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Conserved domains on  [gi|1131020733|ref|WP_075780322|]
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ABC transporter ATP-binding protein [Marinitoga sp. 1137]

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 ...
 4-363 3.67e-179

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


:

Pssm-ID: 443052 [Multi-domain]  Cd Length: 353  Bit Score: 500.78  E-value: 3.67e-179
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131020733   4 KQVSLRLENVTKIFKDkknnteVIAVNNSTFEIKPGELITLLGPSGCGKTTTLRMVAGFELPTKGKIYIGNEDVTFLPPN 83
Cdd:COG3842     2 AMPALELENVSKRYGD------VTALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRILLDGRDVTGLPPE 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131020733  84 KRDTATVFQSYGLFPHMTVFDNVAYGLKLRKLSREEIEKRVFEALEMVGLKDLASRAPSRLSGGQQQRVTLARSIIVEPA 163
Cdd:COG3842    76 KRNVGMVFQDYALFPHLTVAENVAFGLRMRGVPKAEIRARVAELLELVGLEGLADRYPHQLSGGQQQRVALARALAPEPR 155

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131020733 164 ILLLDEPLSNLDALLREQMRIEIKKIQRKLGITAIYVTHDRVEAMSLSDRIIVMKDGKIMQIGTPVEIYEDPISKFVAGF 243
Cdd:COG3842   156 VLLLDEPLSALDAKLREEMREELRRLQRELGITFIYVTHDQEEALALADRIAVMNDGRIEQVGTPEEIYERPATRFVADF 235

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131020733 244 IGKVAFFTVDVIGKENDniIIDFKGKKLIMKKyDNDLDPGDKGVLMARPESLIL-KEEKEGLIEGKIKINVYLGNTVESF 322
Cdd:COG3842   236 IGEANLLPGTVLGDEGG--GVRTGGRTLEVPA-DAGLAAGGPVTVAIRPEDIRLsPEGPENGLPGTVEDVVFLGSHVRYR 312

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|..
gi 1131020733 323 IDTEYG-EIMVQIDNPgQKKIFPEGAAVSIDVVPELCKVFKE 363
Cdd:COG3842   313 VRLGDGqELVVRVPNR-AALPLEPGDRVGLSWDPEDVVVLPA 353
 
Name Accession Description Interval E-value
PotA COG3842
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ...
 4-363 3.67e-179

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


Pssm-ID: 443052 [Multi-domain]  Cd Length: 353  Bit Score: 500.78  E-value: 3.67e-179
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131020733   4 KQVSLRLENVTKIFKDkknnteVIAVNNSTFEIKPGELITLLGPSGCGKTTTLRMVAGFELPTKGKIYIGNEDVTFLPPN 83
Cdd:COG3842     2 AMPALELENVSKRYGD------VTALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRILLDGRDVTGLPPE 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131020733  84 KRDTATVFQSYGLFPHMTVFDNVAYGLKLRKLSREEIEKRVFEALEMVGLKDLASRAPSRLSGGQQQRVTLARSIIVEPA 163
Cdd:COG3842    76 KRNVGMVFQDYALFPHLTVAENVAFGLRMRGVPKAEIRARVAELLELVGLEGLADRYPHQLSGGQQQRVALARALAPEPR 155

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131020733 164 ILLLDEPLSNLDALLREQMRIEIKKIQRKLGITAIYVTHDRVEAMSLSDRIIVMKDGKIMQIGTPVEIYEDPISKFVAGF 243
Cdd:COG3842   156 VLLLDEPLSALDAKLREEMREELRRLQRELGITFIYVTHDQEEALALADRIAVMNDGRIEQVGTPEEIYERPATRFVADF 235

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131020733 244 IGKVAFFTVDVIGKENDniIIDFKGKKLIMKKyDNDLDPGDKGVLMARPESLIL-KEEKEGLIEGKIKINVYLGNTVESF 322
Cdd:COG3842   236 IGEANLLPGTVLGDEGG--GVRTGGRTLEVPA-DAGLAAGGPVTVAIRPEDIRLsPEGPENGLPGTVEDVVFLGSHVRYR 312

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|..
gi 1131020733 323 IDTEYG-EIMVQIDNPgQKKIFPEGAAVSIDVVPELCKVFKE 363
Cdd:COG3842   313 VRLGDGqELVVRVPNR-AALPLEPGDRVGLSWDPEDVVVLPA 353
potA PRK09452
spermidine/putrescine ABC transporter ATP-binding protein PotA;
1-332 1.03e-134

spermidine/putrescine ABC transporter ATP-binding protein PotA;


Pssm-ID: 236523 [Multi-domain]  Cd Length: 375  Bit Score: 388.92  E-value: 1.03e-134
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131020733   1 MKKKQVSLRleNVTKIFKDKKnnteviAVNNSTFEIKPGELITLLGPSGCGKTTTLRMVAGFELPTKGKIYIGNEDVTFL 80
Cdd:PRK09452   10 SLSPLVELR--GISKSFDGKE------VISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLDGQDITHV 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131020733  81 PPNKRDTATVFQSYGLFPHMTVFDNVAYGLKLRKLSREEIEKRVFEALEMVGLKDLASRAPSRLSGGQQQRVTLARSIIV 160
Cdd:PRK09452   82 PAENRHVNTVFQSYALFPHMTVFENVAFGLRMQKTPAAEITPRVMEALRMVQLEEFAQRKPHQLSGGQQQRVAIARAVVN 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131020733 161 EPAILLLDEPLSNLDALLREQMRIEIKKIQRKLGITAIYVTHDRVEAMSLSDRIIVMKDGKIMQIGTPVEIYEDPISKFV 240
Cdd:PRK09452  162 KPKVLLLDESLSALDYKLRKQMQNELKALQRKLGITFVFVTHDQEEALTMSDRIVVMRDGRIEQDGTPREIYEEPKNLFV 241

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131020733 241 AGFIGKVAFFTVDVIGKEND-NIIIDFKGKKLIMkKYDNDLDPGDKGVLMARPESLILKE-----EKEGLIeGKIKINVY 314
Cdd:PRK09452  242 ARFIGEINIFDATVIERLDEqRVRANVEGRECNI-YVNFAVEPGQKLHVLLRPEDLRVEEinddeHAEGLI-GYVRERNY 319

                         330
                  ....*....|....*....
gi 1131020733 315 LGNTVESFIDTEYG-EIMV 332
Cdd:PRK09452  320 KGMTLDSVVELENGkMVMV 338
ABC_PotA_N cd03300
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ...
 8-245 9.15e-128

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: 365.79  E-value: 9.15e-128
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131020733   8 LRLENVTKIFKDKknntevIAVNNSTFEIKPGELITLLGPSGCGKTTTLRMVAGFELPTKGKIYIGNEDVTFLPPNKRDT 87
Cdd:cd03300     1 IELENVSKFYGGF------VALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGKDITNLPPHKRPV 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131020733  88 ATVFQSYGLFPHMTVFDNVAYGLKLRKLSREEIEKRVFEALEMVGLKDLASRAPSRLSGGQQQRVTLARSIIVEPAILLL 167
Cdd:cd03300    75 NTVFQNYALFPHLTVFENIAFGLRLKKLPKAEIKERVAEALDLVQLEGYANRKPSQLSGGQQQRVAIARALVNEPKVLLL 154

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1131020733 168 DEPLSNLDALLREQMRIEIKKIQRKLGITAIYVTHDRVEAMSLSDRIIVMKDGKIMQIGTPVEIYEDPISKFVAGFIG 245
Cdd:cd03300   155 DEPLGALDLKLRKDMQLELKRLQKELGITFVFVTHDQEEALTMSDRIAVMNKGKIQQIGTPEEIYEEPANRFVADFIG 232
PhnT2 TIGR03265
putative 2-aminoethylphosphonate ABC transporter, ATP-binding protein; This ABC transporter ...
 8-319 4.35e-122

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: 355.88  E-value: 4.35e-122
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131020733   8 LRLENVTKIFkdkkNNTEviAVNNSTFEIKPGELITLLGPSGCGKTTTLRMVAGFELPTKGKIYIGNEDVTFLPPNKRDT 87
Cdd:TIGR03265   5 LSIDNIRKRF----GAFT--ALKDISLSVKKGEFVCLLGPSGCGKTTLLRIIAGLERQTAGTIYQGGRDITRLPPQKRDY 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131020733  88 ATVFQSYGLFPHMTVFDNVAYGLKLRKLSREEIEKRVFEALEMVGLKDLASRAPSRLSGGQQQRVTLARSIIVEPAILLL 167
Cdd:TIGR03265  79 GIVFQSYALFPNLTVADNIAYGLKNRGMGRAEVAERVAELLDLVGLPGSERKYPGQLSGGQQQRVALARALATSPGLLLL 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131020733 168 DEPLSNLDALLREQMRIEIKKIQRKLGITAIYVTHDRVEAMSLSDRIIVMKDGKIMQIGTPVEIYEDPISKFVAGFIGKV 247
Cdd:TIGR03265 159 DEPLSALDARVREHLRTEIRQLQRRLGVTTIMVTHDQEEALSMADRIVVMNHGVIEQVGTPQEIYRHPATPFVADFVGEV 238

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1131020733 248 AFFTVDVIGKENdniiidFKGKKLIMKKYDNDLDPGDKGVLMARPESLILK--EEKEGLIEGKIKINVYLGNTV 319
Cdd:TIGR03265 239 NWLPGTRGGGSR------ARVGGLTLACAPGLAQPGASVRLAVRPEDIRVSpaGNAANLLLARVEDMEFLGAFY 306
tungstate_WtpC NF040840
tungstate ABC transporter ATP-binding protein WtpC;
8-245 1.21e-94

tungstate ABC transporter ATP-binding protein WtpC;


Pssm-ID: 468779 [Multi-domain]  Cd Length: 347  Bit Score: 285.82  E-value: 1.21e-94
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131020733   8 LRLENVTKIFKDKKnnteviaVNNSTFEIKPGELITLLGPSGCGKTTTLRMVAGFELPTKGKIYIGNEDVTFLPPNKRDT 87
Cdd:NF040840    2 IRIENLSKDWKEFK-------LRDISLEVKEGEYFIILGPSGAGKTVLLELIAGIWPPDSGKIYLDGKDITNLPPEKRGI 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131020733  88 ATVFQSYGLFPHMTVFDNVAYGLKLRKLSREEIEKRVFEALEMVGLKDLASRAPSRLSGGQQQRVTLARSIIVEPAILLL 167
Cdd:NF040840   75 AYVYQNYMLFPHKTVFENIAFGLKLRKVPKEEIERKVKEIMELLGISHLLHRKPRTLSGGEQQRVALARALIIEPKLLLL 154

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1131020733 168 DEPLSNLDALLREQMRIEIKKIQRKLGITAIYVTHDRVEAMSLSDRIIVMKDGKIMQIGTPVEIYEDPISKFVAGFIG 245
Cdd:NF040840  155 DEPLSALDVQTRDELIREMKRWHREFGFTAIHVTHNFEEALSLADRVGIMLNGRLSQVGDVREVFRRPKNEFVARFVG 232
ABC_ATP_DarD NF038007
darobactin export ABC transporter ATP-binding protein;
8-222 3.32e-50

darobactin export ABC transporter ATP-binding protein;


Pssm-ID: 411600 [Multi-domain]  Cd Length: 218  Bit Score: 167.20  E-value: 3.32e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131020733   8 LRLENVTKIFKDKKNNTEVIavNNSTFEIKPGELITLLGPSGCGKTTTLRMVAGFELPTKGKIYIGNEDVTFLPPNKRDT 87
Cdd:NF038007    2 LNMQNAEKCYITKTIKTKVL--NHLNFSVEKGDFVSIMGPSGSGKSTLLNIIGMFDSLDSGSLTLAGKEVTNLSYSQKII 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131020733  88 ------ATVFQSYGLFPHMTVFDNVAYGLKLRKLSREEIEKRVFEALEMVGLKDLASRAPSRLSGGQQQRVTLARSIIVE 161
Cdd:NF038007   80 lrreliGYIFQSFNLIPHLSIFDNVALPLKYRGVAKKERIERVNQVLNLFGIDNRRNHKPMQLSGGQQQRVAIARAMVSN 159

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1131020733 162 PAILLLDEPLSNLDALLREQMRIEIKKIQRKlGITAIYVTHDRvEAMSLSDRIIVMKDGKI 222
Cdd:NF038007  160 PALLLADEPTGNLDSKNARAVLQQLKYINQK-GTTIIMVTHSD-EASTYGNRIINMKDGKL 218
ABC_tran pfam00005
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ...
 29-172 1.91e-47

ABC transporter; ABC transporters for a large family of proteins responsible for translocation of a variety of compounds across biological membranes. ABC transporters are the largest family of proteins in many completely sequenced bacteria. ABC transporters are composed of two copies of this domain and two copies of a transmembrane domain pfam00664. These four domains may belong to a single polypeptide or belong in different polypeptide chains.


Pssm-ID: 394964 [Multi-domain]  Cd Length: 150  Bit Score: 157.81  E-value: 1.91e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131020733  29 VNNSTFEIKPGELITLLGPSGCGKTTTLRMVAGFELPTKGKIYIGNEDVTF--LPPNKRDTATVFQSYGLFPHMTVFDNV 106
Cdd:pfam00005   1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDLTDdeRKSLRKEIGYVFQDPQLFPRLTVRENL 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131020733 107 AYGLKLRKLSREEIEKRVFEALEMVGLKDLASR----APSRLSGGQQQRVTLARSIIVEPAILLLDEPLS 172
Cdd:pfam00005  81 RLGLLLKGLSKREKDARAEEALEKLGLGDLADRpvgeRPGTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
AztA NF040873
zinc ABC transporter ATP-binding protein AztA;
28-217 4.66e-32

zinc ABC transporter ATP-binding protein AztA;


Pssm-ID: 468810 [Multi-domain]  Cd Length: 191  Bit Score: 118.88  E-value: 4.66e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131020733  28 AVNNSTFEIKPGELITLLGPSGCGKTTTLRMVAGFELPTKGKIYI-GNEDVTFLPPNKRDTATvfqsyglFPhMTVFDNV 106
Cdd:NF040873    7 VLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTVRRaGGARVAYVPQRSEVPDS-------LP-LTVRDLV 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131020733 107 AYGL-----KLRKLSREEiEKRVFEALEMVGLKDLASRAPSRLSGGQQQRVTLARSIIVEPAILLLDEPLSNLDALLREQ 181
Cdd:NF040873   79 AMGRwarrgLWRRLTRDD-RAAVDDALERVGLADLAGRQLGELSGGQRQRALLAQGLAQEADLLLLDEPTTGLDAESRER 157

                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 1131020733 182 MRIEIKKIQRKlGITAIYVTHDRVEAMSlSDRIIVM 217
Cdd:NF040873  158 IIALLAEEHAR-GATVVVVTHDLELVRR-ADPCVLL 191
ABC2_perm_RbbA NF033858
ribosome-associated ATPase/putative transporter RbbA;
28-231 1.04e-24

ribosome-associated ATPase/putative transporter RbbA;


Pssm-ID: 468210 [Multi-domain]  Cd Length: 907  Bit Score: 105.59  E-value: 1.04e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131020733  28 AVNNSTFEIKPGELITLLGPSGCGKTTTLRMVAGFELPTKGKIYI-GNedvtflPPNKRDTAT------VFQSYGLFPHM 100
Cdd:NF033858  281 AVDHVSFRIRRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGEAWLfGQ------PVDAGDIATrrrvgyMSQAFSLYGEL 354

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131020733 101 TVFDNVAYGLKLRKLSREEIEKRVFEALEMVGLKDLASRAPSRLSGGQQQRVTLARSIIVEPAILLLDEPLSNLDALLRE 180
Cdd:NF033858  355 TVRQNLELHARLFHLPAAEIAARVAEMLERFDLADVADALPDSLPLGIRQRLSLAVAVIHKPELLILDEPTSGVDPVARD 434

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1131020733 181 ---QMRIEikkIQRKLGITaIYV-THDRVEAMsLSDRIIVMKDGKIMQIGTPVEI 231
Cdd:NF033858  435 mfwRLLIE---LSREDGVT-IFIsTHFMNEAE-RCDRISLMHAGRVLASDTPAAL 484
40850658_otr NF000106
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
1-229 3.10e-14

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


Pssm-ID: 411078 [Multi-domain]  Cd Length: 351  Bit Score: 72.85  E-value: 3.10e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131020733   1 MKKKQVSLRLENVTKIFKDKKNNTEVIAVNNSTFEIKPGELITLLGPSGCGKTTTlrmvagfELPTkgkiYIGNEDVTFL 80
Cdd:NF000106    1 MTRKTISNGARNAVEVRGLVKHFGEVKAVDGVDLDVREGTVLGVLGP*GAA**RG-------ALPA----HV*GPDAGRR 69

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131020733  81 P-------PNKRDTATVFQSY-----GLFPHMTVFDNVAYGLKLRKLSREEIEKRVFEALEMVGLKDLASRAPSRLSGGQ 148
Cdd:NF000106   70 Pwrf*twcANRRALRRTIG*Hrpvr*GRRESFSGRENLYMIGR*LDLSRKDARARADELLERFSLTEAAGRAAAKYSGGM 149

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131020733 149 QQRVTLARSIIVEPAILLLDEPLSNLDALLREQMRIEIKKIQRKlGITAIYVTHDRVEAMSLS------DRIIVMKDGKI 222
Cdd:NF000106  150 RRRLDLAASMIGRPAVLYLDEPTTGLDPRTRNEVWDEVRSMVRD-GATVLLTTQYMEEAEQLAheltviDRGRVIADGKV 228


                  ....*..
gi 1131020733 223 MQIGTPV 229
Cdd:NF000106  229 DELKTKV 235
ABC2_perm_RbbA NF033858
ribosome-associated ATPase/putative transporter RbbA;
9-233 1.29e-13

ribosome-associated ATPase/putative transporter RbbA;


Pssm-ID: 468210 [Multi-domain]  Cd Length: 907  Bit Score: 72.08  E-value: 1.29e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131020733   9 RLENVTKIFKDkknnteVIAVNNSTFEIKPGELITLLGPSGCGKTTTLRMVAGFELPTKGKIYIGNEDVTflppNKRDTA 88
Cdd:NF033858    3 RLEGVSHRYGK------TVALDDVSLDIPAGCMVGLIGPDGVGKSSLLSLIAGARKIQQGRVEVLGGDMA----DARHRR 72

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131020733  89 TVF-------QSYG--LFPHMTVFDNVAYGLKLRKLSREEIEKRVFEALEMVGLKDLASRAPSRLSGGQQQRVTLARSII 159
Cdd:NF033858   73 AVCpriaympQGLGknLYPTLSVFENLDFFGRLFGQDAAERRRRIDELLRATGLAPFADRPAGKLSGGMKQKLGLCCALI 152

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1131020733 160 VEPAILLLDEPLSNLDALLREQMRIEIKKI-QRKLGITAIYVTHDRVEAMSLsDRIIVMKDGKIMQIGTPVEIYE 233
Cdd:NF033858  153 HDPDLLILDEPTTGVDPLSRRQFWELIDRIrAERPGMSVLVATAYMEEAERF-DWLVAMDAGRVLATGTPAELLA 226
GguA NF040905
sugar ABC transporter ATP-binding protein;
8-221 2.39e-08

sugar ABC transporter ATP-binding protein;


Pssm-ID: 468840 [Multi-domain]  Cd Length: 500  Bit Score: 55.57  E-value: 2.39e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131020733   8 LRLENVTKIFKDkknnteVIAVNNSTFEIKPGELITLLGPSGCGKTTTLRMVAG------FElptkGKIYIGNEDVTFlp 81
Cdd:NF040905    2 LEMRGITKTFPG------VKALDDVNLSVREGEIHALCGENGAGKSTLMKVLSGvyphgsYE----GEILFDGEVCRF-- 69

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131020733  82 PNKRDT-----ATVFQSYGLFPHMTVFDNVAYGLKLRK---LSREEIEKRVFEALEMVGLKDLASRAPSRLSGGQQQRVT 153
Cdd:NF040905   70 KDIRDSealgiVIIHQELALIPYLSIAENIFLGNERAKrgvIDWNETNRRARELLAKVGLDESPDTLVTDIGVGKQQLVE 149

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1131020733 154 LARSIIVEPAILLLDEPLSNL-----DALLREQMRIeikkiqRKLGITAIYVTHDRVEAMSLSDRIIVMKDGK 221
Cdd:NF040905  150 IAKALSKDVKLLILDEPTAALneedsAALLDLLLEL------KAQGITSIIISHKLNEIRRVADSITVLRDGR 216
AAA smart00382
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ...
 38-220 2.56e-07

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: 49.68  E-value: 2.56e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131020733   38 PGELITLLGPSGCGKTTTLRMVAGFELPTKGKIYIGNEDvtflppnkrdtatvfqsyglfphmtvfdnvayglklrklsr 117
Cdd:smart00382   1 PGEVILIVGPPGSGKTTLARALARELGPPGGGVIYIDGE----------------------------------------- 39

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131020733  118 eeiekRVFEALEMVGLKDLASRAPSRLSGGQQQRVTLARSIIVEPAILLLDEPLSNLDA-----LLREQMRIEIKKIQRK 192
Cdd:smart00382  40 -----DILEEVLDQLLLIIVGGKKASGSGELRLRLALALARKLKPDVLILDEITSLLDAeqealLLLLEELRLLLLLKSE 114

                          170       180       190
                   ....*....|....*....|....*....|...
gi 1131020733  193 LGITAIYVTHDRVEAMSL-----SDRIIVMKDG 220
Cdd:smart00382 115 KNLTVILTTNDEKDLGPAllrrrFDRRIVLLLI 147
GguA NF040905
sugar ABC transporter ATP-binding protein;
111-222 1.14e-06

sugar ABC transporter ATP-binding protein;


Pssm-ID: 468840 [Multi-domain]  Cd Length: 500  Bit Score: 50.17  E-value: 1.14e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131020733 111 KLRKLSR-----EEIEKRVFEALEmvglKDLASRAPS------RLSGGQQQRVTLARSIIVEPAILLLDEPLSNLD--Al 177
Cdd:NF040905  365 NLGKVSRrgvidENEEIKVAEEYR----KKMNIKTPSvfqkvgNLSGGNQQKVVLSKWLFTDPDVLILDEPTRGIDvgA- 439

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 1131020733 178 lreqmRIEIKKIQRKL---GITAIYVTHDRVEAMSLSDRIIVMKDGKI 222
Cdd:NF040905  440 -----KYEIYTIINELaaeGKGVIVISSELPELLGMCDRIYVMNEGRI 482
 
Name Accession Description Interval E-value
PotA COG3842
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ...
 4-363 3.67e-179

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


Pssm-ID: 443052 [Multi-domain]  Cd Length: 353  Bit Score: 500.78  E-value: 3.67e-179
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131020733   4 KQVSLRLENVTKIFKDkknnteVIAVNNSTFEIKPGELITLLGPSGCGKTTTLRMVAGFELPTKGKIYIGNEDVTFLPPN 83
Cdd:COG3842     2 AMPALELENVSKRYGD------VTALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRILLDGRDVTGLPPE 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131020733  84 KRDTATVFQSYGLFPHMTVFDNVAYGLKLRKLSREEIEKRVFEALEMVGLKDLASRAPSRLSGGQQQRVTLARSIIVEPA 163
Cdd:COG3842    76 KRNVGMVFQDYALFPHLTVAENVAFGLRMRGVPKAEIRARVAELLELVGLEGLADRYPHQLSGGQQQRVALARALAPEPR 155

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131020733 164 ILLLDEPLSNLDALLREQMRIEIKKIQRKLGITAIYVTHDRVEAMSLSDRIIVMKDGKIMQIGTPVEIYEDPISKFVAGF 243
Cdd:COG3842   156 VLLLDEPLSALDAKLREEMREELRRLQRELGITFIYVTHDQEEALALADRIAVMNDGRIEQVGTPEEIYERPATRFVADF 235

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131020733 244 IGKVAFFTVDVIGKENDniIIDFKGKKLIMKKyDNDLDPGDKGVLMARPESLIL-KEEKEGLIEGKIKINVYLGNTVESF 322
Cdd:COG3842   236 IGEANLLPGTVLGDEGG--GVRTGGRTLEVPA-DAGLAAGGPVTVAIRPEDIRLsPEGPENGLPGTVEDVVFLGSHVRYR 312

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|..
gi 1131020733 323 IDTEYG-EIMVQIDNPgQKKIFPEGAAVSIDVVPELCKVFKE 363
Cdd:COG3842   313 VRLGDGqELVVRVPNR-AALPLEPGDRVGLSWDPEDVVVLPA 353
MalK COG3839
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ...
 7-361 1.67e-157

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


Pssm-ID: 443050 [Multi-domain]  Cd Length: 352  Bit Score: 445.67  E-value: 1.67e-157
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131020733   7 SLRLENVTKIFKDkknnteVIAVNNSTFEIKPGELITLLGPSGCGKTTTLRMVAGFELPTKGKIYIGNEDVTFLPPNKRD 86
Cdd:COG3839     3 SLELENVSKSYGG------VEALKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAGLEDPTSGEILIGGRDVTDLPPKDRN 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131020733  87 TATVFQSYGLFPHMTVFDNVAYGLKLRKLSREEIEKRVFEALEMVGLKDLASRAPSRLSGGQQQRVTLARSIIVEPAILL 166
Cdd:COG3839    77 IAMVFQSYALYPHMTVYENIAFPLKLRKVPKAEIDRRVREAAELLGLEDLLDRKPKQLSGGQRQRVALGRALVREPKVFL 156

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131020733 167 LDEPLSNLDALLREQMRIEIKKIQRKLGITAIYVTHDRVEAMSLSDRIIVMKDGKIMQIGTPVEIYEDPISKFVAGFIG- 245
Cdd:COG3839   157 LDEPLSNLDAKLRVEMRAEIKRLHRRLGTTTIYVTHDQVEAMTLADRIAVMNDGRIQQVGTPEELYDRPANLFVAGFIGs 236

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131020733 246 -KVAFFTVDVIGKEndniiIDFKGKKLIMKKYDnDLDPGDKGVLMARPESLILKEEKEGLIEGKIKINVYLGNtvESFID 324
Cdd:COG3839   237 pPMNLLPGTVEGGG-----VRLGGVRLPLPAAL-AAAAGGEVTLGIRPEHLRLADEGDGGLEATVEVVEPLGS--ETLVH 308

                         330       340       350
                  ....*....|....*....|....*....|....*..
gi 1131020733 325 TEYGEIMVQIDNPGQKKIfPEGAAVSIDVVPELCKVF 361
Cdd:COG3839   309 VRLGGQELVARVPGDTRL-RPGDTVRLAFDPERLHLF 344
potA PRK09452
spermidine/putrescine ABC transporter ATP-binding protein PotA;
1-332 1.03e-134

spermidine/putrescine ABC transporter ATP-binding protein PotA;


Pssm-ID: 236523 [Multi-domain]  Cd Length: 375  Bit Score: 388.92  E-value: 1.03e-134
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131020733   1 MKKKQVSLRleNVTKIFKDKKnnteviAVNNSTFEIKPGELITLLGPSGCGKTTTLRMVAGFELPTKGKIYIGNEDVTFL 80
Cdd:PRK09452   10 SLSPLVELR--GISKSFDGKE------VISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLDGQDITHV 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131020733  81 PPNKRDTATVFQSYGLFPHMTVFDNVAYGLKLRKLSREEIEKRVFEALEMVGLKDLASRAPSRLSGGQQQRVTLARSIIV 160
Cdd:PRK09452   82 PAENRHVNTVFQSYALFPHMTVFENVAFGLRMQKTPAAEITPRVMEALRMVQLEEFAQRKPHQLSGGQQQRVAIARAVVN 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131020733 161 EPAILLLDEPLSNLDALLREQMRIEIKKIQRKLGITAIYVTHDRVEAMSLSDRIIVMKDGKIMQIGTPVEIYEDPISKFV 240
Cdd:PRK09452  162 KPKVLLLDESLSALDYKLRKQMQNELKALQRKLGITFVFVTHDQEEALTMSDRIVVMRDGRIEQDGTPREIYEEPKNLFV 241

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131020733 241 AGFIGKVAFFTVDVIGKEND-NIIIDFKGKKLIMkKYDNDLDPGDKGVLMARPESLILKE-----EKEGLIeGKIKINVY 314
Cdd:PRK09452  242 ARFIGEINIFDATVIERLDEqRVRANVEGRECNI-YVNFAVEPGQKLHVLLRPEDLRVEEinddeHAEGLI-GYVRERNY 319

                         330
                  ....*....|....*....
gi 1131020733 315 LGNTVESFIDTEYG-EIMV 332
Cdd:PRK09452  320 KGMTLDSVVELENGkMVMV 338
ABC_PotA_N cd03300
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ...
 8-245 9.15e-128

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: 365.79  E-value: 9.15e-128
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131020733   8 LRLENVTKIFKDKknntevIAVNNSTFEIKPGELITLLGPSGCGKTTTLRMVAGFELPTKGKIYIGNEDVTFLPPNKRDT 87
Cdd:cd03300     1 IELENVSKFYGGF------VALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGKDITNLPPHKRPV 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131020733  88 ATVFQSYGLFPHMTVFDNVAYGLKLRKLSREEIEKRVFEALEMVGLKDLASRAPSRLSGGQQQRVTLARSIIVEPAILLL 167
Cdd:cd03300    75 NTVFQNYALFPHLTVFENIAFGLRLKKLPKAEIKERVAEALDLVQLEGYANRKPSQLSGGQQQRVAIARALVNEPKVLLL 154

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1131020733 168 DEPLSNLDALLREQMRIEIKKIQRKLGITAIYVTHDRVEAMSLSDRIIVMKDGKIMQIGTPVEIYEDPISKFVAGFIG 245
Cdd:cd03300   155 DEPLGALDLKLRKDMQLELKRLQKELGITFVFVTHDQEEALTMSDRIAVMNKGKIQQIGTPEEIYEEPANRFVADFIG 232
CysA COG1118
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ...
 7-256 3.28e-122

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


Pssm-ID: 440735 [Multi-domain]  Cd Length: 348  Bit Score: 355.99  E-value: 3.28e-122
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131020733   7 SLRLENVTKIFKDKKnnteviAVNNSTFEIKPGELITLLGPSGCGKTTTLRMVAGFELPTKGKIYIGNEDV-TFLPPNKR 85
Cdd:COG1118     2 SIEVRNISKRFGSFT------LLDDVSLEIASGELVALLGPSGSGKTTLLRIIAGLETPDSGRIVLNGRDLfTNLPPRER 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131020733  86 DTATVFQSYGLFPHMTVFDNVAYGLKLRKLSREEIEKRVFEALEMVGLKDLASRAPSRLSGGQQQRVTLARSIIVEPAIL 165
Cdd:COG1118    76 RVGFVFQHYALFPHMTVAENIAFGLRVRPPSKAEIRARVEELLELVQLEGLADRYPSQLSGGQRQRVALARALAVEPEVL 155

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131020733 166 LLDEPLSNLDALLREQMRIEIKKIQRKLGITAIYVTHDRVEAMSLSDRIIVMKDGKIMQIGTPVEIYEDPISKFVAGFIG 245
Cdd:COG1118   156 LLDEPFGALDAKVRKELRRWLRRLHDELGGTTVFVTHDQEEALELADRVVVMNQGRIEQVGTPDEVYDRPATPFVARFLG 235

                         250
                  ....*....|.
gi 1131020733 246 KVAFFTVDVIG 256
Cdd:COG1118   236 CVNVLRGRVIG 246
PhnT2 TIGR03265
putative 2-aminoethylphosphonate ABC transporter, ATP-binding protein; This ABC transporter ...
 8-319 4.35e-122

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: 355.88  E-value: 4.35e-122
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131020733   8 LRLENVTKIFkdkkNNTEviAVNNSTFEIKPGELITLLGPSGCGKTTTLRMVAGFELPTKGKIYIGNEDVTFLPPNKRDT 87
Cdd:TIGR03265   5 LSIDNIRKRF----GAFT--ALKDISLSVKKGEFVCLLGPSGCGKTTLLRIIAGLERQTAGTIYQGGRDITRLPPQKRDY 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131020733  88 ATVFQSYGLFPHMTVFDNVAYGLKLRKLSREEIEKRVFEALEMVGLKDLASRAPSRLSGGQQQRVTLARSIIVEPAILLL 167
Cdd:TIGR03265  79 GIVFQSYALFPNLTVADNIAYGLKNRGMGRAEVAERVAELLDLVGLPGSERKYPGQLSGGQQQRVALARALATSPGLLLL 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131020733 168 DEPLSNLDALLREQMRIEIKKIQRKLGITAIYVTHDRVEAMSLSDRIIVMKDGKIMQIGTPVEIYEDPISKFVAGFIGKV 247
Cdd:TIGR03265 159 DEPLSALDARVREHLRTEIRQLQRRLGVTTIMVTHDQEEALSMADRIVVMNHGVIEQVGTPQEIYRHPATPFVADFVGEV 238

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1131020733 248 AFFTVDVIGKENdniiidFKGKKLIMKKYDNDLDPGDKGVLMARPESLILK--EEKEGLIEGKIKINVYLGNTV 319
Cdd:TIGR03265 239 NWLPGTRGGGSR------ARVGGLTLACAPGLAQPGASVRLAVRPEDIRVSpaGNAANLLLARVEDMEFLGAFY 306
ABC_Carb_Solutes_like cd03259
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ...
 8-226 3.25e-121

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: 348.36  E-value: 3.25e-121
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131020733   8 LRLENVTKIFKDkknnteVIAVNNSTFEIKPGELITLLGPSGCGKTTTLRMVAGFELPTKGKIYIGNEDVTFLPPNKRDT 87
Cdd:cd03259     1 LELKGLSKTYGS------VRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDGRDVTGVPPERRNI 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131020733  88 ATVFQSYGLFPHMTVFDNVAYGLKLRKLSREEIEKRVFEALEMVGLKDLASRAPSRLSGGQQQRVTLARSIIVEPAILLL 167
Cdd:cd03259    75 GMVFQDYALFPHLTVAENIAFGLKLRGVPKAEIRARVRELLELVGLEGLLNRYPHELSGGQQQRVALARALAREPSLLLL 154

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1131020733 168 DEPLSNLDALLREQMRIEIKKIQRKLGITAIYVTHDRVEAMSLSDRIIVMKDGKIMQIG 226
Cdd:cd03259   155 DEPLSALDAKLREELREELKELQRELGITTIYVTHDQEEALALADRIAVMNEGRIVQVG 213
ugpC PRK11650
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
7-304 1.45e-118

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


Pssm-ID: 236947 [Multi-domain]  Cd Length: 356  Bit Score: 347.22  E-value: 1.45e-118
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131020733   7 SLRLENVTKIFKdkkNNTEVIavNNSTFEIKPGELITLLGPSGCGKTTTLRMVAGFELPTKGKIYIGNEDVTFLPPNKRD 86
Cdd:PRK11650    3 GLKLQAVRKSYD---GKTQVI--KGIDLDVADGEFIVLVGPSGCGKSTLLRMVAGLERITSGEIWIGGRVVNELEPADRD 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131020733  87 TATVFQSYGLFPHMTVFDNVAYGLKLRKLSREEIEKRVFEALEMVGLKDLASRAPSRLSGGQQQRVTLARSIIVEPAILL 166
Cdd:PRK11650   78 IAMVFQNYALYPHMSVRENMAYGLKIRGMPKAEIEERVAEAARILELEPLLDRKPRELSGGQRQRVAMGRAIVREPAVFL 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131020733 167 LDEPLSNLDALLREQMRIEIKKIQRKLGITAIYVTHDRVEAMSLSDRIIVMKDGKIMQIGTPVEIYEDPISKFVAGFIGK 246
Cdd:PRK11650  158 FDEPLSNLDAKLRVQMRLEIQRLHRRLKTTSLYVTHDQVEAMTLADRVVVMNGGVAEQIGTPVEVYEKPASTFVASFIGS 237

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131020733 247 VA--FFTVDVigkENDNIIIDFKGKKLIMKKYDNDLDPGDKGVLMARPESLILKEEKEGL 304
Cdd:PRK11650  238 PAmnLLDGRV---SADGAAFELAGGIALPLGGGYRQYAGRKLTLGIRPEHIALSSAEGGV 294
ABC_MalK_N cd03301
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ...
 8-226 2.55e-115

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: 333.45  E-value: 2.55e-115
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131020733   8 LRLENVTKIFKDKKnnteviAVNNSTFEIKPGELITLLGPSGCGKTTTLRMVAGFELPTKGKIYIGNEDVTFLPPNKRDT 87
Cdd:cd03301     1 VELENVTKRFGNVT------ALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGRDVTDLPPKDRDI 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131020733  88 ATVFQSYGLFPHMTVFDNVAYGLKLRKLSREEIEKRVFEALEMVGLKDLASRAPSRLSGGQQQRVTLARSIIVEPAILLL 167
Cdd:cd03301    75 AMVFQNYALYPHMTVYDNIAFGLKLRKVPKDEIDERVREVAELLQIEHLLDRKPKQLSGGQRQRVALGRAIVREPKVFLM 154

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1131020733 168 DEPLSNLDALLREQMRIEIKKIQRKLGITAIYVTHDRVEAMSLSDRIIVMKDGKIMQIG 226
Cdd:cd03301   155 DEPLSNLDAKLRVQMRAELKRLQQRLGTTTIYVTHDQVEAMTMADRIAVMNDGQIQQIG 213
fbpC PRK11432
ferric ABC transporter ATP-binding protein;
8-339 1.54e-114

ferric ABC transporter ATP-binding protein;


Pssm-ID: 183133 [Multi-domain]  Cd Length: 351  Bit Score: 336.69  E-value: 1.54e-114
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131020733   8 LRLENVTKIFKdkkNNTeVIavNNSTFEIKPGELITLLGPSGCGKTTTLRMVAGFELPTKGKIYIGNEDVTFLPPNKRDT 87
Cdd:PRK11432    7 VVLKNITKRFG---SNT-VI--DNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIFIDGEDVTHRSIQQRDI 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131020733  88 ATVFQSYGLFPHMTVFDNVAYGLKLRKLSREEIEKRVFEALEMVGLKDLASRAPSRLSGGQQQRVTLARSIIVEPAILLL 167
Cdd:PRK11432   81 CMVFQSYALFPHMSLGENVGYGLKMLGVPKEERKQRVKEALELVDLAGFEDRYVDQISGGQQQRVALARALILKPKVLLF 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131020733 168 DEPLSNLDALLREQMRIEIKKIQRKLGITAIYVTHDRVEAMSLSDRIIVMKDGKIMQIGTPVEIYEDPISKFVAGFIGKV 247
Cdd:PRK11432  161 DEPLSNLDANLRRSMREKIRELQQQFNITSLYVTHDQSEAFAVSDTVIVMNKGKIMQIGSPQELYRQPASRFMASFMGDA 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131020733 248 AFFTvdviGKENDNiIIDFKGKKLIMKKYDNDLDPGDKGVLMARPESLILKEEKEGLIEGKIKINVYLGNTVESFIDTEY 327
Cdd:PRK11432  241 NIFP----ATLSGD-YVDIYGYRLPRPAAFAFNLPDGECTVGVRPEAITLSEQGEESQRCTIKHVAYMGPQYEVTVDWHG 315

                         330
                  ....*....|..
gi 1131020733 328 GEIMVQIdNPGQ 339
Cdd:PRK11432  316 QELLLQV-NATQ 326
potA TIGR01187
spermidine/putrescine ABC transporter ATP-binding subunit; This model describes spermidine ...
 44-333 1.81e-113

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: 333.31  E-value: 1.81e-113
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131020733  44 LLGPSGCGKTTTLRMVAGFELPTKGKIYIGNEDVTFLPPNKRDTATVFQSYGLFPHMTVFDNVAYGLKLRKLSREEIEKR 123
Cdd:TIGR01187   1 LLGPSGCGKTTLLRLLAGFEQPDSGSIMLDGEDVTNVPPHLRHINMVFQSYALFPHMTVEENVAFGLKMRKVPRAEIKPR 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131020733 124 VFEALEMVGLKDLASRAPSRLSGGQQQRVTLARSIIVEPAILLLDEPLSNLDALLREQMRIEIKKIQRKLGITAIYVTHD 203
Cdd:TIGR01187  81 VLEALRLVQLEEFADRKPHQLSGGQQQRVALARALVFKPKILLLDEPLSALDKKLRDQMQLELKTIQEQLGITFVFVTHD 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131020733 204 RVEAMSLSDRIIVMKDGKIMQIGTPVEIYEDPISKFVAGFIGKVAFFTVDVIGKENDNIIIDfkGKKLIMKKYDNDL--D 281
Cdd:TIGR01187 161 QEEAMTMSDRIAIMRKGKIAQIGTPEEIYEEPANLFVARFIGEINVFEATVIERKSEQVVLA--GVEGRRCDIYTDVpvE 238

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1131020733 282 PGDKGVLMARPESLILKEEKEG----LIEGKIKINVYLGNTVESFIDTEYGE-IMVQ 333
Cdd:TIGR01187 239 KDQPLHVVLRPEKIVIEEEDEAnssnAIIGHVIDITYLGMTLEVHVRLETGQkVLVS 295
PRK11000 PRK11000
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
7-363 4.22e-113

maltose/maltodextrin ABC transporter ATP-binding protein MalK;


Pssm-ID: 182893 [Multi-domain]  Cd Length: 369  Bit Score: 333.92  E-value: 4.22e-113
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131020733   7 SLRLENVTKIFKDkknnteVIAVNNSTFEIKPGELITLLGPSGCGKTTTLRMVAGFELPTKGKIYIGNEDVTFLPPNKRD 86
Cdd:PRK11000    3 SVTLRNVTKAYGD------VVISKDINLDIHEGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLFIGEKRMNDVPPAERG 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131020733  87 TATVFQSYGLFPHMTVFDNVAYGLKLRKLSREEIEKRVFEALEMVGLKDLASRAPSRLSGGQQQRVTLARSIIVEPAILL 166
Cdd:PRK11000   77 VGMVFQSYALYPHLSVAENMSFGLKLAGAKKEEINQRVNQVAEVLQLAHLLDRKPKALSGGQRQRVAIGRTLVAEPSVFL 156

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131020733 167 LDEPLSNLDALLREQMRIEIKKIQRKLGITAIYVTHDRVEAMSLSDRIIVMKDGKIMQIGTPVEIYEDPISKFVAGFIG- 245
Cdd:PRK11000  157 LDEPLSNLDAALRVQMRIEISRLHKRLGRTMIYVTHDQVEAMTLADKIVVLDAGRVAQVGKPLELYHYPANRFVAGFIGs 236

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131020733 246 -KVAFFTVDVIGKENDNIIIDFKGKKLIMKKYD-NDLDPGDKGVLMARPESLILKEEKEGLIEGKIKINVYLGNtvesfi 323
Cdd:PRK11000  237 pKMNFLPVKVTATAIEQVQVELPNRQQVWLPVEgRGVQVGANMSLGIRPEHLLPSDIADVTLEGEVQVVEQLGN------ 310

                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|
gi 1131020733 324 dteygEIMVQIDNPGQKKIF----------PEGAAVSIDVVPELCKVFKE 363
Cdd:PRK11000  311 -----ETQIHIQIPAIRQNLvyrqndvvlvEEGATFAIGLPPERCHLFRE 355
ABC_CysA_sulfate_importer cd03296
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ...
 7-245 3.37e-102

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: 301.18  E-value: 3.37e-102
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131020733   7 SLRLENVTKIFKDkknnteVIAVNNSTFEIKPGELITLLGPSGCGKTTTLRMVAGFELPTKGKIYIGNEDVTFLPPNKRD 86
Cdd:cd03296     2 SIEVRNVSKRFGD------FVALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGGEDATDVPVQERN 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131020733  87 TATVFQSYGLFPHMTVFDNVAYGLKLRKLSRE----EIEKRVFEALEMVGLKDLASRAPSRLSGGQQQRVTLARSIIVEP 162
Cdd:cd03296    76 VGFVFQHYALFRHMTVFDNVAFGLRVKPRSERppeaEIRAKVHELLKLVQLDWLADRYPAQLSGGQRQRVALARALAVEP 155

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131020733 163 AILLLDEPLSNLDALLREQMRIEIKKIQRKLGITAIYVTHDRVEAMSLSDRIIVMKDGKIMQIGTPVEIYEDPISKFVAG 242
Cdd:cd03296   156 KVLLLDEPFGALDAKVRKELRRWLRRLHDELHVTTVFVTHDQEEALEVADRVVVMNKGRIEQVGTPDEVYDHPASPFVYS 235


                  ...
gi 1131020733 243 FIG 245
Cdd:cd03296   236 FLG 238
TauB COG1116
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ...
 1-233 1.24e-96

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


Pssm-ID: 440733 [Multi-domain]  Cd Length: 260  Bit Score: 287.76  E-value: 1.24e-96
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131020733   1 MKKKQVSLRLENVTKIFKDKKNNTEVIA-VNnstFEIKPGELITLLGPSGCGKTTTLRMVAGFELPTKGKIYIGNEDVTF 79
Cdd:COG1116     1 MSAAAPALELRGVSKRFPTGGGGVTALDdVS---LTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPTSGEVLVDGKPVTG 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131020733  80 LPPnkrDTATVFQSYGLFPHMTVFDNVAYGLKLRKLSREEIEKRVFEALEMVGLKDLASRAPSRLSGGQQQRVTLARSII 159
Cdd:COG1116    78 PGP---DRGVVFQEPALLPWLTVLDNVALGLELRGVPKAERRERARELLELVGLAGFEDAYPHQLSGGMRQRVAIARALA 154

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1131020733 160 VEPAILLLDEPLSNLDALLREQMRIEIKKIQRKLGITAIYVTHDRVEAMSLSDRIIVMKDGKimqiGTPVEIYE 233
Cdd:COG1116   155 NDPEVLLMDEPFGALDALTRERLQDELLRLWQETGKTVLFVTHDVDEAVFLADRVVVLSARP----GRIVEEID 224
OpuBA COG1125
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and ...
 9-246 1.83e-96

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


Pssm-ID: 440742 [Multi-domain]  Cd Length: 306  Bit Score: 288.91  E-value: 1.83e-96
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131020733   9 RLENVTKIFKDKKnntevIAVNNSTFEIKPGELITLLGPSGCGKTTTLRMVAGFELPTKGKIYIGNEDVTFLPPNK--RD 86
Cdd:COG1125     3 EFENVTKRYPDGT-----VAVDDLSLTIPAGEFTVLVGPSGCGKTTTLRMINRLIEPTSGRILIDGEDIRDLDPVElrRR 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131020733  87 TATVFQSYGLFPHMTVFDNVAYGLKLRKLSREEIEKRVFEALEMVGL--KDLASRAPSRLSGGQQQRVTLARSIIVEPAI 164
Cdd:COG1125    78 IGYVIQQIGLFPHMTVAENIATVPRLLGWDKERIRARVDELLELVGLdpEEYRDRYPHELSGGQQQRVGVARALAADPPI 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131020733 165 LLLDEPLSNLDALLREQMRIEIKKIQRKLGITAIYVTHDRVEAMSLSDRIIVMKDGKIMQIGTPVEIYEDPISKFVAGFI 244
Cdd:COG1125   158 LLMDEPFGALDPITREQLQDELLRLQRELGKTIVFVTHDIDEALKLGDRIAVMREGRIVQYDTPEEILANPANDFVADFV 237


                  ..
gi 1131020733 245 GK 246
Cdd:COG1125   238 GA 239
tungstate_WtpC NF040840
tungstate ABC transporter ATP-binding protein WtpC;
8-245 1.21e-94

tungstate ABC transporter ATP-binding protein WtpC;


Pssm-ID: 468779 [Multi-domain]  Cd Length: 347  Bit Score: 285.82  E-value: 1.21e-94
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131020733   8 LRLENVTKIFKDKKnnteviaVNNSTFEIKPGELITLLGPSGCGKTTTLRMVAGFELPTKGKIYIGNEDVTFLPPNKRDT 87
Cdd:NF040840    2 IRIENLSKDWKEFK-------LRDISLEVKEGEYFIILGPSGAGKTVLLELIAGIWPPDSGKIYLDGKDITNLPPEKRGI 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131020733  88 ATVFQSYGLFPHMTVFDNVAYGLKLRKLSREEIEKRVFEALEMVGLKDLASRAPSRLSGGQQQRVTLARSIIVEPAILLL 167
Cdd:NF040840   75 AYVYQNYMLFPHKTVFENIAFGLKLRKVPKEEIERKVKEIMELLGISHLLHRKPRTLSGGEQQRVALARALIIEPKLLLL 154

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1131020733 168 DEPLSNLDALLREQMRIEIKKIQRKLGITAIYVTHDRVEAMSLSDRIIVMKDGKIMQIGTPVEIYEDPISKFVAGFIG 245
Cdd:NF040840  155 DEPLSALDVQTRDELIREMKRWHREFGFTAIHVTHNFEEALSLADRVGIMLNGRLSQVGDVREVFRRPKNEFVARFVG 232
potG PRK11607
putrescine ABC transporter ATP-binding subunit PotG;
8-300 3.55e-92

putrescine ABC transporter ATP-binding subunit PotG;


Pssm-ID: 183226 [Multi-domain]  Cd Length: 377  Bit Score: 280.57  E-value: 3.55e-92
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131020733   8 LRLENVTKIFKDKKnnteviAVNNSTFEIKPGELITLLGPSGCGKTTTLRMVAGFELPTKGKIYIGNEDVTFLPPNKRDT 87
Cdd:PRK11607   20 LEIRNLTKSFDGQH------AVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVDLSHVPPYQRPI 93

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131020733  88 ATVFQSYGLFPHMTVFDNVAYGLKLRKLSREEIEKRVFEALEMVGLKDLASRAPSRLSGGQQQRVTLARSIIVEPAILLL 167
Cdd:PRK11607   94 NMMFQSYALFPHMTVEQNIAFGLKQDKLPKAEIASRVNEMLGLVHMQEFAKRKPHQLSGGQRQRVALARSLAKRPKLLLL 173

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131020733 168 DEPLSNLDALLREQMRIEIKKIQRKLGITAIYVTHDRVEAMSLSDRIIVMKDGKIMQIGTPVEIYEDPISKFVAGFIGKV 247
Cdd:PRK11607  174 DEPMGALDKKLRDRMQLEVVDILERVGVTCVMVTHDQEEAMTMAGRIAIMNRGKFVQIGEPEEIYEHPTTRYSAEFIGSV 253

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1131020733 248 AFFTVDVIGKENDNIIIDFKGKKLIMkKYDNDLDPGDkGV---LMARPESLILKEE 300
Cdd:PRK11607  254 NVFEGVLKERQEDGLVIDSPGLVHPL-KVDADASVVD-NVpvhVALRPEKIMLCEE 307
3a0106s01 TIGR00968
sulfate ABC transporter, ATP-binding protein; [Transport and binding proteins, Anions]
 10-247 6.39e-92

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


Pssm-ID: 130041 [Multi-domain]  Cd Length: 237  Bit Score: 275.14  E-value: 6.39e-92
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131020733  10 LENVTKIFKDkknnteVIAVNNSTFEIKPGELITLLGPSGCGKTTTLRMVAGFELPTKGKIYIGNEDVTFLPPNKRDTAT 89
Cdd:TIGR00968   3 IANISKRFGS------FQALDDVNLEVPTGSLVALLGPSGSGKSTLLRIIAGLEQPDSGRIRLNGQDATRVHARDRKIGF 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131020733  90 VFQSYGLFPHMTVFDNVAYGLKLRKLSREEIEKRVFEALEMVGLKDLASRAPSRLSGGQQQRVTLARSIIVEPAILLLDE 169
Cdd:TIGR00968  77 VFQHYALFKHLTVRDNIAFGLEIRKHPKAKIKARVEELLELVQLEGLGDRYPNQLSGGQRQRVALARALAVEPQVLLLDE 156

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1131020733 170 PLSNLDALLREQMRIEIKKIQRKLGITAIYVTHDRVEAMSLSDRIIVMKDGKIMQIGTPVEIYEDPISKFVAGFIGKV 247
Cdd:TIGR00968 157 PFGALDAKVRKELRSWLRKLHDEVHVTTVFVTHDQEEAMEVADRIVVMSNGKIEQIGSPDEVYDHPANPFVMSFLGEV 234
ABC_NrtD_SsuB_transporters cd03293
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ...
 8-217 3.17e-91

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: 272.42  E-value: 3.17e-91
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131020733   8 LRLENVTKIFKDKknNTEVIAVNNSTFEIKPGELITLLGPSGCGKTTTLRMVAGFELPTKGKIYIGNEDVTflPPNkRDT 87
Cdd:cd03293     1 LEVRNVSKTYGGG--GGAVTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVDGEPVT--GPG-PDR 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131020733  88 ATVFQSYGLFPHMTVFDNVAYGLKLRKLSREEIEKRVFEALEMVGLKDLASRAPSRLSGGQQQRVTLARSIIVEPAILLL 167
Cdd:cd03293    76 GYVFQQDALLPWLTVLDNVALGLELQGVPKAEARERAEELLELVGLSGFENAYPHQLSGGMRQRVALARALAVDPDVLLL 155

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 1131020733 168 DEPLSNLDALLREQMRIEIKKIQRKLGITAIYVTHDRVEAMSLSDRIIVM 217
Cdd:cd03293   156 DEPFSALDALTREQLQEELLDIWRETGKTVLLVTHDIDEAVFLADRVVVL 205
ABC_ModC_like cd03299
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ...
 8-245 3.58e-89

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: 268.05  E-value: 3.58e-89
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131020733   8 LRLENVTKIFKDKKnnteviaVNNSTFEIKPGELITLLGPSGCGKTTTLRMVAGFELPTKGKIYIGNEDVTFLPPNKRDT 87
Cdd:cd03299     1 LKVENLSKDWKEFK-------LKNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNGKDITNLPPEKRDI 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131020733  88 ATVFQSYGLFPHMTVFDNVAYGLKLRKLSREEIEKRVFEALEMVGLKDLASRAPSRLSGGQQQRVTLARSIIVEPAILLL 167
Cdd:cd03299    74 SYVPQNYALFPHMTVYKNIAYGLKKRKVDKKEIERKVLEIAEMLGIDHLLNRKPETLSGGEQQRVAIARALVVNPKILLL 153

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1131020733 168 DEPLSNLDALLREQMRIEIKKIQRKLGITAIYVTHDRVEAMSLSDRIIVMKDGKIMQIGTPVEIYEDPISKFVAGFIG 245
Cdd:cd03299   154 DEPFSALDVRTKEKLREELKKIRKEFGVTVLHVTHDFEEAWALADKVAIMLNGKLIQVGKPEEVFKKPKNEFVAEFLG 231
ABC_OpuCA_Osmoprotection cd03295
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ...
 8-246 2.56e-88

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: 266.09  E-value: 2.56e-88
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131020733   8 LRLENVTKIFKDKKNnteviAVNNSTFEIKPGELITLLGPSGCGKTTTLRMVAGFELPTKGKIYIGNEDVTFLPPNK--R 85
Cdd:cd03295     1 IEFENVTKRYGGGKK-----AVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGEDIREQDPVElrR 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131020733  86 DTATVFQSYGLFPHMTVFDNVAYGLKLRKLSREEIEKRVFEALEMVGL--KDLASRAPSRLSGGQQQRVTLARSIIVEPA 163
Cdd:cd03295    76 KIGYVIQQIGLFPHMTVEENIALVPKLLKWPKEKIRERADELLALVGLdpAEFADRYPHELSGGQQQRVGVARALAADPP 155

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131020733 164 ILLLDEPLSNLDALLREQMRIEIKKIQRKLGITAIYVTHDRVEAMSLSDRIIVMKDGKIMQIGTPVEIYEDPISKFVAGF 243
Cdd:cd03295   156 LLLMDEPFGALDPITRDQLQEEFKRLQQELGKTIVFVTHDIDEAFRLADRIAIMKNGEIVQVGTPDEILRSPANDFVAEF 235


                  ...
gi 1131020733 244 IGK 246
Cdd:cd03295   236 VGA 238
PRK10851 PRK10851
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
7-258 2.47e-87

sulfate/thiosulfate ABC transporter ATP-binding protein CysA;


Pssm-ID: 182778 [Multi-domain]  Cd Length: 353  Bit Score: 267.33  E-value: 2.47e-87
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131020733   7 SLRLENVTKIFkdkkNNTEVIavNNSTFEIKPGELITLLGPSGCGKTTTLRMVAGFELPTKGKIYIGNEDVTFLPPNKRD 86
Cdd:PRK10851    2 SIEIANIKKSF----GRTQVL--NDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFHGTDVSRLHARDRK 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131020733  87 TATVFQSYGLFPHMTVFDNVAYGLKL----RKLSREEIEKRVFEALEMVGLKDLASRAPSRLSGGQQQRVTLARSIIVEP 162
Cdd:PRK10851   76 VGFVFQHYALFRHMTVFDNIAFGLTVlprrERPNAAAIKAKVTQLLEMVQLAHLADRYPAQLSGGQKQRVALARALAVEP 155

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131020733 163 AILLLDEPLSNLDALLREQMRIEIKKIQRKLGITAIYVTHDRVEAMSLSDRIIVMKDGKIMQIGTPVEIYEDPISKFVAG 242
Cdd:PRK10851  156 QILLLDEPFGALDAQVRKELRRWLRQLHEELKFTSVFVTHDQEEAMEVADRVVVMSQGNIEQAGTPDQVWREPATRFVLE 235

                         250
                  ....*....|....*.
gi 1131020733 243 FIGKVAFFTVDVIGKE 258
Cdd:PRK10851  236 FMGEVNRLQGTIRGGQ 251
ProV COG4175
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and ...
 8-247 3.77e-85

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


Pssm-ID: 443334 [Multi-domain]  Cd Length: 389  Bit Score: 263.12  E-value: 3.77e-85
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131020733   8 LRLENVTKIF-----------KDKKNNTE-------VIAVNNSTFEIKPGELITLLGPSGCGKTTTLRMVAGFELPTKGK 69
Cdd:COG4175     4 IEVRNLYKIFgkrperalkllDQGKSKDEilektgqTVGVNDASFDVEEGEIFVIMGLSGSGKSTLVRCLNRLIEPTAGE 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131020733  70 IYIGNEDVTFLPPNK------RDTATVFQSYGLFPHMTVFDNVAYGLKLRKLSREEIEKRVFEALEMVGLKDLASRAPSR 143
Cdd:COG4175    84 VLIDGEDITKLSKKElrelrrKKMSMVFQHFALLPHRTVLENVAFGLEIQGVPKAERRERAREALELVGLAGWEDSYPDE 163

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131020733 144 LSGGQQQRVTLARSIIVEPAILLLDEPLSNLDALLREQMRIEIKKIQRKLGITAIYVTHDRVEAMSLSDRIIVMKDGKIM 223
Cdd:COG4175   164 LSGGMQQRVGLARALATDPDILLMDEAFSALDPLIRREMQDELLELQAKLKKTIVFITHDLDEALRLGDRIAIMKDGRIV 243

                         250       260
                  ....*....|....*....|....
gi 1131020733 224 QIGTPVEIYEDPISKFVAGFIGKV 247
Cdd:COG4175   244 QIGTPEEILTNPANDYVADFVEDV 267
ABC_Pro_Gly_Betaine cd03294
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ...
 8-244 1.82e-84

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: 257.19  E-value: 1.82e-84
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131020733   8 LRLENVTKIF-----------KDKKNNTE-------VIAVNNSTFEIKPGELITLLGPSGCGKTTTLRMVAGFELPTKGK 69
Cdd:cd03294     1 IKIKGLYKIFgknpqkafkllAKGKSKEEilkktgqTVGVNDVSLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGK 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131020733  70 IYIGNEDVTFLPPN------KRDTATVFQSYGLFPHMTVFDNVAYGLKLRKLSREEIEKRVFEALEMVGLKDLASRAPSR 143
Cdd:cd03294    81 VLIDGQDIAAMSRKelrelrRKKISMVFQSFALLPHRTVLENVAFGLEVQGVPRAEREERAAEALELVGLEGWEHKYPDE 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131020733 144 LSGGQQQRVTLARSIIVEPAILLLDEPLSNLDALLREQMRIEIKKIQRKLGITAIYVTHDRVEAMSLSDRIIVMKDGKIM 223
Cdd:cd03294   161 LSGGMQQRVGLARALAVDPDILLMDEAFSALDPLIRREMQDELLRLQAELQKTIVFITHDLDEALRLGDRIAIMKDGRLV 240

                         250       260
                  ....*....|....*....|.
gi 1131020733 224 QIGTPVEIYEDPISKFVAGFI 244
Cdd:cd03294   241 QVGTPEEILTNPANDYVREFF 261
LolD COG1136
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
8-222 1.25e-76

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


Pssm-ID: 440751 [Multi-domain]  Cd Length: 227  Bit Score: 235.32  E-value: 1.25e-76
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131020733   8 LRLENVTKIFKDKKNntEVIAVNNSTFEIKPGELITLLGPSGCGKTTTLRMVAGFELPTKGKIYIGNEDVTFLPPNKRDT 87
Cdd:COG1136     5 LELRNLTKSYGTGEG--EVTALRGVSLSIEAGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVLIDGQDISSLSERELAR 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131020733  88 ------ATVFQSYGLFPHMTVFDNVAYGLKLRKLSREEIEKRVFEALEMVGLKDLASRAPSRLSGGQQQRVTLARSIIVE 161
Cdd:COG1136    83 lrrrhiGFVFQFFNLLPELTALENVALPLLLAGVSRKERRERARELLERVGLGDRLDHRPSQLSGGQQQRVAIARALVNR 162

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1131020733 162 PAILLLDEPLSNLDALLREQ-MRIeIKKIQRKLGITAIYVTHDRvEAMSLSDRIIVMKDGKI 222
Cdd:COG1136   163 PKLILADEPTGNLDSKTGEEvLEL-LRELNRELGTTIVMVTHDP-ELAARADRVIRLRDGRI 222
ABC_MJ0796_LolCDE_FtsE cd03255
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ...
 8-222 4.50e-76

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: 233.92  E-value: 4.50e-76
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131020733   8 LRLENVTKIFKdkKNNTEVIAVNNSTFEIKPGELITLLGPSGCGKTTTLRMVAGFELPTKGKIYIGNEDVTFLPPNKRD- 86
Cdd:cd03255     1 IELKNLSKTYG--GGGEKVQALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRVDGTDISKLSEKELAa 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131020733  87 -----TATVFQSYGLFPHMTVFDNVAYGLKLRKLSREEIEKRVFEALEMVGLKDLASRAPSRLSGGQQQRVTLARSIIVE 161
Cdd:cd03255    79 frrrhIGFVFQSFNLLPDLTALENVELPLLLAGVPKKERRERAEELLERVGLGDRLNHYPSELSGGQQQRVAIARALAND 158

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1131020733 162 PAILLLDEPLSNLDALLREQMRIEIKKIQRKLGITAIYVTHDRVEAmSLSDRIIVMKDGKI 222
Cdd:cd03255   159 PKIILADEPTGNLDSETGKEVMELLRELNKEAGTTIVVVTHDPELA-EYADRIIELRDGKI 218
GsiA COG1123
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ...
 8-235 6.40e-75

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: 240.58  E-value: 6.40e-75
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131020733   8 LRLENVTKIFKDKKNnTEVIAVNNSTFEIKPGELITLLGPSGCGKTTTLRMVAGFELPTKGKIYIGNEDVTFLPPNK--- 84
Cdd:COG1123   261 LEVRNLSKRYPVRGK-GGVRAVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRPTSGSILFDGKDLTKLSRRSlre 339

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131020733  85 --RDTATVFQS-YG-LFPHMTVFDNVAYGLKLRK-LSREEIEKRVFEALEMVGL-KDLASRAPSRLSGGQQQRVTLARSI 158
Cdd:COG1123   340 lrRRVQMVFQDpYSsLNPRMTVGDIIAEPLRLHGlLSRAERRERVAELLERVGLpPDLADRYPHELSGGQRQRVAIARAL 419

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131020733 159 IVEPAILLLDEPLSNLDALLREQMRIEIKKIQRKLGITAIYVTHDrveaMSL----SDRIIVMKDGKIMQIGTPVEIYED 234
Cdd:COG1123   420 ALEPKLLILDEPTSALDVSVQAQILNLLRDLQRELGLTYLFISHD----LAVvryiADRVAVMYDGRIVEDGPTEEVFAN 495


                  .
gi 1131020733 235 P 235
Cdd:COG1123   496 P 496
ABC_Class3 cd03229
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ...
 8-221 1.10e-73

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: 226.30  E-value: 1.10e-73
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131020733   8 LRLENVTKIFKDKknntevIAVNNSTFEIKPGELITLLGPSGCGKTTTLRMVAGFELPTKGKIYIGNEDVT----FLPPN 83
Cdd:cd03229     1 LELKNVSKRYGQK------TVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGEDLTdledELPPL 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131020733  84 KRDTATVFQSYGLFPHMTVFDNVAYGlklrklsreeiekrvfealemvglkdlasrapsrLSGGQQQRVTLARSIIVEPA 163
Cdd:cd03229    75 RRRIGMVFQDFALFPHLTVLENIALG----------------------------------LSGGQQQRVALARALAMDPD 120

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1131020733 164 ILLLDEPLSNLDALLREQMRIEIKKIQRKLGITAIYVTHDRVEAMSLSDRIIVMKDGK 221
Cdd:cd03229   121 VLLLDEPTSALDPITRREVRALLKSLQAQLGITVVLVTHDLDEAARLADRVVVLRDGK 178
proV TIGR01186
glycine betaine/L-proline transport ATP binding subunit; This model describes the glycine ...
 27-247 2.37e-73

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: 232.05  E-value: 2.37e-73
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131020733  27 IAVNNSTFEIKPGELITLLGPSGCGKTTTLRMVAGFELPTKGKIYIGNEDVTFLPP------NKRDTATVFQSYGLFPHM 100
Cdd:TIGR01186   7 KGVNDADLAIAKGEIFVIMGLSGSGKSTTVRMLNRLIEPTAGQIFIDGENIMKQSPvelrevRRKKIGMVFQQFALFPHM 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131020733 101 TVFDNVAYGLKLRKLSREEIEKRVFEALEMVGLKDLASRAPSRLSGGQQQRVTLARSIIVEPAILLLDEPLSNLDALLRE 180
Cdd:TIGR01186  87 TILQNTSLGPELLGWPEQERKEKALELLKLVGLEEYEHRYPDELSGGMQQRVGLARALAAEPDILLMDEAFSALDPLIRD 166

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1131020733 181 QMRIEIKKIQRKLGITAIYVTHDRVEAMSLSDRIIVMKDGKIMQIGTPVEIYEDPISKFVAGFIGKV 247
Cdd:TIGR01186 167 SMQDELKKLQATLQKTIVFITHDLDEAIRIGDRIVIMKAGEIVQVGTPDEILRNPANEYVEEFIGKV 233
ThiQ COG3840
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
8-245 3.53e-72

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


Pssm-ID: 443051 [Multi-domain]  Cd Length: 232  Bit Score: 224.25  E-value: 3.53e-72
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131020733   8 LRLENVTKIFkdkkNNTEViavnNSTFEIKPGELITLLGPSGCGKTTTLRMVAGFELPTKGKIYIGNEDVTFLPPNKRDT 87
Cdd:COG3840     2 LRLDDLTYRY----GDFPL----RFDLTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILWNGQDLTALPPAERPV 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131020733  88 ATVFQSYGLFPHMTVFDNVAYGLKLR-KLSREEiEKRVFEALEMVGLKDLASRAPSRLSGGQQQRVTLARSIIVEPAILL 166
Cdd:COG3840    74 SMLFQENNLFPHLTVAQNIGLGLRPGlKLTAEQ-RAQVEQALERVGLAGLLDRLPGQLSGGQRQRVALARCLVRKRPILL 152

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1131020733 167 LDEPLSNLDALLREQMRIEIKKIQRKLGITAIYVTHDRVEAMSLSDRIIVMKDGKIMQIGTPVEIYEDPISKFVAGFIG 245
Cdd:COG3840   153 LDEPFSALDPALRQEMLDLVDELCRERGLTVLMVTHDPEDAARIADRVLLVADGRIAADGPTAALLDGEPPPALAAYLG 231
EcfA2 COG1122
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ...
 8-235 5.43e-71

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: 221.05  E-value: 5.43e-71
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131020733   8 LRLENVTKIFKDKKNnteviAVNNSTFEIKPGELITLLGPSGCGKTTTLRMVAGFELPTKGKIYIGNEDVTFLPPNK--R 85
Cdd:COG1122     1 IELENLSFSYPGGTP-----ALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVDGKDITKKNLRElrR 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131020733  86 DTATVFQS--YGLFpHMTVFDNVAYGLKLRKLSREEIEKRVFEALEMVGLKDLASRAPSRLSGGQQQRVTLARSIIVEPA 163
Cdd:COG1122    76 KVGLVFQNpdDQLF-APTVEEDVAFGPENLGLPREEIRERVEEALELVGLEHLADRPPHELSGGQKQRVAIAGVLAMEPE 154

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1131020733 164 ILLLDEPLSNLDALLREQMRIEIKKIQRKlGITAIYVTHDRVEAMSLSDRIIVMKDGKIMQIGTPVEIYEDP 235
Cdd:COG1122   155 VLVLDEPTAGLDPRGRRELLELLKRLNKE-GKTVIIVTHDLDLVAELADRVIVLDDGRIVADGTPREVFSDY 225
MlaF COG1127
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ...
 8-231 5.23e-70

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: 219.08  E-value: 5.23e-70
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131020733   8 LRLENVTKIFKDKKnnteviAVNNSTFEIKPGELITLLGPSGCGKTTTLRMVAGFELPTKGKIYIGNEDVTFLPPNKRDT 87
Cdd:COG1127     6 IEVRNLTKSFGDRV------VLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEILVDGQDITGLSEKELYE 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131020733  88 A-----TVFQSYGLFPHMTVFDNVAYGLK-LRKLSREEIEKRVFEALEMVGLKDLASRAPSRLSGGQQQRVTLARSIIVE 161
Cdd:COG1127    80 LrrrigMLFQGGALFDSLTVFENVAFPLReHTDLSEAEIRELVLEKLELVGLPGAADKMPSELSGGMRKRVALARALALD 159

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1131020733 162 PAILLLDEPLSNLD----ALLREQmrieIKKIQRKLGITAIYVTHDRVEAMSLSDRIIVMKDGKIMQIGTPVEI 231
Cdd:COG1127   160 PEILLYDEPTAGLDpitsAVIDEL----IRELRDELGLTSVVVTHDLDSAFAIADRVAVLADGKIIAEGTPEEL 229
GlnQ COG1126
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ...
 8-247 2.49e-68

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


Pssm-ID: 440743 [Multi-domain]  Cd Length: 239  Bit Score: 214.86  E-value: 2.49e-68
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131020733   8 LRLENVTKIFKDkknnTEVIavNNSTFEIKPGELITLLGPSGCGKTTTLRMVAGFELPTKGKIYIGNEDVTflPPNK--- 84
Cdd:COG1126     2 IEIENLHKSFGD----LEVL--KGISLDVEKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTITVDGEDLT--DSKKdin 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131020733  85 ---RDTATVFQSYGLFPHMTVFDNVAYGL-KLRKLSREEIEKRVFEALEMVGLKDLASRAPSRLSGGQQQRVTLARSIIV 160
Cdd:COG1126    74 klrRKVGMVFQQFNLFPHLTVLENVTLAPiKVKKMSKAEAEERAMELLERVGLADKADAYPAQLSGGQQQRVAIARALAM 153

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131020733 161 EPAILLLDEPLSNLDAllreQMRIEIKKIQRKL---GITAIYVTHDRVEAMSLSDRIIVMKDGKIMQIGTPVEIYEDPIS 237
Cdd:COG1126   154 EPKVMLFDEPTSALDP----ELVGEVLDVMRDLakeGMTMVVVTHEMGFAREVADRVVFMDGGRIVEEGPPEEFFENPQH 229

                         250
                  ....*....|
gi 1131020733 238 KFVAGFIGKV 247
Cdd:COG1126   230 ERTRAFLSKV 239
FtsE COG2884
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
8-222 1.90e-67

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


Pssm-ID: 442130 [Multi-domain]  Cd Length: 223  Bit Score: 211.83  E-value: 1.90e-67
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131020733   8 LRLENVTKIFKDKKnntevIAVNNSTFEIKPGELITLLGPSGCGKTTTLRMVAGFELPTKGKIYIGNEDVTFLPPNK--- 84
Cdd:COG2884     2 IRFENVSKRYPGGR-----EALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLVNGQDLSRLKRREipy 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131020733  85 --RDTATVFQSYGLFPHMTVFDNVAYGLKLRKLSREEIEKRVFEALEMVGLKDLASRAPSRLSGGQQQRVTLARSIIVEP 162
Cdd:COG2884    77 lrRRIGVVFQDFRLLPDRTVYENVALPLRVTGKSRKEIRRRVREVLDLVGLSDKAKALPHELSGGEQQRVAIARALVNRP 156

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1131020733 163 AILLLDEPLSNLD-ALLREQMRIeIKKIQRkLGITAIYVTHDR--VEAMSLsdRIIVMKDGKI 222
Cdd:COG2884   157 ELLLADEPTGNLDpETSWEIMEL-LEEINR-RGTTVLIATHDLelVDRMPK--RVLELEDGRL 215
CcmA COG1131
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
8-231 2.62e-67

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


Pssm-ID: 440746 [Multi-domain]  Cd Length: 236  Bit Score: 211.85  E-value: 2.62e-67
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131020733   8 LRLENVTKIFKDKKnnteviAVNNSTFEIKPGELITLLGPSGCGKTTTLRMVAGFELPTKGKIYIGNEDVTFLPPN-KRD 86
Cdd:COG1131     1 IEVRGLTKRYGDKT------ALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRVLGEDVARDPAEvRRR 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131020733  87 TATVFQSYGLFPHMTVFDNVAYGLKLRKLSREEIEKRVFEALEMVGLKDLASRAPSRLSGGQQQRVTLARSIIVEPAILL 166
Cdd:COG1131    75 IGYVPQEPALYPDLTVRENLRFFARLYGLPRKEARERIDELLELFGLTDAADRKVGTLSGGMKQRLGLALALLHDPELLI 154

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1131020733 167 LDEPLSNLDALLREQMRIEIKKIQRKlGITAIYVTHDRVEAMSLSDRIIVMKDGKIMQIGTPVEI 231
Cdd:COG1131   155 LDEPTSGLDPEARRELWELLRELAAE-GKTVLLSTHYLEEAERLCDRVAIIDKGRIVADGTPDEL 218
ABC_ModC_molybdenum_transporter cd03297
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ...
 38-226 4.92e-67

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: 210.61  E-value: 4.92e-67
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131020733  38 PGELITLLGPSGCGKTTTLRMVAGFELPTKGKIYIGN------EDVTFLPPNKRDTATVFQSYGLFPHMTVFDNVAYGLK 111
Cdd:cd03297    22 NEEVTGIFGASGAGKSTLLRCIAGLEKPDGGTIVLNGtvlfdsRKKINLPPQQRKIGLVFQQYALFPHLNVRENLAFGLK 101

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131020733 112 lrKLSREEIEKRVFEALEMVGLKDLASRAPSRLSGGQQQRVTLARSIIVEPAILLLDEPLSNLDALLREQMRIEIKKIQR 191
Cdd:cd03297   102 --RKRNREDRISVDELLDLLGLDHLLNRYPAQLSGGEKQRVALARALAAQPELLLLDEPFSALDRALRLQLLPELKQIKK 179

                         170       180       190
                  ....*....|....*....|....*....|....*
gi 1131020733 192 KLGITAIYVTHDRVEAMSLSDRIIVMKDGKIMQIG 226
Cdd:cd03297   180 NLNIPVIFVTHDLSEAEYLADRIVVMEDGRLQYIG 214
PhnC COG3638
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and ...
 8-234 2.84e-65

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


Pssm-ID: 442855 [Multi-domain]  Cd Length: 249  Bit Score: 207.22  E-value: 2.84e-65
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131020733   8 LRLENVTKIFKDKKnntevIAVNNSTFEIKPGELITLLGPSGCGKTTTLRMVAGFELPTKGKIYIGNEDVTFLPPNK--- 84
Cdd:COG3638     3 LELRNLSKRYPGGT-----PALDDVSLEIERGEFVALIGPSGAGKSTLLRCLNGLVEPTSGEILVDGQDVTALRGRAlrr 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131020733  85 --RDTATVFQSYGLFPHMTVFDNVAYG-------LK--LRKLSREEIEkRVFEALEMVGLKDLASRAPSRLSGGQQQRVT 153
Cdd:COG3638    78 lrRRIGMIFQQFNLVPRLSVLTNVLAGrlgrtstWRslLGLFPPEDRE-RALEALERVGLADKAYQRADQLSGGQQQRVA 156

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131020733 154 LARSIIVEPAILLLDEPLSNLD-ALLREQMRIeIKKIQRKLGITAIYVTHDrVE-AMSLSDRIIVMKDGKIMQIGTPVEI 231
Cdd:COG3638   157 IARALVQEPKLILADEPVASLDpKTARQVMDL-LRRIAREDGITVVVNLHQ-VDlARRYADRIIGLRDGRVVFDGPPAEL 234


                  ...
gi 1131020733 232 YED 234
Cdd:COG3638   235 TDA 237
ABC_cobalt_CbiO_domain1 cd03225
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ...
 9-221 3.29e-65

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: 205.78  E-value: 3.29e-65
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131020733   9 RLENVTKIFkdkkNNTEVIAVNNSTFEIKPGELITLLGPSGCGKTTTLRMVAGFELPTKGKIYIGNEDVTFLPPNK--RD 86
Cdd:cd03225     1 ELKNLSFSY----PDGARPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDLTKLSLKElrRK 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131020733  87 TATVFQsyglFP-HM----TVFDNVAYGLKLRKLSREEIEKRVFEALEMVGLKDLASRAPSRLSGGQQQRVTLARSIIVE 161
Cdd:cd03225    77 VGLVFQ----NPdDQffgpTVEEEVAFGLENLGLPEEEIEERVEEALELVGLEGLRDRSPFTLSGGQKQRVAIAGVLAMD 152

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131020733 162 PAILLLDEPLSNLDALLREQMRIEIKKIQRKlGITAIYVTHDRVEAMSLSDRIIVMKDGK 221
Cdd:cd03225   153 PDILLLDEPTAGLDPAGRRELLELLKKLKAE-GKTIIIVTHDLDLLLELADRVIVLEDGK 211
TauB COG4525
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
8-242 1.03e-63

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


Pssm-ID: 443596 [Multi-domain]  Cd Length: 262  Bit Score: 203.56  E-value: 1.03e-63
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131020733   8 LRLENVTKIFKDKKNNTEVIA-VNnstFEIKPGELITLLGPSGCGKTTTLRMVAGFELPTKGKIYIGNEDVTFlPPNKRd 86
Cdd:COG4525     4 LTVRHVSVRYPGGGQPQPALQdVS---LTIESGEFVVALGASGCGKTTLLNLIAGFLAPSSGEITLDGVPVTG-PGADR- 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131020733  87 tATVFQSYGLFPHMTVFDNVAYGLKLRKLSREEIEKRVFEALEMVGLKDLASRAPSRLSGGQQQRVTLARSIIVEPAILL 166
Cdd:COG4525    79 -GVVFQKDALLPWLNVLDNVAFGLRLRGVPKAERRARAEELLALVGLADFARRRIWQLSGGMRQRVGIARALAADPRFLL 157

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1131020733 167 LDEPLSNLDALLREQMRIEIKKIQRKLGITAIYVTHDRVEAMSLSDRIIVMKD--GKImqigtpVEIYEDPISK-FVAG 242
Cdd:COG4525   158 MDEPFGALDALTREQMQELLLDVWQRTGKGVFLITHSVEEALFLATRLVVMSPgpGRI------VERLELDFSRrFLAG 230
DppF COG1124
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ...
 8-235 3.08e-63

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: 201.96  E-value: 3.08e-63
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131020733   8 LRLENVTKIFKDKKNNTEViaVNNSTFEIKPGELITLLGPSGCGKTTTLRMVAGFELPTKGKIYIGNEDVT--FLPPNKR 85
Cdd:COG1124     2 LEVRNLSVSYGQGGRRVPV--LKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVTFDGRPVTrrRRKAFRR 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131020733  86 DTATVFQ-SYG-LFPHMTVFDNVAYGLKLRKLSreEIEKRVFEALEMVGL-KDLASRAPSRLSGGQQQRVTLARSIIVEP 162
Cdd:COG1124    80 RVQMVFQdPYAsLHPRHTVDRILAEPLRIHGLP--DREERIAELLEQVGLpPSFLDRYPHQLSGGQRQRVAIARALILEP 157

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1131020733 163 AILLLDEPLSNLDALLreQMRI--EIKKIQRKLGITAIYVTHDR--VEAMslSDRIIVMKDGKIMQIGTPVEIYEDP 235
Cdd:COG1124   158 ELLLLDEPTSALDVSV--QAEIlnLLKDLREERGLTYLFVSHDLavVAHL--CDRVAVMQNGRIVEELTVADLLAGP 230
AbcC COG1135
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
8-248 8.36e-63

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


Pssm-ID: 440750 [Multi-domain]  Cd Length: 339  Bit Score: 203.77  E-value: 8.36e-63
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131020733   8 LRLENVTKIFKDKKNntEVIAVNNSTFEIKPGELITLLGPSGCGKTTTLRMVAGFELPTKGKIYIGNEDVTFLPPNK--- 84
Cdd:COG1135     2 IELENLSKTFPTKGG--PVTALDDVSLTIEKGEIFGIIGYSGAGKSTLIRCINLLERPTSGSVLVDGVDLTALSERElra 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131020733  85 --RDTATVFQSYGLFPHMTVFDNVAYGLKLRKLSREEIEKRVFEALEMVGLKDLASRAPSRLSGGQQQRVTLARSIIVEP 162
Cdd:COG1135    80 arRKIGMIFQHFNLLSSRTVAENVALPLEIAGVPKAEIRKRVAELLELVGLSDKADAYPSQLSGGQKQRVGIARALANNP 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131020733 163 AILLLDEPLSNLD--------ALLreqmrieiKKIQRKLGITAIYVTHDrveaMS----LSDRIIVMKDGKIMQIGTPVE 230
Cdd:COG1135   160 KVLLCDEATSALDpettrsilDLL--------KDINRELGLTIVLITHE----MDvvrrICDRVAVLENGRIVEQGPVLD 227

                         250
                  ....*....|....*...
gi 1131020733 231 IYEDPISKFVAGFIGKVA 248
Cdd:COG1135   228 VFANPQSELTRRFLPTVL 245
ModC COG4148
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ...
 34-339 9.55e-63

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: 204.18  E-value: 9.55e-63
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131020733  34 FEIKPGELITLLGPSGCGKTTTLRMVAGFELPTKGKIYIGNEDV------TFLPPNKRDTATVFQSYGLFPHMTVFDNVA 107
Cdd:COG4148    20 FTLPGRGVTALFGPSGSGKTTLLRAIAGLERPDSGRIRLGGEVLqdsargIFLPPHRRRIGYVFQEARLFPHLSVRGNLL 99

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131020733 108 YGLKLRKLSREEIEkrvFEAL-EMVGLKDLASRAPSRLSGGQQQRVTLARSIIVEPAILLLDEPLSNLDALLREQMRIEI 186
Cdd:COG4148   100 YGRKRAPRAERRIS---FDEVvELLGIGHLLDRRPATLSGGERQRVAIGRALLSSPRLLLMDEPLAALDLARKAEILPYL 176

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131020733 187 KKIQRKLGITAIYVTHDRVEAMSLSDRIIVMKDGKIMQIGTPVEIYEDPISKFVAGFIGKVAFFTVDVIGKENDN--III 264
Cdd:COG4148   177 ERLRDELDIPILYVSHSLDEVARLADHVVLLEQGRVVASGPLAEVLSRPDLLPLAGGEEAGSVLEATVAAHDPDYglTRL 256

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1131020733 265 DFKGKKLIMKkyDNDLDPGDKgV---LMARPESLILkEEKEGL-IegkikINVyLGNTVESFIDTEYGEIMVQIDNPGQ 339
Cdd:COG4148   257 ALGGGRLWVP--RLDLPPGTR-VrvrIRARDVSLAL-EPPEGSsI-----LNI-LPGRVVEIEPADGGQVLVRLDLGGQ 325
ABC_NikE_OppD_transporters cd03257
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ...
 8-226 2.49e-62

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: 198.88  E-value: 2.49e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131020733   8 LRLENVTKIFKDKKNntEVIAVNNSTFEIKPGELITLLGPSGCGKTTTLRMVAGFELPTKGKIYIGNEDVT-----FLPP 82
Cdd:cd03257     2 LEVKNLSVSFPTGGG--SVKALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGKDLLklsrrLRKI 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131020733  83 NKRDTATVFQSYG--LFPHMTVFDNVAYGLKLRKLSR--EEIEKRVFEALEMVGL-KDLASRAPSRLSGGQQQRVTLARS 157
Cdd:cd03257    80 RRKEIQMVFQDPMssLNPRMTIGEQIAEPLRIHGKLSkkEARKEAVLLLLVGVGLpEEVLNRYPHELSGGQRQRVAIARA 159

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131020733 158 IIVEPAILLLDEPLSNLDALLREQMRIEIKKIQRKLGITAIYVTHD-RVeAMSLSDRIIVMKDGKIMQIG 226
Cdd:cd03257   160 LALNPKLLIADEPTSALDVSVQAQILDLLKKLQEELGLTLLFITHDlGV-VAKIADRVAVMYAGKIVEEG 228
ABC_MetN_methionine_transporter cd03258
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ...
 8-235 2.70e-62

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: 198.96  E-value: 2.70e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131020733   8 LRLENVTKIFKDKKNntEVIAVNNSTFEIKPGELITLLGPSGCGKTTTLRMVAGFELPTKGKIYIGNEDVTFLPPNK--- 84
Cdd:cd03258     2 IELKNVSKVFGDTGG--KVTALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGSVLVDGTDLTLLSGKElrk 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131020733  85 --RDTATVFQSYGLFPHMTVFDNVAYGLKLRKLSREEIEKRVFEALEMVGLKDLASRAPSRLSGGQQQRVTLARSIIVEP 162
Cdd:cd03258    80 arRRIGMIFQHFNLLSSRTVFENVALPLEIAGVPKAEIEERVLELLELVGLEDKADAYPAQLSGGQKQRVGIARALANNP 159

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1131020733 163 AILLLDEPLSNLDALLREQMRIEIKKIQRKLGITAIYVTHDRVEAMSLSDRIIVMKDGKIMQIGTPVEIYEDP 235
Cdd:cd03258   160 KVLLCDEATSALDPETTQSILALLRDINRELGLTIVLITHEMEVVKRICDRVAVMEKGEVVEEGTVEEVFANP 232
ABC_PhnC_transporter cd03256
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ...
 8-234 1.61e-61

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: 197.41  E-value: 1.61e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131020733   8 LRLENVTKIFKDKKNnteviAVNNSTFEIKPGELITLLGPSGCGKTTTLRMVAGFELPTKGKIYIGNEDVTFLPPNK--- 84
Cdd:cd03256     1 IEVENLSKTYPNGKK-----ALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGTDINKLKGKAlrq 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131020733  85 --RDTATVFQSYGLFPHMTVFDNVAYGL---------KLRKLSREEIEkRVFEALEMVGLKDLASRAPSRLSGGQQQRVT 153
Cdd:cd03256    76 lrRQIGMIFQQFNLIERLSVLENVLSGRlgrrstwrsLFGLFPKEEKQ-RALAALERVGLLDKAYQRADQLSGGQQQRVA 154

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131020733 154 LARSIIVEPAILLLDEPLSNLD-ALLREQMRIeIKKIQRKLGITAIYVTHDRVEAMSLSDRIIVMKDGKIMQIGTPVEIY 232
Cdd:cd03256   155 IARALMQQPKLILADEPVASLDpASSRQVMDL-LKRINREEGITVIVSLHQVDLAREYADRIVGLKDGRIVFDGPPAELT 233


                  ..
gi 1131020733 233 ED 234
Cdd:cd03256   234 DE 235
ABC_Org_Solvent_Resistant cd03261
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ...
 8-231 3.19e-61

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: 196.18  E-value: 3.19e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131020733   8 LRLENVTKIFKDKknnteVIaVNNSTFEIKPGELITLLGPSGCGKTTTLRMVAGFELPTKGKIYIGNEDVTFLPPNK--- 84
Cdd:cd03261     1 IELRGLTKSFGGR-----TV-LKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGEDISGLSEAElyr 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131020733  85 --RDTATVFQSYGLFPHMTVFDNVAYGLK-LRKLSREEIEKRVFEALEMVGLKDLASRAPSRLSGGQQQRVTLARSIIVE 161
Cdd:cd03261    75 lrRRMGMLFQSGALFDSLTVFENVAFPLReHTRLSEEEIREIVLEKLEAVGLRGAEDLYPAELSGGMKKRVALARALALD 154

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131020733 162 PAILLLDEPLSNLDALLREQMRIEIKKIQRKLGITAIYVTHDRVEAMSLSDRIIVMKDGKIMQIGTPVEI 231
Cdd:cd03261   155 PELLLYDEPTAGLDPIASGVIDDLIRSLKKELGLTSIMVTHDLDTAFAIADRIAVLYDGKIVAEGTPEEL 224
FepC COG1120
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ...
 8-231 7.85e-61

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: 196.03  E-value: 7.85e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131020733   8 LRLENVTKIFKDKknntevIAVNNSTFEIKPGELITLLGPSGCGKTTTLRMVAGFELPTKGKIYIGNEDVTFLPPNK--R 85
Cdd:COG1120     2 LEAENLSVGYGGR------PVLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDGRDLASLSRRElaR 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131020733  86 DTATVFQSYGLFPHMTVFDNVAYGLK-----LRKLSREEIEKrVFEALEMVGLKDLASRAPSRLSGGQQQRVTLARSIIV 160
Cdd:COG1120    76 RIAYVPQEPPAPFGLTVRELVALGRYphlglFGRPSAEDREA-VEEALERTGLEHLADRPVDELSGGERQRVLIARALAQ 154

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1131020733 161 EPAILLLDEPLSNLDalLREQMRI--EIKKIQRKLGITAIYVTHDRVEAMSLSDRIIVMKDGKIMQIGTPVEI 231
Cdd:COG1120   155 EPPLLLLDEPTSHLD--LAHQLEVleLLRRLARERGRTVVMVLHDLNLAARYADRLVLLKDGRIVAQGPPEEV 225
FtsE TIGR02673
cell division ATP-binding protein FtsE; This model describes FtsE, a member of the ABC ...
 8-221 1.03e-58

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: 189.00  E-value: 1.03e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131020733   8 LRLENVTKIFkdkknNTEVIAVNNSTFEIKPGELITLLGPSGCGKTTTLRMVAGFELPTKGKIYIGNEDVTFLPPN---- 83
Cdd:TIGR02673   2 IEFHNVSKAY-----PGGVAALHDVSLHIRKGEFLFLTGPSGAGKTTLLKLLYGALTPSRGQVRIAGEDVNRLRGRqlpl 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131020733  84 -KRDTATVFQSYGLFPHMTVFDNVAYGLKLRKLSREEIEKRVFEALEMVGLKDLASRAPSRLSGGQQQRVTLARSIIVEP 162
Cdd:TIGR02673  77 lRRRIGVVFQDFRLLPDRTVYENVALPLEVRGKKEREIQRRVGAALRQVGLEHKADAFPEQLSGGEQQRVAIARAIVNSP 156

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1131020733 163 AILLLDEPLSNLDALLREQ-MRIeikkIQR--KLGITAIYVTHDRVEAMSLSDRIIVMKDGK 221
Cdd:TIGR02673 157 PLLLADEPTGNLDPDLSERiLDL----LKRlnKRGTTVIVATHDLSLVDRVAHRVIILDDGR 214
ABC_Mj1267_LivG_branched cd03219
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ...
 8-235 1.24e-58

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: 189.57  E-value: 1.24e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131020733   8 LRLENVTKIFKdkknntEVIAVNNSTFEIKPGELITLLGPSGCGKTTTLRMVAGFELPTKGKIYIGNEDVTFLPPNKRDT 87
Cdd:cd03219     1 LEVRGLTKRFG------GLVALDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFDGEDITGLPPHEIAR 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131020733  88 ATV---FQSYGLFPHMTVFDNVAYGLKLRK----------LSREEIEKRVFEALEMVGLKDLASRAPSRLSGGQQQRVTL 154
Cdd:cd03219    75 LGIgrtFQIPRLFPELTVLENVMVAAQARTgsglllararREEREARERAEELLERVGLADLADRPAGELSYGQQRRLEI 154

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131020733 155 ARSIIVEPAILLLDEPLSNLDALLREQMRIEIKKIqRKLGITAIYVTHDRVEAMSLSDRIIVMKDGKIMQIGTPVEIYED 234
Cdd:cd03219   155 ARALATDPKLLLLDEPAAGLNPEETEELAELIREL-RERGITVLLVEHDMDVVMSLADRVTVLDQGRVIAEGTPDEVRNN 233


                  .
gi 1131020733 235 P 235
Cdd:cd03219   234 P 234
ABC_HisP_GlnQ cd03262
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ...
 8-222 1.52e-58

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: 188.51  E-value: 1.52e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131020733   8 LRLENVTKIFKDKKnnteviAVNNSTFEIKPGELITLLGPSGCGKTTTLRMVAGFELPTKGKIYIGNEDVTFLPPN---- 83
Cdd:cd03262     1 IEIKNLHKSFGDFH------VLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIDGLKLTDDKKNinel 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131020733  84 KRDTATVFQSYGLFPHMTVFDNVAYGL-KLRKLSREEIEKRVFEALEMVGLKDLASRAPSRLSGGQQQRVTLARSIIVEP 162
Cdd:cd03262    75 RQKVGMVFQQFNLFPHLTVLENITLAPiKVKGMSKAEAEERALELLEKVGLADKADAYPAQLSGGQQQRVAIARALAMNP 154

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1131020733 163 AILLLDEPLSNLDAllreQMRIEIKKIQRKL---GITAIYVTHDRVEAMSLSDRIIVMKDGKI 222
Cdd:cd03262   155 KVMLFDEPTSALDP----ELVGEVLDVMKDLaeeGMTMVVVTHEMGFAREVADRVIFMDDGRI 213
ABC_PstB_phosphate_transporter cd03260
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ...
 8-231 2.27e-57

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: 186.23  E-value: 2.27e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131020733   8 LRLENVTKIFKDKKnnteviAVNNSTFEIKPGELITLLGPSGCGKTTTLRMVAGF-----ELPTKGKIYIGNEDVTFLPP 82
Cdd:cd03260     1 IELRDLNVYYGDKH------ALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRLndlipGAPDEGEVLLDGKDIYDLDV 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131020733  83 N----KRDTATVFQSYGLFPhMTVFDNVAYGLKLR-KLSREEIEKRVFEALEMVGLKDLASR--APSRLSGGQQQRVTLA 155
Cdd:cd03260    75 DvlelRRRVGMVFQKPNPFP-GSIYDNVAYGLRLHgIKLKEELDERVEEALRKAALWDEVKDrlHALGLSGGQQQRLCLA 153

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1131020733 156 RSIIVEPAILLLDEPLSNLDALLREqmRIE--IKKIQRKlgITAIYVTHDRVEAMSLSDRIIVMKDGKIMQIGTPVEI 231
Cdd:cd03260   154 RALANEPEVLLLDEPTSALDPISTA--KIEelIAELKKE--YTIVIVTHNMQQAARVADRTAFLLNGRLVEFGPTEQI 227
GsiA COG1123
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ...
 8-235 2.67e-57

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: 194.35  E-value: 2.67e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131020733   8 LRLENVTKIFKDKknntEVIAVNNSTFEIKPGELITLLGPSGCGKTTTLRMVAG---FELPTKGKIYIGNEDVTFLPPNK 84
Cdd:COG1123     5 LEVRDLSVRYPGG----DVPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGllpHGGRISGEVLLDGRDLLELSEAL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131020733  85 R--DTATVFQSYG--LFPhMTVFDNVAYGLKLRKLSREEIEKRVFEALEMVGLKDLASRAPSRLSGGQQQRVTLARSIIV 160
Cdd:COG1123    81 RgrRIGMVFQDPMtqLNP-VTVGDQIAEALENLGLSRAEARARVLELLEAVGLERRLDRYPHQLSGGQRQRVAIAMALAL 159

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1131020733 161 EPAILLLDEPLSNLDALLREQMRIEIKKIQRKLGITAIYVTHDRVEAMSLSDRIIVMKDGKIMQIGTPVEIYEDP 235
Cdd:COG1123   160 DPDLLIADEPTTALDVTTQAEILDLLRELQRERGTTVLLITHDLGVVAEIADRVVVMDDGRIVEDGPPEEILAAP 234
LivG COG0411
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ...
 8-235 1.27e-56

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: 185.24  E-value: 1.27e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131020733   8 LRLENVTKIFKdkknntEVIAVNNSTFEIKPGELITLLGPSGCGKTTTLRMVAGFELPTKGKIYIGNEDVTFLPPNKRDT 87
Cdd:COG0411     5 LEVRGLTKRFG------GLVAVDDVSLEVERGEIVGLIGPNGAGKTTLFNLITGFYRPTSGRILFDGRDITGLPPHRIAR 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131020733  88 ATV---FQSYGLFPHMTVFDNVA---------------YGLKLRKLSREEIEKRVFEALEMVGLKDLASRAPSRLSGGQQ 149
Cdd:COG0411    79 LGIartFQNPRLFPELTVLENVLvaaharlgrgllaalLRLPRARREEREARERAEELLERVGLADRADEPAGNLSYGQQ 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131020733 150 QRVTLARSIIVEPAILLLDEPLSNLDALLREQMRIEIKKIQRKLGITAIYVTHDRVEAMSLSDRIIVMKDGKIMQIGTPV 229
Cdd:COG0411   159 RRLEIARALATEPKLLLLDEPAAGLNPEETEELAELIRRLRDERGITILLIEHDMDLVMGLADRIVVLDFGRVIAEGTPA 238


                  ....*.
gi 1131020733 230 EIYEDP 235
Cdd:COG0411   239 EVRADP 244
NatA COG4555
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ...
 8-233 1.93e-56

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


Pssm-ID: 443618 [Multi-domain]  Cd Length: 243  Bit Score: 184.29  E-value: 1.93e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131020733   8 LRLENVTKIFKDKKnnteviAVNNSTFEIKPGELITLLGPSGCGKTTTLRMVAGFELPTKGKIYIGNEDVTFLPP-NKRD 86
Cdd:COG4555     2 IEVENLSKKYGKVP------ALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIDGEDVRKEPReARRQ 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131020733  87 TATVFQSYGLFPHMTVFDNVAYGLKLRKLSREEIEKRVFEALEMVGLKDLASRAPSRLSGGQQQRVTLARSIIVEPAILL 166
Cdd:COG4555    76 IGVLPDERGLYDRLTVRENIRYFAELYGLFDEELKKRIEELIELLGLEEFLDRRVGELSTGMKKKVALARALVHDPKVLL 155

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1131020733 167 LDEPLSNLDALLREQMRIEIKKIqRKLGITAIYVTHDRVEAMSLSDRIIVMKDGKIMQIGTPVEIYE 233
Cdd:COG4555   156 LDEPTNGLDVMARRLLREILRAL-KKEGKTVLFSSHIMQEVEALCDRVVILHKGKVVAQGSLDELRE 221
YnjD COG4136
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ...
 7-217 2.83e-56

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


Pssm-ID: 443311 [Multi-domain]  Cd Length: 211  Bit Score: 182.68  E-value: 2.83e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131020733   7 SLRLENVTkIFKDKKnnTEVIAVNnstFEIKPGELITLLGPSGCGKTTTLRMVAGF---ELPTKGKIYIGNEDVTFLPPN 83
Cdd:COG4136     1 MLSLENLT-ITLGGR--PLLAPLS---LTVAPGEILTLMGPSGSGKSTLLAAIAGTlspAFSASGEVLLNGRRLTALPAE 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131020733  84 KRDTATVFQSYGLFPHMTVFDNVAYGLKlRKLSREEIEKRVFEALEMVGLKDLASRAPSRLSGGQQQRVTLARSIIVEPA 163
Cdd:COG4136    75 QRRIGILFQDDLLFPHLSVGENLAFALP-PTIGRAQRRARVEQALEEAGLAGFADRDPATLSGGQRARVALLRALLAEPR 153

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1131020733 164 ILLLDEPLSNLDALLREQMRIEIKKIQRKLGITAIYVTHDR--VEAMSlsdRIIVM 217
Cdd:COG4136   154 ALLLDEPFSKLDAALRAQFREFVFEQIRQRGIPALLVTHDEedAPAAG---RVLDL 206
ntrCD TIGR01184
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ...
 29-238 2.90e-56

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: 183.44  E-value: 2.90e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131020733  29 VNNSTFEIKPGELITLLGPSGCGKTTTLRMVAGFELPTKGKIYIGNEDVTFLPPnkrDTATVFQSYGLFPHMTVFDNVAY 108
Cdd:TIGR01184   1 LKGVNLTIQQGEFISLIGHSGCGKSTLLNLISGLAQPTSGGVILEGKQITEPGP---DRMVVFQNYSLLPWLTVRENIAL 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131020733 109 GLK--LRKLSREEIEKRVFEALEMVGLKDLASRAPSRLSGGQQQRVTLARSIIVEPAILLLDEPLSNLDALLREQMRIEI 186
Cdd:TIGR01184  78 AVDrvLPDLSKSERRAIVEEHIALVGLTEAADKRPGQLSGGMKQRVAIARALSIRPKVLLLDEPFGALDALTRGNLQEEL 157

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1131020733 187 KKIQRKLGITAIYVTHDRVEAMSLSDRIIVMKDGKIMQIGtpvEIYEDPISK 238
Cdd:TIGR01184 158 MQIWEEHRVTVLMVTHDVDEALLLSDRVVMLTNGPAANIG---QILEVPFPR 206
ABC_ThiQ_thiamine_transporter cd03298
ATP-binding cassette domain of the thiamine transport system; Part of the ...
 39-226 1.44e-55

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: 181.15  E-value: 1.44e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131020733  39 GELITLLGPSGCGKTTTLRMVAGFELPTKGKIYIGNEDVTFLPPNKRDTATVFQSYGLFPHMTVFDNVAYGLKLRKLSRE 118
Cdd:cd03298    24 GEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLINGVDVTAAPPADRPVSMLFQENNLFAHLTVEQNVGLGLSPGLKLTA 103

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131020733 119 EIEKRVFEALEMVGLKDLASRAPSRLSGGQQQRVTLARSIIVEPAILLLDEPLSNLDALLREQMRIEIKKIQRKLGITAI 198
Cdd:cd03298   104 EDRQAIEVALARVGLAGLEKRLPGELSGGERQRVALARVLVRDKPVLLLDEPFAALDPALRAEMLDLVLDLHAETKMTVL 183

                         170       180
                  ....*....|....*....|....*...
gi 1131020733 199 YVTHDRVEAMSLSDRIIVMKDGKIMQIG 226
Cdd:cd03298   184 MVTHQPEDAKRLAQRVVFLDNGRIAAQG 211
DppD COG0444
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ...
 8-235 6.79e-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: 182.56  E-value: 6.79e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131020733   8 LRLENVTKIFKDKKNntEVIAVNNSTFEIKPGELITLLGPSGCGKTTTLRMVAGFELP---TKGKIYIGNEDVTFLPPNK 84
Cdd:COG0444     2 LEVRNLKVYFPTRRG--VVKAVDGVSFDVRRGETLGLVGESGSGKSTLARAILGLLPPpgiTSGEILFDGEDLLKLSEKE 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131020733  85 ------RDTATVFQ-SYG-LFPHMTVFDNVAYGLKL-RKLSREEIEKRVFEALEMVGLKDLASRA---PSRLSGGQQQRV 152
Cdd:COG0444    80 lrkirgREIQMIFQdPMTsLNPVMTVGDQIAEPLRIhGGLSKAEARERAIELLERVGLPDPERRLdryPHELSGGMRQRV 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131020733 153 TLARSIIVEPAILLLDEPLSNLDALLREQMrIE-IKKIQRKLGITAIYVTHDrveaMSL----SDRIIVMKDGKIMQIGT 227
Cdd:COG0444   160 MIARALALEPKLLIADEPTTALDVTIQAQI-LNlLKDLQRELGLAILFITHD----LGVvaeiADRVAVMYAGRIVEEGP 234


                  ....*...
gi 1131020733 228 PVEIYEDP 235
Cdd:COG0444   235 VEELFENP 242
ECF_ATPase_2 TIGR04521
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ...
 8-235 1.04e-54

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: 180.73  E-value: 1.04e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131020733   8 LRLENVTKIFkDKKNNTEVIAVNNSTFEIKPGELITLLGPSGCGKTTTLRMVAGFELPTKGKIYIGNEDVTFLPPNK--- 84
Cdd:TIGR04521   1 IKLKNVSYIY-QPGTPFEKKALDDVSLTIEDGEFVAIIGHTGSGKSTLIQHLNGLLKPTSGTVTIDGRDITAKKKKKlkd 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131020733  85 --RDTATVFQ--SYGLFpHMTVFDNVAYGLKLRKLSREEIEKRVFEALEMVGL-KDLASRAPSRLSGGQQQRVTLARSII 159
Cdd:TIGR04521  80 lrKKVGLVFQfpEHQLF-EETVYKDIAFGPKNLGLSEEEAEERVKEALELVGLdEEYLERSPFELSGGQMRRVAIAGVLA 158

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1131020733 160 VEPAILLLDEPLSNLDALLREQMRIEIKKIQRKLGITAIYVTHDRVEAMSLSDRIIVMKDGKIMQIGTPVEIYEDP 235
Cdd:TIGR04521 159 MEPEVLILDEPTAGLDPKGRKEILDLFKRLHKEKGLTVILVTHSMEDVAEYADRVIVMHKGKIVLDGTPREVFSDV 234
AppF COG4608
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ...
 8-235 6.89e-54

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


Pssm-ID: 443658 [Multi-domain]  Cd Length: 329  Bit Score: 180.31  E-value: 6.89e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131020733   8 LRLENVTKIFKDK-----KNNTEVIAVNNSTFEIKPGELITLLGPSGCGKTTTLRMVAGFELPTKGKIYIGNEDVTFLPP 82
Cdd:COG4608     8 LEVRDLKKHFPVRgglfgRTVGVVKAVDGVSFDIRRGETLGLVGESGCGKSTLGRLLLRLEEPTSGEILFDGQDITGLSG 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131020733  83 NK-----RDTATVFQ-SYG-LFPHMTVFDNVAYGLKL-RKLSREEIEKRVFEALEMVGLK-DLASRAPSRLSGGQQQRVT 153
Cdd:COG4608    88 RElrplrRRMQMVFQdPYAsLNPRMTVGDIIAEPLRIhGLASKAERRERVAELLELVGLRpEHADRYPHEFSGGQRQRIG 167

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131020733 154 LARSIIVEPAILLLDEPLSNLDA--------LLREqmrieikkIQRKLGITAIYVTHDrveaMS----LSDRIIVMKDGK 221
Cdd:COG4608   168 IARALALNPKLIVCDEPVSALDVsiqaqvlnLLED--------LQDELGLTYLFISHD----LSvvrhISDRVAVMYLGK 235

                         250
                  ....*....|....
gi 1131020733 222 IMQIGTPVEIYEDP 235
Cdd:COG4608   236 IVEIAPRDELYARP 249
ECF_ATPase_1 TIGR04520
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ...
 8-234 2.70e-53

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: 176.85  E-value: 2.70e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131020733   8 LRLENVTKIFKDkknnTEVIAVNNSTFEIKPGELITLLGPSGCGKTTTLRMVAGFELPTKGKIYIGNEDvTFLPPNKRD- 86
Cdd:TIGR04520   1 IEVENVSFSYPE----SEKPALKNVSLSIEKGEFVAIIGHNGSGKSTLAKLLNGLLLPTSGKVTVDGLD-TLDEENLWEi 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131020733  87 ---TATVFQSyglfPH-----MTVFDNVAYGLKLRKLSREEIEKRVFEALEMVGLKDLASRAPSRLSGGQQQRVTLARSI 158
Cdd:TIGR04520  76 rkkVGMVFQN----PDnqfvgATVEDDVAFGLENLGVPREEMRKRVDEALKLVGMEDFRDREPHLLSGGQKQRVAIAGVL 151

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1131020733 159 IVEPAILLLDEPLSNLDALLREQMRIEIKKIQRKLGITAIYVTHDRVEAMsLSDRIIVMKDGKIMQIGTPVEIYED 234
Cdd:TIGR04520 152 AMRPDIIILDEATSMLDPKGRKEVLETIRKLNKEEGITVISITHDMEEAV-LADRVIVMNKGKIVAEGTPREIFSQ 226
metN PRK11153
DL-methionine transporter ATP-binding subunit; Provisional
 9-235 2.72e-53

DL-methionine transporter ATP-binding subunit; Provisional


Pssm-ID: 236863 [Multi-domain]  Cd Length: 343  Bit Score: 179.23  E-value: 2.72e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131020733   9 RLENVTKIFKDKKNntEVIAVNNSTFEIKPGELITLLGPSGCGKTTTLRMVAGFELPTKGKIYIGNEDVTFLPPN----- 83
Cdd:PRK11153    3 ELKNISKVFPQGGR--TIHALNNVSLHIPAGEIFGVIGASGAGKSTLIRCINLLERPTSGRVLVDGQDLTALSEKelrka 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131020733  84 KRDTATVFQSYGLFPHMTVFDNVAYGLKLRKLSREEIEKRVFEALEMVGLKDLASRAPSRLSGGQQQRVTLARSIIVEPA 163
Cdd:PRK11153   81 RRQIGMIFQHFNLLSSRTVFDNVALPLELAGTPKAEIKARVTELLELVGLSDKADRYPAQLSGGQKQRVAIARALASNPK 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131020733 164 ILLLDEPLSNLD--------ALLreqmrieiKKIQRKLGITAIYVTH--DRVEamSLSDRIIVMKDGKIMQIGTPVEIYE 233
Cdd:PRK11153  161 VLLCDEATSALDpattrsilELL--------KDINRELGLTIVLITHemDVVK--RICDRVAVIDAGRLVEQGTVSEVFS 230


                  ..
gi 1131020733 234 DP 235
Cdd:PRK11153  231 HP 232
ABC_phnC TIGR02315
phosphonate ABC transporter, ATP-binding protein; Phosphonates are a class of ...
 8-238 1.68e-52

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: 174.02  E-value: 1.68e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131020733   8 LRLENVTKIFkdkknNTEVIAVNNSTFEIKPGELITLLGPSGCGKTTTLRMVAGFELPTKGKIYIGNEDVTFLPPNK--- 84
Cdd:TIGR02315   2 LEVENLSKVY-----PNGKQALKNINLNINPGEFVAIIGPSGAGKSTLLRCINRLVEPSSGSILLEGTDITKLRGKKlrk 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131020733  85 --RDTATVFQSYGLFPHMTVFDNVAYG---------LKLRKLSREEIEkRVFEALEMVGLKDLASRAPSRLSGGQQQRVT 153
Cdd:TIGR02315  77 lrRRIGMIFQHYNLIERLTVLENVLHGrlgykptwrSLLGRFSEEDKE-RALSALERVGLADKAYQRADQLSGGQQQRVA 155

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131020733 154 LARSIIVEPAILLLDEPLSNLDALLREQMRIEIKKIQRKLGITAIYVTHDRVEAMSLSDRIIVMKDGKIMQIGTPVEIYE 233
Cdd:TIGR02315 156 IARALAQQPDLILADEPIASLDPKTSKQVMDYLKRINKEDGITVIINLHQVDLAKKYADRIVGLKAGEIVFDGAPSELDD 235


                  ....*
gi 1131020733 234 DPISK 238
Cdd:TIGR02315 236 EVLRH 240
thiQ PRK10771
thiamine ABC transporter ATP-binding protein ThiQ;
33-222 6.86e-52

thiamine ABC transporter ATP-binding protein ThiQ;


Pssm-ID: 182716 [Multi-domain]  Cd Length: 232  Bit Score: 172.07  E-value: 6.86e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131020733  33 TFEIKPGELITLLGPSGCGKTTTLRMVAGFELPTKGKIYIGNEDVTFLPPNKRDTATVFQSYGLFPHMTVFDNVAYG--- 109
Cdd:PRK10771   19 DLTVERGERVAILGPSGAGKSTLLNLIAGFLTPASGSLTLNGQDHTTTPPSRRPVSMLFQENNLFSHLTVAQNIGLGlnp 98

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131020733 110 -LKLRKLSREEIEKRVfealEMVGLKDLASRAPSRLSGGQQQRVTLARSIIVEPAILLLDEPLSNLDALLREQMRIEIKK 188
Cdd:PRK10771   99 gLKLNAAQREKLHAIA----RQMGIEDLLARLPGQLSGGQRQRVALARCLVREQPILLLDEPFSALDPALRQEMLTLVSQ 174

                         170       180       190
                  ....*....|....*....|....*....|....
gi 1131020733 189 IQRKLGITAIYVTHDRVEAMSLSDRIIVMKDGKI 222
Cdd:PRK10771  175 VCQERQLTLLMVSHSLEDAARIAPRSLVVADGRI 208
FetA COG4619
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
8-222 1.03e-51

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


Pssm-ID: 443661 [Multi-domain]  Cd Length: 209  Bit Score: 170.77  E-value: 1.03e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131020733   8 LRLENVTKIFKDKKNnteviaVNNSTFEIKPGELITLLGPSGCGKTTTLRMVAGFELPTKGKIYIGNEDVTFLPPNK--R 85
Cdd:COG4619     1 LELEGLSFRVGGKPI------LSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIYLDGKPLSAMPPPEwrR 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131020733  86 DTATVFQSYGLFPhMTVFDNVAYGLKLRKLSREeiEKRVFEALEMVGL-KDLASRAPSRLSGGQQQRVTLARSIIVEPAI 164
Cdd:COG4619    75 QVAYVPQEPALWG-GTVRDNLPFPFQLRERKFD--RERALELLERLGLpPDILDKPVERLSGGERQRLALIRALLLQPDV 151

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131020733 165 LLLDEPLSNLDALLREqmRIE--IKKIQRKLGITAIYVTHDRVEAMSLSDRIIVMKDGKI 222
Cdd:COG4619   152 LLLDEPTSALDPENTR--RVEelLREYLAEEGRAVLWVSHDPEQIERVADRVLTLEAGRL 209
ssuB PRK11247
aliphatic sulfonates transport ATP-binding subunit; Provisional
 8-222 1.20e-51

aliphatic sulfonates transport ATP-binding subunit; Provisional


Pssm-ID: 183055 [Multi-domain]  Cd Length: 257  Bit Score: 172.55  E-value: 1.20e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131020733   8 LRLENVTKIFKDKknntEVIavNNSTFEIKPGELITLLGPSGCGKTTTLRMVAGFELPTKGKIYIGNedvTFLPPNKRDT 87
Cdd:PRK11247   13 LLLNAVSKRYGER----TVL--NQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAGELLAGT---APLAEAREDT 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131020733  88 ATVFQSYGLFPHMTVFDNVAYGLKlrklsrEEIEKRVFEALEMVGLKDLASRAPSRLSGGQQQRVTLARSIIVEPAILLL 167
Cdd:PRK11247   84 RLMFQDARLLPWKKVIDNVGLGLK------GQWRDAALQALAAVGLADRANEWPAALSGGQKQRVALARALIHRPGLLLL 157

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1131020733 168 DEPLSNLDALLREQMRIEIKKIQRKLGITAIYVTHDRVEAMSLSDRIIVMKDGKI 222
Cdd:PRK11247  158 DEPLGALDALTRIEMQDLIESLWQQHGFTVLLVTHDVSEAVAMADRVLLIEEGKI 212
thiQ TIGR01277
thiamine ABC transporter, ATP-binding protein; This model describes the energy-transducing ...
 39-226 1.53e-51

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: 170.81  E-value: 1.53e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131020733  39 GELITLLGPSGCGKTTTLRMVAGFELPTKGKIYIGNEDVTFLPPNKRDTATVFQSYGLFPHMTVFDNVAYGLKLR-KLSR 117
Cdd:TIGR01277  24 GEIVAIMGPSGAGKSTLLNLIAGFIEPASGSIKVNDQSHTGLAPYQRPVSMLFQENNLFAHLTVRQNIGLGLHPGlKLNA 103

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131020733 118 EEIEKrVFEALEMVGLKDLASRAPSRLSGGQQQRVTLARSIIVEPAILLLDEPLSNLDALLREQMRIEIKKIQRKLGITA 197
Cdd:TIGR01277 104 EQQEK-VVDAAQQVGIADYLDRLPEQLSGGQRQRVALARCLVRPNPILLLDEPFSALDPLLREEMLALVKQLCSERQRTL 182

                         170       180
                  ....*....|....*....|....*....
gi 1131020733 198 IYVTHDRVEAMSLSDRIIVMKDGKIMQIG 226
Cdd:TIGR01277 183 LMVTHHLSDARAIASQIAVVSQGKIKVVS 211
glnQ PRK09493
glutamine ABC transporter ATP-binding protein GlnQ;
12-248 4.18e-51

glutamine ABC transporter ATP-binding protein GlnQ;


Pssm-ID: 181906 [Multi-domain]  Cd Length: 240  Bit Score: 170.27  E-value: 4.18e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131020733  12 NVTKIFKDkknnTEVIavNNSTFEIKPGELITLLGPSGCGKTTTLRMVAGFELPTKGKIYIGNEDVtfLPPN------KR 85
Cdd:PRK09493    6 NVSKHFGP----TQVL--HNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGLKV--NDPKvderliRQ 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131020733  86 DTATVFQSYGLFPHMTVFDNVAYG-LKLRKLSREEIEKRVFEALEMVGLKDLASRAPSRLSGGQQQRVTLARSIIVEPAI 164
Cdd:PRK09493   78 EAGMVFQQFYLFPHLTALENVMFGpLRVRGASKEEAEKQARELLAKVGLAERAHHYPSELSGGQQQRVAIARALAVKPKL 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131020733 165 LLLDEPLSNLDALLREqmriEIKKIQRKL---GITAIYVTHDRVEAMSLSDRIIVMKDGKIMQIGTPVEIYEDPISKFVA 241
Cdd:PRK09493  158 MLFDEPTSALDPELRH----EVLKVMQDLaeeGMTMVIVTHEIGFAEKVASRLIFIDKGRIAEDGDPQVLIKNPPSQRLQ 233


                  ....*..
gi 1131020733 242 GFIGKVA 248
Cdd:PRK09493  234 EFLQHVS 240
ABC_subfamily_A cd03263
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ...
 8-231 6.69e-51

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: 169.22  E-value: 6.69e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131020733   8 LRLENVTKIFKDKKNntevIAVNNSTFEIKPGELITLLGPSGCGKTTTLRMVAGFELPTKGKIYI-GNEDVTFLPPNKRD 86
Cdd:cd03263     1 LQIRNLTKTYKKGTK----PAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYInGYSIRTDRKAARQS 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131020733  87 TATVFQSYGLFPHMTVFDNVAYGLKLRKLSREEIEKRVFEALEMVGLKDLASRAPSRLSGGQQQRVTLARSIIVEPAILL 166
Cdd:cd03263    77 LGYCPQFDALFDELTVREHLRFYARLKGLPKSEIKEEVELLLRVLGLTDKANKRARTLSGGMKRKLSLAIALIGGPSVLL 156

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1131020733 167 LDEPLSNLDALLREQMRIEIKKIQRKLGItaIYVTHDRVEAMSLSDRIIVMKDGKIMQIGTPVEI 231
Cdd:cd03263   157 LDEPTSGLDPASRRAIWDLILEVRKGRSI--ILTTHSMDEAEALCDRIAIMSDGKLRCIGSPQEL 219
ABC_FtsE cd03292
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ...
 10-222 2.05e-50

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: 167.97  E-value: 2.05e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131020733  10 LENVTKIFKDkknntEVIAVNNSTFEIKPGELITLLGPSGCGKTTTLRMVAGFELPTKGKIYIGNEDVTFLPPNK----- 84
Cdd:cd03292     3 FINVTKTYPN-----GTAALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQDVSDLRGRAipylr 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131020733  85 RDTATVFQSYGLFPHMTVFDNVAYGLKLRKLSREEIEKRVFEALEMVGLKDLASRAPSRLSGGQQQRVTLARSIIVEPAI 164
Cdd:cd03292    78 RKIGVVFQDFRLLPDRNVYENVAFALEVTGVPPREIRKRVPAALELVGLSHKHRALPAELSGGEQQRVAIARAIVNSPTI 157

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1131020733 165 LLLDEPLSNLDA-LLREQMRIeIKKIQrKLGITAIYVTHDR--VEAMslSDRIIVMKDGKI 222
Cdd:cd03292   158 LIADEPTGNLDPdTTWEIMNL-LKKIN-KAGTTVVVATHAKelVDTT--RHRVIALERGKL 214
ABC_ATP_DarD NF038007
darobactin export ABC transporter ATP-binding protein;
8-222 3.32e-50

darobactin export ABC transporter ATP-binding protein;


Pssm-ID: 411600 [Multi-domain]  Cd Length: 218  Bit Score: 167.20  E-value: 3.32e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131020733   8 LRLENVTKIFKDKKNNTEVIavNNSTFEIKPGELITLLGPSGCGKTTTLRMVAGFELPTKGKIYIGNEDVTFLPPNKRDT 87
Cdd:NF038007    2 LNMQNAEKCYITKTIKTKVL--NHLNFSVEKGDFVSIMGPSGSGKSTLLNIIGMFDSLDSGSLTLAGKEVTNLSYSQKII 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131020733  88 ------ATVFQSYGLFPHMTVFDNVAYGLKLRKLSREEIEKRVFEALEMVGLKDLASRAPSRLSGGQQQRVTLARSIIVE 161
Cdd:NF038007   80 lrreliGYIFQSFNLIPHLSIFDNVALPLKYRGVAKKERIERVNQVLNLFGIDNRRNHKPMQLSGGQQQRVAIARAMVSN 159

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1131020733 162 PAILLLDEPLSNLDALLREQMRIEIKKIQRKlGITAIYVTHDRvEAMSLSDRIIVMKDGKI 222
Cdd:NF038007  160 PALLLADEPTGNLDSKNARAVLQQLKYINQK-GTTIIMVTHSD-EASTYGNRIINMKDGKL 218
YbbA COG4181
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ...
 8-224 4.47e-50

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: 167.61  E-value: 4.47e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131020733   8 LRLENVTKIFKDkkNNTEVIAVNNSTFEIKPGELITLLGPSGCGKTTTLRMVAGFELPTKGKIYIGNEDVTFLppNKRDT 87
Cdd:COG4181     9 IELRGLTKTVGT--GAGELTILKGISLEVEAGESVAIVGASGSGKSTLLGLLAGLDRPTSGTVRLAGQDLFAL--DEDAR 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131020733  88 AT--------VFQSYGLFPHMTVFDNVAYGLKLRklSREEIEKRVFEALEMVGLKDLASRAPSRLSGGQQQRVTLARSII 159
Cdd:COG4181    85 ARlrarhvgfVFQSFQLLPTLTALENVMLPLELA--GRRDARARARALLERVGLGHRLDHYPAQLSGGEQQRVALARAFA 162

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1131020733 160 VEPAILLLDEPLSNLDALLREQMrIE-IKKIQRKLGITAIYVTHDRVEAmSLSDRIIVMKDGKIMQ 224
Cdd:COG4181   163 TEPAILFADEPTGNLDAATGEQI-IDlLFELNRERGTTLVLVTHDPALA-ARCDRVLRLRAGRLVE 226
PRK10070 PRK10070
proline/glycine betaine ABC transporter ATP-binding protein ProV;
27-243 1.20e-49

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


Pssm-ID: 182221 [Multi-domain]  Cd Length: 400  Bit Score: 171.37  E-value: 1.20e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131020733  27 IAVNNSTFEIKPGELITLLGPSGCGKTTTLRMVAGFELPTKGKIYIGNEDVTFLPP------NKRDTATVFQSYGLFPHM 100
Cdd:PRK10070   42 LGVKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAKISDaelrevRRKKIAMVFQSFALMPHM 121

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131020733 101 TVFDNVAYGLKLRKLSREEIEKRVFEALEMVGLKDLASRAPSRLSGGQQQRVTLARSIIVEPAILLLDEPLSNLDALLRE 180
Cdd:PRK10070  122 TVLDNTAFGMELAGINAEERREKALDALRQVGLENYAHSYPDELSGGMRQRVGLARALAINPDILLMDEAFSALDPLIRT 201

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1131020733 181 QMRIEIKKIQRKLGITAIYVTHDRVEAMSLSDRIIVMKDGKIMQIGTPVEIYEDPISKFVAGF 243
Cdd:PRK10070  202 EMQDELVKLQAKHQRTIVFISHDLDEAMRIGDRIAIMQNGEVVQVGTPDEILNNPANDYVRTF 264
SunT COG2274
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ...
 7-233 1.40e-49

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: 176.95  E-value: 1.40e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131020733   7 SLRLENVTkiFKDKKNNTEVIavNNSTFEIKPGELITLLGPSGCGKTTTLRMVAGFELPTKGKIYIGNEDVTFLPPNK-- 84
Cdd:COG2274   473 DIELENVS--FRYPGDSPPVL--DNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEPTSGRILIDGIDLRQIDPASlr 548

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131020733  85 RDTATVFQSYGLFpHMTVFDNVAyglklrkLSREEI-EKRVFEALEMVGLKDLASRAP-----------SRLSGGQQQRV 152
Cdd:COG2274   549 RQIGVVLQDVFLF-SGTIRENIT-------LGDPDAtDEEIIEAARLAGLHDFIEALPmgydtvvgeggSNLSGGQRQRL 620

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131020733 153 TLARSIIVEPAILLLDEPLSNLDAllREQMRIeIKKIQR-KLGITAIYVTHdRVEAMSLSDRIIVMKDGKIMQIGTPVEI 231
Cdd:COG2274   621 AIARALLRNPRILILDEATSALDA--ETEAII-LENLRRlLKGRTVIIIAH-RLSTIRLADRIIVLDKGRIVEDGTHEEL 696


                  ..
gi 1131020733 232 YE 233
Cdd:COG2274   697 LA 698
modC_ABC TIGR02142
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ...
 38-235 2.09e-49

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: 169.52  E-value: 2.09e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131020733  38 PGELIT-LLGPSGCGKTTTLRMVAGFELPTKGKIYIGNEDV------TFLPPNKRDTATVFQSYGLFPHMTVFDNVAYGL 110
Cdd:TIGR02142  21 PGQGVTaIFGRSGSGKTTLIRLIAGLTRPDEGEIVLNGRTLfdsrkgIFLPPEKRRIGYVFQEARLFPHLSVRGNLRYGM 100

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131020733 111 K-----LRKLSREEIekrvfeaLEMVGLKDLASRAPSRLSGGQQQRVTLARSIIVEPAILLLDEPLSNLDALLREQMRIE 185
Cdd:TIGR02142 101 KrarpsERRISFERV-------IELLGIGHLLGRLPGRLSGGEKQRVAIGRALLSSPRLLLMDEPLAALDDPRKYEILPY 173

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 1131020733 186 IKKIQRKLGITAIYVTHDRVEAMSLSDRIIVMKDGKIMQIGTPVEIYEDP 235
Cdd:TIGR02142 174 LERLHAEFGIPILYVSHSLQEVLRLADRVVVLEDGRVAAAGPIAEVWASP 223
LptB COG1137
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ...
 8-235 3.35e-49

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


Pssm-ID: 440752 [Multi-domain]  Cd Length: 240  Bit Score: 165.59  E-value: 3.35e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131020733   8 LRLENVTKIFKDKKnnteviAVNNSTFEIKPGELITLLGPSGCGKTTTLRMVAGFELPTKGKIYIGNEDVTFLPPNKR-- 85
Cdd:COG1137     4 LEAENLVKSYGKRT------VVKDVSLEVNQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGRIFLDGEDITHLPMHKRar 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131020733  86 -------DTATVFQsyglfpHMTVFDNVAYGLKLRKLSREEIEKRVFEALEMVGLKDLASRAPSRLSGGQQQRVTLARSI 158
Cdd:COG1137    78 lgigylpQEASIFR------KLTVEDNILAVLELRKLSKKEREERLEELLEEFGITHLRKSKAYSLSGGERRRVEIARAL 151

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131020733 159 IVEPAILLLDEPLSNLD--ALlreqmrIEIKKIQRKL---GItAIYVT-HDRVEAMSLSDRIIVMKDGKIMQIGTPVEIY 232
Cdd:COG1137   152 ATNPKFILLDEPFAGVDpiAV------ADIQKIIRHLkerGI-GVLITdHNVRETLGICDRAYIISEGKVLAEGTPEEIL 224


                  ...
gi 1131020733 233 EDP 235
Cdd:COG1137   225 NNP 227
YejF COG4172
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ...
 8-235 3.27e-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: 170.25  E-value: 3.27e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131020733   8 LRLENVTKIFKDKKN-----NTEVIAVNNSTFEIKPGELITLLGPSGCGKTTT----LRMVagfelPTKGKIYIGNEDVT 78
Cdd:COG4172   276 LEARDLKVWFPIKRGlfrrtVGHVKAVDGVSLTLRRGETLGLVGESGSGKSTLglalLRLI-----PSEGEIRFDGQDLD 350

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131020733  79 FLP-----PNKRDTATVFQS-YG-LFPHMTVFDNVAYGLKL--RKLSREEIEKRVFEALEMVGLK-DLASRAPSRLSGGQ 148
Cdd:COG4172   351 GLSrralrPLRRRMQVVFQDpFGsLSPRMTVGQIIAEGLRVhgPGLSAAERRARVAEALEEVGLDpAARHRYPHEFSGGQ 430

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131020733 149 QQRVTLARSIIVEPAILLLDEPLSNLD--------ALLREqmrieikkIQRKLGITAIYVTHDR--VEAMslSDRIIVMK 218
Cdd:COG4172   431 RQRIAIARALILEPKLLVLDEPTSALDvsvqaqilDLLRD--------LQREHGLAYLFISHDLavVRAL--AHRVMVMK 500

                         250
                  ....*....|....*..
gi 1131020733 219 DGKIMQIGTPVEIYEDP 235
Cdd:COG4172   501 DGKVVEQGPTEQVFDAP 517
ABC_DR_subfamily_A cd03230
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ...
 8-222 5.86e-48

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: 159.87  E-value: 5.86e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131020733   8 LRLENVTKIFKDKKnnteviAVNNSTFEIKPGELITLLGPSGCGKTTTLRMVAGFELPTKGKIYIGNEDVTFLPPN-KRD 86
Cdd:cd03230     1 IEVRNLSKRYGKKT------ALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVLGKDIKKEPEEvKRR 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131020733  87 TATVFQSYGLFPHMTVFDNVayglklrklsreeiekrvfealemvglkdlasrapsRLSGGQQQRVTLARSIIVEPAILL 166
Cdd:cd03230    75 IGYLPEEPSLYENLTVRENL------------------------------------KLSGGMKQRLALAQALLHDPELLI 118

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1131020733 167 LDEPLSNLDALLREQMRIEIKKIQRKlGITAIYVTHDRVEAMSLSDRIIVMKDGKI 222
Cdd:cd03230   119 LDEPTSGLDPESRREFWELLRELKKE-GKTILLSSHILEEAERLCDRVAILNNGRI 173
cbiO PRK13637
energy-coupling factor transporter ATPase;
7-232 6.32e-48

energy-coupling factor transporter ATPase;


Pssm-ID: 237455 [Multi-domain]  Cd Length: 287  Bit Score: 163.68  E-value: 6.32e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131020733   7 SLRLENVTKIFkDKKNNTEVIAVNNSTFEIKPGELITLLGPSGCGKTTTLRMVAGFELPTKGKIYIGNEDVT----FLPP 82
Cdd:PRK13637    2 SIKIENLTHIY-MEGTPFEKKALDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDGVDITdkkvKLSD 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131020733  83 NKRDTATVFQ--SYGLFPHmTVFDNVAYGLKLRKLSREEIEKRVFEALEMVGLK--DLASRAPSRLSGGQQQRVTLARSI 158
Cdd:PRK13637   81 IRKKVGLVFQypEYQLFEE-TIEKDIAFGPINLGLSEEEIENRVKRAMNIVGLDyeDYKDKSPFELSGGQKRRVAIAGVV 159

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1131020733 159 IVEPAILLLDEPLSNLDALLREQMRIEIKKIQRKLGITAIYVTHDRVEAMSLSDRIIVMKDGKIMQIGTPVEIY 232
Cdd:PRK13637  160 AMEPKILILDEPTAGLDPKGRDEILNKIKELHKEYNMTIILVSHSMEDVAKLADRIIVMNKGKCELQGTPREVF 233
cbiO PRK13635
energy-coupling factor ABC transporter ATP-binding protein;
8-233 7.32e-48

energy-coupling factor ABC transporter ATP-binding protein;


Pssm-ID: 184195 [Multi-domain]  Cd Length: 279  Bit Score: 163.26  E-value: 7.32e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131020733   8 LRLENVTKIFKDkknnTEVIAVNNSTFEIKPGELITLLGPSGCGKTTTLRMVAGFELPTKGKIYIG----NE----DVtf 79
Cdd:PRK13635    6 IRVEHISFRYPD----AATYALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGgmvlSEetvwDV-- 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131020733  80 lppnKRDTATVFQSY-GLFPHMTVFDNVAYGLKLRKLSREEIEKRVFEALEMVGLKDLASRAPSRLSGGQQQRVTLARSI 158
Cdd:PRK13635   80 ----RRQVGMVFQNPdNQFVGATVQDDVAFGLENIGVPREEMVERVDQALRQVGMEDFLNREPHRLSGGQKQRVAIAGVL 155

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1131020733 159 IVEPAILLLDEPLSNLDALLREQMRIEIKKIQRKLGITAIYVTHDRVEAMSlSDRIIVMKDGKIMQIGTPVEIYE 233
Cdd:PRK13635  156 ALQPDIIILDEATSMLDPRGRREVLETVRQLKEQKGITVLSITHDLDEAAQ-ADRVIVMNKGEILEEGTPEEIFK 229
ABC_DrrA cd03265
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ...
 11-231 8.01e-48

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: 161.38  E-value: 8.01e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131020733  11 ENVTKIFKDkknnteVIAVNNSTFEIKPGELITLLGPSGCGKTTTLRMVAGFELPTKGKIYIGNEDVTFLPPN-KRDTAT 89
Cdd:cd03265     4 ENLVKKYGD------FEAVRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATVAGHDVVREPREvRRRIGI 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131020733  90 VFQSYGLFPHMTVFDNVAYGLKLRKLSREEIEKRVFEALEMVGLKDLASRAPSRLSGGQQQRVTLARSIIVEPAILLLDE 169
Cdd:cd03265    78 VFQDLSVDDELTGWENLYIHARLYGVPGAERRERIDELLDFVGLLEAADRLVKTYSGGMRRRLEIARSLVHRPEVLFLDE 157

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1131020733 170 PLSNLDALLREQMRIEIKKIQRKLGITAIYVTHDRVEAMSLSDRIIVMKDGKIMQIGTPVEI 231
Cdd:cd03265   158 PTIGLDPQTRAHVWEYIEKLKEEFGMTILLTTHYMEEAEQLCDRVAIIDHGRIIAEGTPEEL 219
3a0107s01c2 TIGR00972
phosphate ABC transporter, ATP-binding protein; This model represents the ATP-binding protein ...
 8-244 1.33e-47

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: 161.69  E-value: 1.33e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131020733   8 LRLENVTKIFKDKKnnteviAVNNSTFEIKPGELITLLGPSGCGKTTTLR-------MVAGFElpTKGKIYIGNEDVTfl 80
Cdd:TIGR00972   2 IEIENLNLFYGEKE------ALKNINLDIPKNQVTALIGPSGCGKSTLLRslnrmndLVPGVR--IEGKVLFDGQDIY-- 71

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131020733  81 pPNKRDTAT-------VFQSYGLFPhMTVFDNVAYGLKLRKL-SREEIEKRVFEALEMVGL----KDLASRAPSRLSGGQ 148
Cdd:TIGR00972  72 -DKKIDVVElrrrvgmVFQKPNPFP-MSIYDNIAYGPRLHGIkDKKELDEIVEESLKKAALwdevKDRLHDSALGLSGGQ 149

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131020733 149 QQRVTLARSIIVEPAILLLDEPLSNLDALlrEQMRIEIKKIQRKLGITAIYVTHDRVEAMSLSDRIIVMKDGKIMQIGTP 228
Cdd:TIGR00972 150 QQRLCIARALAVEPEVLLLDEPTSALDPI--ATGKIEELIQELKKKYTIVIVTHNMQQAARISDRTAFFYDGELVEYGPT 227

                         250
                  ....*....|....*.
gi 1131020733 229 VEIYEDPISKFVAGFI 244
Cdd:TIGR00972 228 EQIFTNPKEKRTEDYI 243
ABC_tran pfam00005
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ...
 29-172 1.91e-47

ABC transporter; ABC transporters for a large family of proteins responsible for translocation of a variety of compounds across biological membranes. ABC transporters are the largest family of proteins in many completely sequenced bacteria. ABC transporters are composed of two copies of this domain and two copies of a transmembrane domain pfam00664. These four domains may belong to a single polypeptide or belong in different polypeptide chains.


Pssm-ID: 394964 [Multi-domain]  Cd Length: 150  Bit Score: 157.81  E-value: 1.91e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131020733  29 VNNSTFEIKPGELITLLGPSGCGKTTTLRMVAGFELPTKGKIYIGNEDVTF--LPPNKRDTATVFQSYGLFPHMTVFDNV 106
Cdd:pfam00005   1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDLTDdeRKSLRKEIGYVFQDPQLFPRLTVRENL 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131020733 107 AYGLKLRKLSREEIEKRVFEALEMVGLKDLASR----APSRLSGGQQQRVTLARSIIVEPAILLLDEPLS 172
Cdd:pfam00005  81 RLGLLLKGLSKREKDARAEEALEKLGLGDLADRpvgeRPGTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
tauB PRK11248
taurine ABC transporter ATP-binding subunit;
28-220 3.29e-47

taurine ABC transporter ATP-binding subunit;


Pssm-ID: 183056 [Multi-domain]  Cd Length: 255  Bit Score: 160.64  E-value: 3.29e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131020733  28 AVNNSTFEIKPGELITLLGPSGCGKTTTLRMVAGFELPTKGKIYIGNEDVTFlPPNKRdtATVFQSYGLFPHMTVFDNVA 107
Cdd:PRK11248   16 ALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDGKPVEG-PGAER--GVVFQNEGLLPWRNVQDNVA 92

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131020733 108 YGLKLRKLSREEIEKRVFEALEMVGLKDLASRAPSRLSGGQQQRVTLARSIIVEPAILLLDEPLSNLDALLREQMRIEIK 187
Cdd:PRK11248   93 FGLQLAGVEKMQRLEIAHQMLKKVGLEGAEKRYIWQLSGGQRQRVGIARALAANPQLLLLDEPFGALDAFTREQMQTLLL 172

                         170       180       190
                  ....*....|....*....|....*....|...
gi 1131020733 188 KIQRKLGITAIYVTHDRVEAMSLSDRIIVMKDG 220
Cdd:PRK11248  173 KLWQETGKQVLLITHDIEEAVFMATELVLLSPG 205
ABC_YhbG cd03218
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ...
 8-238 6.24e-47

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: 159.25  E-value: 6.24e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131020733   8 LRLENVTKIFKDKKnnteviAVNNSTFEIKPGELITLLGPSGCGKTTTLRMVAGFELPTKGKIYIGNEDVTFLPPNKRDT 87
Cdd:cd03218     1 LRAENLSKRYGKRK------VVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDGQDITKLPMHKRAR 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131020733  88 ATVF---QSYGLFPHMTVFDNVAYGLKLRKLSREEIEKRVFEALEMVGLKDLASRAPSRLSGGQQQRVTLARSIIVEPAI 164
Cdd:cd03218    75 LGIGylpQEASIFRKLTVEENILAVLEIRGLSKKEREEKLEELLEEFHITHLRKSKASSLSGGERRRVEIARALATNPKF 154

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1131020733 165 LLLDEPLSNLDALlreqMRIEIKKIQRKL---GITAIYVTHDRVEAMSLSDRIIVMKDGKIMQIGTPVEIYEDPISK 238
Cdd:cd03218   155 LLLDEPFAGVDPI----AVQDIQKIIKILkdrGIGVLITDHNVRETLSITDRAYIIYEGKVLAEGTPEEIAANELVR 227
ZnuC COG1121
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ...
 8-231 9.29e-47

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


Pssm-ID: 440738 [Multi-domain]  Cd Length: 245  Bit Score: 159.10  E-value: 9.29e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131020733   8 LRLENVTKIFKDKKnnteviAVNNSTFEIKPGELITLLGPSGCGKTTTLRMVAGFELPTKGKIYIGNEDVTflpPNKRDT 87
Cdd:COG1121     7 IELENLTVSYGGRP------VLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLFGKPPR---RARRRI 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131020733  88 ATVFQSYGL---FPhMTVFDNVAYGLK-----LRKLSREEIEkRVFEALEMVGLKDLASRAPSRLSGGQQQRVTLARSII 159
Cdd:COG1121    78 GYVPQRAEVdwdFP-ITVRDVVLMGRYgrrglFRRPSRADRE-AVDEALERVGLEDLADRPIGELSGGQQQRVLLARALA 155

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131020733 160 VEPAILLLDEPLSNLDA--------LLREqmrieikkiQRKLGITAIYVTHDRVEAMSLSDRIIVMKDGKIMQiGTPVEI 231
Cdd:COG1121   156 QDPDLLLLDEPFAGVDAateealyeLLRE---------LRREGKTILVVTHDLGAVREYFDRVLLLNRGLVAH-GPPEEV 225
ABC_Iron-Siderophores_B12_Hemin cd03214
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ...
 9-226 1.04e-46

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: 156.83  E-value: 1.04e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131020733   9 RLENVTKIFKDKKnnteviAVNNSTFEIKPGELITLLGPSGCGKTTTLRMVAGFELPTKGKIYIGNEDvtflppnkrdta 88
Cdd:cd03214     1 EVENLSVGYGGRT------VLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDGKD------------ 62

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131020733  89 tvfqsyglfphmtvfdnvayglkLRKLSREEIEKR---VFEALEMVGLKDLASRAPSRLSGGQQQRVTLARSIIVEPAIL 165
Cdd:cd03214    63 -----------------------LASLSPKELARKiayVPQALELLGLAHLADRPFNELSGGERQRVLLARALAQEPPIL 119

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1131020733 166 LLDEPLSNLDalLREQMRI--EIKKIQRKLGITAIYVTHDRVEAMSLSDRIIVMKDGKIMQIG 226
Cdd:cd03214   120 LLDEPTSHLD--IAHQIELleLLRRLARERGKTVVMVLHDLNLAARYADRVILLKDGRIVAQG 180
cbiO PRK13650
energy-coupling factor transporter ATPase;
21-232 1.09e-46

energy-coupling factor transporter ATPase;


Pssm-ID: 184209 [Multi-domain]  Cd Length: 279  Bit Score: 160.28  E-value: 1.09e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131020733  21 KNNTEVIAVNNSTFEIKPGELITLLGPSGCGKTTTLRMVAGFELPTKGKIYIGNEDVTflPPN----KRDTATVFQSY-G 95
Cdd:PRK13650   15 KEDQEKYTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIIDGDLLT--EENvwdiRHKIGMVFQNPdN 92

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131020733  96 LFPHMTVFDNVAYGLKLRKLSREEIEKRVFEALEMVGLKDLASRAPSRLSGGQQQRVTLARSIIVEPAILLLDEPLSNLD 175
Cdd:PRK13650   93 QFVGATVEDDVAFGLENKGIPHEEMKERVNEALELVGMQDFKEREPARLSGGQKQRVAIAGAVAMRPKIIILDEATSMLD 172

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1131020733 176 ALLREQMRIEIKKIQRKLGITAIYVTHDrVEAMSLSDRIIVMKDGKIMQIGTPVEIY 232
Cdd:PRK13650  173 PEGRLELIKTIKGIRDDYQMTVISITHD-LDEVALSDRVLVMKNGQVESTSTPRELF 228
ABC_NatA_sodium_exporter cd03266
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ...
 8-226 1.39e-46

ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a bacterial ABC-type Na+ transport system called NatAB, which catalyzes ATP-dependent electrogenic Na+ extrusion without mechanically coupled proton or K+ uptake. NatB possess six putative membrane spanning regions at its C-terminus. In B. subtilis, NatAB is inducible by agents such as ethanol and protonophores, which lower the proton-motive force across the membrane. The closest sequence similarity to NatA is exhibited by DrrA of the two-component daunorubicin- and doxorubicin-efflux system. Hence, the functional NatAB is presumably assembled with two copies of a single ATP-binding protein and a single integral membrane protein.


Pssm-ID: 213233 [Multi-domain]  Cd Length: 218  Bit Score: 157.91  E-value: 1.39e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131020733   8 LRLENVTKIFKDKKNNteVIAVNNSTFEIKPGELITLLGPSGCGKTTTLRMVAGFELPTKGKIYIGNEDVTFLPPN-KRD 86
Cdd:cd03266     2 ITADALTKRFRDVKKT--VQAVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDGFDVVKEPAEaRRR 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131020733  87 TATVFQSYGLFPHMTVFDNVAYGLKLRKLSREEIEKRVFEALEMVGLKDLASRAPSRLSGGQQQRVTLARSIIVEPAILL 166
Cdd:cd03266    80 LGFVSDSTGLYDRLTARENLEYFAGLYGLKGDELTARLEELADRLGMEELLDRRVGGFSTGMRQKVAIARALVHDPPVLL 159

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131020733 167 LDEPLSNLDALLREQMRiEIKKIQRKLGITAIYVTHDRVEAMSLSDRIIVMKDGKIMQIG 226
Cdd:cd03266   160 LDEPTTGLDVMATRALR-EFIRQLRALGKCILFSTHIMQEVERLCDRVVVLHRGRVVYEG 218
ArtP COG4161
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
28-244 2.11e-46

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


Pssm-ID: 443326 [Multi-domain]  Cd Length: 242  Bit Score: 158.25  E-value: 2.11e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131020733  28 AVNNSTFEIKPGELITLLGPSGCGKTTTLRMVAGFELPTKGKIYIGNEDVTF-LPPN-------KRDTATVFQSYGLFPH 99
Cdd:COG4161    17 ALFDINLECPSGETLVLLGPSGAGKSSLLRVLNLLETPDSGQLNIAGHQFDFsQKPSekairllRQKVGMVFQQYNLWPH 96

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131020733 100 MTVFDN-VAYGLKLRKLSREEIEKRVFEALEMVGLKDLASRAPSRLSGGQQQRVTLARSIIVEPAILLLDEPLSNLDALL 178
Cdd:COG4161    97 LTVMENlIEAPCKVLGLSKEQAREKAMKLLARLRLTDKADRFPLHLSGGQQQRVAIARALMMEPQVLLFDEPTAALDPEI 176

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131020733 179 REQmrieIKKIQRKL---GITAIYVTHDrVE-AMSLSDRIIVMKDGKIMQIGTpVEIYEDPISKFVAGFI 244
Cdd:COG4161   177 TAQ----VVEIIRELsqtGITQVIVTHE-VEfARKVASQVVYMEKGRIIEQGD-ASHFTQPQTEAFAHYL 240
artP PRK11124
arginine transporter ATP-binding subunit; Provisional
 7-227 5.64e-45

arginine transporter ATP-binding subunit; Provisional


Pssm-ID: 182980 [Multi-domain]  Cd Length: 242  Bit Score: 154.40  E-value: 5.64e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131020733   7 SLRLENVTKIFKDKKnnteviAVNNSTFEIKPGELITLLGPSGCGKTTTLRMVAGFELPTKGKIYIGNEDVTF-LPPN-- 83
Cdd:PRK11124    2 SIQLNGINCFYGAHQ------ALFDITLDCPQGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLNIAGNHFDFsKTPSdk 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131020733  84 -----KRDTATVFQSYGLFPHMTVFDN-VAYGLKLRKLSREEIEKRVFEALEMVGLKDLASRAPSRLSGGQQQRVTLARS 157
Cdd:PRK11124   76 airelRRNVGMVFQQYNLWPHLTVQQNlIEAPCRVLGLSKDQALARAEKLLERLRLKPYADRFPLHLSGGQQQRVAIARA 155

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131020733 158 IIVEPAILLLDEPLSNLDALLREQMRIEIKKIQrKLGITAIYVTHDRVEAMSLSDRIIVMKDGKIMQIGT 227
Cdd:PRK11124  156 LMMEPQVLLFDEPTAALDPEITAQIVSIIRELA-ETGITQVIVTHEVEVARKTASRVVYMENGHIVEQGD 224
nickel_nikE TIGR02769
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a ...
 8-224 1.08e-44

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: 154.58  E-value: 1.08e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131020733   8 LRLENVTKIFKD-----KKNNTEVIavNNSTFEIKPGELITLLGPSGCGKTTTLRMVAGFELPTKGKIYIGNEDVTFLPP 82
Cdd:TIGR02769   3 LEVRDVTHTYRTgglfgAKQRAPVL--TNVSLSIEEGETVGLLGRSGCGKSTLARLLLGLEKPAQGTVSFRGQDLYQLDR 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131020733  83 N-----KRDTATVFQ-SYGLF-PHMTVFDNVAYGLK-LRKLSREEIEKRVFEALEMVGLK-DLASRAPSRLSGGQQQRVT 153
Cdd:TIGR02769  81 KqrrafRRDVQLVFQdSPSAVnPRMTVRQIIGEPLRhLTSLDESEQKARIAELLDMVGLRsEDADKLPRQLSGGQLQRIN 160

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1131020733 154 LARSIIVEPAILLLDEPLSNLDALLREQMRIEIKKIQRKLGITAIYVTHDRVEAMSLSDRIIVMKDGKIMQ 224
Cdd:TIGR02769 161 IARALAVKPKLIVLDEAVSNLDMVLQAVILELLRKLQQAFGTAYLFITHDLRLVQSFCQRVAVMDKGQIVE 231
ABC_putative_ATPase cd03269
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ...
 8-226 1.30e-44

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: 152.43  E-value: 1.30e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131020733   8 LRLENVTKIFKDKKnnteviAVNNSTFEIKPGELITLLGPSGCGKTTTLRMVAGFELPTKGKIYIGNEDVTFLPpnKRDT 87
Cdd:cd03269     1 LEVENVTKRFGRVT------ALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDGKPLDIAA--RNRI 72

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131020733  88 ATVFQSYGLFPHMTVFDNVAYGLKLRKLSREEIEKRVFEALEMVGLKDLASRAPSRLSGGQQQRVTLARSIIVEPAILLL 167
Cdd:cd03269    73 GYLPEERGLYPKMKVIDQLVYLAQLKGLKKEEARRRIDEWLERLELSEYANKRVEELSKGNQQKVQFIAAVIHDPELLIL 152

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1131020733 168 DEPLSNLDALLREQMRIEIKKIQRKlGITAIYVTHDRVEAMSLSDRIIVMKDGKIMQIG 226
Cdd:cd03269   153 DEPFSGLDPVNVELLKDVIRELARA-GKTVILSTHQMELVEELCDRVLLLNKGRAVLYG 210
MdlB COG1132
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
7-230 6.49e-44

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


Pssm-ID: 440747 [Multi-domain]  Cd Length: 579  Bit Score: 159.56  E-value: 6.49e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131020733   7 SLRLENVTkiF---KDKKnnteviAVNNSTFEIKPGELITLLGPSGCGKTTTLRMVAGFELPTKGKIYIGNEDVTFLPPN 83
Cdd:COG1132   339 EIEFENVS--FsypGDRP------VLKDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYDPTSGRILIDGVDIRDLTLE 410

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131020733  84 K-RDT-ATVFQSYGLFpHMTVFDNVAYGLKlrKLSREEIEkrvfEALEMVGLKDLASRAP-----------SRLSGGQQQ 150
Cdd:COG1132   411 SlRRQiGVVPQDTFLF-SGTIRENIRYGRP--DATDEEVE----EAAKAAQAHEFIEALPdgydtvvgergVNLSGGQRQ 483

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131020733 151 RVTLARSIIVEPAILLLDEPLSNLDAllreqmRIEiKKIQRKL-----GITAIYVTHdRVEAMSLSDRIIVMKDGKIMQI 225
Cdd:COG1132   484 RIAIARALLKDPPILILDEATSALDT------ETE-ALIQEALerlmkGRTTIVIAH-RLSTIRNADRILVLDDGRIVEQ 555


                  ....*
gi 1131020733 226 GTPVE 230
Cdd:COG1132   556 GTHEE 560
PstB COG1117
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ...
 1-244 6.92e-44

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


Pssm-ID: 440734 [Multi-domain]  Cd Length: 258  Bit Score: 152.11  E-value: 6.92e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131020733   1 MKKKQVSLRLENVTKIFKDKKnnteviAVNNSTFEIKPGELITLLGPSGCGKTTTLR-------MVAGFElpTKGKIYIG 73
Cdd:COG1117     5 ASTLEPKIEVRNLNVYYGDKQ------ALKDINLDIPENKVTALIGPSGCGKSTLLRclnrmndLIPGAR--VEGEILLD 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131020733  74 NEDV--TFLPPNK--RDTATVFQSYGLFPhMTVFDNVAYGLKLR-KLSREEIEKRVFEALEMVGL----KD-LASRApSR 143
Cdd:COG1117    77 GEDIydPDVDVVElrRRVGMVFQKPNPFP-KSIYDNVAYGLRLHgIKSKSELDEIVEESLRKAALwdevKDrLKKSA-LG 154

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131020733 144 LSGGQQQRVTLARSIIVEPAILLLDEPLSNLDALlrEQMRIE--IKKIQRKLGItaIYVTHDRVEAMSLSDRIIVMKDGK 221
Cdd:COG1117   155 LSGGQQQRLCIARALAVEPEVLLMDEPTSALDPI--STAKIEelILELKKDYTI--VIVTHNMQQAARVSDYTAFFYLGE 230

                         250       260
                  ....*....|....*....|...
gi 1131020733 222 IMQIGTPVEIYEDPISKFVAGFI 244
Cdd:COG1117   231 LVEFGPTEQIFTNPKDKRTEDYI 253
nikE PRK10419
nickel ABC transporter ATP-binding protein NikE;
29-224 1.89e-43

nickel ABC transporter ATP-binding protein NikE;


Pssm-ID: 236689 [Multi-domain]  Cd Length: 268  Bit Score: 151.38  E-value: 1.89e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131020733  29 VNNSTFEIKPGELITLLGPSGCGKTTTLRMVAGFELPTKGKIYIGNEDVTFLPPN-----KRDTATVFQ-SYGLF-PHMT 101
Cdd:PRK10419   28 LNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWRGEPLAKLNRAqrkafRRDIQMVFQdSISAVnPRKT 107

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131020733 102 VFDNVAYGLK-LRKLSREEIEKRVFEALEMVGLKD-LASRAPSRLSGGQQQRVTLARSIIVEPAILLLDEPLSNLDALLR 179
Cdd:PRK10419  108 VREIIREPLRhLLSLDKAERLARASEMLRAVDLDDsVLDKRPPQLSGGQLQRVCLARALAVEPKLLILDEAVSNLDLVLQ 187

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 1131020733 180 EQMRIEIKKIQRKLGITAIYVTHDRVEAMSLSDRIIVMKDGKIMQ 224
Cdd:PRK10419  188 AGVIRLLKKLQQQFGTACLFITHDLRLVERFCQRVMVMDNGQIVE 232
CcmA COG4133
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ...
 8-221 5.78e-43

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


Pssm-ID: 443308 [Multi-domain]  Cd Length: 206  Bit Score: 148.01  E-value: 5.78e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131020733   8 LRLENVTKIFkdkkNNTEVIAvnNSTFEIKPGELITLLGPSGCGKTTTLRMVAGFELPTKGKIYIGNEDVTFLPPN-KRD 86
Cdd:COG4133     3 LEAENLSCRR----GERLLFS--GLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWNGEPIRDAREDyRRR 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131020733  87 TATVFQSYGLFPHMTVFDNVAYGLKLRKLSREEIekRVFEALEMVGLKDLASRAPSRLSGGQQQRVTLARSIIVEPAILL 166
Cdd:COG4133    77 LAYLGHADGLKPELTVRENLRFWAALYGLRADRE--AIDEALEAVGLAGLADLPVRQLSAGQKRRVALARLLLSPAPLWL 154

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1131020733 167 LDEPLSNLD----ALLREQMRIEIKKiqrklGITAIYVTHDRVEAmsLSDRIIVMKDGK 221
Cdd:COG4133   155 LDEPFTALDaagvALLAELIAAHLAR-----GGAVLLTTHQPLEL--AAARVLDLGDFK 206
PRK10908 PRK10908
cell division ATP-binding protein FtsE;
8-222 7.01e-43

cell division ATP-binding protein FtsE;


Pssm-ID: 182829 [Multi-domain]  Cd Length: 222  Bit Score: 148.48  E-value: 7.01e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131020733   8 LRLENVTKIFKDKKNnteviAVNNSTFEIKPGELITLLGPSGCGKTTTLRMVAGFELPTKGKIYIGNEDVTFL-----PP 82
Cdd:PRK10908    2 IRFEHVSKAYLGGRQ-----ALQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDITRLknrevPF 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131020733  83 NKRDTATVFQSYGLFPHMTVFDNVAYGLKLRKLSREEIEKRVFEALEMVGLKDLASRAPSRLSGGQQQRVTLARSIIVEP 162
Cdd:PRK10908   77 LRRQIGMIFQDHHLLMDRTVYDNVAIPLIIAGASGDDIRRRVSAALDKVGLLDKAKNFPIQLSGGEQQRVGIARAVVNKP 156

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131020733 163 AILLLDEPLSNLDALLREQMRIEIKKIQRkLGITAIYVTHDRVEAMSLSDRIIVMKDGKI 222
Cdd:PRK10908  157 AVLLADEPTGNLDDALSEGILRLFEEFNR-VGVTVLMATHDIGLISRRSYRMLTLSDGHL 215
CydD COG4988
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ...
 5-233 7.08e-43

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: 156.46  E-value: 7.08e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131020733   5 QVSLRLENVTKIFKDKKNnteviAVNNSTFEIKPGELITLLGPSGCGKTTTLRMVAGFELPTKGKIYIGNEDVTFLPPN- 83
Cdd:COG4988   334 PPSIELEDVSFSYPGGRP-----ALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPPYSGSILINGVDLSDLDPAs 408

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131020733  84 -KRDTATVFQSYGLFpHMTVFDNVAygLKLRKLSREEIEkrvfEALEMVGLKDLASRAP-----------SRLSGGQQQR 151
Cdd:COG4988   409 wRRQIAWVPQNPYLF-AGTIRENLR--LGRPDASDEELE----AALEAAGLDEFVAALPdgldtplgeggRGLSGGQAQR 481

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131020733 152 VTLARSIIVEPAILLLDEPLSNLDALLREQMRIEIKKIQRklGITAIYVTHdRVEAMSLSDRIIVMKDGKIMQIGTPVEI 231
Cdd:COG4988   482 LALARALLRDAPLLLLDEPTAHLDAETEAEILQALRRLAK--GRTVILITH-RLALLAQADRILVLDDGRIVEQGTHEEL 558


                  ..
gi 1131020733 232 YE 233
Cdd:COG4988   559 LA 560
ABC_ATPase cd00267
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ...
 9-221 2.39e-42

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: 144.69  E-value: 2.39e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131020733   9 RLENVTKIFKDKKnnteviAVNNSTFEIKPGELITLLGPSGCGKTTTLRMVAGFELPTKGKIYIGNEDVTFLPP--NKRD 86
Cdd:cd00267     1 EIENLSFRYGGRT------ALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGKDIAKLPLeeLRRR 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131020733  87 TATVFQsyglfphmtvfdnvayglklrklsreeiekrvfealemvglkdlasrapsrLSGGQQQRVTLARSIIVEPAILL 166
Cdd:cd00267    75 IGYVPQ---------------------------------------------------LSGGQRQRVALARALLLNPDLLL 103

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1131020733 167 LDEPLSNLDALLREQMRIEIKKIQRKlGITAIYVTHDRVEAMSLSDRIIVMKDGK 221
Cdd:cd00267   104 LDEPTSGLDPASRERLLELLRELAEE-GRTVIIVTHDPELAELAADRVIVLKDGK 157
PhnK COG1101
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ...
 8-222 2.84e-42

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


Pssm-ID: 440718 [Multi-domain]  Cd Length: 264  Bit Score: 147.92  E-value: 2.84e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131020733   8 LRLENVTKIFkDKKNNTEVIAVNNSTFEIKPGELITLLGPSGCGKTTTLRMVAGFELPTKGKIYIGNEDVTFLPPNKR-- 85
Cdd:COG1101     2 LELKNLSKTF-NPGTVNEKRALDGLNLTIEEGDFVTVIGSNGAGKSTLLNAIAGSLPPDSGSILIDGKDVTKLPEYKRak 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131020733  86 DTATVFQ--SYGLFPHMTVFDNVA--------YGLKLRkLSREEIEkRVFEALEMVGLkDLASRAPSR---LSGGQQQRV 152
Cdd:COG1101    81 YIGRVFQdpMMGTAPSMTIEENLAlayrrgkrRGLRRG-LTKKRRE-LFRELLATLGL-GLENRLDTKvglLSGGQRQAL 157

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1131020733 153 TLARSIIVEPAILLLDEPLSNLD----ALLreqmrIEI-KKIQRKLGITAIYVTHDRVEAMSLSDRIIVMKDGKI 222
Cdd:COG1101   158 SLLMATLTKPKLLLLDEHTAALDpktaALV-----LELtEKIVEENNLTTLMVTHNMEQALDYGNRLIMMHEGRI 227
ABC_Metallic_Cations cd03235
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ...
 9-224 3.85e-42

ATP-binding cassette domain of the metal-type transporters; This family includes transporters involved in the uptake of various metallic cations such as iron, manganese, and zinc. The ATPases of this group of transporters are very similar to members of iron-siderophore uptake family suggesting that they share a common ancestor. The best characterized metal-type ABC transporters are the YfeABCD system of Y. pestis, the SitABCD system of Salmonella enterica serovar Typhimurium, and the SitABCD transporter of Shigella flexneri. Moreover other uncharacterized homologs of these metal-type transporters are mainly found in pathogens like Haemophilus or enteroinvasive E. coli isolates.


Pssm-ID: 213202 [Multi-domain]  Cd Length: 213  Bit Score: 146.14  E-value: 3.85e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131020733   9 RLENVTKIFKDKknntevIAVNNSTFEIKPGELITLLGPSGCGKTTTLRMVAGFELPTKGKIYIGNEDVTFLPpnkRDTA 88
Cdd:cd03235     1 EVEDLTVSYGGH------PVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFGKPLEKER---KRIG 71

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131020733  89 TVFQSYGL---FPhMTVFDNVAYGL-----KLRKLSREEIEKrVFEALEMVGLKDLASRAPSRLSGGQQQRVTLARSIIV 160
Cdd:cd03235    72 YVPQRRSIdrdFP-ISVRDVVLMGLyghkgLFRRLSKADKAK-VDEALERVGLSELADRQIGELSGGQQQRVLLARALVQ 149

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1131020733 161 EPAILLLDEPLSNLDALLREQMRIEIKKIQRKlGITAIYVTHDRVEAMSLSDRIIVMKDGKIMQ 224
Cdd:cd03235   150 DPDLLLLDEPFAGVDPKTQEDIYELLRELRRE-GMTILVVTHDLGLVLEYFDRVLLLNRTVVAS 212
CydC COG4987
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ...
 4-235 4.40e-42

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: 154.54  E-value: 4.40e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131020733   4 KQVSLRLENVTKIFkdkkNNTEVIAVNNSTFEIKPGELITLLGPSGCGKTTTLRMVAGFELPTKGKIYIGNEDVTFLPPN 83
Cdd:COG4987   330 GGPSLELEDVSFRY----PGAGRPVLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFLDPQSGSITLGGVDLRDLDED 405

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131020733  84 K-RDTATVF-QSYGLFpHMTVFDNvayglkLRkLSREEI-EKRVFEALEMVGLKDLASRAP-----------SRLSGGQQ 149
Cdd:COG4987   406 DlRRRIAVVpQRPHLF-DTTLREN------LR-LARPDAtDEELWAALERVGLGDWLAALPdgldtwlgeggRRLSGGER 477

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131020733 150 QRVTLARSIIVEPAILLLDEPLSNLDALLREQMRIEIKKIQRklGITAIYVTHdRVEAMSLSDRIIVMKDGKIMQIGTPV 229
Cdd:COG4987   478 RRLALARALLRDAPILLLDEPTEGLDAATEQALLADLLEALA--GRTVLLITH-RLAGLERMDRILVLEDGRIVEQGTHE 554


                  ....*.
gi 1131020733 230 EIYEDP 235
Cdd:COG4987   555 ELLAQN 560
ABCC_MRP_Like cd03228
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ...
 8-221 4.76e-42

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: 144.45  E-value: 4.76e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131020733   8 LRLENVTKIFKDKKNNteviAVNNSTFEIKPGELITLLGPSGCGKTTTLRMVAGFELPTKGKIYIGNEDVTFLPPNK-RD 86
Cdd:cd03228     1 IEFKNVSFSYPGRPKP----VLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGVDLRDLDLESlRK 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131020733  87 T-ATVFQSYGLFpHMTVFDNVayglklrklsreeiekrvfealemvglkdlasrapsrLSGGQQQRVTLARSIIVEPAIL 165
Cdd:cd03228    77 NiAYVPQDPFLF-SGTIRENI-------------------------------------LSGGQRQRIAIARALLRDPPIL 118

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1131020733 166 LLDEPLSNLDALLREQMRIEIKKIQRklGITAIYVTHdRVEAMSLSDRIIVMKDGK 221
Cdd:cd03228   119 ILDEATSALDPETEALILEALRALAK--GKTVIVIAH-RLSTIRDADRIIVLDDGR 171
YhaQ COG4152
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ...
 7-231 7.67e-42

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


Pssm-ID: 443322 [Multi-domain]  Cd Length: 298  Bit Score: 147.95  E-value: 7.67e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131020733   7 SLRLENVTKIFKDKKnnteviAVNNSTFEIKPGELITLLGPSGCGKTTTLRMVAGFELPTKGKIYIGNEDVTFLPPNK-- 84
Cdd:COG4152     1 MLELKGLTKRFGDKT------AVDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDSGEVLWDGEPLDPEDRRRig 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131020733  85 -----RdtatvfqsyGLFPHMTVFDNVAYGLKLRKLSREEIEKRVFEALEMVGLKDLASRAPSRLSGGQQQRVTLARSII 159
Cdd:COG4152    75 ylpeeR---------GLYPKMKVGEQLVYLARLKGLSKAEAKRRADEWLERLGLGDRANKKVEELSKGNQQKVQLIAALL 145

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1131020733 160 VEPAILLLDEPLSNLDALLREQMRIEIKKIQRKlGITAIYVTH--DRVEAmsLSDRIIVMKDGKIMQIGTPVEI 231
Cdd:COG4152   146 HDPELLILDEPFSGLDPVNVELLKDVIRELAAK-GTTVIFSSHqmELVEE--LCDRIVIINKGRKVLSGSVDEI 216
livG PRK11300
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
 27-235 5.12e-41

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


Pssm-ID: 183080 [Multi-domain]  Cd Length: 255  Bit Score: 144.75  E-value: 5.12e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131020733  27 IAVNNSTFEIKPGELITLLGPSGCGKTTTLRMVAGFELPTKGKIYIGNEDVTFLPPNK---RDTATVFQSYGLFPHMTVF 103
Cdd:PRK11300   19 LAVNNVNLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTILLRGQHIEGLPGHQiarMGVVRTFQHVRLFREMTVI 98

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131020733 104 DN--VAYGLKL--------------RKLSREEIEkRVFEALEMVGLKDLASRAPSRLSGGQQQRVTLARSIIVEPAILLL 167
Cdd:PRK11300   99 ENllVAQHQQLktglfsgllktpafRRAESEALD-RAATWLERVGLLEHANRQAGNLAYGQQRRLEIARCMVTQPEILML 177

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1131020733 168 DEPLSNLDALLREQMRIEIKKIQRKLGITAIYVTHDRVEAMSLSDRIIVMKDGKIMQIGTPVEIYEDP 235
Cdd:PRK11300  178 DEPAAGLNPKETKELDELIAELRNEHNVTVLLIEHDMKLVMGISDRIYVVNQGTPLANGTPEEIRNNP 245
PRK11264 PRK11264
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
 10-235 4.32e-40

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


Pssm-ID: 183063 [Multi-domain]  Cd Length: 250  Bit Score: 142.20  E-value: 4.32e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131020733  10 LENVTKIFKDKKnnteviAVNNSTFEIKPGELITLLGPSGCGKTTTLRMVAGFELPTKGKIYIGNEDV-TFLPPNKRDTA 88
Cdd:PRK11264    6 VKNLVKKFHGQT------VLHGIDLEVKPGEVVAIIGPSGSGKTTLLRCINLLEQPEAGTIRVGDITIdTARSLSQQKGL 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131020733  89 T---------VFQSYGLFPHMTVFDNVAYG-LKLRKLSREEIEKRVFEALEMVGLKDLASRAPSRLSGGQQQRVTLARSI 158
Cdd:PRK11264   80 IrqlrqhvgfVFQNFNLFPHRTVLENIIEGpVIVKGEPKEEATARARELLAKVGLAGKETSYPRRLSGGQQQRVAIARAL 159

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1131020733 159 IVEPAILLLDEPLSNLDALLREQMRIEIKKI-QRKLgiTAIYVTHDRVEAMSLSDRIIVMKDGKIMQIGTPVEIYEDP 235
Cdd:PRK11264  160 AMRPEVILFDEPTSALDPELVGEVLNTIRQLaQEKR--TMVIVTHEMSFARDVADRAIFMDQGRIVEQGPAKALFADP 235
LPS_export_lptB TIGR04406
LPS export ABC transporter ATP-binding protein; Members of this fmaily are LptB, the ...
 7-240 4.47e-40

LPS export ABC transporter ATP-binding protein; Members of this fmaily are LptB, the ATP-binding cassette protein of an ABC transporter involved in lipopolysaccharide export. [Cell envelope, Biosynthesis and degradation of surface polysaccharides and lipopolysaccharides, Transport and binding proteins, Other]


Pssm-ID: 275199 [Multi-domain]  Cd Length: 239  Bit Score: 141.64  E-value: 4.47e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131020733   7 SLRLENVTKIFKDKKnnteviAVNNSTFEIKPGELITLLGPSGCGKTTTLRMVAGFELPTKGKIYIGNEDVTFLPPNKRD 86
Cdd:TIGR04406   1 TLVAENLIKSYKKRK------VVNDVSLSVKSGEIVGLLGPNGAGKTTSFYMIVGLVRPDAGKILIDGQDITHLPMHERA 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131020733  87 TATV---FQSYGLFPHMTVFDNVAYGLKLRK-LSREEIEKRVFEALEMVGLKDLASRAPSRLSGGQQQRVTLARSIIVEP 162
Cdd:TIGR04406  75 RLGIgylPQEASIFRKLTVEENIMAVLEIRKdLDRAEREERLEALLEEFQISHLRDNKAMSLSGGERRRVEIARALATNP 154

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131020733 163 AILLLDEPLSNLDALlreqMRIEIKKIQRKL---GITAIYVTHDRVEAMSLSDRIIVMKDGKIMQIGTPVEIYEDPISKF 239
Cdd:TIGR04406 155 KFILLDEPFAGVDPI----AVGDIKKIIKHLkerGIGVLITDHNVRETLDICDRAYIISDGKVLAEGTPAEIVANEKVRR 230


                  .
gi 1131020733 240 V 240
Cdd:TIGR04406 231 V 231
ABCC_bacteriocin_exporters cd03245
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ...
 22-222 6.03e-40

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: 140.80  E-value: 6.03e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131020733  22 NNTEVIAVNNSTFEIKPGELITLLGPSGCGKTTTLRMVAGFELPTKGKIYIGNEDVTFLPPN--KRDTATVFQSYGLFpH 99
Cdd:cd03245    13 PNQEIPALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGTDIRQLDPAdlRRNIGYVPQDVTLF-Y 91

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131020733 100 MTVFDNVAYGLKLRKlsreeiEKRVFEALEMVGLKDLASRAP-----------SRLSGGQQQRVTLARSIIVEPAILLLD 168
Cdd:cd03245    92 GTLRDNITLGAPLAD------DERILRAAELAGVTDFVNKHPngldlqigergRGLSGGQRQAVALARALLNDPPILLLD 165

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1131020733 169 EPLSNLDalLREQMRIeIKKIQRKL-GITAIYVTHdRVEAMSLSDRIIVMKDGKI 222
Cdd:cd03245   166 EPTSAMD--MNSEERL-KERLRQLLgDKTLIIITH-RPSLLDLVDRIIVMDSGRI 216
ABC_drug_resistance_like cd03264
ABC-type multidrug transport system, ATPase component; The biological function of this family ...
 8-226 1.76e-39

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: 139.25  E-value: 1.76e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131020733   8 LRLENVTKIFKDKKnnteviAVNNSTFEIKPGeLITLLGPSGCGKTTTLRMVAGFELPTKGKIYIGNEDVTFLPPNKRDT 87
Cdd:cd03264     1 LQLENLTKRYGKKR------ALDGVSLTLGPG-MYGLLGPNGAGKTTLMRILATLTPPSSGTIRIDGQDVLKQPQKLRRR 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131020733  88 -ATVFQSYGLFPHMTVFDNVAYGLKLRKLSREEIEKRVFEALEMVGLKDLASRAPSRLSGGQQQRVTLARSIIVEPAILL 166
Cdd:cd03264    74 iGYLPQEFGVYPNFTVREFLDYIAWLKGIPSKEVKARVDEVLELVNLGDRAKKKIGSLSGGMRRRVGIAQALVGDPSILI 153

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1131020733 167 LDEPLSNLDAllrEQmRIEIKKIQRKLGITAIYV--THDRVEAMSLSDRIIVMKDGKIMQIG 226
Cdd:cd03264   154 VDEPTAGLDP---EE-RIRFRNLLSELGEDRIVIlsTHIVEDVESLCNQVAVLNKGKLVFEG 211
HisP COG4598
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism];
37-244 1.90e-39

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


Pssm-ID: 443652 [Multi-domain]  Cd Length: 259  Bit Score: 140.71  E-value: 1.90e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131020733  37 KPGELITLLGPSGCGKTTTLRMVAGFELPTKGKIYIGNEDVTFLPPNKRDT---------------ATVFQSYGLFPHMT 101
Cdd:COG4598    32 RKGDVISIIGSSGSGKSTFLRCINLLETPDSGEIRVGGEEIRLKPDRDGELvpadrrqlqrirtrlGMVFQSFNLWSHMT 111

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131020733 102 VFDNVAYG-LKLRKLSREEIEKRVFEALEMVGLKDLASRAPSRLSGGQQQRVTLARSIIVEPAILLLDEPLSNLDALLRE 180
Cdd:COG4598   112 VLENVIEApVHVLGRPKAEAIERAEALLAKVGLADKRDAYPAHLSGGQQQRAAIARALAMEPEVMLFDEPTSALDPELVG 191

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1131020733 181 qmriEIKKIQRKL---GITAIYVTHDRVEAMSLSDRIIVMKDGKIMQIGTPVEIYEDPISKFVAGFI 244
Cdd:COG4598   192 ----EVLKVMRDLaeeGRTMLVVTHEMGFARDVSSHVVFLHQGRIEEQGPPAEVFGNPKSERLRQFL 254
COG4559 COG4559
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism];
29-236 2.84e-39

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


Pssm-ID: 443620 [Multi-domain]  Cd Length: 258  Bit Score: 139.87  E-value: 2.84e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131020733  29 VNNSTFEIKPGELITLLGPSGCGKTTTLRMVAGFELPTKGKIYIGNEDVTFLPPN----KRdtATVFQSYGL-FPhMTVF 103
Cdd:COG4559    17 LDDVSLTLRPGELTAIIGPNGAGKSTLLKLLTGELTPSSGEVRLNGRPLAAWSPWelarRR--AVLPQHSSLaFP-FTVE 93

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131020733 104 DNVAYGLKLRKLSREEIEKRVFEALEMVGLKDLASRAPSRLSGGQQQRVTLAR-------SIIVEPAILLLDEPLSNLDa 176
Cdd:COG4559    94 EVVALGRAPHGSSAAQDRQIVREALALVGLAHLAGRSYQTLSGGEQQRVQLARvlaqlwePVDGGPRWLFLDEPTSALD- 172

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1131020733 177 lLREQ---MRIeIKKIQRKlGITAIYVTHDRVEAMSLSDRIIVMKDGKIMQIGTPVEIYEDPI 236
Cdd:COG4559   173 -LAHQhavLRL-ARQLARR-GGGVVAVLHDLNLAAQYADRILLLHQGRLVAQGTPEEVLTDEL 232
ABC_TM1139_LivF_branched cd03224
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ...
 28-234 3.62e-39

ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of the LIV-I bacterial ABC-type two-component transport system that imports neutral, branched-chain amino acids. The E. coli branched-chain amino acid transporter comprises a heterodimer of ABC transporters (LivF and LivG), a heterodimer of six-helix TM domains (LivM and LivH), and one of two alternative soluble periplasmic substrate binding proteins (LivK or LivJ). ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules.


Pssm-ID: 213191 [Multi-domain]  Cd Length: 222  Bit Score: 138.72  E-value: 3.62e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131020733  28 AVNNSTFEIKPGELITLLGPSGCGKTTTLRMVAGFELPTKGKIYIGNEDVTFLPPNKRDT---ATVFQSYGLFPHMTVFD 104
Cdd:cd03224    15 ILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDGRDITGLPPHERARagiGYVPEGRRIFPELTVEE 94

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131020733 105 NVAYGLKLRKLS-REEIEKRVFEALEMvgLKDLASRAPSRLSGGQQQRVTLARSIIVEPAILLLDEPLSNLDALLREQMR 183
Cdd:cd03224    95 NLLLGAYARRRAkRKARLERVYELFPR--LKERRKQLAGTLSGGEQQMLAIARALMSRPKLLLLDEPSEGLAPKIVEEIF 172

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1131020733 184 IEIKKIqRKLGITAIYVTHDRVEAMSLSDRIIVMKDGKIMQIGTPVEIYED 234
Cdd:cd03224   173 EAIREL-RDEGVTILLVEQNARFALEIADRAYVLERGRVVLEGTAAELLAD 222
L_ocin_972_ABC TIGR03608
putative bacteriocin export ABC transporter, lactococcin 972 group; A gene pair with a fairly ...
 10-215 6.90e-39

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


Pssm-ID: 188353 [Multi-domain]  Cd Length: 206  Bit Score: 137.36  E-value: 6.90e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131020733  10 LENVTKIFKDKknntevIAVNNSTFEIKPGELITLLGPSGCGKTTTLRMVAGFELPTKGKIYIgnEDVTFLPPNKRDTAT 89
Cdd:TIGR03608   1 LKNISKKFGDK------VILDDLNLTIEKGKMYAIIGESGSGKSTLLNIIGLLEKFDSGQVYL--NGQETPPLNSKKASK 72

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131020733  90 --------VFQSYGLFPHMTVFDNVAYGLKLRKLSREEIEKRVFEALEMVGLKDLASRAPSRLSGGQQQRVTLARSIIVE 161
Cdd:TIGR03608  73 frreklgyLFQNFALIENETVEENLDLGLKYKKLSKKEKREKKKEALEKVGLNLKLKQKIYELSGGEQQRVALARAILKP 152

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1131020733 162 PAILLLDEPLSNLDALLREQMrIEIKKIQRKLGITAIYVTHDrVEAMSLSDRII 215
Cdd:TIGR03608 153 PPLILADEPTGSLDPKNRDEV-LDLLLELNDEGKTIIIVTHD-PEVAKQADRVI 204
PRK13633 PRK13633
energy-coupling factor transporter ATPase;
11-234 9.95e-39

energy-coupling factor transporter ATPase;


Pssm-ID: 237453 [Multi-domain]  Cd Length: 280  Bit Score: 139.45  E-value: 9.95e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131020733  11 ENVTKIFKDKKNNTEVIAVNNSTFEIKPGELITLLGPSGCGKTTTLRMVAGFELPTKGKIYIGNEDVTflppNKRDTATV 90
Cdd:PRK13633    8 KNVSYKYESNEESTEKLALDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVYVDGLDTS----DEENLWDI 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131020733  91 FQSYGLfphmtVFDN-------------VAYGLKLRKLSREEIEKRVFEALEMVGLKDLASRAPSRLSGGQQQRVTLARS 157
Cdd:PRK13633   84 RNKAGM-----VFQNpdnqivativeedVAFGPENLGIPPEEIRERVDESLKKVGMYEYRRHAPHLLSGGQKQRVAIAGI 158

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1131020733 158 IIVEPAILLLDEPLSNLDALLREQMRIEIKKIQRKLGITAIYVTHDRVEAMSlSDRIIVMKDGKIMQIGTPVEIYED 234
Cdd:PRK13633  159 LAMRPECIIFDEPTAMLDPSGRREVVNTIKELNKKYGITIILITHYMEEAVE-ADRIIVMDSGKVVMEGTPKEIFKE 234
type_I_sec_LssB TIGR03375
type I secretion system ATPase, LssB family; Type I protein secretion is a system in some ...
 7-223 1.30e-38

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: 145.78  E-value: 1.30e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131020733   7 SLRLENVTkiFKdkKNNTEVIAVNNSTFEIKPGELITLLGPSGCGKTTTLRMVAGFELPTKGKIYIGNEDVTFLPPN--K 84
Cdd:TIGR03375 463 EIEFRNVS--FA--YPGQETPALDNVSLTIRPGEKVAIIGRIGSGKSTLLKLLLGLYQPTEGSVLLDGVDIRQIDPAdlR 538

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131020733  85 RDTATVFQSYGLFpHMTVFDNVAYGlklRKLSREEiekRVFEALEMVGLKDLASRAPS-----------RLSGGQQQRVT 153
Cdd:TIGR03375 539 RNIGYVPQDPRLF-YGTLRDNIALG---APYADDE---EILRAAELAGVTEFVRRHPDgldmqigergrSLSGGQRQAVA 611

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1131020733 154 LARSIIVEPAILLLDEPLSNLDALLREQMrieIKKIQRKL-GITAIYVTHdRVEAMSLSDRIIVMKDGKIM 223
Cdd:TIGR03375 612 LARALLRDPPILLLDEPTSAMDNRSEERF---KDRLKRWLaGKTLVLVTH-RTSLLDLVDRIIVMDNGRIV 678
PRK15079 PRK15079
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
 28-235 7.88e-38

oligopeptide ABC transporter ATP-binding protein OppF; Provisional


Pssm-ID: 185037 [Multi-domain]  Cd Length: 331  Bit Score: 138.30  E-value: 7.88e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131020733  28 AVNNSTFEIKPGELITLLGPSGCGKTTTLRMVAGFELPTKGKIYIGNEDVTFLPPNKR-----DTATVFQS--YGLFPHM 100
Cdd:PRK15079   36 AVDGVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGEVAWLGKDLLGMKDDEWravrsDIQMIFQDplASLNPRM 115

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131020733 101 TVFDNVAYGLKLR--KLSREEIEKRVFEALEMVGL-KDLASRAPSRLSGGQQQRVTLARSIIVEPAILLLDEPLSNLDAL 177
Cdd:PRK15079  116 TIGEIIAEPLRTYhpKLSRQEVKDRVKAMMLKVGLlPNLINRYPHEFSGGQCQRIGIARALILEPKLIICDEPVSALDVS 195

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1131020733 178 LREQMRIEIKKIQRKLGITAIYVTHDRVEAMSLSDRIIVMKDGKIMQIGTPVEIYEDP 235
Cdd:PRK15079  196 IQAQVVNLLQQLQREMGLSLIFIAHDLAVVKHISDRVLVMYLGHAVELGTYDEVYHNP 253
met_CoM_red_A2 TIGR03269
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ...
 8-234 9.60e-38

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: 141.86  E-value: 9.60e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131020733   8 LRLENVTKIFKDKKNNTeVIAVNNSTFEIKPGELITLLGPSGCGKTTTLRMVAGFELPTKGKIY--IGNE--DVTFLPPN 83
Cdd:TIGR03269 280 IKVRNVSKRYISVDRGV-VKAVDNVSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGEVNvrVGDEwvDMTKPGPD 358

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131020733  84 KRDTAT-----VFQSYGLFPHMTVFDNVAYGLKLrKLSREEIEKRVFEALEMVGL-----KDLASRAPSRLSGGQQQRVT 153
Cdd:TIGR03269 359 GRGRAKryigiLHQEYDLYPHRTVLDNLTEAIGL-ELPDELARMKAVITLKMVGFdeekaEEILDKYPDELSEGERHRVA 437

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131020733 154 LARSIIVEPAILLLDEPLSNLDALLREQMRIEIKKIQRKLGITAIYVTHDRVEAMSLSDRIIVMKDGKIMQIGTPVEIYE 233
Cdd:TIGR03269 438 LAQVLIKEPRIVILDEPTGTMDPITKVDVTHSILKAREEMEQTFIIVSHDMDFVLDVCDRAALMRDGKIVKIGDPEEIVE 517


                  .
gi 1131020733 234 D 234
Cdd:TIGR03269 518 E 518
cbiO PRK13632
cobalt transporter ATP-binding subunit; Provisional
 1-248 1.59e-37

cobalt transporter ATP-binding subunit; Provisional


Pssm-ID: 237452 [Multi-domain]  Cd Length: 271  Bit Score: 135.89  E-value: 1.59e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131020733   1 MKKKQVSLRLENVTKIFKDKKNNteviAVNNSTFEIKPGELITLLGPSGCGKTTTLRMVAGFELPTKGKIYIGNEDVTF- 79
Cdd:PRK13632    1 IKNKSVMIKVENVSFSYPNSENN----ALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIDGITISKe 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131020733  80 -LPPNKRDTATVFQSY-GLFPHMTVFDNVAYGLKLRKLSREEIEKRVFEALEMVGLKDLASRAPSRLSGGQQQRVTLARS 157
Cdd:PRK13632   77 nLKEIRKKIGIIFQNPdNQFIGATVEDDIAFGLENKKVPPKKMKDIIDDLAKKVGMEDYLDKEPQNLSGGQKQRVAIASV 156

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131020733 158 IIVEPAILLLDEPLSNLDALLREQMRIEIKKIQRKLGITAIYVTHDRVEAMsLSDRIIVMKDGKIMQIGTPVEIYEDP-- 235
Cdd:PRK13632  157 LALNPEIIIFDESTSMLDPKGKREIKKIMVDLRKTRKKTLISITHDMDEAI-LADKVIVFSEGKLIAQGKPKEILNNKei 235

                         250
                  ....*....|....*
gi 1131020733 236 --ISKFVAGFIGKVA 248
Cdd:PRK13632  236 leKAKIDSPFIYKLS 250
cbiO PRK13640
energy-coupling factor transporter ATPase;
11-235 3.74e-37

energy-coupling factor transporter ATPase;


Pssm-ID: 184200 [Multi-domain]  Cd Length: 282  Bit Score: 135.31  E-value: 3.74e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131020733  11 ENVTKIFKDkknnTEVIAVNNSTFEIKPGELITLLGPSGCGKTTTLRMVAGFELP---TKGKIYIG----NEDVTFlppN 83
Cdd:PRK13640    9 KHVSFTYPD----SKKPALNDISFSIPRGSWTALIGHNGSGKSTISKLINGLLLPddnPNSKITVDgitlTAKTVW---D 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131020733  84 KRD-TATVFQSY-GLFPHMTVFDNVAYGLKLRKLSREEIEKRVFEALEMVGLKDLASRAPSRLSGGQQQRVTLARSIIVE 161
Cdd:PRK13640   82 IREkVGIVFQNPdNQFVGATVGDDVAFGLENRAVPRPEMIKIVRDVLADVGMLDYIDSEPANLSGGQKQRVAIAGILAVE 161

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1131020733 162 PAILLLDEPLSNLDALLREQMRIEIKKIQRKLGITAIYVTHDRVEAmSLSDRIIVMKDGKIMQIGTPVEIYEDP 235
Cdd:PRK13640  162 PKIIILDESTSMLDPAGKEQILKLIRKLKKKNNLTVISITHDIDEA-NMADQVLVLDDGKLLAQGSPVEIFSKV 234
modC PRK11144
molybdenum ABC transporter ATP-binding protein ModC;
38-236 8.23e-37

molybdenum ABC transporter ATP-binding protein ModC;


Pssm-ID: 182993 [Multi-domain]  Cd Length: 352  Bit Score: 136.16  E-value: 8.23e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131020733  38 PGELIT-LLGPSGCGKTTTLRMVAGFELPTKGKIYIGN------EDVTFLPPNKRDTATVFQSYGLFPHMTVFDNVAYGL 110
Cdd:PRK11144   22 PAQGITaIFGRSGAGKTSLINAISGLTRPQKGRIVLNGrvlfdaEKGICLPPEKRRIGYVFQDARLFPHYKVRGNLRYGM 101

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131020733 111 KlrKLSREEIEKRVfealEMVGLKDLASRAPSRLSGGQQQRVTLARSIIVEPAILLLDEPLSNLDalL---REQMRIeIK 187
Cdd:PRK11144  102 A--KSMVAQFDKIV----ALLGIEPLLDRYPGSLSGGEKQRVAIGRALLTAPELLLMDEPLASLD--LprkRELLPY-LE 172

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 1131020733 188 KIQRKLGITAIYVTHDRVEAMSLSDRIIVMKDGKIMQIGTPVEIYEDPI 236
Cdd:PRK11144  173 RLAREINIPILYVSHSLDEILRLADRVVVLEQGKVKAFGPLEEVWASSA 221
LivF COG0410
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ...
 25-235 2.15e-36

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


Pssm-ID: 440179 [Multi-domain]  Cd Length: 236  Bit Score: 131.64  E-value: 2.15e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131020733  25 EVIAVNNSTFEIKPGELITLLGPSGCGKTTTLRMVAGFELPTKGKIYIGNEDVTFLPPNKRDT---ATVFQSYGLFPHMT 101
Cdd:COG0410    15 GIHVLHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRSGSIRFDGEDITGLPPHRIARlgiGYVPEGRRIFPSLT 94

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131020733 102 VFDN---VAYGLKLRKLSREEIEkRVFEALEMvgLKDLASRAPSRLSGGQQQRVTLARSIIVEPAILLLDEPLSNLDALL 178
Cdd:COG0410    95 VEENlllGAYARRDRAEVRADLE-RVYELFPR--LKERRRQRAGTLSGGEQQMLAIGRALMSRPKLLLLDEPSLGLAPLI 171

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1131020733 179 REQMRIEIKKIqRKLGITAIYVTHDRVEAMSLSDRIIVMKDGKIMQIGTPVEIYEDP 235
Cdd:COG0410   172 VEEIFEIIRRL-NREGVTILLVEQNARFALEIADRAYVLERGRIVLEGTAAELLADP 227
YejF COG4172
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ...
 8-235 2.44e-36

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: 137.89  E-value: 2.44e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131020733   8 LRLENVTKIFKDKKNNTEviAVNNSTFEIKPGELITLLGPSGCGKTTT----LRMVAGFELPTKGKIYIGNEDVTFLPPN 83
Cdd:COG4172     7 LSVEDLSVAFGQGGGTVE--AVKGVSFDIAAGETLALVGESGSGKSVTalsiLRLLPDPAAHPSGSILFDGQDLLGLSER 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131020733  84 K------RDTATVFQ----SygLFPHMTVFDNVAYGLKL-RKLSREEIEKRVFEALEMVGLKDLASRA---PSRLSGGQQ 149
Cdd:COG4172    85 ElrrirgNRIAMIFQepmtS--LNPLHTIGKQIAEVLRLhRGLSGAAARARALELLERVGIPDPERRLdayPHQLSGGQR 162

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131020733 150 QRVTLARSIIVEPAILLLDEPLSNLDALLREQMRIEIKKIQRKLGITAIYVTHDR--VEAMslSDRIIVMKDGKIMQIGT 227
Cdd:COG4172   163 QRVMIAMALANEPDLLIADEPTTALDVTVQAQILDLLKDLQRELGMALLLITHDLgvVRRF--ADRVAVMRQGEIVEQGP 240


                  ....*...
gi 1131020733 228 PVEIYEDP 235
Cdd:COG4172   241 TAELFAAP 248
PRK11831 PRK11831
phospholipid ABC transporter ATP-binding protein MlaF;
39-249 5.46e-36

phospholipid ABC transporter ATP-binding protein MlaF;


Pssm-ID: 236997 [Multi-domain]  Cd Length: 269  Bit Score: 131.81  E-value: 5.46e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131020733  39 GELITLLGPSGCGKTTTLRMVAGFELPTKGKIYIGNEDV-----TFLPPNKRDTATVFQSYGLFPHMTVFDNVAYGLKLR 113
Cdd:PRK11831   33 GKITAIMGPSGIGKTTLLRLIGGQIAPDHGEILFDGENIpamsrSRLYTVRKRMSMLFQSGALFTDMNVFDNVAYPLREH 112

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131020733 114 -KLSREEIEKRVFEALEMVGLKDLASRAPSRLSGGQQQRVTLARSIIVEPAILLLDEPLSNLDALLREQMRIEIKKIQRK 192
Cdd:PRK11831  113 tQLPAPLLHSTVMMKLEAVGLRGAAKLMPSELSGGMARRAALARAIALEPDLIMFDEPFVGQDPITMGVLVKLISELNSA 192

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1131020733 193 LGITAIYVTHDRVEAMSLSDRIIVMKDGKIMQIGTPVEIYEDP---ISKFVAGFI-GKVAF 249
Cdd:PRK11831  193 LGVTCVVVSHDVPEVLSIADHAYIVADKKIVAHGSAQALQANPdprVRQFLDGIAdGPVPF 253
hmuV PRK13548
hemin importer ATP-binding subunit; Provisional
 29-230 5.65e-36

hemin importer ATP-binding subunit; Provisional


Pssm-ID: 237422 [Multi-domain]  Cd Length: 258  Bit Score: 131.43  E-value: 5.65e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131020733  29 VNNSTFEIKPGELITLLGPSGCGKTTTLRMVAGFELPTKGKIYIGNEDVTFLPPNKRDT--ATVFQSYGL-FPhMTVFDN 105
Cdd:PRK13548   18 LDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLNGRPLADWSPAELARrrAVLPQHSSLsFP-FTVEEV 96

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131020733 106 VAYGLKLRKLSREEIEKRVFEALEMVGLKDLASRAPSRLSGGQQQRVTLARsiiV---------EPAILLLDEPLSNLDa 176
Cdd:PRK13548   97 VAMGRAPHGLSRAEDDALVAAALAQVDLAHLAGRDYPQLSGGEQQRVQLAR---VlaqlwepdgPPRWLLLDEPTSALD- 172

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1131020733 177 lLREQ---MRIeIKKIQRKLGITAIYVTHDRVEAMSLSDRIIVMKDGKIMQIGTPVE 230
Cdd:PRK13548  173 -LAHQhhvLRL-ARQLAHERGLAVIVVLHDLNLAARYADRIVLLHQGRLVADGTPAE 227
ABC_BcrA_bacitracin_resist cd03268
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ...
 8-222 5.98e-36

ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily represents ABC transporters involved in peptide antibiotic resistance. Bacitracin is a dodecapeptide antibiotic produced by B. licheniformis and B. subtilis. The synthesis of bacitracin is non-ribosomally catalyzed by a multi-enzyme complex BcrABC. Bacitracin has potent antibiotic activity against gram-positive bacteria. The inhibition of peptidoglycan biosynthesis is the best characterized bacterial effect of bacitracin. The bacitracin resistance of B. licheniformis is mediated by the ABC transporter Bcr which is composed of two identical BcrA ATP-binding subunits and one each of the integral membrane proteins, BcrB and BcrC. B. subtilis cells carrying bcr genes on high-copy number plasmids develop collateral detergent sensitivity, a similar phenomenon in human cells with overexpressed multi-drug resistance P-glycoprotein.


Pssm-ID: 213235 [Multi-domain]  Cd Length: 208  Bit Score: 129.64  E-value: 5.98e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131020733   8 LRLENVTKIFKDKKnnteviAVNNSTFEIKPGELITLLGPSGCGKTTTLRMVAGFELPTKGKIYIGNEDVTFLPPNKRDT 87
Cdd:cd03268     1 LKTNDLTKTYGKKR------VLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEITFDGKSYQKNIEALRRI 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131020733  88 ATVFQSYGLFPHMTVFDNVAYGLKLRKLSREEIEkrvfEALEMVGLKDLASRAPSRLSGGQQQRVTLARSIIVEPAILLL 167
Cdd:cd03268    75 GALIEAPGFYPNLTARENLRLLARLLGIRKKRID----EVLDVVGLKDSAKKKVKGFSLGMKQRLGIALALLGNPDLLIL 150

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1131020733 168 DEPLSNLDALLREQMRIEIKKIqRKLGITAIYVTHDRVEAMSLSDRIIVMKDGKI 222
Cdd:cd03268   151 DEPTNGLDPDGIKELRELILSL-RDQGITVLISSHLLSEIQKVADRIGIINKGKL 204
cbiO PRK13639
cobalt transporter ATP-binding subunit; Provisional
 28-235 8.36e-36

cobalt transporter ATP-binding subunit; Provisional


Pssm-ID: 184199 [Multi-domain]  Cd Length: 275  Bit Score: 131.35  E-value: 8.36e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131020733  28 AVNNSTFEIKPGELITLLGPSGCGKTTTLRMVAGFELPTKGKIYIGNEDVTF----LPPNKRDTATVFQSYG--LFPHmT 101
Cdd:PRK13639   17 ALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIKGEPIKYdkksLLEVRKTVGIVFQNPDdqLFAP-T 95

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131020733 102 VFDNVAYGLKLRKLSREEIEKRVFEALEMVGLKDLASRAPSRLSGGQQQRVTLARSIIVEPAILLLDEPLSNLDALLREQ 181
Cdd:PRK13639   96 VEEDVAFGPLNLGLSKEEVEKRVKEALKAVGMEGFENKPPHHLSGGQKKRVAIAGILAMKPEIIVLDEPTSGLDPMGASQ 175

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1131020733 182 MRIEIKKIQRKlGITAIYVTHDRVEAMSLSDRIIVMKDGKIMQIGTPVEIYEDP 235
Cdd:PRK13639  176 IMKLLYDLNKE-GITIIISTHDVDLVPVYADKVYVMSDGKIIKEGTPKEVFSDI 228
cbiO PRK13642
energy-coupling factor transporter ATPase;
8-232 8.53e-36

energy-coupling factor transporter ATPase;


Pssm-ID: 184202 [Multi-domain]  Cd Length: 277  Bit Score: 131.37  E-value: 8.53e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131020733   8 LRLENVtkIFKDKKNnTEVIAVNNSTFEIKPGELITLLGPSGCGKTTTLRMVAGFELPTKGKIYIGNEDVTF--LPPNKR 85
Cdd:PRK13642    5 LEVENL--VFKYEKE-SDVNQLNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDGELLTAenVWNLRR 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131020733  86 DTATVFQSY-GLFPHMTVFDNVAYGLKLRKLSREEIEKRVFEALEMVGLKDLASRAPSRLSGGQQQRVTLARSIIVEPAI 164
Cdd:PRK13642   82 KIGMVFQNPdNQFVGATVEDDVAFGMENQGIPREEMIKRVDEALLAVNMLDFKTREPARLSGGQKQRVAVAGIIALRPEI 161

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1131020733 165 LLLDEPLSNLDALLREQMRIEIKKIQRKLGITAIYVTHDRVEAMSlSDRIIVMKDGKIMQIGTPVEIY 232
Cdd:PRK13642  162 IILDESTSMLDPTGRQEIMRVIHEIKEKYQLTVLSITHDLDEAAS-SDRILVMKAGEIIKEAAPSELF 228
MglA COG1129
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
8-227 1.02e-35

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


Pssm-ID: 440745 [Multi-domain]  Cd Length: 497  Bit Score: 135.92  E-value: 1.02e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131020733   8 LRLENVTKIFKDkknnteVIAVNNSTFEIKPGELITLLGPSGCGKTTTLRMVAGFELPTKGKIYIGNEDVTFLPPnkRDT 87
Cdd:COG1129     5 LEMRGISKSFGG------VKALDGVSLELRPGEVHALLGENGAGKSTLMKILSGVYQPDSGEILLDGEPVRFRSP--RDA 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131020733  88 -----ATVFQSYGLFPHMTVFDNVAYGLKLRK---LSREEIEKRVFEALEMVGLkDLASRAP-SRLSGGQQQRVTLARSI 158
Cdd:COG1129    77 qaagiAIIHQELNLVPNLSVAENIFLGREPRRgglIDWRAMRRRARELLARLGL-DIDPDTPvGDLSVAQQQLVEIARAL 155

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1131020733 159 IVEPAILLLDEPLSNLDA----LLREQMRieikKIQRKlGITAIYVTHDRVEAMSLSDRIIVMKDGKImqIGT 227
Cdd:COG1129   156 SRDARVLILDEPTASLTEreveRLFRIIR----RLKAQ-GVAIIYISHRLDEVFEIADRVTVLRDGRL--VGT 221
lolD PRK11629
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
8-224 2.50e-35

lipoprotein-releasing ABC transporter ATP-binding protein LolD;


Pssm-ID: 183244 [Multi-domain]  Cd Length: 233  Bit Score: 129.17  E-value: 2.50e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131020733   8 LRLENVTKIFKDKKNNTEVIavNNSTFEIKPGELITLLGPSGCGKTTTLRMVAGFELPTKGK-IYIGNEDVTFLPPNK-- 84
Cdd:PRK11629    6 LQCDNLCKRYQEGSVQTDVL--HNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDvIFNGQPMSKLSSAAKae 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131020733  85 ---RDTATVFQSYGLFPHMTVFDNVAYGLKLRKLSREEIEKRVFEALEMVGLKDLASRAPSRLSGGQQQRVTLARSIIVE 161
Cdd:PRK11629   84 lrnQKLGFIYQFHHLLPDFTALENVAMPLLIGKKKPAEINSRALEMLAAVGLEHRANHRPSELSGGERQRVAIARALVNN 163

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1131020733 162 PAILLLDEPLSNLDALLREQMRIEIKKIQRKLGITAIYVTHDRVEAMSLSdRIIVMKDGKIMQ 224
Cdd:PRK11629  164 PRLVLADEPTGNLDARNADSIFQLLGELNRLQGTAFLVVTHDLQLAKRMS-RQLEMRDGRLTA 225
cbiO PRK13634
cobalt transporter ATP-binding subunit; Provisional
 36-235 3.36e-35

cobalt transporter ATP-binding subunit; Provisional


Pssm-ID: 237454 [Multi-domain]  Cd Length: 290  Bit Score: 130.14  E-value: 3.36e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131020733  36 IKPGELITLLGPSGCGKTTTLRMVAGFELPTKGKIYIGNEDVTF------LPPNKRDTATVFQsyglFPHM-----TVFD 104
Cdd:PRK13634   30 IPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVTIGERVITAgkknkkLKPLRKKVGIVFQ----FPEHqlfeeTVEK 105

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131020733 105 NVAYGLKLRKLSREEIEKRVFEALEMVGL-KDLASRAPSRLSGGQQQRVTLARSIIVEPAILLLDEPLSNLDALLREQMR 183
Cdd:PRK13634  106 DICFGPMNFGVSEEDAKQKAREMIELVGLpEELLARSPFELSGGQMRRVAIAGVLAMEPEVLVLDEPTAGLDPKGRKEMM 185

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1131020733 184 IEIKKIQRKLGITAIYVTHDRVEAMSLSDRIIVMKDGKIMQIGTPVEIYEDP 235
Cdd:PRK13634  186 EMFYKLHKEKGLTTVLVTHSMEDAARYADQIVVMHKGTVFLQGTPREIFADP 237
fecE PRK11231
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
7-237 3.45e-35

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


Pssm-ID: 183044 [Multi-domain]  Cd Length: 255  Bit Score: 129.36  E-value: 3.45e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131020733   7 SLRLENVTKIFKDKKnnteviAVNNSTFEIKPGELITLLGPSGCGKTTTLRMVAGFELPTKGKIYIGNEDVTFLPPNK-- 84
Cdd:PRK11231    2 TLRTENLTVGYGTKR------ILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDKPISMLSSRQla 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131020733  85 RDTATVFQSYgLFPH-MTVFDNVAYG----LKL-RKLSREEiEKRVFEALEMVGLKDLASRAPSRLSGGQQQRVTLARSI 158
Cdd:PRK11231   76 RRLALLPQHH-LTPEgITVRELVAYGrspwLSLwGRLSAED-NARVNQAMEQTRINHLADRRLTDLSGGQRQRAFLAMVL 153

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131020733 159 IVEPAILLLDEPLSNLDalLREQmrIEIKKIQRKL---GITAIYVTHDRVEAMSLSDRIIVMKDGKIMQIGTP------- 228
Cdd:PRK11231  154 AQDTPVVLLDEPTTYLD--INHQ--VELMRLMRELntqGKTVVTVLHDLNQASRYCDHLVVLANGHVMAQGTPeevmtpg 229

                         250
                  ....*....|....*...
gi 1131020733 229 ---------VEIYEDPIS 237
Cdd:PRK11231  230 llrtvfdveAEIHPEPVS 247
ModF COG1119
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ...
 8-231 3.83e-35

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: 129.05  E-value: 3.83e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131020733   8 LRLENVTKIFKDKKnnteviAVNNSTFEIKPGELITLLGPSGCGKTTTLRMVAGFELPTKGkiyignEDVTFLPpNKRDT 87
Cdd:COG1119     4 LELRNVTVRRGGKT------ILDDISWTVKPGEHWAILGPNGAGKSTLLSLITGDLPPTYG------NDVRLFG-ERRGG 70

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131020733  88 ATVF---QSYGLF---------PHMTVFDNVAYGLK-----LRKLSREEIEkRVFEALEMVGLKDLASRAPSRLSGGQQQ 150
Cdd:COG1119    71 EDVWelrKRIGLVspalqlrfpRDETVLDVVLSGFFdsiglYREPTDEQRE-RARELLELLGLAHLADRPFGTLSQGEQR 149

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131020733 151 RVTLARSIIVEPAILLLDEPLSNLDALLREQMRIEIKKIQRKLGITAIYVTHDRVEAMSLSDRIIVMKDGKIMQIGTPVE 230
Cdd:COG1119   150 RVLIARALVKDPELLILDEPTAGLDLGARELLLALLDKLAAEGAPTLVLVTHHVEEIPPGITHVLLLKDGRVVAAGPKEE 229


                  .
gi 1131020733 231 I 231
Cdd:COG1119   230 V 230
cbiO PRK13648
cobalt transporter ATP-binding subunit; Provisional
 17-234 4.75e-35

cobalt transporter ATP-binding subunit; Provisional


Pssm-ID: 184207 [Multi-domain]  Cd Length: 269  Bit Score: 129.10  E-value: 4.75e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131020733  17 FKD---KKNNTEVIAVNNSTFEIKPGELITLLGPSGCGKTTTLRMVAGFELPTKGKIYIGNEDVTflPPNKRD----TAT 89
Cdd:PRK13648   10 FKNvsfQYQSDASFTLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIFYNNQAIT--DDNFEKlrkhIGI 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131020733  90 VFQS-YGLFPHMTVFDNVAYGLKLRKLSREEIEKRVFEALEMVGLKDLASRAPSRLSGGQQQRVTLARSIIVEPAILLLD 168
Cdd:PRK13648   88 VFQNpDNQFVGSIVKYDVAFGLENHAVPYDEMHRRVSEALKQVDMLERADYEPNALSGGQKQRVAIAGVLALNPSVIILD 167

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1131020733 169 EPLSNLDALLREQMRIEIKKIQRKLGITAIYVTHDRVEAMSlSDRIIVMKDGKIMQIGTPVEIYED 234
Cdd:PRK13648  168 EATSMLDPDARQNLLDLVRKVKSEHNITIISITHDLSEAME-ADHVIVMNKGTVYKEGTPTEIFDH 232
dppF PRK11308
dipeptide transporter ATP-binding subunit; Provisional
 26-235 9.27e-35

dipeptide transporter ATP-binding subunit; Provisional


Pssm-ID: 236898 [Multi-domain]  Cd Length: 327  Bit Score: 130.08  E-value: 9.27e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131020733  26 VIAVNNSTFEIKPGELITLLGPSGCGKTTTLRMVAGFELPTKGKIYIGNEDVTFLPPN-----KRDTATVFQS-YG-LFP 98
Cdd:PRK11308   28 VKALDGVSFTLERGKTLAVVGESGCGKSTLARLLTMIETPTGGELYYQGQDLLKADPEaqkllRQKIQIVFQNpYGsLNP 107

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131020733  99 HMTVFDNVAYGLKLR-KLSREEIEKRVFEALEMVGLK-DLASRAPSRLSGGQQQRVTLARSIIVEPAILLLDEPLSNLDA 176
Cdd:PRK11308  108 RKKVGQILEEPLLINtSLSAAERREKALAMMAKVGLRpEHYDRYPHMFSGGQRQRIAIARALMLDPDVVVADEPVSALDV 187

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1131020733 177 LLREQMRIEIKKIQRKLGITAIYVTHDRVEAMSLSDRIIVMKDGKIMQIGTPVEIYEDP 235
Cdd:PRK11308  188 SVQAQVLNLMMDLQQELGLSYVFISHDLSVVEHIADEVMVMYLGRCVEKGTKEQIFNNP 246
PRK10619 PRK10619
histidine ABC transporter ATP-binding protein HisP;
33-244 1.06e-34

histidine ABC transporter ATP-binding protein HisP;


Pssm-ID: 182592 [Multi-domain]  Cd Length: 257  Bit Score: 128.16  E-value: 1.06e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131020733  33 TFEIKPGELITLLGPSGCGKTTTLRMVAGFELPTKGKIYIGNEDVTFLppnkRDT-------------------ATVFQS 93
Cdd:PRK10619   25 SLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNGQTINLV----RDKdgqlkvadknqlrllrtrlTMVFQH 100

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131020733  94 YGLFPHMTVFDNVAYG-LKLRKLSREEIEKRVFEALEMVGLKDLA-SRAPSRLSGGQQQRVTLARSIIVEPAILLLDEPL 171
Cdd:PRK10619  101 FNLWSHMTVLENVMEApIQVLGLSKQEARERAVKYLAKVGIDERAqGKYPVHLSGGQQQRVSIARALAMEPEVLLFDEPT 180

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1131020733 172 SNLDA-LLREQMRIeIKKIQRKlGITAIYVTHDRVEAMSLSDRIIVMKDGKIMQIGTPVEIYEDPISKFVAGFI 244
Cdd:PRK10619  181 SALDPeLVGEVLRI-MQQLAEE-GKTMVVVTHEMGFARHVSSHVIFLHQGKIEEEGAPEQLFGNPQSPRLQQFL 252
ABCC_Protease_Secretion cd03246
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ...
 8-222 1.40e-34

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: 125.02  E-value: 1.40e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131020733   8 LRLENVTkiFKDKKNNTEVIavNNSTFEIKPGELITLLGPSGCGKTTTLRMVAGFELPTKGKIYIGNEDV-TFLPPNKRD 86
Cdd:cd03246     1 LEVENVS--FRYPGAEPPVL--RNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDGADIsQWDPNELGD 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131020733  87 T-ATVFQSYGLFPHmTVFDNVayglklrklsreeiekrvfealemvglkdlasrapsrLSGGQQQRVTLARSIIVEPAIL 165
Cdd:cd03246    77 HvGYLPQDDELFSG-SIAENI-------------------------------------LSGGQRQRLGLARALYGNPRIL 118

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1131020733 166 LLDEPLSNLDaLLREQMRIEIKKIQRKLGITAIYVTHdRVEAMSLSDRIIVMKDGKI 222
Cdd:cd03246   119 VLDEPNSHLD-VEGERALNQAIAALKAAGATRIVIAH-RPETLASADRILVLEDGRV 173
PRK14247 PRK14247
phosphate ABC transporter ATP-binding protein; Provisional
 23-242 1.66e-34

phosphate ABC transporter ATP-binding protein; Provisional


Pssm-ID: 172735 [Multi-domain]  Cd Length: 250  Bit Score: 127.34  E-value: 1.66e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131020733  23 NTEVIAvnNSTFEIKPGELITLLGPSGCGKTTTLRMVAGF-----ELPTKGKIYIGNEDVTFLPPN--KRDTATVFQSYG 95
Cdd:PRK14247   15 QVEVLD--GVNLEIPDNTITALMGPSGSGKSTLLRVFNRLielypEARVSGEVYLDGQDIFKMDVIelRRRVQMVFQIPN 92

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131020733  96 LFPHMTVFDNVAYGLKLRKL--SREEIEKRVFEALEMVGL----KDLASRAPSRLSGGQQQRVTLARSIIVEPAILLLDE 169
Cdd:PRK14247   93 PIPNLSIFENVALGLKLNRLvkSKKELQERVRWALEKAQLwdevKDRLDAPAGKLSGGQQQRLCIARALAFQPEVLLADE 172

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1131020733 170 PLSNLDAllREQMRIEIKKIQRKLGITAIYVTHDRVEAMSLSDRIIVMKDGKIMQIGTPVEIYEDP----ISKFVAG 242
Cdd:PRK14247  173 PTANLDP--ENTAKIESLFLELKKDMTIVLVTHFPQQAARISDYVAFLYKGQIVEWGPTREVFTNPrhelTEKYVTG 247
ABC_Carb_Monos_I cd03216
First domain of the ATP-binding cassette component of monosaccharide transport system; This ...
 8-222 1.73e-34

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: 124.46  E-value: 1.73e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131020733   8 LRLENVTKIFKDkknnteVIAVNNSTFEIKPGELITLLGPSGCGKTTTLRMVAGFELPTKGKIYIGNEDVTFLPPN---K 84
Cdd:cd03216     1 LELRGITKRFGG------VKALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVDGKEVSFASPRdarR 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131020733  85 RDTATVFQsyglfphmtvfdnvayglklrklsreeiekrvfealemvglkdlasrapsrLSGGQQQRVTLARSIIVEPAI 164
Cdd:cd03216    75 AGIAMVYQ---------------------------------------------------LSVGERQMVEIARALARNARL 103

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1131020733 165 LLLDEPLSNLDALLREQMRIEIKKIQRKlGITAIYVTHDRVEAMSLSDRIIVMKDGKI 222
Cdd:cd03216   104 LILDEPTAALTPAEVERLFKVIRRLRAQ-GVAVIFISHRLDEVFEIADRVTVLRDGRV 160
ABC_MTABC3_MDL1_MDL2 cd03249
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ...
 25-233 2.27e-34

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: 126.50  E-value: 2.27e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131020733  25 EVIAVNNSTFEIKPGELITLLGPSGCGKTTTLRMVAGFELPTKGKIYIGNEDVTFLPPN--KRDTATVFQSYGLFPhMTV 102
Cdd:cd03249    15 DVPILKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEILLDGVDIRDLNLRwlRSQIGLVSQEPVLFD-GTI 93

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131020733 103 FDNVAYGLKLRKLSREEIEKRVFEALEMV-----GLKDLASRAPSRLSGGQQQRVTLARSIIVEPAILLLDEPLSNLDAl 177
Cdd:cd03249    94 AENIRYGKPDATDEEVEEAAKKANIHDFImslpdGYDTLVGERGSQLSGGQKQRIAIARALLRNPKILLLDEATSALDA- 172

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1131020733 178 lreqmRIEiKKIQRKL-----GITAIYVTHdRVEAMSLSDRIIVMKDGKIMQIGTPVEIYE 233
Cdd:cd03249   173 -----ESE-KLVQEALdramkGRTTIVIAH-RLSTIRNADLIAVLQNGQVVEQGTHDELMA 226
ABCC_MsbA cd03251
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ...
 8-234 2.28e-34

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: 126.58  E-value: 2.28e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131020733   8 LRLENVTKIFKDKKNNteviAVNNSTFEIKPGELITLLGPSGCGKTTTLRMVAGFELPTKGKIYIGNEDVTF--LPPNKR 85
Cdd:cd03251     1 VEFKNVTFRYPGDGPP----VLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDGHDVRDytLASLRR 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131020733  86 DTATVFQSYGLFpHMTVFDNVAYGLklRKLSREEIEkrvfEALEMVGLKDLASRAP-----------SRLSGGQQQRVTL 154
Cdd:cd03251    77 QIGLVSQDVFLF-NDTVAENIAYGR--PGATREEVE----EAARAANAHEFIMELPegydtvigergVKLSGGQRQRIAI 149

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131020733 155 ARSIIVEPAILLLDEPLSNLDALLREQMRIEIKKIQRklGITAIYVTHdRVEAMSLSDRIIVMKDGKIMQIGTPVEIYED 234
Cdd:cd03251   150 ARALLKDPPILILDEATSALDTESERLVQAALERLMK--NRTTFVIAH-RLSTIENADRIVVLEDGKIVERGTHEELLAQ 226
MsbA_lipidA TIGR02203
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ...
 8-231 2.93e-34

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: 132.53  E-value: 2.93e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131020733   8 LRLENVTKIFKDkknnTEVIAVNNSTFEIKPGELITLLGPSGCGKTTTLRMVAGFELPTKGKIYIGNEDVT--FLPPNKR 85
Cdd:TIGR02203 331 VEFRNVTFRYPG----RDRPALDSISLVIEPGETVALVGRSGSGKSTLVNLIPRFYEPDSGQILLDGHDLAdyTLASLRR 406

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131020733  86 DTATVFQSYGLFPHmTVFDNVAYGlKLRKLSREEIEkrvfEALEMVGLKDLASRAP-----------SRLSGGQQQRVTL 154
Cdd:TIGR02203 407 QVALVSQDVVLFND-TIANNIAYG-RTEQADRAEIE----RALAAAYAQDFVDKLPlgldtpigengVLLSGGQRQRLAI 480

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1131020733 155 ARSIIVEPAILLLDEPLSNLDALLREQMRIEIKKIQRklGITAIYVTHdRVEAMSLSDRIIVMKDGKIMQIGTPVEI 231
Cdd:TIGR02203 481 ARALLKDAPILILDEATSALDNESERLVQAALERLMQ--GRTTLVIAH-RLSTIEKADRIVVMDDGRIVERGTHNEL 554
CydD TIGR02857
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ...
 7-217 3.52e-34

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: 132.03  E-value: 3.52e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131020733   7 SLRLENVTKIFKDKKNnteviAVNNSTFEIKPGELITLLGPSGCGKTTTLRMVAGFELPTKGKIYIGNEDVTFLPPN--K 84
Cdd:TIGR02857 321 SLEFSGVSVAYPGRRP-----ALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSIAVNGVPLADADADswR 395

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131020733  85 RDTATVFQSYGLFPHmTVFDNVAygLKLRKLSREEIEkrvfEALEMVGLKDLASRAP-----------SRLSGGQQQRVT 153
Cdd:TIGR02857 396 DQIAWVPQHPFLFAG-TIAENIR--LARPDASDAEIR----EALERAGLDEFVAALPqgldtpigeggAGLSGGQAQRLA 468

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1131020733 154 LARSIIVEPAILLLDEPLSNLDALLREQMRIEIKKIQRklGITAIYVTHDRvEAMSLSDRIIVM 217
Cdd:TIGR02857 469 LARAFLRDAPLLLLDEPTAHLDAETEAEVLEALRALAQ--GRTVLLVTHRL-ALAALADRIVVL 529
ArpD COG4618
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ...
 7-231 3.77e-34

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: 132.18  E-value: 3.77e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131020733   7 SLRLENVTKIFkdkkNNTEVIAVNNSTFEIKPGELITLLGPSGCGKTTTLRMVAGFELPTKGKIYIGNEDVT-------- 78
Cdd:COG4618   330 RLSVENLTVVP----PGSKRPILRGVSFSLEPGEVLGVIGPSGSGKSTLARLLVGVWPPTAGSVRLDGADLSqwdreelg 405

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131020733  79 ----FLPpnkrdtatvfQSYGLFPHmTVFDNVAyglKLRKLSREeiekRVFEALEMVGLKDLASRAP-----------SR 143
Cdd:COG4618   406 rhigYLP----------QDVELFDG-TIAENIA---RFGDADPE----KVVAAAKLAGVHEMILRLPdgydtrigeggAR 467

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131020733 144 LSGGQQQRVTLARSIIVEPAILLLDEPLSNLD-----ALLR--EQMRieikkiQRklGITAIYVTHdRVEAMSLSDRIIV 216
Cdd:COG4618   468 LSGGQRQRIGLARALYGDPRLVVLDEPNSNLDdegeaALAAaiRALK------AR--GATVVVITH-RPSLLAAVDKLLV 538

                         250
                  ....*....|....*
gi 1131020733 217 MKDGKIMQIGTPVEI 231
Cdd:COG4618   539 LRDGRVQAFGPRDEV 553
cbiO PRK13641
energy-coupling factor transporter ATPase;
6-235 7.26e-34

energy-coupling factor transporter ATPase;


Pssm-ID: 237456 [Multi-domain]  Cd Length: 287  Bit Score: 126.48  E-value: 7.26e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131020733   6 VSLRLENVTKIFKdKKNNTEVIAVNNSTFEIKPGELITLLGPSGCGKTTTLRMVAGFELPTKGKIYIGNEDVTFLPPNK- 84
Cdd:PRK13641    1 MSIKFENVDYIYS-PGTPMEKKGLDNISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITIAGYHITPETGNKn 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131020733  85 -----RDTATVFQsyglFPHMTVFDN-----VAYGLKLRKLSREEIEKRVFEALEMVGLK-DLASRAPSRLSGGQQQRVT 153
Cdd:PRK13641   80 lkklrKKVSLVFQ----FPEAQLFENtvlkdVEFGPKNFGFSEDEAKEKALKWLKKVGLSeDLISKSPFELSGGQMRRVA 155

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131020733 154 LARSIIVEPAILLLDEPLSNLDALLREQMrIEIKKIQRKLGITAIYVTHDRVEAMSLSDRIIVMKDGKIMQIGTPVEIYE 233
Cdd:PRK13641  156 IAGVMAYEPEILCLDEPAAGLDPEGRKEM-MQLFKDYQKAGHTVILVTHNMDDVAEYADDVLVLEHGKLIKHASPKEIFS 234


                  ..
gi 1131020733 234 DP 235
Cdd:PRK13641  235 DK 236
ABCC_ATM1_transporter cd03253
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ...
 8-230 8.58e-34

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: 125.04  E-value: 8.58e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131020733   8 LRLENVTKIFkdkknNTEVIAVNNSTFEIKPGELITLLGPSGCGKTTTLRMVAGFELPTKGKIYIGNEDVT--FLPPNKR 85
Cdd:cd03253     1 IEFENVTFAY-----DPGRPVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDGQDIRevTLDSLRR 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131020733  86 DTATVFQSYGLFpHMTVFDNVAYGlklrKLSREEIEkrVFEALEMVGLKDLASRAPS-----------RLSGGQQQRVTL 154
Cdd:cd03253    76 AIGVVPQDTVLF-NDTIGYNIRYG----RPDATDEE--VIEAAKAAQIHDKIMRFPDgydtivgerglKLSGGEKQRVAI 148

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131020733 155 ARSIIVEPAILLLDEPLSNLDAlLREQmrieikKIQRKL-----GITAIYVTHdRVEAMSLSDRIIVMKDGKIMQIGTPV 229
Cdd:cd03253   149 ARAILKNPPILLLDEATSALDT-HTER------EIQAALrdvskGRTTIVIAH-RLSTIVNADKIIVLKDGRIVERGTHE 220


                  .
gi 1131020733 230 E 230
Cdd:cd03253   221 E 221
PRK10895 PRK10895
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
 7-240 1.95e-33

lipopolysaccharide ABC transporter ATP-binding protein; Provisional


Pssm-ID: 182817 [Multi-domain]  Cd Length: 241  Bit Score: 124.24  E-value: 1.95e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131020733   7 SLRLENVTKIFKDKKnnteviAVNNSTFEIKPGELITLLGPSGCGKTTTLRMVAGFELPTKGKIYIGNEDVTFLPPN--- 83
Cdd:PRK10895    3 TLTAKNLAKAYKGRR------VVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEDISLLPLHara 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131020733  84 KRDTATVFQSYGLFPHMTVFDNVAYGLKLRK-LSREEIEKRVFEALEMVGLKDLASRAPSRLSGGQQQRVTLARSIIVEP 162
Cdd:PRK10895   77 RRGIGYLPQEASIFRRLSVYDNLMAVLQIRDdLSAEQREDRANELMEEFHIEHLRDSMGQSLSGGERRRVEIARALAANP 156

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131020733 163 AILLLDEPLSNLDALlreqMRIEIKKI---QRKLGITAIYVTHDRVEAMSLSDRIIVMKDGKIMQIGTPVEIYEDPISKF 239
Cdd:PRK10895  157 KFILLDEPFAGVDPI----SVIDIKRIiehLRDSGLGVLITDHNVRETLAVCERAYIVSQGHLIAHGTPTEILQDEHVKR 232


                  .
gi 1131020733 240 V 240
Cdd:PRK10895  233 V 233
CeuD COG4604
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ...
 9-231 1.98e-33

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


Pssm-ID: 443654 [Multi-domain]  Cd Length: 252  Bit Score: 124.43  E-value: 1.98e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131020733   9 RLENVTKIFKDKKnnteviAVNNSTFEIKPGELITLLGPSGCGKTTTLRMVAGFELPTKGKIYIGNEDVTFLPPNK--RD 86
Cdd:COG4604     3 EIKNVSKRYGGKV------VLDDVSLTIPKGGITALIGPNGAGKSTLLSMISRLLPPDSGEVLVDGLDVATTPSRElaKR 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131020733  87 TATVFQSYGLFPHMTVFDNVAYGlklR------KLSREEIEKrVFEALEMVGLKDLASRAPSRLSGGQQQRVTLARSIIV 160
Cdd:COG4604    77 LAILRQENHINSRLTVRELVAFG---RfpyskgRLTAEDREI-IDEAIAYLDLEDLADRYLDELSGGQRQRAFIAMVLAQ 152

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1131020733 161 EPAILLLDEPLSNLD-ALLREQMRIeIKKIQRKLGITAIYVTHDRVEAMSLSDRIIVMKDGKIMQIGTPVEI 231
Cdd:COG4604   153 DTDYVLLDEPLNNLDmKHSVQMMKL-LRRLADELGKTVVIVLHDINFASCYADHIVAMKDGRVVAQGTPEEI 223
PRK10261 PRK10261
glutathione transporter ATP-binding protein; Provisional
 25-235 2.09e-33

glutathione transporter ATP-binding protein; Provisional


Pssm-ID: 182342 [Multi-domain]  Cd Length: 623  Bit Score: 130.75  E-value: 2.09e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131020733  25 EVIAVNNSTFEIKPGELITLLGPSGCGKTTTLRMVAGFELPTKGKIYIGNEDVTFLPPNK-----RDTATVFQS--YGLF 97
Cdd:PRK10261  336 EVHAVEKVSFDLWPGETLSLVGESGSGKSTTGRALLRLVESQGGEIIFNGQRIDTLSPGKlqalrRDIQFIFQDpyASLD 415

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131020733  98 PHMTVFDNVAYGLKLRKLSR-EEIEKRVFEALEMVGLK-DLASRAPSRLSGGQQQRVTLARSIIVEPAILLLDEPLSNLD 175
Cdd:PRK10261  416 PRQTVGDSIMEPLRVHGLLPgKAAAARVAWLLERVGLLpEHAWRYPHEFSGGQRQRICIARALALNPKVIIADEAVSALD 495

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131020733 176 ALLREQMRIEIKKIQRKLGITAIYVTHDRVEAMSLSDRIIVMKDGKIMQIGTPVEIYEDP 235
Cdd:PRK10261  496 VSIRGQIINLLLDLQRDFGIAYLFISHDMAVVERISHRVAVMYLGQIVEIGPRRAVFENP 555
PRK14267 PRK14267
phosphate ABC transporter ATP-binding protein; Provisional
 44-245 2.32e-33

phosphate ABC transporter ATP-binding protein; Provisional


Pssm-ID: 184596 [Multi-domain]  Cd Length: 253  Bit Score: 124.18  E-value: 2.32e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131020733  44 LLGPSGCGKTTTLRMVAGF-----ELPTKGKIYIGNEDVTFLPPN----KRDTATVFQSYGLFPHMTVFDNVAYGLKLRK 114
Cdd:PRK14267   35 LMGPSGCGKSTLLRTFNRLlelneEARVEGEVRLFGRNIYSPDVDpievRREVGMVFQYPNPFPHLTIYDNVAIGVKLNG 114

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131020733 115 L--SREEIEKRVFEALEMVGL----KDLASRAPSRLSGGQQQRVTLARSIIVEPAILLLDEPLSNLDALlrEQMRIEIKK 188
Cdd:PRK14267  115 LvkSKKELDERVEWALKKAALwdevKDRLNDYPSNLSGGQRQRLVIARALAMKPKILLMDEPTANIDPV--GTAKIEELL 192

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1131020733 189 IQRKLGITAIYVTHDRVEAMSLSDRIIVMKDGKIMQIGTPVEIYEDP----ISKFVAGFIG 245
Cdd:PRK14267  193 FELKKEYTIVLVTHSPAQAARVSDYVAFLYLGKLIEVGPTRKVFENPehelTEKYVTGALG 253
PRK15134 PRK15134
microcin C ABC transporter ATP-binding protein YejF; Provisional
 27-235 7.00e-33

microcin C ABC transporter ATP-binding protein YejF; Provisional


Pssm-ID: 237917 [Multi-domain]  Cd Length: 529  Bit Score: 128.28  E-value: 7.00e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131020733  27 IAVNNSTFEIKPGELITLLGPSGCGKTTT----LRMvagfeLPTKGKIYIGNEDVTFLP-----PNKRDTATVFQ--SYG 95
Cdd:PRK15134  300 VVVKNISFTLRPGETLGLVGESGSGKSTTglalLRL-----INSQGEIWFDGQPLHNLNrrqllPVRHRIQVVFQdpNSS 374

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131020733  96 LFPHMTVFDNVAYGLKL--RKLSREEIEKRVFEALEMVGLkDLASRA--PSRLSGGQQQRVTLARSIIVEPAILLLDEPL 171
Cdd:PRK15134  375 LNPRLNVLQIIEEGLRVhqPTLSAAQREQQVIAVMEEVGL-DPETRHryPAEFSGGQRQRIAIARALILKPSLIILDEPT 453

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1131020733 172 SNLDALLREQMRIEIKKIQRKLGITAIYVTHDRVEAMSLSDRIIVMKDGKIMQIGTPVEIYEDP 235
Cdd:PRK15134  454 SSLDKTVQAQILALLKSLQQKHQLAYLFISHDLHVVRALCHQVIVLRQGEVVEQGDCERVFAAP 517
NupO COG3845
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ...
 8-227 1.07e-32

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


Pssm-ID: 443055 [Multi-domain]  Cd Length: 504  Bit Score: 127.45  E-value: 1.07e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131020733   8 LRLENVTKIFKDkknnteVIAVNNSTFEIKPGELITLLGPSGCGKTTTLRMVAGFELPTKGKIYIGNEDVTFLPPNK-RD 86
Cdd:COG3845     6 LELRGITKRFGG------VVANDDVSLTVRPGEIHALLGENGAGKSTLMKILYGLYQPDSGEILIDGKPVRIRSPRDaIA 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131020733  87 T--ATVFQSYGLFPHMTVFDNVAYGL---KLRKLSREEIEKRVFEALEMVGLK-DLASRApSRLSGGQQQRVTLARSIIV 160
Cdd:COG3845    80 LgiGMVHQHFMLVPNLTVAENIVLGLeptKGGRLDRKAARARIRELSERYGLDvDPDAKV-EDLSVGEQQRVEILKALYR 158

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1131020733 161 EPAILLLDEPLSNL-----DALLReqmriEIKKIqRKLGITAIYVTHDRVEAMSLSDRIIVMKDGKImqIGT 227
Cdd:COG3845   159 GARILILDEPTAVLtpqeaDELFE-----ILRRL-AAEGKSIIFITHKLREVMAIADRVTVLRRGKV--VGT 222
PRK15112 PRK15112
peptide ABC transporter ATP-binding protein SapF;
8-236 1.59e-32

peptide ABC transporter ATP-binding protein SapF;


Pssm-ID: 185067 [Multi-domain]  Cd Length: 267  Bit Score: 122.59  E-value: 1.59e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131020733   8 LRLENVTKIFKDKK---NNTEVIAVNNSTFEIKPGELITLLGPSGCGKTTTLRMVAGFELPTKGKIYIGNEDVTFLPPNK 84
Cdd:PRK15112    5 LEVRNLSKTFRYRTgwfRRQTVEAVKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDHPLHFGDYSY 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131020733  85 RDTA--TVFQ--SYGLFPHMTVFDNVAYGLKLR-KLSREEIEKRVFEALEMVGLK-DLASRAPSRLSGGQQQRVTLARSI 158
Cdd:PRK15112   85 RSQRirMIFQdpSTSLNPRQRISQILDFPLRLNtDLEPEQREKQIIETLRQVGLLpDHASYYPHMLAPGQKQRLGLARAL 164

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1131020733 159 IVEPAILLLDEPLSNLDALLREQMRIEIKKIQRKLGITAIYVTHDRVEAMSLSDRIIVMKDGKIMQIGTPVEIYEDPI 236
Cdd:PRK15112  165 ILRPKVIIADEALASLDMSMRSQLINLMLELQEKQGISYIYVTQHLGMMKHISDQVLVMHQGEVVERGSTADVLASPL 242
cbiO PRK13644
energy-coupling factor transporter ATPase;
8-235 3.74e-32

energy-coupling factor transporter ATPase;


Pssm-ID: 106587 [Multi-domain]  Cd Length: 274  Bit Score: 121.63  E-value: 3.74e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131020733   8 LRLENVTKIFKDKKNnteviAVNNSTFEIKPGELITLLGPSGCGKTTTLRMVAGFELPTKGKIYIGNEDV---TFLPPNK 84
Cdd:PRK13644    2 IRLENVSYSYPDGTP-----ALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLVSGIDTgdfSKLQGIR 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131020733  85 RDTATVFQS-YGLFPHMTVFDNVAYGLKLRKLSREEIEKRVFEALEMVGLKDLASRAPSRLSGGQQQRVTLARSIIVEPA 163
Cdd:PRK13644   77 KLVGIVFQNpETQFVGRTVEEDLAFGPENLCLPPIEIRKRVDRALAEIGLEKYRHRSPKTLSGGQGQCVALAGILTMEPE 156

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1131020733 164 ILLLDEPLSNLDALLREQMRIEIKKIQRKlGITAIYVTHDrVEAMSLSDRIIVMKDGKIMQIGTPVEIYEDP 235
Cdd:PRK13644  157 CLIFDEVTSMLDPDSGIAVLERIKKLHEK-GKTIVYITHN-LEELHDADRIIVMDRGKIVLEGEPENVLSDV 226
AztA NF040873
zinc ABC transporter ATP-binding protein AztA;
28-217 4.66e-32

zinc ABC transporter ATP-binding protein AztA;


Pssm-ID: 468810 [Multi-domain]  Cd Length: 191  Bit Score: 118.88  E-value: 4.66e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131020733  28 AVNNSTFEIKPGELITLLGPSGCGKTTTLRMVAGFELPTKGKIYI-GNEDVTFLPPNKRDTATvfqsyglFPhMTVFDNV 106
Cdd:NF040873    7 VLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTVRRaGGARVAYVPQRSEVPDS-------LP-LTVRDLV 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131020733 107 AYGL-----KLRKLSREEiEKRVFEALEMVGLKDLASRAPSRLSGGQQQRVTLARSIIVEPAILLLDEPLSNLDALLREQ 181
Cdd:NF040873   79 AMGRwarrgLWRRLTRDD-RAAVDDALERVGLADLAGRQLGELSGGQRQRALLAQGLAQEADLLLLDEPTTGLDAESRER 157

                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 1131020733 182 MRIEIKKIQRKlGITAIYVTHDRVEAMSlSDRIIVM 217
Cdd:NF040873  158 IIALLAEEHAR-GATVVVVTHDLELVRR-ADPCVLL 191
ABCC_Glucan_exporter_like cd03254
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ...
 23-230 5.72e-32

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: 120.02  E-value: 5.72e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131020733  23 NTEVIAVNNSTFEIKPGELITLLGPSGCGKTTTLRMVAGFELPTKGKIYIGNEDVTFLPPN--KRDTATVFQSYGLFPHm 100
Cdd:cd03254    13 DEKKPVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGIDIRDISRKslRSMIGVVLQDTFLFSG- 91

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131020733 101 TVFDNVAYGlklRKLSREEiekRVFEALEMVGLKDLASRAP-----------SRLSGGQQQRVTLARSIIVEPAILLLDE 169
Cdd:cd03254    92 TIMENIRLG---RPNATDE---EVIEAAKEAGAHDFIMKLPngydtvlgengGNLSQGERQLLAIARAMLRDPKILILDE 165

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1131020733 170 PLSNLDALLREQMRIEIKKIQRklGITAIYVTHdRVEAMSLSDRIIVMKDGKIMQIGTPVE 230
Cdd:cd03254   166 ATSNIDTETEKLIQEALEKLMK--GRTSIIIAH-RLSTIKNADKILVLDDGKIIEEGTHDE 223
cbiO PRK13647
cobalt transporter ATP-binding subunit; Provisional
 10-228 6.81e-32

cobalt transporter ATP-binding subunit; Provisional


Pssm-ID: 237457 [Multi-domain]  Cd Length: 274  Bit Score: 121.00  E-value: 6.81e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131020733  10 LENVTKIFKDkknNTEviAVNNSTFEIKPGELITLLGPSGCGKTTTLRMVAGFELPTKGKIYIGNEDVTflPPNKRD--- 86
Cdd:PRK13647    7 VEDLHFRYKD---GTK--ALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGREVN--AENEKWvrs 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131020733  87 -TATVFQSYG--LFPhMTVFDNVAYGLKLRKLSREEIEKRVFEALEMVGLKDLASRAPSRLSGGQQQRVTLARSIIVEPA 163
Cdd:PRK13647   80 kVGLVFQDPDdqVFS-STVWDDVAFGPVNMGLDKDEVERRVEEALKAVRMWDFRDKPPYHLSYGQKKRVAIAGVLAMDPD 158

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1131020733 164 ILLLDEPLSNLDALLREQMRiEIKKIQRKLGITAIYVTHDRVEAMSLSDRIIVMKDGKIMQIGTP 228
Cdd:PRK13647  159 VIVLDEPMAYLDPRGQETLM-EILDRLHNQGKTVIVATHDVDLAAEWADQVIVLKEGRVLAEGDK 222
PRK13537 PRK13537
nodulation factor ABC transporter ATP-binding protein NodI;
8-236 4.49e-31

nodulation factor ABC transporter ATP-binding protein NodI;


Pssm-ID: 237420 [Multi-domain]  Cd Length: 306  Bit Score: 119.52  E-value: 4.49e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131020733   8 LRLENVTKIFKDKknntevIAVNNSTFEIKPGELITLLGPSGCGKTTTLRMVAGFELPTKGKIYIGNEDVTFLPPNKRD- 86
Cdd:PRK13537    8 IDFRNVEKRYGDK------LVVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCGEPVPSRARHARQr 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131020733  87 TATVFQSYGLFPHMTVFDNVAYGLKLRKLSREEIEKRVFEALEMVGLKDLASRAPSRLSGGQQQRVTLARSIIVEPAILL 166
Cdd:PRK13537   82 VGVVPQFDNLDPDFTVRENLLVFGRYFGLSAAAARALVPPLLEFAKLENKADAKVGELSGGMKRRLTLARALVNDPDVLV 161

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131020733 167 LDEPLSNLDALLREQMRIEIKKIQRKlGITAIYVTHDRVEAMSLSDRIIVMKDGKIMQIGTPVEIYEDPI 236
Cdd:PRK13537  162 LDEPTTGLDPQARHLMWERLRSLLAR-GKTILLTTHFMEEAERLCDRLCVIEEGRKIAEGAPHALIESEI 230
PRK13651 PRK13651
cobalt transporter ATP-binding subunit; Provisional
 8-234 5.63e-31

cobalt transporter ATP-binding subunit; Provisional


Pssm-ID: 184210 [Multi-domain]  Cd Length: 305  Bit Score: 119.42  E-value: 5.63e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131020733   8 LRLENVTKIFkDKKNNTEVIAVNNSTFEIKPGELITLLGPSGCGKTTTLRMVAGFELPTKGKIYIGNED----------- 76
Cdd:PRK13651    3 IKVKNIVKIF-NKKLPTELKALDNVSVEINQGEFIAIIGQTGSGKTTFIEHLNALLLPDTGTIEWIFKDeknkkktkeke 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131020733  77 ---------------VTFLPPNKRDTATVFQ--SYGLFpHMTVFDNVAYGLKLRKLSREEIEKRVFEALEMVGL-KDLAS 138
Cdd:PRK13651   82 kvleklviqktrfkkIKKIKEIRRRVGVVFQfaEYQLF-EQTIEKDIIFGPVSMGVSKEEAKKRAAKYIELVGLdESYLQ 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131020733 139 RAPSRLSGGQQQRVTLARSIIVEPAILLLDEPLSNLDAllreQMRIEIKKIQRKL---GITAIYVTHDRVEAMSLSDRII 215
Cdd:PRK13651  161 RSPFELSGGQKRRVALAGILAMEPDFLVFDEPTAGLDP----QGVKEILEIFDNLnkqGKTIILVTHDLDNVLEWTKRTI 236

                         250
                  ....*....|....*....
gi 1131020733 216 VMKDGKIMQIGTPVEIYED 234
Cdd:PRK13651  237 FFKDGKIIKDGDTYDILSD 255
urea_trans_UrtE TIGR03410
urea ABC transporter, ATP-binding protein UrtE; Members of this protein family are ABC ...
 33-241 5.95e-31

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: 117.24  E-value: 5.95e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131020733  33 TFEIKPGELITLLGPSGCGKTTTLRMVAGFELPTKGKIYIGNEDVTFLPPNKR---DTATVFQSYGLFPHMTVFDNVAYG 109
Cdd:TIGR03410  20 SLEVPKGEVTCVLGRNGVGKTTLLKTLMGLLPVKSGSIRLDGEDITKLPPHERaraGIAYVPQGREIFPRLTVEENLLTG 99

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131020733 110 LKLRKLSREEIEKRVFEaLEMVgLKDLASRAPSRLSGGQQQRVTLARSIIVEPAILLLDEPLSNLDALLREQMRIEIKKI 189
Cdd:TIGR03410 100 LAALPRRSRKIPDEIYE-LFPV-LKEMLGRRGGDLSGGQQQQLAIARALVTRPKLLLLDEPTEGIQPSIIKDIGRVIRRL 177

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1131020733 190 QRKLGITAIYVTHDRVEAMSLSDRIIVMKDGKIMQIGTPVEIYEDPISKFVA 241
Cdd:TIGR03410 178 RAEGGMAILLVEQYLDFARELADRYYVMERGRVVASGAGDELDEDKVRRYLA 229
cbiO PRK13649
energy-coupling factor transporter ATPase;
28-234 1.12e-30

energy-coupling factor transporter ATPase;


Pssm-ID: 184208 [Multi-domain]  Cd Length: 280  Bit Score: 117.92  E-value: 1.12e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131020733  28 AVNNSTFEIKPGELITLLGPSGCGKTTTLRMVAGFELPTKGKIYIGNEDVTFLPPNKrDTATVFQSYGL---FPHM---- 100
Cdd:PRK13649   22 ALFDVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDDTLITSTSKNK-DIKQIRKKVGLvfqFPESqlfe 100

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131020733 101 -TVFDNVAYGLKLRKLSREEIEKRVFEALEMVGL-KDLASRAPSRLSGGQQQRVTLARSIIVEPAILLLDEPLSNLDALL 178
Cdd:PRK13649  101 eTVLKDVAFGPQNFGVSQEEAEALAREKLALVGIsESLFEKNPFELSGGQMRRVAIAGILAMEPKILVLDEPTAGLDPKG 180

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1131020733 179 REQMRIEIKKIQRKlGITAIYVTHDRVEAMSLSDRIIVMKDGKIMQIGTPVEIYED 234
Cdd:PRK13649  181 RKELMTLFKKLHQS-GMTIVLVTHLMDDVANYADFVYVLEKGKLVLSGKPKDIFQD 235
PhnL COG4778
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ...
 8-220 1.28e-30

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: 116.38  E-value: 1.28e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131020733   8 LRLENVTKIFK-DKKNNTEVIAVNNSTFEIKPGELITLLGPSGCGKTTTLRMVAGFELPTKGKIYI----GNEDVTFLPP 82
Cdd:COG4778     5 LEVENLSKTFTlHLQGGKRLPVLDGVSFSVAAGECVALTGPSGAGKSTLLKCIYGNYLPDSGSILVrhdgGWVDLAQASP 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131020733  83 N-----KRDT-ATVFQsyglF----PHMTVFDNVAYGLKLRKLSREEIEKRVFEALEMVGLKD-LASRAPSRLSGGQQQR 151
Cdd:COG4778    85 ReilalRRRTiGYVSQ----FlrviPRVSALDVVAEPLLERGVDREEARARARELLARLNLPErLWDLPPATFSGGEQQR 160

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1131020733 152 VTLARSIIVEPAILLLDEPLSNLDALLREQMR--IEIKKIQrklGITAIYVTHDRvEAMS-LSDRIIVMKDG 220
Cdd:COG4778   161 VNIARGFIADPPLLLLDEPTASLDAANRAVVVelIEEAKAR---GTAIIGIFHDE-EVREaVADRVVDVTPF 228
MsbA_rel TIGR02204
ABC transporter, permease/ATP-binding protein; This protein is related to a Proteobacterial ...
 24-227 1.59e-30

ABC transporter, permease/ATP-binding protein; This protein is related to a Proteobacterial ATP transporter that exports lipid A and to eukaryotic P-glycoproteins.


Pssm-ID: 131259 [Multi-domain]  Cd Length: 576  Bit Score: 122.12  E-value: 1.59e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131020733  24 TEVIAVNNSTFEIKPGELITLLGPSGCGKTTTLRMVAGFELPTKGKIYIGNEDVTFLPPN--KRDTATVFQSYGLFPHmT 101
Cdd:TIGR02204 351 PDQPALDGLNLTVRPGETVALVGPSGAGKSTLFQLLLRFYDPQSGRILLDGVDLRQLDPAelRARMALVPQDPVLFAA-S 429

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131020733 102 VFDNVAYGLKlrKLSREEIEK--RVFEALEMV-GLKD-----LASRApSRLSGGQQQRVTLARSIIVEPAILLLDEPLSN 173
Cdd:TIGR02204 430 VMENIRYGRP--DATDEEVEAaaRAAHAHEFIsALPEgydtyLGERG-VTLSGGQRQRIAIARAILKDAPILLLDEATSA 506

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1131020733 174 LDAlLREQmrieikKIQRKL-----GITAIYVTHdRVEAMSLSDRIIVMKDGKIMQIGT 227
Cdd:TIGR02204 507 LDA-ESEQ------LVQQALetlmkGRTTLIIAH-RLATVLKADRIVVMDQGRIVAQGT 557
ABC_cobalt_CbiO_domain2 cd03226
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ...
 9-222 2.31e-30

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: 115.05  E-value: 2.31e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131020733   9 RLENVTKIFKDKKNnteviAVNNSTFEIKPGELITLLGPSGCGKTTTLRMVAGFELPTKGKIYIGNEDVtflpPNKRDTA 88
Cdd:cd03226     1 RIENISFSYKKGTE-----ILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLNGKPI----KAKERRK 71

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131020733  89 TVFQS-----YGLFPHmTVFDNVAYGLKLRKLSREEIEkrvfEALEMVGLKDLASRAPSRLSGGQQQRVTLARSIIVEPA 163
Cdd:cd03226    72 SIGYVmqdvdYQLFTD-SVREELLLGLKELDAGNEQAE----TVLKDLDLYALKERHPLSLSGGQKQRLAIAAALLSGKD 146

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1131020733 164 ILLLDEPLSNLDallREQMRiEIKKIQRKL---GITAIYVTHDRVEAMSLSDRIIVMKDGKI 222
Cdd:cd03226   147 LLIFDEPTSGLD---YKNME-RVGELIRELaaqGKAVIVITHDYEFLAKVCDRVLLLANGAI 204
ABC_KpsT_Wzt cd03220
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ...
 8-226 3.90e-30

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


Pssm-ID: 213187 [Multi-domain]  Cd Length: 224  Bit Score: 114.94  E-value: 3.90e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131020733   8 LRLENVTK----------------IFKDKKNNTEVIAVNNSTFEIKPGELITLLGPSGCGKTTTLRMVAGFELPTKGKIY 71
Cdd:cd03220     1 IELENVSKsyptykggssslkklgILGRKGEVGEFWALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVT 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131020733  72 IgnedvtflppNKRDTATVFQSYGLFPHMTVFDNVAYGLKLRKLSREEIEKRVFEALEMVGLKDLASRAPSRLSGGQQQR 151
Cdd:cd03220    81 V----------RGRVSSLLGLGGGFNPELTGRENIYLNGRLLGLSRKEIDEKIDEIIEFSELGDFIDLPVKTYSSGMKAR 150

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1131020733 152 VTLARSIIVEPAILLLDEPLSNLDALLREQMRIEIKKIQRKlGITAIYVTHDRVEAMSLSDRIIVMKDGKIMQIG 226
Cdd:cd03220   151 LAFAIATALEPDILLIDEVLAVGDAAFQEKCQRRLRELLKQ-GKTVILVSHDPSSIKRLCDRALVLEKGKIRFDG 224
PRK10247 PRK10247
putative ABC transporter ATP-binding protein YbbL; Provisional
 1-217 3.91e-30

putative ABC transporter ATP-binding protein YbbL; Provisional


Pssm-ID: 182331 [Multi-domain]  Cd Length: 225  Bit Score: 114.81  E-value: 3.91e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131020733   1 MKKKQVSLRLENVtkifkDKKNNTEVIaVNNSTFEIKPGELITLLGPSGCGKTTTLRMVAGFELPTKGKIYIGNEDVTFL 80
Cdd:PRK10247    1 MQENSPLLQLQNV-----GYLAGDAKI-LNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFEGEDISTL 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131020733  81 PPN--KRDTATVFQSYGLFPHmTVFDNVAYGLKLRKLSREeiEKRVFEALEMVGLKD-LASRAPSRLSGGQQQRVTLARS 157
Cdd:PRK10247   75 KPEiyRQQVSYCAQTPTLFGD-TVYDNLIFPWQIRNQQPD--PAIFLDDLERFALPDtILTKNIAELSGGEKQRISLIRN 151

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131020733 158 IIVEPAILLLDEPLSNLDALLREQMRIEIKKIQRKLGITAIYVTHDRVEaMSLSDRIIVM 217
Cdd:PRK10247  152 LQFMPKVLLLDEITSALDESNKHNVNEIIHRYVREQNIAVLWVTHDKDE-INHADKVITL 210
PRK13536 PRK13536
nodulation factor ABC transporter ATP-binding protein NodI;
1-232 4.74e-30

nodulation factor ABC transporter ATP-binding protein NodI;


Pssm-ID: 237419 [Multi-domain]  Cd Length: 340  Bit Score: 117.62  E-value: 4.74e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131020733   1 MKKKQVSLRLENVTKIFKDKknntevIAVNNSTFEIKPGELITLLGPSGCGKTTTLRMVAGFELPTKGKIYIGNEDVtfl 80
Cdd:PRK13536   35 GSMSTVAIDLAGVSKSYGDK------AVVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKITVLGVPV--- 105

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131020733  81 pPNKRDTA-----TVFQSYGLFPHMTVFDN-VAYGLKLRkLSREEIEKRVFEALEMVGLKDLASRAPSRLSGGQQQRVTL 154
Cdd:PRK13536  106 -PARARLArarigVVPQFDNLDLEFTVRENlLVFGRYFG-MSTREIEAVIPSLLEFARLESKADARVSDLSGGMKRRLTL 183

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131020733 155 ARSIIVEPAILLLDEPLSNLDA----LLREQMRIEIKKiqrklGITAIYVTHDRVEAMSLSDRIIVMKDG-KIM------ 223
Cdd:PRK13536  184 ARALINDPQLLILDEPTTGLDPharhLIWERLRSLLAR-----GKTILLTTHFMEEAERLCDRLCVLEAGrKIAegrpha 258

                         250
                  ....*....|....
gi 1131020733 224 ----QIGTPV-EIY 232
Cdd:PRK13536  259 lideHIGCQViEIY 272
ABCC_Hemolysin cd03252
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ...
 10-231 4.85e-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: 4.85e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131020733  10 LENVTkiFKDKKNNTEVIavNNSTFEIKPGELITLLGPSGCGKTTTLRMVAGFELPTKGKIYIGNEDVTFLPPN--KRDT 87
Cdd:cd03252     3 FEHVR--FRYKPDGPVIL--DNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGHDLALADPAwlRRQV 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131020733  88 ATVFQSYGLFpHMTVFDNVAygLKLRKLSREEIEkrvfEALEMVGLKDLASRAP-----------SRLSGGQQQRVTLAR 156
Cdd:cd03252    79 GVVLQENVLF-NRSIRDNIA--LADPGMSMERVI----EAAKLAGAHDFISELPegydtivgeqgAGLSGGQRQRIAIAR 151

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1131020733 157 SIIVEPAILLLDEPLSNLDAllrEQMRIEIKKIQRKL-GITAIYVTHdRVEAMSLSDRIIVMKDGKIMQIGTPVEI 231
Cdd:cd03252   152 ALIHNPRILIFDEATSALDY---ESEHAIMRNMHDICaGRTVIIIAH-RLSTVKNADRIIVMEKGRIVEQGSHDEL 223
cbiO PRK13643
energy-coupling factor transporter ATPase;
34-234 5.89e-30

energy-coupling factor transporter ATPase;


Pssm-ID: 184203 [Multi-domain]  Cd Length: 288  Bit Score: 116.37  E-value: 5.89e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131020733  34 FEIKPGELITLLGPSGCGKTTTLRMVAGFELPTKGKIYIGNEDVTF------LPPNKRDTATVFQsyglFPHM-----TV 102
Cdd:PRK13643   27 LEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVTVGDIVVSStskqkeIKPVRKKVGVVFQ----FPESqlfeeTV 102

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131020733 103 FDNVAYGLKLRKLSREEIEKRVFEALEMVGL-KDLASRAPSRLSGGQQQRVTLARSIIVEPAILLLDEPLSNLDALLREQ 181
Cdd:PRK13643  103 LKDVAFGPQNFGIPKEKAEKIAAEKLEMVGLaDEFWEKSPFELSGGQMRRVAIAGILAMEPEVLVLDEPTAGLDPKARIE 182

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1131020733 182 MRIEIKKIQRKlGITAIYVTHDRVEAMSLSDRIIVMKDGKIMQIGTPVEIYED 234
Cdd:PRK13643  183 MMQLFESIHQS-GQTVVLVTHLMDDVADYADYVYLLEKGHIISCGTPSDVFQE 234
ABCG_White cd03234
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ...
 5-222 7.01e-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: 114.29  E-value: 7.01e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131020733   5 QVSLRLENVTKifKDKKNNTEVIAVNNSTFEIKPGELITLLGPSGCGKTTTLRMVAGFELP---TKGKIYIGNEdvtflp 81
Cdd:cd03234     1 QRVLPWWDVGL--KAKNWNKYARILNDVSLHVESGQVMAILGSSGSGKTTLLDAISGRVEGggtTSGQILFNGQ------ 72

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131020733  82 PNKRDT-----ATVFQSYGLFPHMTVFDNVAYGLKLR---KLSREEIEKRV-FEALEMVGLKDLASRAPSRLSGGQQQRV 152
Cdd:cd03234    73 PRKPDQfqkcvAYVRQDDILLPGLTVRETLTYTAILRlprKSSDAIRKKRVeDVLLRDLALTRIGGNLVKGISGGERRRV 152

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131020733 153 TLARSIIVEPAILLLDEPLSNLDALLREQMRIEIKKIQRKLGITAIYVTHDRVEAMSLSDRIIVMKDGKI 222
Cdd:cd03234   153 SIAVQLLWDPKVLILDEPTSGLDSFTALNLVSTLSQLARRNRIVILTIHQPRSDLFRLFDRILLLSSGEI 222
cbiO PRK13652
cobalt transporter ATP-binding subunit; Provisional
 24-235 1.04e-29

cobalt transporter ATP-binding subunit; Provisional


Pssm-ID: 172200 [Multi-domain]  Cd Length: 277  Bit Score: 115.29  E-value: 1.04e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131020733  24 TEVIAVNNSTFEIKPGELITLLGPSGCGKTTTLRMVAGFELPTKGKIYIGNEDVT--FLPPNKRDTATVFQSYG--LFPh 99
Cdd:PRK13652   15 GSKEALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIRGEPITkeNIREVRKFVGLVFQNPDdqIFS- 93

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131020733 100 MTVFDNVAYGLKLRKLSREEIEKRVFEALEMVGLKDLASRAPSRLSGGQQQRVTLARSIIVEPAILLLDEPLSNLDALLR 179
Cdd:PRK13652   94 PTVEQDIAFGPINLGLDEETVAHRVSSALHMLGLEELRDRVPHHLSGGEKKRVAIAGVIAMEPQVLVLDEPTAGLDPQGV 173

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1131020733 180 EQMRIEIKKIQRKLGITAIYVTHDRVEAMSLSDRIIVMKDGKIMQIGTPVEIYEDP 235
Cdd:PRK13652  174 KELIDFLNDLPETYGMTVIFSTHQLDLVPEMADYIYVMDKGRIVAYGTVEEIFLQP 229
type_I_sec_PrtD TIGR01842
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in ...
 8-231 1.61e-29

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: 118.99  E-value: 1.61e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131020733   8 LRLENVTKIFKDKKNNTeviaVNNSTFEIKPGELITLLGPSGCGKTTTLRMVAGFELPTKGKIYIGNED----------- 76
Cdd:TIGR01842 317 LSVENVTIVPPGGKKPT----LRGISFSLQAGEALAIIGPSGSGKSTLARLIVGIWPPTSGSVRLDGADlkqwdretfgk 392

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131020733  77 -VTFLPpnkrdtatvfQSYGLFPHmTVFDNVAyglklRKLSREEIEKrVFEALEMVGLKDLASRAP-----------SRL 144
Cdd:TIGR01842 393 hIGYLP----------QDVELFPG-TVAENIA-----RFGENADPEK-IIEAAKLAGVHELILRLPdgydtvigpggATL 455

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131020733 145 SGGQQQRVTLARSIIVEPAILLLDEPLSNLDALLREQMRIEIKKIQRKlGITAIYVTHdRVEAMSLSDRIIVMKDGKIMQ 224
Cdd:TIGR01842 456 SGGQRQRIALARALYGDPKLVVLDEPNSNLDEEGEQALANAIKALKAR-GITVVVITH-RPSLLGCVDKILVLQDGRIAR 533


                  ....*..
gi 1131020733 225 IGTPVEI 231
Cdd:TIGR01842 534 FGERDEV 540
nickel_nikD TIGR02770
nickel import ATP-binding protein NikD; This family represents the NikD subunit of a ...
 28-238 3.31e-29

nickel import ATP-binding protein NikD; This family represents the NikD subunit of a multisubunit nickel import ABC transporter complex. Nickel, once imported, may be used in urease and in certain classes of hydrogenase and superoxide dismutase. NikD and NikE are homologous. [Transport and binding proteins, Cations and iron carrying compounds]


Pssm-ID: 131817 [Multi-domain]  Cd Length: 230  Bit Score: 112.46  E-value: 3.31e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131020733  28 AVNNSTFEIKPGELITLLGPSGCGKTTTLRMVAGFELP----TKGKIYIGNEDVTFLPPNKRDTATVFQSyglfPhMTVF 103
Cdd:TIGR02770   1 LVQDLNLSLKRGEVLALVGESGSGKSLTCLAILGLLPPgltqTSGEILLDGRPLLPLSIRGRHIATIMQN----P-RTAF 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131020733 104 D---NVAYGLKLRKLSREEIEK----RVFEALEMVGLKD---LASRAPSRLSGGQQQRVTLARSIIVEPAILLLDEPLSN 173
Cdd:TIGR02770  76 NplfTMGNHAIETLRSLGKLSKqaraLILEALEAVGLPDpeeVLKKYPFQLSGGMLQRVMIALALLLEPPFLIADEPTTD 155

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1131020733 174 LDALLREQMRIEIKKIQRKLGITAIYVTHD-RVEAmSLSDRIIVMKDGKIMQIGTPVEIYEDPISK 238
Cdd:TIGR02770 156 LDVVNQARVLKLLRELRQLFGTGILLITHDlGVVA-RIADEVAVMDDGRIVERGTVKEIFYNPKHE 220
TagH COG1134
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ...
 7-233 3.55e-29

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


Pssm-ID: 440749 [Multi-domain]  Cd Length: 245  Bit Score: 112.87  E-value: 3.55e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131020733   7 SLRLENVTKIFK----------------DKKNNTEVIAVNNSTFEIKPGELITLLGPSGCGKTTTLRMVAGFELPTKGKI 70
Cdd:COG1134     4 MIEVENVSKSYRlyhepsrslkelllrrRRTRREEFWALKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTSGRV 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131020733  71 YIgNEDVTFLppnkRDTATVFQsyglfPHMTVFDNVAYGLKLRKLSREEIEKRVFEALEMVGLKDLASRAPSRLSGGQQQ 150
Cdd:COG1134    84 EV-NGRVSAL----LELGAGFH-----PELTGRENIYLNGRLLGLSRKEIDEKFDEIVEFAELGDFIDQPVKTYSSGMRA 153

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131020733 151 RVTLARSIIVEPAILLLDEPLSNLDALLREQMRIEIKKIQRKlGITAIYVTHDRVEAMSLSDRIIVMKDGKIMQIGTPVE 230
Cdd:COG1134   154 RLAFAVATAVDPDILLVDEVLAVGDAAFQKKCLARIRELRES-GRTVIFVSHSMGAVRRLCDRAIWLEKGRLVMDGDPEE 232


                  ...
gi 1131020733 231 IYE 233
Cdd:COG1134   233 VIA 235
ABCG_EPDR cd03213
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ...
 6-222 4.78e-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: 111.10  E-value: 4.78e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131020733   6 VSLRLENVTKIFKDKKNNTEVIAVNNSTFEIKPGELITLLGPSGCGKTTTLRMVAG--FELPTKGKIYIGNEDVTFLPPN 83
Cdd:cd03213     2 VTLSFRNLTVTVKSSPSKSGKQLLKNVSGKAKPGELTAIMGPSGAGKSTLLNALAGrrTGLGVSGEVLINGRPLDKRSFR 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131020733  84 KRdTATVFQSYGLFPHMTVFDNVAYGLKLRklsreeiekrvfealemvglkdlasrapsRLSGGQQQRVTLARSIIVEPA 163
Cdd:cd03213    82 KI-IGYVPQDDILHPTLTVRETLMFAAKLR-----------------------------GLSGGERKRVSIALELVSNPS 131

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131020733 164 ILLLDEPLSNLDALLREQMRIEIKKIqRKLGITAIYVTHD-RVEAMSLSDRIIVMKDGKI 222
Cdd:cd03213   132 LLFLDEPTSGLDSSSALQVMSLLRRL-ADTGRTIICSIHQpSSEIFELFDKLLLLSQGRV 190
PRK10584 PRK10584
putative ABC transporter ATP-binding protein YbbA; Provisional
 36-222 6.38e-29

putative ABC transporter ATP-binding protein YbbA; Provisional


Pssm-ID: 182569 [Multi-domain]  Cd Length: 228  Bit Score: 111.79  E-value: 6.38e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131020733  36 IKPGELITLLGPSGCGKTTTLRMVAGFELPTKGKIYIGNEDVTFLPPNKR------DTATVFQSYGLFPHMTVFDNVAYG 109
Cdd:PRK10584   33 VKRGETIALIGESGSGKSTLLAILAGLDDGSSGEVSLVGQPLHQMDEEARaklrakHVGFVFQSFMLIPTLNALENVELP 112

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131020733 110 LKLRKLSREEIEKRVFEALEMVGLKDLASRAPSRLSGGQQQRVTLARSIIVEPAILLLDEPLSNLDALLREQMRIEIKKI 189
Cdd:PRK10584  113 ALLRGESSRQSRNGAKALLEQLGLGKRLDHLPAQLSGGEQQRVALARAFNGRPDVLFADEPTGNLDRQTGDKIADLLFSL 192

                         170       180       190
                  ....*....|....*....|....*....|...
gi 1131020733 190 QRKLGITAIYVTHDrVEAMSLSDRIIVMKDGKI 222
Cdd:PRK10584  193 NREHGTTLILVTHD-LQLAARCDRRLRLVNGQL 224
PRK14271 PRK14271
phosphate ABC transporter ATP-binding protein; Provisional
 38-247 6.44e-29

phosphate ABC transporter ATP-binding protein; Provisional


Pssm-ID: 172759 [Multi-domain]  Cd Length: 276  Bit Score: 113.27  E-value: 6.44e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131020733  38 PGELIT-LLGPSGCGKTTTLRMVAGFELPTKGKIYIGN-----------EDVTFLppnKRDTATVFQSYGLFPhMTVFDN 105
Cdd:PRK14271   45 PARAVTsLMGPTGSGKTTFLRTLNRMNDKVSGYRYSGDvllggrsifnyRDVLEF---RRRVGMLFQRPNPFP-MSIMDN 120

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131020733 106 VAYGLKLRKL-SREEIEKRVFEALEMVGL----KDLASRAPSRLSGGQQQRVTLARSIIVEPAILLLDEPLSNLDALLRE 180
Cdd:PRK14271  121 VLAGVRAHKLvPRKEFRGVAQARLTEVGLwdavKDRLSDSPFRLSGGQQQLLCLARTLAVNPEVLLLDEPTSALDPTTTE 200

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1131020733 181 QMRIEIKKIQRKLgiTAIYVTHDRVEAMSLSDRIIVMKDGKIMQIGTPVEIYEDP----ISKFVAGFIGKV 247
Cdd:PRK14271  201 KIEEFIRSLADRL--TVIIVTHNLAQAARISDRAALFFDGRLVEEGPTEQLFSSPkhaeTARYVAGLSGDV 269
cbiO PRK13631
cobalt transporter ATP-binding subunit; Provisional
 3-275 7.33e-29

cobalt transporter ATP-binding subunit; Provisional


Pssm-ID: 237451 [Multi-domain]  Cd Length: 320  Bit Score: 113.79  E-value: 7.33e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131020733   3 KKQVSLRLENVTKIFKDKKNNtEVIAVNNSTFEIKPGELITLLGPSGCGKTTTLRMVAGFELPTKGKIYIGN-------- 74
Cdd:PRK13631   17 SDDIILRVKNLYCVFDEKQEN-ELVALNNISYTFEKNKIYFIIGNSGSGKSTLVTHFNGLIKSKYGTIQVGDiyigdkkn 95

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131020733  75 -EDVTFLPPNK---------RDTATVFQ--SYGLFPHmTVFDNVAYGLKLRKLSREEIEKRVFEALEMVGLKD-LASRAP 141
Cdd:PRK13631   96 nHELITNPYSKkiknfkelrRRVSMVFQfpEYQLFKD-TIEKDIMFGPVALGVKKSEAKKLAKFYLNKMGLDDsYLERSP 174

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131020733 142 SRLSGGQQQRVTLARSIIVEPAILLLDEPLSNLDALlREQMRIEIKKIQRKLGITAIYVTHDRVEAMSLSDRIIVMKDGK 221
Cdd:PRK13631  175 FGLSGGQKRRVAIAGILAIQPEILIFDEPTAGLDPK-GEHEMMQLILDAKANNKTVFVITHTMEHVLEVADEVIVMDKGK 253

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1131020733 222 IMQIGTPVEIYEDPiskfvaGFIGKVAFFTVDVIGKENDNIIIDFKGKKLIMKK 275
Cdd:PRK13631  254 ILKTGTPYEIFTDQ------HIINSTSIQVPRVIQVINDLIKKDPKYKKLYQKQ 301
PRK14239 PRK14239
phosphate transporter ATP-binding protein; Provisional
 8-244 1.33e-28

phosphate transporter ATP-binding protein; Provisional


Pssm-ID: 184585 [Multi-domain]  Cd Length: 252  Bit Score: 111.41  E-value: 1.33e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131020733   8 LRLENVTKIFKDKKnnteviAVNNSTFEIKPGELITLLGPSGCGKTTTLRMVAGF-----ELPTKG-------KIYIGNE 75
Cdd:PRK14239    6 LQVSDLSVYYNKKK------ALNSVSLDFYPNEITALIGPSGSGKSTLLRSINRMndlnpEVTITGsivynghNIYSPRT 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131020733  76 DVTFLppnKRDTATVFQSYGLFPhMTVFDNVAYGLKL-----RKLSREEIEKRVFEALEMVGLKDLASRAPSRLSGGQQQ 150
Cdd:PRK14239   80 DTVDL---RKEIGMVFQQPNPFP-MSIYENVVYGLRLkgikdKQVLDEAVEKSLKGASIWDEVKDRLHDSALGLSGGQQQ 155

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131020733 151 RVTLARSIIVEPAILLLDEPLSNLDALlrEQMRIEIKKIQRKLGITAIYVTHDRVEAMSLSDRIIVMKDGKIMQIGTPVE 230
Cdd:PRK14239  156 RVCIARVLATSPKIILLDEPTSALDPI--SAGKIEETLLGLKDDYTMLLVTRSMQQASRISDRTGFFLDGDLIEYNDTKQ 233

                         250
                  ....*....|....
gi 1131020733 231 IYEDPISKFVAGFI 244
Cdd:PRK14239  234 MFMNPKHKETEDYI 247
PRK10535 PRK10535
macrolide ABC transporter ATP-binding protein/permease MacB;
8-223 1.33e-28

macrolide ABC transporter ATP-binding protein/permease MacB;


Pssm-ID: 182528 [Multi-domain]  Cd Length: 648  Bit Score: 116.75  E-value: 1.33e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131020733   8 LRLENVTKIFKDKKNNTEVIavNNSTFEIKPGELITLLGPSGCGKTTTLRMVAGFELPTKGKIYIGNEDVTFLPPN---- 83
Cdd:PRK10535    5 LELKDIRRSYPSGEEQVEVL--KGISLDIYAGEMVAIVGASGSGKSTLMNILGCLDKPTSGTYRVAGQDVATLDADalaq 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131020733  84 -KRDT-ATVFQSYGLFPHMTVFDNVAYGLKLRKLSREEIEKRVFEALEMVGLKDLASRAPSRLSGGQQQRVTLARSIIVE 161
Cdd:PRK10535   83 lRREHfGFIFQRYHLLSHLTAAQNVEVPAVYAGLERKQRLLRAQELLQRLGLEDRVEYQPSQLSGGQQQRVSIARALMNG 162

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1131020733 162 PAILLLDEPLSNLDALLREQMRIEIKKIQRKlGITAIYVTHDRVEAMSlSDRIIVMKDGKIM 223
Cdd:PRK10535  163 GQVILADEPTGALDSHSGEEVMAILHQLRDR-GHTVIIVTHDPQVAAQ-AERVIEIRDGEIV 222
COG4586 COG4586
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ...
 10-243 1.94e-28

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


Pssm-ID: 443643 [Multi-domain]  Cd Length: 323  Bit Score: 112.87  E-value: 1.94e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131020733  10 LENVTKIFKDKKNN---------------TEVIAVNNSTFEIKPGELITLLGPSGCGKTTTLRMVAGFELPTKGKIYIGN 74
Cdd:COG4586     4 VENLSKTYRVYEKEpglkgalkglfrreyREVEAVDDISFTIEPGEIVGFIGPNGAGKSTTIKMLTGILVPTSGEVRVLG 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131020733  75 EDvtflpPNKRDTA------TVF-QSYGLFPHMTVFDNVAYGLKLRKLSREEIEKRVFEALEMVGLKDLASRAPSRLSGG 147
Cdd:COG4586    84 YV-----PFKRRKEfarrigVVFgQRSQLWWDLPAIDSFRLLKAIYRIPDAEYKKRLDELVELLDLGELLDTPVRQLSLG 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131020733 148 QQQRVTLARSIIVEPAILLLDEPLSNLDALLREQMRIEIKKIQRKLGITAIYVTHD--RVEAmsLSDRIIVMKDGKImqi 225
Cdd:COG4586   159 QRMRCELAAALLHRPKILFLDEPTIGLDVVSKEAIREFLKEYNRERGTTILLTSHDmdDIEA--LCDRVIVIDHGRI--- 233

                         250
                  ....*....|....*...
gi 1131020733 226 gtpveIYEDPISKFVAGF 243
Cdd:COG4586   234 -----IYDGSLEELKERF 246
cbiO PRK13645
energy-coupling factor transporter ATPase;
10-234 3.02e-28

energy-coupling factor transporter ATPase;


Pssm-ID: 184204 [Multi-domain]  Cd Length: 289  Bit Score: 111.64  E-value: 3.02e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131020733  10 LENVTKIFKdKKNNTEVIAVNNSTFEIKPGELITLLGPSGCGKTTTLRMVAGFELPTKGKIYIGNEDVtflPPN------ 83
Cdd:PRK13645    9 LDNVSYTYA-KKTPFEFKALNNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGLIISETGQTIVGDYAI---PANlkkike 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131020733  84 ----KRDTATVFQ--SYGLFPHmTVFDNVAYGLKLRKLSREEIEKRVFEALEMVGL-KDLASRAPSRLSGGQQQRVTLAR 156
Cdd:PRK13645   85 vkrlRKEIGLVFQfpEYQLFQE-TIEKDIAFGPVNLGENKQEAYKKVPELLKLVQLpEDYVKRSPFELSGGQKRRVALAG 163

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1131020733 157 SIIVEPAILLLDEPLSNLDALLREQMRIEIKKIQRKLGITAIYVTHDRVEAMSLSDRIIVMKDGKIMQIGTPVEIYED 234
Cdd:PRK13645  164 IIAMDGNTLVLDEPTGGLDPKGEEDFINLFERLNKEYKKRIIMVTHNMDQVLRIADEVIVMHEGKVISIGSPFEIFSN 241
cbiO PRK13636
cobalt transporter ATP-binding subunit; Provisional
 28-234 3.98e-28

cobalt transporter ATP-binding subunit; Provisional


Pssm-ID: 184196 [Multi-domain]  Cd Length: 283  Bit Score: 111.09  E-value: 3.98e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131020733  28 AVNNSTFEIKPGELITLLGPSGCGKTTTLRMVAGFELPTKGKIYIGNEDVTF----LPPNKRDTATVFQS--YGLFPhMT 101
Cdd:PRK13636   21 ALKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGKPIDYsrkgLMKLRESVGMVFQDpdNQLFS-AS 99

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131020733 102 VFDNVAYGLKLRKLSREEIEKRVFEALEMVGLKDLASRAPSRLSGGQQQRVTLARSIIVEPAILLLDEPLSNLDALLREQ 181
Cdd:PRK13636  100 VYQDVSFGAVNLKLPEDEVRKRVDNALKRTGIEHLKDKPTHCLSFGQKKRVAIAGVLVMEPKVLVLDEPTAGLDPMGVSE 179

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1131020733 182 MRIEIKKIQRKLGITAIYVTHDRVEAMSLSDRIIVMKDGKIMQIGTPVEIYED 234
Cdd:PRK13636  180 IMKLLVEMQKELGLTIIIATHDIDIVPLYCDNVFVMKEGRVILQGNPKEVFAE 232
YddA COG4178
ABC-type uncharacterized transport system, permease and ATPase components [General function ...
 29-230 8.10e-28

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


Pssm-ID: 443337 [Multi-domain]  Cd Length: 571  Bit Score: 114.13  E-value: 8.10e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131020733  29 VNNSTFEIKPGE--LITllGPSGCGKTTTLRMVAGFELPTKGKIYI-GNEDVTFLPpnkrdtatvfQ-SYglFPHMTVFD 104
Cdd:COG4178   379 LEDLSLSLKPGErlLIT--GPSGSGKSTLLRAIAGLWPYGSGRIARpAGARVLFLP----------QrPY--LPLGTLRE 444

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131020733 105 NVAYGLKLRKLSREEIEkrvfEALEMVGLKDLASRA------PSRLSGGQQQRVTLARSIIVEPAILLLDEPLSNLDALL 178
Cdd:COG4178   445 ALLYPATAEAFSDAELR----EALEAVGLGHLAERLdeeadwDQVLSLGEQQRLAFARLLLHKPDWLFLDEATSALDEEN 520

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1131020733 179 REQMrieIKKIQRKL-GITAIYVTHdRVEAMSLSDRIIVMKDGKIMQIgTPVE 230
Cdd:COG4178   521 EAAL---YQLLREELpGTTVISVGH-RSTLAAFHDRVLELTGDGSWQL-LPAE 568
PRK09984 PRK09984
phosphonate ABC transporter ATP-binding protein;
5-227 1.46e-27

phosphonate ABC transporter ATP-binding protein;


Pssm-ID: 182182 [Multi-domain]  Cd Length: 262  Bit Score: 108.95  E-value: 1.46e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131020733   5 QVSLRLENVTKIFKDKKnnteviAVNNSTFEIKPGELITLLGPSGCGKTTTLR----MVAGFELPTKGKIYIGN------ 74
Cdd:PRK09984    2 QTIIRVEKLAKTFNQHQ------ALHAVDLNIHHGEMVALLGPSGSGKSTLLRhlsgLITGDKSAGSHIELLGRtvqreg 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131020733  75 ---EDVTflpPNKRDTATVFQSYGLFPHMTVFDNVAYGLK---------LRKLSREEiEKRVFEALEMVGLKDLASRAPS 142
Cdd:PRK09984   76 rlaRDIR---KSRANTGYIFQQFNLVNRLSVLENVLIGALgstpfwrtcFSWFTREQ-KQRALQALTRVGMVHFAHQRVS 151

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131020733 143 RLSGGQQQRVTLARSIIVEPAILLLDEPLSNLDAllrEQMRI---EIKKIQRKLGITAIYVTHDRVEAMSLSDRIIVMKD 219
Cdd:PRK09984  152 TLSGGQQQRVAIARALMQQAKVILADEPIASLDP---ESARIvmdTLRDINQNDGITVVVTLHQVDYALRYCERIVALRQ 228


                  ....*...
gi 1131020733 220 GKIMQIGT 227
Cdd:PRK09984  229 GHVFYDGS 236
PRK14246 PRK14246
phosphate ABC transporter ATP-binding protein; Provisional
 29-248 2.32e-27

phosphate ABC transporter ATP-binding protein; Provisional


Pssm-ID: 172734 [Multi-domain]  Cd Length: 257  Bit Score: 108.60  E-value: 2.32e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131020733  29 VNNSTFEIKPGELITLLGPSGCGKTTTLRMVAGF------ELPTKGKIYIGNEDVTFLPPNK--RDTATVFQSYGLFPHM 100
Cdd:PRK14246   26 LKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLieiydsKIKVDGKVLYFGKDIFQIDAIKlrKEVGMVFQQPNPFPHL 105

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131020733 101 TVFDNVAYGLKLRKLS-REEIEKRVFEALEMVGL----KDLASRAPSRLSGGQQQRVTLARSIIVEPAILLLDEPLSNLD 175
Cdd:PRK14246  106 SIYDNIAYPLKSHGIKeKREIKKIVEECLRKVGLwkevYDRLNSPASQLSGGQQQRLTIARALALKPKVLLMDEPTSMID 185

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1131020733 176 ALLREQMRIEIKKIQRKLGItaIYVTHDRVEAMSLSDRIIVMKDGKIMQIGTPVEIYEDPISKFVAGF-IGKVA 248
Cdd:PRK14246  186 IVNSQAIEKLITELKNEIAI--VIVSHNPQQVARVADYVAFLYNGELVEWGSSNEIFTSPKNELTEKYvIGRIS 257
ABC_Carb_Monos_II cd03215
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ...
 28-222 2.66e-27

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: 105.98  E-value: 2.66e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131020733  28 AVNNSTFEIKPGELITLLGPSGCGKTTTLRMVAGFELPTKGKIYIGNEDVTFLPPNKRDTATVF------QSYGLFPHMT 101
Cdd:cd03215    15 AVRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITLDGKPVTRRSPRDAIRAGIAyvpedrKREGLVLDLS 94

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131020733 102 VFDNVAyglklrklsreeiekrvfealemvglkdlasrAPSRLSGGQQQRVTLARSIIVEPAILLLDEPLSNLDALLREq 181
Cdd:cd03215    95 VAENIA--------------------------------LSSLLSGGNQQKVVLARWLARDPRVLILDEPTRGVDVGAKA- 141

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 1131020733 182 mriEIKKIQRKL---GITAIYVTHDRVEAMSLSDRIIVMKDGKI 222
Cdd:cd03215   142 ---EIYRLIRELadaGKAVLLISSELDELLGLCDRILVMYEGRI 182
PRK14258 PRK14258
phosphate ABC transporter ATP-binding protein; Provisional
 1-236 3.03e-27

phosphate ABC transporter ATP-binding protein; Provisional


Pssm-ID: 184593 [Multi-domain]  Cd Length: 261  Bit Score: 108.20  E-value: 3.03e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131020733   1 MKKKQVSLRLENVTKIFKDKKnnteviAVNNSTFEIKPGELITLLGPSGCGKTTTLRMVAGF-----ELPTKGKIYIGNE 75
Cdd:PRK14258    1 MSKLIPAIKVNNLSFYYDTQK------ILEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLNRMnelesEVRVEGRVEFFNQ 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131020733  76 DVTFLPPN----KRDTATVFQSYGLFPhMTVFDNVAYGLKL----RKLSREEIEKRVFEALEMVG-LKDLASRAPSRLSG 146
Cdd:PRK14258   75 NIYERRVNlnrlRRQVSMVHPKPNLFP-MSVYDNVAYGVKIvgwrPKLEIDDIVESALKDADLWDeIKHKIHKSALDLSG 153

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131020733 147 GQQQRVTLARSIIVEPAILLLDEPLSNLDALlrEQMRIE--IKKIQRKLGITAIYVTHDRVEAMSLSDRIIVMKD----- 219
Cdd:PRK14258  154 GQQQRLCIARALAVKPKVLLMDEPCFGLDPI--ASMKVEslIQSLRLRSELTMVIVSHNLHQVSRLSDFTAFFKGnenri 231

                         250
                  ....*....|....*..
gi 1131020733 220 GKIMQIGTPVEIYEDPI 236
Cdd:PRK14258  232 GQLVEFGLTKKIFNSPH 248
met_CoM_red_A2 TIGR03269
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ...
 8-243 3.55e-26

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: 109.12  E-value: 3.55e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131020733   8 LRLENVTKIFKDKKnnteviAVNNSTFEIKPGELITLLGPSGCGKTTTLRMVAGFE--LPTKGKI-----------YIG- 73
Cdd:TIGR03269   1 IEVKNLTKKFDGKE------VLKNISFTIEEGEVLGILGRSGAGKSVLMHVLRGMDqyEPTSGRIiyhvalcekcgYVEr 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131020733  74 ----------------NEDVTFLPPNK-------RDTATVFQ-SYGLFPHMTVFDNVAYGLKLRKLSREEIEKRVFEALE 129
Cdd:TIGR03269  75 pskvgepcpvcggtlePEEVDFWNLSDklrrrirKRIAIMLQrTFALYGDDTVLDNVLEALEEIGYEGKEAVGRAVDLIE 154

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131020733 130 MVGLKDLASRAPSRLSGGQQQRVTLARSIIVEPAILLLDEPLSNLDALLREQMRIEIKKIQRKLGITAIYVTHDRVEAMS 209
Cdd:TIGR03269 155 MVQLSHRITHIARDLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALEEAVKASGISMVLTSHWPEVIED 234

                         250       260       270
                  ....*....|....*....|....*....|....
gi 1131020733 210 LSDRIIVMKDGKIMQIGTPVEIyedpISKFVAGF 243
Cdd:TIGR03269 235 LSDKAIWLENGEIKEEGTPDEV----VAVFMEGV 264
ABC_NatA_like cd03267
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ...
 10-223 5.45e-26

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: 103.95  E-value: 5.45e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131020733  10 LENVTKIFKDKKNntEVIAVNNSTFEIKPGELITLLGPSGCGKTTTLRMVAGFELPTKGKIYIGNedvtFLPPNKRDT-- 87
Cdd:cd03267    20 IGSLKSLFKRKYR--EVEALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRVAG----LVPWKRRKKfl 93

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131020733  88 ---ATVF-QSYGLFPHMTVFDNVAYGLKLRKLSREEIEKRVFEALEMVGLKDLASRAPSRLSGGQQQRVTLARSIIVEPA 163
Cdd:cd03267    94 rriGVVFgQKTQLWWDLPVIDSFYLLAAIYDLPPARFKKRLDELSELLDLEELLDTPVRQLSLGQRMRAEIAAALLHEPE 173

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131020733 164 ILLLDEPLSNLDALLREQMRIEIKKIQRKLGITAIYVTHDRVEAMSLSDRIIVMKDGKIM 223
Cdd:cd03267   174 ILFLDEPTIGLDVVAQENIRNFLKEYNRERGTTVLLTSHYMKDIEALARRVLVIDKGRLL 233
cbiO PRK13646
energy-coupling factor transporter ATPase;
6-234 7.39e-26

energy-coupling factor transporter ATPase;


Pssm-ID: 184205 [Multi-domain]  Cd Length: 286  Bit Score: 104.86  E-value: 7.39e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131020733   6 VSLRLENVTKIFKdKKNNTEVIAVNNSTFEIKPGELITLLGPSGCGKTTTLRMVAGFELPTKGKIYIGNEDVT------F 79
Cdd:PRK13646    1 MTIRFDNVSYTYQ-KGTPYEHQAIHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVDDITIThktkdkY 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131020733  80 LPPNKRDTATVFQsyglFPHMTVF-DNVA----YGLKLRKLSREEIEKRVFEALEMVGL-KDLASRAPSRLSGGQQQRVT 153
Cdd:PRK13646   80 IRPVRKRIGMVFQ----FPESQLFeDTVEreiiFGPKNFKMNLDEVKNYAHRLLMDLGFsRDVMSQSPFQMSGGQMRKIA 155

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131020733 154 LARSIIVEPAILLLDEPLSNLDALLREQMRIEIKKIQRKLGITAIYVTHDRVEAMSLSDRIIVMKDGKIMQIGTPVEIYE 233
Cdd:PRK13646  156 IVSILAMNPDIIVLDEPTAGLDPQSKRQVMRLLKSLQTDENKTIILVSHDMNEVARYADEVIVMKEGSIVSQTSPKELFK 235


                  .
gi 1131020733 234 D 234
Cdd:PRK13646  236 D 236
ABCC_cytochrome_bd cd03247
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ...
 8-226 7.73e-26

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: 102.01  E-value: 7.73e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131020733   8 LRLENVTkiFKDKKNNTEVIavNNSTFEIKPGELITLLGPSGCGKTTTLRMVAGFELPTKGKIYIGNEDVTFLPPNKRDT 87
Cdd:cd03247     1 LSINNVS--FSYPEQEQQVL--KNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDGVPVSDLEKALSSL 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131020733  88 ATVF-QSYGLFpHMTVFDNVAyglklrklsreeiekrvfealemvglkdlasrapSRLSGGQQQRVTLARSIIVEPAILL 166
Cdd:cd03247    77 ISVLnQRPYLF-DTTLRNNLG----------------------------------RRFSGGERQRLALARILLQDAPIVL 121

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1131020733 167 LDEPLSNLDALL-REQMRIEIKKIQRKlgiTAIYVTHdRVEAMSLSDRIIVMKDGKIMQIG 226
Cdd:cd03247   122 LDEPTVGLDPITeRQLLSLIFEVLKDK---TLIWITH-HLTGIEHMDKILFLENGKIIMQG 178
CydC TIGR02868
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ...
 27-203 8.58e-26

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: 108.22  E-value: 8.58e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131020733  27 IAVNNSTFEIKPGELITLLGPSGCGKTTTLRMVAGFELPTKGKIYIGNEDVTFLPPNK-RDTATVF-QSYGLFpHMTVFD 104
Cdd:TIGR02868 349 PVLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPLQGEVTLDGVPVSSLDQDEvRRRVSVCaQDAHLF-DTTVRE 427

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131020733 105 NVAyglklrkLSREEI-EKRVFEALEMVGLKDLASRAP-----------SRLSGGQQQRVTLARSIIVEPAILLLDEPLS 172
Cdd:TIGR02868 428 NLR-------LARPDAtDEELWAALERVGLADWLRALPdgldtvlgeggARLSGGERQRLALARALLADAPILLLDEPTE 500

                         170       180       190
                  ....*....|....*....|....*....|.
gi 1131020733 173 NLDALLREQMRIEIKKIQRklGITAIYVTHD 203
Cdd:TIGR02868 501 HLDAETADELLEDLLAALS--GRTVVLITHH 529
PRK11160 PRK11160
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
 4-227 1.30e-25

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


Pssm-ID: 236865 [Multi-domain]  Cd Length: 574  Bit Score: 107.99  E-value: 1.30e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131020733   4 KQVSLRLENVTkiFKDKKNNTEVIavNNSTFEIKPGELITLLGPSGCGKTTTLRMVAGFELPTKGKIYIGNEDVTFLP-P 82
Cdd:PRK11160  335 DQVSLTLNNVS--FTYPDQPQPVL--KGLSLQIKAGEKVALLGRTGCGKSTLLQLLTRAWDPQQGEILLNGQPIADYSeA 410

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131020733  83 NKRDTATVF-QSYGLFPHmTVFDNvaygLKLRKlsREEIEKRVFEALEMVGLKDLASRAPS----------RLSGGQQQR 151
Cdd:PRK11160  411 ALRQAISVVsQRVHLFSA-TLRDN----LLLAA--PNASDEALIEVLQQVGLEKLLEDDKGlnawlgeggrQLSGGEQRR 483

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131020733 152 VTLARSIIVEPAILLLDEPLSNLDA--------LLREQMRieikkiqrklGITAIYVTHdRVEAMSLSDRIIVMKDGKIM 223
Cdd:PRK11160  484 LGIARALLHDAPLLLLDEPTEGLDAeterqileLLAEHAQ----------NKTVLMITH-RLTGLEQFDRICVMDNGQII 552


                  ....
gi 1131020733 224 QIGT 227
Cdd:PRK11160  553 EQGT 556
PRK11174 PRK11174
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
 33-227 1.90e-25

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


Pssm-ID: 236870 [Multi-domain]  Cd Length: 588  Bit Score: 107.24  E-value: 1.90e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131020733  33 TFEIKPGELITLLGPSGCGKTTTLRMVAGFeLPTKGKIYIGNEDVTFLPPN--KRDTATVFQSYGLFpHMTVFDNVAygl 110
Cdd:PRK11174  370 NFTLPAGQRIALVGPSGAGKTSLLNALLGF-LPYQGSLKINGIELRELDPEswRKHLSWVGQNPQLP-HGTLRDNVL--- 444

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131020733 111 klrkLSREEI-EKRVFEALEMVGLKDLASRAP-----------SRLSGGQQQRVTLARSIIVEPAILLLDEPLSNLDALL 178
Cdd:PRK11174  445 ----LGNPDAsDEQLQQALENAWVSEFLPLLPqgldtpigdqaAGLSVGQAQRLALARALLQPCQLLLLDEPTASLDAHS 520

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 1131020733 179 REQMRIEIKKIQRklGITAIYVTHdRVEAMSLSDRIIVMKDGKIMQIGT 227
Cdd:PRK11174  521 EQLVMQALNAASR--RQTTLMVTH-QLEDLAQWDQIWVMQDGQIVQQGD 566
btuD PRK09536
corrinoid ABC transporter ATPase; Reviewed
 25-231 3.53e-25

corrinoid ABC transporter ATPase; Reviewed


Pssm-ID: 236554 [Multi-domain]  Cd Length: 402  Bit Score: 105.31  E-value: 3.53e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131020733  25 EVIAVNNSTFEIKPGELITLLGPSGCGKTTTLRMVAGFELPTKGKIYIGNEDVTFLPPNK--RDTATVFQS--------- 93
Cdd:PRK09536   15 DTTVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGDDVEALSARAasRRVASVPQDtslsfefdv 94

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131020733  94 -----YGLFPHMTVFDNVAyglklrklsrEEIEKRVFEALEMVGLKDLASRAPSRLSGGQQQRVTLARSIIVEPAILLLD 168
Cdd:PRK09536   95 rqvveMGRTPHRSRFDTWT----------ETDRAAVERAMERTGVAQFADRPVTSLSGGERQRVLLARALAQATPVLLLD 164

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1131020733 169 EPLSNLDalLREQMR-IEIKKIQRKLGITAIYVTHDRVEAMSLSDRIIVMKDGKIMQIGTPVEI 231
Cdd:PRK09536  165 EPTASLD--INHQVRtLELVRRLVDDGKTAVAAIHDLDLAARYCDELVLLADGRVRAAGPPADV 226
BtuD COG4138
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ...
 33-231 7.34e-25

ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism];


Pssm-ID: 443313 [Multi-domain]  Cd Length: 248  Bit Score: 101.46  E-value: 7.34e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131020733  33 TFEIKPGELITLLGPSGCGKTTTLRMVAGFeLPTKGKIYIGNEDVTFLPPNK--RDTATVFQSYGLFPHMTVFDNVAYGL 110
Cdd:COG4138    16 SAQVNAGELIHLIGPNGAGKSTLLARMAGL-LPGQGEILLNGRPLSDWSAAElaRHRAYLSQQQSPPFAMPVFQYLALHQ 94

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131020733 111 KlRKLSREEIEKRVFEALEMVGLKDLASRAPSRLSGGQQQRVTLARSII-VEPAI------LLLDEPLSNLD-----ALL 178
Cdd:COG4138    95 P-AGASSEAVEQLLAQLAEALGLEDKLSRPLTQLSGGEWQRVRLAAVLLqVWPTInpegqlLLLDEPMNSLDvaqqaALD 173

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1131020733 179 REQMRIeikkiqRKLGITAIYVTHDRVEAMSLSDRIIVMKDGKIMQIGTPVEI 231
Cdd:COG4138   174 RLLREL------CQQGITVVMSSHDLNHTLRHADRVWLLKQGKLVASGETAEV 220
ABC2_perm_RbbA NF033858
ribosome-associated ATPase/putative transporter RbbA;
28-231 1.04e-24

ribosome-associated ATPase/putative transporter RbbA;


Pssm-ID: 468210 [Multi-domain]  Cd Length: 907  Bit Score: 105.59  E-value: 1.04e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131020733  28 AVNNSTFEIKPGELITLLGPSGCGKTTTLRMVAGFELPTKGKIYI-GNedvtflPPNKRDTAT------VFQSYGLFPHM 100
Cdd:NF033858  281 AVDHVSFRIRRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGEAWLfGQ------PVDAGDIATrrrvgyMSQAFSLYGEL 354

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131020733 101 TVFDNVAYGLKLRKLSREEIEKRVFEALEMVGLKDLASRAPSRLSGGQQQRVTLARSIIVEPAILLLDEPLSNLDALLRE 180
Cdd:NF033858  355 TVRQNLELHARLFHLPAAEIAARVAEMLERFDLADVADALPDSLPLGIRQRLSLAVAVIHKPELLILDEPTSGVDPVARD 434

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1131020733 181 ---QMRIEikkIQRKLGITaIYV-THDRVEAMsLSDRIIVMKDGKIMQIGTPVEI 231
Cdd:NF033858  435 mfwRLLIE---LSREDGVT-IFIsTHFMNEAE-RCDRISLMHAGRVLASDTPAAL 484
3a01208 TIGR00958
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
 33-235 1.15e-24

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: 1.15e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131020733  33 TFEIKPGELITLLGPSGCGKTTTLRMVAGFELPTKGKIYIGNEDVT-----FLppnKRDTATVFQSYGLFPHmTVFDNVA 107
Cdd:TIGR00958 501 TFTLHPGEVVALVGPSGSGKSTVAALLQNLYQPTGGQVLLDGVPLVqydhhYL---HRQVALVGQEPVLFSG-SVRENIA 576

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131020733 108 YGLklRKLSREEIEKrvfeALEMVGLKDLASRAP-----------SRLSGGQQQRVTLARSIIVEPAILLLDEPLSNLDA 176
Cdd:TIGR00958 577 YGL--TDTPDEEIMA----AAKAANAHDFIMEFPngydtevgekgSQLSGGQKQRIAIARALVRKPRVLILDEATSALDA 650

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1131020733 177 LLrEQMRIEIKKIQrklGITAIYVTHdRVEAMSLSDRIIVMKDGKIMQIGTPVEIYEDP 235
Cdd:TIGR00958 651 EC-EQLLQESRSRA---SRTVLLIAH-RLSTVERADQILVLKKGSVVEMGTHKQLMEDQ 704
PRK10253 PRK10253
iron-enterobactin ABC transporter ATP-binding protein;
1-231 3.70e-24

iron-enterobactin ABC transporter ATP-binding protein;


Pssm-ID: 182336 [Multi-domain]  Cd Length: 265  Bit Score: 100.06  E-value: 3.70e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131020733   1 MKKKQVSLRLENVTKIFKDKknntevIAVNNSTFEIKPGELITLLGPSGCGKTTTLRMVAGFELPTKGKIYIGNEDVT-- 78
Cdd:PRK10253    1 MTESVARLRGEQLTLGYGKY------TVAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIQhy 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131020733  79 ----------FLPPNKRD----TATVFQSYGLFPHMTVFDNvayglklrklSREEIEKRVFEALEMVGLKDLASRAPSRL 144
Cdd:PRK10253   75 askevarrigLLAQNATTpgdiTVQELVARGRYPHQPLFTR----------WRKEDEEAVTKAMQATGITHLADQSVDTL 144

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131020733 145 SGGQQQRVTLARSIIVEPAILLLDEPLSNLDALLREQMRIEIKKIQRKLGITAIYVTHDRVEAMSLSDRIIVMKDGKIMQ 224
Cdd:PRK10253  145 SGGQRQRAWIAMVLAQETAIMLLDEPTTWLDISHQIDLLELLSELNREKGYTLAAVLHDLNQACRYASHLIALREGKIVA 224


                  ....*..
gi 1131020733 225 IGTPVEI 231
Cdd:PRK10253  225 QGAPKEI 231
CP_lyasePhnK TIGR02323
phosphonate C-P lyase system protein PhnK; Members of this family are the PhnK protein of C-P ...
 8-235 7.99e-24

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: 98.75  E-value: 7.99e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131020733   8 LRLENVTKIFKDKKnnteviAVNNSTFEIKPGELITLLGPSGCGKTTTLRMVAGFELPTKGKI-YI----GNEDVTFLPP 82
Cdd:TIGR02323   4 LQVSGLSKSYGGGK------GCRDVSFDLYPGEVLGIVGESGSGKSTLLGCLAGRLAPDHGTAtYImrsgAELELYQLSE 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131020733  83 NKR------DTATVFQSY--GLFPHMTVFDNVA----------YGlKLRKLSREEIEKrvfEALEMVGLKDLasraPSRL 144
Cdd:TIGR02323  78 AERrrlmrtEWGFVHQNPrdGLRMRVSAGANIGerlmaigarhYG-NIRATAQDWLEE---VEIDPTRIDDL----PRAF 149

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131020733 145 SGGQQQRVTLARSIIVEPAILLLDEPLSNLDALLREQMRIEIKKIQRKLGITAIYVTHDRVEAMSLSDRIIVMKDGKIMQ 224
Cdd:TIGR02323 150 SGGMQQRLQIARNLVTRPRLVFMDEPTGGLDVSVQARLLDLLRGLVRDLGLAVIIVTHDLGVARLLAQRLLVMQQGRVVE 229

                         250
                  ....*....|.
gi 1131020733 225 IGTPVEIYEDP 235
Cdd:TIGR02323 230 SGLTDQVLDDP 240
araG PRK11288
L-arabinose ABC transporter ATP-binding protein AraG;
8-221 1.06e-23

L-arabinose ABC transporter ATP-binding protein AraG;


Pssm-ID: 183077 [Multi-domain]  Cd Length: 501  Bit Score: 101.91  E-value: 1.06e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131020733   8 LRLENVTKIFKDkknnteVIAVNNSTFEIKPGELITLLGPSGCGKTTTLRMVAGFELPTKGKIYIGNEDVTFlpPNKRDT 87
Cdd:PRK11288    5 LSFDGIGKTFPG------VKALDDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSILIDGQEMRF--ASTTAA 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131020733  88 -----ATVFQSYGLFPHMTVFDNVAYGL---KLRKLSREEIEKRVFEALEMVGLkDLASRAP-SRLSGGQQQRVTLARSI 158
Cdd:PRK11288   77 laagvAIIYQELHLVPEMTVAENLYLGQlphKGGIVNRRLLNYEAREQLEHLGV-DIDPDTPlKYLSIGQRQMVEIAKAL 155

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1131020733 159 IVEPAILLLDEPLSNLDAllREqmrIEI-KKIQRKL---GITAIYVTHDRVEAMSLSDRIIVMKDGK 221
Cdd:PRK11288  156 ARNARVIAFDEPTSSLSA--RE---IEQlFRVIRELraeGRVILYVSHRMEEIFALCDAITVFKDGR 217
PRK14243 PRK14243
phosphate transporter ATP-binding protein; Provisional
 5-212 1.06e-23

phosphate transporter ATP-binding protein; Provisional


Pssm-ID: 184588 [Multi-domain]  Cd Length: 264  Bit Score: 98.70  E-value: 1.06e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131020733   5 QVSLRLENVTKIFKDKknntevIAVNNSTFEIKPGELITLLGPSGCGKTTTLR-------MVAGFELptKGKIYIGNEDV 77
Cdd:PRK14243    8 ETVLRTENLNVYYGSF------LAVKNVWLDIPKNQITAFIGPSGCGKSTILRcfnrlndLIPGFRV--EGKVTFHGKNL 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131020733  78 --TFLPPN--KRDTATVFQSYGLFPHmTVFDNVAYGLKLRKLS---REEIEKRVFEALEMVGLKDLASRAPSRLSGGQQQ 150
Cdd:PRK14243   80 yaPDVDPVevRRRIGMVFQKPNPFPK-SIYDNIAYGARINGYKgdmDELVERSLRQAALWDEVKDKLKQSGLSLSGGQQQ 158

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1131020733 151 RVTLARSIIVEPAILLLDEPLSNLDALlrEQMRIE--IKKIQRKLgiTAIYVTHDRVEAMSLSD 212
Cdd:PRK14243  159 RLCIARAIAVQPEVILMDEPCSALDPI--STLRIEelMHELKEQY--TIIIVTHNMQQAARVSD 218
ABCC_MRP_domain1 cd03250
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ...
 8-221 1.26e-23

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: 96.77  E-value: 1.26e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131020733   8 LRLENVTKIFKDKKNNTEVIaVNNSTFEIKPGELITLLGPSGCGKTTTLRMVAGfELP-TKGKIYIGNEdvtflppnkrd 86
Cdd:cd03250     1 ISVEDASFTWDSGEQETSFT-LKDINLEVPKGELVAIVGPVGSGKSSLLSALLG-ELEkLSGSVSVPGS----------- 67

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131020733  87 TATVFQSYGLFPhMTVFDNVAYGLKLrklsREEIEKRVFEA------LEMVGLKDL---ASRAPSrLSGGQQQRVTLARS 157
Cdd:cd03250    68 IAYVSQEPWIQN-GTIRENILFGKPF----DEERYEKVIKAcalepdLEILPDGDLteiGEKGIN-LSGGQKQRISLARA 141

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1131020733 158 IIVEPAILLLDEPLSNLDA---------LLREQMrieikkiqrKLGITAIYVTHdRVEAMSLSDRIIVMKDGK 221
Cdd:cd03250   142 VYSDADIYLLDDPLSAVDAhvgrhifenCILGLL---------LNNKTRILVTH-QLQLLPHADQIVVLDNGR 204
dppD PRK11022
dipeptide transporter ATP-binding subunit; Provisional
 8-235 1.29e-23

dipeptide transporter ATP-binding subunit; Provisional


Pssm-ID: 182906 [Multi-domain]  Cd Length: 326  Bit Score: 99.43  E-value: 1.29e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131020733   8 LRLENVTKIFKDKKnnTEVIAVNNSTFEIKPGELITLLGPSGCGKTTTLRMVAGF-ELPTK---GKIYIGNEDVTFLPPN 83
Cdd:PRK11022    4 LNVDKLSVHFGDES--APFRAVDRISYSVKQGEVVGIVGESGSGKSVSSLAIMGLiDYPGRvmaEKLEFNGQDLQRISEK 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131020733  84 KR------DTATVFQS--YGLFPHMTVFDNVAYGLKLRKL-SREEIEKRVFEALEMVGLKDLASRA---PSRLSGGQQQR 151
Cdd:PRK11022   82 ERrnlvgaEVAMIFQDpmTSLNPCYTVGFQIMEAIKVHQGgNKKTRRQRAIDLLNQVGIPDPASRLdvyPHQLSGGMSQR 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131020733 152 VTLARSIIVEPAILLLDEPLSNLDALLREQMRIEIKKIQRKLGITAIYVTHDRVEAMSLSDRIIVMKDGKIMQIGTPVEI 231
Cdd:PRK11022  162 VMIAMAIACRPKLLIADEPTTALDVTIQAQIIELLLELQQKENMALVLITHDLALVAEAAHKIIVMYAGQVVETGKAHDI 241


                  ....
gi 1131020733 232 YEDP 235
Cdd:PRK11022  242 FRAP 245
bacteriocin_ABC TIGR01193
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ...
 28-231 1.31e-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: 102.13  E-value: 1.31e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131020733  28 AVNNSTFEIKPGELITLLGPSGCGKTTTLRMVAGFELPTKGKIYIGNEDVTFLppnkrDTATVFQSYGLFPHM------T 101
Cdd:TIGR01193 489 ILSDISLTIKMNSKTTIVGMSGSGKSTLAKLLVGFFQARSGEILLNGFSLKDI-----DRHTLRQFINYLPQEpyifsgS 563

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131020733 102 VFDNVAYGLKlRKLSREEIekrvFEALEMVGLKDLASRAP-----------SRLSGGQQQRVTLARSIIVEPAILLLDEP 170
Cdd:TIGR01193 564 ILENLLLGAK-ENVSQDEI----WAACEIAEIKDDIENMPlgyqtelseegSSISGGQKQRIALARALLTDSKVLILDES 638

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1131020733 171 LSNLDALLREQMRIEIKKIQRKlgiTAIYVTHdRVEAMSLSDRIIVMKDGKIMQIGTPVEI 231
Cdd:TIGR01193 639 TSNLDTITEKKIVNNLLNLQDK---TIIFVAH-RLSVAKQSDKIIVLDHGKIIEQGSHDEL 695
PRK13657 PRK13657
glucan ABC transporter ATP-binding protein/ permease;
28-227 1.32e-23

glucan ABC transporter ATP-binding protein/ permease;


Pssm-ID: 184214 [Multi-domain]  Cd Length: 588  Bit Score: 101.96  E-value: 1.32e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131020733  28 AVNNSTFEIKPGELITLLGPSGCGKTTTLRMVAGFELPTKGKIYIGNEDVTFLPPN--KRDTATVFQSYGLFpHMTVFDN 105
Cdd:PRK13657  350 GVEDVSFEAKPGQTVAIVGPTGAGKSTLINLLQRVFDPQSGRILIDGTDIRTVTRAslRRNIAVVFQDAGLF-NRSIEDN 428

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131020733 106 VAYGlklrklsREE-IEKRVFEALEMVGLKDLASRAP-----------SRLSGGQQQRVTLARSIIVEPAILLLDEPLSN 173
Cdd:PRK13657  429 IRVG-------RPDaTDEEMRAAAERAQAHDFIERKPdgydtvvgergRQLSGGERQRLAIARALLKDPPILILDEATSA 501

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1131020733 174 LDALLREQMRIEIKKIQRklGITAIYVTHdRVEAMSLSDRIIVMKDGKIMQIGT 227
Cdd:PRK13657  502 LDVETEAKVKAALDELMK--GRTTFIIAH-RLSTVRNADRILVFDNGRVVESGS 552
PRK10261 PRK10261
glutathione transporter ATP-binding protein; Provisional
 8-235 1.60e-23

glutathione transporter ATP-binding protein; Provisional


Pssm-ID: 182342 [Multi-domain]  Cd Length: 623  Bit Score: 101.86  E-value: 1.60e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131020733   8 LRLENVTKIFKDKKNntEVIAVNNSTFEIKPGELITLLGPSGCGKTTT----LRMV--AGFELPTKGKIYIG-NEDVTFL 80
Cdd:PRK10261   13 LAVENLNIAFMQEQQ--KIAAVRNLSFSLQRGETLAIVGESGSGKSVTalalMRLLeqAGGLVQCDKMLLRRrSRQVIEL 90

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131020733  81 PPNKR---------DTATVFQS--YGLFPHMTVFDNVAYGLKLRK-LSREEI---EKRVFEALEMVGLKDLASRAPSRLS 145
Cdd:PRK10261   91 SEQSAaqmrhvrgaDMAMIFQEpmTSLNPVFTVGEQIAESIRLHQgASREEAmveAKRMLDQVRIPEAQTILSRYPHQLS 170

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131020733 146 GGQQQRVTLARSIIVEPAILLLDEPLSNLDALLREQMRIEIKKIQRKLGITAIYVTHDRVEAMSLSDRIIVMKDGKIMQI 225
Cdd:PRK10261  171 GGMRQRVMIAMALSCRPAVLIADEPTTALDVTIQAQILQLIKVLQKEMSMGVIFITHDMGVVAEIADRVLVMYQGEAVET 250

                         250
                  ....*....|
gi 1131020733 226 GTPVEIYEDP 235
Cdd:PRK10261  251 GSVEQIFHAP 260
ccmA TIGR01189
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ...
 33-183 1.69e-23

heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein encoded by ccmA in bacteria. An exception is, an arabidopsis protein. Quite likely this is encoded by an organelle. Bacterial c-type cytocromes are located on the periplasmic side of the cytoplasmic membrane. Several gene products encoded in a locus designated as 'ccm' are implicated in the transport and assembly of the functional cytochrome C. This cluster includes genes: ccmA;B;C;D;E;F;G and H. The posttranslational pathway includes the transport of heme moiety, the secretion of the apoprotein and the covalent attachment of the heme with the apoprotein. The proteins ccmA and B represent an ABC transporter; ccmC and D participate in heme transfer to ccmE, which function as a periplasmic heme chaperone. The presence of ccmF, G and H is suggested to be obligatory for the final functional assembly of cytochrome c. [Protein fate, Protein and peptide secretion and trafficking, Transport and binding proteins, Other]


Pssm-ID: 273491 [Multi-domain]  Cd Length: 198  Bit Score: 96.27  E-value: 1.69e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131020733  33 TFEIKPGELITLLGPSGCGKTTTLRMVAGFELPTKGKIYIGNEDVTFLPPN-KRDTATVFQSYGLFPHMTVFDNVAYglk 111
Cdd:TIGR01189  20 SFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRWNGTPLAEQRDEpHENILYLGHLPGLKPELSALENLHF--- 96

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1131020733 112 LRKLSREEiEKRVFEALEMVGLKDLASRAPSRLSGGQQQRVTLARSIIVEPAILLLDEPLSNLD----ALLREQMR 183
Cdd:TIGR01189  97 WAAIHGGA-QRTIEDALAAVGLTGFEDLPAAQLSAGQQRRLALARLWLSRRPLWILDEPTTALDkagvALLAGLLR 171
3a01204 TIGR00955
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ...
 30-230 1.96e-23

The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]


Pssm-ID: 273361 [Multi-domain]  Cd Length: 617  Bit Score: 101.66  E-value: 1.96e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131020733  30 NNSTFEIKPGELITLLGPSGCGKTTTLRMVAgFELPT----KGKIYIGNEDVTfLPPNKRDTATVFQSYGLFPHMTVFDN 105
Cdd:TIGR00955  42 KNVSGVAKPGELLAVMGSSGAGKTTLMNALA-FRSPKgvkgSGSVLLNGMPID-AKEMRAISAYVQQDDLFIPTLTVREH 119

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131020733 106 VAYGLKLR---KLSREEIEKRVFEALEMVGLKDLASR---APSR---LSGGQQQRVTLARSIIVEPAILLLDEPLSNLDA 176
Cdd:TIGR00955 120 LMFQAHLRmprRVTKKEKRERVDEVLQALGLRKCANTrigVPGRvkgLSGGERKRLAFASELLTDPPLLFCDEPTSGLDS 199

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1131020733 177 LLREQMRIEIKKIQRKlGITAIYVTHD-RVEAMSLSDRIIVMKDGKIMQIGTPVE 230
Cdd:TIGR00955 200 FMAYSVVQVLKGLAQK-GKTIICTIHQpSSELFELFDKIILMAEGRVAYLGSPDQ 253
cbiO PRK13638
energy-coupling factor ABC transporter ATP-binding protein;
33-232 2.36e-23

energy-coupling factor ABC transporter ATP-binding protein;


Pssm-ID: 184198 [Multi-domain]  Cd Length: 271  Bit Score: 97.77  E-value: 2.36e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131020733  33 TFEIKPGELITLLGPSGCGKTTTLRMVAGFELPTKGKIYIGNEDVTF----LPPNKRDTATVFQSyglfPHMTVF----- 103
Cdd:PRK13638   21 NLDFSLSPVTGLVGANGCGKSTLFMNLSGLLRPQKGAVLWQGKPLDYskrgLLALRQQVATVFQD----PEQQIFytdid 96

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131020733 104 DNVAYGLKLRKLSREEIEKRVFEALEMVGLKDLASRAPSRLSGGQQQRVTLARSIIVEPAILLLDEPLSNLDALLREQMR 183
Cdd:PRK13638   97 SDIAFSLRNLGVPEAEITRRVDEALTLVDAQHFRHQPIQCLSHGQKKRVAIAGALVLQARYLLLDEPTAGLDPAGRTQMI 176

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 1131020733 184 IEIKKIQRKlGITAIYVTHDRVEAMSLSDRIIVMKDGKIMQIGTPVEIY 232
Cdd:PRK13638  177 AIIRRIVAQ-GNHVIISSHDIDLIYEISDAVYVLRQGQILTHGAPGEVF 224
PRK13539 PRK13539
cytochrome c biogenesis protein CcmA; Provisional
 34-202 2.43e-23

cytochrome c biogenesis protein CcmA; Provisional


Pssm-ID: 237421 [Multi-domain]  Cd Length: 207  Bit Score: 96.10  E-value: 2.43e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131020733  34 FEIKPGELITLLGPSGCGKTTTLRMVAGFELPTKGKIYIGNEDVTFlpPNKRDTATvfqsY-----GLFPHMTVFDNVAY 108
Cdd:PRK13539   23 FTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDGGDIDD--PDVAEACH----YlghrnAMKPALTVAENLEF 96

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131020733 109 GLKLRKLSREEIEkrvfEALEMVGLKDLASRAPSRLSGGQQQRVTLARSIIVEPAILLLDEPLSNLD----ALLREQMRI 184
Cdd:PRK13539   97 WAAFLGGEELDIA----AALEAVGLAPLAHLPFGYLSAGQKRRVALARLLVSNRPIWILDEPTAALDaaavALFAELIRA 172

                         170
                  ....*....|....*...
gi 1131020733 185 EIKKiqrklGITAIYVTH 202
Cdd:PRK13539  173 HLAQ-----GGIVIAATH 185
ABCC_MRP_domain2 cd03244
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ...
 28-228 2.69e-23

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: 96.41  E-value: 2.69e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131020733  28 AVNNSTFEIKPGELITLLGPSGCGKTTT----LRMVAgfelPTKGKIYIGNEDVTFLPPNK-RdtatvfQSYGLFPHmtv 102
Cdd:cd03244    19 VLKNISFSIKPGEKVGIVGRTGSGKSSLllalFRLVE----LSSGSILIDGVDISKIGLHDlR------SRISIIPQ--- 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131020733 103 fDNVAYGLKLRK-------LSREEIekrvFEALEMVGLKDLASRAPSRL-----------SGGQQQRVTLARSIIVEPAI 164
Cdd:cd03244    86 -DPVLFSGTIRSnldpfgeYSDEEL----WQALERVGLKEFVESLPGGLdtvveeggenlSVGQRQLLCLARALLRKSKI 160

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1131020733 165 LLLDEPLSNLDALLREQMRieiKKIQRKL-GITAIYVTHdRVEAMSLSDRIIVMKDGKIMQIGTP 228
Cdd:cd03244   161 LVLDEATASVDPETDALIQ---KTIREAFkDCTVLTIAH-RLDTIIDSDRILVLDKGRVVEFDSP 221
Uup COG0488
ATPase components of ABC transporters with duplicated ATPase domains [General function ...
 10-204 6.51e-23

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


Pssm-ID: 440254 [Multi-domain]  Cd Length: 520  Bit Score: 99.75  E-value: 6.51e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131020733  10 LENVTKIFKDKknnteVIaVNNSTFEIKPGELITLLGPSGCGKTTTLRMVAGFELPTKGKIYI-GNEDVTFLPpnkrdta 88
Cdd:COG0488     1 LENLSKSFGGR-----PL-LDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEVSIpKGLRIGYLP------- 67

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131020733  89 tvfQSYGLFPHMTVFDNVAYGLK-LRKLSRE-------------------------------EIEKRVFEALEMVGLKDL 136
Cdd:COG0488    68 ---QEPPLDDDLTVLDTVLDGDAeLRALEAEleeleaklaepdedlerlaelqeefealggwEAEARAEEILSGLGFPEE 144

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1131020733 137 ASRAP-SRLSGGQQQRVTLARSIIVEPAILLLDEPLSNLDA----LLREQMrieikkiqRKLGITAIYVTHDR 204
Cdd:COG0488   145 DLDRPvSELSGGWRRRVALARALLSEPDLLLLDEPTNHLDLesieWLEEFL--------KNYPGTVLVVSHDR 209
phnK PRK11701
phosphonate C-P lyase system protein PhnK; Provisional
 8-235 8.10e-23

phosphonate C-P lyase system protein PhnK; Provisional


Pssm-ID: 183280 [Multi-domain]  Cd Length: 258  Bit Score: 95.76  E-value: 8.10e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131020733   8 LRLENVTKIFKDKKNNTEViavnnsTFEIKPGELITLLGPSGCGKTTTLRMVAGFELPTKGKI-YIGNE----DVTFLPP 82
Cdd:PRK11701    7 LSVRGLTKLYGPRKGCRDV------SFDLYPGEVLGIVGESGSGKTTLLNALSARLAPDAGEVhYRMRDgqlrDLYALSE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131020733  83 NKR------DTATVFQS--YGLFPHMTVFDNVA----------YGlKLRK-----LSREEIEkrvfealemvglkdlASR 139
Cdd:PRK11701   81 AERrrllrtEWGFVHQHprDGLRMQVSAGGNIGerlmavgarhYG-DIRAtagdwLERVEID---------------AAR 144

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131020733 140 ---APSRLSGGQQQRVTLARSIIVEPAILLLDEPLSNLDA--------LLREqmrieikkIQRKLGITAIYVTHDRVEAM 208
Cdd:PRK11701  145 iddLPTTFSGGMQQRLQIARNLVTHPRLVFMDEPTGGLDVsvqarlldLLRG--------LVRELGLAVVIVTHDLAVAR 216

                         250       260
                  ....*....|....*....|....*..
gi 1131020733 209 SLSDRIIVMKDGKIMQIGTPVEIYEDP 235
Cdd:PRK11701  217 LLAHRLLVMKQGRVVESGLTDQVLDDP 243
PRK13538 PRK13538
cytochrome c biogenesis heme-transporting ATPase CcmA;
33-176 8.64e-23

cytochrome c biogenesis heme-transporting ATPase CcmA;


Pssm-ID: 184125 [Multi-domain]  Cd Length: 204  Bit Score: 94.49  E-value: 8.64e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131020733  33 TFEIKPGELITLLGPSGCGKTTTLRMVAGFELPTKGKIYIGNEDVtflppnKRDTATVFQS--Y-----GLFPHMTVFDN 105
Cdd:PRK13538   21 SFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVLWQGEPI------RRQRDEYHQDllYlghqpGIKTELTALEN 94

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1131020733 106 VAYGLKLRKLSREEiekRVFEALEMVGLK---DLASRapsRLSGGQQQRVTLARSIIVEPAILLLDEPLSNLDA 176
Cdd:PRK13538   95 LRFYQRLHGPGDDE---ALWEALAQVGLAgfeDVPVR---QLSAGQQRRVALARLWLTRAPLWILDEPFTAIDK 162
Uup COG0488
ATPase components of ABC transporters with duplicated ATPase domains [General function ...
 4-222 1.02e-22

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


Pssm-ID: 440254 [Multi-domain]  Cd Length: 520  Bit Score: 98.98  E-value: 1.02e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131020733   4 KQVsLRLENVTKIFKDKknnteVIaVNNSTFEIKPGELITLLGPSGCGKTTTLRMVAGFELPTKGKIYIGnedvtflppn 83
Cdd:COG0488   313 KKV-LELEGLSKSYGDK-----TL-LDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPDSGTVKLG---------- 375

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131020733  84 krdtATVFQSY------GLFPHMTVFDNVAYG------LKLRKL------SREEIEKRVfealemvglkdlasrapSRLS 145
Cdd:COG0488   376 ----ETVKIGYfdqhqeELDPDKTVLDELRDGapggteQEVRGYlgrflfSGDDAFKPV-----------------GVLS 434

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131020733 146 GGQQQRVTLARSIIVEPAILLLDEPLSNLD-----ALlrEQMRIEIKkiqrklGiTAIYVTHDR--VEAmsLSDRIIVMK 218
Cdd:COG0488   435 GGEKARLALAKLLLSPPNVLLLDEPTNHLDietleAL--EEALDDFP------G-TVLLVSHDRyfLDR--VATRILEFE 503


                  ....
gi 1131020733 219 DGKI 222
Cdd:COG0488   504 DGGV 507
PRK10575 PRK10575
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
38-242 1.72e-22

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


Pssm-ID: 182561 [Multi-domain]  Cd Length: 265  Bit Score: 95.24  E-value: 1.72e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131020733  38 PGELITLLGPSGCGKTTTLRMVAGFELPTKGKIYIGNEDVTFLPPN--KRDTATVFQSYGLFPHMTVFDNVAYGL----- 110
Cdd:PRK10575   36 AGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPLESWSSKafARKVAYLPQQLPAAEGMTVRELVAIGRypwhg 115

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131020733 111 KLRKLSREEIEKrVFEALEMVGLKDLASRAPSRLSGGQQQRVTLARSIIVEPAILLLDEPLSNLDALLREQMRIEIKKIQ 190
Cdd:PRK10575  116 ALGRFGAADREK-VEEAISLVGLKPLAHRLVDSLSGGERQRAWIAMLVAQDSRCLLLDEPTSALDIAHQVDVLALVHRLS 194

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1131020733 191 RKLGITAIYVTHDRVEAMSLSDRIIVMKDGKIMQIGTPVEIYEDPISKFVAG 242
Cdd:PRK10575  195 QERGLTVIAVLHDINMAARYCDYLVALRGGEMIAQGTPAELMRGETLEQIYG 246
ABCC_TAP cd03248
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ...
 8-222 1.75e-22

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: 94.46  E-value: 1.75e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131020733   8 LRLENVTKIFKdkkNNTEVIAVNNSTFEIKPGELITLLGPSGCGKTTTLRMVAGFELPTKGKIYIGNEDVTfLPPNK--- 84
Cdd:cd03248    12 VKFQNVTFAYP---TRPDTLVLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDGKPIS-QYEHKylh 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131020733  85 RDTATVFQSYGLFPHmTVFDNVAYGLKLRKLsreeieKRVFEALEMVGLKDLASRAP-----------SRLSGGQQQRVT 153
Cdd:cd03248    88 SKVSLVGQEPVLFAR-SLQDNIAYGLQSCSF------ECVKEAAQKAHAHSFISELAsgydtevgekgSQLSGGQKQRVA 160

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1131020733 154 LARSIIVEPAILLLDEPLSNLDALLREQMRIEIKKIQRKLgiTAIYVTHdRVEAMSLSDRIIVMKDGKI 222
Cdd:cd03248   161 IARALIRNPQVLILDEATSALDAESEQQVQQALYDWPERR--TVLVIAH-RLSTVERADQILVLDGGRI 226
MglA COG1129
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
28-222 3.09e-22

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


Pssm-ID: 440745 [Multi-domain]  Cd Length: 497  Bit Score: 97.40  E-value: 3.09e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131020733  28 AVNNSTFEIKPGELITLLGPSGCGKTTTLRMVAGFELPTKGKIYIGNEDVT-------------FLPPNKRdtatvfqSY 94
Cdd:COG1129   267 VVRDVSFSVRAGEILGIAGLVGAGRTELARALFGADPADSGEIRLDGKPVRirsprdairagiaYVPEDRK-------GE 339

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131020733  95 GLFPHMTVFDNVAYGLkLRKLSR-----EEIEKRVFEALemvgLKDLASRAPSR------LSGGQQQRVTLARSIIVEPA 163
Cdd:COG1129   340 GLVLDLSIRENITLAS-LDRLSRgglldRRRERALAEEY----IKRLRIKTPSPeqpvgnLSGGNQQKVVLAKWLATDPK 414

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1131020733 164 ILLLDEPLSNLD--AllreqmRIEIKKIQRKL---GITAIYVTHDRVEAMSLSDRIIVMKDGKI 222
Cdd:COG1129   415 VLILDEPTRGIDvgA------KAEIYRLIRELaaeGKAVIVISSELPELLGLSDRILVMREGRI 472
PRK03695 PRK03695
vitamin B12-transporter ATPase; Provisional
 33-231 3.35e-22

vitamin B12-transporter ATPase; Provisional


Pssm-ID: 235150 [Multi-domain]  Cd Length: 248  Bit Score: 93.84  E-value: 3.35e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131020733  33 TFEIKPGELITLLGPSGCGKTTTLRMVAGFeLPTKGKIYIGNEDVTFLPPNK--RDTATVFQSYGLFPHMTVFDNVAygL 110
Cdd:PRK03695   16 SAEVRAGEILHLVGPNGAGKSTLLARMAGL-LPGSGSIQFAGQPLEAWSAAElaRHRAYLSQQQTPPFAMPVFQYLT--L 92

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131020733 111 KLRKLSRE-EIEKRVFEALEMVGLKDLASRAPSRLSGGQQQRVTLARSII-VEPAI------LLLDEPLSNLD------- 175
Cdd:PRK03695   93 HQPDKTRTeAVASALNEVAEALGLDDKLGRSVNQLSGGEWQRVRLAAVVLqVWPDInpagqlLLLDEPMNSLDvaqqaal 172

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1131020733 176 -ALLREQMRieikkiqrkLGITAIYVTHDRVEAMSLSDRIIVMKDGKIMQIGTPVEI 231
Cdd:PRK03695  173 dRLLSELCQ---------QGIAVVMSSHDLNHTLRHADRVWLLKQGKLLASGRRDEV 220
livF PRK11614
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
25-223 6.66e-22

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


Pssm-ID: 183231 [Multi-domain]  Cd Length: 237  Bit Score: 93.02  E-value: 6.66e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131020733  25 EVIAVNNSTFEIKPGELITLLGPSGCGKTTTLRMVAGFELPTKGKIYIGNEDVTFLPPNK---RDTATVFQSYGLFPHMT 101
Cdd:PRK11614   17 KIQALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDGKDITDWQTAKimrEAVAIVPEGRRVFSRMT 96

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131020733 102 VFDNVAYG--LKLRKLSREEIEkRVFEALEMvgLKDLASRAPSRLSGGQQQRVTLARSIIVEPAILLLDEPLSNLDALLR 179
Cdd:PRK11614   97 VEENLAMGgfFAERDQFQERIK-WVYELFPR--LHERRIQRAGTMSGGEQQMLAIGRALMSQPRLLLLDEPSLGLAPIII 173

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 1131020733 180 EQMRIEIKKIqRKLGITAIYVTHDRVEAMSLSDRIIVMKDGKIM 223
Cdd:PRK11614  174 QQIFDTIEQL-REQGMTIFLVEQNANQALKLADRGYVLENGHVV 216
rim_protein TIGR01257
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ...
 10-229 1.72e-21

retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim protein) in eukaryotes. It is the member of ABC transporter superfamily. Rim protein is a membrane glycoprotein which is localized in the photoreceptor outer segment discs. Mutation/s in its genetic loci is implicated in the recessive Stargardt's disease. [Transport and binding proteins, Other]


Pssm-ID: 130324 [Multi-domain]  Cd Length: 2272  Bit Score: 96.24  E-value: 1.72e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131020733   10 LENVTKIFkDKKNNTEVIAVNNSTFEikpGELITLLGPSGCGKTTTLRMVAGFELPTKGKIYIGNEDV-TFLPPNKRDTA 88
Cdd:TIGR01257  931 VKNLVKIF-EPSGRPAVDRLNITFYE---NQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGKDIeTNLDAVRQSLG 1006

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131020733   89 TVFQSYGLFPHMTVFDNVAYGLKLRKLSREEIEKRVFEALEMVGLKDLASRAPSRLSGGQQQRVTLARSIIVEPAILLLD 168
Cdd:TIGR01257 1007 MCPQHNILFHHLTVAEHILFYAQLKGRSWEEAQLEMEAMLEDTGLHHKRNEEAQDLSGGMQRKLSVAIAFVGDAKVVVLD 1086

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1131020733  169 EPLSNLDALLREQMRIEIKKIQRklGITAIYVTHDRVEAMSLSDRIIVMKDGKIMQIGTPV 229
Cdd:TIGR01257 1087 EPTSGVDPYSRRSIWDLLLKYRS--GRTIIMSTHHMDEADLLGDRIAIISQGRLYCSGTPL 1145
rim_protein TIGR01257
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ...
 8-244 3.04e-21

retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim protein) in eukaryotes. It is the member of ABC transporter superfamily. Rim protein is a membrane glycoprotein which is localized in the photoreceptor outer segment discs. Mutation/s in its genetic loci is implicated in the recessive Stargardt's disease. [Transport and binding proteins, Other]


Pssm-ID: 130324 [Multi-domain]  Cd Length: 2272  Bit Score: 95.47  E-value: 3.04e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131020733    8 LRLENVTKIFkdkkNNTEVIAVNNSTFEIKPGELITLLGPSGCGKTTTLRMVAGFELPTKGKIYIGNEDVTflppnkRDT 87
Cdd:TIGR01257 1938 LRLNELTKVY----SGTSSPAVDRLCVGVRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAGKSIL------TNI 2007

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131020733   88 ATVFQSYGLFPHMTVFDNVAYG-------LKLRKLSREEIEKRVFEALEMVGLKDLASRAPSRLSGGQQQRVTLARSIIV 160
Cdd:TIGR01257 2008 SDVHQNMGYCPQFDAIDDLLTGrehlylyARLRGVPAEEIEKVANWSIQSLGLSLYADRLAGTYSGGNKRKLSTAIALIG 2087

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131020733  161 EPAILLLDEPLSNLDALLREQMRIEIKKIQRKlGITAIYVTHDRVEAMSLSDRIIVMKDGKIMQIGTPVEIYedpiSKFV 240
Cdd:TIGR01257 2088 CPPLVLLDEPTTGMDPQARRMLWNTIVSIIRE-GRAVVLTSHSMEECEALCTRLAIMVKGAFQCLGTIQHLK----SKFG 2162


                   ....
gi 1131020733  241 AGFI 244
Cdd:TIGR01257 2163 DGYI 2166
ATM1 COG5265
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ...
 34-227 3.87e-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: 94.50  E-value: 3.87e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131020733  34 FEIKPGELITLLGPSGCGKTTTLRMVAGFELPTKGKIYIGNEDVTFLPPN--KRDTATVFQSYGLFpHMTVFDNVAYGlk 111
Cdd:COG5265   379 FEVPAGKTVAIVGPSGAGKSTLARLLFRFYDVTSGRILIDGQDIRDVTQAslRAAIGIVPQDTVLF-NDTIAYNIAYG-- 455

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131020733 112 lR-KLSREEIEkrvfEALEMVGLKDLASRAPS-----------RLSGGQQQRVTLARSIIVEPAILLLDEPLSNLDallr 179
Cdd:COG5265   456 -RpDASEEEVE----AAARAAQIHDFIESLPDgydtrvgerglKLSGGEKQRVAIARTLLKNPPILIFDEATSALD---- 526

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1131020733 180 eqMRIEiKKIQRKL-----GITAIYVTHdR----VEAmslsDRIIVMKDGKIMQIGT 227
Cdd:COG5265   527 --SRTE-RAIQAALrevarGRTTLVIAH-RlstiVDA----DEILVLEAGRIVERGT 575
NupO COG3845
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ...
 8-223 4.05e-21

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


Pssm-ID: 443055 [Multi-domain]  Cd Length: 504  Bit Score: 94.32  E-value: 4.05e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131020733   8 LRLENVTKifkdkKNNTEVIAVNNSTFEIKPGELITLLGPSGCGKTTTLRMVAGFELPTKGKIYIGNEDVTFLPPNKRDT 87
Cdd:COG3845   258 LEVENLSV-----RDDRGVPALKDVSLEVRAGEILGIAGVAGNGQSELAEALAGLRPPASGSIRLDGEDITGLSPRERRR 332

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131020733  88 ATVF------QSYGLFPHMTVFDNVAyglkLRKLSREEIEKRVF--------EALEMVglKDLASRAPS------RLSGG 147
Cdd:COG3845   333 LGVAyipedrLGRGLVPDMSVAENLI----LGRYRRPPFSRGGFldrkairaFAEELI--EEFDVRTPGpdtparSLSGG 406

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1131020733 148 QQQRVTLARSIIVEPAILLLDEPLSNLDALLREQMRIEIKKiQRKLGITAIYVTHDRVEAMSLSDRIIVMKDGKIM 223
Cdd:COG3845   407 NQQKVILARELSRDPKLLIAAQPTRGLDVGAIEFIHQRLLE-LRDAGAAVLLISEDLDEILALSDRIAVMYEGRIV 481
PRK15439 PRK15439
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
 34-222 1.00e-20

autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional


Pssm-ID: 185336 [Multi-domain]  Cd Length: 510  Bit Score: 93.19  E-value: 1.00e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131020733  34 FEIKPGELITLLGPSGCGKTTTLRMVAGFELPTKGKIYIGNEDVTFLPPNKRDTATVF---QSYGLFPHMTVFDNVAYGL 110
Cdd:PRK15439   32 FTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIGGNPCARLTPAKAHQLGIYlvpQEPLLFPNLSVKENILFGL 111

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131020733 111 KlrklSREEIEKRVFEALEMVGLK-DLASRAPSrLSGGQQQRVTLARSIIVEPAILLLDEPLSNLDALLREQMRIEIKKI 189
Cdd:PRK15439  112 P----KRQASMQKMKQLLAALGCQlDLDSSAGS-LEVADRQIVEILRGLMRDSRILILDEPTASLTPAETERLFSRIREL 186

                         170       180       190
                  ....*....|....*....|....*....|...
gi 1131020733 190 QRKlGITAIYVTHDRVEAMSLSDRIIVMKDGKI 222
Cdd:PRK15439  187 LAQ-GVGIVFISHKLPEIRQLADRISVMRDGTI 218
nikD PRK10418
nickel transporter ATP-binding protein NikD; Provisional
 8-235 4.00e-20

nickel transporter ATP-binding protein NikD; Provisional


Pssm-ID: 236688 [Multi-domain]  Cd Length: 254  Bit Score: 88.60  E-value: 4.00e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131020733   8 LRLENVTKifkdkknNTEVIAVNNSTFEIKPGELITLLGPSGCGKTTTLRMVAGFeLP-----TKGKIYIGNEDVTFLPP 82
Cdd:PRK10418    5 IELRNIAL-------QAAQPLVHGVSLTLQRGRVLALVGGSGSGKSLTCAAALGI-LPagvrqTAGRVLLDGKPVAPCAL 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131020733  83 NKRDTATVFQSyglfPHmTVFDNV----AYGLK-LRKLSREEIEKRVFEALEMVGLKD---LASRAPSRLSGGQQQRVTL 154
Cdd:PRK10418   77 RGRKIATIMQN----PR-SAFNPLhtmhTHAREtCLALGKPADDATLTAALEAVGLENaarVLKLYPFEMSGGMLQRMMI 151

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131020733 155 ARSIIVEPAILLLDEPLSNLDALLreQMRI--EIKKIQRKLGITAIYVTHDRVEAMSLSDRIIVMKDGKIMQIGTPVEIY 232
Cdd:PRK10418  152 ALALLCEAPFIIADEPTTDLDVVA--QARIldLLESIVQKRALGMLLVTHDMGVVARLADDVAVMSHGRIVEQGDVETLF 229


                  ...
gi 1131020733 233 EDP 235
Cdd:PRK10418  230 NAP 232
oppD PRK09473
oligopeptide transporter ATP-binding component; Provisional
 26-247 4.06e-20

oligopeptide transporter ATP-binding component; Provisional


Pssm-ID: 181888 [Multi-domain]  Cd Length: 330  Bit Score: 89.78  E-value: 4.06e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131020733  26 VIAVNNSTFEIKPGELITLLGPSGCGKTTTLRMVAGFeLPTKGKI-----YIGNEDVTfLPPNK------RDTATVFQS- 93
Cdd:PRK09473   29 VTAVNDLNFSLRAGETLGIVGESGSGKSQTAFALMGL-LAANGRIggsatFNGREILN-LPEKElnklraEQISMIFQDp 106

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131020733  94 -YGLFPHMTVFDNVAYGLKLRK-LSREE-IEK--RVFEALEMVGLKDLASRAPSRLSGGQQQRVTLARSIIVEPAILLLD 168
Cdd:PRK09473  107 mTSLNPYMRVGEQLMEVLMLHKgMSKAEaFEEsvRMLDAVKMPEARKRMKMYPHEFSGGMRQRVMIAMALLCRPKLLIAD 186

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1131020733 169 EPLSNLDALLREQMRIEIKKIQRKLGITAIYVTHDRVEAMSLSDRIIVMKDGKIMQIGTPVEIYEDPISKFVAGFIGKV 247
Cdd:PRK09473  187 EPTTALDVTVQAQIMTLLNELKREFNTAIIMITHDLGVVAGICDKVLVMYAGRTMEYGNARDVFYQPSHPYSIGLLNAV 265
PRK13549 PRK13549
xylose transporter ATP-binding subunit; Provisional
 8-227 6.96e-20

xylose transporter ATP-binding subunit; Provisional


Pssm-ID: 184134 [Multi-domain]  Cd Length: 506  Bit Score: 90.76  E-value: 6.96e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131020733   8 LRLENVTKIFKDkknnteVIAVNNSTFEIKPGELITLLGPSGCGKTTTLRMVAG------FElptkGKIYIGNEDVTFlp 81
Cdd:PRK13549    6 LEMKNITKTFGG------VKALDNVSLKVRAGEIVSLCGENGAGKSTLMKVLSGvyphgtYE----GEIIFEGEELQA-- 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131020733  82 PNKRDT-----ATVFQSYGLFPHMTVFDNVAYGLKLRKLSR---EEIEKRVFEALEMVGLK-DLASRApSRLSGGQQQRV 152
Cdd:PRK13549   74 SNIRDTeragiAIIHQELALVKELSVLENIFLGNEITPGGImdyDAMYLRAQKLLAQLKLDiNPATPV-GNLGLGQQQLV 152

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1131020733 153 TLARSIIVEPAILLLDEPLSNLDALLREQMRIEIKKIQRKlGITAIYVTHDRVEAMSLSDRIIVMKDGKimQIGT 227
Cdd:PRK13549  153 EIAKALNKQARLLILDEPTASLTESETAVLLDIIRDLKAH-GIACIYISHKLNEVKAISDTICVIRDGR--HIGT 224
znuC PRK09544
high-affinity zinc transporter ATPase; Reviewed
 8-239 1.35e-19

high-affinity zinc transporter ATPase; Reviewed


Pssm-ID: 181939 [Multi-domain]  Cd Length: 251  Bit Score: 86.71  E-value: 1.35e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131020733   8 LRLENVTKIFKDKKnnteviAVNNSTFEIKPGELITLLGPSGCGKTTTLRMVAGFELPTKGKIyignedvtfLPPNKRDT 87
Cdd:PRK09544    5 VSLENVSVSFGQRR------VLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVI---------KRNGKLRI 69

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131020733  88 ATVFQSYGLFPHMTVfdNVAYGLKLRKLSREeieKRVFEALEMVGLKDLASRAPSRLSGGQQQRVTLARSIIVEPAILLL 167
Cdd:PRK09544   70 GYVPQKLYLDTTLPL--TVNRFLRLRPGTKK---EDILPALKRVQAGHLIDAPMQKLSGGETQRVLLARALLNRPQLLVL 144

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1131020733 168 DEPLSNLDALLREQMRIEIKKIQRKLGITAIYVTHDRVEAMSLSDRIIVMkDGKIMQIGTP--VEIYEDPISKF 239
Cdd:PRK09544  145 DEPTQGVDVNGQVALYDLIDQLRRELDCAVLMVSHDLHLVMAKTDEVLCL-NHHICCSGTPevVSLHPEFISMF 217
ABCF_EF-3 cd03221
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ...
 8-221 1.95e-19

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: 83.65  E-value: 1.95e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131020733   8 LRLENVTKIFKDKKnnteviAVNNSTFEIKPGELITLLGPSGCGKTTTLRMVAGFELPTKGKIYIGnedvtflppnkrDT 87
Cdd:cd03221     1 IELENLSKTYGGKL------LLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIVTWG------------ST 62

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131020733  88 ATVfqsyGLFPHmtvfdnvayglklrklsreeiekrvfealemvglkdlasrapsrLSGGQQQRVTLARSIIVEPAILLL 167
Cdd:cd03221    63 VKI----GYFEQ--------------------------------------------LSGGEKMRLALAKLLLENPNLLLL 94

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1131020733 168 DEPLSNLDALLREQMRIEIKKIQRklgiTAIYVTHDRVEAMSLSDRIIVMKDGK 221
Cdd:cd03221    95 DEPTNHLDLESIEALEEALKEYPG----TVILVSHDRYFLDQVATKIIELEDGK 144
SufC COG0396
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, ...
 34-228 2.20e-19

Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 440165 [Multi-domain]  Cd Length: 245  Bit Score: 86.27  E-value: 2.20e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131020733  34 FEIKPGELITLLGPSGCGKTTTLRMVAGFEL--PTKGKIYIGNEDVTFLPPNKRDTAtvfqsyGLF---------PHMTV 102
Cdd:COG0396    21 LTIKPGEVHAIMGPNGSGKSTLAKVLMGHPKyeVTSGSILLDGEDILELSPDERARA------GIFlafqypveiPGVSV 94

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131020733 103 FD--NVAYGLKLRK-LSREEIEKRVFEALEMVGL-KDLASRA-PSRLSGGQQQRVTLARSIIVEPAILLLDEPLSNLD-- 175
Cdd:COG0396    95 SNflRTALNARRGEeLSAREFLKLLKEKMKELGLdEDFLDRYvNEGFSGGEKKRNEILQMLLLEPKLAILDETDSGLDid 174

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131020733 176 ALlreqmRIEIKKIQ--RKLGITAIYVTH-----DRVEAmslsDRIIVMKDGKIMQIGTP 228
Cdd:COG0396   175 AL-----RIVAEGVNklRSPDRGILIITHyqrilDYIKP----DFVHVLVDGRIVKSGGK 225
PRK11176 PRK11176
lipid A ABC transporter ATP-binding protein/permease MsbA;
8-233 3.04e-19

lipid A ABC transporter ATP-binding protein/permease MsbA;


Pssm-ID: 183016 [Multi-domain]  Cd Length: 582  Bit Score: 88.92  E-value: 3.04e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131020733   8 LRLENVTKIFKDKknntEVIAVNNSTFEIKPGELITLLGPSGCGKTTTLRMVAGFELPTKGKIYIGNEDVT-FLPPNKRD 86
Cdd:PRK11176  342 IEFRNVTFTYPGK----EVPALRNINFKIPAGKTVALVGRSGSGKSTIANLLTRFYDIDEGEILLDGHDLRdYTLASLRN 417

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131020733  87 -TATVFQSYGLFpHMTVFDNVAYGLKlRKLSREEIEK--RVFEALEMV-----GLKDLASRAPSRLSGGQQQRVTLARSI 158
Cdd:PRK11176  418 qVALVSQNVHLF-NDTIANNIAYART-EQYSREQIEEaaRMAYAMDFInkmdnGLDTVIGENGVLLSGGQRQRIAIARAL 495

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131020733 159 IVEPAILLLDEPLSNLDAllrEQMRIeikkIQRKLGI-----TAIYVTHdRVEAMSLSDRIIVMKDGKIMQIGTPVEIYE 233
Cdd:PRK11176  496 LRDSPILILDEATSALDT---ESERA----IQAALDElqknrTSLVIAH-RLSTIEKADEILVVEDGEIVERGTHAELLA 567
PRK15134 PRK15134
microcin C ABC transporter ATP-binding protein YejF; Provisional
 8-221 4.78e-19

microcin C ABC transporter ATP-binding protein YejF; Provisional


Pssm-ID: 237917 [Multi-domain]  Cd Length: 529  Bit Score: 88.22  E-value: 4.78e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131020733   8 LRLENVTKIFKDKKNNTEViaVNNSTFEIKPGELITLLGPSGCGKTTT----LRMvagfeLPTKGKIYIGNeDVTF---- 79
Cdd:PRK15134    6 LAIENLSVAFRQQQTVRTV--VNDVSLQIEAGETLALVGESGSGKSVTalsiLRL-----LPSPPVVYPSG-DIRFhges 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131020733  80 -----------LPPNKrdTATVFQS--YGLFPHMTVFDNVAYGLKL-RKLSREEIEKRVFEALEMVGLKDLASRA---PS 142
Cdd:PRK15134   78 llhaseqtlrgVRGNK--IAMIFQEpmVSLNPLHTLEKQLYEVLSLhRGMRREAARGEILNCLDRVGIRQAAKRLtdyPH 155

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1131020733 143 RLSGGQQQRVTLARSIIVEPAILLLDEPLSNLDALLREQMRIEIKKIQRKLGITAIYVTHDRVEAMSLSDRIIVMKDGK 221
Cdd:PRK15134  156 QLSGGERQRVMIAMALLTRPELLIADEPTTALDVSVQAQILQLLRELQQELNMGLLFITHNLSIVRKLADRVAVMQNGR 234
PRK09700 PRK09700
D-allose ABC transporter ATP-binding protein AlsA;
8-242 8.09e-19

D-allose ABC transporter ATP-binding protein AlsA;


Pssm-ID: 182036 [Multi-domain]  Cd Length: 510  Bit Score: 87.53  E-value: 8.09e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131020733   8 LRLENVTKIFkdkknnTEVIAVNNSTFEIKPGELITLLGPSGCGKTTTLRMVAGFELPTKGKIYIGNEDVTFLPPN---K 84
Cdd:PRK09700    6 ISMAGIGKSF------GPVHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNINYNKLDHKlaaQ 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131020733  85 RDTATVFQSYGLFPHMTVFDNVAYG-LKLRK------LSREEIEKRVFEALEMVGLKDLASRAPSRLSGGQQQRVTLARS 157
Cdd:PRK09700   80 LGIGIIYQELSVIDELTVLENLYIGrHLTKKvcgvniIDWREMRVRAAMMLLRVGLKVDLDEKVANLSISHKQMLEIAKT 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131020733 158 IIVEPAILLLDEPLSNLDALLREQMRIEIKKIqRKLGITAIYVTHDRVEAMSLSDRIIVMKDGKIMQIGTPVEIYEDPIS 237
Cdd:PRK09700  160 LMLDAKVIIMDEPTSSLTNKEVDYLFLIMNQL-RKEGTAIVYISHKLAEIRRICDRYTVMKDGSSVCSGMVSDVSNDDIV 238


                  ....*
gi 1131020733 238 KFVAG 242
Cdd:PRK09700  239 RLMVG 243
ABCC_NFT1 cd03369
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ...
 28-228 1.15e-18

ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type transporter 1). NFT1 belongs to the MRP (multidrug resistance-associated protein) family of ABC transporters. Some of the MRP members have five additional transmembrane segments in their N-terminus, but the function of these additional membrane-spanning domains is not clear. The MRP was found in the multidrug-resisting lung cancer cell in which p-glycoprotein was not overexpressed. MRP exports glutathione by drug stimulation, as well as, certain substrates in conjugated forms with anions such as glutathione, glucuronate, and sulfate.


Pssm-ID: 213269 [Multi-domain]  Cd Length: 207  Bit Score: 83.23  E-value: 1.15e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131020733  28 AVNNSTFEIKPGELITLLGPSGCGKTTTLRMVAGFELPTKGKIYIGNEDVTFLPPNK--RDTATVFQSYGLFPHmTVFDN 105
Cdd:cd03369    23 VLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDGIDISTIPLEDlrSSLTIIPQDPTLFSG-TIRSN 101

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131020733 106 V-AYGlklrklsrEEIEKRVFEALEMvglkdlaSRAPSRLSGGQQQRVTLARSIIVEPAILLLDEPLSNL----DALLRE 180
Cdd:cd03369   102 LdPFD--------EYSDEEIYGALRV-------SEGGLNLSQGQRQLLCLARALLKRPRVLVLDEATASIdyatDALIQK 166

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 1131020733 181 QMRIEIKkiqrklGITAIYVTHdRVEAMSLSDRIIVMKDGKIMQIGTP 228
Cdd:cd03369   167 TIREEFT------NSTILTIAH-RLRTIIDYDKILVMDAGEVKEYDHP 207
xylG TIGR02633
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ...
 8-227 1.78e-18

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: 86.42  E-value: 1.78e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131020733   8 LRLENVTKIFKDkknnteVIAVNNSTFEIKPGELITLLGPSGCGKTTTLRMVAGFeLPT---KGKIYIGNEDVTflPPNK 84
Cdd:TIGR02633   2 LEMKGIVKTFGG------VKALDGIDLEVRPGECVGLCGENGAGKSTLMKILSGV-YPHgtwDGEIYWSGSPLK--ASNI 72

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131020733  85 RDT-----ATVFQSYGLFPHMTVFDNVAYG----LKLRKLSREEIEKRVFEALEMVGLKDL-ASRAPSRLSGGQQQRVTL 154
Cdd:TIGR02633  73 RDTeragiVIIHQELTLVPELSVAENIFLGneitLPGGRMAYNAMYLRAKNLLRELQLDADnVTRPVGDYGGGQQQLVEI 152

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1131020733 155 ARSIIVEPAILLLDEPLSNLDALLREQMRIEIKKIQRKlGITAIYVTHDRVEAMSLSDRIIVMKDGKimQIGT 227
Cdd:TIGR02633 153 AKALNKQARLLILDEPSSSLTEKETEILLDIIRDLKAH-GVACVYISHKLNEVKAVCDTICVIRDGQ--HVAT 222
ABC_CcmA_heme_exporter cd03231
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ...
 34-183 1.80e-18

Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the bacterial CcmAB transporter. The CCM family is involved in bacterial cytochrome c biogenesis. Cytochrome c maturation in E. coli requires the ccm operon, which encodes eight membrane proteins (CcmABCDEFGH). CcmE is a periplasmic heme chaperon that binds heme covalently and transfers it onto apocytochrome c in the presence of CcmF, CcmG, and CcmH. The CcmAB proteins represent an ABC transporter and the CcmCD proteins participate in heme transfer to CcmE.


Pssm-ID: 213198 [Multi-domain]  Cd Length: 201  Bit Score: 82.54  E-value: 1.80e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131020733  34 FEIKPGELITLLGPSGCGKTTTLRMVAGFELPTKGKIYIGNEDVTFLPPN-KRDTATVFQSYGLFPHMTVFDNvayglkL 112
Cdd:cd03231    21 FTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNGGPLDFQRDSiARGLLYLGHAPGIKTTLSVLEN------L 94

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1131020733 113 RKLSREEIEKRVFEALEMVGLKDLASRAPSRLSGGQQQRVTLARSIIVEPAILLLDEPLSNLD----ALLREQMR 183
Cdd:cd03231    95 RFWHADHSDEQVEEALARVGLNGFEDRPVAQLSAGQQRRVALARLLLSGRPLWILDEPTTALDkagvARFAEAMA 169
ABCD_peroxisomal_ALDP cd03223
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ...
 29-202 2.08e-18

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: 81.43  E-value: 2.08e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131020733  29 VNNSTFEIKPGELITLLGPSGCGKTTTLRMVAGFELPTKGKIYI-GNEDVTFLPPnkrdtatvfQSYglFPHMTVFDNVA 107
Cdd:cd03223    17 LKDLSFEIKPGDRLLITGPSGTGKSSLFRALAGLWPWGSGRIGMpEGEDLLFLPQ---------RPY--LPLGTLREQLI 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131020733 108 YglklrklsreeiekrvfeALEMVglkdlasrapsrLSGGQQQRVTLARSIIVEPAILLLDEPLSNLDallrEQMRIEIK 187
Cdd:cd03223    86 Y------------------PWDDV------------LSGGEQQRLAFARLLLHKPKFVFLDEATSALD----EESEDRLY 131

                         170
                  ....*....|....*
gi 1131020733 188 KIQRKLGITAIYVTH 202
Cdd:cd03223   132 QLLKELGITVISVGH 146
MK0520 COG2401
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ...
 30-219 2.36e-18

ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];


Pssm-ID: 441957 [Multi-domain]  Cd Length: 222  Bit Score: 82.70  E-value: 2.36e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131020733  30 NNSTFEIKPGELITLLGPSGCGKTTTLRMVAGFELPTKGKIYIGNEDVTFlPPNKrdtatvfqsyglfphmTVFDNVAyg 109
Cdd:COG2401    47 RDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGALKGTPVAGCVDVPDNQF-GREA----------------SLIDAIG-- 107

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131020733 110 lklrklsREEIEKRVFEALEMVGLKDLAS--RAPSRLSGGQQQRVTLARSIIVEPAILLLDEPLSNLDALLREQMRIEIK 187
Cdd:COG2401   108 -------RKGDFKDAVELLNAVGLSDAVLwlRRFKELSTGQKFRFRLALLLAERPKLLVIDEFCSHLDRQTAKRVARNLQ 180

                         170       180       190
                  ....*....|....*....|....*....|....
gi 1131020733 188 KIQRKLGITAIYVTH--DRVEAmsLSDRIIVMKD 219
Cdd:COG2401   181 KLARRAGITLVVATHhyDVIDD--LQPDLLIFVG 212
hmuV PRK13547
heme ABC transporter ATP-binding protein;
29-231 1.11e-17

heme ABC transporter ATP-binding protein;


Pssm-ID: 184132 [Multi-domain]  Cd Length: 272  Bit Score: 81.80  E-value: 1.11e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131020733  29 VNNSTFEIKPGELITLLGPSGCGKTTTLRMVAGfELP---------TKGKIYIGNEDVTFLPPNK--RDTATVFQ----- 92
Cdd:PRK13547   17 LRDLSLRIEPGRVTALLGRNGAGKSTLLKALAG-DLTgggaprgarVTGDVTLNGEPLAAIDAPRlaRLRAVLPQaaqpa 95

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131020733  93 ---------SYGLFPHMtvfdnvayglklRKLSREEIEKR--VFEALEMVGLKDLASRAPSRLSGGQQQRVTLARSI--- 158
Cdd:PRK13547   96 fafsareivLLGRYPHA------------RRAGALTHRDGeiAWQALALAGATALVGRDVTTLSGGELARVQFARVLaql 163

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1131020733 159 ------IVEPAILLLDEPLSNLDALLREQMRIEIKKIQRKLGITAIYVTHDRVEAMSLSDRIIVMKDGKIMQIGTPVEI 231
Cdd:PRK13547  164 wpphdaAQPPRYLLLDEPTAALDLAHQHRLLDTVRRLARDWNLGVLAIVHDPNLAARHADRIAMLADGAIVAHGAPADV 242
ABC_RNaseL_inhibitor_domain2 cd03237
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ...
 35-221 1.35e-17

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: 81.30  E-value: 1.35e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131020733  35 EIKPGELITLLGPSGCGKTTTLRMVAGFELPTKGKIYIGNEDVTFLPpnkrdtatvfQSYGLFPHMTVfDNVAYGLKLRK 114
Cdd:cd03237    21 SISESEVIGILGPNGIGKTTFIKMLAGVLKPDEGDIEIELDTVSYKP----------QYIKADYEGTV-RDLLSSITKDF 89

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131020733 115 LSREEIEKRVFEALEMVGLKDlasRAPSRLSGGQQQRVTLARSIIVEPAILLLDEPLSNLDAllrEQmRIEIKKIQRKLG 194
Cdd:cd03237    90 YTHPYFKTEIAKPLQIEQILD---REVPELSGGELQRVAIAACLSKDADIYLLDEPSAYLDV---EQ-RLMASKVIRRFA 162

                         170       180       190
                  ....*....|....*....|....*....|.
gi 1131020733 195 I----TAIYVTHDRVEAMSLSDRIIVMkDGK 221
Cdd:cd03237   163 EnnekTAFVVEHDIIMIDYLADRLIVF-EGE 192
ABCG_PDR_domain1 cd03233
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ...
 12-222 1.51e-17

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: 80.00  E-value: 1.51e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131020733  12 NVTKIFKDKKNNTEVIavNNSTFEIKPGELITLLGPSGCGKTTTLRMVAGfELPTKGKI-----YIGNEDVTFLPPNKRD 86
Cdd:cd03233     8 NISFTTGKGRSKIPIL--KDFSGVVKPGEMVLVLGRPGSGCSTLLKALAN-RTEGNVSVegdihYNGIPYKEFAEKYPGE 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131020733  87 TATVFQSYGLFPHMTVFDNVAYGLKLRklsreeiekrvfeALEMVglkdlasrapSRLSGGQQQRVTLARSIIVEPAILL 166
Cdd:cd03233    85 IIYVSEEDVHFPTLTVRETLDFALRCK-------------GNEFV----------RGISGGERKRVSIAEALVSRASVLC 141

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1131020733 167 LDEPLSNLDALLREQMRIEIKKIQRKLGITAIY-VTHDRVEAMSLSDRIIVMKDGKI 222
Cdd:cd03233   142 WDNSTRGLDSSTALEILKCIRTMADVLKTTTFVsLYQASDEIYDLFDKVLVLYEGRQ 198
ABC_FeS_Assembly cd03217
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ...
 8-234 1.61e-17

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: 79.88  E-value: 1.61e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131020733   8 LRLENVTKIFKDKKnnteviAVNNSTFEIKPGELITLLGPSGCGKTTTLRMVAGFE--LPTKGKIYIGNEDVTFLPPNKR 85
Cdd:cd03217     1 LEIKDLHVSVGGKE------ILKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMGHPkyEVTEGEILFKGEDITDLPPEER 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131020733  86 DTATVFQSYGLFPHMTvfdnvayGLKLRKLSREeiekrVFEAlemvglkdlasrapsrLSGGQQQRVTLARSIIVEPAIL 165
Cdd:cd03217    75 ARLGIFLAFQYPPEIP-------GVKNADFLRY-----VNEG----------------FSGGEKKRNEILQLLLLEPDLA 126

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1131020733 166 LLDEPLSNLDAllrEQMRIEIKKIQ--RKLGITAIYVTH-DRVEAMSLSDRIIVMKDGKIMQIGtPVEIYED 234
Cdd:cd03217   127 ILDEPDSGLDI---DALRLVAEVINklREEGKSVLIITHyQRLLDYIKPDRVHVLYDGRIVKSG-DKELALE 194
PRK15439 PRK15439
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
 31-222 3.92e-17

autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional


Pssm-ID: 185336 [Multi-domain]  Cd Length: 510  Bit Score: 82.41  E-value: 3.92e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131020733  31 NSTFEIKPGELITLLGPSGCGKTTTLRMVAGFELPTKGKIYIGNEDVTFLPPNKR-DTATVF-----QSYGLFPHMTVFD 104
Cdd:PRK15439  281 NISLEVRAGEILGLAGVVGAGRTELAETLYGLRPARGGRIMLNGKEINALSTAQRlARGLVYlpedrQSSGLYLDAPLAW 360

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131020733 105 NVaYGLKLRKLS---REEIEKRVFE----ALemvGLKDLASRAPSR-LSGGQQQRVTLARSIIVEPAILLLDEPLSNLDA 176
Cdd:PRK15439  361 NV-CALTHNRRGfwiKPARENAVLEryrrAL---NIKFNHAEQAARtLSGGNQQKVLIAKCLEASPQLLIVDEPTRGVDV 436

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 1131020733 177 LLREQMRIEIKKIQrKLGITAIYVTHDRVEAMSLSDRIIVMKDGKI 222
Cdd:PRK15439  437 SARNDIYQLIRSIA-AQNVAVLFISSDLEEIEQMADRVLVMHQGEI 481
PRK13543 PRK13543
heme ABC exporter ATP-binding protein CcmA;
34-175 6.28e-17

heme ABC exporter ATP-binding protein CcmA;


Pssm-ID: 184129 [Multi-domain]  Cd Length: 214  Bit Score: 78.74  E-value: 6.28e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131020733  34 FEIKPGELITLLGPSGCGKTTTLRMVAGFELPTKGKIYIGNEdvtflpPNKRDTATVFQSY-----GLFPHMTVFDNVAY 108
Cdd:PRK13543   32 FHVDAGEALLVQGDNGAGKTTLLRVLAGLLHVESGQIQIDGK------TATRGDRSRFMAYlghlpGLKADLSTLENLHF 105

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1131020733 109 glkLRKLSREEIEKRVFEALEMVGLKDLASRAPSRLSGGQQQRVTLARsIIVEPAIL-LLDEPLSNLD 175
Cdd:PRK13543  106 ---LCGLHGRRAKQMPGSALAIVGLAGYEDTLVRQLSAGQKKRLALAR-LWLSPAPLwLLDEPYANLD 169
xylG TIGR02633
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ...
 4-222 1.71e-16

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: 80.64  E-value: 1.71e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131020733   4 KQVSLRLENVTKIFKDkknNTEVIAVNNSTFEIKPGELITLLGPSGCGKTTTLRMVAG-FELPTKGKIYIGNEDVTFLPP 82
Cdd:TIGR02633 254 GDVILEARNLTCWDVI---NPHRKRVDDVSFSLRRGEILGVAGLVGAGRTELVQALFGaYPGKFEGNVFINGKPVDIRNP 330

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131020733  83 NKRDTATVF------QSYGLFPHMTVFDNVAYGL-----KLRKLSREEIEKRVFEALEMVGLKDLASRAP-SRLSGGQQQ 150
Cdd:TIGR02633 331 AQAIRAGIAmvpedrKRHGIVPILGVGKNITLSVlksfcFKMRIDAAAELQIIGSAIQRLKVKTASPFLPiGRLSGGNQQ 410

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1131020733 151 RVTLARSIIVEPAILLLDEPLSNLDAllreQMRIEIKKIQRKL---GITAIYVTHDRVEAMSLSDRIIVMKDGKI 222
Cdd:TIGR02633 411 KAVLAKMLLTNPRVLILDEPTRGVDV----GAKYEIYKLINQLaqeGVAIIVVSSELAEVLGLSDRVLVIGEGKL 481
PRK10789 PRK10789
SmdA family multidrug ABC transporter permease/ATP-binding protein;
24-227 1.97e-16

SmdA family multidrug ABC transporter permease/ATP-binding protein;


Pssm-ID: 182732 [Multi-domain]  Cd Length: 569  Bit Score: 80.53  E-value: 1.97e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131020733  24 TEVIAVNNSTFEIKPGELITLLGPSGCGKTTTLRMVAGFELPTKGKIYIGNEDVTFLPPN--KRDTATVFQSYGLFPHmT 101
Cdd:PRK10789  326 TDHPALENVNFTLKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGDIRFHDIPLTKLQLDswRSRLAVVSQTPFLFSD-T 404

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131020733 102 VFDNVAYGLKlrKLSREEIEkrvfEALEMVGLKDLASRAPS-----------RLSGGQQQRVTLARSIIVEPAILLLDEP 170
Cdd:PRK10789  405 VANNIALGRP--DATQQEIE----HVARLASVHDDILRLPQgydtevgergvMLSGGQKQRISIARALLLNAEILILDDA 478

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1131020733 171 LSNLDAllREQMRIEIKKIQRKLGITAIYVTHdRVEAMSLSDRIIVMKDGKIMQIGT 227
Cdd:PRK10789  479 LSAVDG--RTEHQILHNLRQWGEGRTVIISAH-RLSALTEASEILVMQHGHIAQRGN 532
PRK09700 PRK09700
D-allose ABC transporter ATP-binding protein AlsA;
29-225 3.94e-16

D-allose ABC transporter ATP-binding protein AlsA;


Pssm-ID: 182036 [Multi-domain]  Cd Length: 510  Bit Score: 79.44  E-value: 3.94e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131020733  29 VNNSTFEIKPGELITLLGPSGCGKTTTLRMVAGFELPTKGKIYIGNEDVT-------------FLPPNKRDTatvfqsyG 95
Cdd:PRK09700  279 VRDISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEIRLNGKDISprspldavkkgmaYITESRRDN-------G 351

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131020733  96 LFPHMTVFDNVAYGLKLRK--------LSREEIEKRVFEALEmvglKDLASRAPS------RLSGGQQQRVTLARSIIVE 161
Cdd:PRK09700  352 FFPNFSIAQNMAISRSLKDggykgamgLFHEVDEQRTAENQR----ELLALKCHSvnqnitELSGGNQQKVLISKWLCCC 427

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1131020733 162 PAILLLDEPLSNLDAllreQMRIEIKKIQRKL---GITAIYVTHDRVEAMSLSDRIIVMKDGKIMQI 225
Cdd:PRK09700  428 PEVIIFDEPTRGIDV----GAKAEIYKVMRQLaddGKVILMVSSELPEIITVCDRIAVFCEGRLTQI 490
PRK10790 PRK10790
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
27-227 5.52e-16

SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;


Pssm-ID: 182733 [Multi-domain]  Cd Length: 592  Bit Score: 78.99  E-value: 5.52e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131020733  27 IAVNNSTFEIKPGEL--------------ITLLGPSGCGKTTTLRMVAGFELPTKGKIYIGNEDVTFLPPN--KRDTATV 90
Cdd:PRK10790  341 IDIDNVSFAYRDDNLvlqninlsvpsrgfVALVGHTGSGKSTLASLLMGYYPLTEGEIRLDGRPLSSLSHSvlRQGVAMV 420

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131020733  91 FQSYGLFPHmTVFDNVAYGlklrklsREEIEKRVFEALEMVGLKDLASRAP-----------SRLSGGQQQRVTLARSII 159
Cdd:PRK10790  421 QQDPVVLAD-TFLANVTLG-------RDISEEQVWQALETVQLAELARSLPdglytplgeqgNNLSVGQKQLLALARVLV 492

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1131020733 160 VEPAILLLDEPLSNLDAlLREQmrieikKIQRKLGI-----TAIYVTHdRVEAMSLSDRIIVMKDGKIMQIGT 227
Cdd:PRK10790  493 QTPQILILDEATANIDS-GTEQ------AIQQALAAvrehtTLVVIAH-RLSTIVEADTILVLHRGQAVEQGT 557
ABC_ABC_ChvD TIGR03719
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ...
 8-204 6.10e-16

ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of the ABC transporter ATP-binding cassette, but are found outside the common ABC transporter operon structure that features integral membrane permease proteins and substrate-binding proteins encoded next to the ATP-binding cassette (ABC domain) protein. The member protein ChvD from Agrobacterium tumefaciens was identified as both a candidate to interact with VirB8, based on yeast two-hybrid analysis, and as an apparent regulator of VirG. The general function of this protein family is unknown.


Pssm-ID: 274744 [Multi-domain]  Cd Length: 552  Bit Score: 78.82  E-value: 6.10e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131020733   8 LRLENVTKIFKDKknntevIAVNNSTFEIKPGELITLLGPSGCGKTTTLRMVAGFELPTKGKIYIGnEDVtflppnkrDT 87
Cdd:TIGR03719 323 IEAENLTKAFGDK------LLIDDLSFKLPPGGIVGVIGPNGAGKSTLFRMITGQEQPDSGTIEIG-ETV--------KL 387

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131020733  88 ATVFQSY-GLFPHMTVFDNVAYGLKLRKLSREEIEKRVFEALEMVGLKDLASRApSRLSGGQQQRVTLARSIIVEPAILL 166
Cdd:TIGR03719 388 AYVDQSRdALDPNKTVWEEISGGLDIIKLGKREIPSRAYVGRFNFKGSDQQKKV-GQLSGGERNRVHLAKTLKSGGNVLL 466

                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 1131020733 167 LDEPLSNLDAllrEQMRIEIKKIQRKLGiTAIYVTHDR 204
Cdd:TIGR03719 467 LDEPTNDLDV---ETLRALEEALLNFAG-CAVVISHDR 500
PLN03211 PLN03211
ABC transporter G-25; Provisional
 14-226 6.71e-16

ABC transporter G-25; Provisional


Pssm-ID: 215634 [Multi-domain]  Cd Length: 659  Bit Score: 79.15  E-value: 6.71e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131020733  14 TKIFKDKKNNTEVIAVNNSTFEIKPGELITLLGPSGCGKTTTLRMVAGFELPT--KGKIYIGNEDVTflPPNKRDTATVF 91
Cdd:PLN03211   69 PKISDETRQIQERTILNGVTGMASPGEILAVLGPSGSGKSTLLNALAGRIQGNnfTGTILANNRKPT--KQILKRTGFVT 146

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131020733  92 QSYGLFPHMTVFDNVAYGLKLR---KLSREEIEKRVFEALEMVGLKDLASRAPSR-----LSGGQQQRVTLARSIIVEPA 163
Cdd:PLN03211  147 QDDILYPHLTVRETLVFCSLLRlpkSLTKQEKILVAESVISELGLTKCENTIIGNsfirgISGGERKRVSIAHEMLINPS 226

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1131020733 164 ILLLDEPLSNLDALLREQMRIEIKKIQR--KLGITAIYVTHDRVEAMslSDRIIVMKDGKIMQIG 226
Cdd:PLN03211  227 LLILDEPTSGLDATAAYRLVLTLGSLAQkgKTIVTSMHQPSSRVYQM--FDSVLVLSEGRCLFFG 289
PRK13549 PRK13549
xylose transporter ATP-binding subunit; Provisional
 6-222 1.75e-15

xylose transporter ATP-binding subunit; Provisional


Pssm-ID: 184134 [Multi-domain]  Cd Length: 506  Bit Score: 77.28  E-value: 1.75e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131020733   6 VSLRLENVTKIfkdKKNNTEVIAVNNSTFEIKPGELITLLGPSGCGKTTTLRMVAG-FELPTKGKIYIGNEDVTFLPPN- 83
Cdd:PRK13549  258 VILEVRNLTAW---DPVNPHIKRVDDVSFSLRRGEILGIAGLVGAGRTELVQCLFGaYPGRWEGEIFIDGKPVKIRNPQq 334

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131020733  84 --KRDTATVFQS---YGLFPHMTVFDNVAyglkLRKLSREEIEKRVFEALEMV----GLKDLASRAPS------RLSGGQ 148
Cdd:PRK13549  335 aiAQGIAMVPEDrkrDGIVPVMGVGKNIT----LAALDRFTGGSRIDDAAELKtileSIQRLKVKTASpelaiaRLSGGN 410

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1131020733 149 QQRVTLARSIIVEPAILLLDEPLSNLDAllreQMRIEIKKIQRKL---GITAIYVTHDRVEAMSLSDRIIVMKDGKI 222
Cdd:PRK13549  411 QQKAVLAKCLLLNPKILILDEPTRGIDV----GAKYEIYKLINQLvqqGVAIIVISSELPEVLGLSDRVLVMHEGKL 483
MRP_assoc_pro TIGR00957
multi drug resistance-associated protein (MRP); This model describes multi drug ...
 29-227 3.48e-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: 77.29  E-value: 3.48e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131020733   29 VNNSTFEIKPGELITLLGPSGCGKTTTLRMVAGFELPTKGKIYIGNEdVTFLPPnkrdtatvfQSYglFPHMTVFDNVAY 108
Cdd:TIGR00957  654 LNGITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVHMKGS-VAYVPQ---------QAW--IQNDSLRENILF 721

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131020733  109 GLKLRklsrEEIEKRVFEA------LEMV--GLKDLASRAPSRLSGGQQQRVTLARSIIVEPAILLLDEPLSNLDALLRE 180
Cdd:TIGR00957  722 GKALN----EKYYQQVLEAcallpdLEILpsGDRTEIGEKGVNLSGGQKQRVSLARAVYSNADIYLFDDPLSAVDAHVGK 797

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|.
gi 1131020733  181 QMrieIKKIQRKLGI----TAIYVTHDrVEAMSLSDRIIVMKDGKIMQIGT 227
Cdd:TIGR00957  798 HI---FEHVIGPEGVlknkTRILVTHG-ISYLPQVDVIIVMSGGKISEMGS 844
Rli1 COG1245
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ...
 35-216 3.67e-15

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: 76.75  E-value: 3.67e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131020733  35 EIKPGELITLLGPSGCGKTTTLRMVAGFELPTKGKIyIGNEDVTFLPpnkrdtatvfQSYGLFPHMTVFDNvayglkLRK 114
Cdd:COG1245   362 EIREGEVLGIVGPNGIGKTTFAKILAGVLKPDEGEV-DEDLKISYKP----------QYISPDYDGTVEEF------LRS 424

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131020733 115 LSREEIEKRVFEA--LEMVGLKDLASRAPSRLSGGQQQRVTLARSIIVEPAILLLDEPLSNLDAllrEQmRIE----IKK 188
Cdd:COG1245   425 ANTDDFGSSYYKTeiIKPLGLEKLLDKNVKDLSGGELQRVAIAACLSRDADLYLLDEPSAHLDV---EQ-RLAvakaIRR 500

                         170       180
                  ....*....|....*....|....*...
gi 1131020733 189 IQRKLGITAIYVTHDRVEAMSLSDRIIV 216
Cdd:COG1245   501 FAENRGKTAMVVDHDIYLIDYISDRLMV 528
PRK10522 PRK10522
multidrug transporter membrane component/ATP-binding component; Provisional
 8-222 8.81e-15

multidrug transporter membrane component/ATP-binding component; Provisional


Pssm-ID: 236707 [Multi-domain]  Cd Length: 547  Bit Score: 75.39  E-value: 8.81e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131020733   8 LRLENVTkiFKDKKNNTEVIAVNnstFEIKPGELITLLGPSGCGKTTTLRMVAGFELPTKGKIYIGNEDVTFLPPN--KR 85
Cdd:PRK10522  323 LELRNVT--FAYQDNGFSVGPIN---LTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKPVTAEQPEdyRK 397

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131020733  86 DTATVFQSYGLFPHMtvfdnvayglkLRKLSREEIEKRVFEALEMVGLKDLASRAPSR-----LSGGQQQRVTLARSIIV 160
Cdd:PRK10522  398 LFSAVFTDFHLFDQL-----------LGPEGKPANPALVEKWLERLKMAHKLELEDGRisnlkLSKGQKKRLALLLALAE 466

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1131020733 161 EPAILLLDEPLSNLDALLREQMRIEIKKIQRKLGITAIYVTHDRvEAMSLSDRIIVMKDGKI 222
Cdd:PRK10522  467 ERDILLLDEWAADQDPHFRREFYQVLLPLLQEMGKTIFAISHDD-HYFIHADRLLEMRNGQL 527
PRK15056 PRK15056
manganese/iron ABC transporter ATP-binding protein;
28-230 2.87e-14

manganese/iron ABC transporter ATP-binding protein;


Pssm-ID: 185016 [Multi-domain]  Cd Length: 272  Bit Score: 72.22  E-value: 2.87e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131020733  28 AVNNSTFEIKPGELITLLGPSGCGKTTTLRMVAGFELPTKGKIYIGNEDVTfLPPNKRDTATVFQSYGL---FPhMTVFD 104
Cdd:PRK15056   22 ALRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKISILGQPTR-QALQKNLVAYVPQSEEVdwsFP-VLVED 99

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131020733 105 NVAYG----LKLRKLSREEIEKRVFEALEMVGLKDLASRAPSRLSGGQQQRVTLARSIIVEPAILLLDEPLSNLD----- 175
Cdd:PRK15056  100 VVMMGryghMGWLRRAKKRDRQIVTAALARVDMVEFRHRQIGELSGGQKKRVFLARAIAQQGQVILLDEPFTGVDvktea 179

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1131020733 176 ---ALLREqMRIEikkiqrklGITAIYVTHDRVEAMSLSDRIIVMKdGKIMQIGtPVE 230
Cdd:PRK15056  180 riiSLLRE-LRDE--------GKTMLVSTHNLGSVTEFCDYTVMVK-GTVLASG-PTE 226
40850658_otr NF000106
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
1-229 3.10e-14

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


Pssm-ID: 411078 [Multi-domain]  Cd Length: 351  Bit Score: 72.85  E-value: 3.10e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131020733   1 MKKKQVSLRLENVTKIFKDKKNNTEVIAVNNSTFEIKPGELITLLGPSGCGKTTTlrmvagfELPTkgkiYIGNEDVTFL 80
Cdd:NF000106    1 MTRKTISNGARNAVEVRGLVKHFGEVKAVDGVDLDVREGTVLGVLGP*GAA**RG-------ALPA----HV*GPDAGRR 69

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131020733  81 P-------PNKRDTATVFQSY-----GLFPHMTVFDNVAYGLKLRKLSREEIEKRVFEALEMVGLKDLASRAPSRLSGGQ 148
Cdd:NF000106   70 Pwrf*twcANRRALRRTIG*Hrpvr*GRRESFSGRENLYMIGR*LDLSRKDARARADELLERFSLTEAAGRAAAKYSGGM 149

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131020733 149 QQRVTLARSIIVEPAILLLDEPLSNLDALLREQMRIEIKKIQRKlGITAIYVTHDRVEAMSLS------DRIIVMKDGKI 222
Cdd:NF000106  150 RRRLDLAASMIGRPAVLYLDEPTTGLDPRTRNEVWDEVRSMVRD-GATVLLTTQYMEEAEQLAheltviDRGRVIADGKV 228


                  ....*..
gi 1131020733 223 MQIGTPV 229
Cdd:NF000106  229 DELKTKV 235
3a01205 TIGR00956
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
 14-238 6.37e-14

Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]


Pssm-ID: 273362 [Multi-domain]  Cd Length: 1394  Bit Score: 73.22  E-value: 6.37e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131020733   14 TKIFKDKKNNTEVIAVNNSTFeIKPGELITLLGPSGCGKTTTLRMVA----GFELPTKGKI-YIGNEDVTFLPPNKRDTA 88
Cdd:TIGR00956   63 RKLKKFRDTKTFDILKPMDGL-IKPGELTVVLGRPGSGCSTLLKTIAsntdGFHIGVEGVItYDGITPEEIKKHYRGDVV 141

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131020733   89 TVFQSYGLFPHMTVFDNVAYGLKLRK-------LSREE-IEKRVFEALEMVGLK---------DLAsRApsrLSGGQQQR 151
Cdd:TIGR00956  142 YNAETDVHFPHLTVGETLDFAARCKTpqnrpdgVSREEyAKHIADVYMATYGLShtrntkvgnDFV-RG---VSGGERKR 217

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131020733  152 VTLARSIIVEPAILLLDEPLSNLDALLREQMRIEIKKIQRKLGIT---AIYVTHDrvEAMSLSDRIIVMKDGKImqigtp 228
Cdd:TIGR00956  218 VSIAEASLGGAKIQCWDNATRGLDSATALEFIRALKTSANILDTTplvAIYQCSQ--DAYELFDKVIVLYEGYQ------ 289

                          250
                   ....*....|
gi 1131020733  229 veIYEDPISK 238
Cdd:TIGR00956  290 --IYFGPADK 297
PRK10762 PRK10762
D-ribose transporter ATP binding protein; Provisional
 29-222 6.63e-14

D-ribose transporter ATP binding protein; Provisional


Pssm-ID: 236755 [Multi-domain]  Cd Length: 501  Bit Score: 72.73  E-value: 6.63e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131020733  29 VNNSTFEIKPGELITLLGPSGCGKTTTLRMVAGfELP-TKGKIYIGNEDVTFLPPN--------------KRDtatvfqs 93
Cdd:PRK10762  268 VNDVSFTLRKGEILGVSGLMGAGRTELMKVLYG-ALPrTSGYVTLDGHEVVTRSPQdglangivyisedrKRD------- 339

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131020733  94 yGLFPHMTVFDNVAYgLKLRKLSREEIEKRVFEALEMVG--LKDLASRAPSR------LSGGQQQRVTLARSIIVEPAIL 165
Cdd:PRK10762  340 -GLVLGMSVKENMSL-TALRYFSRAGGSLKHADEQQAVSdfIRLFNIKTPSMeqaiglLSGGNQQKVAIARGLMTRPKVL 417

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1131020733 166 LLDEPLSNLDALLREQMRIEIKKIQRKlGITAIYVTHDRVEAMSLSDRIIVMKDGKI 222
Cdd:PRK10762  418 ILDEPTRGVDVGAKKEIYQLINQFKAE-GLSIILVSSEMPEVLGMSDRILVMHEGRI 473
araG PRK11288
L-arabinose ABC transporter ATP-binding protein AraG;
33-222 6.63e-14

L-arabinose ABC transporter ATP-binding protein AraG;


Pssm-ID: 183077 [Multi-domain]  Cd Length: 501  Bit Score: 72.64  E-value: 6.63e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131020733  33 TFEIKPGELITLLGPSGCGKTTTLRMVAGFELPTKGKIYIGNEDVTF------------LPPNKRdtatvfQSYGLFPHM 100
Cdd:PRK11288  273 SFSVRAGEIVGLFGLVGAGRSELMKLLYGATRRTAGQVYLDGKPIDIrsprdairagimLCPEDR------KAEGIIPVH 346

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131020733 101 TVFDNVA-----YGLKLRKLSREEIEKRVFEALemvgLKDLASRAPSR------LSGGQQQRVTLARSIIVEPAILLLDE 169
Cdd:PRK11288  347 SVADNINisarrHHLRAGCLINNRWEAENADRF----IRSLNIKTPSReqlimnLSGGNQQKAILGRWLSEDMKVILLDE 422

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1131020733 170 PLSNLDAllreQMRIEIKKIQRKL---GITAIYVTHDRVEAMSLSDRIIVMKDGKI 222
Cdd:PRK11288  423 PTRGIDV----GAKHEIYNVIYELaaqGVAVLFVSSDLPEVLGVADRIVVMREGRI 474
ABCC_SUR1_N cd03290
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ...
 29-220 7.43e-14

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: 70.05  E-value: 7.43e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131020733  29 VNNSTFEIKPGELITLLGPSGCGKTTTLRMVAGFELPTKGKIYIGNED------VTFLPPNKRDTATVFQSYGLFpHMTV 102
Cdd:cd03290    17 LSNINIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWSNKNesepsfEATRSRNRYSVAYAAQKPWLL-NATV 95

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131020733 103 FDNVAYGLKLRKlsreEIEKRVFEALEMVGLKDLASRAPS--------RLSGGQQQRVTLARSIIVEPAILLLDEPLSNL 174
Cdd:cd03290    96 EENITFGSPFNK----QRYKAVTDACSLQPDIDLLPFGDQteigergiNLSGGQRQRICVARALYQNTNIVFLDDPFSAL 171

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 1131020733 175 DALLREQ-MRIEIKKIQRKLGITAIYVTHdRVEAMSLSDRIIVMKDG 220
Cdd:cd03290   172 DIHLSDHlMQEGILKFLQDDKRTLVLVTH-KLQYLPHADWIIAMKDG 217
PRK13540 PRK13540
cytochrome c biogenesis protein CcmA; Provisional
 29-205 9.89e-14

cytochrome c biogenesis protein CcmA; Provisional


Pssm-ID: 184127 [Multi-domain]  Cd Length: 200  Bit Score: 69.21  E-value: 9.89e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131020733  29 VNNSTFEIKPGELITLLGPSGCGKTTTLRMVAGFELPTKGKIYIGNEDVtflppnKRDTAT-------VFQSYGLFPHMT 101
Cdd:PRK13540   17 LQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEILFERQSI------KKDLCTyqkqlcfVGHRSGINPYLT 90

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131020733 102 VFDNVAYGLKLRKLSREeiekrVFEALEMVGLKDLASRAPSRLSGGQQQRVTLARSIIVEPAILLLDEPLSNLDALLREQ 181
Cdd:PRK13540   91 LRENCLYDIHFSPGAVG-----ITELCRLFSLEHLIDYPCGLLSSGQKRQVALLRLWMSKAKLWLLDEPLVALDELSLLT 165

                         170       180
                  ....*....|....*....|....*.
gi 1131020733 182 MrieIKKIQ--RKLGITAIYVTHDRV 205
Cdd:PRK13540  166 I---ITKIQehRAKGGAVLLTSHQDL 188
ABC2_perm_RbbA NF033858
ribosome-associated ATPase/putative transporter RbbA;
9-233 1.29e-13

ribosome-associated ATPase/putative transporter RbbA;


Pssm-ID: 468210 [Multi-domain]  Cd Length: 907  Bit Score: 72.08  E-value: 1.29e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131020733   9 RLENVTKIFKDkknnteVIAVNNSTFEIKPGELITLLGPSGCGKTTTLRMVAGFELPTKGKIYIGNEDVTflppNKRDTA 88
Cdd:NF033858    3 RLEGVSHRYGK------TVALDDVSLDIPAGCMVGLIGPDGVGKSSLLSLIAGARKIQQGRVEVLGGDMA----DARHRR 72

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131020733  89 TVF-------QSYG--LFPHMTVFDNVAYGLKLRKLSREEIEKRVFEALEMVGLKDLASRAPSRLSGGQQQRVTLARSII 159
Cdd:NF033858   73 AVCpriaympQGLGknLYPTLSVFENLDFFGRLFGQDAAERRRRIDELLRATGLAPFADRPAGKLSGGMKQKLGLCCALI 152

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1131020733 160 VEPAILLLDEPLSNLDALLREQMRIEIKKI-QRKLGITAIYVTHDRVEAMSLsDRIIVMKDGKIMQIGTPVEIYE 233
Cdd:NF033858  153 HDPDLLILDEPTTGVDPLSRRQFWELIDRIrAERPGMSVLVATAYMEEAERF-DWLVAMDAGRVLATGTPAELLA 226
PLN03232 PLN03232
ABC transporter C family member; Provisional
 33-239 1.64e-13

ABC transporter C family member; Provisional


Pssm-ID: 215640 [Multi-domain]  Cd Length: 1495  Bit Score: 71.93  E-value: 1.64e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131020733   33 TFEIKPGELITLLGPSGCGKTTTLRMVAGFELPTKGKIYIGNEDVTF--LPPNKRDTATVFQSYGLFPHMTVFDNVAYGl 110
Cdd:PLN03232  1256 SFFVSPSEKVGVVGRTGAGKSSMLNALFRIVELEKGRIMIDDCDVAKfgLTDLRRVLSIIPQSPVLFSGTVRFNIDPFS- 1334

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131020733  111 klrklsrEEIEKRVFEALEMVGLKDLASRAPSRL-----------SGGQQQRVTLARSIIVEPAILLLDEPLSNL----D 175
Cdd:PLN03232  1335 -------EHNDADLWEALERAHIKDVIDRNPFGLdaevseggenfSVGQRQLLSLARALLRRSKILVLDEATASVdvrtD 1407

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1131020733  176 ALLREQMRIEIKKiqrklgITAIYVTHdRVEAMSLSDRIIVMKDGKIMQIGTPVEIYEDPISKF 239
Cdd:PLN03232  1408 SLIQRTIREEFKS------CTMLVIAH-RLNTIIDCDKILVLSSGQVLEYDSPQELLSRDTSAF 1464
PRK13409 PRK13409
ribosome biogenesis/translation initiation ATPase RLI;
35-216 1.79e-13

ribosome biogenesis/translation initiation ATPase RLI;


Pssm-ID: 184037 [Multi-domain]  Cd Length: 590  Bit Score: 71.38  E-value: 1.79e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131020733  35 EIKPGELITLLGPSGCGKTTTLRMVAGFELPTKGKIYIgNEDVTFLPpnkrdtatvfQSYGLFPHMTVFDNvayglkLRK 114
Cdd:PRK13409  361 EIYEGEVIGIVGPNGIGKTTFAKLLAGVLKPDEGEVDP-ELKISYKP----------QYIKPDYDGTVEDL------LRS 423

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131020733 115 LS--------REEIEKRVfealemvGLKDLASRAPSRLSGGQQQRVTLARSIIVEPAILLLDEPLSNLDAllrEQmRIE- 185
Cdd:PRK13409  424 ITddlgssyyKSEIIKPL-------QLERLLDKNVKDLSGGELQRVAIAACLSRDADLYLLDEPSAHLDV---EQ-RLAv 492

                         170       180       190
                  ....*....|....*....|....*....|....
gi 1131020733 186 ---IKKIQRKLGITAIYVTHDRVEAMSLSDRIIV 216
Cdd:PRK13409  493 akaIRRIAEEREATALVVDHDIYMIDYISDRLMV 526
PRK15064 PRK15064
ABC transporter ATP-binding protein; Provisional
 8-222 2.72e-13

ABC transporter ATP-binding protein; Provisional


Pssm-ID: 237894 [Multi-domain]  Cd Length: 530  Bit Score: 70.69  E-value: 2.72e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131020733   8 LRLENVTKIFKDKKnnteviAVNNSTFEIKPGELITLLGPSGCGKTTTLRMVAGFELPTKGKI-YIGNEDVTFLPpnkRD 86
Cdd:PRK15064  320 LEVENLTKGFDNGP------LFKNLNLLLEAGERLAIIGENGVGKTTLLRTLVGELEPDSGTVkWSENANIGYYA---QD 390

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131020733  87 TATVFQSyglfpHMTVFD------------NVAYGLKLRKL-SREEIEKRVfealemvglkdlasrapSRLSGGQQQRVT 153
Cdd:PRK15064  391 HAYDFEN-----DLTLFDwmsqwrqegddeQAVRGTLGRLLfSQDDIKKSV-----------------KVLSGGEKGRML 448

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1131020733 154 LARSIIVEPAILLLDEPLSNLDALLREQMRIEIKKIQrklGiTAIYVTHDRVEAMSLSDRIIVMKDGKI 222
Cdd:PRK15064  449 FGKLMMQKPNVLVMDEPTNHMDMESIESLNMALEKYE---G-TLIFVSHDREFVSSLATRIIEITPDGV 513
PRK11819 PRK11819
putative ABC transporter ATP-binding protein; Reviewed
 11-175 4.12e-13

putative ABC transporter ATP-binding protein; Reviewed


Pssm-ID: 236992 [Multi-domain]  Cd Length: 556  Bit Score: 70.15  E-value: 4.12e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131020733  11 ENVTKIFKDKknntevIAVNNSTFEIKPGELITLLGPSGCGKTTTLRMVAGFELPTKGKIYIGnEDVTFlppnkrdtATV 90
Cdd:PRK11819  328 ENLSKSFGDR------LLIDDLSFSLPPGGIVGIIGPNGAGKSTLFKMITGQEQPDSGTIKIG-ETVKL--------AYV 392

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131020733  91 FQSY-GLFPHMTVFDNVAYGLklrklsrEEIekrvfealeMVGLKDLASRA-PSR--------------LSGGQQQRVTL 154
Cdd:PRK11819  393 DQSRdALDPNKTVWEEISGGL-------DII---------KVGNREIPSRAyVGRfnfkggdqqkkvgvLSGGERNRLHL 456

                         170       180
                  ....*....|....*....|.
gi 1131020733 155 ARSIIVEPAILLLDEPLSNLD 175
Cdd:PRK11819  457 AKTLKQGGNVLLLDEPTNDLD 477
ABC_ABC_ChvD TIGR03719
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ...
 12-204 4.34e-13

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: 70.35  E-value: 4.34e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131020733  12 NVTKIFKDKKNNTEVIAVnnSTFeikPGELITLLGPSGCGKTTTLRMVAGFELPTKGKIYIG-NEDVTFLPpnkrdtatv 90
Cdd:TIGR03719   9 RVSKVVPPKKEILKDISL--SFF---PGAKIGVLGLNGAGKSTLLRIMAGVDKDFNGEARPQpGIKVGYLP--------- 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131020733  91 fQSYGLFPHMTVFDNVAYGL--KLRKLSR-EEI------EKRVFEAL--EMVGLKDL------------------ASRAP 141
Cdd:TIGR03719  75 -QEPQLDPTKTVRENVEEGVaeIKDALDRfNEIsakyaePDADFDKLaaEQAELQEIidaadawdldsqleiamdALRCP 153

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1131020733 142 ------SRLSGGQQQRVTLARSIIVEPAILLLDEPLSNLDA---LLREQMRIEIKKiqrklgiTAIYVTHDR 204
Cdd:TIGR03719 154 pwdadvTKLSGGERRRVALCRLLLSKPDMLLLDEPTNHLDAesvAWLERHLQEYPG-------TVVAVTHDR 218
PRK13541 PRK13541
cytochrome c biogenesis protein CcmA; Provisional
 38-175 5.05e-13

cytochrome c biogenesis protein CcmA; Provisional


Pssm-ID: 184128 [Multi-domain]  Cd Length: 195  Bit Score: 67.20  E-value: 5.05e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131020733  38 PGELITLLGPSGCGKTTTLRMVAGFELPTKGKIYIGNEDVTFLPpnKRDTATVFQSYGLFPHMTVFDNVAYGLKLRKLSr 117
Cdd:PRK13541   25 PSAITYIKGANGCGKSSLLRMIAGIMQPSSGNIYYKNCNINNIA--KPYCTYIGHNLGLKLEMTVFENLKFWSEIYNSA- 101

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1131020733 118 eeieKRVFEALEMVGLKDLASRAPSRLSGGQQQRVTLARSIIVEPAILLLDEPLSNLD 175
Cdd:PRK13541  102 ----ETLYAAIHYFKLHDLLDEKCYSLSSGMQKIVAIARLIACQSDLWLLDEVETNLS 155
PRK11147 PRK11147
ABC transporter ATPase component; Reviewed
 31-222 6.99e-13

ABC transporter ATPase component; Reviewed


Pssm-ID: 236861 [Multi-domain]  Cd Length: 635  Bit Score: 69.59  E-value: 6.99e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131020733  31 NSTFEIKPGELITLLGPSGCGKTTTLRMVAGFELPTKGKI-YIGNEDVTFL---PPnkRDTATvfqsyglfphmTVFDNV 106
Cdd:PRK11147   21 NAELHIEDNERVCLVGRNGAGKSTLMKILNGEVLLDDGRIiYEQDLIVARLqqdPP--RNVEG-----------TVYDFV 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131020733 107 AYGLK------------LRKLSREEIEK------RVFEALEMVGLKDLASR-------------AP-SRLSGGQQQRVTL 154
Cdd:PRK11147   88 AEGIEeqaeylkryhdiSHLVETDPSEKnlnelaKLQEQLDHHNLWQLENRinevlaqlgldpdAAlSSLSGGWLRKAAL 167

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1131020733 155 ARSIIVEPAILLLDEPLSNLDALLREQMRIEIKKIQRKLgitaIYVTHDRVEAMSLSDRIIVMKDGKI 222
Cdd:PRK11147  168 GRALVSNPDVLLLDEPTNHLDIETIEWLEGFLKTFQGSI----IFISHDRSFIRNMATRIVDLDRGKL 231
PRK11147 PRK11147
ABC transporter ATPase component; Reviewed
 10-204 7.71e-13

ABC transporter ATPase component; Reviewed


Pssm-ID: 236861 [Multi-domain]  Cd Length: 635  Bit Score: 69.59  E-value: 7.71e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131020733  10 LENVTKIFKDKKnnteviAVNNSTFEIKPGELITLLGPSGCGKTTTLRMVAGFELPTKGKIYIGnedvtflppNKRDTAt 89
Cdd:PRK11147  322 MENVNYQIDGKQ------LVKDFSAQVQRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRIHCG---------TKLEVA- 385

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131020733  90 VFQSY--GLFPHMTVFDNVAYGlklrklsREEIekrvfealeMVG---------LKDL-----ASRAPSR-LSGGQQQRV 152
Cdd:PRK11147  386 YFDQHraELDPEKTVMDNLAEG-------KQEV---------MVNgrprhvlgyLQDFlfhpkRAMTPVKaLSGGERNRL 449

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1131020733 153 TLARsIIVEPAILL-LDEPLSNLDA----LLREQmrieIKKIQrklGiTAIYVTHDR 204
Cdd:PRK11147  450 LLAR-LFLKPSNLLiLDEPTNDLDVetleLLEEL----LDSYQ---G-TVLLVSHDR 497
PLN03130 PLN03130
ABC transporter C family member; Provisional
 31-234 1.08e-12

ABC transporter C family member; Provisional


Pssm-ID: 215595 [Multi-domain]  Cd Length: 1622  Bit Score: 69.38  E-value: 1.08e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131020733   31 NSTFEIKPGELITLLGPSGCGKTTTLRMVAGfELPTK--GKIYIgnedvtflppnkRDT-ATVFQSYGLFpHMTVFDNVA 107
Cdd:PLN03130   635 NINLDVPVGSLVAIVGSTGEGKTSLISAMLG-ELPPRsdASVVI------------RGTvAYVPQVSWIF-NATVRDNIL 700

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131020733  108 YGLKLRKlsreeieKRVFEALEMVGLK-DLASRAPSRL----------SGGQQQRVTLARSIIVEPAILLLDEPLSNLDA 176
Cdd:PLN03130   701 FGSPFDP-------ERYERAIDVTALQhDLDLLPGGDLteigergvniSGGQKQRVSMARAVYSNSDVYIFDDPLSALDA 773

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 1131020733  177 LLREQmrIEIKKIQRKL-GITAIYVThDRVEAMSLSDRIIVMKDGKIMQIGTpveiYED 234
Cdd:PLN03130   774 HVGRQ--VFDKCIKDELrGKTRVLVT-NQLHFLSQVDRIILVHEGMIKEEGT----YEE 825
ABCC_CFTR2 cd03289
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ...
 31-224 1.54e-12

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: 67.19  E-value: 1.54e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131020733  31 NSTFEIKPGELITLLGPSGCGKTTTLRMVAGFeLPTKGKIYIGNEDVTFLPPNKRDTAtvfqsYGLFPHMTVFDNVAYGL 110
Cdd:cd03289    22 NISFSISPGQRVGLLGRTGSGKSTLLSAFLRL-LNTEGDIQIDGVSWNSVPLQKWRKA-----FGVIPQKVFIFSGTFRK 95

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131020733 111 KLR---KLSREEIEKrvfeALEMVGLKDLASRAPSRL-----------SGGQQQRVTLARSIIVEPAILLLDEPLSNLDA 176
Cdd:cd03289    96 NLDpygKWSDEEIWK----VAEEVGLKSVIEQFPGQLdfvlvdggcvlSHGHKQLMCLARSVLSKAKILLLDEPSAHLDP 171

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 1131020733 177 LLREQMRIEIKkiQRKLGITAIYVTHdRVEAMSLSDRIIVMKDGKIMQ 224
Cdd:cd03289   172 ITYQVIRKTLK--QAFADCTVILSEH-RIEAMLECQRFLVIEENKVRQ 216
PRK10636 PRK10636
putative ABC transporter ATP-binding protein; Provisional
 8-233 2.26e-12

putative ABC transporter ATP-binding protein; Provisional


Pssm-ID: 236729 [Multi-domain]  Cd Length: 638  Bit Score: 68.27  E-value: 2.26e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131020733   8 LRLENVTKIFKDKknntevIAVNNSTFEIKPGELITLLGPSGCGKTTTLRMVAGFELPTKGKI---------YIGNEDVT 78
Cdd:PRK10636  313 LKMEKVSAGYGDR------IILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELAPVSGEIglakgiklgYFAQHQLE 386

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131020733  79 FLppnkRDTATVFQsyglfpHMTvfdnvayglklrKLSREEIEKRVFEALEMVGLK-DLASRAPSRLSGGQQQRVTLARS 157
Cdd:PRK10636  387 FL----RADESPLQ------HLA------------RLAPQELEQKLRDYLGGFGFQgDKVTEETRRFSGGEKARLVLALI 444

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1131020733 158 IIVEPAILLLDEPLSNLDALLREQMRIEIKKIQRKLgitaIYVTHDRVEAMSLSDRIIVMKDGKIMQIGTPVEIYE 233
Cdd:PRK10636  445 VWQRPNLLLLDEPTNHLDLDMRQALTEALIDFEGAL----VVVSHDRHLLRSTTDDLYLVHDGKVEPFDGDLEDYQ 516
PTZ00265 PTZ00265
multidrug resistance protein (mdr1); Provisional
 17-219 5.33e-12

multidrug resistance protein (mdr1); Provisional


Pssm-ID: 240339 [Multi-domain]  Cd Length: 1466  Bit Score: 67.36  E-value: 5.33e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131020733   17 FKDKKNNteviavNNSTFEIKPGELITLLGPSGCGKTTTLrmvagfeLPTKGKIYIgnEDVTFLPPNKRDTATVF----Q 92
Cdd:PTZ00265  1239 EQDYQGD------EEQNVGMKNVNEFSLTKEGGSGEDSTV-------FKNSGKILL--DGVDICDYNLKDLRNLFsivsQ 1303

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131020733   93 SYGLFpHMTVFDNVAYGLKlrKLSREEIEKrvfeALEMVGLKDLASRAPSR-----------LSGGQQQRVTLARSIIVE 161
Cdd:PTZ00265  1304 EPMLF-NMSIYENIKFGKE--DATREDVKR----ACKFAAIDEFIESLPNKydtnvgpygksLSGGQKQRIAIARALLRE 1376

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 1131020733  162 PAILLLDEPLSNLDALLREQMRIEIKKIQRKLGITAIYVTHdRVEAMSLSDRIIVMKD 219
Cdd:PTZ00265  1377 PKILLLDEATSSLDSNSEKLIEKTIVDIKDKADKTIITIAH-RIASIKRSDKIVVFNN 1433
PLN03232 PLN03232
ABC transporter C family member; Provisional
 24-236 7.45e-12

ABC transporter C family member; Provisional


Pssm-ID: 215640 [Multi-domain]  Cd Length: 1495  Bit Score: 66.92  E-value: 7.45e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131020733   24 TEVIAVNNSTFEIKPGELITLLGPSGCGKTTTLRMVAGFELPTKGKIYIGNEDVTFLPpnkrDTATVFQSyglfphmTVF 103
Cdd:PLN03232   628 TSKPTLSDINLEIPVGSLVAIVGGTGEGKTSLISAMLGELSHAETSSVVIRGSVAYVP----QVSWIFNA-------TVR 696

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131020733  104 DNVAYGLKLRklsreeiEKRVFEALEMVGLKDLASRAPSR-----------LSGGQQQRVTLARSIIVEPAILLLDEPLS 172
Cdd:PLN03232   697 ENILFGSDFE-------SERYWRAIDVTALQHDLDLLPGRdlteigergvnISGGQKQRVSMARAVYSNSDIYIFDDPLS 769

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1131020733  173 NLDALLREQMRIEIKKIQRKlGITAIYVThDRVEAMSLSDRIIVMKDGKIMQIGTPVEIYEDPI 236
Cdd:PLN03232   770 ALDAHVAHQVFDSCMKDELK-GKTRVLVT-NQLHFLPLMDRIILVSEGMIKEEGTFAELSKSGS 831
CFTR_protein TIGR01271
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ...
 31-264 1.42e-11

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: 66.09  E-value: 1.42e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131020733   31 NSTFEIKPGELITLLGPSGCGKTTTLRMVAGFELPTKGKIYIGNEdVTFLPpnkrdtatvfQSYGLFPHmTVFDNVAYGL 110
Cdd:TIGR01271  444 NISFKLEKGQLLAVAGSTGSGKSSLLMMIMGELEPSEGKIKHSGR-ISFSP----------QTSWIMPG-TIKDNIIFGL 511

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131020733  111 KLRKLSREEIEK--RVFEALEMVGLKD--LASRAPSRLSGGQQQRVTLARSIIVEPAILLLDEPLSNLDALLREQM--RI 184
Cdd:TIGR01271  512 SYDEYRYTSVIKacQLEEDIALFPEKDktVLGEGGITLSGGQRARISLARAVYKDADLYLLDSPFTHLDVVTEKEIfeSC 591

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131020733  185 EIKKIQRKlgiTAIYVThDRVEAMSLSDRIIVMKDGKIMQIGTPVEIY-EDPisKFVAGFIGKVAFftvDVIGKENDNII 263
Cdd:TIGR01271  592 LCKLMSNK---TRILVT-SKLEHLKKADKILLLHEGVCYFYGTFSELQaKRP--DFSSLLLGLEAF---DNFSAERRNSI 662


                   .
gi 1131020733  264 I 264
Cdd:TIGR01271  663 L 663
ABC_RNaseL_inhibitor cd03222
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ...
 35-216 2.04e-11

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: 62.20  E-value: 2.04e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131020733  35 EIKPGELITLLGPSGCGKTTTLRMVAGFELPTKGKiyignedvtflppnkrdtatvfqsyglfphmTVFDNVAYGLKLRK 114
Cdd:cd03222    21 VVKEGEVIGIVGPNGTGKTTAVKILAGQLIPNGDN-------------------------------DEWDGITPVYKPQY 69

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131020733 115 LSreeiekrvfealemvglkdlasrapsrLSGGQQQRVTLARSIIVEPAILLLDEPLSNLDALLREQMRIEIKKIQRKLG 194
Cdd:cd03222    70 ID---------------------------LSGGELQRVAIAAALLRNATFYLFDEPSAYLDIEQRLNAARAIRRLSEEGK 122

                         170       180
                  ....*....|....*....|..
gi 1131020733 195 ITAIYVTHDRVEAMSLSDRIIV 216
Cdd:cd03222   123 KTALVVEHDLAVLDYLSDRIHV 144
ycf16 CHL00131
sulfate ABC transporter protein; Validated
 1-227 2.81e-11

sulfate ABC transporter protein; Validated


Pssm-ID: 214372 [Multi-domain]  Cd Length: 252  Bit Score: 63.12  E-value: 2.81e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131020733   1 MKKKQVSLRLENVtkifKDKKNNTEVIavNNSTFEIKPGELITLLGPSGCGKTTTLRMVAGFelP----TKGKIYIGNED 76
Cdd:CHL00131    1 MNKNKPILEIKNL----HASVNENEIL--KGLNLSINKGEIHAIMGPNGSGKSTLSKVIAGH--PaykiLEGDILFKGES 72

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131020733  77 VTFLPPNKRDTATVFQSYGLFPHMTVFDN-----VAYGLKLRKLSREEIEKRVF-----EALEMVGLKD--LASRAPSRL 144
Cdd:CHL00131   73 ILDLEPEERAHLGIFLAFQYPIEIPGVSNadflrLAYNSKRKFQGLPELDPLEFleiinEKLKLVGMDPsfLSRNVNEGF 152

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131020733 145 SGGQQQRVTLARSIIVEPAILLLDEPLSNLDALLREQMRIEIKKIQRKlGITAIYVTH-DRVEAMSLSDRIIVMKDGKIM 223
Cdd:CHL00131  153 SGGEKKRNEILQMALLDSELAILDETDSGLDIDALKIIAEGINKLMTS-ENSIILITHyQRLLDYIKPDYVHVMQNGKII 231


                  ....
gi 1131020733 224 QIGT 227
Cdd:CHL00131  232 KTGD 235
PRK13546 PRK13546
teichoic acids export ABC transporter ATP-binding subunit TagH;
4-226 3.05e-11

teichoic acids export ABC transporter ATP-binding subunit TagH;


Pssm-ID: 184131 [Multi-domain]  Cd Length: 264  Bit Score: 62.91  E-value: 3.05e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131020733   4 KQVSLRLENVTKIFKDKKNNTEVI--------------AVNNSTFEIKPGELITLLGPSGCGKTTTLRMVAGFELPTKGK 69
Cdd:PRK13546    1 MNVSVNIKNVTKEYRIYRTNKERMkdalipkhknktffALDDISLKAYEGDVIGLVGINGSGKSTLSNIIGGSLSPTVGK 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131020733  70 IYiGNEDVTFLPPNKrdtatvfqsyGLFPHMTVFDNVAYGLKLRKLSREEIEKRVFEALEMVGLKDLASRAPSRLSGGQQ 149
Cdd:PRK13546   81 VD-RNGEVSVIAISA----------GLSGQLTGIENIEFKMLCMGFKRKEIKAMTPKIIEFSELGEFIYQPVKKYSSGMR 149

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1131020733 150 QRVTLARSIIVEPAILLLDEPLSNLDALLREQMRIEIKKIQRKlGITAIYVTHDRVEAMSLSDRIIVMKDGKIMQIG 226
Cdd:PRK13546  150 AKLGFSINITVNPDILVIDEALSVGDQTFAQKCLDKIYEFKEQ-NKTIFFVSHNLGQVRQFCTKIAWIEGGKLKDYG 225
PvdE COG4615
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ...
 7-222 3.79e-11

ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion transport and metabolism];


Pssm-ID: 443659 [Multi-domain]  Cd Length: 547  Bit Score: 64.05  E-value: 3.79e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131020733   7 SLRLENVTKIFKDKKNNtEVIAVNNSTFEIKPGELITLLGPSGCGKTTTLRMVAGFELPTKGKIYIGNEDVTflpPNKRD 86
Cdd:COG4615   327 TLELRGVTYRYPGEDGD-EGFTLGPIDLTIRRGELVFIVGGNGSGKSTLAKLLTGLYRPESGEILLDGQPVT---ADNRE 402

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131020733  87 T-----ATVFQSYGLFPHMTVFDNVAyglkLRKLSREEIEKrvfeaLEM---VGLKD--LASRApsrLSGGQQQRVTLAR 156
Cdd:COG4615   403 AyrqlfSAVFSDFHLFDRLLGLDGEA----DPARARELLER-----LELdhkVSVEDgrFSTTD---LSQGQRKRLALLV 470

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1131020733 157 SIIVEPAILLLDEPLSNLDALLR----EQMRIEIKkiqrKLGITAIYVTHD-RveAMSLSDRIIVMKDGKI 222
Cdd:COG4615   471 ALLEDRPILVFDEWAADQDPEFRrvfyTELLPELK----ARGKTVIAISHDdR--YFDLADRVLKMDYGKL 535
CFTR_protein TIGR01271
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ...
 31-224 5.84e-11

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: 64.16  E-value: 5.84e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131020733   31 NSTFEIKPGELITLLGPSGCGKTTTLRMVAGFeLPTKGKIYIgnEDVTFlppNKRDTATVFQSYGLFPHMTVFDNVAYGL 110
Cdd:TIGR01271 1237 DLSFSVEGGQRVGLLGRTGSGKSTLLSALLRL-LSTEGEIQI--DGVSW---NSVTLQTWRKAFGVIPQKVFIFSGTFRK 1310

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131020733  111 KL---RKLSREEIEKrvfeALEMVGLKDLASRAPSRL-----------SGGQQQRVTLARSIIVEPAILLLDEPLSNLDA 176
Cdd:TIGR01271 1311 NLdpyEQWSDEEIWK----VAEEVGLKSVIEQFPDKLdfvlvdggyvlSNGHKQLMCLARSILSKAKILLLDEPSAHLDP 1386

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*...
gi 1131020733  177 LLREQMRIEIKkiQRKLGITAIYVTHdRVEAMSLSDRIIVMKDGKIMQ 224
Cdd:TIGR01271 1387 VTLQIIRKTLK--QSFSNCTVILSEH-RVEALLECQQFLVIEGSSVKQ 1431
3a01205 TIGR00956
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
 30-220 6.01e-11

Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]


Pssm-ID: 273362 [Multi-domain]  Cd Length: 1394  Bit Score: 63.97  E-value: 6.01e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131020733   30 NNSTFEIKPGELITLLGPSGCGKTTTLRMVAgfELPTKGKIYIGNEDVTFLPPNK---RDTATVFQSYGLFPHMTVFDNV 106
Cdd:TIGR00956  780 NNVDGWVKPGTLTALMGASGAGKTTLLNVLA--ERVTTGVITGGDRLVNGRPLDSsfqRSIGYVQQQDLHLPTSTVRESL 857

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131020733  107 AYGLKLR---KLSREE----IEKrVFEALEMVGLKD-LASRAPSRLSGGQQQRVTLARSIIVEPAILL-LDEPLSNLDAl 177
Cdd:TIGR00956  858 RFSAYLRqpkSVSKSEkmeyVEE-VIKLLEMESYADaVVGVPGEGLNVEQRKRLTIGVELVAKPKLLLfLDEPTSGLDS- 935

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*..
gi 1131020733  178 lreQMRIEIKKIQRKLGIT--AIYVTHDRVEAMSLS--DRIIVMKDG 220
Cdd:TIGR00956  936 ---QTAWSICKLMRKLADHgqAILCTIHQPSAILFEefDRLLLLQKG 979
tagH PRK13545
teichoic acids export protein ATP-binding subunit; Provisional
 2-231 6.17e-11

teichoic acids export protein ATP-binding subunit; Provisional


Pssm-ID: 184130 [Multi-domain]  Cd Length: 549  Bit Score: 63.76  E-value: 6.17e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131020733   2 KKKQVSLRLENVTKIFKDKKNNTEVIAVNNSTFEIKPGELITLLGPSGCGKTTTLRMVAGFELPTKGKIYIgnedvtflp 81
Cdd:PRK13545   13 KYKMYNKPFDKLKDLFFRSKDGEYHYALNNISFEVPEGEIVGIIGLNGSGKSTLSNLIAGVTMPNKGTVDI--------- 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131020733  82 pnKRDTATVFQSYGLFPHMTVFDNVAYGLKLRKLSREEIEKRVFEALEMVGLKDLASRAPSRLSGGQQQRVTLARSIIVE 161
Cdd:PRK13545   84 --KGSAALIAISSGLNGQLTGIENIELKGLMMGLTKEKIKEIIPEIIEFADIGKFIYQPVKTYSSGMKSRLGFAISVHIN 161

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131020733 162 PAILLLDEPLSNLDALLREQMRIEIKKIQRKlGITAIYVTHDRVEAMSLSDRIIVMKDGKIMQIGTPVEI 231
Cdd:PRK13545  162 PDILVIDEALSVGDQTFTKKCLDKMNEFKEQ-GKTIFFISHSLSQVKSFCTKALWLHYGQVKEYGDIKEV 230
PLN03140 PLN03140
ABC transporter G family member; Provisional
 37-176 7.95e-11

ABC transporter G family member; Provisional


Pssm-ID: 215599 [Multi-domain]  Cd Length: 1470  Bit Score: 63.71  E-value: 7.95e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131020733   37 KPGELITLLGPSGCGKTTTLRMVAGFElpTKGkiYI-GNEDVTFLPPNKRDTATVF----QSYGLFPHMTVFDNVAYGLK 111
Cdd:PLN03140   904 RPGVLTALMGVSGAGKTTLMDVLAGRK--TGG--YIeGDIRISGFPKKQETFARISgyceQNDIHSPQVTVRESLIYSAF 979

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1131020733  112 LR---KLSREE---IEKRVFEALEMVGLKDLASRAP--SRLSGGQQQRVTLARSIIVEPAILLLDEPLSNLDA 176
Cdd:PLN03140   980 LRlpkEVSKEEkmmFVDEVMELVELDNLKDAIVGLPgvTGLSTEQRKRLTIAVELVANPSIIFMDEPTSGLDA 1052
ABCC_CFTR1 cd03291
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ...
 31-264 1.16e-10

ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The CFTR subfamily domain 1. The cystic fibrosis transmembrane regulator (CFTR), the product of the gene mutated in patients with cystic fibrosis, has adapted the ABC transporter structural motif to form a tightly regulated anion channel at the apical surface of many epithelia. Use of the term assembly of a functional ion channel implies the coming together of subunits, or at least smaller not-yet functional components of the active whole. In fact, on the basis of current knowledge only the CFTR polypeptide itself is required to form an ATP- and protein kinase A-dependent low-conductance chloride channel of the type present in the apical membrane of many epithelial cells. CFTR displays the typical organization (IM-ABC)2 and carries a characteristic hydrophilic R-domain that separates IM1-ABC1 from IM2-ABC2.


Pssm-ID: 213258 [Multi-domain]  Cd Length: 282  Bit Score: 61.41  E-value: 1.16e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131020733  31 NSTFEIKPGELITLLGPSGCGKTTTLRMVAGFELPTKGKIYIGNEdVTFLPpnkrdtatvfQSYGLFPHmTVFDNVAYGL 110
Cdd:cd03291    55 NINLKIEKGEMLAITGSTGSGKTSLLMLILGELEPSEGKIKHSGR-ISFSS----------QFSWIMPG-TIKENIIFGV 122

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131020733 111 KLRklsreeiEKRVFEALEMVGLKDLASRAPSR-----------LSGGQQQRVTLARSIIVEPAILLLDEPLSNLDALLR 179
Cdd:cd03291   123 SYD-------EYRYKSVVKACQLEEDITKFPEKdntvlgeggitLSGGQRARISLARAVYKDADLYLLDSPFGYLDVFTE 195

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131020733 180 EQM--RIEIKKIQRKlgiTAIYVThDRVEAMSLSDRIIVMKDGKIMQIGTPVEIyEDPISKFVAGFIGKVAFftvDVIGK 257
Cdd:cd03291   196 KEIfeSCVCKLMANK---TRILVT-SKMEHLKKADKILILHEGSSYFYGTFSEL-QSLRPDFSSKLMGYDTF---DQFSA 267


                  ....*..
gi 1131020733 258 ENDNIII 264
Cdd:cd03291   268 ERRNSIL 274
PLN03130 PLN03130
ABC transporter C family member; Provisional
 33-239 1.39e-10

ABC transporter C family member; Provisional


Pssm-ID: 215595 [Multi-domain]  Cd Length: 1622  Bit Score: 62.83  E-value: 1.39e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131020733   33 TFEIKPGELITLLGPSGCGKTTTLRMVAGFELPTKGKIYIGNEDVTflppnKRDTATVFQSYGLFPHMTVFDNVAYGLKL 112
Cdd:PLN03130  1259 SFEISPSEKVGIVGRTGAGKSSMLNALFRIVELERGRILIDGCDIS-----KFGLMDLRKVLGIIPQAPVLFSGTVRFNL 1333

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131020733  113 RKLSrEEIEKRVFEALEMVGLKDLASRAPSRL-----------SGGQQQRVTLARSIIVEPAILLLDEPLSNL----DAL 177
Cdd:PLN03130  1334 DPFN-EHNDADLWESLERAHLKDVIRRNSLGLdaevseagenfSVGQRQLLSLARALLRRSKILVLDEATAAVdvrtDAL 1412

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1131020733  178 LREQMRIEIKkiqrklGITAIYVTHdRVEAMSLSDRIIVMKDGKIMQIGTPVEIYEDPISKF 239
Cdd:PLN03130  1413 IQKTIREEFK------SCTMLIIAH-RLNTIIDCDRILVLDAGRVVEFDTPENLLSNEGSAF 1467
ABCG_PDR_domain2 cd03232
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ...
 30-220 1.62e-10

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: 59.56  E-value: 1.62e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131020733  30 NNSTFEIKPGELITLLGPSGCGKTTTLRMVAGFELP--TKGKIYIGNE--DVTFLppnkRDTATVFQSYGLFPHMTVFDN 105
Cdd:cd03232    24 NNISGYVKPGTLTALMGESGAGKTTLLDVLAGRKTAgvITGEILINGRplDKNFQ----RSTGYVEQQDVHSPNLTVREA 99

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131020733 106 VAYGLKLRKLSREEiEKRVFEALEmvglkdLASRapsrlsggqqqrvtlarsiivePAILLLDEPLSNLDAllreQMRIE 185
Cdd:cd03232   100 LRFSALLRGLSVEQ-RKRLTIGVE------LAAK----------------------PSILFLDEPTSGLDS----QAAYN 146

                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 1131020733 186 IKKIQRKL---GITAIYVTHDRVEA-MSLSDRIIVMKDG 220
Cdd:cd03232   147 IVRFLKKLadsGQAILCTIHQPSASiFEKFDRLLLLKRG 185
PTZ00243 PTZ00243
ABC transporter; Provisional
 33-239 1.76e-10

ABC transporter; Provisional


Pssm-ID: 240327 [Multi-domain]  Cd Length: 1560  Bit Score: 62.49  E-value: 1.76e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131020733   33 TFEIKPGELITLLGPSGCGKTTTL----RMV--AGFELPTKGKiYIGNEDVTFLppnKRDTATVFQSYGLFPHmTVFDNV 106
Cdd:PTZ00243  1330 SFRIAPREKVGIVGRTGSGKSTLLltfmRMVevCGGEIRVNGR-EIGAYGLREL---RRQFSMIPQDPVLFDG-TVRQNV 1404

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131020733  107 AYGLKLrklSREEiekrVFEALEMVGLKD-LASRAP----------SRLSGGQQQRVTLARSIIVE-PAILLLDEPLSNL 174
Cdd:PTZ00243  1405 DPFLEA---SSAE----VWAALELVGLRErVASESEgidsrvleggSNYSVGQRQLMCMARALLKKgSGFILMDEATANI 1477

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131020733  175 DALLREQmrieikkIQRKL-----GITAIYVTHdRVEAMSLSDRIIVMKDGKIMQIGTPVEIYEDPISKF 239
Cdd:PTZ00243  1478 DPALDRQ-------IQATVmsafsAYTVITIAH-RLHTVAQYDKIIVMDHGAVAEMGSPRELVMNRQSIF 1539
PRK11819 PRK11819
putative ABC transporter ATP-binding protein; Reviewed
 12-204 2.42e-10

putative ABC transporter ATP-binding protein; Reviewed


Pssm-ID: 236992 [Multi-domain]  Cd Length: 556  Bit Score: 61.67  E-value: 2.42e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131020733  12 NVTKIFKDKKnntEVIA-VNNSTFeikPGELITLLGPSGCGKTTTLRMVAGFELPTKGK------IYIGnedvtFLPpnk 84
Cdd:PRK11819   11 RVSKVVPPKK---QILKdISLSFF---PGAKIGVLGLNGAGKSTLLRIMAGVDKEFEGEarpapgIKVG-----YLP--- 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131020733  85 rdtatvfQSYGLFPHMTVFDNVAYGL--KLRKLSR-EEI------EKRVFEAL--EMVGLKDL----------------- 136
Cdd:PRK11819   77 -------QEPQLDPEKTVRENVEEGVaeVKAALDRfNEIyaayaePDADFDALaaEQGELQEIidaadawdldsqleiam 149

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1131020733 137 -ASRAP------SRLSGGQQQRVTLARSIIVEPAILLLDEPLSNLDA---LLREQMrieikkIQRKLGiTAIYVTHDR 204
Cdd:PRK11819  150 dALRCPpwdakvTKLSGGERRRVALCRLLLEKPDMLLLDEPTNHLDAesvAWLEQF------LHDYPG-TVVAVTHDR 220
PTZ00265 PTZ00265
multidrug resistance protein (mdr1); Provisional
 9-235 3.61e-10

multidrug resistance protein (mdr1); Provisional


Pssm-ID: 240339 [Multi-domain]  Cd Length: 1466  Bit Score: 61.58  E-value: 3.61e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131020733    9 RLENVTKI-FK------DKKNNTEViaVNNSTFEIKPGELITLLGPSGCGKTTTLRMVAGFELPTKGKIYIGN----EDV 77
Cdd:PTZ00265   376 KLKDIKKIqFKnvrfhyDTRKDVEI--YKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIIINDshnlKDI 453

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131020733   78 TfLPPNKRDTATVFQSYGLFPHmTVFDNVAYGL-KLRKL----------------------------------------S 116
Cdd:PTZ00265   454 N-LKWWRSKIGVVSQDPLLFSN-SIKNNIKYSLySLKDLealsnyynedgndsqenknkrnscrakcagdlndmsnttdS 531

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131020733  117 REEIEKR----------VFEALEMVGLKDLASRAP-----------SRLSGGQQQRVTLARSIIVEPAILLLDEPLSNLD 175
Cdd:PTZ00265   532 NELIEMRknyqtikdseVVDVSKKVLIHDFVSALPdkyetlvgsnaSKLSGGQKQRISIARAIIRNPKILILDEATSSLD 611

                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131020733  176 ALLREQMRIEIKKIQRKLGITAIYVTHdRVEAMSLSDRIIVMKDGKIMQIGTPVEIYEDP 235
Cdd:PTZ00265   612 NKSEYLVQKTINNLKGNENRITIIIAH-RLSTIRYANTIFVLSNRERGSTVDVDIIGEDP 670
PRK10982 PRK10982
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
 10-221 4.57e-10

galactose/methyl galaxtoside transporter ATP-binding protein; Provisional


Pssm-ID: 182880 [Multi-domain]  Cd Length: 491  Bit Score: 60.90  E-value: 4.57e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131020733  10 LENVTKIFKDKKnnteviAVNNSTFEIKPGELITLLGPSGCGKTTTLRMVAGFELPTKGKIYIGNEDVTFLPPNK---RD 86
Cdd:PRK10982    1 MSNISKSFPGVK------ALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEIDFKSSKEaleNG 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131020733  87 TATVFQSYGLFPHMTVFDNVAYG--------LKLRKLSREeiEKRVFEALEMvglkDLASRAP-SRLSGGQQQRVTLARS 157
Cdd:PRK10982   75 ISMVHQELNLVLQRSVMDNMWLGryptkgmfVDQDKMYRD--TKAIFDELDI----DIDPRAKvATLSVSQMQMIEIAKA 148

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1131020733 158 IIVEPAILLLDEPLSNLDALLREQMRIEIKKIQRKlGITAIYVTHDRVEAMSLSDRIIVMKDGK 221
Cdd:PRK10982  149 FSYNAKIVIMDEPTSSLTEKEVNHLFTIIRKLKER-GCGIVYISHKMEEIFQLCDEITILRDGQ 211
PRK10762 PRK10762
D-ribose transporter ATP binding protein; Provisional
 5-221 6.61e-10

D-ribose transporter ATP binding protein; Provisional


Pssm-ID: 236755 [Multi-domain]  Cd Length: 501  Bit Score: 60.40  E-value: 6.61e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131020733   5 QVSLRLENVTKIFKDKKnnteviAVNNSTFEIKPGELITLLGPSGCGKTTTLRMVAGFELPTKGKIYIGNEDVTFLPPNK 84
Cdd:PRK10762    2 QALLQLKGIDKAFPGVK------ALSGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSILYLGKEVTFNGPKS 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131020733  85 RDTA---TVFQSYGLFPHMTVFDNVAYGLKLR-KLSREEIEKRVFEA---LEMVGLKDLASRAPSRLSGGQQQRVTLARS 157
Cdd:PRK10762   76 SQEAgigIIHQELNLIPQLTIAENIFLGREFVnRFGRIDWKKMYAEAdklLARLNLRFSSDKLVGELSIGEQQMVEIAKV 155

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1131020733 158 IIVEPAILLLDEPlsnLDAL--------------LREQMRieikkiqrklGItaIYVTHDRVEAMSLSDRIIVMKDGK 221
Cdd:PRK10762  156 LSFESKVIIMDEP---TDALtdteteslfrvireLKSQGR----------GI--VYISHRLKEIFEICDDVTVFRDGQ 218
PTZ00243 PTZ00243
ABC transporter; Provisional
 35-242 7.39e-10

ABC transporter; Provisional


Pssm-ID: 240327 [Multi-domain]  Cd Length: 1560  Bit Score: 60.56  E-value: 7.39e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131020733   35 EIKPGELITLLGPSGCGKTTTLRMVAG-FELpTKGKIYIgnedvtflppnKRDTATVFQSYGLFpHMTVFDNVAYglklr 113
Cdd:PTZ00243   682 SVPRGKLTVVLGATGSGKSTLLQSLLSqFEI-SEGRVWA-----------ERSIAYVPQQAWIM-NATVRGNILF----- 743

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131020733  114 klSREEIEKRVFEALEMVGLK-DLASRAPS----------RLSGGQQQRVTLARSIIVEPAILLLDEPLSNLDALLREQM 182
Cdd:PTZ00243   744 --FDEEDAARLADAVRVSQLEaDLAQLGGGleteigekgvNLSGGQKARVSLARAVYANRDVYLLDDPLSALDAHVGERV 821

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131020733  183 rIEIKKIQRKLGITAIYVTHdRVEAMSLSDRIIVMKDGKIMQIGTPVEIYEDPISKFVAG 242
Cdd:PTZ00243   822 -VEECFLGALAGKTRVLATH-QVHVVPRADYVVALGDGRVEFSGSSADFMRTSLYATLAA 879
ABCC_SUR2 cd03288
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The ...
 36-231 2.30e-09

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: 57.61  E-value: 2.30e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131020733  36 IKPGELITLLGPSGCGKTTT----LRMVAGFElptkGKIYIGNEDVTFLPPN--KRDTATVFQSYGLFPHMTVFDnvayg 109
Cdd:cd03288    44 IKPGQKVGICGRTGSGKSSLslafFRMVDIFD----GKIVIDGIDISKLPLHtlRSRLSIILQDPILFSGSIRFN----- 114

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131020733 110 lklRKLSREEIEKRVFEALEMVGLKDLASRAPSRL-----------SGGQQQRVTLARSIIVEPAILLLDEPLSNLDall 178
Cdd:cd03288   115 ---LDPECKCTDDRLWEALEIAQLKNMVKSLPGGLdavvteggenfSVGQRQLFCLARAFVRKSSILIMDEATASID--- 188

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1131020733 179 reqmrIEIKKIQRKLGITA------IYVTHdRVEAMSLSDRIIVMKDGKIMQIGTPVEI 231
Cdd:cd03288   189 -----MATENILQKVVMTAfadrtvVTIAH-RVSTILDADLVLVLSRGILVECDTPENL 241
ABC_RNaseL_inhibitor_domain1 cd03236
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ...
 37-217 2.38e-09

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: 57.38  E-value: 2.38e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131020733  37 KPGELITLLGPSGCGKTTTLRMVAGFELPTKGKI------------YIGNEDVTFLPPNKRDTATVF---QSYGLFPHmT 101
Cdd:cd03236    24 REGQVLGLVGPNGIGKSTALKILAGKLKPNLGKFddppdwdeildeFRGSELQNYFTKLLEGDVKVIvkpQYVDLIPK-A 102

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131020733 102 VFDNVAYGLKlRKLSREEIEKrVFEALEMVGLKDlasRAPSRLSGGQQQRVTLARSIIVEPAILLLDEPLSNLDAllreQ 181
Cdd:cd03236   103 VKGKVGELLK-KKDERGKLDE-LVDQLELRHVLD---RNIDQLSGGELQRVAIAAALARDADFYFFDEPSSYLDI----K 173

                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 1131020733 182 MRIEIKKIQRKL---GITAIYVTHDRVEAMSLSDRIIVM 217
Cdd:cd03236   174 QRLNAARLIRELaedDNYVLVVEHDLAVLDYLSDYIHCL 212
3a01203 TIGR00954
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ...
 27-202 4.68e-09

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: 57.84  E-value: 4.68e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131020733  27 IAVNNSTFEIKPGELITLLGPSGCGKTTTLRMVAGF--------ELPTKGKIYignedvtFLPPNKRDTATVFQSYGLFP 98
Cdd:TIGR00954 466 VLIESLSFEVPSGNNLLICGPNGCGKSSLFRILGELwpvyggrlTKPAKGKLF-------YVPQRPYMTLGTLRDQIIYP 538

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131020733  99 hMTVFDnvaygLKLRKLSREEIEKrvfeALEMVGLKDLASRAPS---------RLSGGQQQRVTLARSIIVEPAILLLDE 169
Cdd:TIGR00954 539 -DSSED-----MKRRGLSDKDLEQ----ILDNVQLTHILEREGGwsavqdwmdVLSGGEKQRIAMARLFYHKPQFAILDE 608

                         170       180       190
                  ....*....|....*....|....*....|...
gi 1131020733 170 PLSNLDAllreQMRIEIKKIQRKLGITAIYVTH 202
Cdd:TIGR00954 609 CTSAVSV----DVEGYMYRLCREFGITLFSVSH 637
ABC_UvrA cd03238
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ...
 28-217 1.74e-08

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: 53.48  E-value: 1.74e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131020733  28 AVNNSTFEIKPGELITLLGPSGCGKTTTLRmvAGFELPTKGKIyignedVTFLPPNkrdtatvfqsyglFPHMTVFdnva 107
Cdd:cd03238    10 NLQNLDVSIPLNVLVVVTGVSGSGKSTLVN--EGLYASGKARL------ISFLPKF-------------SRNKLIF---- 64

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131020733 108 yglkLRKLSReeiekrvfeaLEMVGLKDLA-SRAPSRLSGGQQQRVTLARSIIVEP--AILLLDEPLSNLDALLREQMRI 184
Cdd:cd03238    65 ----IDQLQF----------LIDVGLGYLTlGQKLSTLSGGELQRVKLASELFSEPpgTLFILDEPSTGLHQQDINQLLE 130

                         170       180       190
                  ....*....|....*....|....*....|...
gi 1131020733 185 EIKKIqRKLGITAIYVTHDRvEAMSLSDRIIVM 217
Cdd:cd03238   131 VIKGL-IDLGNTVILIEHNL-DVLSSADWIIDF 161
GguA NF040905
sugar ABC transporter ATP-binding protein;
8-221 2.39e-08

sugar ABC transporter ATP-binding protein;


Pssm-ID: 468840 [Multi-domain]  Cd Length: 500  Bit Score: 55.57  E-value: 2.39e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131020733   8 LRLENVTKIFKDkknnteVIAVNNSTFEIKPGELITLLGPSGCGKTTTLRMVAG------FElptkGKIYIGNEDVTFlp 81
Cdd:NF040905    2 LEMRGITKTFPG------VKALDDVNLSVREGEIHALCGENGAGKSTLMKVLSGvyphgsYE----GEILFDGEVCRF-- 69

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131020733  82 PNKRDT-----ATVFQSYGLFPHMTVFDNVAYGLKLRK---LSREEIEKRVFEALEMVGLKDLASRAPSRLSGGQQQRVT 153
Cdd:NF040905   70 KDIRDSealgiVIIHQELALIPYLSIAENIFLGNERAKrgvIDWNETNRRARELLAKVGLDESPDTLVTDIGVGKQQLVE 149

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1131020733 154 LARSIIVEPAILLLDEPLSNL-----DALLREQMRIeikkiqRKLGITAIYVTHDRVEAMSLSDRIIVMKDGK 221
Cdd:NF040905  150 IAKALSKDVKLLILDEPTAALneedsAALLDLLLEL------KAQGITSIIISHKLNEIRRVADSITVLRDGR 216
SapD COG4170
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms];
26-235 3.61e-08

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


Pssm-ID: 443330 [Multi-domain]  Cd Length: 331  Bit Score: 54.53  E-value: 3.61e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131020733  26 VIAVNNSTFEIKPGELITLLGPSGCGKTTTLRMVAGFELP----TKGKIYIGNEDVTFLPPNKR------DTATVFQ--- 92
Cdd:COG4170    20 VKAVDRVSLTLNEGEIRGLVGESGSGKSLIAKAICGITKDnwhvTADRFRWNGIDLLKLSPRERrkiigrEIAMIFQeps 99

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131020733  93 SYgLFPHMTVFDNVAYGLKLRKLS------REEIEKRVFEALEMVGLKD---LASRAPSRLSGGQQQRVTLARSIIVEPA 163
Cdd:COG4170   100 SC-LDPSAKIGDQLIEAIPSWTFKgkwwqrFKWRKKRAIELLHRVGIKDhkdIMNSYPHELTEGECQKVMIAMAIANQPR 178

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1131020733 164 ILLLDEPLSNLDALLREQMRIEIKKIQRKLGITAIYVTHDrVEAMS-LSDRIIVMKDGKIMQIGTPVEIYEDP 235
Cdd:COG4170   179 LLIADEPTNAMESTTQAQIFRLLARLNQLQGTSILLISHD-LESISqWADTITVLYCGQTVESGPTEQILKSP 250
PRK10938 PRK10938
putative molybdenum transport ATP-binding protein ModF; Provisional
 30-183 3.66e-08

putative molybdenum transport ATP-binding protein ModF; Provisional


Pssm-ID: 182852 [Multi-domain]  Cd Length: 490  Bit Score: 55.02  E-value: 3.66e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131020733  30 NNSTFEIKPGELITLLGPSGCGKTTTLRMVAGfELPT----------------------KGKI-YIGNEdvtfLPPNKRD 86
Cdd:PRK10938  277 HNLSWQVNPGEHWQIVGPNGAGKSTLLSLITG-DHPQgysndltlfgrrrgsgetiwdiKKHIgYVSSS----LHLDYRV 351

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131020733  87 TATV--------FQSYGLFphMTVFDnvayglKLRKLSREeiekrvfeALEMVGLKDLASRAPSR-LSGGQQQRVTLARS 157
Cdd:PRK10938  352 STSVrnvilsgfFDSIGIY--QAVSD------RQQKLAQQ--------WLDILGIDKRTADAPFHsLSWGQQRLALIVRA 415

                         170       180
                  ....*....|....*....|....*.
gi 1131020733 158 IIVEPAILLLDEPLSNLDALLREQMR 183
Cdd:PRK10938  416 LVKHPTLLILDEPLQGLDPLNRQLVR 441
ABC_UvrA_I cd03270
ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair ...
 31-217 3.92e-08

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: 53.42  E-value: 3.92e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131020733  31 NSTFEIKPGELITLLGPSGCGKTT----------------TLRMVAGFELPTKGKIYIgnEDVTFLPPnkrdTATVFQ-S 93
Cdd:cd03270    13 NVDVDIPRNKLVVITGVSGSGKSSlafdtiyaegqrryveSLSAYARQFLGQMDKPDV--DSIEGLSP----AIAIDQkT 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131020733  94 YGLFPHMTVFDNVAYGLKLRKL-SREEIEKRVFEALEmVGLKDLA-SRAPSRLSGGQQQRVTLARSIIVE--PAILLLDE 169
Cdd:cd03270    87 TSRNPRSTVGTVTEIYDYLRLLfARVGIRERLGFLVD-VGLGYLTlSRSAPTLSGGEAQRIRLATQIGSGltGVLYVLDE 165

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 1131020733 170 PLSNLDAllREQMR-IEIKKIQRKLGITAIYVTHDRvEAMSLSDRIIVM 217
Cdd:cd03270   166 PSIGLHP--RDNDRlIETLKRLRDLGNTVLVVEHDE-DTIRAADHVIDI 211
uvra TIGR00630
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ...
 97-237 1.23e-07

excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of proteins of which all members for which functions are known except the UvrA proteins are involved in the transport of material through membranes. UvrA orthologs are involved in the recognition of DNA damage as a step in nucleotide excision repair. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]


Pssm-ID: 273184 [Multi-domain]  Cd Length: 925  Bit Score: 53.48  E-value: 1.23e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131020733  97 FPHMTVFDNVAY--GLKL---RKLSREEIEKRVFEALEM---VGLKDLA-SRAPSRLSGGQQQRVTLARSIIVE--PAIL 165
Cdd:TIGR00630 433 VSELSIREAHEFfnQLTLtpeEKKIAEEVLKEIRERLGFlidVGLDYLSlSRAAGTLSGGEAQRIRLATQIGSGltGVLY 512

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1131020733 166 LLDEPLSNLDAllREQMR-IEIKKIQRKLGITAIYVTHDRvEAMSLSDRIIVM------KDGKIMQIGTPVEIYEDPIS 237
Cdd:TIGR00630 513 VLDEPSIGLHQ--RDNRRlINTLKRLRDLGNTLIVVEHDE-DTIRAADYVIDIgpgageHGGEVVASGTPEEILANPDS 588
AAA smart00382
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ...
 38-220 2.56e-07

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: 49.68  E-value: 2.56e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131020733   38 PGELITLLGPSGCGKTTTLRMVAGFELPTKGKIYIGNEDvtflppnkrdtatvfqsyglfphmtvfdnvayglklrklsr 117
Cdd:smart00382   1 PGEVILIVGPPGSGKTTLARALARELGPPGGGVIYIDGE----------------------------------------- 39

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131020733  118 eeiekRVFEALEMVGLKDLASRAPSRLSGGQQQRVTLARSIIVEPAILLLDEPLSNLDA-----LLREQMRIEIKKIQRK 192
Cdd:smart00382  40 -----DILEEVLDQLLLIIVGGKKASGSGELRLRLALALARKLKPDVLILDEITSLLDAeqealLLLLEELRLLLLLKSE 114

                          170       180       190
                   ....*....|....*....|....*....|...
gi 1131020733  193 LGITAIYVTHDRVEAMSL-----SDRIIVMKDG 220
Cdd:smart00382 115 KNLTVILTTNDEKDLGPAllrrrFDRRIVLLLI 147
ABC_Rad50 cd03240
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ...
 35-204 5.15e-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: 49.53  E-value: 5.15e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131020733  35 EIKPGELITLL-GPSGCGKTTTLRMV--AGF-ELPTKGKIYIGNEDVTFLPPNKRDTATVFQS-----YGLFPHMTVFDN 105
Cdd:cd03240    17 EIEFFSPLTLIvGQNGAGKTTIIEALkyALTgELPPNSKGGAHDPKLIREGEVRAQVKLAFENangkkYTITRSLAILEN 96

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131020733 106 VAYglklrkLSREEIEKRVfeaLEMVGlkdlasrapsRLSGGQQQ------RVTLARSIIVEPAILLLDEPLSNLDALLR 179
Cdd:cd03240    97 VIF------CHQGESNWPL---LDMRG----------RCSGGEKVlasliiRLALAETFGSNCGILALDEPTTNLDEENI 157

                         170       180
                  ....*....|....*....|....*.
gi 1131020733 180 EQMRIEIKKIQRKLGI-TAIYVTHDR 204
Cdd:cd03240   158 EESLAEIIEERKSQKNfQLIVITHDE 183
PLN03073 PLN03073
ABC transporter F family; Provisional
 31-175 5.42e-07

ABC transporter F family; Provisional


Pssm-ID: 215558 [Multi-domain]  Cd Length: 718  Bit Score: 51.40  E-value: 5.42e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131020733  31 NSTFEIKPGELITLLGPSGCGKTTTLRMVAGFELPTKGKIyignedvtFLPPNKRdtATVFQSYglfpHMTVFD-NVAYG 109
Cdd:PLN03073  527 NLNFGIDLDSRIAMVGPNGIGKSTILKLISGELQPSSGTV--------FRSAKVR--MAVFSQH----HVDGLDlSSNPL 592

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1131020733 110 LKLRKLSREEIEKRVFEALEMVGLK-DLASRAPSRLSGGQQQRVTLARSIIVEPAILLLDEPLSNLD 175
Cdd:PLN03073  593 LYMMRCFPGVPEQKLRAHLGSFGVTgNLALQPMYTLSGGQKSRVAFAKITFKKPHILLLDEPSNHLD 659
PRK10982 PRK10982
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
 144-225 6.85e-07

galactose/methyl galaxtoside transporter ATP-binding protein; Provisional


Pssm-ID: 182880 [Multi-domain]  Cd Length: 491  Bit Score: 50.88  E-value: 6.85e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131020733 144 LSGGQQQRVTLARSIIVEPAILLLDEPLSNLDALLREQMRIEIKKIQRK-LGItaIYVTHDRVEAMSLSDRIIVMKDGKI 222
Cdd:PRK10982  392 LSGGNQQKVIIGRWLLTQPEILMLDEPTRGIDVGAKFEIYQLIAELAKKdKGI--IIISSEMPELLGITDRILVMSNGLV 469


                  ...
gi 1131020733 223 MQI 225
Cdd:PRK10982  470 AGI 472
PRK13409 PRK13409
ribosome biogenesis/translation initiation ATPase RLI;
36-203 9.11e-07

ribosome biogenesis/translation initiation ATPase RLI;


Pssm-ID: 184037 [Multi-domain]  Cd Length: 590  Bit Score: 50.58  E-value: 9.11e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131020733  36 IKPGELITLLGPSGCGKTTTLRMVAGFELPTKGKIyigNEDVTFLPPNKRDTATVFQSYglfphmtvFDNVAYGlKLR-- 113
Cdd:PRK13409   96 PKEGKVTGILGPNGIGKTTAVKILSGELIPNLGDY---EEEPSWDEVLKRFRGTELQNY--------FKKLYNG-EIKvv 163

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131020733 114 -------------KLSREEIEKRVFEA------LEMVGLKDLASRAPSRLSGGQQQRVTLARSIIVEPAILLLDEPLSNL 174
Cdd:PRK13409  164 hkpqyvdlipkvfKGKVRELLKKVDERgkldevVERLGLENILDRDISELSGGELQRVAIAAALLRDADFYFFDEPTSYL 243

                         170       180       190
                  ....*....|....*....|....*....|.
gi 1131020733 175 DalLREqmRIEIKKIQRKL--GITAIYVTHD 203
Cdd:PRK13409  244 D--IRQ--RLNVARLIRELaeGKYVLVVEHD 270
GguA NF040905
sugar ABC transporter ATP-binding protein;
111-222 1.14e-06

sugar ABC transporter ATP-binding protein;


Pssm-ID: 468840 [Multi-domain]  Cd Length: 500  Bit Score: 50.17  E-value: 1.14e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131020733 111 KLRKLSR-----EEIEKRVFEALEmvglKDLASRAPS------RLSGGQQQRVTLARSIIVEPAILLLDEPLSNLD--Al 177
Cdd:NF040905  365 NLGKVSRrgvidENEEIKVAEEYR----KKMNIKTPSvfqkvgNLSGGNQQKVVLSKWLFTDPDVLILDEPTRGIDvgA- 439

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 1131020733 178 lreqmRIEIKKIQRKL---GITAIYVTHDRVEAMSLSDRIIVMKDGKI 222
Cdd:NF040905  440 -----KYEIYTIINELaaeGKGVIVISSELPELLGMCDRIYVMNEGRI 482
PRK15093 PRK15093
peptide ABC transporter ATP-binding protein SapD;
122-235 1.16e-06

peptide ABC transporter ATP-binding protein SapD;


Pssm-ID: 185049 [Multi-domain]  Cd Length: 330  Bit Score: 49.80  E-value: 1.16e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131020733 122 KRVFEALEMVGLKD---LASRAPSRLSGGQQQRVTLARSIIVEPAILLLDEPLSNLDALLREQMRIEIKKIQRKLGITAI 198
Cdd:PRK15093  134 RRAIELLHRVGIKDhkdAMRSFPYELTEGECQKVMIAIALANQPRLLIADEPTNAMEPTTQAQIFRLLTRLNQNNNTTIL 213

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 1131020733 199 YVTHDrVEAMS-LSDRIIVMKDGKIMQIGTPVEIYEDP 235
Cdd:PRK15093  214 LISHD-LQMLSqWADKINVLYCGQTVETAPSKELVTTP 250
Rli1 COG1245
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ...
 37-203 1.31e-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: 50.17  E-value: 1.31e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131020733  37 KPGELITLLGPSGCGKTTTLRMVAGFELPTKGKIyignEDvtflPPNKRDTATVFQSYGLFPHmtvfdnvayglkLRKLS 116
Cdd:COG1245    97 KKGKVTGILGPNGIGKSTALKILSGELKPNLGDY----DE----EPSWDEVLKRFRGTELQDY------------FKKLA 156

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131020733 117 REEIE-----------KRVF------------------EALEMVGLKDLASRAPSRLSGGQQQRVTLARSIIVEPAILLL 167
Cdd:COG1245   157 NGEIKvahkpqyvdliPKVFkgtvrellekvdergkldELAEKLGLENILDRDISELSGGELQRVAIAAALLRDADFYFF 236

                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 1131020733 168 DEPLSNLDalLREqmRIEIKKIQRKL---GITAIYVTHD 203
Cdd:COG1245   237 DEPSSYLD--IYQ--RLNVARLIRELaeeGKYVLVVEHD 271
PRK10636 PRK10636
putative ABC transporter ATP-binding protein; Provisional
 29-215 2.94e-06

putative ABC transporter ATP-binding protein; Provisional


Pssm-ID: 236729 [Multi-domain]  Cd Length: 638  Bit Score: 49.01  E-value: 2.94e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131020733  29 VNNSTFEIKPGELITLLGPSGCGKTTTLRMVagfelptKGKIYIGNEDVTFlpPNKRDTATVFQSYGLFPhMTVFDNVAY 108
Cdd:PRK10636   17 LDNATATINPGQKVGLVGKNGCGKSTLLALL-------KNEISADGGSYTF--PGNWQLAWVNQETPALP-QPALEYVID 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131020733 109 G-LKLRKLSRE--------------------------EIEKRVFEALEMVGL-KDLASRAPSRLSGGQQQRVTLARSIIV 160
Cdd:PRK10636   87 GdREYRQLEAQlhdanerndghaiatihgkldaidawTIRSRAASLLHGLGFsNEQLERPVSDFSGGWRMRLNLAQALIC 166

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1131020733 161 EPAILLLDEPLSNLDAllreQMRIEIKKIQRKLGITAIYVTHDRVEAMSLSDRII 215
Cdd:PRK10636  167 RSDLLLLDEPTNHLDL----DAVIWLEKWLKSYQGTLILISHDRDFLDPIVDKII 217
MRP_assoc_pro TIGR00957
multi drug resistance-associated protein (MRP); This model describes multi drug ...
 121-231 3.93e-06

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: 48.79  E-value: 3.93e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131020733  121 EKRVFEALEMVGLKDLASRAPSRL-----------SGGQQQRVTLARSIIVEPAILLLDEPLSNLDA----LLREQMRIE 185
Cdd:TIGR00957 1388 DEEVWWALELAHLKTFVSALPDKLdhecaeggenlSVGQRQLVCLARALLRKTKILVLDEATAAVDLetdnLIQSTIRTQ 1467

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*.
gi 1131020733  186 IKKiqrklgITAIYVTHdRVEAMSLSDRIIVMKDGKIMQIGTPVEI 231
Cdd:TIGR00957 1468 FED------CTVLTIAH-RLNTIMDYTRVIVLDKGEVAEFGAPSNL 1506
sufC PRK09580
cysteine desulfurase ATPase component; Reviewed
 35-175 6.24e-06

cysteine desulfurase ATPase component; Reviewed


Pssm-ID: 181965 [Multi-domain]  Cd Length: 248  Bit Score: 47.09  E-value: 6.24e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131020733  35 EIKPGELITLLGPSGCGKTTTLRMVAGFE--LPTKGKIYIGNEDVTFLPPNKRDTATVFQSY----------GLFPHMTV 102
Cdd:PRK09580   23 EVRPGEVHAIMGPNGSGKSTLSATLAGREdyEVTGGTVEFKGKDLLELSPEDRAGEGIFMAFqypveipgvsNQFFLQTA 102

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1131020733 103 FDNVAYGLKLRKLSREEIEKRVFEALEMVGL-KDLASRAPSR-LSGGQQQRVTLARSIIVEPAILLLDEPLSNLD 175
Cdd:PRK09580  103 LNAVRSYRGQEPLDRFDFQDLMEEKIALLKMpEDLLTRSVNVgFSGGEKKRNDILQMAVLEPELCILDESDSGLD 177
PLN03073 PLN03073
ABC transporter F family; Provisional
 135-175 2.38e-05

ABC transporter F family; Provisional


Pssm-ID: 215558 [Multi-domain]  Cd Length: 718  Bit Score: 46.39  E-value: 2.38e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 1131020733 135 DLASRAPSRLSGGQQQRVTLARSIIVEPAILLLDEPLSNLD 175
Cdd:PLN03073  336 EMQVKATKTFSGGWRMRIALARALFIEPDLLLLDEPTNHLD 376
PRK00635 PRK00635
excinuclease ABC subunit A; Provisional
 139-215 3.45e-04

excinuclease ABC subunit A; Provisional


Pssm-ID: 234806 [Multi-domain]  Cd Length: 1809  Bit Score: 42.89  E-value: 3.45e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131020733  139 RAPSRLSGGQQQRVTLARSIIVEPA--ILLLDEPLSNLDALLREQMRIEIKKIqRKLGITAIYVTHDrvEAM-SLSDRII 215
Cdd:PRK00635   472 RALATLSGGEQERTALAKHLGAELIgiTYILDEPSIGLHPQDTHKLINVIKKL-RDQGNTVLLVEHD--EQMiSLADRII 548
PRK15064 PRK15064
ABC transporter ATP-binding protein; Provisional
 44-204 3.45e-04

ABC transporter ATP-binding protein; Provisional


Pssm-ID: 237894 [Multi-domain]  Cd Length: 530  Bit Score: 42.57  E-value: 3.45e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131020733  44 LLGPSGCGKTTTLRMVAGFELPTKGKIyignedvtFLPPNKRdTATVFQSYGLFPHMTVFDNVAYG-LKLRKLSREEieK 122
Cdd:PRK15064   32 LIGANGCGKSTFMKILGGDLEPSAGNV--------SLDPNER-LGKLRQDQFAFEEFTVLDTVIMGhTELWEVKQER--D 100

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131020733 123 RVFEALEMV---GLK--DLA------------SRAPSRLSG-----------------GQQQRVTLARSIIVEPAILLLD 168
Cdd:PRK15064  101 RIYALPEMSeedGMKvaDLEvkfaemdgytaeARAGELLLGvgipeeqhyglmsevapGWKLRVLLAQALFSNPDILLLD 180

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 1131020733 169 EPLSNLDallreqmrieIKKI--------QRKlgITAIYVTHDR 204
Cdd:PRK15064  181 EPTNNLD----------INTIrwledvlnERN--STMIIISHDR 212
UvrA COG0178
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair];
118-237 5.65e-04

Excinuclease UvrABC ATPase subunit [Replication, recombination and repair];


Pssm-ID: 439948 [Multi-domain]  Cd Length: 941  Bit Score: 41.94  E-value: 5.65e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131020733 118 EEIEKRV-FeaLEMVGLKDLA-SRAPSRLSGGQQQRVTLARSI---------IvepaillLDEP-----------LsnLD 175
Cdd:COG0178   460 KEIRSRLgF--LVDVGLDYLTlDRSAGTLSGGEAQRIRLATQIgsglvgvlyV-------LDEPsiglhqrdndrL--IE 528

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1131020733 176 ALLReqmrieikkiQRKLGITAIYVTHDRvEAMSLSDRIIVM------KDGKIMQIGTPVEIYEDPIS 237
Cdd:COG0178   529 TLKR----------LRDLGNTVIVVEHDE-DTIRAADYIIDIgpgageHGGEVVAQGTPEEILKNPDS 585
PRK10938 PRK10938
putative molybdenum transport ATP-binding protein ModF; Provisional
 132-234 5.72e-04

putative molybdenum transport ATP-binding protein ModF; Provisional


Pssm-ID: 182852 [Multi-domain]  Cd Length: 490  Bit Score: 41.54  E-value: 5.72e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131020733 132 GLKDLASRAPSRLSGGQQQRVTLARSIIVEPAILLLDEPLSNLDALLREQMRIEIKKIQRKlGITAIYVTHDRVEAMSLS 211
Cdd:PRK10938  124 GITALLDRRFKYLSTGETRKTLLCQALMSEPDLLILDEPFDGLDVASRQQLAELLASLHQS-GITLVLVLNRFDEIPDFV 202

                          90       100
                  ....*....|....*....|...
gi 1131020733 212 DRIIVMKDGKIMQIGTPVEIYED 234
Cdd:PRK10938  203 QFAGVLADCTLAETGEREEILQQ 225
ABC_Class2 cd03227
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ...
 143-218 1.07e-03

ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems involved in cellular processes other than transport. These families are characterized by the fact that the ABC subunit is made up of duplicated, fused ABC modules (ABC2). No known transmembrane proteins or domains are associated with these proteins.


Pssm-ID: 213194 [Multi-domain]  Cd Length: 162  Bit Score: 39.27  E-value: 1.07e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131020733 143 RLSGGQQQRVTLA-----RSIIVEPaILLLDEPLSNLDalLREQMRIE--IKKiQRKLGITAIYVTHDRvEAMSLSDRII 215
Cdd:cd03227    77 QLSGGEKELSALAlilalASLKPRP-LYILDEIDRGLD--PRDGQALAeaILE-HLVKGAQVIVITHLP-ELAELADKLI 151


                  ...
gi 1131020733 216 VMK 218
Cdd:cd03227   152 HIK 154
AAA_16 pfam13191
AAA ATPase domain; This family of domains contain a P-loop motif that is characteriztic of the ...
 39-181 6.28e-03

AAA ATPase domain; This family of domains contain a P-loop motif that is characteriztic of the AAA superfamily.


Pssm-ID: 433025 [Multi-domain]  Cd Length: 167  Bit Score: 37.10  E-value: 6.28e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131020733  39 GELITLLGPSGCGKTTTLRMVAGfelptkgkiYIGNEDVTFLppnkRDTATVFQSYGLFPHMTVFDNVAYGLKLRKLSRE 118
Cdd:pfam13191  24 PPSVLLTGEAGTGKTTLLRELLR---------ALERDGGYFL----RGKCDENLPYSPLLEALTREGLLRQLLDELESSL 90

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131020733 119 EIEKRVFEALEMVGLKDLASRAPSRLSGGQQQRVTLARSIIvEPAILLLDE-------PLSNLDALLREQ 181
Cdd:pfam13191  91 LEAWRAALLEALAPVPELPGDLAERLLDLLLRLLDLLARGE-RPLVLVLDDlqwadeaSLQLLAALLRLL 159
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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