIILDDG 213

ABC_Mj1267_LivG_branched

cd03219

ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ...

5-223

1.23e-46

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: 157.98 E-value: 1.23e-46

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099586   5 LSIQNLTCQYDTQTVLESLSLNVEHGEIVCLLGASGCGKTTLLKAIAGLLPLSSGIMSLNGMTIDDgkhwLAPEQRN--- 81
Cdd:cd03219    1 LEVRGLTKRFGGLVALDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFDGEDITG----LPPHEIArlg 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099586  82 IGMIFQDYALFPHLTVAENI----------AFGLRQMAAEERHL--QVQQMLELVHLSGFGDRYPHQLSGGQQQRVAIAR 149
Cdd:cd03219   77 IGRTFQIPRLFPELTVLENVmvaaqartgsGLLLARARREEREAreRAEELLERVGLADLADRPAGELSYGQQRRLEIAR 156

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 521099586 150 SLAYKPDLLLLDEPFSNIDTQVRHDLIGEIRKIfKKQGVTAIFVTHSREEAFAFADKMAVMNHG-VIEQyGTASE 223
Cdd:cd03219  157 ALATDPKLLLLDEPAAGLNPEETEELAELIREL-RERGITVLLVEHDMDVVMSLADRVTVLDQGrVIAE-GTPDE 229

heterocyst_DevA

TIGR02982

ABC exporter ATP-binding subunit, DevA family; Members of this protein family are found mostly ...

4-195

2.69e-46

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: 156.72 E-value: 2.69e-46

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099586    4 ALSIQNLTCQYDT----QTVLESLSLNVEHGEIVCLLGASGCGKTTLLKAIAGLLPLSSGIMSLNGMTIDD-GKHWLAPE 78
Cdd:TIGR02982   1 VISIRNLNHYYGHgslrKQVLFDINLEINPGEIVILTGPSGSGKTTLLTLIGGLRSVQEGSLKVLGQELHGaSKKQLVQL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099586   79 QRNIGMIFQDYALFPHLTVAENIAFGL---RQMAAEERHLQVQQMLELVHLSGFGDRYPHQLSGGQQQRVAIARSLAYKP 155
Cdd:TIGR02982  81 RRRIGYIFQAHNLLGFLTARQNVQMALelqPNLSYQEARERARAMLEAVGLGDHLNYYPHNLSGGQKQRVAIARALVHHP 160

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 521099586  156 DLLLLDEPFSNIDTQVRHDLIGEIRKIFKKQGVTAIFVTH 195
Cdd:TIGR02982 161 KLVLADEPTAALDSKSGRDVVELMQKLAKEQGCTILMVTH 200

CydD

COG4988

ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ...

4-225

3.18e-46

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: 164.93 E-value: 3.18e-46

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099586   4 ALSIQNLTCQY-DTQTVLESLSLNVEHGEIVCLLGASGCGKTTLLKAIAGLLPLSSGIMSLNGMTID--DGKHWlapeQR 80
Cdd:COG4988  336 SIELEDVSFSYpGGRPALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPPYSGSILINGVDLSdlDPASW----RR 411

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099586  81 NIGMIFQDYALFpHLTVAENIAFGLRQmAAEErhlQVQQMLELVHLSGFGDRYPH-----------QLSGGQQQRVAIAR 149
Cdd:COG4988  412 QIAWVPQNPYLF-AGTIRENLRLGRPD-ASDE---ELEAALEAAGLDEFVAALPDgldtplgeggrGLSGGQAQRLALAR 486

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 521099586 150 SLAYKPDLLLLDEPFSNIDTQVRHDLIGEIRKIFKkqGVTAIFVTHsREEAFAFADKMAVMNHGVIEQYGTASELY 225
Cdd:COG4988  487 ALLRDAPLLLLDEPTAHLDAETEAEILQALRRLAK--GRTVILITH-RLALLAQADRILVLDDGRIVEQGTHEELL 559

cbiO

PRK13650

energy-coupling factor transporter ATPase;

1-279

8.05e-46

energy-coupling factor transporter ATPase;

Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 157.20 E-value: 8.05e-46

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099586   1 MSCALSIQNLTCQYD---TQTVLESLSLNVEHGEIVCLLGASGCGKTTLLKAIAGLLPLSSGIMSLNGMTIDDGKHWlaP 77
Cdd:PRK13650   1 MSNIIEVKNLTFKYKedqEKYTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIIDGDLLTEENVW--D 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099586  78 EQRNIGMIFQDY-ALFPHLTVAENIAFGL--RQMAAEERHLQVQQMLELVHLSGFGDRYPHQLSGGQQQRVAIARSLAYK 154
Cdd:PRK13650  79 IRHKIGMVFQNPdNQFVGATVEDDVAFGLenKGIPHEEMKERVNEALELVGMQDFKEREPARLSGGQKQRVAIAGAVAMR 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099586 155 PDLLLLDEPFSNIDTQVRHDLIGEIRKIFKKQGVTAIFVTHSREEAfAFADKMAVMNHGVIEQYGTASELYYRPSskfva 234
Cdd:PRK13650 159 PKIIILDEATSMLDPEGRLELIKTIKGIRDDYQMTVISITHDLDEV-ALSDRVLVMKNGQVESTSTPRELFSRGN----- 232

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*.
gi 521099586 235 DFLGGGSYLP-ATRLAEHQYQTPLGVVDAYAQQSIAQGSQCELLLR 279
Cdd:PRK13650 233 DLLQLGLDIPfTTSLVQSLRQNGYDLPEGYLTEKELEEQLWELISK 278

ABC_ThiQ_thiamine_transporter

cd03298

ATP-binding cassette domain of the thiamine transport system; Part of the ...

23-215

1.22e-45

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: 154.57 E-value: 1.22e-45

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099586  23 LSLNVEHGEIVCLLGASGCGKTTLLKAIAGLLPLSSGIMSLNGMtidDGKHwLAPEQRNIGMIFQDYALFPHLTVAENIA 102
Cdd:cd03298   17 FDLTFAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLINGV---DVTA-APPADRPVSMLFQENNLFAHLTVEQNVG 92

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099586 103 FGLR---QMAAEERHlQVQQMLELVHLSGFGDRYPHQLSGGQQQRVAIARSLAYKPDLLLLDEPFSNIDTQVRHDLIGEI 179
Cdd:cd03298   93 LGLSpglKLTAEDRQ-AIEVALARVGLAGLEKRLPGELSGGERQRVALARVLVRDKPVLLLDEPFAALDPALRAEMLDLV 171

                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 521099586 180 RKIFKKQGVTAIFVTHSREEAFAFADKMAVMNHGVI 215
Cdd:cd03298  172 LDLHAETKMTVLMVTHQPEDAKRLAQRVVFLDNGRI 207

metN

PRK11153

DL-methionine transporter ATP-binding subunit; Provisional

7-228

1.56e-45

DL-methionine transporter ATP-binding subunit; Provisional

Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 158.43 E-value: 1.56e-45

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099586   7 IQNLTCQYDTQ----TVLESLSLNVEHGEIVCLLGASGCGKTTLLKAIAGLLPLSSGIMSLNG---MTIDDGKhwLAPEQ 79
Cdd:PRK11153   4 LKNISKVFPQGgrtiHALNNVSLHIPAGEIFGVIGASGAGKSTLIRCINLLERPTSGRVLVDGqdlTALSEKE--LRKAR 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099586  80 RNIGMIFQDYALFPHLTVAENIAFGLR--QMAAEERHLQVQQMLELVHLSGFGDRYPHQLSGGQQQRVAIARSLAYKPDL 157
Cdd:PRK11153  82 RQIGMIFQHFNLLSSRTVFDNVALPLElaGTPKAEIKARVTELLELVGLSDKADRYPAQLSGGQKQRVAIARALASNPKV 161

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 521099586 158 LLLDEPFSNIDTQVRHDLIGEIRKIFKKQGVTAIFVTHSREEAFAFADKMAVMNHG-VIEQyGTASELYYRP 228
Cdd:PRK11153 162 LLCDEATSALDPATTRSILELLKDINRELGLTIVLITHEMDVVKRICDRVAVIDAGrLVEQ-GTVSEVFSHP 232

ABCC_MRP_Like

cd03228

ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ...

5-213

1.71e-45

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: 152.92 E-value: 1.71e-45

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099586   5 LSIQNLTCQYDT--QTVLESLSLNVEHGEIVCLLGASGCGKTTLLKAIAGLLPLSSGIMSLNGMTIDD-GKHWLapeQRN 81
Cdd:cd03228    1 IEFKNVSFSYPGrpKPVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGVDLRDlDLESL---RKN 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099586  82 IGMIFQDYALFpHLTVAENIafglrqmaaeerhlqvqqmlelvhlsgfgdryphqLSGGQQQRVAIARSLAYKPDLLLLD 161
Cdd:cd03228   78 IAYVPQDPFLF-SGTIRENI-----------------------------------LSGGQRQRIAIARALLRDPPILILD 121

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 521099586 162 EPFSNIDTQVRHDLIGEIRKIfkKQGVTAIFVTHsREEAFAFADKMAVMNHG 213
Cdd:cd03228  122 EATSALDPETEALILEALRAL--AKGKTVIVIAH-RLSTIRDADRIIVLDDG 170

HisP

COG4598

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

3-240

2.28e-45

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

Pssm-ID: 443652 [Multi-domain] Cd Length: 259 Bit Score: 155.34 E-value: 2.28e-45

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099586   3 CALSIQNLTCQYDTQTVLESLSLNVEHGEIVCLLGASGCGKTTLLKAIAGLLPLSSGIMSLNGMTID---DGKHWLAPEQ 79
Cdd:COG4598    7 PALEVRDLHKSFGDLEVLKGVSLTARKGDVISIIGSSGSGKSTFLRCINLLETPDSGEIRVGGEEIRlkpDRDGELVPAD 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099586  80 R--------NIGMIFQDYALFPHLTVAENI------AFGLRQMAAEERhlqVQQMLELVHLSGFGDRYPHQLSGGQQQRV 145
Cdd:COG4598   87 RrqlqrirtRLGMVFQSFNLWSHMTVLENVieapvhVLGRPKAEAIER---AEALLAKVGLADKRDAYPAHLSGGQQQRA 163

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099586 146 AIARSLAYKPDLLLLDEPFSNIDTQvrhdLIGEIRKIFKK---QGVTAIFVTHsrEEAFA--FADKMAVMNHGVIEQYGT 220
Cdd:COG4598  164 AIARALAMEPEVMLFDEPTSALDPE----LVGEVLKVMRDlaeEGRTMLVVTH--EMGFArdVSSHVVFLHQGRIEEQGP 237

                        250       260
                 ....*....|....*....|
gi 521099586 221 ASELYYRPSSKFVADFLGGG 240
Cdd:COG4598  238 PAEVFGNPKSERLRQFLSSS 257

ABC_DrrA

cd03265

Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ...

7-224

1.16e-44

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

Pssm-ID: 213232 [Multi-domain] Cd Length: 220 Bit Score: 152.52 E-value: 1.16e-44

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099586   7 IQNLTCQYDTQTVLESLSLNVEHGEIVCLLGASGCGKTTLLKAIAGLLPLSSGIMSLNGMTI--DDGKhwlapEQRNIGM 84
Cdd:cd03265    3 VENLVKKYGDFEAVRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATVAGHDVvrEPRE-----VRRRIGI 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099586  85 IFQDYALFPHLTVAENIAF--GLRQMAAEERHLQVQQMLELVHLSGFGDRYPHQLSGGQQQRVAIARSLAYKPDLLLLDE 162
Cdd:cd03265   78 VFQDLSVDDELTGWENLYIhaRLYGVPGAERRERIDELLDFVGLLEAADRLVKTYSGGMRRRLEIARSLVHRPEVLFLDE 157

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 521099586 163 PFSNIDTQVRHDLIGEIRKIFKKQGVTAIFVTHSREEAFAFADKMAVMNHGVIEQYGTASEL 224
Cdd:cd03265  158 PTIGLDPQTRAHVWEYIEKLKEEFGMTILLTTHYMEEAEQLCDRVAIIDHGRIIAEGTPEEL 219

3a0107s01c2

TIGR00972

phosphate ABC transporter, ATP-binding protein; This model represents the ATP-binding protein ...

4-239

2.40e-44

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: 152.45 E-value: 2.40e-44

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099586    4 ALSIQNLTCQYDTQTVLESLSLNVEHGEIVCLLGASGCGKTTLLKAIAGLLPLSSGI-----MSLNGMTIDDGKHWLAPE 78
Cdd:TIGR00972   1 AIEIENLNLFYGEKEALKNINLDIPKNQVTALIGPSGCGKSTLLRSLNRMNDLVPGVriegkVLFDGQDIYDKKIDVVEL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099586   79 QRNIGMIFQDYALFPhLTVAENIAFGLRQMAAEERHL---QVQQMLELV----------HLSGFGdryphqLSGGQQQRV 145
Cdd:TIGR00972  81 RRRVGMVFQKPNPFP-MSIYDNIAYGPRLHGIKDKKEldeIVEESLKKAalwdevkdrlHDSALG------LSGGQQQRL 153

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099586  146 AIARSLAYKPDLLLLDEPFSNID---TQVRHDLIGEIRKIFkkqgvTAIFVTHSREEAFAFADKMAVMNHGVIEQYGTAS 222
Cdd:TIGR00972 154 CIARALAVEPEVLLLDEPTSALDpiaTGKIEELIQELKKKY-----TIVIVTHNMQQAARISDRTAFFYDGELVEYGPTE 228

                         250
                  ....*....|....*..
gi 521099586  223 ELYYRPSSKFVADFLGG 239
Cdd:TIGR00972 229 QIFTNPKEKRTEDYISG 245

PstB

COG1117

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

4-239

2.94e-44

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

Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 152.50 E-value: 2.94e-44

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099586   4 ALSIQNLTCQYDTQTVLESLSLNVEHGEIVCLLGASGCGKTTLLKaiagllplssgimSLNGM--TID----------DG 71
Cdd:COG1117   11 KIEVRNLNVYYGDKQALKDINLDIPENKVTALIGPSGCGKSTLLR-------------CLNRMndLIPgarvegeillDG 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099586  72 KHWLAPEQ------RNIGMIFQDYALFPHlTVAENIAFGLRQM------AAEERhlqVQQMLELVHL----------SGF 129
Cdd:COG1117   78 EDIYDPDVdvvelrRRVGMVFQKPNPFPK-SIYDNVAYGLRLHgiksksELDEI---VEESLRKAALwdevkdrlkkSAL 153

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099586 130 GdryphqLSGGQQQRVAIARSLAYKPDLLLLDEPFSNID---TQVRHDLIGEIRKIFkkqgvTAIFVTHSREEAFAFADK 206
Cdd:COG1117  154 G------LSGGQQQRLCIARALAVEPEVLLMDEPTSALDpisTAKIEELILELKKDY-----TIVIVTHNMQQAARVSDY 222

                        250       260       270
                 ....*....|....*....|....*....|...
gi 521099586 207 MAVMNHGVIEQYGTASELYYRPSSKFVADFLGG 239
Cdd:COG1117  223 TAFFYLGELVEFGPTEQIFTNPKDKRTEDYITG 255

CydC

COG4987

ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ...

4-227

3.49e-44

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: 159.55 E-value: 3.49e-44

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099586   4 ALSIQNLTCQYD--TQTVLESLSLNVEHGEIVCLLGASGCGKTTLLKAIAGLLPLSSGIMSLNGMTIDDgkhwLAPEQ-- 79
Cdd:COG4987  333 SLELEDVSFRYPgaGRPVLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFLDPQSGSITLGGVDLRD----LDEDDlr 408

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099586  80 RNIGMIFQDYALFpHLTVAENIAFGlRQMAAEErhlQVQQMLELVHLSGFGDRYPH-----------QLSGGQQQRVAIA 148
Cdd:COG4987  409 RRIAVVPQRPHLF-DTTLRENLRLA-RPDATDE---ELWAALERVGLGDWLAALPDgldtwlgeggrRLSGGERRRLALA 483

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099586 149 RSLAYKPDLLLLDEPFSNIDTQVRHDLIGEIRKIFkkQGVTAIFVTHsREEAFAFADKMAVMNHGVIEQYGTASEL---- 224
Cdd:COG4987  484 RALLRDAPILLLDEPTEGLDAATEQALLADLLEAL--AGRTVLLITH-RLAGLERMDRILVLEDGRIVEQGTHEELlaqn 560


                 ....
gi 521099586 225 -YYR 227
Cdd:COG4987  561 gRYR 564

urea_trans_UrtE

TIGR03410

urea ABC transporter, ATP-binding protein UrtE; Members of this protein family are ABC ...

5-224

3.73e-44

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: 151.52 E-value: 3.73e-44

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099586    5 LSIQNLTCQYDTQTVLESLSLNVEHGEIVCLLGASGCGKTTLLKAIAGLLPLSSGIMSLNGMTIDDgkhwLAPEQR---N 81
Cdd:TIGR03410   1 LEVSNLNVYYGQSHILRGVSLEVPKGEVTCVLGRNGVGKTTLLKTLMGLLPVKSGSIRLDGEDITK----LPPHERaraG 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099586   82 IGMIFQDYALFPHLTVAENIAFGLRQMAAEERHLqVQQMLEL--VhLSGFGDRYPHQLSGGQQQRVAIARSLAYKPDLLL 159
Cdd:TIGR03410  77 IAYVPQGREIFPRLTVEENLLTGLAALPRRSRKI-PDEIYELfpV-LKEMLGRRGGDLSGGQQQQLAIARALVTRPKLLL 154

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 521099586  160 LDEPFSNIDTQVRHDLIGEIRKIFKKQGVTAIFVTHSREEAFAFADKMAVMNHGVIEQYGTASEL 224
Cdd:TIGR03410 155 LDEPTEGIQPSIIKDIGRVIRRLRAEGGMAILLVEQYLDFARELADRYYVMERGRVVASGAGDEL 219

ABC_FtsE

cd03292

Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ...

8-198

4.14e-44

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: 151.02 E-value: 4.14e-44

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099586   8 QNLTCQYDTQTV-LESLSLNVEHGEIVCLLGASGCGKTTLLKAIAGLLPLSSGIMSLNGMTIDDGKHWLAPE-QRNIGMI 85
Cdd:cd03292    4 INVTKTYPNGTAaLDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQDVSDLRGRAIPYlRRKIGVV 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099586  86 FQDYALFPHLTVAENIAFGLRQMAAEERHLQ--VQQMLELVHLSGFGDRYPHQLSGGQQQRVAIARSLAYKPDLLLLDEP 163
Cdd:cd03292   84 FQDFRLLPDRNVYENVAFALEVTGVPPREIRkrVPAALELVGLSHKHRALPAELSGGEQQRVAIARAIVNSPTILIADEP 163

                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 521099586 164 FSNIDTqvrhDLIGEIRKIFK---KQGVTAIFVTHSRE 198
Cdd:cd03292  164 TGNLDP----DTTWEIMNLLKkinKAGTTVVVATHAKE 197

AppF

COG4608

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

24-228

2.11e-43

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

Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 152.19 E-value: 2.11e-43

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099586  24 SLNVEHGEIVCLLGASGCGKTTLLKAIAGLLPLSSGIMSLNGMTIDD-GKHWLAPEQRNIGMIFQD-YA-LFPHLTVAEN 100
Cdd:COG4608   38 SFDIRRGETLGLVGESGCGKSTLGRLLLRLEEPTSGEILFDGQDITGlSGRELRPLRRRMQMVFQDpYAsLNPRMTVGDI 117

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099586 101 IAFGLR---QMAAEERHLQVQQMLELVHLS-GFGDRYPHQLSGGQQQRVAIARSLAYKPDLLLLDEPFSNIDTQVRH--- 173
Cdd:COG4608  118 IAEPLRihgLASKAERRERVAELLELVGLRpEHADRYPHEFSGGQRQRIGIARALALNPKLIVCDEPVSALDVSIQAqvl 197

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 521099586 174 DLIGEIRKIFkkqGVTAIFVTHS----REeafaFADKMAVMNHGVIEQYGTASELYYRP 228
Cdd:COG4608  198 NLLEDLQDEL---GLTYLFISHDlsvvRH----ISDRVAVMYLGKIVEIAPRDELYARP 249

modC

PRK11144

molybdenum ABC transporter ATP-binding protein ModC;

32-228

7.79e-43

molybdenum ABC transporter ATP-binding protein ModC;

Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 151.57 E-value: 7.79e-43

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099586  32 IVCLLGASGCGKTTLLKAIAGLLPLSSGIMSLNGMTIDD--GKHWLAPEQRNIGMIFQDYALFPHLTVAENIAFGL-RQM 108
Cdd:PRK11144  26 ITAIFGRSGAGKTSLINAISGLTRPQKGRIVLNGRVLFDaeKGICLPPEKRRIGYVFQDARLFPHYKVRGNLRYGMaKSM 105

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099586 109 AAEerHLQVQQMLELVHLSgfgDRYPHQLSGGQQQRVAIARSLAYKPDLLLLDEPFSNIDTQVRHDLIGEIRKIFKKQGV 188
Cdd:PRK11144 106 VAQ--FDKIVALLGIEPLL---DRYPGSLSGGEKQRVAIGRALLTAPELLLMDEPLASLDLPRKRELLPYLERLAREINI 180

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|
gi 521099586 189 TAIFVTHSREEAFAFADKMAVMNHGVIEQYGTASELYYRP 228
Cdd:PRK11144 181 PILYVSHSLDEILRLADRVVVLEQGKVKAFGPLEEVWASS 220

L_ocin_972_ABC

TIGR03608

putative bacteriocin export ABC transporter, lactococcin 972 group; A gene pair with a fairly ...

7-198

1.52e-42

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: 146.61 E-value: 1.52e-42

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099586    7 IQNLTCQYDTQTVLESLSLNVEHGEIVCLLGASGCGKTTLLKAIAGLLPLSSGIMSLNGMTIDDGKHWLAPE-QRN-IGM 84
Cdd:TIGR03608   1 LKNISKKFGDKVILDDLNLTIEKGKMYAIIGESGSGKSTLLNIIGLLEKFDSGQVYLNGQETPPLNSKKASKfRREkLGY 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099586   85 IFQDYALFPHLTVAENIAFGL---RQMAAEERHLQVQqMLELVHLSGFGDRYPHQLSGGQQQRVAIARSLAYKPDLLLLD 161
Cdd:TIGR03608  81 LFQNFALIENETVEENLDLGLkykKLSKKEKREKKKE-ALEKVGLNLKLKQKIYELSGGEQQRVALARAILKPPPLILAD 159

                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 521099586  162 EPFSNIDTQVRHDLIgEIRKIFKKQGVTAIFVTHSRE 198
Cdd:TIGR03608 160 EPTGSLDPKNRDEVL-DLLLELNDEGKTIIIVTHDPE 195

PRK10070

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

24-239

2.79e-42

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

Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 151.34 E-value: 2.79e-42

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099586  24 SLNVEHGEIVCLLGASGCGKTTLLKAIAGLLPLSSGIMSLNGMTIDDGKHWLAPEQR--NIGMIFQDYALFPHLTVAENI 101
Cdd:PRK10070  48 SLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAKISDAELREVRrkKIAMVFQSFALMPHMTVLDNT 127

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099586 102 AFG--LRQMAAEERHLQVQQMLELVHLSGFGDRYPHQLSGGQQQRVAIARSLAYKPDLLLLDEPFSNIDTQVRHDLIGEI 179
Cdd:PRK10070 128 AFGmeLAGINAEERREKALDALRQVGLENYAHSYPDELSGGMRQRVGLARALAINPDILLMDEAFSALDPLIRTEMQDEL 207

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099586 180 RKIFKKQGVTAIFVTHSREEAFAFADKMAVMNHGVIEQYGTASELYYRPSSKFVADFLGG 239
Cdd:PRK10070 208 VKLQAKHQRTIVFISHDLDEAMRIGDRIAIMQNGEVVQVGTPDEILNNPANDYVRTFFRG 267

MdlB

COG1132

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

4-227

4.91e-42

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

Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 153.78 E-value: 4.91e-42

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099586   4 ALSIQNLTCQYDTQT-VLESLSLNVEHGEIVCLLGASGCGKTTLLKAIAGLLPLSSGIMSLNGMTIDDgkhwLAPEQ--R 80
Cdd:COG1132  339 EIEFENVSFSYPGDRpVLKDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYDPTSGRILIDGVDIRD----LTLESlrR 414

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099586  81 NIGMIFQDYALFpHLTVAENIAFGlRQMAAEErhlQVQQMLELVHLSGFGDRYPH-----------QLSGGQQQRVAIAR 149
Cdd:COG1132  415 QIGVVPQDTFLF-SGTIRENIRYG-RPDATDE---EVEEAAKAAQAHEFIEALPDgydtvvgergvNLSGGQRQRIAIAR 489

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099586 150 SLAYKPDLLLLDEPFSNIDTQVRHDLIGEIRKIFKkqGVTAIFVTHsREEAFAFADKMAVMNHGVIEQYGT------ASE 223
Cdd:COG1132  490 ALLKDPPILILDEATSALDTETEALIQEALERLMK--GRTTIVIAH-RLSTIRNADRILVLDDGRIVEQGTheellaRGG 566


                 ....
gi 521099586 224 LYYR 227
Cdd:COG1132  567 LYAR 570

YbbA

COG4181

Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ...

1-223

6.85e-42

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: 145.65 E-value: 6.85e-42

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099586   1 MSC----ALSIQNLTCQYDTQ----TVLESLSLNVEHGEIVCLLGASGCGKTTLLKAIAGLLPLSSGIMSLNGMTIDDgk 72
Cdd:COG4181    1 MSSssapIIELRGLTKTVGTGagelTILKGISLEVEAGESVAIVGASGSGKSTLLGLLAGLDRPTSGTVRLAGQDLFA-- 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099586  73 hwLAPEQR------NIGMIFQDYALFPHLTVAENIA-----FGLRQmaAEERhlqVQQMLELVHLSGFGDRYPHQLSGGQ 141
Cdd:COG4181   79 --LDEDARarlrarHVGFVFQSFQLLPTLTALENVMlplelAGRRD--ARAR---ARALLERVGLGHRLDHYPAQLSGGE 151

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099586 142 QQRVAIARSLAYKPDLLLLDEPFSNIDTQVRHDLIGEIRKIFKKQGVTAIFVTHSREEAfAFADKMAVMNHGVIEQYGTA 221
Cdd:COG4181  152 QQRVALARAFATEPAILFADEPTGNLDAATGEQIIDLLFELNRERGTTLVLVTHDPALA-ARCDRVLRLRAGRLVEDTAA 230


                 ..
gi 521099586 222 SE 223
Cdd:COG4181  231 TA 232

SapF

COG4167

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

1-228

1.76e-41

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

Pssm-ID: 443328 [Multi-domain] Cd Length: 265 Bit Score: 145.37 E-value: 1.76e-41

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099586   1 MSCALSIQNLTCQYDTQT---------VLESLSLNVEHGEIVCLLGASGCGKTTLLKAIAGLLPLSSGIMSLNGMTIDDG 71
Cdd:COG4167    1 MSALLEVRNLSKTFKYRTglfrrqqfeAVKPVSFTLEAGQTLAIIGENGSGKSTLAKMLAGIIEPTSGEILINGHKLEYG 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099586  72 KHwlapEQR--NIGMIFQD--YALFPHLTVAENIAFGLR---QMAAEERHLQVQQMLELVHLSG-FGDRYPHQLSGGQQQ 143
Cdd:COG4167   81 DY----KYRckHIRMIFQDpnTSLNPRLNIGQILEEPLRlntDLTAEEREERIFATLRLVGLLPeHANFYPHMLSSGQKQ 156

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099586 144 RVAIARSLAYKPDLLLLDEPFSNIDTQVRHDLIGEIRKIFKKQGVTAIFVTHSREEAFAFADKMAVMNHGVIEQYGTASE 223
Cdd:COG4167  157 RVALARALILQPKIIIADEALAALDMSVRSQIINLMLELQEKLGISYIYVSQHLGIVKHISDKVLVMHQGEVVEYGKTAE 236


                 ....*
gi 521099586 224 LYYRP 228
Cdd:COG4167  237 VFANP 241

cbiO

PRK13634

cobalt transporter ATP-binding subunit; Provisional

20-259

4.19e-41

cobalt transporter ATP-binding subunit; Provisional

Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 145.16 E-value: 4.19e-41

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099586  20 LESLSLNVEHGEIVCLLGASGCGKTTLLKAIAGLLPLSSGIMSLNGMTIDDGKHW--LAPEQRNIGMIFQ--DYALFPHl 95
Cdd:PRK13634  23 LYDVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVTIGERVITAGKKNkkLKPLRKKVGIVFQfpEHQLFEE- 101

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099586  96 TVAENIAFGLRQ--MAAEERHLQVQQMLELVHLS-GFGDRYPHQLSGGQQQRVAIARSLAYKPDLLLLDEPFSNIDTQVR 172
Cdd:PRK13634 102 TVEKDICFGPMNfgVSEEDAKQKAREMIELVGLPeELLARSPFELSGGQMRRVAIAGVLAMEPEVLVLDEPTAGLDPKGR 181

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099586 173 HDLIGEIRKIFKKQGVTAIFVTHSREEAFAFADKMAVMNHGVIEQYGTASELYYRPsskfvADFLGGGSYLPATRLAEHQ 252
Cdd:PRK13634 182 KEMMEMFYKLHKEKGLTTVLVTHSMEDAARYADQIVVMHKGTVFLQGTPREIFADP-----DELEAIGLDLPETVKFKRA 256


                 ....*..
gi 521099586 253 YQTPLGV 259
Cdd:PRK13634 257 LEEKFGI 263

ABC_BcrA_bacitracin_resist

cd03268

ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ...

5-215

5.88e-41

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: 142.36 E-value: 5.88e-41

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099586   5 LSIQNLTCQYDTQTVLESLSLNVEHGEIVCLLGASGCGKTTLLKAIAGLLPLSSGIMSLNGMTIDDgkhwLAPEQRNIGM 84
Cdd:cd03268    1 LKTNDLTKTYGKKRVLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEITFDGKSYQK----NIEALRRIGA 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099586  85 IFQDYALFPHLTVAENIAFGLRQMAAEERhlQVQQMLELVHLSGFGDRYPHQLSGGQQQRVAIARSLAYKPDLLLLDEPF 164
Cdd:cd03268   77 LIEAPGFYPNLTARENLRLLARLLGIRKK--RIDEVLDVVGLKDSAKKKVKGFSLGMKQRLGIALALLGNPDLLILDEPT 154

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 521099586 165 SNIDTqvrhDLIGEIRKIF---KKQGVTAIFVTHSREEAFAFADKMAVMNHGVI 215
Cdd:cd03268  155 NGLDP----DGIKELRELIlslRDQGITVLISSHLLSEIQKVADRIGIINKGKL 204

ssuB

PRK11247

aliphatic sulfonates transport ATP-binding subunit; Provisional

5-215

1.78e-40

aliphatic sulfonates transport ATP-binding subunit; Provisional

Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 142.89 E-value: 1.78e-40

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099586   5 LSIQNLTCQYDTQTVLESLSLNVEHGEIVCLLGASGCGKTTLLKAIAGLLPLSSGIMsLNGMTIddgkhwLAPEQRNIGM 84
Cdd:PRK11247  13 LLLNAVSKRYGERTVLNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAGEL-LAGTAP------LAEAREDTRL 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099586  85 IFQDYALFPHLTVAENIAFGLRQMAAEERHlqvqQMLELVHLSGFGDRYPHQLSGGQQQRVAIARSLAYKPDLLLLDEPF 164
Cdd:PRK11247  86 MFQDARLLPWKKVIDNVGLGLKGQWRDAAL----QALAAVGLADRANEWPAALSGGQKQRVALARALIHRPGLLLLDEPL 161

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 521099586 165 SNIDTQVRHDLIGEIRKIFKKQGVTAIFVTHSREEAFAFADKMAVMNHGVI 215
Cdd:PRK11247 162 GALDALTRIEMQDLIESLWQQHGFTVLLVTHDVSEAVAMADRVLLIEEGKI 212

ABC_cobalt_CbiO_domain2

cd03226

Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ...

6-215

2.85e-40

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: 140.47 E-value: 2.85e-40

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099586   6 SIQNLTCQY-DTQTVLESLSLNVEHGEIVCLLGASGCGKTTLLKAIAGLLPLSSGIMSLNGMTIDDGKhwlapEQRNIGM 84
Cdd:cd03226    1 RIENISFSYkKGTEILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLNGKPIKAKE-----RRKSIGY 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099586  85 IFQD--YALFPHlTVAENIAFGLrqMAAEERHLQVQQMLELVHLSGFGDRYPHQLSGGQQQRVAIARSLAYKPDLLLLDE 162
Cdd:cd03226   76 VMQDvdYQLFTD-SVREELLLGL--KELDAGNEQAETVLKDLDLYALKERHPLSLSGGQKQRLAIAAALLSGKDLLIFDE 152

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 521099586 163 PFSNIDTqvRH-DLIGEIRKIFKKQGVTAIFVTHSREEAFAFADKMAVMNHGVI 215
Cdd:cd03226  153 PTSGLDY--KNmERVGELIRELAAQGKAVIVITHDYEFLAKVCDRVLLLANGAI 204

cbiO

PRK13632

cobalt transporter ATP-binding subunit; Provisional

4-224

2.89e-40

cobalt transporter ATP-binding subunit; Provisional

Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 142.44 E-value: 2.89e-40

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099586   4 ALSIQNLTCQYDTQT--VLESLSLNVEHGEIVCLLGASGCGKTTLLKAIAGLLPLSSGIMSLNGMTIDdgKHWLAPEQRN 81
Cdd:PRK13632   7 MIKVENVSFSYPNSEnnALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIDGITIS--KENLKEIRKK 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099586  82 IGMIFQ--DYAlFPHLTVAENIAFGL--RQMAAEERHLQVQQMLELVHLSGFGDRYPHQLSGGQQQRVAIARSLAYKPDL 157
Cdd:PRK13632  85 IGIIFQnpDNQ-FIGATVEDDIAFGLenKKVPPKKMKDIIDDLAKKVGMEDYLDKEPQNLSGGQKQRVAIASVLALNPEI 163

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 521099586 158 LLLDEPFSNIDTQVRHDLIGEIRKIFKKQGVTAIFVTHSREEAFaFADKMAVMNHGVIEQYGTASEL 224
Cdd:PRK13632 164 IIFDESTSMLDPKGKREIKKIMVDLRKTRKKTLISITHDMDEAI-LADKVIVFSEGKLIAQGKPKEI 229

nickel_nikE

TIGR02769

nickel import ATP-binding protein NikE; This family represents the NikE subunit of a ...

5-231

4.66e-40

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: 141.87 E-value: 4.66e-40

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099586    5 LSIQNLTCQYDT---------QTVLESLSLNVEHGEIVCLLGASGCGKTTLLKAIAGLLPLSSGIMSLNGMTID--DGKH 73
Cdd:TIGR02769   3 LEVRDVTHTYRTgglfgakqrAPVLTNVSLSIEEGETVGLLGRSGCGKSTLARLLLGLEKPAQGTVSFRGQDLYqlDRKQ 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099586   74 WLApEQRNIGMIFQDY--ALFPHLTVAENIAFGLRQ---MAAEERHLQVQQMLELVHL-SGFGDRYPHQLSGGQQQRVAI 147
Cdd:TIGR02769  83 RRA-FRRDVQLVFQDSpsAVNPRMTVRQIIGEPLRHltsLDESEQKARIAELLDMVGLrSEDADKLPRQLSGGQLQRINI 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099586  148 ARSLAYKPDLLLLDEPFSNIDTQVRHDLIGEIRKIFKKQGVTAIFVTHSREEAFAFADKMAVMNHG-VIEQYGTASELYY 226
Cdd:TIGR02769 162 ARALAVKPKLIVLDEAVSNLDMVLQAVILELLRKLQQAFGTAYLFITHDLRLVQSFCQRVAVMDKGqIVEECDVAQLLSF 241


                  ....*.
gi 521099586  227 R-PSSK 231
Cdd:TIGR02769 242 KhPAGR 247

hmuV

PRK13548

hemin importer ATP-binding subunit; Provisional

4-223

1.10e-39

hemin importer ATP-binding subunit; Provisional

Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 140.68 E-value: 1.10e-39

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099586   4 ALSIQNLTCQYDTQTVLESLSLNVEHGEIVCLLGASGCGKTTLLKAIAGLLPLSSGIMSLNGMTIDDGKHW-LApeqRNI 82
Cdd:PRK13548   2 MLEARNLSVRLGGRTLLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLNGRPLADWSPAeLA---RRR 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099586  83 GMIFQDYAL-FPhLTVAENIAFGLRQMAAEERHLQ--VQQMLELVHLSGFGDRYPHQLSGGQQQRVAIARSLA------Y 153
Cdd:PRK13548  79 AVLPQHSSLsFP-FTVEEVVAMGRAPHGLSRAEDDalVAAALAQVDLAHLAGRDYPQLSGGEQQRVQLARVLAqlwepdG 157

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099586 154 KPDLLLLDEPFSNIDTQVRHDLIGEIRKIFKKQGVTAIFVTHSREEAFAFADKMAVMNHGVIEQYGTASE 223
Cdd:PRK13548 158 PPRWLLLDEPTSALDLAHQHHVLRLARQLAHERGLAVIVVLHDLNLAARYADRIVLLHQGRLVADGTPAE 227

MglA

COG1129

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

4-210

1.43e-39

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

Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 145.93 E-value: 1.43e-39

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099586   4 ALSIQNLTCQYDTQTVLESLSLNVEHGEIVCLLGASGCGKTTLLKAIAGLLPLSSGIMSLNG--MTIDDGKHwlApEQRN 81
Cdd:COG1129    4 LLEMRGISKSFGGVKALDGVSLELRPGEVHALLGENGAGKSTLMKILSGVYQPDSGEILLDGepVRFRSPRD--A-QAAG 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099586  82 IGMIFQDYALFPHLTVAENIAFGL----------RQMAAEerhlqVQQMLELVHLsgfgDRYPHQ----LSGGQQQRVAI 147
Cdd:COG1129   81 IAIIHQELNLVPNLSVAENIFLGReprrgglidwRAMRRR-----ARELLARLGL----DIDPDTpvgdLSVAQQQLVEI 151

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 521099586 148 ARSLAYKPDLLLLDEPFSNI-DTQVRHdLIGEIRKiFKKQGVTAIFVTHSREEAFAFADKMAVM 210
Cdd:COG1129  152 ARALSRDARVLILDEPTASLtEREVER-LFRIIRR-LKAQGVAIIYISHRLDEVFEIADRVTVL 213

PRK10619

histidine ABC transporter ATP-binding protein HisP;

5-239

2.63e-39

histidine ABC transporter ATP-binding protein HisP;

Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 139.72 E-value: 2.63e-39

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099586   5 LSIQNLTCQYDTQTVLESLSLNVEHGEIVCLLGASGCGKTTLLKAIAGLLPLSSGIMSLNGMTI-----DDG------KH 73
Cdd:PRK10619   6 LNVIDLHKRYGEHEVLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNGQTInlvrdKDGqlkvadKN 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099586  74 WLAPEQRNIGMIFQDYALFPHLTVAENI------AFGLRQMAAEERHLQvqqMLELVHLSGFG-DRYPHQLSGGQQQRVA 146
Cdd:PRK10619  86 QLRLLRTRLTMVFQHFNLWSHMTVLENVmeapiqVLGLSKQEARERAVK---YLAKVGIDERAqGKYPVHLSGGQQQRVS 162

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099586 147 IARSLAYKPDLLLLDEPFSNIDTQvrhdLIGEIRKIFKK---QGVTAIFVTHSREEAFAFADKMAVMNHGVIEQYGTASE 223
Cdd:PRK10619 163 IARALAMEPEVLLFDEPTSALDPE----LVGEVLRIMQQlaeEGKTMVVVTHEMGFARHVSSHVIFLHQGKIEEEGAPEQ 238

                        250
                 ....*....|....*.
gi 521099586 224 LYYRPSSKFVADFLGG 239
Cdd:PRK10619 239 LFGNPQSPRLQQFLKG 254

COG4559

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

5-223

6.62e-39

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

Pssm-ID: 443620 [Multi-domain] Cd Length: 258 Bit Score: 138.71 E-value: 6.62e-39

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099586   5 LSIQNLTCQYDTQTVLESLSLNVEHGEIVCLLGASGCGKTTLLKAIAGLLPLSSGIMSLNGMTIDDGKHW-LApeqRNIG 83
Cdd:COG4559    2 LEAENLSVRLGGRTLLDDVSLTLRPGELTAIIGPNGAGKSTLLKLLTGELTPSSGEVRLNGRPLAAWSPWeLA---RRRA 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099586  84 MIFQDYAL-FPhLTVAENIAFGL---RQMAAEERHLqVQQMLELVHLSGFGDRYPHQLSGGQQQRVAIARSLA------- 152
Cdd:COG4559   79 VLPQHSSLaFP-FTVEEVVALGRaphGSSAAQDRQI-VREALALVGLAHLAGRSYQTLSGGEQQRVQLARVLAqlwepvd 156

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 521099586 153 YKPDLLLLDEPFSNIDTQVRHDLIGEIRKiFKKQGVTAIFVTHSREEAFAFADKMAVMNHGVIEQYGTASE 223
Cdd:COG4559  157 GGPRWLFLDEPTSALDLAHQHAVLRLARQ-LARRGGGVVAVLHDLNLAAQYADRILLLHQGRLVAQGTPEE 226

ABC_Carb_Monos_I

cd03216

First domain of the ATP-binding cassette component of monosaccharide transport system; This ...

5-215

6.80e-39

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

Pssm-ID: 213183 [Multi-domain] Cd Length: 163 Bit Score: 135.63 E-value: 6.80e-39

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099586   5 LSIQNLTCQYDTQTVLESLSLNVEHGEIVCLLGASGCGKTTLLKAIAGLLPLSSGIMSLNGMTIddgkHWLAP---EQRN 81
Cdd:cd03216    1 LELRGITKRFGGVKALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVDGKEV----SFASPrdaRRAG 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099586  82 IGMIfqdyalfphltvaeniafglrqmaaeerhlqvqqmlelvhlsgfgdrypHQLSGGQQQRVAIARSLAYKPDLLLLD 161
Cdd:cd03216   77 IAMV-------------------------------------------------YQLSVGERQMVEIARALARNARLLILD 107

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 521099586 162 EPFSNIDTQVRHDLIGEIRKiFKKQGVTAIFVTHSREEAFAFADKMAVMNHGVI 215
Cdd:cd03216  108 EPTAALTPAEVERLFKVIRR-LRAQGVAVIFISHRLDEVFEIADRVTVLRDGRV 160

ModF

COG1119

ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ...

4-224

1.63e-38

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: 137.14 E-value: 1.63e-38

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099586   4 ALSIQNLTCQYDTQTVLESLSLNVEHGEIVCLLGASGCGKTTLLKAIAGLLPLSSGI------MSLNGMTIDDGKhwlap 77
Cdd:COG1119    3 LLELRNVTVRRGGKTILDDISWTVKPGEHWAILGPNGAGKSTLLSLITGDLPPTYGNdvrlfgERRGGEDVWELR----- 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099586  78 eqRNIGMI---FQDYaLFPHLTVAENIA------FGLRQMAAEERHLQVQQMLELVHLSGFGDRYPHQLSGGQQQRVAIA 148
Cdd:COG1119   78 --KRIGLVspaLQLR-FPRDETVLDVVLsgffdsIGLYREPTDEQRERARELLELLGLAHLADRPFGTLSQGEQRRVLIA 154

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 521099586 149 RSLAYKPDLLLLDEPFSNIDTQVRHDLIGEIRKIFKKQGVTAIFVTHSREEAFAFADKMAVMNHGVIEQYGTASEL 224
Cdd:COG1119  155 RALVKDPELLILDEPTAGLDLGARELLLALLDKLAAEGAPTLVLVTHHVEEIPPGITHVLLLKDGRVVAAGPKEEV 230

LptB

COG1137

ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ...

5-225

1.83e-38

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

Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 136.70 E-value: 1.83e-38

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099586   5 LSIQNLTCQYDTQTVLESLSLNVEHGEIVCLLGASGCGKTTLLKAIAGLLPLSSGIMSLNGMTIDDgkhwLAPEQR---N 81
Cdd:COG1137    4 LEAENLVKSYGKRTVVKDVSLEVNQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGRIFLDGEDITH----LPMHKRarlG 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099586  82 IGMIFQDYALFPHLTVAENI--AFGLRQMAAEERHLQVQQMLELVHLSGFGDRYPHQLSGGQQQRVAIARSLAYKPDLLL 159
Cdd:COG1137   80 IGYLPQEASIFRKLTVEDNIlaVLELRKLSKKEREERLEELLEEFGITHLRKSKAYSLSGGERRRVEIARALATNPKFIL 159

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 521099586 160 LDEPFSNID--TqvrhdlIGEIRKIF---KKQGVtAIFVT-HSREEAFAFADKMAVMNHGVIEQYGTASELY 225
Cdd:COG1137  160 LDEPFAGVDpiA------VADIQKIIrhlKERGI-GVLITdHNVRETLGICDRAYIISEGKVLAEGTPEEIL 224

ABC_YhbG

cd03218

ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ...

5-225

2.58e-38

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: 136.13 E-value: 2.58e-38

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099586   5 LSIQNLTCQYDTQTVLESLSLNVEHGEIVCLLGASGCGKTTLLKAIAGLLPLSSGIMSLNGMTIDDgkhwLAPEQR---N 81
Cdd:cd03218    1 LRAENLSKRYGKRKVVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDGQDITK----LPMHKRarlG 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099586  82 IGMIFQDYALFPHLTVAENI--AFGLRQMAAEERHLQVQQMLELVHLSGFGDRYPHQLSGGQQQRVAIARSLAYKPDLLL 159
Cdd:cd03218   77 IGYLPQEASIFRKLTVEENIlaVLEIRGLSKKEREEKLEELLEEFHITHLRKSKASSLSGGERRRVEIARALATNPKFLL 156

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 521099586 160 LDEPFSNIDTQVRHDlIGEIRKIFKKQGVtAIFVT-HSREEAFAFADKMAVMNHGVIEQYGTASELY 225
Cdd:cd03218  157 LDEPFAGVDPIAVQD-IQKIIKILKDRGI-GVLITdHNVRETLSITDRAYIIYEGKVLAEGTPEEIA 221

PRK13633

energy-coupling factor transporter ATPase;

8-225

3.50e-38

energy-coupling factor transporter ATPase;

Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 137.53 E-value: 3.50e-38

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099586   8 QNLTCQY------DTQTVLESLSLNVEHGEIVCLLGASGCGKTTLLKAIAGLLPLSSGIMSLNGMTIDDGKH-WlapEQR 80
Cdd:PRK13633   8 KNVSYKYesneesTEKLALDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVYVDGLDTSDEENlW---DIR 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099586  81 N-IGMIFQ--DYALFPHLtVAENIAFGLRQM--AAEERHLQVQQMLELVHLSGFGDRYPHQLSGGQQQRVAIARSLAYKP 155
Cdd:PRK13633  85 NkAGMVFQnpDNQIVATI-VEEDVAFGPENLgiPPEEIRERVDESLKKVGMYEYRRHAPHLLSGGQKQRVAIAGILAMRP 163

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099586 156 DLLLLDEPFSNIDTQVRHDLIGEIRKIFKKQGVTAIFVTHSREEAfAFADKMAVMNHGVIEQYGTASELY 225
Cdd:PRK13633 164 ECIIFDEPTAMLDPSGRREVVNTIKELNKKYGITIILITHYMEEA-VEADRIIVMDSGKVVMEGTPKEIF 232

ABC_putative_ATPase

cd03269

ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ...

5-219

7.38e-38

ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the subfamily A transporters involved in drug resistance, nodulation, lipid transport, and bacteriocin and lantibiotic immunity. In eubacteria and archaea, the typical organization consists of one ABC and one or two integral membranes. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region in addition to the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.

Pssm-ID: 213236 [Multi-domain] Cd Length: 210 Bit Score: 134.33 E-value: 7.38e-38

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099586   5 LSIQNLTCQYDTQTVLESLSLNVEHGEIVCLLGASGCGKTTLLKAIAGLLPLSSGIMSLNG--MTIDDGKH--WLaPEQR 80
Cdd:cd03269    1 LEVENVTKRFGRVTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDGkpLDIAARNRigYL-PEER 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099586  81 nigmifqdyALFPHLTVAEN-IAFG-LRQMAAEERHLQVQQMLELVHLSGFGDRYPHQLSGGQQQRVAIARSLAYKPDLL 158
Cdd:cd03269   80 ---------GLYPKMKVIDQlVYLAqLKGLKKEEARRRIDEWLERLELSEYANKRVEELSKGNQQKVQFIAAVIHDPELL 150

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 521099586 159 LLDEPFSNIDTqVRHDLIGEIRKIFKKQGVTAIFVTHSREEAFAFADKMAVMNHGVIEQYG 219
Cdd:cd03269  151 ILDEPFSGLDP-VNVELLKDVIRELARAGKTVILSTHQMELVEELCDRVLLLNKGRAVLYG 210

ABC_drug_resistance_like

cd03264

ABC-type multidrug transport system, ATPase component; The biological function of this family ...

5-219

1.47e-37

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: 133.47 E-value: 1.47e-37

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099586   5 LSIQNLTCQYDTQTVLESLSLNVEHGeIVCLLGASGCGKTTLLKAIAGLLPLSSGIMSLNGmtIDDGKHWLAPEQRnIGM 84
Cdd:cd03264    1 LQLENLTKRYGKKRALDGVSLTLGPG-MYGLLGPNGAGKTTLMRILATLTPPSSGTIRIDG--QDVLKQPQKLRRR-IGY 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099586  85 IFQDYALFPHLTVAENIAF--GLRQMAAEERHLQVQQMLELVHLSGFGDRYPHQLSGGQQQRVAIARSLAYKPDLLLLDE 162
Cdd:cd03264   77 LPQEFGVYPNFTVREFLDYiaWLKGIPSKEVKARVDEVLELVNLGDRAKKKIGSLSGGMRRRVGIAQALVGDPSILIVDE 156

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 521099586 163 PFSNIDTQVRHDLigeiRKIFKKQGVTAIFV--THSREEAFAFADKMAVMNHGVIEQYG 219
Cdd:cd03264  157 PTAGLDPEERIRF----RNLLSELGEDRIVIlsTHIVEDVESLCNQVAVLNKGKLVFEG 211

nikE

PRK10419

nickel ABC transporter ATP-binding protein NikE;

5-215

2.07e-37

nickel ABC transporter ATP-binding protein NikE;

Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 134.81 E-value: 2.07e-37

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099586   5 LSIQNLTCQYDT---------QTVLESLSLNVEHGEIVCLLGASGCGKTTLLKAIAGLLPLSSGIMSLNGMTID--DGKH 73
Cdd:PRK10419   4 LNVSGLSHHYAHgglsgkhqhQTVLNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWRGEPLAklNRAQ 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099586  74 WLApEQRNIGMIFQDY--ALFPHLTVAENIAFGLRQ---MAAEERHLQVQQMLELVHLS-GFGDRYPHQLSGGQQQRVAI 147
Cdd:PRK10419  84 RKA-FRRDIQMVFQDSisAVNPRKTVREIIREPLRHllsLDKAERLARASEMLRAVDLDdSVLDKRPPQLSGGQLQRVCL 162

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 521099586 148 ARSLAYKPDLLLLDEPFSNIDTQVRHDLIGEIRKIFKKQGVTAIFVTHSREEAFAFADKMAVMNHGVI 215
Cdd:PRK10419 163 ARALAVEPKLLILDEAVSNLDLVLQAGVIRLLKKLQQQFGTACLFITHDLRLVERFCQRVMVMDNGQI 230

YejF

COG4172

ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ...

5-228

3.12e-37

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: 139.82 E-value: 3.12e-37

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099586   5 LSIQNLTCQYDT----QTVLESLSLNVEHGEIVCLLGASGCGKT-TLLkAIAGLLPLSSGIMSlnGMTIDDGKHWL-APE 78
Cdd:COG4172    7 LSVEDLSVAFGQgggtVEAVKGVSFDIAAGETLALVGESGSGKSvTAL-SILRLLPDPAAHPS--GSILFDGQDLLgLSE 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099586  79 Q-------RNIGMIFQD--YALFPHLTVAENIA------FGLRQMAAEERhlqVQQMLELVHLSGFG---DRYPHQLSGG 140
Cdd:COG4172   84 RelrrirgNRIAMIFQEpmTSLNPLHTIGKQIAevlrlhRGLSGAAARAR---ALELLERVGIPDPErrlDAYPHQLSGG 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099586 141 QQQRVAIARSLAYKPDLLLLDEPFSNIDTQVRH---DLIGEIRkifKKQGVTAIFVTH-----SReeafaFADKMAVMNH 212
Cdd:COG4172  161 QRQRVMIAMALANEPDLLIADEPTTALDVTVQAqilDLLKDLQ---RELGMALLLITHdlgvvRR-----FADRVAVMRQ 232

                        250
                 ....*....|....*.
gi 521099586 213 GVIEQYGTASELYYRP 228
Cdd:COG4172  233 GEIVEQGPTAELFAAP 248

cbiO

PRK13639

cobalt transporter ATP-binding subunit; Provisional

5-225

4.90e-37

cobalt transporter ATP-binding subunit; Provisional

Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 134.05 E-value: 4.90e-37

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099586   5 LSIQNLTCQYDTQT-VLESLSLNVEHGEIVCLLGASGCGKTTLLKAIAGLLPLSSGIMSLNGMTIDDGKHWLAPEQRNIG 83
Cdd:PRK13639   2 LETRDLKYSYPDGTeALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIKGEPIKYDKKSLLEVRKTVG 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099586  84 MIFQ--DYALF-PhlTVAENIAFGLRQMA--AEERHLQVQQMLELVHLSGFGDRYPHQLSGGQQQRVAIARSLAYKPDLL 158
Cdd:PRK13639  82 IVFQnpDDQLFaP--TVEEDVAFGPLNLGlsKEEVEKRVKEALKAVGMEGFENKPPHHLSGGQKKRVAIAGILAMKPEII 159

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 521099586 159 LLDEPFSNIDTQ-------VRHDLigeirkifKKQGVTAIFVTHSREEAFAFADKMAVMNHGVIEQYGTASELY 225
Cdd:PRK13639 160 VLDEPTSGLDPMgasqimkLLYDL--------NKEGITIIISTHDVDLVPVYADKVYVMSDGKIIKEGTPKEVF 225

ABCC_MsbA

cd03251

ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ...

5-225

1.20e-36

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: 131.97 E-value: 1.20e-36

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099586   5 LSIQNLTCQY--DTQTVLESLSLNVEHGEIVCLLGASGCGKTTLLKAIAGLLPLSSGIMSLNGMTIDDGKhwLAPEQRNI 82
Cdd:cd03251    1 VEFKNVTFRYpgDGPPVLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDGHDVRDYT--LASLRRQI 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099586  83 GMIFQDYALFpHLTVAENIAFGLRQMAAEErhlqVQQMLELVHLSGFGDRYPH-----------QLSGGQQQRVAIARSL 151
Cdd:cd03251   79 GLVSQDVFLF-NDTVAENIAYGRPGATREE----VEEAARAANAHEFIMELPEgydtvigergvKLSGGQRQRIAIARAL 153

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 521099586 152 AYKPDLLLLDEPFSNIDTQVRHDLIGEIRKIFKkqGVTAIFVTHsREEAFAFADKMAVMNHGVIEQYGTASELY 225
Cdd:cd03251  154 LKDPPILILDEATSALDTESERLVQAALERLMK--NRTTFVIAH-RLSTIENADRIVVLEDGKIVERGTHEELL 224

NupO

COG3845

ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ...

1-213

2.08e-36

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

Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 137.08 E-value: 2.08e-36

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099586   1 MSCALSIQNLTCQYDTQTVLESLSLNVEHGEIVCLLGASGCGKTTLLKAIAGLLPLSSGIMSLNG--MTIDDGKHWLApe 78
Cdd:COG3845    2 MPPALELRGITKRFGGVVANDDVSLTVRPGEIHALLGENGAGKSTLMKILYGLYQPDSGEILIDGkpVRIRSPRDAIA-- 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099586  79 qRNIGMIFQDYALFPHLTVAENIAFGLRQ-------MAAEERHLQvqqmlELVHLSGFG---DRYPHQLSGGQQQRVAIA 148
Cdd:COG3845   80 -LGIGMVHQHFMLVPNLTVAENIVLGLEPtkggrldRKAARARIR-----ELSERYGLDvdpDAKVEDLSVGEQQRVEIL 153

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 521099586 149 RSLAYKPDLLLLDEPFSNIDTQVRHDLIGEIRKiFKKQGVTAIFVTHSREEAFAFADKMAVMNHG 213
Cdd:COG3845  154 KALYRGARILILDEPTAVLTPQEADELFEILRR-LAAEGKSIIFITHKLREVMAIADRVTVLRRG 217

ArpD

COG4618

ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ...

5-223

2.33e-36

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: 137.96 E-value: 2.33e-36

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099586   5 LSIQNLTCQY--DTQTVLESLSLNVEHGEIVCLLGASGCGKTTLLKAIAGLLPLSSGIMSLNGMTIDdgkHWlAPEQ--R 80
Cdd:COG4618  331 LSVENLTVVPpgSKRPILRGVSFSLEPGEVLGVIGPSGSGKSTLARLLVGVWPPTAGSVRLDGADLS---QW-DREElgR 406

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099586  81 NIGMIFQDYALFPHlTVAENIAfglR-------------QMAAeerhlqvqqmlelVH--LSGFGDRY-------PHQLS 138
Cdd:COG4618  407 HIGYLPQDVELFDG-TIAENIA---RfgdadpekvvaaaKLAG-------------VHemILRLPDGYdtrigegGARLS 469

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099586 139 GGQQQRVAIARSLAYKPDLLLLDEPFSNIDTQVRHDLIGEIRKIfKKQGVTAIFVTHsREEAFAFADKMAVMNHGVIEQY 218
Cdd:COG4618  470 GGQRQRIGLARALYGDPRLVVLDEPNSNLDDEGEAALAAAIRAL-KARGATVVVITH-RPSLLAAVDKLLVLRDGRVQAF 547


                 ....*
gi 521099586 219 GTASE 223
Cdd:COG4618  548 GPRDE 552

ABCC_Protease_Secretion

cd03246

ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ...

5-215

2.56e-36

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: 129.26 E-value: 2.56e-36

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099586   5 LSIQNLTCQY--DTQTVLESLSLNVEHGEIVCLLGASGCGKTTLLKAIAGLLPLSSGIMSLNGMTIDDgkhwLAPEQ--R 80
Cdd:cd03246    1 LEVENVSFRYpgAEPPVLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDGADISQ----WDPNElgD 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099586  81 NIGMIFQDYALFPHlTVAENIafglrqmaaeerhlqvqqmlelvhlsgfgdryphqLSGGQQQRVAIARSLAYKPDLLLL 160
Cdd:cd03246   77 HVGYLPQDDELFSG-SIAENI-----------------------------------LSGGQRQRLGLARALYGNPRILVL 120

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 521099586 161 DEPFSNIDTQVRHDLIGEIRKIfKKQGVTAIFVTHsREEAFAFADKMAVMNHGVI 215
Cdd:cd03246  121 DEPNSHLDVEGERALNQAIAAL-KAAGATRIVIAH-RPETLASADRILVLEDGRV 173

ABC_NatA_sodium_exporter

cd03266

ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ...

5-215

3.28e-36

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: 130.18 E-value: 3.28e-36

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099586   5 LSIQNLTCQYD----TQTVLESLSLNVEHGEIVCLLGASGCGKTTLLKAIAGLLPLSSGIMSLNGMtidDGKHWLAPEQR 80
Cdd:cd03266    2 ITADALTKRFRdvkkTVQAVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDGF---DVVKEPAEARR 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099586  81 NIGMIFQDYALFPHLTVAENIAF--GLRQMAAEERHLQVQQMLELVHLSGFGDRYPHQLSGGQQQRVAIARSLAYKPDLL 158
Cdd:cd03266   79 RLGFVSDSTGLYDRLTARENLEYfaGLYGLKGDELTARLEELADRLGMEELLDRRVGGFSTGMRQKVAIARALVHDPPVL 158

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 521099586 159 LLDEPFSNIDTQVRHDLIGEIRKIfKKQGVTAIFVTHSREEAFAFADKMAVMNHGVI 215
Cdd:cd03266  159 LLDEPTTGLDVMATRALREFIRQL-RALGKCILFSTHIMQEVERLCDRVVVLHRGRV 214

YhaQ

COG4152

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

4-224

4.07e-36

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

Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 132.15 E-value: 4.07e-36

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099586   4 ALSIQNLTCQYDTQTVLESLSLNVEHGEIVCLLGASGCGKTTLLKAIAGLLPLSSGIMSLNGMTIDDGKhwlapeQRNIG 83
Cdd:COG4152    1 MLELKGLTKRFGDKTAVDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDSGEVLWDGEPLDPED------RRRIG 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099586  84 mifqdY-----ALFPHLTVAENIAF--GLRQMAAEERHLQVQQMLELVHLSGFGDRYPHQLSGGQQQRVAIARSLAYKPD 156
Cdd:COG4152   75 -----YlpeerGLYPKMKVGEQLVYlaRLKGLSKAEAKRRADEWLERLGLGDRANKKVEELSKGNQQKVQLIAALLHDPE 149

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 521099586 157 LLLLDEPFS-----NIDTqvrhdLIGEIRKiFKKQGVTAIFVTHSREEAFAFADKMAVMNHGVIEQYGTASEL 224
Cdd:COG4152  150 LLILDEPFSgldpvNVEL-----LKDVIRE-LAAKGTTVIFSSHQMELVEELCDRIVIINKGRKVLSGSVDEI 216

PRK11831

phospholipid ABC transporter ATP-binding protein MlaF;

19-239

2.02e-35

phospholipid ABC transporter ATP-binding protein MlaF;

Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 129.88 E-value: 2.02e-35

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099586  19 VLESLSLNVEHGEIVCLLGASGCGKTTLLKAIAGLLPLSSGIMSLNGMTIDD-GKHWLAPEQRNIGMIFQDYALFPHLTV 97
Cdd:PRK11831  22 IFDNISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEILFDGENIPAmSRSRLYTVRKRMSMLFQSGALFTDMNV 101

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099586  98 AENIAFGLR---QMAAEERHLQVQQMLELVHLSGFGDRYPHQLSGGQQQRVAIARSLAYKPDLLLLDEPFSNIDTQVRHD 174
Cdd:PRK11831 102 FDNVAYPLRehtQLPAPLLHSTVMMKLEAVGLRGAAKLMPSELSGGMARRAALARAIALEPDLIMFDEPFVGQDPITMGV 181

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 521099586 175 LIGEIRKIFKKQGVTAIFVTHSREEAFAFADKMAVMNHGVIEQYGTASELYYRPSSKfVADFLGG 239
Cdd:PRK11831 182 LVKLISELNSALGVTCVVVSHDVPEVLSIADHAYIVADKKIVAHGSAQALQANPDPR-VRQFLDG 245

PRK15079

oligopeptide ABC transporter ATP-binding protein OppF; Provisional

24-229

8.98e-35

oligopeptide ABC transporter ATP-binding protein OppF; Provisional

Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 129.44 E-value: 8.98e-35

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099586  24 SLNVEHGEIVCLLGASGCGKTTLLKAIAGLLPLSSGIMSLNG--MTIDDGKHWLApEQRNIGMIFQD--YALFPHLTVAE 99
Cdd:PRK15079  41 TLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGEVAWLGkdLLGMKDDEWRA-VRSDIQMIFQDplASLNPRMTIGE 119

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099586 100 NIAFGLR----QMAAEERHLQVQQMLELVHL-SGFGDRYPHQLSGGQQQRVAIARSLAYKPDLLLLDEPFSNIDTQVRHD 174
Cdd:PRK15079 120 IIAEPLRtyhpKLSRQEVKDRVKAMMLKVGLlPNLINRYPHEFSGGQCQRIGIARALILEPKLIICDEPVSALDVSIQAQ 199

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 521099586 175 LIGEIRKIFKKQGVTAIFVTHSREEAFAFADKMAVMNHGVIEQYGTASELYYRPS 229
Cdd:PRK15079 200 VVNLLQQLQREMGLSLIFIAHDLAVVKHISDRVLVMYLGHAVELGTYDEVYHNPL 254

PRK14267

phosphate ABC transporter ATP-binding protein; Provisional

1-239

9.30e-35

phosphate ABC transporter ATP-binding protein; Provisional

Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 127.65 E-value: 9.30e-35

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099586   1 MSCALSIQNLTCQYDTQTVLESLSLNVEHGEIVCLLGASGCGKTTLLKAIAGLLPLSSgIMSLNGMTIDDGKHWLAPE-- 78
Cdd:PRK14267   1 MKFAIETVNLRVYYGSNHVIKGVDLKIPQNGVFALMGPSGCGKSTLLRTFNRLLELNE-EARVEGEVRLFGRNIYSPDvd 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099586  79 ----QRNIGMIFQDYALFPHLTVAENIAFGLR----QMAAEERHLQVQQMLELVHL-SGFGDR---YPHQLSGGQQQRVA 146
Cdd:PRK14267  80 pievRREVGMVFQYPNPFPHLTIYDNVAIGVKlnglVKSKKELDERVEWALKKAALwDEVKDRlndYPSNLSGGQRQRLV 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099586 147 IARSLAYKPDLLLLDEPFSNID---TQVRHDLIGEIRKIFkkqgvTAIFVTHSREEAFAFADKMAVMNHGVIEQYGTASE 223
Cdd:PRK14267 160 IARALAMKPKILLMDEPTANIDpvgTAKIEELLFELKKEY-----TIVLVTHSPAQAARVSDYVAFLYLGKLIEVGPTRK 234

                        250
                 ....*....|....*.
gi 521099586 224 LYYRPSSKFVADFLGG 239
Cdd:PRK14267 235 VFENPEHELTEKYVTG 250

CydD

TIGR02857

thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ...

4-210

9.33e-35

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: 133.18 E-value: 9.33e-35

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099586    4 ALSIQNLTCQY-DTQTVLESLSLNVEHGEIVCLLGASGCGKTTLLKAIAGLLPLSSGIMSLNGMTIDDG--KHWlapeQR 80
Cdd:TIGR02857 321 SLEFSGVSVAYpGRRPALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSIAVNGVPLADAdaDSW----RD 396

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099586   81 NIGMIFQDYALFPHlTVAENIAFGLRQMAAEErhlqVQQMLELVHLSGF------------GDRyPHQLSGGQQQRVAIA 148
Cdd:TIGR02857 397 QIAWVPQHPFLFAG-TIAENIRLARPDASDAE----IREALERAGLDEFvaalpqgldtpiGEG-GAGLSGGQAQRLALA 470

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 521099586  149 RSLAYKPDLLLLDEPFSNIDTQVRHDLIGEIRKIFkkQGVTAIFVTHSREEAfAFADKMAVM 210
Cdd:TIGR02857 471 RAFLRDAPLLLLDEPTAHLDAETEAEVLEALRALA--QGRTVLLVTHRLALA-ALADRIVVL 529

cbiO

PRK13648

cobalt transporter ATP-binding subunit; Provisional

13-225

2.59e-34

cobalt transporter ATP-binding subunit; Provisional

Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 126.79 E-value: 2.59e-34

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099586  13 QYDTQTVLESLSLNVEHGEIVCLLGASGCGKTTLLKAIAGLLPLSSGIMSLNGMTIDDgkHWLAPEQRNIGMIFQD-YAL 91
Cdd:PRK13648  18 QSDASFTLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIFYNNQAITD--DNFEKLRKHIGIVFQNpDNQ 95

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099586  92 FPHLTVAENIAFGLRQMAA--EERHLQVQQMLELVHLSGFGDRYPHQLSGGQQQRVAIARSLAYKPDLLLLDEPFSNIDT 169
Cdd:PRK13648  96 FVGSIVKYDVAFGLENHAVpyDEMHRRVSEALKQVDMLERADYEPNALSGGQKQRVAIAGVLALNPSVIILDEATSMLDP 175

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 521099586 170 QVRHDLIGEIRKIFKKQGVTAIFVTHSREEAfAFADKMAVMNHGVIEQYGTASELY 225
Cdd:PRK13648 176 DARQNLLDLVRKVKSEHNITIISITHDLSEA-MEADHVIVMNKGTVYKEGTPTEIF 230

PRK14239

phosphate transporter ATP-binding protein; Provisional

5-239

2.68e-34

phosphate transporter ATP-binding protein; Provisional

Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 126.43 E-value: 2.68e-34

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099586   5 LSIQNLTCQYDTQTVLESLSLNVEHGEIVCLLGASGCGKTTLLKAIAGLLPLSSGImSLNGMTIDDGKHWLAPE------ 78
Cdd:PRK14239   6 LQVSDLSVYYNKKKALNSVSLDFYPNEITALIGPSGSGKSTLLRSINRMNDLNPEV-TITGSIVYNGHNIYSPRtdtvdl 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099586  79 QRNIGMIFQDYALFPhLTVAENIAFGLRQM---------AAEERHLQVQQMLELV----HLSGFGdryphqLSGGQQQRV 145
Cdd:PRK14239  85 RKEIGMVFQQPNPFP-MSIYENVVYGLRLKgikdkqvldEAVEKSLKGASIWDEVkdrlHDSALG------LSGGQQQRV 157

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099586 146 AIARSLAYKPDLLLLDEPFSNID----TQVRHDLIGeirkifKKQGVTAIFVTHSREEAFAFADKMAVMNHGVIEQYGTA 221
Cdd:PRK14239 158 CIARVLATSPKIILLDEPTSALDpisaGKIEETLLG------LKDDYTMLLVTRSMQQASRISDRTGFFLDGDLIEYNDT 231

                        250
                 ....*....|....*...
gi 521099586 222 SELYYRPSSKFVADFLGG 239
Cdd:PRK14239 232 KQMFMNPKHKETEDYISG 249

CeuD

COG4604

ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ...

6-224

8.54e-34

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

Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 124.81 E-value: 8.54e-34

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099586   6 SIQNLTCQYDTQTVLESLSLNVEHGEIVCLLGASGCGKTTLLKAIAGLLPLSSGIMSLNGMTIddgKHW----LApeqRN 81
Cdd:COG4604    3 EIKNVSKRYGGKVVLDDVSLTIPKGGITALIGPNGAGKSTLLSMISRLLPPDSGEVLVDGLDV---ATTpsreLA---KR 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099586  82 IGMIFQDYALFPHLTVAENIAFGL------RQMAAEERHlqVQQMLELVHLSGFGDRYPHQLSGGQQQRVAIARSLAYKP 155
Cdd:COG4604   77 LAILRQENHINSRLTVRELVAFGRfpyskgRLTAEDREI--IDEAIAYLDLEDLADRYLDELSGGQRQRAFIAMVLAQDT 154

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 521099586 156 DLLLLDEPFSNIDtqVRH--DLIGEIRKIFKKQGVTAIFVTHSREEAFAFADKMAVMNHGVIEQYGTASEL 224
Cdd:COG4604  155 DYVLLDEPLNNLD--MKHsvQMMKLLRRLADELGKTVVIVLHDINFASCYADHIVAMKDGRVVAQGTPEEI 223

cbiO

PRK13631

cobalt transporter ATP-binding subunit; Provisional

5-228

1.03e-33

cobalt transporter ATP-binding subunit; Provisional

Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 126.50 E-value: 1.03e-33

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099586   5 LSIQNLTCQYDTQT-----VLESLSLNVEHGEIVCLLGASGCGKTTLLKAIAGLLPLSSGIMSL----NGMTIDDGKHWL 75
Cdd:PRK13631  22 LRVKNLYCVFDEKQenelvALNNISYTFEKNKIYFIIGNSGSGKSTLVTHFNGLIKSKYGTIQVgdiyIGDKKNNHELIT 101

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099586  76 APEQRNI----------GMIFQ--DYALFPHlTVAENIAFG---LRQMAAEERHLQVQQMLELVHLSGFGDRYPHQLSGG 140
Cdd:PRK13631 102 NPYSKKIknfkelrrrvSMVFQfpEYQLFKD-TIEKDIMFGpvaLGVKKSEAKKLAKFYLNKMGLDDSYLERSPFGLSGG 180

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099586 141 QQQRVAIARSLAYKPDLLLLDEPFSNIDTQVRHDLIgEIRKIFKKQGVTAIFVTHSREEAFAFADKMAVMNHGVIEQYGT 220
Cdd:PRK13631 181 QKRRVAIAGILAIQPEILIFDEPTAGLDPKGEHEMM-QLILDAKANNKTVFVITHTMEHVLEVADEVIVMDKGKILKTGT 259


                 ....*...
gi 521099586 221 ASELYYRP 228
Cdd:PRK13631 260 PYEIFTDQ 267

cbiO

PRK13652

cobalt transporter ATP-binding subunit; Provisional

5-228

1.71e-33

cobalt transporter ATP-binding subunit; Provisional

Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 124.92 E-value: 1.71e-33

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099586   5 LSIQNLTCQYDTQT-VLESLSLNVEHGEIVCLLGASGCGKTTLLKAIAGLLPLSSGIMSLNGMTIDdgKHWLAPEQRNIG 83
Cdd:PRK13652   4 IETRDLCYSYSGSKeALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIRGEPIT--KENIREVRKFVG 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099586  84 MIFQ--DYALFPHlTVAENIAFGLRQMAAEERHL--QVQQMLELVHLSGFGDRYPHQLSGGQQQRVAIARSLAYKPDLLL 159
Cdd:PRK13652  82 LVFQnpDDQIFSP-TVEQDIAFGPINLGLDEETVahRVSSALHMLGLEELRDRVPHHLSGGEKKRVAIAGVIAMEPQVLV 160

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 521099586 160 LDEPFSNIDTQVRHDLIGEIRKIFKKQGVTAIFVTHSREEAFAFADKMAVMNHGVIEQYGTASELYYRP 228
Cdd:PRK13652 161 LDEPTAGLDPQGVKELIDFLNDLPETYGMTVIFSTHQLDLVPEMADYIYVMDKGRIVAYGTVEEIFLQP 229

cbiO

PRK13641

energy-coupling factor transporter ATPase;

20-240

2.08e-33

energy-coupling factor transporter ATPase;

Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 124.94 E-value: 2.08e-33

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099586  20 LESLSLNVEHGEIVCLLGASGCGKTTLLKAIAGLLPLSSGIMSLNGMTI--DDGKHWLAPEQRNIGMIFQ--DYALFPHl 95
Cdd:PRK13641  23 LDNISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITIAGYHItpETGNKNLKKLRKKVSLVFQfpEAQLFEN- 101

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099586  96 TVAENIAFGLRQMAAEERHLQVQ--QMLELVHLS-GFGDRYPHQLSGGQQQRVAIARSLAYKPDLLLLDEPFSNIDTQVR 172
Cdd:PRK13641 102 TVLKDVEFGPKNFGFSEDEAKEKalKWLKKVGLSeDLISKSPFELSGGQMRRVAIAGVMAYEPEILCLDEPAAGLDPEGR 181

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099586 173 HDLIgEIRKIFKKQGVTAIFVTHSREEAFAFADKMAVMNHGVIEQYGTASELYYRP------------SSKFVADFLGGG 240
Cdd:PRK13641 182 KEMM-QLFKDYQKAGHTVILVTHNMDDVAEYADDVLVLEHGKLIKHASPKEIFSDKewlkkhyldepaTSRFASKLEKGG 260

cbiO

PRK13640

energy-coupling factor transporter ATPase;

4-229

2.10e-33

energy-coupling factor transporter ATPase;

Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 124.91 E-value: 2.10e-33

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099586   4 ALSIQNLTCQY-DTQT-VLESLSLNVEHGEIVCLLGASGCGKTTLLKAIAGLL---PLSSGIMSLNGMTIDDGKHWLAPE 78
Cdd:PRK13640   5 IVEFKHVSFTYpDSKKpALNDISFSIPRGSWTALIGHNGSGKSTISKLINGLLlpdDNPNSKITVDGITLTAKTVWDIRE 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099586  79 QrnIGMIFQDY-ALFPHLTVAENIAFGL--RQMAAEERHLQVQQMLELVHLSGFGDRYPHQLSGGQQQRVAIARSLAYKP 155
Cdd:PRK13640  85 K--VGIVFQNPdNQFVGATVGDDVAFGLenRAVPRPEMIKIVRDVLADVGMLDYIDSEPANLSGGQKQRVAIAGILAVEP 162

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 521099586 156 DLLLLDEPFSNIDTQVRHDLIGEIRKIFKKQGVTAIFVTHSREEAfAFADKMAVMNHGVIEQYGTASELYYRPS 229
Cdd:PRK13640 163 KIIILDESTSMLDPAGKEQILKLIRKLKKKNNLTVISITHDIDEA-NMADQVLVLDDGKLLAQGSPVEIFSKVE 235

fecE

PRK11231

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

5-223

3.16e-33

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

Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 123.59 E-value: 3.16e-33

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099586   5 LSIQNLTCQYDTQTVLESLSLNVEHGEIVCLLGASGCGKTTLLKAIAGLLPLSSGIMSLNGMTIDDgkhwLAPEQ--RNI 82
Cdd:PRK11231   3 LRTENLTVGYGTKRILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDKPISM----LSSRQlaRRL 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099586  83 GMIFQDYALFPHLTVAENIAFGlR--------QMAAEERHLqVQQMLELVHLSGFGDRYPHQLSGGQQQRVAIARSLAYK 154
Cdd:PRK11231  79 ALLPQHHLTPEGITVRELVAYG-RspwlslwgRLSAEDNAR-VNQAMEQTRINHLADRRLTDLSGGQRQRAFLAMVLAQD 156

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 521099586 155 PDLLLLDEPFSNIDTQVRHDLIGEIRKIfKKQGVTAIFVTHSREEAFAFADKMAVMNHGVIEQYGTASE 223
Cdd:PRK11231 157 TPVVLLDEPTTYLDINHQVELMRLMREL-NTQGKTVVTVLHDLNQASRYCDHLVVLANGHVMAQGTPEE 224

type_I_sec_PrtD

TIGR01842

type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in ...

17-224

4.63e-33

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: 128.62 E-value: 4.63e-33

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099586   17 QTVLESLSLNVEHGEIVCLLGASGCGKTTLLKAIAGLLPLSSGIMSLNGMTIddgKHWlAPEQ--RNIGMIFQDYALFPH 94
Cdd:TIGR01842 331 KPTLRGISFSLQAGEALAIIGPSGSGKSTLARLIVGIWPPTSGSVRLDGADL---KQW-DRETfgKHIGYLPQDVELFPG 406

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099586   95 lTVAENIA-FGlrqmaaeeRHLQVQQMLELVHLSGFGD---RYPH-----------QLSGGQQQRVAIARSLAYKPDLLL 159
Cdd:TIGR01842 407 -TVAENIArFG--------ENADPEKIIEAAKLAGVHElilRLPDgydtvigpggaTLSGGQRQRIALARALYGDPKLVV 477

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 521099586  160 LDEPFSNIDTQVRHDLIGEIRKIfKKQGVTAIFVTHsREEAFAFADKMAVMNHGVIEQYGTASEL 224
Cdd:TIGR01842 478 LDEPNSNLDEEGEQALANAIKAL-KARGITVVVITH-RPSLLGCVDKILVLQDGRIARFGERDEV 540

ABC_Carb_Monos_II

cd03215

Second domain of the ATP-binding cassette component of monosaccharide transport system; This ...

4-213

1.01e-32

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: 119.84 E-value: 1.01e-32

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099586   4 ALSIQNLTCQYdtqtVLESLSLNVEHGEIVCLLGASGCGKTTLLKAIAGLLPLSSGIMSLNGMTIddgkHWLAPEQRN-- 81
Cdd:cd03215    4 VLEVRGLSVKG----AVRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITLDGKPV----TRRSPRDAIra 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099586  82 -IGMIFQD---YALFPHLTVAENIAFglrqmaaeerhlqvqqmlelvhlsgfgdryPHQLSGGQQQRVAIARSLAYKPDL 157
Cdd:cd03215   76 gIAYVPEDrkrEGLVLDLSVAENIAL------------------------------SSLLSGGNQQKVVLARWLARDPRV 125

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 521099586 158 LLLDEPFSNIDTQVRHDLIGEIRKiFKKQGVTAIFVTHSREEAFAFADKMAVMNHG 213
Cdd:cd03215  126 LILDEPTRGVDVGAKAEIYRLIRE-LADAGKAVLLISSELDELLGLCDRILVMYEG 180

PRK14246

phosphate ABC transporter ATP-binding protein; Provisional

5-239

2.74e-32

phosphate ABC transporter ATP-binding protein; Provisional

Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 121.31 E-value: 2.74e-32

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099586   5 LSIQNLTCQYDTQTVLESLSLNVEHGEIVCLLGASGCGKTTLLKAIAGLLPLSSGIMSLNGMTIDDGKHWLAPE----QR 80
Cdd:PRK14246  11 FNISRLYLYINDKAILKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLIEIYDSKIKVDGKVLYFGKDIFQIDaiklRK 90

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099586  81 NIGMIFQDYALFPHLTVAENIAFGLRQMAAEERHLQVQQMLELVHLSGFG----DRY---PHQLSGGQQQRVAIARSLAY 153
Cdd:PRK14246  91 EVGMVFQQPNPFPHLSIYDNIAYPLKSHGIKEKREIKKIVEECLRKVGLWkevyDRLnspASQLSGGQQQRLTIARALAL 170

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099586 154 KPDLLLLDEPFSNID---TQVRHDLIGEIrkifkKQGVTAIFVTHSREEAFAFADKMAVMNHGVIEQYGTASELYYRPSS 230
Cdd:PRK14246 171 KPKVLLMDEPTSMIDivnSQAIEKLITEL-----KNEIAIVIVSHNPQQVARVADYVAFLYNGELVEWGSSNEIFTSPKN 245


                 ....*....
gi 521099586 231 KFVADFLGG 239
Cdd:PRK14246 246 ELTEKYVIG 254

cbiO

PRK13642

energy-coupling factor transporter ATPase;

1-252

2.83e-32

energy-coupling factor transporter ATPase;

Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 121.74 E-value: 2.83e-32

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099586   1 MSCALSIQNLTCQYDTQT---VLESLSLNVEHGEIVCLLGASGCGKTTLLKAIAGLLPLSSGIMSLNGMTIDDGKHWlaP 77
Cdd:PRK13642   1 MNKILEVENLVFKYEKESdvnQLNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDGELLTAENVW--N 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099586  78 EQRNIGMIFQDY-ALFPHLTVAENIAFGLRQ--MAAEERHLQVQQMLELVHLSGFGDRYPHQLSGGQQQRVAIARSLAYK 154
Cdd:PRK13642  79 LRRKIGMVFQNPdNQFVGATVEDDVAFGMENqgIPREEMIKRVDEALLAVNMLDFKTREPARLSGGQKQRVAVAGIIALR 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099586 155 PDLLLLDEPFSNIDTQVRHDLIGEIRKIFKKQGVTAIFVTHSREEAfAFADKMAVMNHGVIEQYGTASELYYRP------ 228
Cdd:PRK13642 159 PEIIILDESTSMLDPTGRQEIMRVIHEIKEKYQLTVLSITHDLDEA-ASSDRILVMKAGEIIKEAAPSELFATSedmvei 237

                        250       260       270
                 ....*....|....*....|....*....|
gi 521099586 229 ------SSKFVADFLGGGSYLPATRLAEHQ 252
Cdd:PRK13642 238 gldvpfSSNLMKDLRKNGFDLPEKYLSEDE 267

ABCC_ATM1_transporter

cd03253

ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ...

9-224

1.32e-31

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: 118.87 E-value: 1.32e-31

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099586   9 NLTCQYDT-QTVLESLSLNVEHGEIVCLLGASGCGKTTLLKAIAGLLPLSSGIMSLNGMTIDDGKhwLAPEQRNIGMIFQ 87
Cdd:cd03253    5 NVTFAYDPgRPVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDGQDIREVT--LDSLRRAIGVVPQ 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099586  88 DYALFpHLTVAENIAFGlRQMAAEErhlQVQQMLELVHLSGFGDRYPHQ-----------LSGGQQQRVAIARSLAYKPD 156
Cdd:cd03253   83 DTVLF-NDTIGYNIRYG-RPDATDE---EVIEAAKAAQIHDKIMRFPDGydtivgerglkLSGGEKQRVAIARAILKNPP 157

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 521099586 157 LLLLDEPFSNIDTQVRHDLIGEIRKIFKkqGVTAIFVTHsREEAFAFADKMAVMNHGVIEQYGTASEL 224
Cdd:cd03253  158 ILLLDEATSALDTHTEREIQAALRDVSK--GRTTIVIAH-RLSTIVNADKIIVLKDGRIVERGTHEEL 222

type_I_sec_LssB

TIGR03375

type I secretion system ATPase, LssB family; Type I protein secretion is a system in some ...

9-215

1.33e-31

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: 125.36 E-value: 1.33e-31

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099586    9 NLTCQY--DTQTVLESLSLNVEHGEIVCLLGASGCGKTTLLKAIAGLLPLSSGIMSLNGMTIddgkHWLAPE--QRNIGM 84
Cdd:TIGR03375 468 NVSFAYpgQETPALDNVSLTIRPGEKVAIIGRIGSGKSTLLKLLLGLYQPTEGSVLLDGVDI----RQIDPAdlRRNIGY 543

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099586   85 IFQDYALFpHLTVAENIAFGlRQMAAEERHLQVqqmLELVHLSGFGDRYPH-----------QLSGGQQQRVAIARSLAY 153
Cdd:TIGR03375 544 VPQDPRLF-YGTLRDNIALG-APYADDEEILRA---AELAGVTEFVRRHPDgldmqigergrSLSGGQRQAVALARALLR 618

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 521099586  154 KPDLLLLDEPFSNIDTQVRHDLIGEIRKIFKKQgvTAIFVTHsREEAFAFADKMAVMNHGVI 215
Cdd:TIGR03375 619 DPPILLLDEPTSAMDNRSEERFKDRLKRWLAGK--TLVLVTH-RTSLLDLVDRIIVMDNGRI 677

ccmA

TIGR01189

heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ...

5-195

1.43e-31

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: 117.46 E-value: 1.43e-31

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099586    5 LSIQNLTCQYDTQTVLESLSLNVEHGEIVCLLGASGCGKTTLLKAIAGLLPLSSGIMSLNGMTIDDGKHWLapeQRNIGM 84
Cdd:TIGR01189   1 LAARNLACSRGERMLFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRWNGTPLAEQRDEP---HENILY 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099586   85 IFQDYALFPHLTVAENIAFGLRQMAAEERhlQVQQMLELVHLSGFGDRYPHQLSGGQQQRVAIARSLAYKPDLLLLDEPF 164
Cdd:TIGR01189  78 LGHLPGLKPELSALENLHFWAAIHGGAQR--TIEDALAAVGLTGFEDLPAAQLSAGQQRRLALARLWLSRRPLWILDEPT 155

                         170       180       190
                  ....*....|....*....|....*....|.
gi 521099586  165 SNIDTQVRHDLIGEIRKIFKKQGVtAIFVTH 195
Cdd:TIGR01189 156 TALDKAGVALLAGLLRAHLARGGI-VLLTTH 185

PRK10895

lipopolysaccharide ABC transporter ATP-binding protein; Provisional

5-224

2.29e-31

lipopolysaccharide ABC transporter ATP-binding protein; Provisional

Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 118.46 E-value: 2.29e-31

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099586   5 LSIQNLTCQYDTQTVLESLSLNVEHGEIVCLLGASGCGKTTLLKAIAGLLPLSSGimslnGMTIDDGKHWLAP----EQR 80
Cdd:PRK10895   4 LTAKNLAKAYKGRRVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAG-----NIIIDDEDISLLPlharARR 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099586  81 NIGMIFQDYALFPHLTVAENIAFGL---RQMAAEERHLQVQQMLELVHLSGFGDRYPHQLSGGQQQRVAIARSLAYKPDL 157
Cdd:PRK10895  79 GIGYLPQEASIFRRLSVYDNLMAVLqirDDLSAEQREDRANELMEEFHIEHLRDSMGQSLSGGERRRVEIARALAANPKF 158

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 521099586 158 LLLDEPFSNIDTQVRHDlIGEIRKIFKKQGVTAIFVTHSREEAFAFADKMAVMNHGVIEQYGTASEL 224
Cdd:PRK10895 159 ILLDEPFAGVDPISVID-IKRIIEHLRDSGLGVLITDHNVRETLAVCERAYIVSQGHLIAHGTPTEI 224

PRK13537

nodulation factor ABC transporter ATP-binding protein NodI;

1-213

1.02e-30

nodulation factor ABC transporter ATP-binding protein NodI;

Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 118.37 E-value: 1.02e-30

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099586   1 MSCA-LSIQNLTCQYDTQTVLESLSLNVEHGEIVCLLGASGCGKTTLLKAIAGLLPLSSGIMSLNGMTIDDGkhwlAPEQ 79
Cdd:PRK13537   3 MSVApIDFRNVEKRYGDKLVVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCGEPVPSR----ARHA 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099586  80 R-NIGMIFQDYALFPHLTVAENIA-----FGLRQMAAEERhlqVQQMLELVHLSGFGDRYPHQLSGGQQQRVAIARSLAY 153
Cdd:PRK13537  79 RqRVGVVPQFDNLDPDFTVRENLLvfgryFGLSAAAARAL---VPPLLEFAKLENKADAKVGELSGGMKRRLTLARALVN 155

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099586 154 KPDLLLLDEPFSNIDTQVRHdLIGEIRKIFKKQGVTAIFVTHSREEAFAFADKMAVMNHG 213
Cdd:PRK13537 156 DPDVLVLDEPTTGLDPQARH-LMWERLRSLLARGKTILLTTHFMEEAERLCDRLCVIEEG 214

PRK14247

phosphate ABC transporter ATP-binding protein; Provisional

5-242

1.04e-30

phosphate ABC transporter ATP-binding protein; Provisional

Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 116.94 E-value: 1.04e-30

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099586   5 LSIQNLTCQYDTQTVLESLSLNVEHGEIVCLLGASGCGKTTLLKAIAGLLPLS-----SGIMSLNGMTIddGKHWLAPEQ 79
Cdd:PRK14247   4 IEIRDLKVSFGQVEVLDGVNLEIPDNTITALMGPSGSGKSTLLRVFNRLIELYpearvSGEVYLDGQDI--FKMDVIELR 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099586  80 RNIGMIFQDYALFPHLTVAENIAFGLR--QMAAEERHLQ--VQQMLELVHL-SGFGDRY---PHQLSGGQQQRVAIARSL 151
Cdd:PRK14247  82 RRVQMVFQIPNPIPNLSIFENVALGLKlnRLVKSKKELQerVRWALEKAQLwDEVKDRLdapAGKLSGGQQQRLCIARAL 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099586 152 AYKPDLLLLDEPFSNID---TQVRHDLIGEIRKifkkqGVTAIFVTHSREEAFAFADKMAVMNHGVIEQYGTASELYYRP 228
Cdd:PRK14247 162 AFQPEVLLADEPTANLDpenTAKIESLFLELKK-----DMTIVLVTHFPQQAARISDYVAFLYKGQIVEWGPTREVFTNP 236

                        250
                 ....*....|....
gi 521099586 229 SSKFVADFLGGGSY 242
Cdd:PRK14247 237 RHELTEKYVTGRLY 250

ABCC_Glucan_exporter_like

cd03254

ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ...

7-224

1.13e-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: 116.17 E-value: 1.13e-30

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099586   7 IQNLTCQYDTQT-VLESLSLNVEHGEIVCLLGASGCGKTTLLKAIAGLLPLSSGIMSLNGMTIDD-GKHWLapeQRNIGM 84
Cdd:cd03254    5 FENVNFSYDEKKpVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGIDIRDiSRKSL---RSMIGV 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099586  85 IFQDYALFPHlTVAENIAFGlRQMAAEERhlqVQQMLELVHLSGFGDRYP-----------HQLSGGQQQRVAIARSLAY 153
Cdd:cd03254   82 VLQDTFLFSG-TIMENIRLG-RPNATDEE---VIEAAKEAGAHDFIMKLPngydtvlgengGNLSQGERQLLAIARAMLR 156

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 521099586 154 KPDLLLLDEPFSNIDTQVRHDLIGEIRKIFKkqGVTAIFVTHsREEAFAFADKMAVMNHGVIEQYGTASEL 224
Cdd:cd03254  157 DPKILILDEATSNIDTETEKLIQEALEKLMK--GRTSIIIAH-RLSTIKNADKILVLDDGKIIEEGTHDEL 224

cbiO

PRK13647

cobalt transporter ATP-binding subunit; Provisional

1-224

1.25e-30

cobalt transporter ATP-binding subunit; Provisional

Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 117.14 E-value: 1.25e-30

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099586   1 MSCALSIQNLTCQY-DTQTVLESLSLNVEHGEIVCLLGASGCGKTTLLKAIAGLLPLSSGIMSLNGMTID-DGKHWLape 78
Cdd:PRK13647   1 MDNIIEVEDLHFRYkDGTKALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGREVNaENEKWV--- 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099586  79 QRNIGMIFQDY--ALFPhLTVAENIAFGLRQM--AAEERHLQVQQMLELVHLSGFGDRYPHQLSGGQQQRVAIARSLAYK 154
Cdd:PRK13647  78 RSKVGLVFQDPddQVFS-STVWDDVAFGPVNMglDKDEVERRVEEALKAVRMWDFRDKPPYHLSYGQKKRVAIAGVLAMD 156

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099586 155 PDLLLLDEPFSNIDTQVRhDLIGEIRKIFKKQGVTAIFVTHSREEAFAFADKMAVMNHGVIEQYGTASEL 224
Cdd:PRK13647 157 PDVIVLDEPMAYLDPRGQ-ETLMEILDRLHNQGKTVIVATHDVDLAAEWADQVIVLKEGRVLAEGDKSLL 225

AztA

NF040873

zinc ABC transporter ATP-binding protein AztA;

14-200

1.31e-30

zinc ABC transporter ATP-binding protein AztA;

Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 114.64 E-value: 1.31e-30

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099586  14 YDTQTVLESLSLNVEHGEIVCLLGASGCGKTTLLKAIAGLLPLSSGIMSLNGmtiddgkhwlapeQRNIGMIFQDYAL-- 91
Cdd:NF040873   2 YGGRPVLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTVRRAG-------------GARVAYVPQRSEVpd 68

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099586  92 -FPhLTVAENIAFG-------LRQMAAEERhLQVQQMLELVHLSGFGDRYPHQLSGGQQQRVAIARSLAYKPDLLLLDEP 163
Cdd:NF040873  69 sLP-LTVRDLVAMGrwarrglWRRLTRDDR-AAVDDALERVGLADLAGRQLGELSGGQRQRALLAQGLAQEADLLLLDEP 146

                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 521099586 164 FSNIDTQVRHDLIGEIRKIfKKQGVTAIFVTHSREEA 200
Cdd:NF040873 147 TTGLDAESRERIIALLAEE-HARGATVVVVTHDLELV 182

ABCG_White

cd03234

White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ...

19-215

3.26e-30

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: 114.68 E-value: 3.26e-30

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099586  19 VLESLSLNVEHGEIVCLLGASGCGKTTLLKAIAGLLP---LSSGIMSLNGMTIDDGKHwlapeQRNIGMIFQDYALFPHL 95
Cdd:cd03234   22 ILNDVSLHVESGQVMAILGSSGSGKTTLLDAISGRVEgggTTSGQILFNGQPRKPDQF-----QKCVAYVRQDDILLPGL 96

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099586  96 TVAENIAFGL-----RQMAAEERHLQVQQM-LELVHLSGFGDRYPHQLSGGQQQRVAIARSLAYKPDLLLLDEPFSNIDT 169
Cdd:cd03234   97 TVRETLTYTAilrlpRKSSDAIRKKRVEDVlLRDLALTRIGGNLVKGISGGERRRVSIAVQLLWDPKVLILDEPTSGLDS 176

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 521099586 170 QVRHDLIGEIRKIFKKqGVTAIFVTHS-REEAFAFADKMAVMNHGVI 215
Cdd:cd03234  177 FTALNLVSTLSQLARR-NRIVILTIHQpRSDLFRLFDRILLLSSGEI 222

ABCC_Hemolysin

cd03252

ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ...

15-224

4.24e-30

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: 114.89 E-value: 4.24e-30

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099586  15 DTQTVLESLSLNVEHGEIVCLLGASGCGKTTLLKAIAGLLPLSSGIMSLNGM---TIDdgKHWLapeQRNIGMIFQDYAL 91
Cdd:cd03252   13 DGPVILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGHdlaLAD--PAWL---RRQVGVVLQENVL 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099586  92 FpHLTVAENIAFGLRQMAAEE---------RHLQVQQMLE----LVHLSGFGdryphqLSGGQQQRVAIARSLAYKPDLL 158
Cdd:cd03252   88 F-NRSIRDNIALADPGMSMERvieaaklagAHDFISELPEgydtIVGEQGAG------LSGGQRQRIAIARALIHNPRIL 160

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 521099586 159 LLDEPFSNIDTQVRHDLIGEIRKIFKkqGVTAIFVTHsREEAFAFADKMAVMNHGVIEQYGTASEL 224
Cdd:cd03252  161 IFDEATSALDYESEHAIMRNMHDICA--GRTVIIIAH-RLSTVKNADRIIVMEKGRIVEQGSHDEL 223

PRK14258

phosphate ABC transporter ATP-binding protein; Provisional

4-237

1.13e-29

phosphate ABC transporter ATP-binding protein; Provisional

Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 114.36 E-value: 1.13e-29

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099586   4 ALSIQNLTCQYDTQTVLESLSLNVEHGEIVCLLGASGCGKTTLLKAIAGLLPLSS-----GIMSLNGMTIDDGKHWLAPE 78
Cdd:PRK14258   7 AIKVNNLSFYYDTQKILEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLNRMNELESevrveGRVEFFNQNIYERRVNLNRL 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099586  79 QRNIGMIFQDYALFPhLTVAENIAFGLRQMAAEERhLQVQQMLE-LVHLSGFGDRYPHQ-------LSGGQQQRVAIARS 150
Cdd:PRK14258  87 RRQVSMVHPKPNLFP-MSVYDNVAYGVKIVGWRPK-LEIDDIVEsALKDADLWDEIKHKihksaldLSGGQQQRLCIARA 164

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099586 151 LAYKPDLLLLDEPFSNIDTQVRHDLIGEIRKIFKKQGVTAIFVTHSREEAFAFADKMAVM--NHGVIEQ---YGTASELY 225
Cdd:PRK14258 165 LAVKPKVLLMDEPCFGLDPIASMKVESLIQSLRLRSELTMVIVSHNLHQVSRLSDFTAFFkgNENRIGQlveFGLTKKIF 244

                        250
                 ....*....|..
gi 521099586 226 YRPSSKFVADFL 237
Cdd:PRK14258 245 NSPHDSRTREYV 256

ABC_MTABC3_MDL1_MDL2

cd03249

ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ...

17-225

1.26e-29

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: 113.40 E-value: 1.26e-29

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099586  17 QTVLESLSLNVEHGEIVCLLGASGCGKTTLLKAIAGLLPLSSGIMSLNGMTIDDGK-HWLapeQRNIGMIFQDYALFPhL 95
Cdd:cd03249   16 VPILKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEILLDGVDIRDLNlRWL---RSQIGLVSQEPVLFD-G 91

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099586  96 TVAENIAFGLRQMAAEErhlqVQQMLELVHLSGFGDRYPH-----------QLSGGQQQRVAIARSLAYKPDLLLLDEPF 164
Cdd:cd03249   92 TIAENIRYGKPDATDEE----VEEAAKKANIHDFIMSLPDgydtlvgergsQLSGGQKQRIAIARALLRNPKILLLDEAT 167

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 521099586 165 SNIDTQVRH---DLIGEIRKifkkqGVTAIFVTHsREEAFAFADKMAVMNHGVIEQYGTASELY 225
Cdd:cd03249  168 SALDAESEKlvqEALDRAMK-----GRTTIVIAH-RLSTIRNADLIAVLQNGQVVEQGTHDELM 225

ABCG_EPDR

cd03213

Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ...

5-213

1.55e-29

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: 111.87 E-value: 1.55e-29

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099586   5 LSIQNLTCQYD------TQTVLESLSLNVEHGEIVCLLGASGCGKTTLLKAIAGLL--PLSSGIMSLNGMTIDdgKHWLa 76
Cdd:cd03213    4 LSFRNLTVTVKsspsksGKQLLKNVSGKAKPGELTAIMGPSGAGKSTLLNALAGRRtgLGVSGEVLINGRPLD--KRSF- 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099586  77 peQRNIGMIFQDYALFPHLTVAENIAFglrqmAAeerhlqvqqmlelvHLSGfgdryphqLSGGQQQRVAIARSLAYKPD 156
Cdd:cd03213   81 --RKIIGYVPQDDILHPTLTVRETLMF-----AA--------------KLRG--------LSGGERKRVSIALELVSNPS 131

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 521099586 157 LLLLDEPFSNIDTQVRHDLIGEIRKIfKKQGVTAIFVTHS-REEAFAFADKMAVMNHG 213
Cdd:cd03213  132 LLFLDEPTSGLDSSSALQVMSLLRRL-ADTGRTIICSIHQpSSEIFELFDKLLLLSQG 188

PRK10584

putative ABC transporter ATP-binding protein YbbA; Provisional

18-200

2.09e-29

putative ABC transporter ATP-binding protein YbbA; Provisional

Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 112.56 E-value: 2.09e-29

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099586  18 TVLESLSLNVEHGEIVCLLGASGCGKTTLLKAIAGLLPLSSGIMSLNGMTIddgkHWLAPEQR------NIGMIFQDYAL 91
Cdd:PRK10584  24 SILTGVELVVKRGETIALIGESGSGKSTLLAILAGLDDGSSGEVSLVGQPL----HQMDEEARaklrakHVGFVFQSFML 99

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099586  92 FPHLTVAENIAFG--LRQMAAEERHLQVQQMLELVHLSGFGDRYPHQLSGGQQQRVAIARSLAYKPDLLLLDEPFSNIDT 169
Cdd:PRK10584 100 IPTLNALENVELPalLRGESSRQSRNGAKALLEQLGLGKRLDHLPAQLSGGEQQRVALARAFNGRPDVLFADEPTGNLDR 179

                        170       180       190
                 ....*....|....*....|....*....|.
gi 521099586 170 QVRHDLIGEIRKIFKKQGVTAIFVTHSREEA 200
Cdd:PRK10584 180 QTGDKIADLLFSLNREHGTTLILVTHDLQLA 210

PRK15134

microcin C ABC transporter ATP-binding protein YejF; Provisional

15-237

2.48e-29

microcin C ABC transporter ATP-binding protein YejF; Provisional

Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 117.88 E-value: 2.48e-29

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099586  15 DTQTVLESLSLNVEHGEIVCLLGASGCGKTTLLKAIAGLLPlSSGIMSLNGMTIDD-GKHWLAPEQRNIGMIFQD--YAL 91
Cdd:PRK15134 297 DHNVVVKNISFTLRPGETLGLVGESGSGKSTTGLALLRLIN-SQGEIWFDGQPLHNlNRRQLLPVRHRIQVVFQDpnSSL 375

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099586  92 FPHLTVAENIAFGLR----QMAAEERHLQVQQMLELVHLSGFG-DRYPHQLSGGQQQRVAIARSLAYKPDLLLLDEPFSN 166
Cdd:PRK15134 376 NPRLNVLQIIEEGLRvhqpTLSAAQREQQVIAVMEEVGLDPETrHRYPAEFSGGQRQRIAIARALILKPSLIILDEPTSS 455

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 521099586 167 IDTQVRHDLIGEIRKIFKKQGVTAIFVTHSREEAFAFADKMAVMNHG-VIEQyGTASELYYRPSSKFVADFL 237
Cdd:PRK15134 456 LDKTVQAQILALLKSLQQKHQLAYLFISHDLHVVRALCHQVIVLRQGeVVEQ-GDCERVFAAPQQEYTRQLL 526

cbiO

PRK13636

cobalt transporter ATP-binding subunit; Provisional

5-225

2.73e-29

cobalt transporter ATP-binding subunit; Provisional

Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 113.79 E-value: 2.73e-29

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099586   5 LSIQNLTCQY-DTQTVLESLSLNVEHGEIVCLLGASGCGKTTLLKAIAGLLPLSSGIMSLNGMTIDDGKHWLAPEQRNIG 83
Cdd:PRK13636   6 LKVEELNYNYsDGTHALKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGKPIDYSRKGLMKLRESVG 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099586  84 MIFQ--DYALFPhLTVAENIAFGL--RQMAAEERHLQVQQMLELVHLSGFGDRYPHQLSGGQQQRVAIARSLAYKPDLLL 159
Cdd:PRK13636  86 MVFQdpDNQLFS-ASVYQDVSFGAvnLKLPEDEVRKRVDNALKRTGIEHLKDKPTHCLSFGQKKRVAIAGVLVMEPKVLV 164

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 521099586 160 LDEPFSNIDTQVRHDLIGEIRKIFKKQGVTAIFVTHSREEAFAFADKMAVMNHGVIEQYGTASELY 225
Cdd:PRK13636 165 LDEPTAGLDPMGVSEIMKLLVEMQKELGLTIIIATHDIDIVPLYCDNVFVMKEGRVILQGNPKEVF 230

PhnK

COG1101

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

5-215

2.94e-29

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

Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 113.26 E-value: 2.94e-29

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099586   5 LSIQNLTCQYDTQTVLE-----SLSLNVEHGEIVCLLGASGCGKTTLLKAIAGLLPLSSGIMSLNGMTIDDgkhwLAPEQ 79
Cdd:COG1101    2 LELKNLSKTFNPGTVNEkraldGLNLTIEEGDFVTVIGSNGAGKSTLLNAIAGSLPPDSGSILIDGKDVTK----LPEYK 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099586  80 R--NIGMIFQDYAL--FPHLTVAENIA--------FGLRQ-MAAEERHLqVQQMLELVHLsGFGDRYPHQ---LSGGQQQ 143
Cdd:COG1101   78 RakYIGRVFQDPMMgtAPSMTIEENLAlayrrgkrRGLRRgLTKKRREL-FRELLATLGL-GLENRLDTKvglLSGGQRQ 155

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 521099586 144 RVAIARSLAYKPDLLLLDEPFSNIDTQvRHDLIGEI-RKIFKKQGVTAIFVTHSREEAFAFADKMAVMNHGVI 215
Cdd:COG1101  156 ALSLLMATLTKPKLLLLDEHTAALDPK-TAALVLELtEKIVEENNLTTLMVTHNMEQALDYGNRLIMMHEGRI 227

ABCC_bacteriocin_exporters

cd03245

ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ...

19-215

3.07e-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: 111.91 E-value: 3.07e-29

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099586  19 VLESLSLNVEHGEIVCLLGASGCGKTTLLKAIAGLLPLSSGIMSLNGMTIDDgkhwLAPE--QRNIGMIFQDYALFpHLT 96
Cdd:cd03245   19 ALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGTDIRQ----LDPAdlRRNIGYVPQDVTLF-YGT 93

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099586  97 VAENIAFGlRQMAAEERHLQVqqmLELVHLSGFGDRYPH-----------QLSGGQQQRVAIARSLAYKPDLLLLDEPFS 165
Cdd:cd03245   94 LRDNITLG-APLADDERILRA---AELAGVTDFVNKHPNgldlqigergrGLSGGQRQAVALARALLNDPPILLLDEPTS 169

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|
gi 521099586 166 NIDTQVRHDLIGEIRKIFKkqGVTAIFVTHsREEAFAFADKMAVMNHGVI 215
Cdd:cd03245  170 AMDMNSEERLKERLRQLLG--DKTLIIITH-RPSLLDLVDRIIVMDSGRI 216

MglA

COG1129

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

4-215

4.28e-29

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

Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 116.66 E-value: 4.28e-29

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099586   4 ALSIQNLTCQydtqTVLESLSLNVEHGEIVCLLGASGCGKTTLLKAIAGLLPLSSGIMSLNGMTIDDG------KHWLA- 76
Cdd:COG1129  256 VLEVEGLSVG----GVVRDVSFSVRAGEILGIAGLVGAGRTELARALFGADPADSGEIRLDGKPVRIRsprdaiRAGIAy 331

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099586  77 -PEQRnigmifQDYALFPHLTVAENIA---------FGLRQMAAEERhlQVQQMLELVHLsgfgdRYPH------QLSGG 140
Cdd:COG1129  332 vPEDR------KGEGLVLDLSIRENITlasldrlsrGGLLDRRRERA--LAEEYIKRLRI-----KTPSpeqpvgNLSGG 398

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099586 141 QQQRVAIARSLAYKPDLLLLDEPFSNIDtqVR-----HDLIGEirkiFKKQGVTAIFVTHSREEAFAFADKMAVMNHGVI 215
Cdd:COG1129  399 NQQKVVLAKWLATDPKVLILDEPTRGID--VGakaeiYRLIRE----LAAEGKAVIVISSELPELLGLSDRILVMREGRI 472

cbiO

PRK13645

energy-coupling factor transporter ATPase;

7-225

4.96e-29

energy-coupling factor transporter ATPase;

Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 113.18 E-value: 4.96e-29

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099586   7 IQNLTCQYDTQT-----VLESLSLNVEHGEIVCLLGASGCGKTTLLKAIAGLLPLSSGIMSLNGMTIDDGKHWLAPEQ-- 79
Cdd:PRK13645   9 LDNVSYTYAKKTpfefkALNNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGLIISETGQTIVGDYAIPANLKKIKEVKrl 88

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099586  80 -RNIGMIFQ--DYALFPHlTVAENIAFGLRQMAA--EERHLQVQQMLELVHL-SGFGDRYPHQLSGGQQQRVAIARSLAY 153
Cdd:PRK13645  89 rKEIGLVFQfpEYQLFQE-TIEKDIAFGPVNLGEnkQEAYKKVPELLKLVQLpEDYVKRSPFELSGGQKRRVALAGIIAM 167

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 521099586 154 KPDLLLLDEPFSNIDTQVRHDLIGEIRKIFKKQGVTAIFVTHSREEAFAFADKMAVMNHGVIEQYGTASELY 225
Cdd:PRK13645 168 DGNTLVLDEPTGGLDPKGEEDFINLFERLNKEYKKRIIMVTHNMDQVLRIADEVIVMHEGKVISIGSPFEIF 239

PRK13539

cytochrome c biogenesis protein CcmA; Provisional

5-196

6.94e-29

cytochrome c biogenesis protein CcmA; Provisional

Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 110.73 E-value: 6.94e-29

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099586   5 LSIQNLTCQYDTQTVLESLSLNVEHGEIVCLLGASGCGKTTLLKAIAGLLPLSSGIMSLNGMTIDDGK-----HWLAPeq 79
Cdd:PRK13539   3 LEGEDLACVRGGRVLFSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDGGDIDDPDvaeacHYLGH-- 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099586  80 RNigmifqdyALFPHLTVAENIAFGLRQMAAEErhLQVQQMLELVHLSGFGDRYPHQLSGGQQQRVAIARSLAYKPDLLL 159
Cdd:PRK13539  81 RN--------AMKPALTVAENLEFWAAFLGGEE--LDIAAALEAVGLAPLAHLPFGYLSAGQKRRVALARLLVSNRPIWI 150

                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 521099586 160 LDEPFSNIDtqvRH--DLIGEIRKIFKKQGVTAIFVTHS 196
Cdd:PRK13539 151 LDEPTAALD---AAavALFAELIRAHLAQGGIVIAATHI 186

cbiO

PRK13638

energy-coupling factor ABC transporter ATP-binding protein;

5-227

1.15e-28

energy-coupling factor ABC transporter ATP-binding protein;

Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 112.02 E-value: 1.15e-28

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099586   5 LSIQNLTCQYDTQTVLESLSLNVEHGEIVCLLGASGCGKTTLLKAIAGLLPLSSGIMSLNGMTIDDGKHWLAPEQRNIGM 84
Cdd:PRK13638   2 LATSDLWFRYQDEPVLKGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLRPQKGAVLWQGKPLDYSKRGLLALRQQVAT 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099586  85 IFQD--YALFpHLTVAENIAFGLRQMAAEERHL--QVQQMLELVHLSGFGDRYPHQLSGGQQQRVAIARSLAYKPDLLLL 160
Cdd:PRK13638  82 VFQDpeQQIF-YTDIDSDIAFSLRNLGVPEAEItrRVDEALTLVDAQHFRHQPIQCLSHGQKKRVAIAGALVLQARYLLL 160

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 521099586 161 DEPFSNIDTQVRHDLIGEIRKIFkKQGVTAIFVTHSREEAFAFADKMAVMNHGVIEQYGTASELYYR 227
Cdd:PRK13638 161 DEPTAGLDPAGRTQMIAIIRRIV-AQGNHVIISSHDIDLIYEISDAVYVLRQGQILTHGAPGEVFAC 226

met_CoM_red_A2

TIGR03269

methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ...

20-224

1.59e-28

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: 115.67 E-value: 1.59e-28

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099586   20 LESLSLNVEHGEIVCLLGASGCGKTTLLKAIAGLLPLSSGIMSLN------GMTiDDGKHWLAPEQRNIGMIFQDYALFP 93
Cdd:TIGR03269 300 VDNVSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGEVNVRvgdewvDMT-KPGPDGRGRAKRYIGILHQEYDLYP 378

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099586   94 HLTVAENI--AFGLrQMAAEerhLQVQQMLELVHLSGFG--------DRYPHQLSGGQQQRVAIARSLAYKPDLLLLDEP 163
Cdd:TIGR03269 379 HRTVLDNLteAIGL-ELPDE---LARMKAVITLKMVGFDeekaeeilDKYPDELSEGERHRVALAQVLIKEPRIVILDEP 454

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 521099586  164 FSNIDTQVRHDLIGEIRKIFKKQGVTAIFVTHSREEAFAFADKMAVMNHGVIEQYGTASEL 224
Cdd:TIGR03269 455 TGTMDPITKVDVTHSILKAREEMEQTFIIVSHDMDFVLDVCDRAALMRDGKIVKIGDPEEI 515

Uup

COG0488

ATPase components of ABC transporters with duplicated ATPase domains [General function ...

7-218

2.10e-28

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

Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 115.16 E-value: 2.10e-28

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099586   7 IQNLTCQYDTQTVLESLSLNVEHGEIVCLLGASGCGKTTLLKAIAGLLplssgimslngmTIDDGKHWLAPEQRnIGMIF 86
Cdd:COG0488    1 LENLSKSFGGRPLLDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGEL------------EPDSGEVSIPKGLR-IGYLP 67

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099586  87 QDYALFPHLTVAENIAFG---LRQMAAE---------------ERHLQVQQMLELVH-----------LSGFG------D 131
Cdd:COG0488   68 QEPPLDDDLTVLDTVLDGdaeLRALEAEleeleaklaepdedlERLAELQEEFEALGgweaearaeeiLSGLGfpeedlD 147

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099586 132 RYPHQLSGGQQQRVAIARSLAYKPDLLLLDEPFSNIDTQVRHDLIGEIRKiFKKqgvTAIFVTHSREeaF--AFADKMAV 209
Cdd:COG0488  148 RPVSELSGGWRRRVALARALLSEPDLLLLDEPTNHLDLESIEWLEEFLKN-YPG---TVLVVSHDRY--FldRVATRILE 221


                 ....*....
gi 521099586 210 MNHGVIEQY 218
Cdd:COG0488  222 LDRGKLTLY 230

ABC_CcmA_heme_exporter

cd03231

Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ...

5-195

2.36e-28

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: 109.12 E-value: 2.36e-28

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099586   5 LSIQNLTCQYDTQTVLESLSLNVEHGEIVCLLGASGCGKTTLLKAIAGLLPLSSGIMSLNGMTIDDGKHWLApeqRNIGM 84
Cdd:cd03231    1 LEADELTCERDGRALFSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNGGPLDFQRDSIA---RGLLY 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099586  85 IFQDYALFPHLTVAENIAFgLRQMAAEErhlQVQQMLELVHLSGFGDRYPHQLSGGQQQRVAIARSLAYKPDLLLLDEPF 164
Cdd:cd03231   78 LGHAPGIKTTLSVLENLRF-WHADHSDE---QVEEALARVGLNGFEDRPVAQLSAGQQRRVALARLLLSGRPLWILDEPT 153

                        170       180       190
                 ....*....|....*....|....*....|.
gi 521099586 165 SNIDTQVRHDLIGEIRKiFKKQGVTAIFVTH 195
Cdd:cd03231  154 TALDKAGVARFAEAMAG-HCARGGMVVLTTH 183

cbiO

PRK13646

energy-coupling factor transporter ATPase;

20-225

2.95e-28

energy-coupling factor transporter ATPase;

Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 111.02 E-value: 2.95e-28

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099586  20 LESLSLNVEHGEIVCLLGASGCGKTTLLKAIAGLLPLSSGIMSLNGMTI---DDGKHwLAPEQRNIGMIFQ--DYALFPH 94
Cdd:PRK13646  23 IHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVDDITIthkTKDKY-IRPVRKRIGMVFQfpESQLFED 101

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099586  95 lTVAENIAFGLR--QMAAEE-RHLQVQQMLELVHLSGFGDRYPHQLSGGQQQRVAIARSLAYKPDLLLLDEPFSNIDTQV 171
Cdd:PRK13646 102 -TVEREIIFGPKnfKMNLDEvKNYAHRLLMDLGFSRDVMSQSPFQMSGGQMRKIAIVSILAMNPDIIVLDEPTAGLDPQS 180

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 521099586 172 RHDLIGEIRKIFKKQGVTAIFVTHSREEAFAFADKMAVMNHGVIEQYGTASELY 225
Cdd:PRK13646 181 KRQVMRLLKSLQTDENKTIILVSHDMNEVARYADEVIVMKEGSIVSQTSPKELF 234

ABCC_MRP_domain1

cd03250

ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ...

5-213

4.62e-28

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: 108.33 E-value: 4.62e-28

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099586   5 LSIQNLTCQYD-----TQTVLESLSLNVEHGEIVCLLGASGCGKTTLLKAIAGLLPLSSGIMSLNGMTiddgkhWLAPEQ 79
Cdd:cd03250    1 ISVEDASFTWDsgeqeTSFTLKDINLEVPKGELVAIVGPVGSGKSSLLSALLGELEKLSGSVSVPGSI------AYVSQE 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099586  80 rnigmifqdyALFPHLTVAENIAFGLRqmAAEERHLQV------QQMLELVHlsgFGDryphQ---------LSGGQQQR 144
Cdd:cd03250   75 ----------PWIQNGTIRENILFGKP--FDEERYEKVikacalEPDLEILP---DGD----LteigekginLSGGQKQR 135

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099586 145 VAIARSLAYKPDLLLLDEPFSNIDTQVRHDLIGE-IRKIFKKqGVTAIFVTHsREEAFAFADKMAVMNHG 213
Cdd:cd03250  136 ISLARAVYSDADIYLLDDPLSAVDAHVGRHIFENcILGLLLN-NKTRILVTH-QLQLLPHADQIVVLDNG 203

PRK10908

cell division ATP-binding protein FtsE;

20-195

6.52e-28

cell division ATP-binding protein FtsE;

Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 108.42 E-value: 6.52e-28

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099586  20 LESLSLNVEHGEIVCLLGASGCGKTTLLKAIAGLLPLSSGIMSLNGMTIDDGKHWLAP-EQRNIGMIFQDYALFPHLTVA 98
Cdd:PRK10908  18 LQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDITRLKNREVPfLRRQIGMIFQDHHLLMDRTVY 97

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099586  99 ENIAFGLRQMAA--EERHLQVQQMLELVHLSGFGDRYPHQLSGGQQQRVAIARSLAYKPDLLLLDEPFSNIDTQVRHDLI 176
Cdd:PRK10908  98 DNVAIPLIIAGAsgDDIRRRVSAALDKVGLLDKAKNFPIQLSGGEQQRVGIARAVVNKPAVLLADEPTGNLDDALSEGIL 177

                        170
                 ....*....|....*....
gi 521099586 177 gEIRKIFKKQGVTAIFVTH 195
Cdd:PRK10908 178 -RLFEEFNRVGVTVLMATH 195

PRK09984

phosphonate ABC transporter ATP-binding protein;

1-213

1.05e-27

phosphonate ABC transporter ATP-binding protein;

Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 108.95 E-value: 1.05e-27

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099586   1 MSCALSIQNLTCQYDTQTVLESLSLNVEHGEIVCLLGASGCGKTTLLKAIAGLLPLSSGIMS---LNGMTID-DGKhwLA 76
Cdd:PRK09984   1 MQTIIRVEKLAKTFNQHQALHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGLITGDKSAGShieLLGRTVQrEGR--LA 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099586  77 PEQR----NIGMIFQDYALFPHLTVAENIAFG-----------LRQMAAEERHlQVQQMLELVHLSGFGDRYPHQLSGGQ 141
Cdd:PRK09984  79 RDIRksraNTGYIFQQFNLVNRLSVLENVLIGalgstpfwrtcFSWFTREQKQ-RALQALTRVGMVHFAHQRVSTLSGGQ 157

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 521099586 142 QQRVAIARSLAYKPDLLLLDEPFSNIDTQVRHDLIGEIRKIFKKQGVTAIFVTHSREEAFAFADKMAVMNHG 213
Cdd:PRK09984 158 QQRVAIARALMQQAKVILADEPIASLDPESARIVMDTLRDINQNDGITVVVTLHQVDYALRYCERIVALRQG 229

PRK13549

xylose transporter ATP-binding subunit; Provisional

1-213

1.47e-27

xylose transporter ATP-binding subunit; Provisional

Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 112.71 E-value: 1.47e-27

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099586   1 MSCALSIQNLTCQYDTQTVLESLSLNVEHGEIVCLLGASGCGKTTLLKAIAGLLPlsSGimSLNGMTIDDGKHWLA---- 76
Cdd:PRK13549   2 MEYLLEMKNITKTFGGVKALDNVSLKVRAGEIVSLCGENGAGKSTLMKVLSGVYP--HG--TYEGEIIFEGEELQAsnir 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099586  77 -PEQRNIGMIFQDYALFPHLTVAENI-------AFGLrqMAAEERHLQVQQMLELVHLsgfgDRYPH----QLSGGQQQR 144
Cdd:PRK13549  78 dTERAGIAIIHQELALVKELSVLENIflgneitPGGI--MDYDAMYLRAQKLLAQLKL----DINPAtpvgNLGLGQQQL 151

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 521099586 145 VAIARSLAYKPDLLLLDEPFSNI---DTQVRHDLIgeirKIFKKQGVTAIFVTHSREEAFAFADKMAVMNHG 213
Cdd:PRK13549 152 VEIAKALNKQARLLILDEPTASLtesETAVLLDII----RDLKAHGIACIYISHKLNEVKAISDTICVIRDG 219

MsbA_lipidA

TIGR02203

lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ...

5-224

2.41e-27

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: 112.50 E-value: 2.41e-27

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099586    5 LSIQNLTCQY--DTQTVLESLSLNVEHGEIVCLLGASGCGKTTLLKAIAGLLPLSSGIMSLNGMTIDDGKhwLAPEQRNI 82
Cdd:TIGR02203 331 VEFRNVTFRYpgRDRPALDSISLVIEPGETVALVGRSGSGKSTLVNLIPRFYEPDSGQILLDGHDLADYT--LASLRRQV 408

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099586   83 GMIFQDYALFPHlTVAENIAFGLRQMAAEERhlqVQQMLELVHLSGFGDRYP---HQ--------LSGGQQQRVAIARSL 151
Cdd:TIGR02203 409 ALVSQDVVLFND-TIANNIAYGRTEQADRAE---IERALAAAYAQDFVDKLPlglDTpigengvlLSGGQRQRLAIARAL 484

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 521099586  152 AYKPDLLLLDEPFSNIDTQVRHDLIGEIRKIFkkQGVTAIFVTHsREEAFAFADKMAVMNHGVIEQYGTASEL 224
Cdd:TIGR02203 485 LKDAPILILDEATSALDNESERLVQAALERLM--QGRTTLVIAH-RLSTIEKADRIVVMDDGRIVERGTHNEL 554

PRK10535

macrolide ABC transporter ATP-binding protein/permease MacB;

1-195

2.78e-27

macrolide ABC transporter ATP-binding protein/permease MacB;

Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 112.51 E-value: 2.78e-27

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099586   1 MSCALSIQNLTCQY----DTQTVLESLSLNVEHGEIVCLLGASGCGKTTLLKAIAGLLPLSSGIMSLNGMTIDD-GKHWL 75
Cdd:PRK10535   1 MTALLELKDIRRSYpsgeEQVEVLKGISLDIYAGEMVAIVGASGSGKSTLMNILGCLDKPTSGTYRVAGQDVATlDADAL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099586  76 APEQR-NIGMIFQDYALFPHLTVAENIAFGlRQMAAEERHLQVQQMLELVHLSGFGDR---YPHQLSGGQQQRVAIARSL 151
Cdd:PRK10535  81 AQLRReHFGFIFQRYHLLSHLTAAQNVEVP-AVYAGLERKQRLLRAQELLQRLGLEDRveyQPSQLSGGQQQRVSIARAL 159

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....
gi 521099586 152 AYKPDLLLLDEPFSNIDTQVRHDLIGeIRKIFKKQGVTAIFVTH 195
Cdd:PRK10535 160 MNGGQVILADEPTGALDSHSGEEVMA-ILHQLRDRGHTVIIVTH 202

PRK13538

cytochrome c biogenesis heme-transporting ATPase CcmA;

5-195

3.03e-27

cytochrome c biogenesis heme-transporting ATPase CcmA;

Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 106.04 E-value: 3.03e-27

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099586   5 LSIQNLTCQYDTQTVLESLSLNVEHGEIVCLLGASGCGKTTLLKAIAGLLPLSSGIMSLNGMTIDdgkhwlapEQRNigm 84
Cdd:PRK13538   2 LEARNLACERDERILFSGLSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVLWQGEPIR--------RQRD--- 70

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099586  85 IFQDYALF--------PHLTVAENIAF--GLRQMAAEERHLQVqqmLELVHLSGFGDRYPHQLSGGQQQRVAIARSLAYK 154
Cdd:PRK13538  71 EYHQDLLYlghqpgikTELTALENLRFyqRLHGPGDDEALWEA---LAQVGLAGFEDVPVRQLSAGQQRRVALARLWLTR 147

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 521099586 155 PDLLLLDEPFSNIDTQVRHDLIGEIRKiFKKQGVTAIFVTH 195
Cdd:PRK13538 148 APLWILDEPFTAIDKQGVARLEALLAQ-HAEQGGMVILTTH 187

dppF

PRK11308

dipeptide transporter ATP-binding subunit; Provisional

20-228

3.78e-27

dipeptide transporter ATP-binding subunit; Provisional

Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 108.90 E-value: 3.78e-27

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099586  20 LESLSLNVEHGEIVCLLGASGCGKTTLLKAIAGLLPLSSGIMSLNGM-TIDDGKHWLAPEQRNIGMIFQD-YA-LFPHLT 96
Cdd:PRK11308  31 LDGVSFTLERGKTLAVVGESGCGKSTLARLLTMIETPTGGELYYQGQdLLKADPEAQKLLRQKIQIVFQNpYGsLNPRKK 110

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099586  97 VAENIAFGLR---QMAAEERHLQVQQMLELVHL-SGFGDRYPHQLSGGQQQRVAIARSLAYKPDLLLLDEPFSNIDTQVR 172
Cdd:PRK11308 111 VGQILEEPLLintSLSAAERREKALAMMAKVGLrPEHYDRYPHMFSGGQRQRIAIARALMLDPDVVVADEPVSALDVSVQ 190

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 521099586 173 HDLIGEIRKIFKKQGVTAIFVTHSREEAFAFADKMAVMNHG-VIEQyGTASELYYRP 228
Cdd:PRK11308 191 AQVLNLMMDLQQELGLSYVFISHDLSVVEHIADEVMVMYLGrCVEK-GTKEQIFNNP 246

cbiO

PRK13643

energy-coupling factor transporter ATPase;

20-225

5.68e-27

energy-coupling factor transporter ATPase;

Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 107.90 E-value: 5.68e-27

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099586  20 LESLSLNVEHGEIVCLLGASGCGKTTLLKAIAGLLPLSSGIMSLNGMTIDD--GKHWLAPEQRNIGMIFQ--DYALFPHl 95
Cdd:PRK13643  22 LFDIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVTVGDIVVSStsKQKEIKPVRKKVGVVFQfpESQLFEE- 100

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099586  96 TVAENIAFGLRQ--MAAEERHLQVQQMLELVHLSG-FGDRYPHQLSGGQQQRVAIARSLAYKPDLLLLDEPFSNIDTQVR 172
Cdd:PRK13643 101 TVLKDVAFGPQNfgIPKEKAEKIAAEKLEMVGLADeFWEKSPFELSGGQMRRVAIAGILAMEPEVLVLDEPTAGLDPKAR 180

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 521099586 173 HDLIGEIRKIfKKQGVTAIFVTHSREEAFAFADKMAVMNHGVIEQYGTASELY 225
Cdd:PRK13643 181 IEMMQLFESI-HQSGQTVVLVTHLMDDVADYADYVYLLEKGHIISCGTPSDVF 232

PRK11174

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

5-224

8.52e-27

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

Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 110.70 E-value: 8.52e-27

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099586   5 LSIQNLT-CQYDTQTVLESLSLNVEHGEIVCLLGASGCGKTTLLKAIAGLLPLSsGIMSLNGMTIDDgkhwLAPEQ--RN 81
Cdd:PRK11174 350 IEAEDLEiLSPDGKTLAGPLNFTLPAGQRIALVGPSGAGKTSLLNALLGFLPYQ-GSLKINGIELRE----LDPESwrKH 424

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099586  82 IGMIFQDYALFpHLTVAENIAFGlRQMAAEErhlQVQQMLELVHLSGFGDRYPH-----------QLSGGQQQRVAIARS 150
Cdd:PRK11174 425 LSWVGQNPQLP-HGTLRDNVLLG-NPDASDE---QLQQALENAWVSEFLPLLPQgldtpigdqaaGLSVGQAQRLALARA 499

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 521099586 151 LAYKPDLLLLDEPFSNIDTQVRHDLIGEIRKIFKKQgvTAIFVTHsREEAFAFADKMAVMNHGVIEQYGTASEL 224
Cdd:PRK11174 500 LLQPCQLLLLDEPTASLDAHSEQLVMQALNAASRRQ--TTLMVTH-QLEDLAQWDQIWVMQDGQIVQQGDYAEL 570

cbiO

PRK13649

energy-coupling factor transporter ATPase;

4-225

1.49e-26

energy-coupling factor transporter ATPase;

Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 106.37 E-value: 1.49e-26

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099586   4 ALSIQNLTCQYDTQTVLES-----LSLNVEHGEIVCLLGASGCGKTTLLKAIAGLLPLSSGIMSLNGMTI--DDGKHWLA 76
Cdd:PRK13649   2 GINLQNVSYTYQAGTPFEGralfdVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDDTLItsTSKNKDIK 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099586  77 PEQRNIGMIFQ--DYALFPHlTVAENIAFGLRQ--MAAEERHLQVQQMLELVHLS-GFGDRYPHQLSGGQQQRVAIARSL 151
Cdd:PRK13649  82 QIRKKVGLVFQfpESQLFEE-TVLKDVAFGPQNfgVSQEEAEALAREKLALVGISeSLFEKNPFELSGGQMRRVAIAGIL 160

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 521099586 152 AYKPDLLLLDEPFSNIDTQVRHDLIgeirKIFKK---QGVTAIFVTHSREEAFAFADKMAVMNHGVIEQYGTASELY 225
Cdd:PRK13649 161 AMEPKILVLDEPTAGLDPKGRKELM----TLFKKlhqSGMTIVLVTHLMDDVANYADFVYVLEKGKLVLSGKPKDIF 233

PRK15439

autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional

1-224

1.59e-26

autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional

Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 109.76 E-value: 1.59e-26

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099586   1 MSCALSIQNLTCQYDTQTVLESLSLNVEHGEIVCLLGASGCGKTTLLKAIAGLLPLSSGIMSLNGMTIddgkHWLAP--- 77
Cdd:PRK15439   8 APPLLCARSISKQYSGVEVLKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIGGNPC----ARLTPaka 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099586  78 EQRNIGMIFQDYALFPHLTVAENIAFGL-RQMAAEERHLQVQQMLElVHLSgfgdryPHQLSG----GQQQRVAIARSLA 152
Cdd:PRK15439  84 HQLGIYLVPQEPLLFPNLSVKENILFGLpKRQASMQKMKQLLAALG-CQLD------LDSSAGslevADRQIVEILRGLM 156

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 521099586 153 YKPDLLLLDEPFSNIDTQVRHDLIGEIRKIfKKQGVTAIFVTHSREEAFAFADKMAVMNHGVIEQYGTASEL 224
Cdd:PRK15439 157 RDSRILILDEPTASLTPAETERLFSRIREL-LAQGVGIVFISHKLPEIRQLADRISVMRDGTIALSGKTADL 227

PRK10261

glutathione transporter ATP-binding protein; Provisional

20-228

1.60e-26

glutathione transporter ATP-binding protein; Provisional

Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 110.33 E-value: 1.60e-26

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099586  20 LESLSLNVEHGEIVCLLGASGCGKTTLLKAIAGLLPLSSGIMSLNGMTID---DGKhwLAPEQRNIGMIFQD-YA-LFPH 94
Cdd:PRK10261 340 VEKVSFDLWPGETLSLVGESGSGKSTTGRALLRLVESQGGEIIFNGQRIDtlsPGK--LQALRRDIQFIFQDpYAsLDPR 417

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099586  95 LTVAENIAFGLR---QMAAEERHLQVQQMLELVHL-SGFGDRYPHQLSGGQQQRVAIARSLAYKPDLLLLDEPFSNIDTQ 170
Cdd:PRK10261 418 QTVGDSIMEPLRvhgLLPGKAAAARVAWLLERVGLlPEHAWRYPHEFSGGQRQRICIARALALNPKVIIADEAVSALDVS 497

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 521099586 171 VRHDLIGEIRKIFKKQGVTAIFVTHSREEAFAFADKMAVMNHGVIEQYGTASELYYRP 228
Cdd:PRK10261 498 IRGQIINLLLDLQRDFGIAYLFISHDMAVVERISHRVAVMYLGQIVEIGPRRAVFENP 555

PRK14243

phosphate transporter ATP-binding protein; Provisional

5-239

2.92e-26

phosphate transporter ATP-binding protein; Provisional

Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 105.25 E-value: 2.92e-26

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099586   5 LSIQNLTCQYDTQTVLESLSLNVEHGEIVCLLGASGCGKTTLLKAIAGLLPLSSGiMSLNGMTIDDGKHWLAPE------ 78
Cdd:PRK14243  11 LRTENLNVYYGSFLAVKNVWLDIPKNQITAFIGPSGCGKSTILRCFNRLNDLIPG-FRVEGKVTFHGKNLYAPDvdpvev 89

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099586  79 QRNIGMIFQDYALFPHlTVAENIAFGLRQMAAE-------ERHL-------QVQQMLELVHLSgfgdryphqLSGGQQQR 144
Cdd:PRK14243  90 RRRIGMVFQKPNPFPK-SIYDNIAYGARINGYKgdmdelvERSLrqaalwdEVKDKLKQSGLS---------LSGGQQQR 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099586 145 VAIARSLAYKPDLLLLDEPFSNID---TQVRHDLIGEIrkifkKQGVTAIFVTHSREEAFAFADKMAVMN---------H 212
Cdd:PRK14243 160 LCIARAIAVQPEVILMDEPCSALDpisTLRIEELMHEL-----KEQYTIIIVTHNMQQAARVSDMTAFFNveltegggrY 234

                        250       260
                 ....*....|....*....|....*..
gi 521099586 213 GVIEQYGTASELYYRPSSKFVADFLGG 239
Cdd:PRK14243 235 GYLVEFDRTEKIFNSPQQQATRDYVSG 261

phnK

PRK11701

phosphonate C-P lyase system protein PhnK; Provisional

5-217

3.59e-26

phosphonate C-P lyase system protein PhnK; Provisional

Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 104.62 E-value: 3.59e-26

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099586   5 LSIQNLTCQYDTQTVLESLSLNVEHGEIVCLLGASGCGKTTLLKAIAGLLPLSSGIMSLNGMtiDDGKHWLA----PEQR 80
Cdd:PRK11701   7 LSVRGLTKLYGPRKGCRDVSFDLYPGEVLGIVGESGSGKTTLLNALSARLAPDAGEVHYRMR--DGQLRDLYalseAERR 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099586  81 NI-----GMIFQDYA--LFPHLTVAENIafGLRQMAAEERHL-----QVQQMLELVHL-SGFGDRYPHQLSGGQQQRVAI 147
Cdd:PRK11701  85 RLlrtewGFVHQHPRdgLRMQVSAGGNI--GERLMAVGARHYgdiraTAGDWLERVEIdAARIDDLPTTFSGGMQQRLQI 162

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 521099586 148 ARSLAYKPDLLLLDEPFSNIDTQVRHDLIGEIRKIFKKQGVTAIFVTHSREEAFAFADKMAVMNHG-VIEQ 217
Cdd:PRK11701 163 ARNLVTHPRLVFMDEPTGGLDVSVQARLLDLLRGLVRELGLAVVIVTHDLAVARLLAHRLLVMKQGrVVES 233

PRK13536

nodulation factor ABC transporter ATP-binding protein NodI;

2-214

3.70e-26

nodulation factor ABC transporter ATP-binding protein NodI;

Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 106.45 E-value: 3.70e-26

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099586   2 SCALSIQNLTCQYDTQTVLESLSLNVEHGEIVCLLGASGCGKTTLLKAIAGLLPLSSGIMSLNGMTIDDgKHWLApeQRN 81
Cdd:PRK13536  39 TVAIDLAGVSKSYGDKAVVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKITVLGVPVPA-RARLA--RAR 115

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099586  82 IGMIFQDYALFPHLTVAEN-IAFGLR-QMAAEERHLQVQQMLELVHLSGFGDRYPHQLSGGQQQRVAIARSLAYKPDLLL 159
Cdd:PRK13536 116 IGVVPQFDNLDLEFTVRENlLVFGRYfGMSTREIEAVIPSLLEFARLESKADARVSDLSGGMKRRLTLARALINDPQLLI 195

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 521099586 160 LDEPFSNIDTQVRHdLIGEIRKIFKKQGVTAIFVTHSREEAFAFADKMAVMNHGV 214
Cdd:PRK13536 196 LDEPTTGLDPHARH-LIWERLRSLLARGKTILLTTHFMEEAERLCDRLCVLEAGR 249

YddA

COG4178

ABC-type uncharacterized transport system, permease and ATPase components [General function ...

4-206

5.50e-26

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

Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 108.36 E-value: 5.50e-26

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099586   4 ALSIQNLTCQ-YDTQTVLESLSLNVEHGEIVCLLGASGCGKTTLLKAIAGLLPLSSGimslngmtiddgkHWLAPEQRNI 82
Cdd:COG4178  362 ALALEDLTLRtPDGRPLLEDLSLSLKPGERLLITGPSGSGKSTLLRAIAGLWPYGSG-------------RIARPAGARV 428

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099586  83 GMIFQD-YalFPHLTVAENIAFGlrqmAAEERH--LQVQQMLELVHLSGFGDRY------PHQLSGGQQQRVAIARSLAY 153
Cdd:COG4178  429 LFLPQRpY--LPLGTLREALLYP----ATAEAFsdAELREALEAVGLGHLAERLdeeadwDQVLSLGEQQRLAFARLLLH 502

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 521099586 154 KPDLLLLDEPFSNIDTQVRHDLIGEIRKIFKkqGVTAIFVTHsREEAFAFADK 206
Cdd:COG4178  503 KPDWLFLDEATSALDEENEAALYQLLREELP--GTTVISVGH-RSTLAAFHDR 552

PRK15112

peptide ABC transporter ATP-binding protein SapF;

5-224

5.53e-26

peptide ABC transporter ATP-binding protein SapF;

Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 104.49 E-value: 5.53e-26

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099586   5 LSIQNL--TCQYDT-----QTV--LESLSLNVEHGEIVCLLGASGCGKTTLLKAIAGLLPLSSGIMSLNGMTIDDGKHwl 75
Cdd:PRK15112   5 LEVRNLskTFRYRTgwfrrQTVeaVKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDHPLHFGDY-- 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099586  76 APEQRNIGMIFQD--YALFPHLTVAENIAFGLR---QMAAEERHLQVQQMLELVHL-SGFGDRYPHQLSGGQQQRVAIAR 149
Cdd:PRK15112  83 SYRSQRIRMIFQDpsTSLNPRQRISQILDFPLRlntDLEPEQREKQIIETLRQVGLlPDHASYYPHMLAPGQKQRLGLAR 162

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 521099586 150 SLAYKPDLLLLDEPFSNIDTQVRHDLIGEIRKIFKKQGVTAIFVTHSREEAFAFADKMAVMNHG-VIEQYGTASEL 224
Cdd:PRK15112 163 ALILRPKVIIADEALASLDMSMRSQLINLMLELQEKQGISYIYVTQHLGMMKHISDQVLVMHQGeVVERGSTADVL 238

TagH

COG1134

ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ...

1-223

6.03e-26

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

Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 103.62 E-value: 6.03e-26

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099586   1 MSCALSIQNLTCQY----------------------DTQTVLESLSLNVEHGEIVCLLGASGCGKTTLLKAIAGLLPLSS 58
Cdd:COG1134    1 MSSMIEVENVSKSYrlyhepsrslkelllrrrrtrrEEFWALKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTS 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099586  59 GIMSLNGmTIddgkHWLApeqrNIGMIFQdyalfPHLTVAENIAFGLRQMAAEERhlQVQQML-ELVHLSGFGD------ 131
Cdd:COG1134   81 GRVEVNG-RV----SALL----ELGAGFH-----PELTGRENIYLNGRLLGLSRK--EIDEKFdEIVEFAELGDfidqpv 144

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099586 132 -RYphqlSGGQQQRVAIARSLAYKPDLLLLDEPFSNIDTQVRHDLIGEIRKiFKKQGVTAIFVTHSREEAFAFADKMAVM 210
Cdd:COG1134  145 kTY----SSGMRARLAFAVATAVDPDILLVDEVLAVGDAAFQKKCLARIRE-LRESGRTVIFVSHSMGAVRRLCDRAIWL 219

                        250
                 ....*....|...
gi 521099586 211 NHGVIEQYGTASE 223
Cdd:COG1134  220 EKGRLVMDGDPEE 232

lolD

PRK11629

lipoprotein-releasing ABC transporter ATP-binding protein LolD;

19-195

8.31e-26

lipoprotein-releasing ABC transporter ATP-binding protein LolD;

Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 102.97 E-value: 8.31e-26

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099586  19 VLESLSLNVEHGEIVCLLGASGCGKTTLLKAIAGLLPLSSGIMSLNGMTIDDGKHWLAPEQRN--IGMIFQDYALFPHLT 96
Cdd:PRK11629  24 VLHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPMSKLSSAAKAELRNqkLGFIYQFHHLLPDFT 103

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099586  97 VAENIAFGLR--QMAAEERHLQVQQMLELVHLSGFGDRYPHQLSGGQQQRVAIARSLAYKPDLLLLDEPFSNIDTQVRH- 173
Cdd:PRK11629 104 ALENVAMPLLigKKKPAEINSRALEMLAAVGLEHRANHRPSELSGGERQRVAIARALVNNPRLVLADEPTGNLDARNADs 183

                        170       180
                 ....*....|....*....|....
gi 521099586 174 --DLIGEIRkifKKQGVTAIFVTH 195
Cdd:PRK11629 184 ifQLLGELN---RLQGTAFLVVTH 204

PRK10247

putative ABC transporter ATP-binding protein YbbL; Provisional

5-206

1.36e-25

putative ABC transporter ATP-binding protein YbbL; Provisional

Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 102.48 E-value: 1.36e-25

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099586   5 LSIQNLTCQYDTQTVLESLSLNVEHGEIVCLLGASGCGKTTLLKAIAGLLPLSSGIMSLNGMTIDDgkhwLAPEQ--RNI 82
Cdd:PRK10247   8 LQLQNVGYLAGDAKILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFEGEDIST----LKPEIyrQQV 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099586  83 GMIFQDYALFPHlTVAENIAF--GLRQMAAEERHLQVQqmlelvhLSGFG------DRYPHQLSGGQQQRVAIARSLAYK 154
Cdd:PRK10247  84 SYCAQTPTLFGD-TVYDNLIFpwQIRNQQPDPAIFLDD-------LERFAlpdtilTKNIAELSGGEKQRISLIRNLQFM 155

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 521099586 155 PDLLLLDEPFSNIDTQVRHDLIGEIRKIFKKQGVTAIFVTHSREEaFAFADK 206
Cdd:PRK10247 156 PKVLLLDEITSALDESNKHNVNEIIHRYVREQNIAVLWVTHDKDE-INHADK 206

oppD

PRK09473

oligopeptide transporter ATP-binding component; Provisional

5-229

1.37e-25

oligopeptide transporter ATP-binding component; Provisional

Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 104.81 E-value: 1.37e-25

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099586   5 LSIQNLTCQYDTQ----TVLESLSLNVEHGEIVCLLGASGCGKTTLLKAIAGLLPlSSGIMSlnGMTIDDGKHWLA-PEQ 79
Cdd:PRK09473  13 LDVKDLRVTFSTPdgdvTAVNDLNFSLRAGETLGIVGESGSGKSQTAFALMGLLA-ANGRIG--GSATFNGREILNlPEK 89

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099586  80 R-------NIGMIFQD--YALFPHLTVAENIAFGL---RQMAAEERHLQVQQMLELVHLSGFGDR---YPHQLSGGQQQR 144
Cdd:PRK09473  90 ElnklraeQISMIFQDpmTSLNPYMRVGEQLMEVLmlhKGMSKAEAFEESVRMLDAVKMPEARKRmkmYPHEFSGGMRQR 169

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099586 145 VAIARSLAYKPDLLLLDEPFSNIDTQVRHD---LIGEIRKIFKkqgvTA-IFVTHSREEAFAFADKMAVMNHGVIEQYGT 220
Cdd:PRK09473 170 VMIAMALLCRPKLLIADEPTTALDVTVQAQimtLLNELKREFN----TAiIMITHDLGVVAGICDKVLVMYAGRTMEYGN 245


                 ....*....
gi 521099586 221 ASELYYRPS 229
Cdd:PRK09473 246 ARDVFYQPS 254

PRK13651

cobalt transporter ATP-binding subunit; Provisional

7-215

1.50e-25

cobalt transporter ATP-binding subunit; Provisional

Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 104.01 E-value: 1.50e-25

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099586   7 IQNLTCQYDTQT-----VLESLSLNVEHGEIVCLLGASGCGKTTLLKAIAGLLPLSSGIMSLNGMTIDDGKHWLAPE--- 78
Cdd:PRK13651   5 VKNIVKIFNKKLptelkALDNVSVEINQGEFIAIIGQTGSGKTTFIEHLNALLLPDTGTIEWIFKDEKNKKKTKEKEkvl 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099586  79 -------------------QRNIGMIFQ--DYALFPHlTVAENIAFGLRQMAA--EERHLQVQQMLELVHLS-GFGDRYP 134
Cdd:PRK13651  85 eklviqktrfkkikkikeiRRRVGVVFQfaEYQLFEQ-TIEKDIIFGPVSMGVskEEAKKRAAKYIELVGLDeSYLQRSP 163

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099586 135 HQLSGGQQQRVAIARSLAYKPDLLLLDEPFSNIDTQVrhdlIGEIRKIFK---KQGVTAIFVTHSREEAFAFADKMAVMN 211
Cdd:PRK13651 164 FELSGGQKRRVALAGILAMEPDFLVFDEPTAGLDPQG----VKEILEIFDnlnKQGKTIILVTHDLDNVLEWTKRTIFFK 239


                 ....
gi 521099586 212 HGVI 215
Cdd:PRK13651 240 DGKI 243

PRK10261

glutathione transporter ATP-binding protein; Provisional

5-267

1.81e-25

glutathione transporter ATP-binding protein; Provisional

Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 107.25 E-value: 1.81e-25

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099586   5 LSIQNLTC--QYDTQTV--LESLSLNVEHGEIVCLLGASGCGKTTLLKAIAGLLPLSSGIMSLNGM--------TIDDGK 72
Cdd:PRK10261  13 LAVENLNIafMQEQQKIaaVRNLSFSLQRGETLAIVGESGSGKSVTALALMRLLEQAGGLVQCDKMllrrrsrqVIELSE 92

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099586  73 HWLAPEQR----NIGMIFQD--YALFPHLTVAENIAFGLR---QMAAEERHLQVQQMLELVHL---SGFGDRYPHQLSGG 140
Cdd:PRK10261  93 QSAAQMRHvrgaDMAMIFQEpmTSLNPVFTVGEQIAESIRlhqGASREEAMVEAKRMLDQVRIpeaQTILSRYPHQLSGG 172

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099586 141 QQQRVAIARSLAYKPDLLLLDEPFSNIDTQVRHDLIGEIRKIFKKQGVTAIFVTHSREEAFAFADKMAVMNHGVIEQYGT 220
Cdd:PRK10261 173 MRQRVMIAMALSCRPAVLIADEPTTALDVTIQAQILQLIKVLQKEMSMGVIFITHDMGVVAEIADRVLVMYQGEAVETGS 252

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*..
gi 521099586 221 ASELYYRPSSKFVADFLGGGSYLPATRLAEHQYQTPLGVVDAYAQQS 267
Cdd:PRK10261 253 VEQIFHAPQHPYTRALLAAVPQLGAMKGLDYPRRFPLISLEHPAKQE 299

xylG

TIGR02633

D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ...

5-213

2.26e-25

D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose isomerase and xylulokinase enzymes for xylose utilization. Members of this protein family are the ATP-binding cassette (ABC) subunit of the known or predicted high-affinity xylose ABC transporter for xylose import. These genes, which closely resemble other sugar transport ABC transporter genes, typically are encoded near xylose utilization enzymes and regulatory proteins. Note that this form of the transporter contains two copies of the ABC transporter domain (pfam00005). [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]

Pssm-ID: 131681 [Multi-domain] Cd Length: 500 Bit Score: 106.45 E-value: 2.26e-25

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099586    5 LSIQNLTCQYDTQTVLESLSLNVEHGEIVCLLGASGCGKTTLLKAIAGLLPLSsgimSLNGMTIDDGKHWLA-----PEQ 79
Cdd:TIGR02633   2 LEMKGIVKTFGGVKALDGIDLEVRPGECVGLCGENGAGKSTLMKILSGVYPHG----TWDGEIYWSGSPLKAsnirdTER 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099586   80 RNIGMIFQDYALFPHLTVAENIAFGLR------QMAAEERHLQVQQMLELVHLSGFGDRYP-HQLSGGQQQRVAIARSLA 152
Cdd:TIGR02633  78 AGIVIIHQELTLVPELSVAENIFLGNEitlpggRMAYNAMYLRAKNLLRELQLDADNVTRPvGDYGGGQQQLVEIAKALN 157

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 521099586  153 YKPDLLLLDEPFSNIDTQVRHDLIGEIRKIfKKQGVTAIFVTHSREEAFAFADKMAVMNHG 213
Cdd:TIGR02633 158 KQARLLILDEPSSSLTEKETEILLDIIRDL-KAHGVACVYISHKLNEVKAVCDTICVIRDG 217

CydC

TIGR02868

thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ...

5-196

2.48e-25

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: 106.29 E-value: 2.48e-25

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099586    5 LSIQNLTCQYDT-QTVLESLSLNVEHGEIVCLLGASGCGKTTLLKAIAGLLPLSSGIMSLNGMTIDDGKHWLApeQRNIG 83
Cdd:TIGR02868 335 LELRDLSAGYPGaPPVLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPLQGEVTLDGVPVSSLDQDEV--RRRVS 412

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099586   84 MIFQDYALFpHLTVAENIAFGlRQMAAEErhlQVQQMLELVHLSGFGDRYPH-----------QLSGGQQQRVAIARSLA 152
Cdd:TIGR02868 413 VCAQDAHLF-DTTVRENLRLA-RPDATDE---ELWAALERVGLADWLRALPDgldtvlgeggaRLSGGERQRLALARALL 487

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 521099586  153 YKPDLLLLDEPFSNIDTQVRHDLIGEIRKIfkKQGVTAIFVTHS 196
Cdd:TIGR02868 488 ADAPILLLDEPTEHLDAETADELLEDLLAA--LSGRTVVLITHH 529

PRK15134

microcin C ABC transporter ATP-binding protein YejF; Provisional

5-228

3.33e-25

microcin C ABC transporter ATP-binding protein YejF; Provisional

Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 105.94 E-value: 3.33e-25

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099586   5 LSIQNLTC----QYDTQTVLESLSLNVEHGEIVCLLGASGCGKTTLLKAIAGLLPlSSGIMSLNGMTIDDGKHWL-APEQ 79
Cdd:PRK15134   6 LAIENLSVafrqQQTVRTVVNDVSLQIEAGETLALVGESGSGKSVTALSILRLLP-SPPVVYPSGDIRFHGESLLhASEQ 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099586  80 R-------NIGMIFQD--YALFPHLTVAENIAFGL---RQMAAEERHLQVQQMLELVHLSGFGDR---YPHQLSGGQQQR 144
Cdd:PRK15134  85 TlrgvrgnKIAMIFQEpmVSLNPLHTLEKQLYEVLslhRGMRREAARGEILNCLDRVGIRQAAKRltdYPHQLSGGERQR 164

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099586 145 VAIARSLAYKPDLLLLDEPFSNIDTQVRHDLIGEIRKIFKKQGVTAIFVTHSREEAFAFADKMAVMNHGVIEQYGTASEL 224
Cdd:PRK15134 165 VMIAMALLTRPELLIADEPTTALDVSVQAQILQLLRELQQELNMGLLFITHNLSIVRKLADRVAVMQNGRCVEQNRAATL 244


                 ....
gi 521099586 225 YYRP 228
Cdd:PRK15134 245 FSAP 248

CP_lyasePhnK

TIGR02323

phosphonate C-P lyase system protein PhnK; Members of this family are the PhnK protein of C-P ...

5-217

3.75e-25

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: 101.83 E-value: 3.75e-25

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099586    5 LSIQNLTCQYDTQTVLESLSLNVEHGEIVCLLGASGCGKTTLLKAIAGLLPLSSGimSLNGMTIDDGKHWL----APEQR 80
Cdd:TIGR02323   4 LQVSGLSKSYGGGKGCRDVSFDLYPGEVLGIVGESGSGKSTLLGCLAGRLAPDHG--TATYIMRSGAELELyqlsEAERR 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099586   81 NI-----GMIFQDYALFPHLTVAENIAFGLRQMAAEERHL-----QVQQMLELVHLS-GFGDRYPHQLSGGQQQRVAIAR 149
Cdd:TIGR02323  82 RLmrtewGFVHQNPRDGLRMRVSAGANIGERLMAIGARHYgniraTAQDWLEEVEIDpTRIDDLPRAFSGGMQQRLQIAR 161

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 521099586  150 SLAYKPDLLLLDEPFSNIDTQVRHDLIGEIRKIFKKQGVTAIFVTHSREEAFAFADKMAVMNHG-VIEQ 217
Cdd:TIGR02323 162 NLVTRPRLVFMDEPTGGLDVSVQARLLDLLRGLVRDLGLAVIIVTHDLGVARLLAQRLLVMQQGrVVES 230

cbiO

PRK13644

energy-coupling factor transporter ATPase;

5-279

3.76e-25

energy-coupling factor transporter ATPase;

Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 102.37 E-value: 3.76e-25

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099586   5 LSIQNLTCQY-DTQTVLESLSLNVEHGEIVCLLGASGCGKTTLLKAIAGLLPLSSGIMSLNGMtiDDGKHWLAPEQRNI- 82
Cdd:PRK13644   2 IRLENVSYSYpDGTPALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLVSGI--DTGDFSKLQGIRKLv 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099586  83 GMIFQD-YALFPHLTVAENIAFGLRQMAAE--ERHLQVQQMLELVHLSGFGDRYPHQLSGGQQQRVAIARSLAYKPDLLL 159
Cdd:PRK13644  80 GIVFQNpETQFVGRTVEEDLAFGPENLCLPpiEIRKRVDRALAEIGLEKYRHRSPKTLSGGQGQCVALAGILTMEPECLI 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099586 160 LDEPFSNIDTQVRHDLIGEIRKIFKKqGVTAIFVTHSREEAFAfADKMAVMNHGVIEQYGTASELYYRPSSKFVadflgg 239
Cdd:PRK13644 160 FDEVTSMLDPDSGIAVLERIKKLHEK-GKTIVYITHNLEELHD-ADRIIVMDRGKIVLEGEPENVLSDVSLQTL------ 231

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*
gi 521099586 240 GSYLP-----ATRLAEHQYQTPLGvvDAYAQQSIAQgSQCELLLR 279
Cdd:PRK13644 232 GLTPPslielAENLKMHGVVIPWE--NTSSPSSFAE-EICRLFLK 273

3a01208

TIGR00958

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

17-228

7.64e-25

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

Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 105.57 E-value: 7.64e-25

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099586   17 QTVLESLSLNVEHGEIVCLLGASGCGKTTLLKAIAGLLPLSSGIMSLNGMTIDDGKH-WLapeQRNIGMIFQDYALFPHl 95
Cdd:TIGR00958 494 VPVLKGLTFTLHPGEVVALVGPSGSGKSTVAALLQNLYQPTGGQVLLDGVPLVQYDHhYL---HRQVALVGQEPVLFSG- 569

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099586   96 TVAENIAFGLRQMAAEERHLQVQQMLELVHLSGFGDRY-----PH--QLSGGQQQRVAIARSLAYKPDLLLLDEPFSNID 168
Cdd:TIGR00958 570 SVRENIAYGLTDTPDEEIMAAAKAANAHDFIMEFPNGYdtevgEKgsQLSGGQKQRIAIARALVRKPRVLILDEATSALD 649

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099586  169 TQVRHdLIGEIRkifKKQGVTAIFVTHsREEAFAFADKMAVMNHGVIEQYGTASELYYRP 228
Cdd:TIGR00958 650 AECEQ-LLQESR---SRASRTVLLIAH-RLSTVERADQILVLKKGSVVEMGTHKQLMEDQ 704

ABCD_peroxisomal_ALDP

cd03223

ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ...

5-206

9.91e-25

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: 98.38 E-value: 9.91e-25

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099586   5 LSIQNLT-CQYDTQTVLESLSLNVEHGEIVCLLGASGCGKTTLLKAIAGLLPLSSGIMSLngmtiddgkhwlaPEQRNIG 83
Cdd:cd03223    1 IELENLSlATPDGRVLLKDLSFEIKPGDRLLITGPSGTGKSSLFRALAGLWPWGSGRIGM-------------PEGEDLL 67

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099586  84 MIFQDyALFPHLTVAENIAfglrqmaaeerhlqvqqmlelvhlsgfgdrYP--HQLSGGQQQRVAIARSLAYKPDLLLLD 161
Cdd:cd03223   68 FLPQR-PYLPLGTLREQLI------------------------------YPwdDVLSGGEQQRLAFARLLLHKPKFVFLD 116

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*
gi 521099586 162 EPFSNIDTQVRHDLigeiRKIFKKQGVTAIFVTHsREEAFAFADK 206
Cdd:cd03223  117 EATSALDEESEDRL----YQLLKELGITVISVGH-RPSLWKFHDR 156

rim_protein

TIGR01257

retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ...

20-247

1.42e-24

retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim protein) in eukaryotes. It is the member of ABC transporter superfamily. Rim protein is a membrane glycoprotein which is localized in the photoreceptor outer segment discs. Mutation/s in its genetic loci is implicated in the recessive Stargardt's disease. [Transport and binding proteins, Other]

Pssm-ID: 130324 [Multi-domain] Cd Length: 2272 Bit Score: 105.10 E-value: 1.42e-24

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099586    20 LESLSLNVEHGEIVCLLGASGCGKTTLLKAIAGLLPLSSGIMSLNGMTIDDGkhwLAPEQRNIGMIFQDYALFPHLTVAE 99
Cdd:TIGR01257  946 VDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGKDIETN---LDAVRQSLGMCPQHNILFHHLTVAE 1022

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099586   100 NIAF--GLRQMAAEERHLQVQQMLELVHLSGFGDRYPHQLSGGQQQRVAIARSLAYKPDLLLLDEPFSNIDTQVRHDLIG 177
Cdd:TIGR01257 1023 HILFyaQLKGRSWEEAQLEMEAMLEDTGLHHKRNEEAQDLSGGMQRKLSVAIAFVGDAKVVVLDEPTSGVDPYSRRSIWD 1102

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099586   178 EIRKIfkKQGVTAIFVTHSREEAFAFADKMAVMNHGvieqygtasELYYRPSSKFVADFLGGGSYLPATR 247
Cdd:TIGR01257 1103 LLLKY--RSGRTIIMSTHHMDEADLLGDRIAIISQG---------RLYCSGTPLFLKNCFGTGFYLTLVR 1161

ABCF_EF-3

cd03221

ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ...

5-198

1.93e-24

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: 96.75 E-value: 1.93e-24

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099586   5 LSIQNLTCQYDTQTVLESLSLNVEHGEIVCLLGASGCGKTTLLKAIAGLLPLSSGImslngmtiddgkhwlapeqrnigm 84
Cdd:cd03221    1 IELENLSKTYGGKLLLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGI------------------------ 56

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099586  85 ifqdyalfphLTVAENIAFGlrqmaaeerhlqvqqmlelvhlsgfgdrYPHQLSGGQQQRVAIARSLAYKPDLLLLDEPF 164
Cdd:cd03221   57 ----------VTWGSTVKIG----------------------------YFEQLSGGEKMRLALAKLLLENPNLLLLDEPT 98

                        170       180       190
                 ....*....|....*....|....*....|....
gi 521099586 165 SNIDTQVRHDLIGEIRKiFKKqgvTAIFVTHSRE 198
Cdd:cd03221   99 NHLDLESIEALEEALKE-YPG---TVILVSHDRY 128

Uup

COG0488

ATPase components of ABC transporters with duplicated ATPase domains [General function ...

5-220

2.10e-24

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

Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 103.61 E-value: 2.10e-24

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099586   5 LSIQNLTCQYDTQTVLESLSLNVEHGEIVCLLGASGCGKTTLLKAIAGLLPLSSGIMSLnGMTIddgkhwlapeqrNIGM 84
Cdd:COG0488  316 LELEGLSKSYGDKTLLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPDSGTVKL-GETV------------KIGY 382

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099586  85 IFQDYALF-PHLTVAENIafglRQMAAEERHLQVQQMLElvhlsGFG------DRYPHQLSGGQQQRVAIARSLAYKPDL 157
Cdd:COG0488  383 FDQHQEELdPDKTVLDEL----RDGAPGGTEQEVRGYLG-----RFLfsgddaFKPVGVLSGGEKARLALAKLLLSPPNV 453

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 521099586 158 LLLDEPFSNIDTQVRH---DLIGEirkiFKkqGvTAIFVTHSREeafaFADKMA-----VMNHGVIEQYGT 220
Cdd:COG0488  454 LLLDEPTNHLDIETLEaleEALDD----FP--G-TVLLVSHDRY----FLDRVAtrileFEDGGVREYPGG 513

PRK14271

phosphate ABC transporter ATP-binding protein; Provisional

4-241

3.42e-24

phosphate ABC transporter ATP-binding protein; Provisional

Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 99.79 E-value: 3.42e-24

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099586   4 ALSIQNLTCQYDTQTVLESLSLNVEHGEIVCLLGASGCGKTTLLKAIAGLLPLSSGI-----MSLNGMTIDDGKHWLApE 78
Cdd:PRK14271  21 AMAAVNLTLGFAGKTVLDQVSMGFPARAVTSLMGPTGSGKTTFLRTLNRMNDKVSGYrysgdVLLGGRSIFNYRDVLE-F 99

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099586  79 QRNIGMIFQDYALFPhLTVAENIAFGLRQMA----AEERHLQVQQMLELVHLSGFGDRY---PHQLSGGQQQRVAIARSL 151
Cdd:PRK14271 100 RRRVGMLFQRPNPFP-MSIMDNVLAGVRAHKlvprKEFRGVAQARLTEVGLWDAVKDRLsdsPFRLSGGQQQLLCLARTL 178

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099586 152 AYKPDLLLLDEPFSNIDTQVRHDLIGEIRKIFKKqgVTAIFVTHSREEAFAFADKMAVMNHGVIEQYGTASELYYRPSSK 231
Cdd:PRK14271 179 AVNPEVLLLDEPTSALDPTTTEKIEEFIRSLADR--LTVIIVTHNLAQAARISDRAALFFDGRLVEEGPTEQLFSSPKHA 256

                        250
                 ....*....|
gi 521099586 232 FVADFLGGGS 241
Cdd:PRK14271 257 ETARYVAGLS 266

ABC_NatA_like

cd03267

ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ...

14-215

3.47e-24

ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; NatA is the ATPase component of a bacterial ABC-type Na+ transport system called NatAB, which catalyzes ATP-dependent electrogenic Na+ extrusion without mechanically coupled to proton or K+ uptake. NatB possess six putative membrane spanning regions at its C-terminus. In B. subtilis, NatAB is inducible by agents such as ethanol and protonophores, which lower the proton-motive force across the membrane. The closest sequence similarity to NatA is exhibited by DrrA of the two-component daunorubicin- and doxorubicin-efflux system. Hence, the functional NatAB is presumably assembled with two copies of the single ATP-binding protein and the single integral membrane protein.

Pssm-ID: 213234 [Multi-domain] Cd Length: 236 Bit Score: 98.94 E-value: 3.47e-24

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099586  14 YDTQTVLESLSLNVEHGEIVCLLGASGCGKTTLLKAIAGLLPLSSGIMSLNGMTIDDGKHWLApeqRNIGMIF-QDYALF 92
Cdd:cd03267   31 YREVEALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRVAGLVPWKRRKKFL---RRIGVVFgQKTQLW 107

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099586  93 PHLTVAENIAF-----GLRQMAAEERHLQVQQMLELVHLSgfgDRYPHQLSGGQQQRVAIARSLAYKPDLLLLDEPFSNI 167
Cdd:cd03267  108 WDLPVIDSFYLlaaiyDLPPARFKKRLDELSELLDLEELL---DTPVRQLSLGQRMRAEIAAALLHEPEILFLDEPTIGL 184

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*...
gi 521099586 168 DTQVRHDLIGEIRKIFKKQGVTAIFVTHSREEAFAFADKMAVMNHGVI 215
Cdd:cd03267  185 DVVAQENIRNFLKEYNRERGTTVLLTSHYMKDIEALARRVLVIDKGRL 232

ABC_KpsT_Wzt

cd03220

ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ...

12-219

7.86e-24

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: 97.60 E-value: 7.86e-24

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099586  12 CQYDTQTVLESLSLNVEHGEIVCLLGASGCGKTTLLKAIAGLLPLSSGIMSLNGmtiddGKHWLApeqrNIGMIFQdyal 91
Cdd:cd03220   30 GEVGEFWALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVTVRG-----RVSSLL----GLGGGFN---- 96

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099586  92 fPHLTVAENIAFGLRQMA--AEERHLQVQQMLELVHLSGFGDRYPHQLSGGQQQRVAIARSLAYKPDLLLLDEPFSNIDT 169
Cdd:cd03220   97 -PELTGRENIYLNGRLLGlsRKEIDEKIDEIIEFSELGDFIDLPVKTYSSGMKARLAFAIATALEPDILLIDEVLAVGDA 175

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|
gi 521099586 170 QVRHDLIGEIRKiFKKQGVTAIFVTHSREEAFAFADKMAVMNHGVIEQYG 219
Cdd:cd03220  176 AFQEKCQRRLRE-LLKQGKTVILVSHDPSSIKRLCDRALVLEKGKIRFDG 224

nikD

PRK10418

nickel transporter ATP-binding protein NikD; Provisional

5-252

1.52e-23

nickel transporter ATP-binding protein NikD; Provisional

Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 97.46 E-value: 1.52e-23

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099586   5 LSIQNLTCQYDTQTVlESLSLNVEHGEIVCLLGASGCGKTTLLKAIAGLLPlsSGIMSLNGMTIDDGKHwLAPEQ---RN 81
Cdd:PRK10418   5 IELRNIALQAAQPLV-HGVSLTLQRGRVLALVGGSGSGKSLTCAAALGILP--AGVRQTAGRVLLDGKP-VAPCAlrgRK 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099586  82 IGMIFQD--YALFPHLTVAeniAFGLRQMAAEERHLQVQQMLELVHLSGFGD------RYPHQLSGGQQQRVAIARSLAY 153
Cdd:PRK10418  81 IATIMQNprSAFNPLHTMH---THARETCLALGKPADDATLTAALEAVGLENaarvlkLYPFEMSGGMLQRMMIALALLC 157

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099586 154 KPDLLLLDEPFSNIDTQVRHDLIGEIRKIFKKQGVTAIFVTHSREEAFAFADKMAVMNHGVIEQYGTASELYYRPSSkfv 233
Cdd:PRK10418 158 EAPFIIADEPTTDLDVVAQARILDLLESIVQKRALGMLLVTHDMGVVARLADDVAVMSHGRIVEQGDVETLFNAPKH--- 234

                        250       260
                 ....*....|....*....|.
gi 521099586 234 adflgggsylPATR--LAEHQ 252
Cdd:PRK10418 235 ----------AVTRslVSAHL 245

livF

PRK11614

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

1-221

2.04e-23

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

Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 96.87 E-value: 2.04e-23

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099586   1 MSCALSIQNLTCQYDTQTVLESLSLNVEHGEIVCLLGASGCGKTTLLKAIAGLLPLSSGIMSLNGMTIDDgkhWLAPE-- 78
Cdd:PRK11614   2 EKVMLSFDKVSAHYGKIQALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDGKDITD---WQTAKim 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099586  79 QRNIGMIFQDYALFPHLTVAENIAFGlrQMAAEERhlQVQQMLELVHlsgfgDRYP------HQ----LSGGQQQRVAIA 148
Cdd:PRK11614  79 REAVAIVPEGRRVFSRMTVEENLAMG--GFFAERD--QFQERIKWVY-----ELFPrlherrIQragtMSGGEQQMLAIG 149

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 521099586 149 RSLAYKPDLLLLDEP---FSNIDTQVRHDLIGEIRkifkKQGVTAIFVTHSREEAFAFADKMAVMNHG--VIEQYGTA 221
Cdd:PRK11614 150 RALMSQPRLLLLDEPslgLAPIIIQQIFDTIEQLR----EQGMTIFLVEQNANQALKLADRGYVLENGhvVLEDTGDA 223

bacteriocin_ABC

TIGR01193

ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ...

5-224

2.24e-23

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: 100.97 E-value: 2.24e-23

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099586    5 LSIQNLTCQYD-TQTVLESLSLNVEHGEIVCLLGASGCGKTTLLKAIAGLLPLSSGIMSLNGMTIDD-GKHWLapeQRNI 82
Cdd:TIGR01193 474 IVINDVSYSYGyGSNILSDISLTIKMNSKTTIVGMSGSGKSTLAKLLVGFFQARSGEILLNGFSLKDiDRHTL---RQFI 550

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099586   83 GMIFQDYALFPHlTVAENIAFGLRQMAAEErhlQVQQMLELVHLS--------GFGDRYPHQ---LSGGQQQRVAIARSL 151
Cdd:TIGR01193 551 NYLPQEPYIFSG-SILENLLLGAKENVSQD---EIWAACEIAEIKddienmplGYQTELSEEgssISGGQKQRIALARAL 626

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 521099586  152 AYKPDLLLLDEPFSNIDTQVRHDLIGEIRKIFKKqgvTAIFVTHsREEAFAFADKMAVMNHGVIEQYGTASEL 224
Cdd:TIGR01193 627 LTDSKVLILDESTSNLDTITEKKIVNNLLNLQDK---TIIFVAH-RLSVAKQSDKIIVLDHGKIIEQGSHDEL 695

3a01204

TIGR00955

The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ...

16-237

2.90e-23

The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]

Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 100.51 E-value: 2.90e-23

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099586   16 TQTVLESLSLNVEHGEIVCLLGASGCGKTTLLKAIAGLLP---LSSGIMSLNGMTIDdgkhwlAPEQRNI-GMIFQDYAL 91
Cdd:TIGR00955  37 RKHLLKNVSGVAKPGELLAVMGSSGAGKTTLMNALAFRSPkgvKGSGSVLLNGMPID------AKEMRAIsAYVQQDDLF 110

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099586   92 FPHLTVAENIAFGL-----RQMAAEERHLQVQQMLELVHLS-------GFGDRYpHQLSGGQQQRVAIARSLAYKPDLLL 159
Cdd:TIGR00955 111 IPTLTVREHLMFQAhlrmpRRVTKKEKRERVDEVLQALGLRkcantriGVPGRV-KGLSGGERKRLAFASELLTDPPLLF 189

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099586  160 LDEPFSNIDTQVRHDLIGEIRKIFKKqGVTAIFVTHS-REEAFAFADKMAVMNHGVIEQYGTASEL--------YYRPSS 230
Cdd:TIGR00955 190 CDEPTSGLDSFMAYSVVQVLKGLAQK-GKTIICTIHQpSSELFELFDKIILMAEGRVAYLGSPDQAvpffsdlgHPCPEN 268


                  ....*..
gi 521099586  231 KFVADFL 237
Cdd:TIGR00955 269 YNPADFY 275

livG

PRK11300

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

5-213

5.78e-23

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

Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 95.83 E-value: 5.78e-23

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099586   5 LSIQNLTCQYDTQTVLESLSLNVEHGEIVCLLGASGCGKTTLLKAIAGLLPLSSGIMSLNGMTIDdGK--HWLApeqrNI 82
Cdd:PRK11300   6 LSVSGLMMRFGGLLAVNNVNLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTILLRGQHIE-GLpgHQIA----RM 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099586  83 GMI--FQDYALFPHLTVAENIafglrqMAAEERHLQV-----------------------QQMLELVHLSGFGDRYPHQL 137
Cdd:PRK11300  81 GVVrtFQHVRLFREMTVIENL------LVAQHQQLKTglfsgllktpafrraesealdraATWLERVGLLEHANRQAGNL 154

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 521099586 138 SGGQQQRVAIARSLAYKPDLLLLDEPFSNIDTQVRHD---LIGEIRKIFkkqGVTAIFVTHSREEAFAFADKMAVMNHG 213
Cdd:PRK11300 155 AYGQQRRLEIARCMVTQPEILMLDEPAAGLNPKETKEldeLIAELRNEH---NVTVLLIEHDMKLVMGISDRIYVVNQG 230

btuD

PRK09536

corrinoid ABC transporter ATPase; Reviewed

5-239

1.35e-22

corrinoid ABC transporter ATPase; Reviewed

Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 97.60 E-value: 1.35e-22

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099586   5 LSIQNLTCQYDTQTVLESLSLNVEHGEIVCLLGASGCGKTTLLKAIAGLLPLSSGIMSLNGmtiDDGKHWLAPE-QRNIG 83
Cdd:PRK09536   4 IDVSDLSVEFGDTTVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAG---DDVEALSARAaSRRVA 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099586  84 MIFQDYALFPHLTVAENIAFGL--------RQMAAEERhlQVQQMLELVHLSGFGDRYPHQLSGGQQQRVAIARSLAYKP 155
Cdd:PRK09536  81 SVPQDTSLSFEFDVRQVVEMGRtphrsrfdTWTETDRA--AVERAMERTGVAQFADRPVTSLSGGERQRVLLARALAQAT 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099586 156 DLLLLDEPFSNIDT--QVRhdlIGEIRKIFKKQGVTAIFVTHSREEAFAFADKMAVMNHGVIEQYGtaselyyRPSSKFV 233
Cdd:PRK09536 159 PVLLLDEPTASLDInhQVR---TLELVRRLVDDGKTAVAAIHDLDLAARYCDELVLLADGRVRAAG-------PPADVLT 228


                 ....*.
gi 521099586 234 ADFLGG 239
Cdd:PRK09536 229 ADTLRA 234

ABC2_perm_RbbA

NF033858

ribosome-associated ATPase/putative transporter RbbA;

8-222

1.37e-22

ribosome-associated ATPase/putative transporter RbbA;

Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 99.04 E-value: 1.37e-22

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099586   8 QNLTCQYDTQTVLESLSLNVEHGEIVCLLGASGCGKTTLLKAIAGLLPLSSGIMSLNGMTIDDGKhwLAPEQRnIGMIFQ 87
Cdd:NF033858 270 RGLTMRFGDFTAVDHVSFRIRRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGEAWLFGQPVDAGD--IATRRR-VGYMSQ 346

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099586  88 DYALFPHLTVAENIAFGLR--QMAAEERHLQVQQMLELVHLSGFGDRYPHQLSGGQQQRVAIARSLAYKPDLLLLDEPFS 165
Cdd:NF033858 347 AFSLYGELTVRQNLELHARlfHLPAAEIAARVAEMLERFDLADVADALPDSLPLGIRQRLSLAVAVIHKPELLILDEPTS 426

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 521099586 166 NIDTQVR----HDLIGEIRkifkKQGVTaIFV-THSREEAfAFADKMAVMNHG----------VIEQYGTAS 222
Cdd:NF033858 427 GVDPVARdmfwRLLIELSR----EDGVT-IFIsTHFMNEA-ERCDRISLMHAGrvlasdtpaaLVAARGAAT 492

dppD

PRK11022

dipeptide transporter ATP-binding subunit; Provisional

23-228

1.53e-22

dipeptide transporter ATP-binding subunit; Provisional

Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 96.35 E-value: 1.53e-22

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099586  23 LSLNVEHGEIVCLLGASGCGKTTLLKAIAGLLPLSSGIM----SLNGMTIDDgkhwLAPEQR------NIGMIFQD--YA 90
Cdd:PRK11022  26 ISYSVKQGEVVGIVGESGSGKSVSSLAIMGLIDYPGRVMaeklEFNGQDLQR----ISEKERrnlvgaEVAMIFQDpmTS 101

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099586  91 LFPHLTVAENIAFGLRQMAAEERHLQVQQMLELVHLSGFGDR------YPHQLSGGQQQRVAIARSLAYKPDLLLLDEPF 164
Cdd:PRK11022 102 LNPCYTVGFQIMEAIKVHQGGNKKTRRQRAIDLLNQVGIPDPasrldvYPHQLSGGMSQRVMIAMAIACRPKLLIADEPT 181

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 521099586 165 SNIDTQVRHDLIGEIRKIFKKQGVTAIFVTHSREEAFAFADKMAVMNHGVIEQYGTASELYYRP 228
Cdd:PRK11022 182 TALDVTIQAQIIELLLELQQKENMALVLITHDLALVAEAAHKIIVMYAGQVVETGKAHDIFRAP 245

NupO

COG3845

ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ...

4-215

1.80e-22

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

Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 97.79 E-value: 1.80e-22

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099586   4 ALSIQNLTCQYDT-QTVLESLSLNVEHGEIVCLLGASGCGKTTLLKAIAGLLPLSSGIMSLNGMTIDDgkhwLAPEQR-- 80
Cdd:COG3845  257 VLEVENLSVRDDRgVPALKDVSLEVRAGEILGIAGVAGNGQSELAEALAGLRPPASGSIRLDGEDITG----LSPRERrr 332

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099586  81 -NIGMIFQD---YALFPHLTVAENIAFG------------LRQMAAEERhlqVQQMLElvhlsGFGDRYPH------QLS 138
Cdd:COG3845  333 lGVAYIPEDrlgRGLVPDMSVAENLILGryrrppfsrggfLDRKAIRAF---AEELIE-----EFDVRTPGpdtparSLS 404

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099586 139 GGQQQRVAIARSLAYKPDLLLLDEPFSNIDtqvrhdlIGEIRKIFKK------QGVTAIFVTHSREEAFAFADKMAVMNH 212
Cdd:COG3845  405 GGNQQKVILARELSRDPKLLIAAQPTRGLD-------VGAIEFIHQRllelrdAGAAVLLISEDLDEILALSDRIAVMYE 477


                 ...
gi 521099586 213 GVI 215
Cdd:COG3845  478 GRI 480

PRK10253

iron-enterobactin ABC transporter ATP-binding protein;

8-224

1.89e-22

iron-enterobactin ABC transporter ATP-binding protein;

Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 94.67 E-value: 1.89e-22

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099586   8 QNLTCQYDTQTVLESLSLNVEHGEIVCLLGASGCGKTTLLKAIAGLLPLSSGIMSLNGMTIddgKHWLAPE-QRNIGMIF 86
Cdd:PRK10253  11 EQLTLGYGKYTVAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHI---QHYASKEvARRIGLLA 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099586  87 QDYALFPHLTVAENIAFG------LRQMAAEERHLQVQQMLELVHLSGFGDRYPHQLSGGQQQRVAIARSLAYKPDLLLL 160
Cdd:PRK10253  88 QNATTPGDITVQELVARGryphqpLFTRWRKEDEEAVTKAMQATGITHLADQSVDTLSGGQRQRAWIAMVLAQETAIMLL 167

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 521099586 161 DEPFSNIDTQVRHDLIGEIRKIFKKQGVTAIFVTHSREEAFAFADKMAVMNHGVIEQYGTASEL 224
Cdd:PRK10253 168 DEPTTWLDISHQIDLLELLSELNREKGYTLAAVLHDLNQACRYASHLIALREGKIVAQGAPKEI 231

met_CoM_red_A2

TIGR03269

methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ...

5-262

3.60e-22

Pssm-ID: 132313 [Multi-domain] Cd Length: 520 Bit Score: 97.18 E-value: 3.60e-22

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099586    5 LSIQNLTCQYDTQTVLESLSLNVEHGEIVCLLGASGCGKTTL---LKAIAGLLPLSSGI---MSL--------------- 63
Cdd:TIGR03269   1 IEVKNLTKKFDGKEVLKNISFTIEEGEVLGILGRSGAGKSVLmhvLRGMDQYEPTSGRIiyhVALcekcgyverpskvge 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099586   64 ------NGMTIDDGKHWLAPE------QRNIGMIFQ-DYALFPHLTVAENIAFGLRQMAAEERHlQVQQMLELVHLSGFG 130
Cdd:TIGR03269  81 pcpvcgGTLEPEEVDFWNLSDklrrriRKRIAIMLQrTFALYGDDTVLDNVLEALEEIGYEGKE-AVGRAVDLIEMVQLS 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099586  131 DRYPH---QLSGGQQQRVAIARSLAYKPDLLLLDEPFSNIDTQVRhDLIGE-IRKIFKKQGVTAIFVTHSREEAFAFADK 206
Cdd:TIGR03269 160 HRITHiarDLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTA-KLVHNaLEEAVKASGISMVLTSHWPEVIEDLSDK 238

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 521099586  207 MAVMNHGVIEQYGTASELyyrpSSKFV---------ADFLGGGSYLPATRLAEHQYQTPLGVVDA 262
Cdd:TIGR03269 239 AIWLENGEIKEEGTPDEV----VAVFMegvsevekeCEVEVGEPIIKVRNVSKRYISVDRGVVKA 299

PRK09700

D-allose ABC transporter ATP-binding protein AlsA;

5-213

4.49e-22

D-allose ABC transporter ATP-binding protein AlsA;

Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 96.78 E-value: 4.49e-22

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099586   5 LSIQNLTCQYDTQTVLESLSLNVEHGEIVCLLGASGCGKTTLLKAIAGLLPLSSGIMSLNGMTIDDGKHWLAPEQrNIGM 84
Cdd:PRK09700   6 ISMAGIGKSFGPVHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNINYNKLDHKLAAQL-GIGI 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099586  85 IFQDYALFPHLTVAENI---------AFGLRQMAAEERHLQVQQMLELVHLSGFGDRYPHQLSGGQQQRVAIARSLAYKP 155
Cdd:PRK09700  85 IYQELSVIDELTVLENLyigrhltkkVCGVNIIDWREMRVRAAMMLLRVGLKVDLDEKVANLSISHKQMLEIAKTLMLDA 164

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 521099586 156 DLLLLDEPFSNIdTQVRHDLIGEIRKIFKKQGVTAIFVTHSREEAFAFADKMAVMNHG 213
Cdd:PRK09700 165 KVIIMDEPTSSL-TNKEVDYLFLIMNQLRKEGTAIVYISHKLAEIRRICDRYTVMKDG 221

ABCC_MRP_domain2

cd03244

ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ...

5-220

8.04e-22

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: 91.79 E-value: 8.04e-22

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099586   5 LSIQNLTCQY--DTQTVLESLSLNVEHGEIVCLLGASGCGKTTLLKAIAGLLPLSSGIMSLNGMTIDD-GKHWLapeQRN 81
Cdd:cd03244    3 IEFKNVSLRYrpNLPPVLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSILIDGVDISKiGLHDL---RSR 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099586  82 IGMIFQDYALFPHlTVAENIA-FGLrqmAAEErhlQVQQMLELVHLSGFGDRYPHQL-----------SGGQQQRVAIAR 149
Cdd:cd03244   80 ISIIPQDPVLFSG-TIRSNLDpFGE---YSDE---ELWQALERVGLKEFVESLPGGLdtvveeggenlSVGQRQLLCLAR 152

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 521099586 150 SLAYKPDLLLLDEPFSNIDTQVRHdLIGE-IRKIFKkqGVTAIFVTHsREEAFAFADKMAVMNHGVIEQYGT 220
Cdd:cd03244  153 ALLRKSKILVLDEATASVDPETDA-LIQKtIREAFK--DCTVLTIAH-RLDTIIDSDRILVLDKGRVVEFDS 220

ATM1

COG5265

ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ...

14-224

1.24e-21

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: 95.66 E-value: 1.24e-21

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099586  14 YDTQ-TVLESLSLNVEHGEIVCLLGASGCGKTTLLKAIAGLLPLSSGIMSLNGMTIDDgkhwLAPE--QRNIGMIFQDYA 90
Cdd:COG5265  367 YDPErPILKGVSFEVPAGKTVAIVGPSGAGKSTLARLLFRFYDVTSGRILIDGQDIRD----VTQAslRAAIGIVPQDTV 442

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099586  91 LFpHLTVAENIAFGlRQMAAEErhlQVQQMLELVHLSGFGDRYPHQ-----------LSGGQQQRVAIARSLAYKPDLLL 159
Cdd:COG5265  443 LF-NDTIAYNIAYG-RPDASEE---EVEAAARAAQIHDFIESLPDGydtrvgerglkLSGGEKQRVAIARTLLKNPPILI 517

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 521099586 160 LDEPFSNIDTQVRHDLIGEIRKIfkKQGVTAIFVTHsREEAFAFADKMAVMNHGVIEQYGTASEL 224
Cdd:COG5265  518 FDEATSALDSRTERAIQAALREV--ARGRTTLVIAH-RLSTIVDADEILVLEAGRIVERGTHAEL 579

ABCC_cytochrome_bd

cd03247

ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ...

5-219

1.25e-21

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

Pssm-ID: 213214 [Multi-domain] Cd Length: 178 Bit Score: 90.45 E-value: 1.25e-21

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099586   5 LSIQNLTCQYD--TQTVLESLSLNVEHGEIVCLLGASGCGKTTLLKAIAGLLPLSSGIMSLNGMTIDDGKHWLApeqRNI 82
Cdd:cd03247    1 LSINNVSFSYPeqEQQVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDGVPVSDLEKALS---SLI 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099586  83 GMIFQDyalfPHL---TVAENIafGLRqmaaeerhlqvqqmlelvhlsgfgdryphqLSGGQQQRVAIARSLAYKPDLLL 159
Cdd:cd03247   78 SVLNQR----PYLfdtTLRNNL--GRR------------------------------FSGGERQRLALARILLQDAPIVL 121

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099586 160 LDEPFSNIDTQVRHDLIGEIRKIFKkqGVTAIFVTHsREEAFAFADKMAVMNHGVIEQYG 219
Cdd:cd03247  122 LDEPTVGLDPITERQLLSLIFEVLK--DKTLIWITH-HLTGIEHMDKILFLENGKIIMQG 178

ABC_FeS_Assembly

cd03217

ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ...

5-215

2.17e-21

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: 90.28 E-value: 2.17e-21

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099586   5 LSIQNLTCQYDTQTVLESLSLNVEHGEIVCLLGASGCGKTTLLKAIAGlLP---LSSGIMSLNGMTIDDgkhwLAPEQR- 80
Cdd:cd03217    1 LEIKDLHVSVGGKEILKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMG-HPkyeVTEGEILFKGEDITD----LPPEERa 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099586  81 --NIGMIFQDYALFPHLTVAENIafglrqmaaeeRHLQVqqmlelvhlsGFgdryphqlSGGQQQRVAIARSLAYKPDLL 158
Cdd:cd03217   76 rlGIFLAFQYPPEIPGVKNADFL-----------RYVNE----------GF--------SGGEKKRNEILQLLLLEPDLA 126

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099586 159 LLDEPFSNID-TQVRhdLIGEIRKIFKKQGVTAIFVTHsREEAFAF--ADKMAVMNHGVI 215
Cdd:cd03217  127 ILDEPDSGLDiDALR--LVAEVINKLREEGKSVLIITH-YQRLLDYikPDRVHVLYDGRI 183

PRK11160

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

4-224

3.47e-21

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

Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 94.51 E-value: 3.47e-21

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099586   4 ALSIQNLTCQY--DTQTVLESLSLNVEHGEIVCLLGASGCGKTTLLKAIAGLLPLSSGIMSLNGMTIDDgkhWlaPEQ-- 79
Cdd:PRK11160 338 SLTLNNVSFTYpdQPQPVLKGLSLQIKAGEKVALLGRTGCGKSTLLQLLTRAWDPQQGEILLNGQPIAD---Y--SEAal 412

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099586  80 -RNIGMIFQDYALFPHlTVAENIAFGLRQmAAEERHLQVQQMLELVHLS----------GFGDRyphQLSGGQQQRVAIA 148
Cdd:PRK11160 413 rQAISVVSQRVHLFSA-TLRDNLLLAAPN-ASDEALIEVLQQVGLEKLLeddkglnawlGEGGR---QLSGGEQRRLGIA 487

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 521099586 149 RSLAYKPDLLLLDEPFSNIDTQVRHDLIGEIRKIFkkQGVTAIFVTHsREEAFAFADKMAVMNHGVIEQYGTASEL 224
Cdd:PRK11160 488 RALLHDAPLLLLDEPTEGLDAETERQILELLAEHA--QNKTVLMITH-RLTGLEQFDRICVMDNGQIIEQGTHQEL 560

SapD

COG4170

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

5-228

4.22e-21

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

Pssm-ID: 443330 [Multi-domain] Cd Length: 331 Bit Score: 92.28 E-value: 4.22e-21

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099586   5 LSIQNLTCQYDTQT----VLESLSLNVEHGEIVCLLGASGCGKTTLLKAIAGLLPLSSGI----MSLNGmtIDDGKhwLA 76
Cdd:COG4170    4 LDIRNLTIEIDTPQgrvkAVDRVSLTLNEGEIRGLVGESGSGKSLIAKAICGITKDNWHVtadrFRWNG--IDLLK--LS 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099586  77 PEQR------NIGMIFQD--YALFPHLTVAENIAFGLRQMAAEERHLQV-----QQMLELVHLSGFGDR------YPHQL 137
Cdd:COG4170   80 PRERrkiigrEIAMIFQEpsSCLDPSAKIGDQLIEAIPSWTFKGKWWQRfkwrkKRAIELLHRVGIKDHkdimnsYPHEL 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099586 138 SGGQQQRVAIARSLAYKPDLLLLDEPFSNID--TQVRhdligeirkIF-------KKQGVTAIFVTHSREEAFAFADKMA 208
Cdd:COG4170  160 TEGECQKVMIAMAIANQPRLLIADEPTNAMEstTQAQ---------IFrllarlnQLQGTSILLISHDLESISQWADTIT 230

                        250       260
                 ....*....|....*....|
gi 521099586 209 VMNHGVIEQYGTASELYYRP 228
Cdd:COG4170  231 VLYCGQTVESGPTEQILKSP 250

PRK10575

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

6-224

6.34e-21

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

Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 90.62 E-value: 6.34e-21

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099586   6 SIQNLTCQYDTQTVLESLSLNVEHGEIVCLLGASGCGKTTLLKAIAGLLPLSSGIMSLNGMTIDDgkhWLAPE-QRNIGM 84
Cdd:PRK10575  13 ALRNVSFRVPGRTLLHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPLES---WSSKAfARKVAY 89

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099586  85 IFQDYALFPHLTVAENIAFG-------LRQMAAEERHlQVQQMLELVHLSGFGDRYPHQLSGGQQQRVAIARSLAYKPDL 157
Cdd:PRK10575  90 LPQQLPAAEGMTVRELVAIGrypwhgaLGRFGAADRE-KVEEAISLVGLKPLAHRLVDSLSGGERQRAWIAMLVAQDSRC 168

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 521099586 158 LLLDEPFSNIDTQVRHDLIGEIRKIFKKQGVTAIFVTHSREEAFAFADKMAVMNHGVIEQYGTASEL 224
Cdd:PRK10575 169 LLLDEPTSALDIAHQVDVLALVHRLSQERGLTVIAVLHDINMAARYCDYLVALRGGEMIAQGTPAEL 235

ABCC_NFT1

cd03369

ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ...

5-220

1.04e-20

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: 88.62 E-value: 1.04e-20

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099586   5 LSIQNLTCQY--DTQTVLESLSLNVEHGEIVCLLGASGCGKTTLLKAIAGLLPLSSGIMSLNGmtIDDGKHWLAPEQRNI 82
Cdd:cd03369    7 IEVENLSVRYapDLPPVLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDG--IDISTIPLEDLRSSL 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099586  83 GMIFQDYALFPHlTVAENIAfglrqmaaEERHLQVQQMLELVHLSGFGDryphQLSGGQQQRVAIARSLAYKPDLLLLDE 162
Cdd:cd03369   85 TIIPQDPTLFSG-TIRSNLD--------PFDEYSDEEIYGALRVSEGGL----NLSQGQRQLLCLARALLKRPRVLVLDE 151

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 521099586 163 PFSNIDTQVRHDLIGEIRKIFkkQGVTAIFVTHsREEAFAFADKMAVMNHGVIEQYGT 220
Cdd:cd03369  152 ATASIDYATDALIQKTIREEF--TNSTILTIAH-RLRTIIDYDKILVMDAGEVKEYDH 206

PhnL

COG4778

Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ...

19-213

1.23e-20

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: 89.03 E-value: 1.23e-20

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099586  19 VLESLSLNVEHGEIVCLLGASGCGKTTLLKAIAG-LLPLSSGIMslngmtIDDGKHWL----APEQ-------RNIGMIF 86
Cdd:COG4778   26 VLDGVSFSVAAGECVALTGPSGAGKSTLLKCIYGnYLPDSGSIL------VRHDGGWVdlaqASPReilalrrRTIGYVS 99

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099586  87 QdyalF----PHLT----VAEN-IAFGLRQMAAEER------HLQVQQmlELVHLsgfgdrYPHQLSGGQQQRVAIARSL 151
Cdd:COG4778  100 Q----FlrviPRVSaldvVAEPlLERGVDREEARARarellaRLNLPE--RLWDL------PPATFSGGEQQRVNIARGF 167

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 521099586 152 AYKPDLLLLDEPFSNIDTQVRH---DLIGEIrkifKKQGVTAIFVTHSREEAFAFADKMAVMNHG 213
Cdd:COG4778  168 IADPPLLLLDEPTASLDAANRAvvvELIEEA----KARGTAIIGIFHDEEVREAVADRVVDVTPF 228

PRK11176

lipid A ABC transporter ATP-binding protein/permease MsbA;

5-224

1.94e-20

lipid A ABC transporter ATP-binding protein/permease MsbA;

Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 92.00 E-value: 1.94e-20

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099586   5 LSIQNLTCQYDTQTV--LESLSLNVEHGEIVCLLGASGCGKTTllkaIAGLLP----LSSGIMSLNGMTIDDGKhwLAPE 78
Cdd:PRK11176 342 IEFRNVTFTYPGKEVpaLRNINFKIPAGKTVALVGRSGSGKST----IANLLTrfydIDEGEILLDGHDLRDYT--LASL 415

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099586  79 QRNIGMIFQDYALFpHLTVAENIAFglrqmAAEERHL--QVQQMLELVHLSGFGDRYPH-----------QLSGGQQQRV 145
Cdd:PRK11176 416 RNQVALVSQNVHLF-NDTIANNIAY-----ARTEQYSreQIEEAARMAYAMDFINKMDNgldtvigengvLLSGGQRQRI 489

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 521099586 146 AIARSLAYKPDLLLLDEPFSNIDTQVRHDLIGEIRKIFKKQgvTAIFVTHsREEAFAFADKMAVMNHGVIEQYGTASEL 224
Cdd:PRK11176 490 AIARALLRDSPILILDEATSALDTESERAIQAALDELQKNR--TSLVIAH-RLSTIEKADEILVVEDGEIVERGTHAEL 565

ABCG_PDR_domain1

cd03233

First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ...

15-219

2.02e-20

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: 87.70 E-value: 2.02e-20

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099586  15 DTQTVLESLSLNVEHGEIVCLLGASGCGKTTLLKAIAGLLPLS---SGIMSLNGMTIDDGKHwlaPEQRNIGMIFQDYAL 91
Cdd:cd03233   18 SKIPILKDFSGVVKPGEMVLVLGRPGSGCSTLLKALANRTEGNvsvEGDIHYNGIPYKEFAE---KYPGEIIYVSEEDVH 94

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099586  92 FPHLTVAENIAFGLRqmaaeerhLQvqqmlelvhlsgfGDRYPHQLSGGQQQRVAIARSLAYKPDLLLLDEPFSNIDTQV 171
Cdd:cd03233   95 FPTLTVRETLDFALR--------CK-------------GNEFVRGISGGERKRVSIAEALVSRASVLCWDNSTRGLDSST 153

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 521099586 172 RHDLIGEIRKIFKKQGVTAIF-VTHSREEAFAFADKMAVMNHGVIEQYG 219
Cdd:cd03233  154 ALEILKCIRTMADVLKTTTFVsLYQASDEIYDLFDKVLVLYEGRQIYYG 202

PRK15056

manganese/iron ABC transporter ATP-binding protein;

1-224

3.46e-20

manganese/iron ABC transporter ATP-binding protein;

Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 88.79 E-value: 3.46e-20

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099586   1 MSCALSIQNLTCQY-DTQTVLESLSLNVEHGEIVCLLGASGCGKTTLLKAIAGLLPLSSGIMSLNGMTIDDgkhwlAPEQ 79
Cdd:PRK15056   3 QQAGIVVNDVTVTWrNGHTALRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKISILGQPTRQ-----ALQK 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099586  80 RNIGMIFQ----DYAlFPHLtVAENIAFG-------LRQMAAEERHLqVQQMLELVHLSGFGDRYPHQLSGGQQQRVAIA 148
Cdd:PRK15056  78 NLVAYVPQseevDWS-FPVL-VEDVVMMGryghmgwLRRAKKRDRQI-VTAALARVDMVEFRHRQIGELSGGQKKRVFLA 154

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099586 149 RSLAYKPDLLLLDEPFSNIDTQVRHDLIGEIRKIfKKQGVTAIFVTHSREEAFAFAD-----KMAVMNHGVIEQYGTASE 223
Cdd:PRK15056 155 RAIAQQGQVILLDEPFTGVDVKTEARIISLLREL-RDEGKTMLVSTHNLGSVTEFCDytvmvKGTVLASGPTETTFTAEN 233


                 .
gi 521099586 224 L 224
Cdd:PRK15056 234 L 234

GguA

NF040905

sugar ABC transporter ATP-binding protein;

20-213

4.94e-20

sugar ABC transporter ATP-binding protein;

Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 90.62 E-value: 4.94e-20

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099586  20 LESLSLNVEHGEIVCLLGASGCGKTTLLKAIAGLLPLSS--GIMSLNGMT-----IDDGkhwlapEQRNIGMIFQDYALF 92
Cdd:NF040905  17 LDDVNLSVREGEIHALCGENGAGKSTLMKVLSGVYPHGSyeGEILFDGEVcrfkdIRDS------EALGIVIIHQELALI 90

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099586  93 PHLTVAENIAFGLRQMAA-----EERHLQVQQMLELVHLsgfgDRYPHQLSG----GQQQRVAIARSLAYKPDLLLLDEP 163
Cdd:NF040905  91 PYLSIAENIFLGNERAKRgvidwNETNRRARELLAKVGL----DESPDTLVTdigvGKQQLVEIAKALSKDVKLLILDEP 166

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 521099586 164 ---FSNIDTQVRHDLIGEirkiFKKQGVTAIFVTHSREEAFAFADKMAVMNHG 213
Cdd:NF040905 167 taaLNEEDSAALLDLLLE----LKAQGITSIIISHKLNEIRRVADSITVLRDG 215

ABCC_TAP

cd03248

ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ...

8-173

5.83e-20

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: 87.14 E-value: 5.83e-20

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099586   8 QNLTCQYDTQT---VLESLSLNVEHGEIVCLLGASGCGKTTLLKAIAGLLPLSSGIMSLNGMTIDDGKHWLAPEQrnIGM 84
Cdd:cd03248   15 QNVTFAYPTRPdtlVLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDGKPISQYEHKYLHSK--VSL 92

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099586  85 IFQDYALFPHlTVAENIAFGLRQMAAEErhlqVQQMLELVHLSGFGDRYPH-----------QLSGGQQQRVAIARSLAY 153
Cdd:cd03248   93 VGQEPVLFAR-SLQDNIAYGLQSCSFEC----VKEAAQKAHAHSFISELASgydtevgekgsQLSGGQKQRVAIARALIR 167

                        170       180
                 ....*....|....*....|
gi 521099586 154 KPDLLLLDEPFSNIDTQVRH 173
Cdd:cd03248  168 NPQVLILDEATSALDAESEQ 187

BtuD

COG4138

ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ...

20-223

8.87e-20

ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism];

Pssm-ID: 443313 [Multi-domain] Cd Length: 248 Bit Score: 86.82 E-value: 8.87e-20

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099586  20 LESLSLNVEHGEIVCLLGASGCGKTTLLKAIAGLLPlSSGIMSLNGMTIDDgkhWLAPEQ-RNIGMIFQDYALFPHLTVA 98
Cdd:COG4138   12 LGPISAQVNAGELIHLIGPNGAGKSTLLARMAGLLP-GQGEILLNGRPLSD---WSAAELaRHRAYLSQQQSPPFAMPVF 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099586  99 ENIAFGLRQMAAEERHLQVqqMLELVHLSGFGDRYP---HQLSGGQQQRVAIARSL-----AYKPD--LLLLDEPFSNID 168
Cdd:COG4138   88 QYLALHQPAGASSEAVEQL--LAQLAEALGLEDKLSrplTQLSGGEWQRVRLAAVLlqvwpTINPEgqLLLLDEPMNSLD 165

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099586 169 tqVRH-----DLIGEirkiFKKQGVTAIFVTHSREEAFAFADKMAVMNHGVIEQYGTASE 223
Cdd:COG4138  166 --VAQqaaldRLLRE----LCQQGITVVMSSHDLNHTLRHADRVWLLKQGKLVASGETAE 219

ABC2_perm_RbbA

NF033858

ribosome-associated ATPase/putative transporter RbbA;

4-252

1.70e-19

ribosome-associated ATPase/putative transporter RbbA;

Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 89.80 E-value: 1.70e-19

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099586   4 ALSIQNLTCQYDTQTVLESLSLNVEHGEIVCLLGASGCGKTTLLKAIAGLLPLSSG-IMSLNGmTIDDGKH--WLAPE-- 78
Cdd:NF033858   1 VARLEGVSHRYGKTVALDDVSLDIPAGCMVGLIGPDGVGKSSLLSLIAGARKIQQGrVEVLGG-DMADARHrrAVCPRia 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099586  79 ---Q---RNigmifqdyaLFPHLTVAENIAF-----GLrqmAAEERHLQVQQMLELVHLSGFGDRYPHQLSGGQQQRVAI 147
Cdd:NF033858  80 ympQglgKN---------LYPTLSVFENLDFfgrlfGQ---DAAERRRRIDELLRATGLAPFADRPAGKLSGGMKQKLGL 147

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099586 148 ARSLAYKPDLLLLDEPFSNIDTQVRH---DLIGEIRKifKKQGVTAIFVTHSREEAFAFaDKMAVMNHGVIEQYGTASEL 224
Cdd:NF033858 148 CCALIHDPDLLILDEPTTGVDPLSRRqfwELIDRIRA--ERPGMSVLVATAYMEEAERF-DWLVAMDAGRVLATGTPAEL 224

                        250       260       270
                 ....*....|....*....|....*....|...
gi 521099586 225 YYRPSSK-----FVAdflgggsYLPATRLAEHQ 252
Cdd:NF033858 225 LARTGADtleaaFIA-------LLPEEKRRGHQ 250

COG4586

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

13-215

2.04e-19

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

Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 87.45 E-value: 2.04e-19

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099586  13 QYDTQTVLESLSLNVEHGEIVCLLGASGCGKTTLLKAIAGLLPLSSGIMSLNGMTIDDGKHWLApeqRNIGMIF-QDYAL 91
Cdd:COG4586   31 EYREVEAVDDISFTIEPGEIVGFIGPNGAGKSTTIKMLTGILVPTSGEVRVLGYVPFKRRKEFA---RRIGVVFgQRSQL 107

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099586  92 FPHLTVAENIAFgLRQM------AAEERhlqVQQMLELVHLSGFGDRYPHQLSGGQQQRVAIARSLAYKPDLLLLDEPFS 165
Cdd:COG4586  108 WWDLPAIDSFRL-LKAIyripdaEYKKR---LDELVELLDLGELLDTPVRQLSLGQRMRCELAAALLHRPKILFLDEPTI 183

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 521099586 166 NID--TQVR-HDLIGEIRkifKKQGVTAIFVTHSREEAFAFADKMAVMNHGVI 215
Cdd:COG4586  184 GLDvvSKEAiREFLKEYN---RERGTTILLTSHDMDDIEALCDRVIVIDHGRI 233

PLN03211

ABC transporter G-25; Provisional

6-236

5.68e-19

ABC transporter G-25; Provisional

Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 88.01 E-value: 5.68e-19

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099586   6 SIQNLTCQYDTQTVLESLSLNVEHGEIVCLLGASGCGKTTLLKAIAGLLPLSSgimsLNGMTIDDGKHWLAPEQRNIGMI 85
Cdd:PLN03211  70 KISDETRQIQERTILNGVTGMASPGEILAVLGPSGSGKSTLLNALAGRIQGNN----FTGTILANNRKPTKQILKRTGFV 145

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099586  86 FQDYALFPHLTVAENIAFGL-----RQMAAEERHLQVQQMLELVHLSG-----FGDRYPHQLSGGQQQRVAIARSLAYKP 155
Cdd:PLN03211 146 TQDDILYPHLTVRETLVFCSllrlpKSLTKQEKILVAESVISELGLTKcentiIGNSFIRGISGGERKRVSIAHEMLINP 225

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099586 156 DLLLLDEPFSNIDTQVRHDLIGEIRKIFKKQG--VTAIFVTHSReeAFAFADKMAVMNHGVIEQYGTASE-LYYRPSSKF 232
Cdd:PLN03211 226 SLLILDEPTSGLDATAAYRLVLTLGSLAQKGKtiVTSMHQPSSR--VYQMFDSVLVLSEGRCLFFGKGSDaMAYFESVGF 303


                 ....
gi 521099586 233 VADF 236
Cdd:PLN03211 304 SPSF 307

MK0520

COG2401

ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ...

15-199

6.49e-19

ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];

Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 83.85 E-value: 6.49e-19

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099586  15 DTQTVLESLSLNVEHGEIVCLLGASGCGKTTLLKAIAGLLPLssgimslngmtiddgkhwlAPEQRNIGMifQDYALFPH 94
Cdd:COG2401   41 VERYVLRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGALKG-------------------TPVAGCVDV--PDNQFGRE 99

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099586  95 LTVAENIAfglrqmaaeeRHLQVQQMLELVHLSGFGD-----RYPHQLSGGQQQRVAIARSLAYKPDLLLLDEPFSNIDT 169
Cdd:COG2401  100 ASLIDAIG----------RKGDFKDAVELLNAVGLSDavlwlRRFKELSTGQKFRFRLALLLAERPKLLVIDEFCSHLDR 169

                        170       180       190
                 ....*....|....*....|....*....|
gi 521099586 170 QVRHDLIGEIRKIFKKQGVTAIFVTHsREE 199
Cdd:COG2401  170 QTAKRVARNLQKLARRAGITLVVATH-HYD 198

PRK13657

glucan ABC transporter ATP-binding protein/ permease;

4-224

7.60e-19

glucan ABC transporter ATP-binding protein/ permease;

Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 87.32 E-value: 7.60e-19

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099586   4 ALSIQNLTCQYD-TQTVLESLSLNVEHGEIVCLLGASGCGKTTLLkaiaGLL-----PlSSGIMSLNGMTIDDGKhwLAP 77
Cdd:PRK13657 334 AVEFDDVSFSYDnSRQGVEDVSFEAKPGQTVAIVGPTGAGKSTLI----NLLqrvfdP-QSGRILIDGTDIRTVT--RAS 406

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099586  78 EQRNIGMIFQDYALFPHlTVAENIAFGlRQMAAEErhlQVQQMLELVHLSGFGDRYPH-----------QLSGGQQQRVA 146
Cdd:PRK13657 407 LRRNIAVVFQDAGLFNR-SIEDNIRVG-RPDATDE---EMRAAAERAQAHDFIERKPDgydtvvgergrQLSGGERQRLA 481

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099586 147 IARSLAYKPDLLLLDEPFSNID--TQVR-HDLIGEIRKifkkqGVTAIFVTHsREEAFAFADKMAVMNHGVIEQYGTASE 223
Cdd:PRK13657 482 IARALLKDPPILILDEATSALDveTEAKvKAALDELMK-----GRTTFIIAH-RLSTVRNADRILVFDNGRVVESGSFDE 555


                 .
gi 521099586 224 L 224
Cdd:PRK13657 556 L 556

rim_protein

TIGR01257

retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ...

5-227

9.91e-19

Pssm-ID: 130324 [Multi-domain] Cd Length: 2272 Bit Score: 87.76 E-value: 9.91e-19

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099586     5 LSIQNLTCQYD--TQTVLESLSLNVEHGEIVCLLGASGCGKTTLLKAIAGLLPLSSGIMSLNGMTIddgkhwlapeQRNI 82
Cdd:TIGR01257 1938 LRLNELTKVYSgtSSPAVDRLCVGVRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAGKSI----------LTNI 2007

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099586    83 GMIFQDYALFPHLTVAENIAFG---------LRQMAAEERHLQVQQMLELVHLSGFGDRYPHQLSGGQQQRVAIARSLAY 153
Cdd:TIGR01257 2008 SDVHQNMGYCPQFDAIDDLLTGrehlylyarLRGVPAEEIEKVANWSIQSLGLSLYADRLAGTYSGGNKRKLSTAIALIG 2087

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 521099586   154 KPDLLLLDEPFSNIDTQVRHDLIGEIRKIFkKQGVTAIFVTHSREEAFAFADKMAVMNHGVIEQYGTASELYYR 227
Cdd:TIGR01257 2088 CPPLVLLDEPTTGMDPQARRMLWNTIVSII-REGRAVVLTSHSMEECEALCTRLAIMVKGAFQCLGTIQHLKSK 2160

PRK13540

cytochrome c biogenesis protein CcmA; Provisional

5-197

1.58e-18

cytochrome c biogenesis protein CcmA; Provisional

Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 82.31 E-value: 1.58e-18

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099586   5 LSIQNLTCQYDTQTVLESLSLNVEHGEIVCLLGASGCGKTTLLKAIAGLLPLSSGIMSLNGMTIDDGkhwLAPEQRNIGM 84
Cdd:PRK13540   2 LDVIELDFDYHDQPLLQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEILFERQSIKKD---LCTYQKQLCF 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099586  85 IFQDYALFPHLTVAENIAFGLRQMAAeerHLQVQQMLELVHLSGFGDRYPHQLSGGQQQRVAIARSLAYKPDLLLLDEPF 164
Cdd:PRK13540  79 VGHRSGINPYLTLRENCLYDIHFSPG---AVGITELCRLFSLEHLIDYPCGLLSSGQKRQVALLRLWMSKAKLWLLDEPL 155

                        170       180       190
                 ....*....|....*....|....*....|...
gi 521099586 165 SNIDTQVRHDLIGEIRKiFKKQGVTAIFVTHSR 197
Cdd:PRK13540 156 VALDELSLLTIITKIQE-HRAKGGAVLLTSHQD 187

PRK10762

D-ribose transporter ATP binding protein; Provisional

20-215

3.53e-18

D-ribose transporter ATP binding protein; Provisional

Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 85.06 E-value: 3.53e-18

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099586  20 LESLSLNVEHGEIVCLLGASGCGKTTLLKAIAGLLPLSSGIMSLNGMTID-----DGkhwLApeqRNIGMIFQDY---AL 91
Cdd:PRK10762 268 VNDVSFTLRKGEILGVSGLMGAGRTELMKVLYGALPRTSGYVTLDGHEVVtrspqDG---LA---NGIVYISEDRkrdGL 341

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099586  92 FPHLTVAENIAF-GLRQMAAEERHLQVQQMLELV--HLSGFGDRYPHQ------LSGGQQQRVAIARSLAYKPDLLLLDE 162
Cdd:PRK10762 342 VLGMSVKENMSLtALRYFSRAGGSLKHADEQQAVsdFIRLFNIKTPSMeqaiglLSGGNQQKVAIARGLMTRPKVLILDE 421

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 521099586 163 PFSNIDTQVR---HDLIGEirkiFKKQGVTAIFVTHSREEAFAFADKMAVMNHGVI 215
Cdd:PRK10762 422 PTRGVDVGAKkeiYQLINQ----FKAEGLSIILVSSEMPEVLGMSDRILVMHEGRI 473

PRK09700

D-allose ABC transporter ATP-binding protein AlsA;

7-223

4.28e-18

D-allose ABC transporter ATP-binding protein AlsA;

Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 84.84 E-value: 4.28e-18

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099586   7 IQNLTcQYDTQTVlESLSLNVEHGEIVCLLGASGCGKTTLLKAIAGLLPLSSGIMSLNGMTIDDGKHWLAPEQrniGMIF 86
Cdd:PRK09700 268 VRNVT-SRDRKKV-RDISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEIRLNGKDISPRSPLDAVKK---GMAY 342

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099586  87 -----QDYALFPHLTVAENIA-------------FGLRQMAAEERHLQVQQMLELVHLSGFgDRYPHQLSGGQQQRVAIA 148
Cdd:PRK09700 343 itesrRDNGFFPNFSIAQNMAisrslkdggykgaMGLFHEVDEQRTAENQRELLALKCHSV-NQNITELSGGNQQKVLIS 421

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 521099586 149 RSLAYKPDLLLLDEPFSNIDTQVRhdliGEIRKIFKK---QGVTAIFVTHSREEAFAFADKMAVMNHGVIEQYGTASE 223
Cdd:PRK09700 422 KWLCCCPEVIIFDEPTRGIDVGAK----AEIYKVMRQladDGKVILMVSSELPEIITVCDRIAVFCEGRLTQILTNRD 495

ABCC_CFTR1

cd03291

ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ...

19-242

5.23e-18

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: 82.60 E-value: 5.23e-18

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099586  19 VLESLSLNVEHGEIVCLLGASGCGKTTLLKAIAGLLPLSSGIMSLNG-MTIDDGKHWLAPEqrnigmifqdyalfphlTV 97
Cdd:cd03291   52 VLKNINLKIEKGEMLAITGSTGSGKTSLLMLILGELEPSEGKIKHSGrISFSSQFSWIMPG-----------------TI 114

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099586  98 AENIAFGLRQmaAEERHLQVQQMLELVH-LSGFGDRYPH-------QLSGGQQQRVAIARSLAYKPDLLLLDEPFSNIDt 169
Cdd:cd03291  115 KENIIFGVSY--DEYRYKSVVKACQLEEdITKFPEKDNTvlgeggiTLSGGQRARISLARAVYKDADLYLLDSPFGYLD- 191

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099586 170 qvrhdlIGEIRKIFKK------QGVTAIFVThSREEAFAFADKMAVMNHGVIEQYGTASELY-YRPSskFVADFLGGGSY 242
Cdd:cd03291  192 ------VFTEKEIFEScvcklmANKTRILVT-SKMEHLKKADKILILHEGSSYFYGTFSELQsLRPD--FSSKLMGYDTF 262

PRK10762

D-ribose transporter ATP binding protein; Provisional

1-213

6.63e-18

D-ribose transporter ATP binding protein; Provisional

Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 84.28 E-value: 6.63e-18

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099586   1 MSCALSIQNLTCQYDTQTVLESLSLNVEHGEIVCLLGASGCGKTTLLKAIAGLLPLSSGIMSLNG--MTIDDGKhwlAPE 78
Cdd:PRK10762   1 MQALLQLKGIDKAFPGVKALSGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSILYLGkeVTFNGPK---SSQ 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099586  79 QRNIGMIFQDYALFPHLTVAENI--------AFGL---RQMAAEERHLqvQQMLELVHLSgfgDRYPHQLSGGQQQRVAI 147
Cdd:PRK10762  78 EAGIGIIHQELNLIPQLTIAENIflgrefvnRFGRidwKKMYAEADKL--LARLNLRFSS---DKLVGELSIGEQQMVEI 152

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 521099586 148 ARSLAYKPDLLLLDEP---FSNIDTQVRHDLIGEIRkifkKQGVTAIFVTHSREEAFAFADKMAVMNHG 213
Cdd:PRK10762 153 AKVLSFESKVIIMDEPtdaLTDTETESLFRVIRELK----SQGRGIVYISHRLKEIFEICDDVTVFRDG 217

hmuV

PRK13547

heme ABC transporter ATP-binding protein;

5-220

7.19e-18

heme ABC transporter ATP-binding protein;

Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 82.18 E-value: 7.19e-18

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099586   5 LSIQNLTCQYDTQTVLESLSLNVEHGEIVCLLGASGCGKTTLLKAIAGLLPLS--------SGIMSLNG---MTIDDGKh 73
Cdd:PRK13547   2 LTADHLHVARRHRAILRDLSLRIEPGRVTALLGRNGAGKSTLLKALAGDLTGGgaprgarvTGDVTLNGeplAAIDAPR- 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099586  74 wLA------PEQRNIGMIFQDYAL-----FPHLTVAENIAFGLRQMAAeerhlqvqQMLELVHLSGFGDRYPHQLSGGQQ 142
Cdd:PRK13547  81 -LArlravlPQAAQPAFAFSAREIvllgrYPHARRAGALTHRDGEIAW--------QALALAGATALVGRDVTTLSGGEL 151

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099586 143 QRVAIARSLAY---------KPDLLLLDEPFSNIDTQVRHDLIGEIRKIFKKQGVTAIFVTHSREEAFAFADKMAVMNHG 213
Cdd:PRK13547 152 ARVQFARVLAQlwpphdaaqPPRYLLLDEPTAALDLAHQHRLLDTVRRLARDWNLGVLAIVHDPNLAARHADRIAMLADG 231


                 ....*..
gi 521099586 214 VIEQYGT 220
Cdd:PRK13547 232 AIVAHGA 238

znuC

PRK09544

high-affinity zinc transporter ATPase; Reviewed

1-212

1.85e-17

high-affinity zinc transporter ATPase; Reviewed

Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 80.54 E-value: 1.85e-17

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099586   1 MSCALSIQNLTCQYDTQTVLESLSLNVEHGEIVCLLGASGCGKTTLLKAIAGLLPLSSGIMslngmtiddgkhwLAPEQR 80
Cdd:PRK09544   1 MTSLVSLENVSVSFGQRRVLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVI-------------KRNGKL 67

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099586  81 NIGMIFQDYALFPHLTVAENIAFGLRQMAAEERHLQVQQMLELVHLSgfgdRYPHQ-LSGGQQQRVAIARSLAYKPDLLL 159
Cdd:PRK09544  68 RIGYVPQKLYLDTTLPLTVNRFLRLRPGTKKEDILPALKRVQAGHLI----DAPMQkLSGGETQRVLLARALLNRPQLLV 143

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 521099586 160 LDEPFSNIDT--QVR-HDLIGEIRKIFkkqGVTAIFVTHSREEAFAFADKMAVMNH 212
Cdd:PRK09544 144 LDEPTQGVDVngQVAlYDLIDQLRREL---DCAVLMVSHDLHLVMAKTDEVLCLNH 196

SufC

COG0396

Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, ...

5-195

2.17e-17

Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, chaperones];

Pssm-ID: 440165 [Multi-domain] Cd Length: 245 Bit Score: 80.11 E-value: 2.17e-17

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099586   5 LSIQNLTCQYDTQTVLESLSLNVEHGEIVCLLGASGCGKTTLLKAIAGLlP---LSSGIMSLNGMTIDDgkhwLAPEQR- 80
Cdd:COG0396    1 LEIKNLHVSVEGKEILKGVNLTIKPGEVHAIMGPNGSGKSTLAKVLMGH-PkyeVTSGSILLDGEDILE----LSPDERa 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099586  81 --NIGMIFQDYALFPHLTV------AENiAFGLRQMAAEERHLQVQQMLELVHLS-GFGDRYPHQ-LSGGQQQRVAIARS 150
Cdd:COG0396   76 raGIFLAFQYPVEIPGVSVsnflrtALN-ARRGEELSAREFLKLLKEKMKELGLDeDFLDRYVNEgFSGGEKKRNEILQM 154

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 521099586 151 LAYKPDLLLLDEPFSNIDtqvrhdlIGEIRKI------FKKQGVTAIFVTH 195
Cdd:COG0396  155 LLLEPKLAILDETDSGLD-------IDALRIVaegvnkLRSPDRGILIITH 198

PRK15439

autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional

23-215

5.49e-17

autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional

Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 81.64 E-value: 5.49e-17

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099586  23 LSLNVEHGEIVCLLGASGCGKTTLLKAIAGLLPLSSGIMSLNGMTIDDgkhwLAPEQR-NIGMIF-----QDYALFPHLT 96
Cdd:PRK15439 282 ISLEVRAGEILGLAGVVGAGRTELAETLYGLRPARGGRIMLNGKEINA----LSTAQRlARGLVYlpedrQSSGLYLDAP 357

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099586  97 VAENIA------FGLRQMAAEERhlqvqQMLELVHLSgFGDRYPH------QLSGGQQQRVAIARSLAYKPDLLLLDEPF 164
Cdd:PRK15439 358 LAWNVCalthnrRGFWIKPAREN-----AVLERYRRA-LNIKFNHaeqaarTLSGGNQQKVLIAKCLEASPQLLIVDEPT 431

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 521099586 165 SNIDTQVRHDLIGEIRKIfKKQGVTAIFVTHSREEAFAFADKMAVMNHGVI 215
Cdd:PRK15439 432 RGVDVSARNDIYQLIRSI-AAQNVAVLFISSDLEEIEQMADRVLVMHQGEI 481

araG

PRK11288

L-arabinose ABC transporter ATP-binding protein AraG;

1-213

5.67e-17

L-arabinose ABC transporter ATP-binding protein AraG;

Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 81.50 E-value: 5.67e-17

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099586   1 MSCALSIQNLTCQYDTQTVLESLSLNVEHGEIVCLLGASGCGKTTLLKAIAGLLPLSSGIMSLNGMT---------IDDG 71
Cdd:PRK11288   1 SSPYLSFDGIGKTFPGVKALDDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSILIDGQEmrfasttaaLAAG 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099586  72 khwlapeqrnIGMIFQDYALFPHLTVAENIAFGlrQMAA-----EERHLQVQQMLELVHLsgfGDRY-PHQ----LSGGQ 141
Cdd:PRK11288  81 ----------VAIIYQELHLVPEMTVAENLYLG--QLPHkggivNRRLLNYEAREQLEHL---GVDIdPDTplkyLSIGQ 145

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 521099586 142 QQRVAIARSLAYKPDLLLLDEPFSNI---DTQVRHDLIGEIRkifkKQGVTAIFVTHSREEAFAFADKMAVMNHG 213
Cdd:PRK11288 146 RQMVEIAKALARNARVIAFDEPTSSLsarEIEQLFRVIRELR----AEGRVILYVSHRMEEIFALCDAITVFKDG 216

CFTR_protein

TIGR01271

cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ...

19-242

6.65e-17

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: 81.88 E-value: 6.65e-17

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099586    19 VLESLSLNVEHGEIVCLLGASGCGKTTLLKAIAGLLPLSSGIMSLNG-MTIDDGKHWLAPEqrnigmifqdyalfphlTV 97
Cdd:TIGR01271  441 VLKNISFKLEKGQLLAVAGSTGSGKSSLLMMIMGELEPSEGKIKHSGrISFSPQTSWIMPG-----------------TI 503

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099586    98 AENIAFGLRQmaAEERHLQVQ---QMLELVHLSGFGDRYPH-----QLSGGQQQRVAIARSLAYKPDLLLLDEPFSNIDT 169
Cdd:TIGR01271  504 KDNIIFGLSY--DEYRYTSVIkacQLEEDIALFPEKDKTVLgeggiTLSGGQRARISLARAVYKDADLYLLDSPFTHLDV 581

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 521099586   170 QVRHDLIGE-IRKIFKKQgvTAIFVThSREEAFAFADKMAVMNHGVIEQYGTASELY-YRPSskFVADFLGGGSY 242
Cdd:TIGR01271  582 VTEKEIFEScLCKLMSNK--TRILVT-SKLEHLKKADKILLLHEGVCYFYGTFSELQaKRPD--FSSLLLGLEAF 651

PRK10790

SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;

1-224

6.95e-17

SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;

Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 81.69 E-value: 6.95e-17

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099586   1 MSCALSIQNLTCQY-DTQTVLESLSLNVEHGEIVCLLGASGCGKTTLLKAIAGLLPLSSGIMSLNGMTIDDGKHwlAPEQ 79
Cdd:PRK10790 337 QSGRIDIDNVSFAYrDDNLVLQNINLSVPSRGFVALVGHTGSGKSTLASLLMGYYPLTEGEIRLDGRPLSSLSH--SVLR 414

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099586  80 RNIGMIFQDYALFPHlTVAENIAFGlRQMAAEerhlQVQQMLELVHLSGFGDRYP-----------HQLSGGQQQRVAIA 148
Cdd:PRK10790 415 QGVAMVQQDPVVLAD-TFLANVTLG-RDISEE----QVWQALETVQLAELARSLPdglytplgeqgNNLSVGQKQLLALA 488

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 521099586 149 RSLAYKPDLLLLDEPFSNIDTQVRHDLIGEIRKIfkKQGVTAIFVTHsREEAFAFADKMAVMNHGVIEQYGTASEL 224
Cdd:PRK10790 489 RVLVQTPQILILDEATANIDSGTEQAIQQALAAV--REHTTLVVIAH-RLSTIVEADTILVLHRGQAVEQGTHQQL 561

PRK15093

peptide ABC transporter ATP-binding protein SapD;

5-228

1.35e-16

peptide ABC transporter ATP-binding protein SapD;

Pssm-ID: 185049 [Multi-domain] Cd Length: 330 Bit Score: 79.46 E-value: 1.35e-16

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099586   5 LSIQNLTCQYDTQ----TVLESLSLNVEHGEIVCLLGASGCGKTTLLKAIAGLLPLSSGIMSlNGMTIDDGKHW-LAPEQ 79
Cdd:PRK15093   4 LDIRNLTIEFKTSdgwvKAVDRVSMTLTEGEIRGLVGESGSGKSLIAKAICGVTKDNWRVTA-DRMRFDDIDLLrLSPRE 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099586  80 R------NIGMIFQDyalfPH--LTVAENIAFGLRQMAA---------EERHLQVQQMLELVHLSGFGDR------YPHQ 136
Cdd:PRK15093  83 RrklvghNVSMIFQE----PQscLDPSERVGRQLMQNIPgwtykgrwwQRFGWRKRRAIELLHRVGIKDHkdamrsFPYE 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099586 137 LSGGQQQRVAIARSLAYKPDLLLLDEPFSNIDTQVRHDLIGEIRKIFKKQGVTAIFVTHSREEAFAFADKMAVMNHGVIE 216
Cdd:PRK15093 159 LTEGECQKVMIAIALANQPRLLIADEPTNAMEPTTQAQIFRLLTRLNQNNNTTILLISHDLQMLSQWADKINVLYCGQTV 238

                        250
                 ....*....|..
gi 521099586 217 QYGTASELYYRP 228
Cdd:PRK15093 239 ETAPSKELVTTP 250

PRK10789

SmdA family multidrug ABC transporter permease/ATP-binding protein;

4-228

2.06e-16

SmdA family multidrug ABC transporter permease/ATP-binding protein;

Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 80.14 E-value: 2.06e-16

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099586   4 ALSIQNLTCQYDTQTVLESLSLNVEHGEIVCLLGASGCGKTTLLKAIAGLLPLSSGIMSLNGMTIDDGK--HWlapeQRN 81
Cdd:PRK10789 315 DVNIRQFTYPQTDHPALENVNFTLKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGDIRFHDIPLTKLQldSW----RSR 390

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099586  82 IGMIFQDYALFPHlTVAENIAFGlRQMAAEERHLQVQQmLELVH----------LSGFGDRyPHQLSGGQQQRVAIARSL 151
Cdd:PRK10789 391 LAVVSQTPFLFSD-TVANNIALG-RPDATQQEIEHVAR-LASVHddilrlpqgyDTEVGER-GVMLSGGQKQRISIARAL 466

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 521099586 152 AYKPDLLLLDEPFSNIDTQVRHDLIGEIRKIfkKQGVTAIFVTHsREEAFAFADKMAVMNHGVIEQYGTASELYYRP 228
Cdd:PRK10789 467 LLNAEILILDDALSAVDGRTEHQILHNLRQW--GEGRTVIISAH-RLSALTEASEILVMQHGHIAQRGNHDQLAQQS 540

PLN03232

ABC transporter C family member; Provisional

4-225

2.13e-16

ABC transporter C family member; Provisional

Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 80.41 E-value: 2.13e-16

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099586    4 ALSIQNLTCQYDTQT---VLESLSLNVEHGEIVCLLGASGCGKTTLLKAIAGLLPLSSgimslNGMTIDDGKHWLAPEqr 80
Cdd:PLN03232  614 AISIKNGYFSWDSKTskpTLSDINLEIPVGSLVAIVGGTGEGKTSLISAMLGELSHAE-----TSSVVIRGSVAYVPQ-- 686

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099586   81 nIGMIFqdyalfpHLTVAENIAFGLRqmAAEERHLQVQQMLELVH---------LSGFGDRYPHqLSGGQQQRVAIARSL 151
Cdd:PLN03232  687 -VSWIF-------NATVRENILFGSD--FESERYWRAIDVTALQHdldllpgrdLTEIGERGVN-ISGGQKQRVSMARAV 755

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 521099586  152 AYKPDLLLLDEPFSNIDTQVRHDLIGEIRKiFKKQGVTAIFVThSREEAFAFADKMAVMNHGVIEQYGTASELY 225
Cdd:PLN03232  756 YSNSDIYIFDDPLSALDAHVAHQVFDSCMK-DELKGKTRVLVT-NQLHFLPLMDRIILVSEGMIKEEGTFAELS 827

PRK03695

vitamin B12-transporter ATPase; Provisional

20-223

2.42e-16

vitamin B12-transporter ATPase; Provisional

Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 77.28 E-value: 2.42e-16

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099586  20 LESLSLNVEHGEIVCLLGASGCGKTTLLKAIAGLLPlSSGIMSLNGMTIDDGKH--------WLAPEQRN-IGM-IFQDY 89
Cdd:PRK03695  12 LGPLSAEVRAGEILHLVGPNGAGKSTLLARMAGLLP-GSGSIQFAGQPLEAWSAaelarhraYLSQQQTPpFAMpVFQYL 90

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099586  90 ALF-PHLTVAENIAFGLRQMAaeeRHLQVQQMLElvhlsgfgdRYPHQLSGGQQQRVAIARS-LAYKPD------LLLLD 161
Cdd:PRK03695  91 TLHqPDKTRTEAVASALNEVA---EALGLDDKLG---------RSVNQLSGGEWQRVRLAAVvLQVWPDinpagqLLLLD 158

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 521099586 162 EPFSNIDT--QVRHDLIgeIRKiFKKQGVTAIFVTHSREEAFAFADKMAVMNHGVIEQYGTASE 223
Cdd:PRK03695 159 EPMNSLDVaqQAALDRL--LSE-LCQQGIAVVMSSHDLNHTLRHADRVWLLKQGKLLASGRRDE 219

PRK13543

heme ABC exporter ATP-binding protein CcmA;

5-180

3.73e-16

heme ABC exporter ATP-binding protein CcmA;

Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 76.04 E-value: 3.73e-16

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099586   5 LSIQNLTCQYDTQTVLESLSLNVEHGEIVCLLGASGCGKTTLLKAIAGLLPLSSGIMSLNGMTIDDGKhwlapEQRNIGM 84
Cdd:PRK13543  12 LAAHALAFSRNEEPVFGPLDFHVDAGEALLVQGDNGAGKTTLLRVLAGLLHVESGQIQIDGKTATRGD-----RSRFMAY 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099586  85 IFQDYALFPHLTVAENIAFglrQMAAEERHlqVQQM----LELVHLSGFGDRYPHQLSGGQQQRVAIARSLAYKPDLLLL 160
Cdd:PRK13543  87 LGHLPGLKADLSTLENLHF---LCGLHGRR--AKQMpgsaLAIVGLAGYEDTLVRQLSAGQKKRLALARLWLSPAPLWLL 161

                        170       180
                 ....*....|....*....|....
gi 521099586 161 DEPFSNID----TQVRHDLIGEIR 180
Cdd:PRK13543 162 DEPYANLDlegiTLVNRMISAHLR 185

PvdE

COG4615

ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ...

23-216

5.42e-16

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: 78.69 E-value: 5.42e-16

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099586  23 LSLNVEHGEIVCLLGASGCGKTTLLKAIAGLLPLSSGIMSLNGMTIDDgkHWLAPEQRNIGMIFQDYALFPHLtvaenia 102
Cdd:COG4615  351 IDLTIRRGELVFIVGGNGSGKSTLAKLLTGLYRPESGEILLDGQPVTA--DNREAYRQLFSAVFSDFHLFDRL------- 421

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099586 103 FGLRQMAAEERhlqVQQMLELVHLSG--------FGDRyphQLSGGQQQRVAIARSLAYKPDLLLLDEPFSNIDTQVR-- 172
Cdd:COG4615  422 LGLDGEADPAR---ARELLERLELDHkvsvedgrFSTT---DLSQGQRKRLALLVALLEDRPILVFDEWAADQDPEFRrv 495

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*.
gi 521099586 173 --HDLIGEirkiFKKQGVTAIFVTHSrEEAFAFADKMAVMNHGVIE 216
Cdd:COG4615  496 fyTELLPE----LKARGKTVIAISHD-DRYFDLADRVLKMDYGKLV 536

araG

PRK11288

L-arabinose ABC transporter ATP-binding protein AraG;

21-215

8.67e-16

L-arabinose ABC transporter ATP-binding protein AraG;

Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 78.03 E-value: 8.67e-16

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099586  21 ESLSLNVEHGEIVCLLGASGCGKTTLLKAIAGLLPLSSGIMSLNG--MTIDDGKH------WLAPEQRNigmifQDyALF 92
Cdd:PRK11288 270 EPISFSVRAGEIVGLFGLVGAGRSELMKLLYGATRRTAGQVYLDGkpIDIRSPRDairagiMLCPEDRK-----AE-GII 343

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099586  93 PHLTVAENIAFGLRQmaaeerhlqvqqmlelvHLSGFG------------DRY----------PHQ----LSGGQQQRVA 146
Cdd:PRK11288 344 PVHSVADNINISARR-----------------HHLRAGclinnrweaenaDRFirslniktpsREQlimnLSGGNQQKAI 406

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 521099586 147 IARSLAYKPDLLLLDEPFSNIDTQVRHdligEIRKIF---KKQGVTAIFVTHSREEAFAFADKMAVMNHGVI 215
Cdd:PRK11288 407 LGRWLSEDMKVILLDEPTRGIDVGAKH----EIYNVIyelAAQGVAVLFVSSDLPEVLGVADRIVVMREGRI 474

PRK11147

ABC transporter ATPase component; Reviewed

5-208

9.26e-16

ABC transporter ATPase component; Reviewed

Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 78.07 E-value: 9.26e-16

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099586   5 LSIQNLTCQYDTQTVLESLSLNVEHGEIVCLLGASGCGKTTLLKAIAGLLPLssgimslngmtiDDGKhwLAPEQ----- 79
Cdd:PRK11147   4 ISIHGAWLSFSDAPLLDNAELHIEDNERVCLVGRNGAGKSTLMKILNGEVLL------------DDGR--IIYEQdliva 69

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099586  80 -------RNI-GMIFqDYalfphltVAENIAFG----------LRQMAAE--ERHL----QVQQMLElvHLSG--FGDRY 133
Cdd:PRK11147  70 rlqqdppRNVeGTVY-DF-------VAEGIEEQaeylkryhdiSHLVETDpsEKNLnelaKLQEQLD--HHNLwqLENRI 139

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099586 134 ----------PHQ----LSGGQQQRVAIARSLAYKPDLLLLDEPFSNIDTqvrhDLIGEIRKIFKKQGVTAIFVTHSRee 199
Cdd:PRK11147 140 nevlaqlgldPDAalssLSGGWLRKAALGRALVSNPDVLLLDEPTNHLDI----ETIEWLEGFLKTFQGSIIFISHDR-- 213


                 ....*....
gi 521099586 200 afAFADKMA 208
Cdd:PRK11147 214 --SFIRNMA 220

ABCC_SUR1_N

cd03290

ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ...

20-213

1.46e-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: 74.67 E-value: 1.46e-15

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099586  20 LESLSLNVEHGEIVCLLGASGCGKTTLLKAIAGLLPLSSGIMSLNGmTIDDGKHWLAPEQRNIGMIfqDYA----LFPHL 95
Cdd:cd03290   17 LSNINIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWSN-KNESEPSFEATRSRNRYSV--AYAaqkpWLLNA 93

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099586  96 TVAENIAFGlrQMAAEERHLQVQQMLEL---VHLSGFGDRYPH-----QLSGGQQQRVAIARSLAYKPDLLLLDEPFSNI 167
Cdd:cd03290   94 TVEENITFG--SPFNKQRYKAVTDACSLqpdIDLLPFGDQTEIgergiNLSGGQRQRICVARALYQNTNIVFLDDPFSAL 171

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 521099586 168 DTQVRHDLIGE-IRKIFKKQGVTAIFVTHsREEAFAFADKMAVMNHG 213
Cdd:cd03290  172 DIHLSDHLMQEgILKFLQDDKRTLVLVTH-KLQYLPHADWIIAMKDG 217

MRP_assoc_pro

TIGR00957

multi drug resistance-associated protein (MRP); This model describes multi drug ...

4-237

1.87e-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: 77.68 E-value: 1.87e-15

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099586     4 ALSIQNLTCQY--DTQTVLESLSLNVEHGEIVCLLGASGCGKTTLLKAIAGLLPLSSGIMSLNGMTIddgkhwLAPEQrn 81
Cdd:TIGR00957  636 SITVHNATFTWarDLPPTLNGITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVHMKGSVA------YVPQQ-- 707

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099586    82 igmifqdyALFPHLTVAENIAFGlrQMAAEERHLQVQQ----MLELVHLSGfGDRYP-----HQLSGGQQQRVAIARSLA 152
Cdd:TIGR00957  708 --------AWIQNDSLRENILFG--KALNEKYYQQVLEacalLPDLEILPS-GDRTEigekgVNLSGGQKQRVSLARAVY 776

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099586   153 YKPDLLLLDEPFSNIDTQVRhdligeiRKIFKK--------QGVTAIFVTHSReEAFAFADKMAVMNHGVIEQYGTASEL 224
Cdd:TIGR00957  777 SNADIYLFDDPLSAVDAHVG-------KHIFEHvigpegvlKNKTRILVTHGI-SYLPQVDVIIVMSGGKISEMGSYQEL 848

                          250
                   ....*....|...
gi 521099586   225 YYRPSSkfVADFL 237
Cdd:TIGR00957  849 LQRDGA--FAEFL 859

PLN03130

ABC transporter C family member; Provisional

4-224

2.32e-15

ABC transporter C family member; Provisional

Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 77.47 E-value: 2.32e-15

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099586    4 ALSIQNLTCQYDT---QTVLESLSLNVEHGEIVCLLGASGCGKTTLLKAIAGLLPLSSGimslnGMTIDDGKHWLAPEqr 80
Cdd:PLN03130  614 AISIKNGYFSWDSkaeRPTLSNINLDVPVGSLVAIVGSTGEGKTSLISAMLGELPPRSD-----ASVVIRGTVAYVPQ-- 686

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099586   81 nIGMIFqdyalfpHLTVAENIAFGLRQMAAE-ERHLQV---QQMLELV---HLSGFGDRYPHqLSGGQQQRVAIARSLAY 153
Cdd:PLN03130  687 -VSWIF-------NATVRDNILFGSPFDPERyERAIDVtalQHDLDLLpggDLTEIGERGVN-ISGGQKQRVSMARAVYS 757

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 521099586  154 KPDLLLLDEPFSNIDTQVRhdligeiRKIFKK------QGVTAIFVThSREEAFAFADKMAVMNHGVIEQYGTASEL 224
Cdd:PLN03130  758 NSDVYIFDDPLSALDAHVG-------RQVFDKcikdelRGKTRVLVT-NQLHFLSQVDRIILVHEGMIKEEGTYEEL 826

PRK10522

multidrug transporter membrane component/ATP-binding component; Provisional

5-215

5.44e-15

multidrug transporter membrane component/ATP-binding component; Provisional

Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 75.78 E-value: 5.44e-15

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099586   5 LSIQNLTCQYDTQTV-LESLSLNVEHGEIVCLLGASGCGKTTLLKAIAGLLPLSSGIMSLNGMTIDDGKhwLAPEQRNIG 83
Cdd:PRK10522 323 LELRNVTFAYQDNGFsVGPINLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKPVTAEQ--PEDYRKLFS 400

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099586  84 MIFQDYALFPHLTVAENIAFGLRQMAAEERHLQVQQMLELVHlsgfGDRYPHQLSGGQQQRVAIARSLAYKPDLLLLDEP 163
Cdd:PRK10522 401 AVFTDFHLFDQLLGPEGKPANPALVEKWLERLKMAHKLELED----GRISNLKLSKGQKKRLALLLALAEERDILLLDEW 476

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 521099586 164 FSNIDTQVRHDLIGEIRKIFKKQGVTAIFVTHSrEEAFAFADKMAVMNHGVI 215
Cdd:PRK10522 477 AADQDPHFRREFYQVLLPLLQEMGKTIFAISHD-DHYFIHADRLLEMRNGQL 527

PTZ00243

ABC transporter; Provisional

19-232

1.89e-14

ABC transporter; Provisional

Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 74.43 E-value: 1.89e-14

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099586   19 VLESLSLNVEHGEIVCLLGASGCGKTTLLKAIAGLLPLSSGIMSLNGMTIddGKHWLAPEQRNIGMIFQDYALFPHlTVA 98
Cdd:PTZ00243 1325 VLRGVSFRIAPREKVGIVGRTGSGKSTLLLTFMRMVEVCGGEIRVNGREI--GAYGLRELRRQFSMIPQDPVLFDG-TVR 1401

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099586   99 ENIAFGLRQMAAEerhlqVQQMLELVHLSGF---------------GDRYphqlSGGQQQRVAIARSLAYK-PDLLLLDE 162
Cdd:PTZ00243 1402 QNVDPFLEASSAE-----VWAALELVGLRERvasesegidsrvlegGSNY----SVGQRQLMCMARALLKKgSGFILMDE 1472

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099586  163 PFSNIDTQVRHDLIGEIRKIFkkQGVTAIFVTHsREEAFAFADKMAVMNHGVIEQYGTASELYYRPSSKF 232
Cdd:PTZ00243 1473 ATANIDPALDRQIQATVMSAF--SAYTVITIAH-RLHTVAQYDKIIVMDHGAVAEMGSPRELVMNRQSIF 1539

3a01205

TIGR00956

Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]

27-182

2.86e-14

Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]

Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 73.99 E-value: 2.86e-14

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099586    27 VEHGEIVCLLGASGCGKTTLLKAIAGLLP---LSSGIMSLNGMTIDdgkhwlAPEQRNIGMIFQDYALFPHLTVAENIAF 103
Cdd:TIGR00956  786 VKPGTLTALMGASGAGKTTLLNVLAERVTtgvITGGDRLVNGRPLD------SSFQRSIGYVQQQDLHLPTSTVRESLRF 859

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099586   104 G--LRQMAA---EERHLQVQQMLELVHLSGFGDRY---PHQ-LSGGQQQRVAIARSLAYKPDLLL-LDEPFSNIDTQVRH 173
Cdd:TIGR00956  860 SayLRQPKSvskSEKMEYVEEVIKLLEMESYADAVvgvPGEgLNVEQRKRLTIGVELVAKPKLLLfLDEPTSGLDSQTAW 939


                   ....*....
gi 521099586   174 DLIGEIRKI 182
Cdd:TIGR00956  940 SICKLMRKL 948

PRK13546

teichoic acids export ABC transporter ATP-binding subunit TagH;

1-236

2.93e-14

teichoic acids export ABC transporter ATP-binding subunit TagH;

Pssm-ID: 184131 [Multi-domain] Cd Length: 264 Bit Score: 71.77 E-value: 2.93e-14

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099586   1 MSCALSIQNLTCQY--------------------DTQTVLESLSLNVEHGEIVCLLGASGCGKTTLLKAIAGLLPLSSGI 60
Cdd:PRK13546   1 MNVSVNIKNVTKEYriyrtnkermkdalipkhknKTFFALDDISLKAYEGDVIGLVGINGSGKSTLSNIIGGSLSPTVGK 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099586  61 MSLNGmtiddgkhwlapeqrNIGMIFQDYALFPHLTVAENIAFGLRQMAAEERHLQvQQMLELVHLSGFGDrYPHQ---- 136
Cdd:PRK13546  81 VDRNG---------------EVSVIAISAGLSGQLTGIENIEFKMLCMGFKRKEIK-AMTPKIIEFSELGE-FIYQpvkk 143

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099586 137 LSGGQQQRVAIARSLAYKPDLLLLDEPFSNID---TQVRHDLIGEirkiFKKQGVTAIFVTHSREEAFAFADKMAVMNHG 213
Cdd:PRK13546 144 YSSGMRAKLGFSINITVNPDILVIDEALSVGDqtfAQKCLDKIYE----FKEQNKTIFFVSHNLGQVRQFCTKIAWIEGG 219

                        250       260
                 ....*....|....*....|...
gi 521099586 214 VIEQYGTASELYYRpSSKFVADF 236
Cdd:PRK13546 220 KLKDYGELDDVLPK-YEAFLNDF 241

MRP_assoc_pro

TIGR00957

multi drug resistance-associated protein (MRP); This model describes multi drug ...

15-224

3.93e-14

Pssm-ID: 188098 [Multi-domain] Cd Length: 1522 Bit Score: 73.83 E-value: 3.93e-14

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099586    15 DTQTVLESLSLNVEHGEIVCLLGASGCGKTTLLKAIAGLLPLSSGIMSLNGMTIDD-GKHWLapeQRNIGMIFQDYALFP 93
Cdd:TIGR00957 1297 DLDLVLRHINVTIHGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGLNIAKiGLHDL---RFKITIIPQDPVLFS 1373

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099586    94 HlTVAENI-AFGlrQMAAEErhlqVQQMLELVHLSGFGDRYP----HQ-------LSGGQQQRVAIARSLAYKPDLLLLD 161
Cdd:TIGR00957 1374 G-SLRMNLdPFS--QYSDEE----VWWALELAHLKTFVSALPdkldHEcaeggenLSVGQRQLVCLARALLRKTKILVLD 1446

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 521099586   162 EPFSNIDTQVRHDLIGEIRKIFkkQGVTAIFVTHSREEAFAFAdKMAVMNHGVIEQYGTASEL 224
Cdd:TIGR00957 1447 EATAAVDLETDNLIQSTIRTQF--EDCTVLTIAHRLNTIMDYT-RVIVLDKGEVAEFGAPSNL 1506

3a01203

TIGR00954

Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ...

17-195

4.61e-14

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: 73.24 E-value: 4.61e-14

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099586   17 QTVLESLSLNVEHGEIVCLLGASGCGKTTLLKAIAGLLPLSSGImslngMTID-DGKHWLAPEQRNIGM-IFQDYALFPH 94
Cdd:TIGR00954 465 DVLIESLSFEVPSGNNLLICGPNGCGKSSLFRILGELWPVYGGR-----LTKPaKGKLFYVPQRPYMTLgTLRDQIIYPD 539

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099586   95 lTVAENIAFGLRQMAAEerhlqvqQMLELVHLSGFGDR---------YPHQLSGGQQQRVAIARSLAYKPDLLLLDEPFS 165
Cdd:TIGR00954 540 -SSEDMKRRGLSDKDLE-------QILDNVQLTHILEReggwsavqdWMDVLSGGEKQRIAMARLFYHKPQFAILDECTS 611

                         170       180       190
                  ....*....|....*....|....*....|
gi 521099586  166 NIDTQVRhdliGEIRKIFKKQGVTAIFVTH 195
Cdd:TIGR00954 612 AVSVDVE----GYMYRLCREFGITLFSVSH 637

ABCG_PDR_domain2

cd03232

Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ...

3-182

1.24e-13

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: 68.42 E-value: 1.24e-13

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099586   3 CALSIQNLTcqYDTQTVLESLSL------NVEHGEIVCLLGASGCGKTTLLKAIAG--LLPLSSGIMSLNGMTIDDGKhw 74
Cdd:cd03232    2 SVLTWKNLN--YTVPVKGGKRQLlnnisgYVKPGTLTALMGESGAGKTTLLDVLAGrkTAGVITGEILINGRPLDKNF-- 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099586  75 lapeQRNIGMIFQDYALFPHLTVAENIAFG--LRQMAAEERhlqvqqmlelvhlsgfgdryphqlsggqqQRVAIARSLA 152
Cdd:cd03232   78 ----QRSTGYVEQQDVHSPNLTVREALRFSalLRGLSVEQR-----------------------------KRLTIGVELA 124

                        170       180       190
                 ....*....|....*....|....*....|
gi 521099586 153 YKPDLLLLDEPFSNIDTQVRHDLIGEIRKI 182
Cdd:cd03232  125 AKPSILFLDEPTSGLDSQAAYNIVRFLKKL 154

Rli1

COG1245

Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ...

20-195

2.07e-13

Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ribosomal structure and biogenesis];

Pssm-ID: 440858 [Multi-domain] Cd Length: 592 Bit Score: 70.97 E-value: 2.07e-13

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099586  20 LESLSLNVEHG-----EIVCLLGASGCGKTTLLKAIAGLLPLSSGIMSLNgMTIDDGKHWLAPEQrnigmifqdyalfpH 94
Cdd:COG1245  351 YGGFSLEVEGGeiregEVLGIVGPNGIGKTTFAKILAGVLKPDEGEVDED-LKISYKPQYISPDY--------------D 415

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099586  95 LTVAENiafgLRQMAAEE-----------RHLQVQQMLelvhlsgfgDRYPHQLSGGQQQRVAIARSLAYKPDLLLLDEP 163
Cdd:COG1245  416 GTVEEF----LRSANTDDfgssyykteiiKPLGLEKLL---------DKNVKDLSGGELQRVAIAACLSRDADLYLLDEP 482

                        170       180       190
                 ....*....|....*....|....*....|..
gi 521099586 164 FSNIDTQVRHDLIGEIRKIFKKQGVTAIFVTH 195
Cdd:COG1245  483 SAHLDVEQRLAVAKAIRRFAENRGKTAMVVDH 514

PRK10938

putative molybdenum transport ATP-binding protein ModF; Provisional

9-200

2.83e-13

putative molybdenum transport ATP-binding protein ModF; Provisional

Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 70.43 E-value: 2.83e-13

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099586   9 NLTCQYDTQTVLESLSLNVEHGEIVCLLGASGCGKTTLLKAIAGLLPLS-SGIMSL------NGMTIDDGKhwlapeqRN 81
Cdd:PRK10938 265 NGVVSYNDRPILHNLSWQVNPGEHWQIVGPNGAGKSTLLSLITGDHPQGySNDLTLfgrrrgSGETIWDIK-------KH 337

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099586  82 IGM----IFQDYALFphlTVAENI-------AFGLRQMAAEERHLQVQQMLELVHLSGFGDRYP-HQLSGGQQQRVAIAR 149
Cdd:PRK10938 338 IGYvsssLHLDYRVS---TSVRNVilsgffdSIGIYQAVSDRQQKLAQQWLDILGIDKRTADAPfHSLSWGQQRLALIVR 414

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 521099586 150 SLAYKPDLLLLDEPFSNIDTQVRHdLIGEIRKIFKKQGVTA-IFVTHSREEA 200
Cdd:PRK10938 415 ALVKHPTLLILDEPLQGLDPLNRQ-LVRRFVDVLISEGETQlLFVSHHAEDA 465

xylG

TIGR02633

D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ...

5-213

2.88e-13

Pssm-ID: 131681 [Multi-domain] Cd Length: 500 Bit Score: 70.24 E-value: 2.88e-13

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099586    5 LSIQNLTCQYDTQT---VLESLSLNVEHGEIVCLLGASGCGKTTLLKAIAGLLPLS-SGIMSLNGMTIDDGKHWLAPEQr 80
Cdd:TIGR02633 258 LEARNLTCWDVINPhrkRVDDVSFSLRRGEILGVAGLVGAGRTELVQALFGAYPGKfEGNVFINGKPVDIRNPAQAIRA- 336

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099586   81 NIGMIFQD---YALFPHLTVAENIAF-------GLRQMAAEERHLQVQQMLELVHLSGFGDRYP-HQLSGGQQQRVAIAR 149
Cdd:TIGR02633 337 GIAMVPEDrkrHGIVPILGVGKNITLsvlksfcFKMRIDAAAELQIIGSAIQRLKVKTASPFLPiGRLSGGNQQKAVLAK 416

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 521099586  150 SLAYKPDLLLLDEPFSNIDTQVRHdligEIRKI---FKKQGVTAIFVTHSREEAFAFADKMAVMNHG 213
Cdd:TIGR02633 417 MLLTNPRVLILDEPTRGVDVGAKY----EIYKLinqLAQEGVAIIVVSSELAEVLGLSDRVLVIGEG 479

PRK13409

ribosome biogenesis/translation initiation ATPase RLI;

20-195

4.01e-13

ribosome biogenesis/translation initiation ATPase RLI;

Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 70.22 E-value: 4.01e-13

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099586  20 LESLSLNVEHGEI-----VCLLGASGCGKTTLLKAIAGLLPLSSGIMSLN--------------GMTIDDgkhWLapeqR 80
Cdd:PRK13409 350 LGDFSLEVEGGEIyegevIGIVGPNGIGKTTFAKLLAGVLKPDEGEVDPElkisykpqyikpdyDGTVED---LL----R 422

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099586  81 NIGMIFQDYALFPHLTvaeniafglrqmaaeeRHLQVQQMLelvhlsgfgDRYPHQLSGGQQQRVAIARSLAYKPDLLLL 160
Cdd:PRK13409 423 SITDDLGSSYYKSEII----------------KPLQLERLL---------DKNVKDLSGGELQRVAIAACLSRDADLYLL 477

                        170       180       190
                 ....*....|....*....|....*....|....*
gi 521099586 161 DEPFSNIDTQVRHDLIGEIRKIFKKQGVTAIFVTH 195
Cdd:PRK13409 478 DEPSAHLDVEQRLAVAKAIRRIAEEREATALVVDH 512

PRK13549

xylose transporter ATP-binding subunit; Provisional

5-215

6.32e-13

xylose transporter ATP-binding subunit; Provisional

Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 69.19 E-value: 6.32e-13

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099586   5 LSIQNLTCQYDTQT---VLESLSLNVEHGEIVCLLGASGCGKTTLLKAIAGLLP-LSSGIMSLNGMTIDDGkhwlAPEQ- 79
Cdd:PRK13549 260 LEVRNLTAWDPVNPhikRVDDVSFSLRRGEILGIAGLVGAGRTELVQCLFGAYPgRWEGEIFIDGKPVKIR----NPQQa 335

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099586  80 --RNIGMIFQD---YALFPHLTVAENIA---------FGLRQMAAEERHLQvQQMLEL-VHLSGfgdryPHQ----LSGG 140
Cdd:PRK13549 336 iaQGIAMVPEDrkrDGIVPVMGVGKNITlaaldrftgGSRIDDAAELKTIL-ESIQRLkVKTAS-----PELaiarLSGG 409

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 521099586 141 QQQRVAIARSLAYKPDLLLLDEPFSNIDTQVRHdligEIRKI---FKKQGVTAIFVTHSREEAFAFADKMAVMNHGVI 215
Cdd:PRK13549 410 NQQKAVLAKCLLLNPKILILDEPTRGIDVGAKY----EIYKLinqLVQQGVAIIVISSELPEVLGLSDRVLVMHEGKL 483

tagH

PRK13545

teichoic acids export protein ATP-binding subunit; Provisional

20-224

7.51e-13

teichoic acids export protein ATP-binding subunit; Provisional

Pssm-ID: 184130 [Multi-domain] Cd Length: 549 Bit Score: 69.15 E-value: 7.51e-13

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099586  20 LESLSLNVEHGEIVCLLGASGCGKTTLLKAIAGLLPLSSGIMSLNGmtiddgkhwlapeqrNIGMIFQDYALFPHLTVAE 99
Cdd:PRK13545  40 LNNISFEVPEGEIVGIIGLNGSGKSTLSNLIAGVTMPNKGTVDIKG---------------SAALIAISSGLNGQLTGIE 104

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099586 100 NIAFGLRQMAAEERHLQ--VQQMLELVHLSGFGDRYPHQLSGGQQQRVAIARSLAYKPDLLLLDEPFSNIDTQVRHDLIG 177
Cdd:PRK13545 105 NIELKGLMMGLTKEKIKeiIPEIIEFADIGKFIYQPVKTYSSGMKSRLGFAISVHINPDILVIDEALSVGDQTFTKKCLD 184

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 521099586 178 EIRKiFKKQGVTAIFVTHSREEAFAFADKMAVMNHGVIEQYGTASEL 224
Cdd:PRK13545 185 KMNE-FKEQGKTIFFISHSLSQVKSFCTKALWLHYGQVKEYGDIKEV 230

PLN03232

ABC transporter C family member; Provisional

19-232

1.38e-12

ABC transporter C family member; Provisional

Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 68.85 E-value: 1.38e-12

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099586   19 VLESLSLNVEHGEIVCLLGASGCGKTTLLKAIAGLLPLSSGIMSLNGmtIDDGKHWLAPEQRNIGMIFQDYALFPHlTVA 98
Cdd:PLN03232 1251 VLHGLSFFVSPSEKVGVVGRTGAGKSSMLNALFRIVELEKGRIMIDD--CDVAKFGLTDLRRVLSIIPQSPVLFSG-TVR 1327

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099586   99 ENIafglrQMAAEERHLQVQQMLELVHLSGFGDRYPHQL-----------SGGQQQRVAIARSLAYKPDLLLLDEPFSNI 167
Cdd:PLN03232 1328 FNI-----DPFSEHNDADLWEALERAHIKDVIDRNPFGLdaevseggenfSVGQRQLLSLARALLRRSKILVLDEATASV 1402

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 521099586  168 DTQVRHDLIGEIRKIFKKqgVTAIFVTHsREEAFAFADKMAVMNHGVIEQYGTASELYYRPSSKF 232
Cdd:PLN03232 1403 DVRTDSLIQRTIREEFKS--CTMLVIAH-RLNTIIDCDKILVLSSGQVLEYDSPQELLSRDTSAF 1464

PRK15064

ABC transporter ATP-binding protein; Provisional

4-198

2.86e-12

ABC transporter ATP-binding protein; Provisional

Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 67.22 E-value: 2.86e-12

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099586   4 ALSIQNLTCQYDTQTVLESLSLNVEHGEIVCLLGASGCGKTTLLKAIAGLLPLSSGIMslngmtiddgkHWlaPEQRNIG 83
Cdd:PRK15064 319 ALEVENLTKGFDNGPLFKNLNLLLEAGERLAIIGENGVGKTTLLRTLVGELEPDSGTV-----------KW--SENANIG 385

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099586  84 MIFQDYAL-FPH-LTVAENIAfGLRQMAAEErhLQVQQMLELVHLSgfGDRYPHQ---LSGGQQQRVAIARSLAYKPDLL 158
Cdd:PRK15064 386 YYAQDHAYdFENdLTLFDWMS-QWRQEGDDE--QAVRGTLGRLLFS--QDDIKKSvkvLSGGEKGRMLFGKLMMQKPNVL 460

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|
gi 521099586 159 LLDEPFSNIDTQVrhdlIGEIRKIFKKQGVTAIFVTHSRE 198
Cdd:PRK15064 461 VMDEPTNHMDMES----IESLNMALEKYEGTLIFVSHDRE 496

ABC_ABC_ChvD

TIGR03719

ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ...

19-197

3.21e-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: 67.27 E-value: 3.21e-12

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099586   19 VLESLSLNVEHGEIVCLLGASGCGKTTLLKAIAGllplssgimslngmtID---DGKHWLAPEqRNIGMIFQDYALFPHL 95
Cdd:TIGR03719  20 ILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAG---------------VDkdfNGEARPQPG-IKVGYLPQEPQLDPTK 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099586   96 TVAENIAFGLR------------------------QMAAEERHLQ----------VQQMLELVHLS---GFGDRYPHQLS 138
Cdd:TIGR03719  84 TVRENVEEGVAeikdaldrfneisakyaepdadfdKLAAEQAELQeiidaadawdLDSQLEIAMDAlrcPPWDADVTKLS 163

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 521099586  139 GGQQQRVAIARSLAYKPDLLLLDEPFSNIDT-------QVRHDLIGeirkifkkqgvTAIFVTHSR 197
Cdd:TIGR03719 164 GGERRRVALCRLLLSKPDMLLLDEPTNHLDAesvawleRHLQEYPG-----------TVVAVTHDR 218

PTZ00265

multidrug resistance protein (mdr1); Provisional

57-224

3.37e-12

multidrug resistance protein (mdr1); Provisional

Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 67.75 E-value: 3.37e-12

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099586   57 SSGIMSLNGMTIDDgkhWLAPEQRNIGMIFQDYALFPHLTVAENIAFGlRQMAAEErhlQVQQMLELVHLSGFGDRYPHQ 136
Cdd:PTZ00265 1275 NSGKILLDGVDICD---YNLKDLRNLFSIVSQEPMLFNMSIYENIKFG-KEDATRE---DVKRACKFAAIDEFIESLPNK 1347

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099586  137 -----------LSGGQQQRVAIARSLAYKPDLLLLDEPFSNIDTQVRHDLIGEIRKIFKKQGVTAIFVTHsREEAFAFAD 205
Cdd:PTZ00265 1348 ydtnvgpygksLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDIKDKADKTIITIAH-RIASIKRSD 1426

                         170       180
                  ....*....|....*....|....
gi 521099586  206 KMAVMNH-----GVIEQYGTASEL 224
Cdd:PTZ00265 1427 KIVVFNNpdrtgSFVQAHGTHEEL 1450

ABC_RNaseL_inhibitor_domain2

cd03237

The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ...

20-222

4.77e-12

The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI), is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI's are not transport proteins and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLI's have an N-terminal Fe-S domain and two nucleotide-binding domains which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity of more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.

Pssm-ID: 213204 [Multi-domain] Cd Length: 246 Bit Score: 65.12 E-value: 4.77e-12

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099586  20 LESLSLNVEHG-----EIVCLLGASGCGKTTLLKAIAGLLPLSSGIMSLNGMTIDDGKHWLAPEQRniGMIfqDYALFPH 94
Cdd:cd03237   10 LGEFTLEVEGGsisesEVIGILGPNGIGKTTFIKMLAGVLKPDEGDIEIELDTVSYKPQYIKADYE--GTV--RDLLSSI 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099586  95 LTVAENIAFGLRQMAaeeRHLQVQQMLelvhlsgfgDRYPHQLSGGQQQRVAIARSLAYKPDLLLLDEPFSNIDTQVRHD 174
Cdd:cd03237   86 TKDFYTHPYFKTEIA---KPLQIEQIL---------DREVPELSGGELQRVAIAACLSKDADIYLLDEPSAYLDVEQRLM 153

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*...
gi 521099586 175 LIGEIRKIFKKQGVTAIFVTHSREEAFAFADKMAVMNhGVIEQYGTAS 222
Cdd:cd03237  154 ASKVIRRFAENNEKTAFVVEHDIIMIDYLADRLIVFE-GEPSVNGVAN 200

CFTR_protein

TIGR01271

cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ...

5-224

4.90e-12

Pssm-ID: 273530 [Multi-domain] Cd Length: 1490 Bit Score: 67.24 E-value: 4.90e-12

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099586     5 LSIQNLTCQY--DTQTVLESLSLNVEHGEIVCLLGASGCGKTTLLKAIAGLLplssgimSLNGMTIDDGKHW----LAPE 78
Cdd:TIGR01271 1218 MDVQGLTAKYteAGRAVLQDLSFSVEGGQRVGLLGRTGSGKSTLLSALLRLL-------STEGEIQIDGVSWnsvtLQTW 1290

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099586    79 QRNIGMIFQDYALF---------PH--------LTVAENIafGLRQMAAeerhlQVQQMLELVHLSGfgdryPHQLSGGQ 141
Cdd:TIGR01271 1291 RKAFGVIPQKVFIFsgtfrknldPYeqwsdeeiWKVAEEV--GLKSVIE-----QFPDKLDFVLVDG-----GYVLSNGH 1358

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099586   142 QQRVAIARSLAYKPDLLLLDEPFSNIDT---QVrhdligeIRKIFKK--QGVTAIFVTHsREEAFAFADKMAVMNHGVIE 216
Cdd:TIGR01271 1359 KQLMCLARSILSKAKILLLDEPSAHLDPvtlQI-------IRKTLKQsfSNCTVILSEH-RVEALLECQQFLVIEGSSVK 1430


                   ....*...
gi 521099586   217 QYGTASEL 224
Cdd:TIGR01271 1431 QYDSIQKL 1438

PRK13541

cytochrome c biogenesis protein CcmA; Provisional

5-196

7.87e-12

cytochrome c biogenesis protein CcmA; Provisional

Pssm-ID: 184128 [Multi-domain] Cd Length: 195 Bit Score: 63.35 E-value: 7.87e-12

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099586   5 LSIQNLTCQYDtQTVLESLSLNVEHGEIVCLLGASGCGKTTLLKAIAGLLPLSSGIMSLNGMTIDD-GKHWLAPEQRNIG 83
Cdd:PRK13541   2 LSLHQLQFNIE-QKNLFDLSITFLPSAITYIKGANGCGKSSLLRMIAGIMQPSSGNIYYKNCNINNiAKPYCTYIGHNLG 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099586  84 MIFQdyalfphLTVAENIAFGLRQMAAEErhlQVQQMLELVHLSGFGDRYPHQLSGGQQQRVAIARSLAYKPDLLLLDEP 163
Cdd:PRK13541  81 LKLE-------MTVFENLKFWSEIYNSAE---TLYAAIHYFKLHDLLDEKCYSLSSGMQKIVAIARLIACQSDLWLLDEV 150

                        170       180       190
                 ....*....|....*....|....*....|...
gi 521099586 164 FSNIDTQVRhDLIGEIRKIFKKQGVTAIFVTHS 196
Cdd:PRK13541 151 ETNLSKENR-DLLNNLIVMKANSGGIVLLSSHL 182

ABCC_CFTR2

cd03289

ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ...

5-224

1.11e-11

ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator (CFTR), the product of the gene mutated in patients with cystic fibrosis, has adapted the ABC transporter structural motif to form a tightly regulated anion channel at the apical surface of many epithelia. Use of the term assembly of a functional ion channel implies the coming together of subunits or at least smaller not-yet functional components of the active whole. In fact, on the basis of current knowledge only the CFTR polypeptide itself is required to form an ATP- and protein kinase A-dependent low-conductance chloride channel of the type present in the apical membrane of many epithelial cells. CFTR displays the typical organization (IM-ABC)2 and carries a characteristic hydrophilic R-domain that separates IM1-ABC1 from IM2-ABC2.

Pssm-ID: 213256 [Multi-domain] Cd Length: 275 Bit Score: 64.49 E-value: 1.11e-11

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099586   5 LSIQNLTCQY--DTQTVLESLSLNVEHGEIVCLLGASGCGKTTLLKAIAGLLPLSSGI----MSLNGMTIddgKHWlape 78
Cdd:cd03289    3 MTVKDLTAKYteGGNAVLENISFSISPGQRVGLLGRTGSGKSTLLSAFLRLLNTEGDIqidgVSWNSVPL---QKW---- 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099586  79 QRNIGMIFQDYALFPHlTVAENI-AFGlrQMAAEErhlqVQQMLELVHLSGFGDRYPHQ-----------LSGGQQQRVA 146
Cdd:cd03289   76 RKAFGVIPQKVFIFSG-TFRKNLdPYG--KWSDEE----IWKVAEEVGLKSVIEQFPGQldfvlvdggcvLSHGHKQLMC 148

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099586 147 IARSLAYKPDLLLLDEPFSNID---TQVrhdligeIRKIFKK--QGVTAIFVTHsREEAFAFADKMAVMNHGVIEQYGTA 221
Cdd:cd03289  149 LARSVLSKAKILLLDEPSAHLDpitYQV-------IRKTLKQafADCTVILSEH-RIEAMLECQRFLVIEENKVRQYDSI 220


                 ...
gi 521099586 222 SEL 224
Cdd:cd03289  221 QKL 223

PRK10938

putative molybdenum transport ATP-binding protein ModF; Provisional

14-210

1.63e-11

putative molybdenum transport ATP-binding protein ModF; Provisional

Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 65.04 E-value: 1.63e-11

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099586  14 YDTQTV-LESLSLNVehGEIVCLLGASGCGKTTLLKAIAGLLPLSSGIMSLNGMTIddgkHWLAPEQ-----------RN 81
Cdd:PRK10938  14 SDTKTLqLPSLTLNA--GDSWAFVGANGSGKSALARALAGELPLLSGERQSQFSHI----TRLSFEQlqklvsdewqrNN 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099586  82 IGMIFQDYALFPHlTVAENIAFGLRqmaAEERHLQVQQMLELVHLSgfgDRYPHQLSGGQQQRVAIARSLAYKPDLLLLD 161
Cdd:PRK10938  88 TDMLSPGEDDTGR-TTAEIIQDEVK---DPARCEQLAQQFGITALL---DRRFKYLSTGETRKTLLCQALMSEPDLLILD 160

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 521099586 162 EPFSNIDTQVRHDLIGEIRKIfKKQGVTAIFVTHSREEAFAFADKMAVM 210
Cdd:PRK10938 161 EPFDGLDVASRQQLAELLASL-HQSGITLVLVLNRFDEIPDFVQFAGVL 208

ycf16

CHL00131

sulfate ABC transporter protein; Validated

5-222

2.83e-11

sulfate ABC transporter protein; Validated

Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 62.74 E-value: 2.83e-11

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099586   5 LSIQNLTCQYDTQTVLESLSLNVEHGEIVCLLGASGCGKTTLLKAIAG--LLPLSSGIMSLNGMTIDDgkhwLAPEQRN- 81
Cdd:CHL00131   8 LEIKNLHASVNENEILKGLNLSINKGEIHAIMGPNGSGKSTLSKVIAGhpAYKILEGDILFKGESILD----LEPEERAh 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099586  82 --IGMIFQDYALFPHLTVAE--NIAFGLRQMAAEERHLQ-------VQQMLELVHLS-GFGDRYPHQ-LSGGQQQRVAIA 148
Cdd:CHL00131  84 lgIFLAFQYPIEIPGVSNADflRLAYNSKRKFQGLPELDplefleiINEKLKLVGMDpSFLSRNVNEgFSGGEKKRNEIL 163

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 521099586 149 RSLAYKPDLLLLDEPFSNIDTqvrhDLIGEIRK---IFKKQGVTAIFVTH-SREEAFAFADKMAVMNHGVIEQYGTAS 222
Cdd:CHL00131 164 QMALLDSELAILDETDSGLDI----DALKIIAEginKLMTSENSIILITHyQRLLDYIKPDYVHVMQNGKIIKTGDAE 237

PRK10982

galactose/methyl galaxtoside transporter ATP-binding protein; Provisional

20-213

4.04e-11

galactose/methyl galaxtoside transporter ATP-binding protein; Provisional

Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 63.98 E-value: 4.04e-11

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099586  20 LESLSLNVEHGEIVCLLGASGCGKTTLLKAIAGLLPLSSGIMSLNGMTID--DGKHWLapeQRNIGMIFQDYALFPHLTV 97
Cdd:PRK10982  14 LDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEIDfkSSKEAL---ENGISMVHQELNLVLQRSV 90

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099586  98 AENIAFG---LRQMAAEERHL--QVQQMLELVHLsgfgDRYPHQ----LSGGQQQRVAIARSLAYKPDLLLLDEPFSNI- 167
Cdd:PRK10982  91 MDNMWLGrypTKGMFVDQDKMyrDTKAIFDELDI----DIDPRAkvatLSVSQMQMIEIAKAFSYNAKIVIMDEPTSSLt 166

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*.
gi 521099586 168 DTQVRHdLIGEIRKIfKKQGVTAIFVTHSREEAFAFADKMAVMNHG 213
Cdd:PRK10982 167 EKEVNH-LFTIIRKL-KERGCGIVYISHKMEEIFQLCDEITILRDG 210

3a01205

TIGR00956

Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]

15-237

4.23e-11

Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]

Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 64.36 E-value: 4.23e-11

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099586    15 DTQTVLESLSLNVEHGEIVCLLGASGCGKTTLLKAIA----GLLPLSSGIMSLNGMTIDDGKHWLAPEQRNIGmifQDYA 90
Cdd:TIGR00956   72 KTFDILKPMDGLIKPGELTVVLGRPGSGCSTLLKTIAsntdGFHIGVEGVITYDGITPEEIKKHYRGDVVYNA---ETDV 148

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099586    91 LFPHLTVAENIAFGLR--------------QMAAEERHLqVQQMLELVHL--SGFGDRYPHQLSGGQQQRVAIARSLAYK 154
Cdd:TIGR00956  149 HFPHLTVGETLDFAARcktpqnrpdgvsreEYAKHIADV-YMATYGLSHTrnTKVGNDFVRGVSGGERKRVSIAEASLGG 227

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099586   155 PDLLLLDEPFSNIDTQVRHDLIGEIRKIFKKQGVTAiFVT--HSREEAFAFADKMAVMNHGVIEQYGTASEL-------- 224
Cdd:TIGR00956  228 AKIQCWDNATRGLDSATALEFIRALKTSANILDTTP-LVAiyQCSQDAYELFDKVIVLYEGYQIYFGPADKAkqyfekmg 306

                          250
                   ....*....|...
gi 521099586   225 YYRPSSKFVADFL 237
Cdd:TIGR00956  307 FKCPDRQTTADFL 319

AAA

smart00382

ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ...

29-199

5.42e-11

Pssm-ID: 214640 [Multi-domain] Cd Length: 148 Bit Score: 60.08 E-value: 5.42e-11

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099586    29 HGEIVCLLGASGCGKTTLLKAIAGLL-PLSSGIMSLNGMTIDDGKHWLAPEQRnigmifqdyalfphltvaeniafglrq 107
Cdd:smart00382   1 PGEVILIVGPPGSGKTTLARALARELgPPGGGVIYIDGEDILEEVLDQLLLII--------------------------- 53

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099586   108 maaeerhlqvqqmlelvhlsgfGDRYPHQLSGGQQQRVAIARSLAYKPDLLLLDEPFSNIDTQVRHDLIGEIRKIFKKQ- 186
Cdd:smart00382  54 ----------------------VGGKKASGSGELRLRLALALARKLKPDVLILDEITSLLDAEQEALLLLLEELRLLLLl 111

                          170
                   ....*....|....*..
gi 521099586   187 ----GVTAIFVTHSREE 199
Cdd:smart00382 112 ksekNLTVILTTNDEKD 128

ABC_ABC_ChvD

TIGR03719

ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ...

5-168

8.89e-11

Pssm-ID: 274744 [Multi-domain] Cd Length: 552 Bit Score: 63.03 E-value: 8.89e-11

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099586    5 LSIQNLTCQYDTQTVLESLSLNVEHGEIVCLLGASGCGKTTLLKAIAGLLPLSSGIMSLnGMTIDdgkhwlapeqrnIGM 84
Cdd:TIGR03719 323 IEAENLTKAFGDKLLIDDLSFKLPPGGIVGVIGPNGAGKSTLFRMITGQEQPDSGTIEI-GETVK------------LAY 389

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099586   85 IFQDY-ALFPHLTVAENIAFGLRQMAAEERHLQVQQMLELVHLSGfGD--RYPHQLSGGQQQRVAIARSLAYKPDLLLLD 161
Cdd:TIGR03719 390 VDQSRdALDPNKTVWEEISGGLDIIKLGKREIPSRAYVGRFNFKG-SDqqKKVGQLSGGERNRVHLAKTLKSGGNVLLLD 468


                  ....*..
gi 521099586  162 EPFSNID 168
Cdd:TIGR03719 469 EPTNDLD 475

PTZ00265

multidrug resistance protein (mdr1); Provisional

5-212

1.67e-10

multidrug resistance protein (mdr1); Provisional

Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 62.35 E-value: 1.67e-10

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099586    5 LSIQNLTCQYDTQTVLE---SLSLNVEHGEIVCLLGASGCGKTTLLKAIAGLLPLSSGIMSLN---GMTIDDGKHWlape 78
Cdd:PTZ00265  383 IQFKNVRFHYDTRKDVEiykDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIIINdshNLKDINLKWW---- 458

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099586   79 QRNIGMIFQDYALFPHlTVAENIAFGL------------------------------RQMAAEERHLQVQQML--ELVHL 126
Cdd:PTZ00265  459 RSKIGVVSQDPLLFSN-SIKNNIKYSLyslkdlealsnyynedgndsqenknkrnscRAKCAGDLNDMSNTTDsnELIEM 537

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099586  127 -------------------------SGFGDRY-------PHQLSGGQQQRVAIARSLAYKPDLLLLDEPFSNIDTQVRHD 174
Cdd:PTZ00265  538 rknyqtikdsevvdvskkvlihdfvSALPDKYetlvgsnASKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYL 617

                         250       260       270
                  ....*....|....*....|....*....|....*...
gi 521099586  175 LIGEIRKIFKKQGVTAIFVTHsREEAFAFADKMAVMNH 212
Cdd:PTZ00265  618 VQKTINNLKGNENRITIIIAH-RLSTIRYANTIFVLSN 654

PTZ00243

ABC transporter; Provisional

13-216

2.86e-10

ABC transporter; Provisional

Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 61.72 E-value: 2.86e-10

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099586   13 QYDTQTVLESLSLNVEHGEIVCLLGASGCGKTTLLKAIAGLLPLSSGIMslngmtiddgkhWlapEQRNIGMIFQDyALF 92
Cdd:PTZ00243  669 ELEPKVLLRDVSVSVPRGKLTVVLGATGSGKSTLLQSLLSQFEISEGRV------------W---AERSIAYVPQQ-AWI 732

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099586   93 PHLTVAENIAFGLRQMAAE-ERHLQVQQM-LELVHLSG-----FGDRYPHqLSGGQQQRVAIARSLAYKPDLLLLDEPFS 165
Cdd:PTZ00243  733 MNATVRGNILFFDEEDAARlADAVRVSQLeADLAQLGGgleteIGEKGVN-LSGGQKARVSLARAVYANRDVYLLDDPLS 811

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 521099586  166 NIDTQVRHDLIGEIRkIFKKQGVTAIFVTHsREEAFAFADKMAVMNHGVIE 216
Cdd:PTZ00243  812 ALDAHVGERVVEECF-LGALAGKTRVLATH-QVHVVPRADYVVALGDGRVE 860

40850658_otr

NF000106

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

108-224

5.70e-10

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

Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 59.75 E-value: 5.70e-10

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099586 108 MAAEERHLQVQQMLELVHLSGFGDRYPHQLSGGQQQRVAIARSLAYKPDLLLLDEPFSNIDTQVRHDLIGEIRKIFkKQG 187
Cdd:NF000106 116 LSRKDARARADELLERFSLTEAAGRAAAKYSGGMRRRLDLAASMIGRPAVLYLDEPTTGLDPRTRNEVWDEVRSMV-RDG 194

                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 521099586 188 VTAIFVTHSREEAFAFADKMAVMNHGVIEQYGTASEL 224
Cdd:NF000106 195 ATVLLTTQYMEEAEQLAHELTVIDRGRVIADGKVDEL 231

PRK11819

putative ABC transporter ATP-binding protein; Reviewed

19-163

7.15e-10

putative ABC transporter ATP-binding protein; Reviewed

Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 60.13 E-value: 7.15e-10

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099586  19 VLESLSLNVEHGEIVCLLGASGCGKTTLLKAIAGllplssgimslngmtID---DGKHWLAPEQRnIGMIFQDYALFPHL 95
Cdd:PRK11819  22 ILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAG---------------VDkefEGEARPAPGIK-VGYLPQEPQLDPEK 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099586  96 TVAENIAFGLR--------------QMAAE--------ERHLQVQQMLElvHLSGF-----------------GDRYPHQ 136
Cdd:PRK11819  86 TVRENVEEGVAevkaaldrfneiyaAYAEPdadfdalaAEQGELQEIID--AADAWdldsqleiamdalrcppWDAKVTK 163

                        170       180
                 ....*....|....*....|....*..
gi 521099586 137 LSGGQQQRVAIARSLAYKPDLLLLDEP 163
Cdd:PRK11819 164 LSGGERRRVALCRLLLEKPDMLLLDEP 190

PRK10982

galactose/methyl galaxtoside transporter ATP-binding protein; Provisional

5-233

1.00e-09

galactose/methyl galaxtoside transporter ATP-binding protein; Provisional

Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 59.36 E-value: 1.00e-09

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099586   5 LSIQNLTCQydTQTVLESLSLNVEHGEIVCLLGASGCGKTTLLKAIAGLLPLSSGIMSLNGMT---------IDDGKHWL 75
Cdd:PRK10982 251 LEVRNLTSL--RQPSIRDVSFDLHKGEILGIAGLVGAKRTDIVETLFGIREKSAGTITLHGKKinnhnaneaINHGFALV 328

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099586  76 APEQRNIGmifqdyaLFPHLTVAEN--IA--------FGL---RQMAAEerhlqVQQMLELVHLSGFGDRYP-HQLSGGQ 141
Cdd:PRK10982 329 TEERRSTG-------IYAYLDIGFNslISnirnyknkVGLldnSRMKSD-----TQWVIDSMRVKTPGHRTQiGSLSGGN 396

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099586 142 QQRVAIARSLAYKPDLLLLDEPFSNIDTQVRHD---LIGEIRKifKKQGVtaIFVTHSREEAFAFADKMAVMNHG----V 214
Cdd:PRK10982 397 QQKVIIGRWLLTQPEILMLDEPTRGIDVGAKFEiyqLIAELAK--KDKGI--IIISSEMPELLGITDRILVMSNGlvagI 472

                        250
                 ....*....|....*....
gi 521099586 215 IEQYGTASELYYRPSSKFV 233
Cdd:PRK10982 473 VDTKTTTQNEILRLASLHL 491

PRK10636

putative ABC transporter ATP-binding protein; Provisional

5-175

1.27e-09

putative ABC transporter ATP-binding protein; Provisional

Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 59.41 E-value: 1.27e-09

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099586   5 LSIQNLTCQYDTQTVLESLSLNVEHGEIVCLLGASGCGKTTLLKAIAG-LLPLSSGIMSLNGMTIDdgkhWLApeQRNIG 83
Cdd:PRK10636 313 LKMEKVSAGYGDRIILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGeLAPVSGEIGLAKGIKLG----YFA--QHQLE 386

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099586  84 MIFQDYALFPHLTvaeniafglrQMAAEERHLQVQQmlelvHLSGFG---DRYPH---QLSGGQQQRVAIARSLAYKPDL 157
Cdd:PRK10636 387 FLRADESPLQHLA----------RLAPQELEQKLRD-----YLGGFGfqgDKVTEetrRFSGGEKARLVLALIVWQRPNL 451

                        170
                 ....*....|....*...
gi 521099586 158 LLLDEPFSNIDTQVRHDL 175
Cdd:PRK10636 452 LLLDEPTNHLDLDMRQAL 469

PRK11147

ABC transporter ATPase component; Reviewed

7-218

1.84e-09

ABC transporter ATPase component; Reviewed

Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 58.81 E-value: 1.84e-09

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099586   7 IQNLTCQYDTQTVLESLSLNVEHGEIVCLLGASGCGKTTLLKAIAGLLPLSSGimslngmTIDDG-KHWLApeqrnigmI 85
Cdd:PRK11147 322 MENVNYQIDGKQLVKDFSAQVQRGDKIALIGPNGCGKTTLLKLMLGQLQADSG-------RIHCGtKLEVA--------Y 386

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099586  86 FQDY--ALFPHLTVAENIAFGLRQMA--AEERHLqvqqmleLVHLSGF-----GDRYP-HQLSGGQQQRVAIARsLAYKP 155
Cdd:PRK11147 387 FDQHraELDPEKTVMDNLAEGKQEVMvnGRPRHV-------LGYLQDFlfhpkRAMTPvKALSGGERNRLLLAR-LFLKP 458

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099586 156 -DLLLLDEPFSNIDTQVRhDLIGEIrkIFKKQGvTAIFVTHSReeafAFADKmAVMN------HGVIEQY 218
Cdd:PRK11147 459 sNLLILDEPTNDLDVETL-ELLEEL--LDSYQG-TVLLVSHDR----QFVDN-TVTEcwifegNGKIGRY 519

PLN03130

ABC transporter C family member; Provisional

19-232

6.31e-09

ABC transporter C family member; Provisional

Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 57.44 E-value: 6.31e-09

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099586   19 VLESLSLNVEHGEIVCLLGASGCGKTTLLKAIAGLLPLSSGIMSLNGmtIDDGKHWLAPEQRNIGMIFQDYALFphltvA 98
Cdd:PLN03130 1254 VLHGLSFEISPSEKVGIVGRTGAGKSSMLNALFRIVELERGRILIDG--CDISKFGLMDLRKVLGIIPQAPVLF-----S 1326

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099586   99 ENIAFGLRQMAaEERHLQVQQMLELVHLSGFGDRYPHQL-----------SGGQQQRVAIARSLAYKPDLLLLDEPFSNI 167
Cdd:PLN03130 1327 GTVRFNLDPFN-EHNDADLWESLERAHLKDVIRRNSLGLdaevseagenfSVGQRQLLSLARALLRRSKILVLDEATAAV 1405

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 521099586  168 DtqVRHD-LIGE-IRKIFKkqGVTAIFVTHsREEAFAFADKMAVMNHGVIEQYGTASELYYRPSSKF 232
Cdd:PLN03130 1406 D--VRTDaLIQKtIREEFK--SCTMLIIAH-RLNTIIDCDRILVLDAGRVVEFDTPENLLSNEGSAF 1467

PRK11819

putative ABC transporter ATP-binding protein; Reviewed

8-169

6.45e-08

putative ABC transporter ATP-binding protein; Reviewed

Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 53.97 E-value: 6.45e-08

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099586   8 QNLTCQYDTQTVLESLSLNVEHGEIVCLLGASGCGKTTLLKAIAGLLPLSSGIMSLnGMT-----IDDGKHWLAPEQrni 82
Cdd:PRK11819 328 ENLSKSFGDRLLIDDLSFSLPPGGIVGIIGPNGAGKSTLFKMITGQEQPDSGTIKI-GETvklayVDQSRDALDPNK--- 403

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099586  83 gmifqdyalfphlTVAENIAFGLRQMaaeerHLQVQQMLELVHLSGFGDRYPHQ------LSGGQQQRVAIARSLAYKPD 156
Cdd:PRK11819 404 -------------TVWEEISGGLDII-----KVGNREIPSRAYVGRFNFKGGDQqkkvgvLSGGERNRLHLAKTLKQGGN 465

                        170
                 ....*....|...
gi 521099586 157 LLLLDEPFSNIDT 169
Cdd:PRK11819 466 VLLLDEPTNDLDV 478

ABC_Class2

cd03227

ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ...

135-206

7.35e-08

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: 51.21 E-value: 7.35e-08

                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 521099586 135 HQLSGGQQQRVAIARSLA---YKPD-LLLLDEPFSNIDTQVRHDLIGEIRKIFKKqGVTAIFVTHsREEAFAFADK 206
Cdd:cd03227   76 LQLSGGEKELSALALILAlasLKPRpLYILDEIDRGLDPRDGQALAEAILEHLVK-GAQVIVITH-LPELAELADK 149

ABCC_SUR2

cd03288

ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The ...

5-232

8.37e-08

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: 52.60 E-value: 8.37e-08

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099586   5 LSIQNLTCQYDT--QTVLESLSLNVEHGEIVCLLGASGCGKTTLLKAIAGLLPLSSGIMSLNGmtIDDGKHWLAPEQRNI 82
Cdd:cd03288   20 IKIHDLCVRYENnlKPVLKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVIDG--IDISKLPLHTLRSRL 97

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099586  83 GMIFQDYALFphltvAENIAFGL--RQMAAEERhlqVQQMLELVHLSGFGDRYPHQL-----------SGGQQQRVAIAR 149
Cdd:cd03288   98 SIILQDPILF-----SGSIRFNLdpECKCTDDR---LWEALEIAQLKNMVKSLPGGLdavvteggenfSVGQRQLFCLAR 169

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099586 150 SLAYKPDLLLLDEPFSNIDTQVRHDLIGEIRKIFKKQgvTAIFVTHsREEAFAFADKMAVMNHGVIEQYGTASELYYRPS 229
Cdd:cd03288  170 AFVRKSSILIMDEATASIDMATENILQKVVMTAFADR--TVVTIAH-RVSTILDADLVLVLSRGILVECDTPENLLAQED 246


                 ...
gi 521099586 230 SKF 232
Cdd:cd03288  247 GVF 249

ABC_RNaseL_inhibitor

cd03222

ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ...

27-223

9.01e-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: 51.42 E-value: 9.01e-08

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099586  27 VEHGEIVCLLGASGCGKTTLLKAIAGLLPLSSGIMSLNGMTIDDGKHWLapeqrnigmifqdyalfphltvaeniafglr 106
Cdd:cd03222   22 VKEGEVIGIVGPNGTGKTTAVKILAGQLIPNGDNDEWDGITPVYKPQYI------------------------------- 70

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099586 107 qmaaeerhlqvqqmlelvhlsgfgdryphQLSGGQQQRVAIARSLAYKPDLLLLDEPFSNIDTQVRHDLIGEIRKIFKKQ 186
Cdd:cd03222   71 -----------------------------DLSGGELQRVAIAAALLRNATFYLFDEPSAYLDIEQRLNAARAIRRLSEEG 121

                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 521099586 187 GVTAIFVTHSREEAFAFADKMAVMnHGVIEQYGTASE 223
Cdd:cd03222  122 KKTALVVEHDLAVLDYLSDRIHVF-EGEPGVYGIASQ 157

PRK15064

ABC transporter ATP-binding protein; Provisional

5-224

1.24e-07

ABC transporter ATP-binding protein; Provisional

Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 52.97 E-value: 1.24e-07

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099586   5 LSIQNLTCQYDTQTVLESLSLNVEHGEIVCLLGASGCGKTTLLKAIAGLLPLSSGIMSLNgmtiddgkhwlaPEQRnIGM 84
Cdd:PRK15064   2 LSTANITMQFGAKPLFENISVKFGGGNRYGLIGANGCGKSTFMKILGGDLEPSAGNVSLD------------PNER-LGK 68

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099586  85 IFQDYALFPHLTVAENIAFGLRQM--AAEER------------------HLQVQ--QM---------LELvhLSGFG-DR 132
Cdd:PRK15064  69 LRQDQFAFEEFTVLDTVIMGHTELweVKQERdriyalpemseedgmkvaDLEVKfaEMdgytaearaGEL--LLGVGiPE 146

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099586 133 YPH-----QLSGGQQQRVAIARSLAYKPDLLLLDEPFSNIDtqvrhdlIGEIR---KIFKKQGVTAIFVTHSREEAFAFA 204
Cdd:PRK15064 147 EQHyglmsEVAPGWKLRVLLAQALFSNPDILLLDEPTNNLD-------INTIRwleDVLNERNSTMIIISHDRHFLNSVC 219

                        250       260
                 ....*....|....*....|....*..
gi 521099586 205 DKMAVMNHGVI-------EQYGTASEL 224
Cdd:PRK15064 220 THMADLDYGELrvypgnyDEYMTAATQ 246

ABC_RNaseL_inhibitor_domain1

cd03236

The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ...

30-172

2.31e-07

The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI), is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI s are not transport proteins and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLIs have an N-terminal Fe-S domain and two nucleotide binding domains which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.

Pssm-ID: 213203 [Multi-domain] Cd Length: 255 Bit Score: 51.21 E-value: 2.31e-07

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099586  30 GEIVCLLGASGCGKTTLLKAIAGLLplssgIMSLngmtiddGKHWLAPEQRNI-----GMIFQDY--------------- 89
Cdd:cd03236   26 GQVLGLVGPNGIGKSTALKILAGKL-----KPNL-------GKFDDPPDWDEIldefrGSELQNYftkllegdvkvivkp 93

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099586  90 ---ALFPHlTVAENIAFGLRQmaAEERHLQ--VQQMLELVHLSgfgDRYPHQLSGGQQQRVAIARSLAYKPDLLLLDEPF 164
Cdd:cd03236   94 qyvDLIPK-AVKGKVGELLKK--KDERGKLdeLVDQLELRHVL---DRNIDQLSGGELQRVAIAAALARDADFYFFDEPS 167


                 ....*...
gi 521099586 165 SNIDTQVR 172
Cdd:cd03236  168 SYLDIKQR 175

ABC_UvrA

cd03238

ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ...

20-198

2.44e-07

ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins, and UvrB having one ATP binding site that is structurally related to that of helicases.

Pssm-ID: 213205 [Multi-domain] Cd Length: 176 Bit Score: 50.01 E-value: 2.44e-07

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099586  20 LESLSLNVEHGEIVCLLGASGCGKTTLLKAIagllplssgimslngmtiddgkhwLAPEQRNigMIFQDYALFPHLTVae 99
Cdd:cd03238   11 LQNLDVSIPLNVLVVVTGVSGSGKSTLVNEG------------------------LYASGKA--RLISFLPKFSRNKL-- 62

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099586 100 nIAFGlrqmaaeerhlQVQQMLELvhlsGFG----DRYPHQLSGGQQQRVAIARSLA--YKPDLLLLDEPFSNIDTQVRH 173
Cdd:cd03238   63 -IFID-----------QLQFLIDV----GLGyltlGQKLSTLSGGELQRVKLASELFsePPGTLFILDEPSTGLHQQDIN 126

                        170       180
                 ....*....|....*....|....*
gi 521099586 174 DLIGEIRKIfKKQGVTAIFVTHSRE 198
Cdd:cd03238  127 QLLEVIKGL-IDLGNTVILIEHNLD 150

ABC_Rad50

cd03240

ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ...

5-198

2.49e-07

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: 50.68 E-value: 2.49e-07

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099586   5 LSIQNLTCQYDTQTVleslslNVEHGeIVCLLGASGCGKTTLLKAIA----GLLPLSSgimslngmtiDDGKHW--LAPE 78
Cdd:cd03240    4 LSIRNIRSFHERSEI------EFFSP-LTLIVGQNGAGKTTIIEALKyaltGELPPNS----------KGGAHDpkLIRE 66

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099586  79 QRNIGMI---FQ-----DYALFPHLTVAENIAFgLRQmaaEERHLQVQQMLElvhlsgfgdryphQLSGGQQQ------R 144
Cdd:cd03240   67 GEVRAQVklaFEnangkKYTITRSLAILENVIF-CHQ---GESNWPLLDMRG-------------RCSGGEKVlasliiR 129

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 521099586 145 VAIARSLAYKPDLLLLDEPFSNIDT-QVRHDLIGEIRKIFKKQGVTAIFVTHSRE 198
Cdd:cd03240  130 LALAETFGSNCGILALDEPTTNLDEeNIEESLAEIIEERKSQKNFQLIVITHDEE 184

sufC

PRK09580

cysteine desulfurase ATPase component; Reviewed

5-168

3.51e-07

cysteine desulfurase ATPase component; Reviewed

Pssm-ID: 181965 [Multi-domain] Cd Length: 248 Bit Score: 50.56 E-value: 3.51e-07

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099586   5 LSIQNLTCQYDTQTVLESLSLNVEHGEIVCLLGASGCGKTTLLKAIAGL--LPLSSGIMSLNGMTIDDgkhwLAPEQR-- 80
Cdd:PRK09580   2 LSIKDLHVSVEDKAILRGLNLEVRPGEVHAIMGPNGSGKSTLSATLAGRedYEVTGGTVEFKGKDLLE----LSPEDRag 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099586  81 -NIGMIFQDYALFP------HLTVAENIAFGLRQMAAEERHLQVQQMLELVHLSgfgdRYPHQL---------SGGQQQR 144
Cdd:PRK09580  78 eGIFMAFQYPVEIPgvsnqfFLQTALNAVRSYRGQEPLDRFDFQDLMEEKIALL----KMPEDLltrsvnvgfSGGEKKR 153

                        170       180
                 ....*....|....*....|....
gi 521099586 145 VAIARSLAYKPDLLLLDEPFSNID 168
Cdd:PRK09580 154 NDILQMAVLEPELCILDESDSGLD 177

Rli1

COG1245

Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ...

30-168

6.20e-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: 47.86 E-value: 6.20e-06

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099586  30 GEIVCLLGASGCGKTTLLKAIAGLLplssgIMSLngmtiddGKHWLAPEQRNI-----GMIFQDYalFPHL-----TVA- 98
Cdd:COG1245   99 GKVTGILGPNGIGKSTALKILSGEL-----KPNL-------GDYDEEPSWDEVlkrfrGTELQDY--FKKLangeiKVAh 164

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099586  99 -----ENIAfglRQ---------MAAEERHL--QVQQMLELVHLSgfgDRYPHQLSGGQQQRVAIARSLAYKPDLLLLDE 162
Cdd:COG1245  165 kpqyvDLIP---KVfkgtvrellEKVDERGKldELAEKLGLENIL---DRDISELSGGELQRVAIAAALLRDADFYFFDE 238


                 ....*.
gi 521099586 163 PFSNID 168
Cdd:COG1245  239 PSSYLD 244

PLN03073

ABC transporter F family; Provisional

24-198

9.55e-06

ABC transporter F family; Provisional

Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 47.16 E-value: 9.55e-06

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099586  24 SLNVEHGEIVCLLGASGCGKTTLLK-----AIAGLlPLSSGIMSLNGMTIDDGKHWL-----APEQRNIGMIFQDYALFP 93
Cdd:PLN03073 197 SVTLAFGRHYGLVGRNGTGKTTFLRymamhAIDGI-PKNCQILHVEQEVVGDDTTALqcvlnTDIERTQLLEEEAQLVAQ 275

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099586  94 HLTVAENIAFGLRQMA---------AEERHLQVQQMLELVH-----------LSGFG------DRYPHQLSGGQQQRVAI 147
Cdd:PLN03073 276 QRELEFETETGKGKGAnkdgvdkdaVSQRLEEIYKRLELIDaytaearaasiLAGLSftpemqVKATKTFSGGWRMRIAL 355

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 521099586 148 ARSLAYKPDLLLLDEPFSNIDTQVRHDLIGEIRKIFKkqgvTAIFVTHSRE 198
Cdd:PLN03073 356 ARALFIEPDLLLLDEPTNHLDLHAVLWLETYLLKWPK----TFIVVSHARE 402

TOBE_2

pfam08402

TOBE domain; The TOBE domain (Transport-associated OB) always occurs as a dimer as the ...

276-342

1.34e-05

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: 42.61 E-value: 1.34e-05

                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 521099586  276 LLLRPQQISIYADEES-SVTVLEQQFMGDHCRYVIDAHGSKLLA-----TSSRGLAVGQTVAVSIDTQGVLAF 342
Cdd:pfam08402   1 LAIRPEKIRLAAAANGlSGTVTDVEYLGDHTRYHVELAGGEELVvrvpnAHARPPAPGDRVGLGWDPEDAHVL 73

PRK00635

excinuclease ABC subunit A; Provisional

131-207

1.63e-05

excinuclease ABC subunit A; Provisional

Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 46.75 E-value: 1.63e-05

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099586  131 DRYPHQLSGGQQQRVAIARSLAykPDLL----LLDEPFSNIDTQVRHDLIGEIRKIfKKQGVTAIFVTHSrEEAFAFADK 206
Cdd:PRK00635  471 ERALATLSGGEQERTALAKHLG--AELIgityILDEPSIGLHPQDTHKLINVIKKL-RDQGNTVLLVEHD-EQMISLADR 546


                  .
gi 521099586  207 M 207
Cdd:PRK00635  547 I 547

SbcC

COG0419

DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair];

5-182

3.50e-05

DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair];

Pssm-ID: 440188 [Multi-domain] Cd Length: 204 Bit Score: 44.23 E-value: 3.50e-05

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099586   5 LSIQNLTCQYDTQTVleslslNVEHGeIVCLLGASGCGKTTLLKAIAGLL--------PLSSGIMSLN--GMTID----- 69
Cdd:COG0419    5 LRLENFRSYRDTETI------DFDDG-LNLIVGPNGAGKSTILEAIRYALygkarsrsKLRSDLINVGseEASVElefeh 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099586  70 DGKHW--------------LAPEQR--NIGMIFQDYALFPHLTVAENIAFGLRQMAAEERHLQVQQMLELVHLSGFGDry 133
Cdd:COG0419   78 GGKRYrierrqgefaefleAKPSERkeALKRLLGLEIYEELKERLKELEEALESALEELAELQKLKQEILAQLSGLDP-- 155

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 521099586 134 PHQLSGGQQQRVAIARSLAykpdlLLLDepFSNIDTQVRHDLIGEIRKI 182
Cdd:COG0419  156 IETLSGGERLRLALADLLS-----LILD--FGSLDEERLERLLDALEEL 197

PLN03073

ABC transporter F family; Provisional

33-176

6.26e-05

ABC transporter F family; Provisional

Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 44.85 E-value: 6.26e-05

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099586  33 VCLLGASGCGKTTLLKAIAGLLPLSSGIMslngmtiddgkhWLAPEQRnIGMIFQDYALFPHLTVAENIAFGLRQMAAEE 112
Cdd:PLN03073 538 IAMVGPNGIGKSTILKLISGELQPSSGTV------------FRSAKVR-MAVFSQHHVDGLDLSSNPLLYMMRCFPGVPE 604

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099586 113 RHLQVqqmlelvHLSGFGD------RYPHQLSGGQQQRVAIARSLAYKPDLLLLDEPFSNIDTQVRHDLI 176
Cdd:PLN03073 605 QKLRA-------HLGSFGVtgnlalQPMYTLSGGQKSRVAFAKITFKKPHILLLDEPSNHLDLDAVEALI 667

PRK13409

ribosome biogenesis/translation initiation ATPase RLI;

30-168

8.78e-05

ribosome biogenesis/translation initiation ATPase RLI;

Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 44.03 E-value: 8.78e-05

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099586  30 GEIVCLLGASGCGKTTLLKAIAGLLplssgIMSLngmtiddGKHWLAPEQRNI-----GMIFQDYalFPHL--------- 95
Cdd:PRK13409  99 GKVTGILGPNGIGKTTAVKILSGEL-----IPNL-------GDYEEEPSWDEVlkrfrGTELQNY--FKKLyngeikvvh 164

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099586  96 --------------TVAENIafglrqMAAEERHL--QVQQMLELVHLSgfgDRYPHQLSGGQQQRVAIARSLAYKPDLLL 159
Cdd:PRK13409 165 kpqyvdlipkvfkgKVRELL------KKVDERGKldEVVERLGLENIL---DRDISELSGGELQRVAIAAALLRDADFYF 235


                 ....*....
gi 521099586 160 LDEPFSNID 168
Cdd:PRK13409 236 FDEPTSYLD 244

GguA

NF040905

sugar ABC transporter ATP-binding protein;

4-168

2.69e-04

sugar ABC transporter ATP-binding protein;

Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 42.47 E-value: 2.69e-04

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099586   4 ALSIQNLTCQYDTQT---VLESLSLNVEHGEIVCLLGASGCGKTTLLKAIAGLlplS-----SGIMSLNGMTIDDG---- 71
Cdd:NF040905 257 VFEVKNWTVYHPLHPerkVVDDVSLNVRRGEIVGIAGLMGAGRTELAMSVFGR---SygrniSGTVFKDGKEVDVStvsd 333

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099586  72 --KHWLA--PEQR-NIGMIFQDyalfphlTVAENI-AFGLRQMAaeeRHLQVQQMLELVHLSGFGD----RYPH------ 135
Cdd:NF040905 334 aiDAGLAyvTEDRkGYGLNLID-------DIKRNItLANLGKVS---RRGVIDENEEIKVAEEYRKkmniKTPSvfqkvg 403

                        170       180       190
                 ....*....|....*....|....*....|...
gi 521099586 136 QLSGGQQQRVAIARSLAYKPDLLLLDEPFSNID 168
Cdd:NF040905 404 NLSGGNQQKVVLSKWLFTDPDVLILDEPTRGID 436

PRK10636

putative ABC transporter ATP-binding protein; Provisional

16-198

3.26e-04

putative ABC transporter ATP-binding protein; Provisional

Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 42.46 E-value: 3.26e-04

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099586  16 TQTVLESLSLNVEHGEIVCLLGASGCGKTTLLKAIAGLLPLSSGIMSLngmtiddgkhwlaPEQRNIGMIFQDYalfPHL 95
Cdd:PRK10636  13 VRVLLDNATATINPGQKVGLVGKNGCGKSTLLALLKNEISADGGSYTF-------------PGNWQLAWVNQET---PAL 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099586  96 TVA--ENIAFGLRQMAAEERHLQVQ------QMLELVH------------------LSGFG------DRYPHQLSGGQQQ 143
Cdd:PRK10636  77 PQPalEYVIDGDREYRQLEAQLHDAnerndgHAIATIHgkldaidawtirsraaslLHGLGfsneqlERPVSDFSGGWRM 156

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 521099586 144 RVAIARSLAYKPDLLLLDEPFSNIDTqvrhDLIGEIRKIFKKQGVTAIFVTHSRE 198
Cdd:PRK10636 157 RLNLAQALICRSDLLLLDEPTNHLDL----DAVIWLEKWLKSYQGTLILISHDRD 207

SbcC_Walker_B

pfam13558

SbcC/RAD50-like, Walker B motif; This entry represents the Walker B domain of RAD50 from ...

136-181

5.44e-04

SbcC/RAD50-like, Walker B motif; This entry represents the Walker B domain of RAD50 from eukaryotes and the prokaryotic homolog SbcCD complex subunit C. RAD50-ATPase forms a complex with Mre11-nuclease that detects and processes diverse and obstructed DNA ends. This domain is separated of the Walker A domain by a long coiled-coil domain and forms the nucleotide-binding domain (NBD) when the coiled coils fold back on themselves and bring together Walker A and B domains. Two RAD50-NBDs forms heterotetramers with a Mre11 nuclease dimer that assemble as catalytic head module that binds and cleaves DNA in an ATP-dependent reaction. Through secondary structural analysis, it has been suggested that there is a wide structural conservation in the Rad50/SMC protein family as seen in structural similarities between RAD50's hook and ABC-ATPase MukB's elbow region.

Pssm-ID: 463921 [Multi-domain] Cd Length: 90 Bit Score: 38.37 E-value: 5.44e-04

                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 521099586  136 QLSGGQQQR---VAIARSLAY----------KPDLLLLDEPFSNIDTQVRHDLIGEIRK 181
Cdd:pfam13558  32 GLSGGEKQLlayLPLAAALAAqygsaegrppAPRLVFLDEAFAKLDEENIRTALELLRA 90

AAA_25

pfam13481

AAA domain; This AAA domain is found in a wide variety of presumed DNA repair proteins.

30-200

5.76e-04

AAA domain; This AAA domain is found in a wide variety of presumed DNA repair proteins.

Pssm-ID: 463892 [Multi-domain] Cd Length: 193 Bit Score: 40.44 E-value: 5.76e-04

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099586   30 GEIVCLLGASGCGKTTLlkaiagLLPLSSGIMSlngmtiddGKHWL----APEQRNIGMIfqdyalfphltVAENIAFGL 105
Cdd:pfam13481  33 GGLGLLAGAPGTGKTTL------ALDLAAAVAT--------GKPWLggprVPEQGKVLYV-----------SAEGPADEL 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099586  106 RQ-MAAEERHLQVQQMLELVHLSG----FGDRYPHQLSggQQQRVAIARSL--AYKPDLLLLDePFS-------NIDTQV 171
Cdd:pfam13481  88 RRrLRAAGADLDLPARLLFLSLVEslplFFLDRGGPLL--DADVDALEAALeeVEDPDLVVID-PLAralggdeNSNSDV 164

                         170       180
                  ....*....|....*....|....*....
gi 521099586  172 RHdLIGEIRKIFKKQGVTAIFVTHSREEA 200
Cdd:pfam13481 165 GR-LVKALDRLARRTGATVLLVHHVGKDG 192

AAA

cd00009

The AAA+ (ATPases Associated with a wide variety of cellular Activities) superfamily ...

28-68

7.87e-04

The AAA+ (ATPases Associated with a wide variety of cellular Activities) superfamily represents an ancient group of ATPases belonging to the ASCE (for additional strand, catalytic E) division of the P-loop NTPase fold. The ASCE division also includes ABC, RecA-like, VirD4-like, PilT-like, and SF1/2 helicases. Members of the AAA+ ATPases function as molecular chaperons, ATPase subunits of proteases, helicases, or nucleic-acid stimulated ATPases. The AAA+ proteins contain several distinct features in addition to the conserved alpha-beta-alpha core domain structure and the Walker A and B motifs of the P-loop NTPases.

Pssm-ID: 99707 [Multi-domain] Cd Length: 151 Bit Score: 39.44 E-value: 7.87e-04

                         10        20        30        40
                 ....*....|....*....|....*....|....*....|..
gi 521099586  28 EHGEIVCLLGASGCGKTTLLKAIAGLLPLSSG-IMSLNGMTI 68
Cdd:cd00009   17 PPPKNLLLYGPPGTGKTTLARAIANELFRPGApFLYLNASDL 58

RecA-like_BCS1

cd19510

Mitochondrial chaperone BCS1; Mitochondrial chaperone BCS1 is necessary for the assembly of ...

35-70

5.23e-03

Mitochondrial chaperone BCS1; Mitochondrial chaperone BCS1 is necessary for the assembly of mitochondrial respiratory chain complex III and plays an important role in the maintenance of mitochondrial tubular networks, respiratory chain assembly and formation of the LETM1 complex. RecA-like NTPases. This family includes the NTP binding domain of F1 and V1 H(+)ATPases, DnaB and related helicases as well as bacterial RecA and related eukaryotic and archaeal recombinases. This group also includes bacterial conjugation proteins and related DNA transfer proteins involved in type II and type IV secretion.

Pssm-ID: 410918 [Multi-domain] Cd Length: 153 Bit Score: 36.95 E-value: 5.23e-03

                         10        20        30
                 ....*....|....*....|....*....|....*.
gi 521099586  35 LLGASGCGKTTLLKAIAGLLPLSSGIMSLNGMTIDD 70
Cdd:cd19510   28 LYGPPGTGKSSFIAALAGELDYDICDLNLSEVVLTD 63

ABC_UvrA_I

cd03270

ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair ...

137-205

7.38e-03

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: 37.24 E-value: 7.38e-03

                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 521099586 137 LSGGQQQRVAIARSLAYKPD--LLLLDEPFSNIDTQVRHDLIGEIRKIfKKQGVTAIFVTHSrEEAFAFAD 205
Cdd:cd03270  138 LSGGEAQRIRLATQIGSGLTgvLYVLDEPSIGLHPRDNDRLIETLKRL-RDLGNTVLVVEHD-EDTIRAAD 206

AAA_28

pfam13521

AAA domain;

33-51

7.46e-03

AAA domain;

Pssm-ID: 433278 [Multi-domain] Cd Length: 164 Bit Score: 36.86 E-value: 7.46e-03

                          10
                  ....*....|....*....
gi 521099586   33 VCLLGASGCGKTTLLKAIA 51
Cdd:pfam13521   2 IVITGGPSTGKTTLAEALA 20

AAA_14

pfam13173

AAA domain; This family of domains contain a P-loop motif that is characteriztic of the AAA ...

29-70

8.74e-03

AAA domain; This family of domains contain a P-loop motif that is characteriztic of the AAA superfamily.

Pssm-ID: 463799 [Multi-domain] Cd Length: 128 Bit Score: 36.03 E-value: 8.74e-03

                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 521099586   29 HGEIVCLLGASGCGKTTLLKAIAGLLPLSSGIMSLNGMTIDD 70
Cdd:pfam13173   1 SRKILVITGPRQVGKTTLLLQLIKELLPPENILYINLDDPRL 42

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