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Conserved domains on  [gi|556496326|ref|WP_023344013|]
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MULTISPECIES: osmoprotectant ABC transporter ATP-binding protein OsmV [Enterobacter]

Protein Classification

ABC transporter ATP-binding protein( domain architecture ID 11438324)

ABC transporter ATP-binding protein/permease contains the ATPase catalytic subunit and permease component 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

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
OpuBA COG1125
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and ...
 1-311 0e+00

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


:

Pssm-ID: 440742 [Multi-domain]  Cd Length: 306  Bit Score: 548.54  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556496326   1 MIKLENLTKHFsqkhGQTFKAVDNVNLNVPEGEMCVLLGPSGCGKTTTLKMINRLITPSSGTILINGEDTSGMDTVTLRR 80
Cdd:COG1125    1 MIEFENVTKRY----PDGTVAVDDLSLTIPAGEFTVLVGPSGCGKTTTLRMINRLIEPTSGRILIDGEDIRDLDPVELRR 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556496326  81 NIGYVIQQIGLFPNMTIEENITVVPRMLGWDKARCKTRAEELMDMVALDPHKFLNRYPREMSGGQQQRIGVIRALAADPP 160
Cdd:COG1125   77 RIGYVIQQIGLFPHMTVAENIATVPRLLGWDKERIRARVDELLELVGLDPEEYRDRYPHELSGGQQQRVGVARALAADPP 156

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556496326 161 VLLMDEPFGAVDPINREVIQNQFLEMQRKLKKTVMLVSHDIDEALKLGDRIAVFRQGKIVQCASPDELLAKPANEFVGSF 240
Cdd:COG1125  157 ILLMDEPFGALDPITREQLQDELLRLQRELGKTIVFVTHDIDEALKLGDRIAVMREGRIVQYDTPEEILANPANDFVADF 236

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 556496326 241 VGQDRTLKRLLLVSAGDVTDQQPtITVRGSTPLPEAFATMDDNDIRAITVVDEHGKPLGFVKRREARNASG 311
Cdd:COG1125  237 VGADRGLRRLSLLRVEDLMLPEP-PTVSPDASLREALSLMLERGVDWLLVVDEDGRPLGWLTLEDLLRALA 306
CBS_pair_ABC_OpuCA_assoc cd04582
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains found associated with ...
 258-368 6.38e-61

Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains found associated with the ABC transporter OpuCA; This cd contains two tandem repeats of the cystathionine beta-synthase (CBS pair) domains found in association with the ABC transporter OpuCA. OpuCA is the ATP binding component of a bacterial solute transporter that serves a protective role to cells growing in a hyperosmolar environment but the function of the CBS domains in OpuCA remains unknown. In the related ABC transporter, OpuA, the tandem CBS domains have been shown to function as sensors for ionic strength, whereby they control the transport activity through an electronic switching mechanism. 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. They 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. The CBS domain, named after human CBS, is a small domain originally identified in cystathionine beta-synthase and is subsequently found in a wide range of different proteins. CBS domains usually occur in tandem repeats. They associate to form a so-called Bateman domain or a CBS pair based on crystallographic studies in bacteria. The CBS pair was used as a basis for this cd hierarchy since the human CBS proteins can adopt the typical core structure and form an intramolecular CBS pair. The interface between the two CBS domains forms a cleft that is a potential ligand binding site. The CBS pair coexists with a variety of other functional domains and this has been used to help in its classification here. It has been proposed that the CBS domain may play a regulatory role, although its exact function is unknown. Mutations of conserved residues within this domain are associated with a variety of human hereditary diseases, including congenital myotonia, idiopathic generalized epilepsy, hypercalciuric nephrolithiasis, and classic Bartter syndrome (CLC chloride channel family members), Wolff-Parkinson-White syndrome (gamma 2 subunit of AMP-activated protein kinase), retinitis pigmentosa (IMP dehydrogenase-1), and homocystinuria (cystathionine beta-synthase).


:

Pssm-ID: 341359 [Multi-domain]  Cd Length: 111  Bit Score: 191.83  E-value: 6.38e-61
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556496326 258 VTDQQPTITVRGSTPLPEAFATMDDNDIRAITVVDEHGKPLGFVKRREARNASGTCADILHPFRMTGKAEDNLRVVLSRL 337
Cdd:cd04582    1 EDAATPTPTVRPSTPLSDALGIMDDADSRYLVVVDADGRPLGYVTRRDARGASGTCGDFAHPFKATVPVDENLRVVLSRM 80

                         90       100       110
                 ....*....|....*....|....*....|.
gi 556496326 338 YESNTSWMPIVDEDGRYNGEISQDYIAEYLS 368
Cdd:cd04582   81 YEHNTSWLPVVDEDGRYAGEVTQDSIADYLS 111
 
Name Accession Description Interval E-value
OpuBA COG1125
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and ...
 1-311 0e+00

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


Pssm-ID: 440742 [Multi-domain]  Cd Length: 306  Bit Score: 548.54  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556496326   1 MIKLENLTKHFsqkhGQTFKAVDNVNLNVPEGEMCVLLGPSGCGKTTTLKMINRLITPSSGTILINGEDTSGMDTVTLRR 80
Cdd:COG1125    1 MIEFENVTKRY----PDGTVAVDDLSLTIPAGEFTVLVGPSGCGKTTTLRMINRLIEPTSGRILIDGEDIRDLDPVELRR 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556496326  81 NIGYVIQQIGLFPNMTIEENITVVPRMLGWDKARCKTRAEELMDMVALDPHKFLNRYPREMSGGQQQRIGVIRALAADPP 160
Cdd:COG1125   77 RIGYVIQQIGLFPHMTVAENIATVPRLLGWDKERIRARVDELLELVGLDPEEYRDRYPHELSGGQQQRVGVARALAADPP 156

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556496326 161 VLLMDEPFGAVDPINREVIQNQFLEMQRKLKKTVMLVSHDIDEALKLGDRIAVFRQGKIVQCASPDELLAKPANEFVGSF 240
Cdd:COG1125  157 ILLMDEPFGALDPITREQLQDELLRLQRELGKTIVFVTHDIDEALKLGDRIAVMREGRIVQYDTPEEILANPANDFVADF 236

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 556496326 241 VGQDRTLKRLLLVSAGDVTDQQPtITVRGSTPLPEAFATMDDNDIRAITVVDEHGKPLGFVKRREARNASG 311
Cdd:COG1125  237 VGADRGLRRLSLLRVEDLMLPEP-PTVSPDASLREALSLMLERGVDWLLVVDEDGRPLGWLTLEDLLRALA 306
ABC_OpuCA_Osmoprotection cd03295
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ...
 2-247 1.72e-143

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: 406.69  E-value: 1.72e-143
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556496326   2 IKLENLTKHFsqkhGQTFKAVDNVNLNVPEGEMCVLLGPSGCGKTTTLKMINRLITPSSGTILINGEDTSGMDTVTLRRN 81
Cdd:cd03295    1 IEFENVTKRY----GGGKKAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGEDIREQDPVELRRK 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556496326  82 IGYVIQQIGLFPNMTIEENITVVPRMLGWDKARCKTRAEELMDMVALDPHKFLNRYPREMSGGQQQRIGVIRALAADPPV 161
Cdd:cd03295   77 IGYVIQQIGLFPHMTVEENIALVPKLLKWPKEKIRERADELLALVGLDPAEFADRYPHELSGGQQQRVGVARALAADPPL 156

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556496326 162 LLMDEPFGAVDPINREVIQNQFLEMQRKLKKTVMLVSHDIDEALKLGDRIAVFRQGKIVQCASPDELLAKPANEFVGSFV 241
Cdd:cd03295  157 LLMDEPFGALDPITRDQLQEEFKRLQQELGKTIVFVTHDIDEAFRLADRIAIMKNGEIVQVGTPDEILRSPANDFVAEFV 236


                 ....*.
gi 556496326 242 GQDRTL 247
Cdd:cd03295  237 GADRLL 242
proV TIGR01186
glycine betaine/L-proline transport ATP binding subunit; This model describes the glycine ...
 20-360 5.33e-108

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: 321.42  E-value: 5.33e-108
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556496326   20 KAVDNVNLNVPEGEMCVLLGPSGCGKTTTLKMINRLITPSSGTILINGEDTSGMDTVTL----RRNIGYVIQQIGLFPNM 95
Cdd:TIGR01186   7 KGVNDADLAIAKGEIFVIMGLSGSGKSTTVRMLNRLIEPTAGQIFIDGENIMKQSPVELrevrRKKIGMVFQQFALFPHM 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556496326   96 TIEENITVVPRMLGWDKARCKTRAEELMDMVALDphKFLNRYPREMSGGQQQRIGVIRALAADPPVLLMDEPFGAVDPIN 175
Cdd:TIGR01186  87 TILQNTSLGPELLGWPEQERKEKALELLKLVGLE--EYEHRYPDELSGGMQQRVGLARALAAEPDILLMDEAFSALDPLI 164

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556496326  176 REVIQNQFLEMQRKLKKTVMLVSHDIDEALKLGDRIAVFRQGKIVQCASPDELLAKPANEFVGSFVGQDRTLKRLllvSA 255
Cdd:TIGR01186 165 RDSMQDELKKLQATLQKTIVFITHDLDEAIRIGDRIVIMKAGEIVQVGTPDEILRNPANEYVEEFIGKVDLSQVF---DA 241

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556496326  256 GDVTDQQPT--ITVRGSTPLPEAFATMDDNDIRAITVVDEHGKPLGFVK---RREARNASGTCADILHPFRMTGKAEDNL 330
Cdd:TIGR01186 242 ERIAQRMNTgpITKTADKGPRSALQLMRDERVDSLYVVDRQNKLVGVVDvesIKQARKKAQGLQDVLIDDIYTVDAGTLL 321

                         330       340       350
                  ....*....|....*....|....*....|
gi 556496326  331 RVVLSRLYESNTSwMPIVDEDGRYNGEISQ 360
Cdd:TIGR01186 322 RETVRKVLKAGIK-VPVVDEDQRLVGIVTR 350
potA PRK09452
spermidine/putrescine ABC transporter ATP-binding protein PotA;
2-243 3.74e-66

spermidine/putrescine ABC transporter ATP-binding protein PotA;


Pssm-ID: 236523 [Multi-domain]  Cd Length: 375  Bit Score: 214.43  E-value: 3.74e-66
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556496326   2 IKLENLTKHFSQKhgqtfKAVDNVNLNVPEGEMCVLLGPSGCGKTTTLKMINRLITPSSGTILINGEDTSGMDTVtlRRN 81
Cdd:PRK09452  15 VELRGISKSFDGK-----EVISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLDGQDITHVPAE--NRH 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556496326  82 IGYVIQQIGLFPNMTIEENITVVPRMLGWDKARCKTRAEELMDMVALDphKFLNRYPREMSGGQQQRIGVIRALAADPPV 161
Cdd:PRK09452  88 VNTVFQSYALFPHMTVFENVAFGLRMQKTPAAEITPRVMEALRMVQLE--EFAQRKPHQLSGGQQQRVAIARAVVNKPKV 165

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556496326 162 LLMDEPFGAVDPINREVIQNQFLEMQRKLKKTVMLVSHDIDEALKLGDRIAVFRQGKIVQCASPDELLAKPANEFVGSFV 241
Cdd:PRK09452 166 LLLDESLSALDYKLRKQMQNELKALQRKLGITFVFVTHDQEEALTMSDRIVVMRDGRIEQDGTPREIYEEPKNLFVARFI 245


                 ..
gi 556496326 242 GQ 243
Cdd:PRK09452 246 GE 247
CBS_pair_ABC_OpuCA_assoc cd04582
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains found associated with ...
 258-368 6.38e-61

Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains found associated with the ABC transporter OpuCA; This cd contains two tandem repeats of the cystathionine beta-synthase (CBS pair) domains found in association with the ABC transporter OpuCA. OpuCA is the ATP binding component of a bacterial solute transporter that serves a protective role to cells growing in a hyperosmolar environment but the function of the CBS domains in OpuCA remains unknown. In the related ABC transporter, OpuA, the tandem CBS domains have been shown to function as sensors for ionic strength, whereby they control the transport activity through an electronic switching mechanism. 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. They 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. The CBS domain, named after human CBS, is a small domain originally identified in cystathionine beta-synthase and is subsequently found in a wide range of different proteins. CBS domains usually occur in tandem repeats. They associate to form a so-called Bateman domain or a CBS pair based on crystallographic studies in bacteria. The CBS pair was used as a basis for this cd hierarchy since the human CBS proteins can adopt the typical core structure and form an intramolecular CBS pair. The interface between the two CBS domains forms a cleft that is a potential ligand binding site. The CBS pair coexists with a variety of other functional domains and this has been used to help in its classification here. It has been proposed that the CBS domain may play a regulatory role, although its exact function is unknown. Mutations of conserved residues within this domain are associated with a variety of human hereditary diseases, including congenital myotonia, idiopathic generalized epilepsy, hypercalciuric nephrolithiasis, and classic Bartter syndrome (CLC chloride channel family members), Wolff-Parkinson-White syndrome (gamma 2 subunit of AMP-activated protein kinase), retinitis pigmentosa (IMP dehydrogenase-1), and homocystinuria (cystathionine beta-synthase).


Pssm-ID: 341359 [Multi-domain]  Cd Length: 111  Bit Score: 191.83  E-value: 6.38e-61
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556496326 258 VTDQQPTITVRGSTPLPEAFATMDDNDIRAITVVDEHGKPLGFVKRREARNASGTCADILHPFRMTGKAEDNLRVVLSRL 337
Cdd:cd04582    1 EDAATPTPTVRPSTPLSDALGIMDDADSRYLVVVDADGRPLGYVTRRDARGASGTCGDFAHPFKATVPVDENLRVVLSRM 80

                         90       100       110
                 ....*....|....*....|....*....|.
gi 556496326 338 YESNTSWMPIVDEDGRYNGEISQDYIAEYLS 368
Cdd:cd04582   81 YEHNTSWLPVVDEDGRYAGEVTQDSIADYLS 111
ABC_tran pfam00005
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ...
 22-168 2.57e-50

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: 165.90  E-value: 2.57e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556496326   22 VDNVNLNVPEGEMCVLLGPSGCGKTTTLKMINRLITPSSGTILINGEDTSGMDTVTLRRNIGYVIQQIGLFPNMTIEENI 101
Cdd:pfam00005   1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDLTDDERKSLRKEIGYVFQDPQLFPRLTVRENL 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 556496326  102 TVVPRMLGWDKARCKTRAEELMDMVAL--DPHKFLNRYPREMSGGQQQRIGVIRALAADPPVLLMDEPF 168
Cdd:pfam00005  81 RLGLLLKGLSKREKDARAEEALEKLGLgdLADRPVGERPGTLSGGQRQRVAIARALLTKPKLLLLDEPT 149
ABC_ATP_DarD NF038007
darobactin export ABC transporter ATP-binding protein;
1-219 6.64e-39

darobactin export ABC transporter ATP-binding protein;


Pssm-ID: 411600 [Multi-domain]  Cd Length: 218  Bit Score: 138.31  E-value: 6.64e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556496326   1 MIKLENLTKHFSQKHGQTfKAVDNVNLNVPEGEMCVLLGPSGCGKTTTLKMINRLITPSSGTILINGEDTSGM---DTVT 77
Cdd:NF038007   1 MLNMQNAEKCYITKTIKT-KVLNHLNFSVEKGDFVSIMGPSGSGKSTLLNIIGMFDSLDSGSLTLAGKEVTNLsysQKII 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556496326  78 LRRN-IGYVIQQIGLFPNMTIEENITVVPRMLGWDKARCKTRAEELMDMVALDPHKflNRYPREMSGGQQQRIGVIRALA 156
Cdd:NF038007  80 LRRElIGYIFQSFNLIPHLSIFDNVALPLKYRGVAKKERIERVNQVLNLFGIDNRR--NHKPMQLSGGQQQRVAIARAMV 157

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 556496326 157 ADPPVLLMDEPFGAVDPIN-REVIQNqfLEMQRKLKKTVMLVSHDiDEALKLGDRIAVFRQGKI 219
Cdd:NF038007 158 SNPALLLADEPTGNLDSKNaRAVLQQ--LKYINQKGTTIIMVTHS-DEASTYGNRIINMKDGKL 218
ABC2_perm_RbbA NF033858
ribosome-associated ATPase/putative transporter RbbA;
2-231 9.22e-28

ribosome-associated ATPase/putative transporter RbbA;


Pssm-ID: 468210 [Multi-domain]  Cd Length: 907  Bit Score: 115.22  E-value: 9.22e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556496326   2 IKLENLTKHFSqkhgqTFKAVDNVNLNVPEGEMCVLLGPSGCGKTTTLKMINRLITPSSGTILINGE--DTSGMDTvtlR 79
Cdd:NF033858 267 IEARGLTMRFG-----DFTAVDHVSFRIRRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGEAWLFGQpvDAGDIAT---R 338

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556496326  80 RNIGYVIQQIGLFPNMTIEENITVVPRMLGWDKARCKTRAEELMDMVALDPHkfLNRYPREMSGGQQQRIgvirALAA-- 157
Cdd:NF033858 339 RRVGYMSQAFSLYGELTVRQNLELHARLFHLPAAEIAARVAEMLERFDLADV--ADALPDSLPLGIRQRL----SLAVav 412

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 556496326 158 --DPPVLLMDEPFGAVDPINREVIQNQFLEMQRKLKKTVMLVSHDIDEALKLgDRIAVFRQGKIVQCASPDELLAK 231
Cdd:NF033858 413 ihKPELLILDEPTSGVDPVARDMFWRLLIELSREDGVTIFISTHFMNEAERC-DRISLMHAGRVLASDTPAALVAA 487
AztA NF040873
zinc ABC transporter ATP-binding protein AztA;
21-205 2.13e-25

zinc ABC transporter ATP-binding protein AztA;


Pssm-ID: 468810 [Multi-domain]  Cd Length: 191  Bit Score: 101.54  E-value: 2.13e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556496326  21 AVDNVNLNVPEGEMCVLLGPSGCGKTTTLKMINRLITPSSGTIlingedtsgmdTVTLRRNIGYVIQQIGL---FPnMTI 97
Cdd:NF040873   7 VLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTV-----------RRAGGARVAYVPQRSEVpdsLP-LTV 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556496326  98 EENITV--VPRMLGWDKARCKTRAEELMDMVALDPHKFLNRYPREMSGGQQQRIGVIRALAADPPVLLMDEPFGAVDPIN 175
Cdd:NF040873  75 RDLVAMgrWARRGLWRRLTRDDRAAVDDALERVGLADLAGRQLGELSGGQRQRALLAQGLAQEADLLLLDEPTTGLDAES 154

                        170       180       190
                 ....*....|....*....|....*....|
gi 556496326 176 REVIqNQFLEMQRKLKKTVMLVSHDIDEAL 205
Cdd:NF040873 155 RERI-IALLAEEHARGATVVVVTHDLELVR 183
ABC2_perm_RbbA NF033858
ribosome-associated ATPase/putative transporter RbbA;
2-231 5.18e-21

ribosome-associated ATPase/putative transporter RbbA;


Pssm-ID: 468210 [Multi-domain]  Cd Length: 907  Bit Score: 94.81  E-value: 5.18e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556496326   2 IKLENLTKHFsqkhGQTfKAVDNVNLNVPEGEMCVLLGPSGCGKTTTLKMIN--RLItpSSGTILINGEDtsgMDTVTLR 79
Cdd:NF033858   2 ARLEGVSHRY----GKT-VALDDVSLDIPAGCMVGLIGPDGVGKSSLLSLIAgaRKI--QQGRVEVLGGD---MADARHR 71

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556496326  80 RN----IGYVIQQIG--LFPNMTIEENITVVPRMLGWDKARCKTRAEELMDMVALDPhkFLNRYPREMSGGQQQRIGVIR 153
Cdd:NF033858  72 RAvcprIAYMPQGLGknLYPTLSVFENLDFFGRLFGQDAAERRRRIDELLRATGLAP--FADRPAGKLSGGMKQKLGLCC 149

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556496326 154 ALAADPPVLLMDEPFGAVDPINReviqNQFLEMQRKLKK-----TVMLVSHDIDEALKLgDRIAVFRQGKIVQCASPDEL 228
Cdd:NF033858 150 ALIHDPDLLILDEPTTGVDPLSR----RQFWELIDRIRAerpgmSVLVATAYMEEAERF-DWLVAMDAGRVLATGTPAEL 224


                 ...
gi 556496326 229 LAK 231
Cdd:NF033858 225 LAR 227
40850658_otr NF000106
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
2-231 1.68e-16

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


Pssm-ID: 411078 [Multi-domain]  Cd Length: 351  Bit Score: 79.78  E-value: 1.68e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556496326   2 IKLENLTKHFSQkhgqtFKAVDNVNLNVPEGEMCVLLGPSGCGKTttlkminRLITPSSgtilINGED---------TSG 72
Cdd:NF000106  14 VEVRGLVKHFGE-----VKAVDGVDLDVREGTVLGVLGP*GAA**-------RGALPAH----V*GPDagrrpwrf*TWC 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556496326  73 MDTVTLRRNIG-YVIQQIGLFPNMTIEENITVVPRMLGWDKARCKTRAEELMDMVALDphKFLNRYPREMSGGQQQRIGV 151
Cdd:NF000106  78 ANRRALRRTIG*HRPVR*GRRESFSGRENLYMIGR*LDLSRKDARARADELLERFSLT--EAAGRAAAKYSGGMRRRLDL 155

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556496326 152 IRALAADPPVLLMDEPFGAVDPINREVIQNQFLEMQRKlKKTVMLVSHDIDEALKLGDRIAVFRQGKIVQCASPDELLAK 231
Cdd:NF000106 156 AASMIGRPAVLYLDEPTTGLDPRTRNEVWDEVRSMVRD-GATVLLTTQYMEEAEQLAHELTVIDRGRVIADGKVDELKTK 234
GguA NF040905
sugar ABC transporter ATP-binding protein;
18-221 3.47e-14

sugar ABC transporter ATP-binding protein;


Pssm-ID: 468840 [Multi-domain]  Cd Length: 500  Bit Score: 73.67  E-value: 3.47e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556496326  18 TF---KAVDNVNLNVPEGEMCVLLGPSGCGKTTTLKMINRlITPS---SGTILINGEdtsgmdtVTLRRNI------GYV 85
Cdd:NF040905  10 TFpgvKALDDVNLSVREGEIHALCGENGAGKSTLMKVLSG-VYPHgsyEGEILFDGE-------VCRFKDIrdsealGIV 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556496326  86 I--QQIGLFPNMTIEENItvvprMLG----------WDKARckTRAEELMDMVALDPHkflnryPREMSG----GQQQRI 149
Cdd:NF040905  82 IihQELALIPYLSIAENI-----FLGnerakrgvidWNETN--RRARELLAKVGLDES------PDTLVTdigvGKQQLV 148

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 556496326 150 GVIRALAADPPVLLMDEPFGAvdpINREVIQNqFLEMQRKLKK---TVMLVSHDIDEALKLGDRIAVFRQGKIVQ 221
Cdd:NF040905 149 EIAKALSKDVKLLILDEPTAA---LNEEDSAA-LLDLLLELKAqgiTSIIISHKLNEIRRVADSITVLRDGRTIE 219
COG3448 COG3448
CBS-domain-containing membrane protein [Signal transduction mechanisms];
265-367 6.66e-12

CBS-domain-containing membrane protein [Signal transduction mechanisms];


Pssm-ID: 442671 [Multi-domain]  Cd Length: 136  Bit Score: 62.58  E-value: 6.66e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556496326 265 ITVRGSTPLPEAFATMDDNDIRAITVVDEHGKPLGFVKRREARNASG--------------TCADILHPFRMTGKAEDNL 330
Cdd:COG3448   13 VTVSPDTTLREALELMREHGIRGLPVVDEDGRLVGIVTERDLLRALLpdrldeleerlldlPVEDVMTRPVVTVTPDTPL 92

                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 556496326 331 RVVLSRLYESNTSWMPIVDEDGRYNGEISQDYIAEYL 367
Cdd:COG3448   93 EEAAELMLEHGIHRLPVVDDDGRLVGIVTRTDLLRAL 129
AAA smart00382
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ...
 32-216 6.57e-10

ATPases associated with a variety of cellular activities; AAA - ATPases associated with a variety of cellular activities. This profile/alignment only detects a fraction of this vast family. The poorly conserved N-terminal helix is missing from the alignment.


Pssm-ID: 214640 [Multi-domain]  Cd Length: 148  Bit Score: 57.00  E-value: 6.57e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556496326    32 GEMCVLLGPSGCGKTTTLKMINRLITPSSGT-ILINGEDTSGMDTVTLRrnigyviqqiglfpnmtieenitvvprmlgw 110
Cdd:smart00382   2 GEVILIVGPPGSGKTTLARALARELGPPGGGvIYIDGEDILEEVLDQLL------------------------------- 50

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556496326   111 dkarcktraeelmdmvaldpHKFLNRYPREMSGGQQQRIGVIRALAADPPVLLMDEPFGAVDPINREVIQ-----NQFLE 185
Cdd:smart00382  51 --------------------LIIVGGKKASGSGELRLRLALALARKLKPDVLILDEITSLLDAEQEALLLlleelRLLLL 110

                          170       180       190
                   ....*....|....*....|....*....|.
gi 556496326   186 MQRKLKKTVMLVSHDIDEALKLGDRIAVFRQ 216
Cdd:smart00382 111 LKSEKNLTVILTTNDEKDLGPALLRRRFDRR 141
GguA NF040905
sugar ABC transporter ATP-binding protein;
20-220 3.30e-06

sugar ABC transporter ATP-binding protein;


Pssm-ID: 468840 [Multi-domain]  Cd Length: 500  Bit Score: 49.02  E-value: 3.30e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556496326  20 KAVDNVNLNVPEGEMCVLLGPSGCGKTTtLKM------INRLItpsSGTILINGEDtsgMDTVTLRRNIG----YVIQ-- 87
Cdd:NF040905 274 KVVDDVSLNVRRGEIVGIAGLMGAGRTE-LAMsvfgrsYGRNI---SGTVFKDGKE---VDVSTVSDAIDaglaYVTEdr 346

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556496326  88 -QIGLFPNMTIEENITVvPRMLGWDKARCKTRAEELMdmVALDPHKFLN-RYP------REMSGGQQQRIGVIRALAADP 159
Cdd:NF040905 347 kGYGLNLIDDIKRNITL-ANLGKVSRRGVIDENEEIK--VAEEYRKKMNiKTPsvfqkvGNLSGGNQQKVVLSKWLFTDP 423

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556496326 160 PVLLMDEPFGAVDP---------INREVIQNqflemqrklkKTVMLVSHDIDEALKLGDRIAVFRQGKIV 220
Cdd:NF040905 424 DVLILDEPTRGIDVgakyeiytiINELAAEG----------KGVIVISSELPELLGMCDRIYVMNEGRIT 483
CBS pfam00571
CBS domain; CBS domains are small intracellular modules that pair together to form a stable ...
 325-369 6.53e-03

CBS domain; CBS domains are small intracellular modules that pair together to form a stable globular domain. This family represents a single CBS domain. Pairs of these domains have been termed a Bateman domain. CBS domains have been shown to bind ligands with an adenosyl group such as AMP, ATP and S-AdoMet. CBS domains are found attached to a wide range of other protein domains suggesting that CBS domains may play a regulatory role making proteins sensitive to adenosyl carrying ligands. The region containing the CBS domains in Cystathionine-beta synthase is involved in regulation by S-AdoMet. CBS domain pairs from AMPK bind AMP or ATP. The CBS domains from IMPDH and the chloride channel CLC2 bind ATP.


Pssm-ID: 425756 [Multi-domain]  Cd Length: 57  Bit Score: 34.50  E-value: 6.53e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 556496326  325 KAEDNLRVVLSRLYESNTSWMPIVDEDGRYNGEISQDYIAEYLSS 369
Cdd:pfam00571  13 SPDTTLEEALELMREHGISRLPVVDEDGKLVGIVTLKDLLRALLG 57
 
Name Accession Description Interval E-value
OpuBA COG1125
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and ...
 1-311 0e+00

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


Pssm-ID: 440742 [Multi-domain]  Cd Length: 306  Bit Score: 548.54  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556496326   1 MIKLENLTKHFsqkhGQTFKAVDNVNLNVPEGEMCVLLGPSGCGKTTTLKMINRLITPSSGTILINGEDTSGMDTVTLRR 80
Cdd:COG1125    1 MIEFENVTKRY----PDGTVAVDDLSLTIPAGEFTVLVGPSGCGKTTTLRMINRLIEPTSGRILIDGEDIRDLDPVELRR 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556496326  81 NIGYVIQQIGLFPNMTIEENITVVPRMLGWDKARCKTRAEELMDMVALDPHKFLNRYPREMSGGQQQRIGVIRALAADPP 160
Cdd:COG1125   77 RIGYVIQQIGLFPHMTVAENIATVPRLLGWDKERIRARVDELLELVGLDPEEYRDRYPHELSGGQQQRVGVARALAADPP 156

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556496326 161 VLLMDEPFGAVDPINREVIQNQFLEMQRKLKKTVMLVSHDIDEALKLGDRIAVFRQGKIVQCASPDELLAKPANEFVGSF 240
Cdd:COG1125  157 ILLMDEPFGALDPITREQLQDELLRLQRELGKTIVFVTHDIDEALKLGDRIAVMREGRIVQYDTPEEILANPANDFVADF 236

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 556496326 241 VGQDRTLKRLLLVSAGDVTDQQPtITVRGSTPLPEAFATMDDNDIRAITVVDEHGKPLGFVKRREARNASG 311
Cdd:COG1125  237 VGADRGLRRLSLLRVEDLMLPEP-PTVSPDASLREALSLMLERGVDWLLVVDEDGRPLGWLTLEDLLRALA 306
ABC_OpuCA_Osmoprotection cd03295
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ...
 2-247 1.72e-143

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: 406.69  E-value: 1.72e-143
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556496326   2 IKLENLTKHFsqkhGQTFKAVDNVNLNVPEGEMCVLLGPSGCGKTTTLKMINRLITPSSGTILINGEDTSGMDTVTLRRN 81
Cdd:cd03295    1 IEFENVTKRY----GGGKKAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGEDIREQDPVELRRK 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556496326  82 IGYVIQQIGLFPNMTIEENITVVPRMLGWDKARCKTRAEELMDMVALDPHKFLNRYPREMSGGQQQRIGVIRALAADPPV 161
Cdd:cd03295   77 IGYVIQQIGLFPHMTVEENIALVPKLLKWPKEKIRERADELLALVGLDPAEFADRYPHELSGGQQQRVGVARALAADPPL 156

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556496326 162 LLMDEPFGAVDPINREVIQNQFLEMQRKLKKTVMLVSHDIDEALKLGDRIAVFRQGKIVQCASPDELLAKPANEFVGSFV 241
Cdd:cd03295  157 LLMDEPFGALDPITRDQLQEEFKRLQQELGKTIVFVTHDIDEAFRLADRIAIMKNGEIVQVGTPDEILRSPANDFVAEFV 236


                 ....*.
gi 556496326 242 GQDRTL 247
Cdd:cd03295  237 GADRLL 242
ProV COG4175
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and ...
 1-361 7.82e-110

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


Pssm-ID: 443334 [Multi-domain]  Cd Length: 389  Bit Score: 326.68  E-value: 7.82e-110
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556496326   1 MIKLENLTKHFSQKHGQTFK-------------------AVDNVNLNVPEGEMCVLLGPSGCGKTTTLKMINRLITPSSG 61
Cdd:COG4175    3 KIEVRNLYKIFGKRPERALKlldqgkskdeilektgqtvGVNDASFDVEEGEIFVIMGLSGSGKSTLVRCLNRLIEPTAG 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556496326  62 TILINGEDTSGMDTVTL----RRNIGYVIQQIGLFPNMTIEENITVVPRMLGWDKARCKTRAEELMDMVALDPHKflNRY 137
Cdd:COG4175   83 EVLIDGEDITKLSKKELrelrRKKMSMVFQHFALLPHRTVLENVAFGLEIQGVPKAERRERAREALELVGLAGWE--DSY 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556496326 138 PREMSGGQQQRIGVIRALAADPPVLLMDEPFGAVDPINREVIQNQFLEMQRKLKKTVMLVSHDIDEALKLGDRIAVFRQG 217
Cdd:COG4175  161 PDELSGGMQQRVGLARALATDPDILLMDEAFSALDPLIRREMQDELLELQAKLKKTIVFITHDLDEALRLGDRIAIMKDG 240

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556496326 218 KIVQCASPDELLAKPANEFVGSFV-GQDRTlkRLLlvSAGDVTdQQPTITVRGSTPLPEAFATMDDNDIRAITVVDEHGK 296
Cdd:COG4175  241 RIVQIGTPEEILTNPANDYVADFVeDVDRS--KVL--TAGSVM-RPPEAVVSEKDGPRVALRRMREEGISSLYVVDRDRR 315

                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 556496326 297 PLGFVKRREARNASGTCADILHPFRMTG---KAEDNLRVVLSRLYESNTSwMPIVDEDGRYNGEISQD 361
Cdd:COG4175  316 LLGVVTADDALEAVKGEKDLEEILLTDVptvSPDTPLRDLLPLVAESPYP-LAVVDEDGRLLGVISRG 382
proV TIGR01186
glycine betaine/L-proline transport ATP binding subunit; This model describes the glycine ...
 20-360 5.33e-108

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: 321.42  E-value: 5.33e-108
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556496326   20 KAVDNVNLNVPEGEMCVLLGPSGCGKTTTLKMINRLITPSSGTILINGEDTSGMDTVTL----RRNIGYVIQQIGLFPNM 95
Cdd:TIGR01186   7 KGVNDADLAIAKGEIFVIMGLSGSGKSTTVRMLNRLIEPTAGQIFIDGENIMKQSPVELrevrRKKIGMVFQQFALFPHM 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556496326   96 TIEENITVVPRMLGWDKARCKTRAEELMDMVALDphKFLNRYPREMSGGQQQRIGVIRALAADPPVLLMDEPFGAVDPIN 175
Cdd:TIGR01186  87 TILQNTSLGPELLGWPEQERKEKALELLKLVGLE--EYEHRYPDELSGGMQQRVGLARALAAEPDILLMDEAFSALDPLI 164

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556496326  176 REVIQNQFLEMQRKLKKTVMLVSHDIDEALKLGDRIAVFRQGKIVQCASPDELLAKPANEFVGSFVGQDRTLKRLllvSA 255
Cdd:TIGR01186 165 RDSMQDELKKLQATLQKTIVFITHDLDEAIRIGDRIVIMKAGEIVQVGTPDEILRNPANEYVEEFIGKVDLSQVF---DA 241

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556496326  256 GDVTDQQPT--ITVRGSTPLPEAFATMDDNDIRAITVVDEHGKPLGFVK---RREARNASGTCADILHPFRMTGKAEDNL 330
Cdd:TIGR01186 242 ERIAQRMNTgpITKTADKGPRSALQLMRDERVDSLYVVDRQNKLVGVVDvesIKQARKKAQGLQDVLIDDIYTVDAGTLL 321

                         330       340       350
                  ....*....|....*....|....*....|
gi 556496326  331 RVVLSRLYESNTSwMPIVDEDGRYNGEISQ 360
Cdd:TIGR01186 322 RETVRKVLKAGIK-VPVVDEDQRLVGIVTR 350
PotA COG3842
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ...
 1-243 3.80e-100

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


Pssm-ID: 443052 [Multi-domain]  Cd Length: 353  Bit Score: 300.86  E-value: 3.80e-100
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556496326   1 MIKLENLTKHFSQkhgqtFKAVDNVNLNVPEGEMCVLLGPSGCGKTTTLKMINRLITPSSGTILINGEDTSGMdtVTLRR 80
Cdd:COG3842    5 ALELENVSKRYGD-----VTALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRILLDGRDVTGL--PPEKR 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556496326  81 NIGYVIQQIGLFPNMTIEENITVVPRMLGWDKARCKTRAEELMDMVALDphKFLNRYPREMSGGQQQRIGVIRALAADPP 160
Cdd:COG3842   78 NVGMVFQDYALFPHLTVAENVAFGLRMRGVPKAEIRARVAELLELVGLE--GLADRYPHQLSGGQQQRVALARALAPEPR 155

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556496326 161 VLLMDEPFGAVDPINREVIQNQFLEMQRKLKKTVMLVSHDIDEALKLGDRIAVFRQGKIVQCASPDELLAKPANEFVGSF 240
Cdd:COG3842  156 VLLLDEPLSALDAKLREEMREELRRLQRELGITFIYVTHDQEEALALADRIAVMNDGRIEQVGTPEEIYERPATRFVADF 235


                 ...
gi 556496326 241 VGQ 243
Cdd:COG3842  236 IGE 238
ABC_Pro_Gly_Betaine cd03294
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ...
 2-246 3.61e-91

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: 274.91  E-value: 3.61e-91
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556496326   2 IKLENLTKHFSQKHGQTFK-------------------AVDNVNLNVPEGEMCVLLGPSGCGKTTTLKMINRLITPSSGT 62
Cdd:cd03294    1 IKIKGLYKIFGKNPQKAFKllakgkskeeilkktgqtvGVNDVSLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGK 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556496326  63 ILINGEDTSGMDTVTL----RRNIGYVIQQIGLFPNMTIEENITVVPRMLGWDKARCKTRAEELMDMVALdpHKFLNRYP 138
Cdd:cd03294   81 VLIDGQDIAAMSRKELrelrRKKISMVFQSFALLPHRTVLENVAFGLEVQGVPRAEREERAAEALELVGL--EGWEHKYP 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556496326 139 REMSGGQQQRIGVIRALAADPPVLLMDEPFGAVDPINREVIQNQFLEMQRKLKKTVMLVSHDIDEALKLGDRIAVFRQGK 218
Cdd:cd03294  159 DELSGGMQQRVGLARALAVDPDILLMDEAFSALDPLIRREMQDELLRLQAELQKTIVFITHDLDEALRLGDRIAIMKDGR 238

                        250       260
                 ....*....|....*....|....*....
gi 556496326 219 IVQCASPDELLAKPANEFVGSFV-GQDRT 246
Cdd:cd03294  239 LVQVGTPEEILTNPANDYVREFFrGVDRA 267
ABC_Carb_Solutes_like cd03259
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ...
 2-223 4.75e-91

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: 272.47  E-value: 4.75e-91
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556496326   2 IKLENLTKHFSQKHgqtfkAVDNVNLNVPEGEMCVLLGPSGCGKTTTLKMINRLITPSSGTILINGEDTSGMDTVtlRRN 81
Cdd:cd03259    1 LELKGLSKTYGSVR-----ALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDGRDVTGVPPE--RRN 73

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556496326  82 IGYVIQQIGLFPNMTIEENITVVPRMLGWDKARCKTRAEELMDMVALDPHkfLNRYPREMSGGQQQRIGVIRALAADPPV 161
Cdd:cd03259   74 IGMVFQDYALFPHLTVAENIAFGLKLRGVPKAEIRARVRELLELVGLEGL--LNRYPHELSGGQQQRVALARALAREPSL 151

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 556496326 162 LLMDEPFGAVDPINREVIQNQFLEMQRKLKKTVMLVSHDIDEALKLGDRIAVFRQGKIVQCA 223
Cdd:cd03259  152 LLLDEPLSALDAKLREELREELKELQRELGITTIYVTHDQEEALALADRIAVMNEGRIVQVG 213
TauB COG1116
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ...
 1-220 1.08e-89

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


Pssm-ID: 440733 [Multi-domain]  Cd Length: 260  Bit Score: 270.81  E-value: 1.08e-89
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556496326   1 MIKLENLTKHFSQKHGqTFKAVDNVNLNVPEGEMCVLLGPSGCGKTTTLKMINRLITPSSGTILINGEDTSGmdtvtLRR 80
Cdd:COG1116    7 ALELRGVSKRFPTGGG-GVTALDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPTSGEVLVDGKPVTG-----PGP 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556496326  81 NIGYVIQQIGLFPNMTIEENITVVPRMLGWDKARCKTRAEELMDMVALDphKFLNRYPREMSGGQQQRIGVIRALAADPP 160
Cdd:COG1116   81 DRGVVFQEPALLPWLTVLDNVALGLELRGVPKAERRERARELLELVGLA--GFEDAYPHQLSGGMRQRVAIARALANDPE 158

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 556496326 161 VLLMDEPFGAVDPINREVIQNQFLEMQRKLKKTVMLVSHDIDEALKLGDRIAVF--RQGKIV 220
Cdd:COG1116  159 VLLMDEPFGALDALTRERLQDELLRLWQETGKTVLFVTHDVDEAVFLADRVVVLsaRPGRIV 220
MalK COG3839
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ...
 1-242 4.98e-89

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


Pssm-ID: 443050 [Multi-domain]  Cd Length: 352  Bit Score: 272.33  E-value: 4.98e-89
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556496326   1 MIKLENLTKHFSQkhgqtFKAVDNVNLNVPEGEMCVLLGPSGCGKTTTLKMINRLITPSSGTILINGEDTSGMDTVtlRR 80
Cdd:COG3839    3 SLELENVSKSYGG-----VEALKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAGLEDPTSGEILIGGRDVTDLPPK--DR 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556496326  81 NIGYVIQQIGLFPNMTIEENITVVPRMLGWDKARCKTRAEELMDMVALDPhkFLNRYPREMSGGQQQRIGVIRALAADPP 160
Cdd:COG3839   76 NIAMVFQSYALYPHMTVYENIAFPLKLRKVPKAEIDRRVREAAELLGLED--LLDRKPKQLSGGQRQRVALGRALVREPK 153

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556496326 161 VLLMDEPFGAVDPINREVIQNQFLEMQRKLKKTVMLVSHDIDEALKLGDRIAVFRQGKIVQCASPDELLAKPANEFVGSF 240
Cdd:COG3839  154 VFLLDEPLSNLDAKLRVEMRAEIKRLHRRLGTTTIYVTHDQVEAMTLADRIAVMNDGRIQQVGTPEELYDRPANLFVAGF 233


                 ..
gi 556496326 241 VG 242
Cdd:COG3839  234 IG 235
ABC_NrtD_SsuB_transporters cd03293
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ...
 2-221 1.11e-87

ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ATP-binding subunits of the bacterial ABC-type nitrate and sulfonate transport systems, respectively. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.


Pssm-ID: 213260 [Multi-domain]  Cd Length: 220  Bit Score: 264.33  E-value: 1.11e-87
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556496326   2 IKLENLTKHFSQKhGQTFKAVDNVNLNVPEGEMCVLLGPSGCGKTTTLKMINRLITPSSGTILINGEDTSGmdtvtLRRN 81
Cdd:cd03293    1 LEVRNVSKTYGGG-GGAVTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVDGEPVTG-----PGPD 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556496326  82 IGYVIQQIGLFPNMTIEENITVVPRMLGWDKARCKTRAEELMDMVALDphKFLNRYPREMSGGQQQRIGVIRALAADPPV 161
Cdd:cd03293   75 RGYVFQQDALLPWLTVLDNVALGLELQGVPKAEARERAEELLELVGLS--GFENAYPHQLSGGMRQRVALARALAVDPDV 152

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 556496326 162 LLMDEPFGAVDPINREVIQNQFLEMQRKLKKTVMLVSHDIDEALKLGDRIAVF--RQGKIVQ 221
Cdd:cd03293  153 LLLDEPFSALDALTREQLQEELLDIWRETGKTVLLVTHDIDEAVFLADRVVVLsaRPGRIVA 214
CysA COG1118
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ...
 2-242 1.28e-87

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


Pssm-ID: 440735 [Multi-domain]  Cd Length: 348  Bit Score: 268.55  E-value: 1.28e-87
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556496326   2 IKLENLTKHFSQkhgqtFKAVDNVNLNVPEGEMCVLLGPSGCGKTTTLKMINRLITPSSGTILINGEDTSGmDTVTLRRN 81
Cdd:COG1118    3 IEVRNISKRFGS-----FTLLDDVSLEIASGELVALLGPSGSGKTTLLRIIAGLETPDSGRIVLNGRDLFT-NLPPRERR 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556496326  82 IGYVIQQIGLFPNMTIEENITVVPRMLGWDKARCKTRAEELMDMVALDphKFLNRYPREMSGGQQQRIGVIRALAADPPV 161
Cdd:COG1118   77 VGFVFQHYALFPHMTVAENIAFGLRVRPPSKAEIRARVEELLELVQLE--GLADRYPSQLSGGQRQRVALARALAVEPEV 154

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556496326 162 LLMDEPFGAVDPINREVIQNQFLEMQRKLKKTVMLVSHDIDEALKLGDRIAVFRQGKIVQCASPDELLAKPANEFVGSFV 241
Cdd:COG1118  155 LLLDEPFGALDAKVRKELRRWLRRLHDELGGTTVFVTHDQEEALELADRVVVMNQGRIEQVGTPDEVYDRPATPFVARFL 234


                 .
gi 556496326 242 G 242
Cdd:COG1118  235 G 235
ABC_PotA_N cd03300
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ...
 2-242 7.54e-83

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: 252.16  E-value: 7.54e-83
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556496326   2 IKLENLTKHFSQkhgqtFKAVDNVNLNVPEGEMCVLLGPSGCGKTTTLKMINRLITPSSGTILINGEDTSGMDTvtLRRN 81
Cdd:cd03300    1 IELENVSKFYGG-----FVALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGKDITNLPP--HKRP 73

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556496326  82 IGYVIQQIGLFPNMTIEENITVVPRMLGWDKARCKTRAEELMDMVALDPHKflNRYPREMSGGQQQRIGVIRALAADPPV 161
Cdd:cd03300   74 VNTVFQNYALFPHLTVFENIAFGLRLKKLPKAEIKERVAEALDLVQLEGYA--NRKPSQLSGGQQQRVAIARALVNEPKV 151

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556496326 162 LLMDEPFGAVDPINREVIQNQFLEMQRKLKKTVMLVSHDIDEALKLGDRIAVFRQGKIVQCASPDELLAKPANEFVGSFV 241
Cdd:cd03300  152 LLLDEPLGALDLKLRKDMQLELKRLQKELGITFVFVTHDQEEALTMSDRIAVMNKGKIQQIGTPEEIYEEPANRFVADFI 231


                 .
gi 556496326 242 G 242
Cdd:cd03300  232 G 232
ABC_CysA_sulfate_importer cd03296
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ...
 2-243 5.98e-80

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: 245.33  E-value: 5.98e-80
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556496326   2 IKLENLTKHFSQkhgqtFKAVDNVNLNVPEGEMCVLLGPSGCGKTTTLKMINRLITPSSGTILINGEDTSGMDTvtLRRN 81
Cdd:cd03296    3 IEVRNVSKRFGD-----FVALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGGEDATDVPV--QERN 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556496326  82 IGYVIQQIGLFPNMTIEENIT----VVPRMLGWDKARCKTRAEELMDMVALDphKFLNRYPREMSGGQQQRIGVIRALAA 157
Cdd:cd03296   76 VGFVFQHYALFRHMTVFDNVAfglrVKPRSERPPEAEIRAKVHELLKLVQLD--WLADRYPAQLSGGQRQRVALARALAV 153

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556496326 158 DPPVLLMDEPFGAVDPINREVIQNQFLEMQRKLKKTVMLVSHDIDEALKLGDRIAVFRQGKIVQCASPDELLAKPANEFV 237
Cdd:cd03296  154 EPKVLLLDEPFGALDAKVRKELRRWLRRLHDELHVTTVFVTHDQEEALEVADRVVVMNKGRIEQVGTPDEVYDHPASPFV 233


                 ....*.
gi 556496326 238 GSFVGQ 243
Cdd:cd03296  234 YSFLGE 239
GsiA COG1123
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ...
 1-235 1.23e-79

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: 253.29  E-value: 1.23e-79
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556496326   1 MIKLENLTKHFSQKHGQTFKAVDNVNLNVPEGEMCVLLGPSGCGKTTTLKMINRLITPSSGTILINGEDTSGM---DTVT 77
Cdd:COG1123  260 LLEVRNLSKRYPVRGKGGVRAVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRPTSGSILFDGKDLTKLsrrSLRE 339

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556496326  78 LRRNIGYVIQ----QigLFPNMTIEENITVVPRMLGW-DKARCKTRAEELMDMVALDPHkFLNRYPREMSGGQQQRIGVI 152
Cdd:COG1123  340 LRRRVQMVFQdpysS--LNPRMTVGDIIAEPLRLHGLlSRAERRERVAELLERVGLPPD-LADRYPHELSGGQRQRVAIA 416

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556496326 153 RALAADPPVLLMDEPFGAVDPINREVIQNQFLEMQRKLKKTVMLVSHDIDEALKLGDRIAVFRQGKIVQCASPDELLAKP 232
Cdd:COG1123  417 RALALEPKLLILDEPTSALDVSVQAQILNLLRDLQRELGLTYLFISHDLAVVRYIADRVAVMYDGRIVEDGPTEEVFANP 496


                 ...
gi 556496326 233 ANE 235
Cdd:COG1123  497 QHP 499
CcmA COG1131
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
2-231 7.68e-79

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


Pssm-ID: 440746 [Multi-domain]  Cd Length: 236  Bit Score: 242.28  E-value: 7.68e-79
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556496326   2 IKLENLTKHFSQKHgqtfkAVDNVNLNVPEGEMCVLLGPSGCGKTTTLKMINRLITPSSGTILINGEDTSGmDTVTLRRN 81
Cdd:COG1131    1 IEVRGLTKRYGDKT-----ALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRVLGEDVAR-DPAEVRRR 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556496326  82 IGYVIQQIGLFPNMTIEENITVVPRMLGWDKARCKTRAEELMDMVALDPHKflNRYPREMSGGQQQRIGVIRALAADPPV 161
Cdd:COG1131   75 IGYVPQEPALYPDLTVRENLRFFARLYGLPRKEARERIDELLELFGLTDAA--DRKVGTLSGGMKQRLGLALALLHDPEL 152

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556496326 162 LLMDEPFGAVDPINREVIQNQFLEMQRKlKKTVMLVSHDIDEALKLGDRIAVFRQGKIVQCASPDELLAK 231
Cdd:COG1131  153 LILDEPTSGLDPEARRELWELLRELAAE-GKTVLLSTHYLEEAERLCDRVAIIDKGRIVADGTPDELKAR 221
ABC_choXWV_ATP TIGR03415
choline ABC transporter, ATP-binding protein; Members of this protein family are the ...
 21-367 1.32e-75

choline ABC transporter, ATP-binding protein; Members of this protein family are the ATP-binding subunit of a three-protein transporter. This family belongs, more broadly, to the family of proline and glycine-betaine transporters, but members have been identified by direct characterization and by bioinformatic means as choline transporters. Many species have several closely-related members of this family, probably with variable abilities to act additionally on related quaternary amines. [Transport and binding proteins, Amino acids, peptides and amines]


Pssm-ID: 188317 [Multi-domain]  Cd Length: 382  Bit Score: 238.91  E-value: 1.32e-75
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556496326   21 AVDNVNLNVPEGEMCVLLGPSGCGKTTTLKMINRLITPSSGTILINGEDTS----GMDTVTLRR----NIGYVIQQIGLF 92
Cdd:TIGR03415  39 GVHNASLDIEEGEICVLMGLSGSGKSTLLRAVNGLNPVSRGSVLVKDGDGSvdvaNCDAATLRRlrthRVSMVFQQFALL 118

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556496326   93 PNMTIEENITVVPRMLGWDKARCKTRAEELMDMVALDphKFLNRYPREMSGGQQQRIGVIRALAADPPVLLMDEPFGAVD 172
Cdd:TIGR03415 119 PWRTVEENVAFGLEMQGMPKAERRKRVDEQLELVGLA--QWADRKPGELSGGMQQRVGLARAFATEAPILLMDEPFSALD 196

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556496326  173 PINREVIQNQFLEMQRKLKKTVMLVSHDIDEALKLGDRIAVFRQGKIVQCASPDELLAKPANEFVGSFVGQDRTLKRLLl 252
Cdd:TIGR03415 197 PLIRTQLQDELLELQSKLKKTIVFVSHDLDEALKIGNRIAIMEGGRIIQHGTPEEIVLNPANDYVADFVAHTNPLNVLT- 275

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556496326  253 vsAGDV-TDQQPTITVRGSTPLPEAFATMDDNDIRAitvVDEHGKPLGFvkrreARNASGTCADILHPFRMTGKAEDNLR 331
Cdd:TIGR03415 276 --ARDLmRPLTTLEKVDGEWCVSKRYDTWLKTADKQ---VRRAAAGLPV-----AAWAAEQEVESLEKLPTVINPDTPMR 345

                         330       340       350
                  ....*....|....*....|....*....|....*.
gi 556496326  332 VVLSRLYESNTSwmPIVDEDGRYNGEISQDYIAEYL 367
Cdd:TIGR03415 346 DVLAARHRTGGA--ILLVENGRIVGVIGDQNIYHAL 379
PhnT2 TIGR03265
putative 2-aminoethylphosphonate ABC transporter, ATP-binding protein; This ABC transporter ...
 2-248 4.10e-74

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: 234.16  E-value: 4.10e-74
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556496326    2 IKLENLTKHFSQkhgqtFKAVDNVNLNVPEGEMCVLLGPSGCGKTTTLKMINRLITPSSGTILINGEDTSgmDTVTLRRN 81
Cdd:TIGR03265   5 LSIDNIRKRFGA-----FTALKDISLSVKKGEFVCLLGPSGCGKTTLLRIIAGLERQTAGTIYQGGRDIT--RLPPQKRD 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556496326   82 IGYVIQQIGLFPNMTIEENITV--VPRmlGWDKARCKTRAEELMDMVALDPHKflNRYPREMSGGQQQRIGVIRALAADP 159
Cdd:TIGR03265  78 YGIVFQSYALFPNLTVADNIAYglKNR--GMGRAEVAERVAELLDLVGLPGSE--RKYPGQLSGGQQQRVALARALATSP 153

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556496326  160 PVLLMDEPFGAVDPINREVIQNQFLEMQRKLKKTVMLVSHDIDEALKLGDRIAVFRQGKIVQCASPDELLAKPANEFVGS 239
Cdd:TIGR03265 154 GLLLLDEPLSALDARVREHLRTEIRQLQRRLGVTTIMVTHDQEEALSMADRIVVMNHGVIEQVGTPQEIYRHPATPFVAD 233


                  ....*....
gi 556496326  240 FVGQDRTLK 248
Cdd:TIGR03265 234 FVGEVNWLP 242
MlaF COG1127
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ...
 1-241 4.19e-74

ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 440744 [Multi-domain]  Cd Length: 241  Bit Score: 230.25  E-value: 4.19e-74
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556496326   1 MIKLENLTKHFSQKHgqtfkAVDNVNLNVPEGEMCVLLGPSGCGKTTTLKMINRLITPSSGTILINGEDTSGMDT---VT 77
Cdd:COG1127    5 MIEVRNLTKSFGDRV-----VLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEILVDGQDITGLSEkelYE 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556496326  78 LRRNIGYVIQQIGLFPNMTIEENITVVPRMLG-WDKARCKTRAEELMDMVALDPHKflNRYPREMSGGQQQRIGVIRALA 156
Cdd:COG1127   80 LRRRIGMLFQGGALFDSLTVFENVAFPLREHTdLSEAEIRELVLEKLELVGLPGAA--DKMPSELSGGMRKRVALARALA 157

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556496326 157 ADPPVLLMDEPFGAVDPINREVIQNQFLEMQRKLKKTVMLVSHDIDEALKLGDRIAVFRQGKIVQCASPDELLAKPaNEF 236
Cdd:COG1127  158 LDPEILLYDEPTAGLDPITSAVIDELIRELRDELGLTSVVVTHDLDSAFAIADRVAVLADGKIIAEGTPEELLASD-DPW 236


                 ....*
gi 556496326 237 VGSFV 241
Cdd:COG1127  237 VRQFL 241
ABC_MJ0796_LolCDE_FtsE cd03255
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ...
 2-219 9.87e-74

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: 228.53  E-value: 9.87e-74
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556496326   2 IKLENLTKHFSQKhGQTFKAVDNVNLNVPEGEMCVLLGPSGCGKTTTLKMINRLITPSSGTILINGEDTSGMDTVTL--- 78
Cdd:cd03255    1 IELKNLSKTYGGG-GEKVQALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRVDGTDISKLSEKELaaf 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556496326  79 -RRNIGYVIQQIGLFPNMTIEENITVVPRMLGWDKARCKTRAEELMDMVALDphKFLNRYPREMSGGQQQRIGVIRALAA 157
Cdd:cd03255   80 rRRHIGFVFQSFNLLPDLTALENVELPLLLAGVPKKERRERAEELLERVGLG--DRLNHYPSELSGGQQQRVAIARALAN 157

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 556496326 158 DPPVLLMDEPFGAVDPINREVIQNQFLEMQRKLKKTVMLVSHDIDEAlKLGDRIAVFRQGKI 219
Cdd:cd03255  158 DPKIILADEPTGNLDSETGKEVMELLRELNKEAGTTIVVVTHDPELA-EYADRIIELRDGKI 218
LolD COG1136
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
1-220 4.44e-73

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


Pssm-ID: 440751 [Multi-domain]  Cd Length: 227  Bit Score: 227.23  E-value: 4.44e-73
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556496326   1 MIKLENLTKHFsQKHGQTFKAVDNVNLNVPEGEMCVLLGPSGCGKTTTLKMINRLITPSSGTILINGEDTSGMDTVTL-- 78
Cdd:COG1136    4 LLELRNLTKSY-GTGEGEVTALRGVSLSIEAGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVLIDGQDISSLSERELar 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556496326  79 --RRNIGYVIQQIGLFPNMTIEENITVVPRMLGWDKARCKTRAEELMDMVALDphKFLNRYPREMSGGQQQRIGVIRALA 156
Cdd:COG1136   83 lrRRHIGFVFQFFNLLPELTALENVALPLLLAGVSRKERRERARELLERVGLG--DRLDHRPSQLSGGQQQRVAIARALV 160

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 556496326 157 ADPPVLLMDEPFGAVDPINREVIQNQFLEMQRKLKKTVMLVSHDiDEALKLGDRIAVFRQGKIV 220
Cdd:COG1136  161 NRPKLILADEPTGNLDSKTGEEVLELLRELNRELGTTIVMVTHD-PELAARADRVIRLRDGRIV 223
GlnQ COG1126
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ...
 1-235 7.46e-73

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


Pssm-ID: 440743 [Multi-domain]  Cd Length: 239  Bit Score: 226.80  E-value: 7.46e-73
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556496326   1 MIKLENLTKHFSQKHgqtfkAVDNVNLNVPEGEMCVLLGPSGCGKTTTLKMINRLITPSSGTILINGED--TSGMDTVTL 78
Cdd:COG1126    1 MIEIENLHKSFGDLE-----VLKGISLDVEKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTITVDGEDltDSKKDINKL 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556496326  79 RRNIGYVIQQIGLFPNMTIEENITVVPRM-LGWDKARCKTRAEELMDMVALDPHKflNRYPREMSGGQQQRIGVIRALAA 157
Cdd:COG1126   76 RRKVGMVFQQFNLFPHLTVLENVTLAPIKvKKMSKAEAEERAMELLERVGLADKA--DAYPAQLSGGQQQRVAIARALAM 153

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556496326 158 DPPVLLMDEPFGAVDPIN-REViqnqfLEMQRKLKK---TVMLVSHDIDEALKLGDRIAVFRQGKIVQCASPDELLAKPA 233
Cdd:COG1126  154 EPKVMLFDEPTSALDPELvGEV-----LDVMRDLAKegmTMVVVTHEMGFAREVADRVVFMDGGRIVEEGPPEEFFENPQ 228


                 ..
gi 556496326 234 NE 235
Cdd:COG1126  229 HE 230
3a0106s01 TIGR00968
sulfate ABC transporter, ATP-binding protein; [Transport and binding proteins, Anions]
 2-247 1.75e-72

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


Pssm-ID: 130041 [Multi-domain]  Cd Length: 237  Bit Score: 225.83  E-value: 1.75e-72
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556496326    2 IKLENLTKHFSqkhgqTFKAVDNVNLNVPEGEMCVLLGPSGCGKTTTLKMINRLITPSSGTILINGEDTSGMDTvtLRRN 81
Cdd:TIGR00968   1 IEIANISKRFG-----SFQALDDVNLEVPTGSLVALLGPSGSGKSTLLRIIAGLEQPDSGRIRLNGQDATRVHA--RDRK 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556496326   82 IGYVIQQIGLFPNMTIEENITVVPRMLGWDKARCKTRAEELMDMVALDphKFLNRYPREMSGGQQQRIGVIRALAADPPV 161
Cdd:TIGR00968  74 IGFVFQHYALFKHLTVRDNIAFGLEIRKHPKAKIKARVEELLELVQLE--GLGDRYPNQLSGGQRQRVALARALAVEPQV 151

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556496326  162 LLMDEPFGAVDPINREVIQNQFLEMQRKLKKTVMLVSHDIDEALKLGDRIAVFRQGKIVQCASPDELLAKPANEFVGSFV 241
Cdd:TIGR00968 152 LLLDEPFGALDAKVRKELRSWLRKLHDEVHVTTVFVTHDQEEAMEVADRIVVMSNGKIEQIGSPDEVYDHPANPFVMSFL 231


                  ....*.
gi 556496326  242 GQDRTL 247
Cdd:TIGR00968 232 GEVNVL 237
ABC_Class3 cd03229
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ...
 2-218 5.47e-71

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: 220.14  E-value: 5.47e-71
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556496326   2 IKLENLTKHFSQKHgqtfkAVDNVNLNVPEGEMCVLLGPSGCGKTTTLKMINRLITPSSGTILINGEDTSGMD--TVTLR 79
Cdd:cd03229    1 LELKNVSKRYGQKT-----VLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGEDLTDLEdeLPPLR 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556496326  80 RNIGYVIQQIGLFPNMTIEENITvvprmlgwdkarcktraeelmdmvaldphkflnrYPreMSGGQQQRIGVIRALAADP 159
Cdd:cd03229   76 RRIGMVFQDFALFPHLTVLENIA----------------------------------LG--LSGGQQQRVALARALAMDP 119

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 556496326 160 PVLLMDEPFGAVDPINREVIQNQFLEMQRKLKKTVMLVSHDIDEALKLGDRIAVFRQGK 218
Cdd:cd03229  120 DVLLLDEPTSALDPITRREVRALLKSLQAQLGITVVLVTHDLDEAARLADRVVVLRDGK 178
ABC_ModC_like cd03299
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ...
 2-242 6.20e-69

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: 216.82  E-value: 6.20e-69
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556496326   2 IKLENLTKHFSQkhgqtFKaVDNVNLNVPEGEMCVLLGPSGCGKTTTLKMINRLITPSSGTILINGEDTSGMDTVtlRRN 81
Cdd:cd03299    1 LKVENLSKDWKE-----FK-LKNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNGKDITNLPPE--KRD 72

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556496326  82 IGYVIQQIGLFPNMTIEENITVVPRMLGWDKARCKTRAEELMDMVALDpHkFLNRYPREMSGGQQQRIGVIRALAADPPV 161
Cdd:cd03299   73 ISYVPQNYALFPHMTVYKNIAYGLKKRKVDKKEIERKVLEIAEMLGID-H-LLNRKPETLSGGEQQRVAIARALVVNPKI 150

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556496326 162 LLMDEPFGAVDPINREVIQNQFLEMQRKLKKTVMLVSHDIDEALKLGDRIAVFRQGKIVQCASPDELLAKPANEFVGSFV 241
Cdd:cd03299  151 LLLDEPFSALDVRTKEKLREELKKIRKEFGVTVLHVTHDFEEAWALADKVAIMLNGKLIQVGKPEEVFKKPKNEFVAEFL 230


                 .
gi 556496326 242 G 242
Cdd:cd03299  231 G 231
ABC_Org_Solvent_Resistant cd03261
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ...
 2-240 4.04e-67

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: 211.98  E-value: 4.04e-67
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556496326   2 IKLENLTKHFSQKHgqtfkAVDNVNLNVPEGEMCVLLGPSGCGKTTTLKMINRLITPSSGTILINGEDTSGM---DTVTL 78
Cdd:cd03261    1 IELRGLTKSFGGRT-----VLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGEDISGLseaELYRL 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556496326  79 RRNIGYVIQQIGLFPNMTIEENITVVPRMLG-WDKARCKTRAEELMDMVALDPhkFLNRYPREMSGGQQQRIGVIRALAA 157
Cdd:cd03261   76 RRRMGMLFQSGALFDSLTVFENVAFPLREHTrLSEEEIREIVLEKLEAVGLRG--AEDLYPAELSGGMKKRVALARALAL 153

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556496326 158 DPPVLLMDEPFGAVDPINREVIQNQFLEMQRKLKKTVMLVSHDIDEALKLGDRIAVFRQGKIVQCASPDELLAKPaNEFV 237
Cdd:cd03261  154 DPELLLYDEPTAGLDPIASGVIDDLIRSLKKELGLTSIMVTHDLDTAFAIADRIAVLYDGKIVAEGTPEELRASD-DPLV 232


                 ...
gi 556496326 238 GSF 240
Cdd:cd03261  233 RQF 235
ABC_MalK_N cd03301
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ...
 2-221 4.56e-67

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: 211.34  E-value: 4.56e-67
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556496326   2 IKLENLTKHFSQKhgqtfKAVDNVNLNVPEGEMCVLLGPSGCGKTTTLKMINRLITPSSGTILINGEDTSgmDTVTLRRN 81
Cdd:cd03301    1 VELENVTKRFGNV-----TALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGRDVT--DLPPKDRD 73

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556496326  82 IGYVIQQIGLFPNMTIEENITVVPRMLGWDKARCKTRAEELMDMVALDphKFLNRYPREMSGGQQQRIGVIRALAADPPV 161
Cdd:cd03301   74 IAMVFQNYALYPHMTVYDNIAFGLKLRKVPKDEIDERVREVAELLQIE--HLLDRKPKQLSGGQRQRVALGRAIVREPKV 151

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 556496326 162 LLMDEPFGAVDPINREVIQNQFLEMQRKLKKTVMLVSHDIDEALKLGDRIAVFRQGKIVQ 221
Cdd:cd03301  152 FLMDEPLSNLDAKLRVQMRAELKRLQQRLGTTTIYVTHDQVEAMTMADRIAVMNDGQIQQ 211
ABC_NikE_OppD_transporters cd03257
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ...
 1-220 1.33e-66

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: 210.44  E-value: 1.33e-66
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556496326   1 MIKLENLTKHFSQKHGqTFKAVDNVNLNVPEGEMCVLLGPSGCGKTTTLKMINRLITPSSGTILINGEDTSGMDTVTL-- 78
Cdd:cd03257    1 LLEVKNLSVSFPTGGG-SVKALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGKDLLKLSRRLRki 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556496326  79 -RRNIGYVIQQIG--LFPNMTIEENITVVPRMLG--WDKARCKTRAEELMDMVALDPhKFLNRYPREMSGGQQQRIGVIR 153
Cdd:cd03257   80 rRKEIQMVFQDPMssLNPRMTIGEQIAEPLRIHGklSKKEARKEAVLLLLVGVGLPE-EVLNRYPHELSGGQRQRVAIAR 158

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 556496326 154 ALAADPPVLLMDEPFGAVDPINREVIQNQFLEMQRKLKKTVMLVSHDIDEALKLGDRIAVFRQGKIV 220
Cdd:cd03257  159 ALALNPKLLIADEPTSALDVSVQAQILDLLKKLQEELGLTLLFITHDLGVVAKIADRVAVMYAGKIV 225
NatA COG4555
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ...
 1-235 3.21e-66

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: 210.10  E-value: 3.21e-66
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556496326   1 MIKLENLTKHFSQKHgqtfkAVDNVNLNVPEGEMCVLLGPSGCGKTTTLKMINRLITPSSGTILINGEDtSGMDTVTLRR 80
Cdd:COG4555    1 MIEVENLSKKYGKVP-----ALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIDGED-VRKEPREARR 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556496326  81 NIGYVIQQIGLFPNMTIEENITVVPRMLGWDKARCKTRAEELMDMVALDPhkFLNRYPREMSGGQQQRIGVIRALAADPP 160
Cdd:COG4555   75 QIGVLPDERGLYDRLTVRENIRYFAELYGLFDEELKKRIEELIELLGLEE--FLDRRVGELSTGMKKKVALARALVHDPK 152

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 556496326 161 VLLMDEPFGAVDPINREVIQNQFLEMqRKLKKTVMLVSHDIDEALKLGDRIAVFRQGKIVQCASPDELLAKPANE 235
Cdd:COG4555  153 VLLLDEPTNGLDVMARRLLREILRAL-KKEGKTVLFSSHIMQEVEALCDRVVILHKGKVVAQGSLDELREEIGEE 226
potA PRK09452
spermidine/putrescine ABC transporter ATP-binding protein PotA;
2-243 3.74e-66

spermidine/putrescine ABC transporter ATP-binding protein PotA;


Pssm-ID: 236523 [Multi-domain]  Cd Length: 375  Bit Score: 214.43  E-value: 3.74e-66
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556496326   2 IKLENLTKHFSQKhgqtfKAVDNVNLNVPEGEMCVLLGPSGCGKTTTLKMINRLITPSSGTILINGEDTSGMDTVtlRRN 81
Cdd:PRK09452  15 VELRGISKSFDGK-----EVISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLDGQDITHVPAE--NRH 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556496326  82 IGYVIQQIGLFPNMTIEENITVVPRMLGWDKARCKTRAEELMDMVALDphKFLNRYPREMSGGQQQRIGVIRALAADPPV 161
Cdd:PRK09452  88 VNTVFQSYALFPHMTVFENVAFGLRMQKTPAAEITPRVMEALRMVQLE--EFAQRKPHQLSGGQQQRVAIARAVVNKPKV 165

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556496326 162 LLMDEPFGAVDPINREVIQNQFLEMQRKLKKTVMLVSHDIDEALKLGDRIAVFRQGKIVQCASPDELLAKPANEFVGSFV 241
Cdd:PRK09452 166 LLLDESLSALDYKLRKQMQNELKALQRKLGITFVFVTHDQEEALTMSDRIVVMRDGRIEQDGTPREIYEEPKNLFVARFI 245


                 ..
gi 556496326 242 GQ 243
Cdd:PRK09452 246 GE 247
ABC_MetN_methionine_transporter cd03258
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ...
 1-232 1.87e-64

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: 205.12  E-value: 1.87e-64
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556496326   1 MIKLENLTKHFSQKHGQtFKAVDNVNLNVPEGEMCVLLGPSGCGKTTTLKMINRLITPSSGTILINGED---TSGMDTVT 77
Cdd:cd03258    1 MIELKNVSKVFGDTGGK-VTALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGSVLVDGTDltlLSGKELRK 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556496326  78 LRRNIGYVIQQIGLFPNMTIEENITVVPRMLGWDKARCKTRAEELMDMVALDPHKflNRYPREMSGGQQQRIGVIRALAA 157
Cdd:cd03258   80 ARRRIGMIFQHFNLLSSRTVFENVALPLEIAGVPKAEIEERVLELLELVGLEDKA--DAYPAQLSGGQKQRVGIARALAN 157

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 556496326 158 DPPVLLMDEPFGAVDPINREVIQNQFLEMQRKLKKTVMLVSHDIDEALKLGDRIAVFRQGKIVQCASPDELLAKP 232
Cdd:cd03258  158 NPKVLLCDEATSALDPETTQSILALLRDINRELGLTIVLITHEMEVVKRICDRVAVMEKGEVVEEGTVEEVFANP 232
EcfA2 COG1122
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ...
 2-232 2.18e-64

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: 204.87  E-value: 2.18e-64
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556496326   2 IKLENLTKHFSQKHgqtfKAVDNVNLNVPEGEMCVLLGPSGCGKTTTLKMINRLITPSSGTILINGEDTSGMDTVTLRRN 81
Cdd:COG1122    1 IELENLSFSYPGGT----PALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVDGKDITKKNLRELRRK 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556496326  82 IGYVIQ----QigLFpNMTIEENITVVPRMLGWDKARCKTRAEELMDMVALDphKFLNRYPREMSGGQQQRIGVIRALAA 157
Cdd:COG1122   77 VGLVFQnpddQ--LF-APTVEEDVAFGPENLGLPREEIRERVEEALELVGLE--HLADRPPHELSGGQKQRVAIAGVLAM 151

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 556496326 158 DPPVLLMDEPFGAVDPINREVIQNQFLEMQRKlKKTVMLVSHDIDEALKLGDRIAVFRQGKIVQCASPDELLAKP 232
Cdd:COG1122  152 EPEVLVLDEPTAGLDPRGRRELLELLKRLNKE-GKTVIIVTHDLDLVAELADRVIVLDDGRIVADGTPREVFSDY 225
AbcC COG1135
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
1-271 2.34e-64

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


Pssm-ID: 440750 [Multi-domain]  Cd Length: 339  Bit Score: 208.39  E-value: 2.34e-64
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556496326   1 MIKLENLTKHFSQKhGQTFKAVDNVNLNVPEGEMCVLLGPSGCGKTTTLKMINRLITPSSGTILINGEDTSGMDT---VT 77
Cdd:COG1135    1 MIELENLSKTFPTK-GGPVTALDDVSLTIEKGEIFGIIGYSGAGKSTLIRCINLLERPTSGSVLVDGVDLTALSErelRA 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556496326  78 LRRNIGYVIQQIGLFPNMTIEENITVVPRMLGWDKARCKTRAEELMDMVALDPHKflNRYPREMSGGQQQRIGVIRALAA 157
Cdd:COG1135   80 ARRKIGMIFQHFNLLSSRTVAENVALPLEIAGVPKAEIRKRVAELLELVGLSDKA--DAYPSQLSGGQKQRVGIARALAN 157

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556496326 158 DPPVLLMDEPFGAVDP------------INREviqnqflemqrkLKKTVMLVSHDIDEALKLGDRIAVFRQGKIVQCASP 225
Cdd:COG1135  158 NPKVLLCDEATSALDPettrsildllkdINRE------------LGLTIVLITHEMDVVRRICDRVAVLENGRIVEQGPV 225

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|
gi 556496326 226 DELLAKP----ANEFVGSFVGQDRTLKRLLLVSAGDVTDQQPTITVRGST 271
Cdd:COG1135  226 LDVFANPqselTRRFLPTVLNDELPEELLARLREAAGGGRLVRLTFVGES 275
fbpC PRK11432
ferric ABC transporter ATP-binding protein;
4-279 4.78e-64

ferric ABC transporter ATP-binding protein;


Pssm-ID: 183133 [Multi-domain]  Cd Length: 351  Bit Score: 208.03  E-value: 4.78e-64
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556496326   4 LENLTKHFSQKhgqtfKAVDNVNLNVPEGEMCVLLGPSGCGKTTTLKMINRLITPSSGTILINGEDTSgmDTVTLRRNIG 83
Cdd:PRK11432   9 LKNITKRFGSN-----TVIDNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIFIDGEDVT--HRSIQQRDIC 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556496326  84 YVIQQIGLFPNMTIEENITVVPRMLGWDKARCKTRAEELMDMVALDphKFLNRYPREMSGGQQQRIGVIRALAADPPVLL 163
Cdd:PRK11432  82 MVFQSYALFPHMSLGENVGYGLKMLGVPKEERKQRVKEALELVDLA--GFEDRYVDQISGGQQQRVALARALILKPKVLL 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556496326 164 MDEPFGAVDPINREVIQNQFLEMQRKLKKTVMLVSHDIDEALKLGDRIAVFRQGKIVQCASPDELLAKPANEFVGSFVGQ 243
Cdd:PRK11432 160 FDEPLSNLDANLRRSMREKIRELQQQFNITSLYVTHDQSEAFAVSDTVIVMNKGKIMQIGSPQELYRQPASRFMASFMGD 239

                        250       260       270
                 ....*....|....*....|....*....|....*..
gi 556496326 244 DRTLkrlllvsagDVTDQQPTITVRG-STPLPEAFAT 279
Cdd:PRK11432 240 ANIF---------PATLSGDYVDIYGyRLPRPAAFAF 267
potA TIGR01187
spermidine/putrescine ABC transporter ATP-binding subunit; This model describes spermidine ...
 37-243 5.76e-64

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: 206.96  E-value: 5.76e-64
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556496326   37 LLGPSGCGKTTTLKMINRLITPSSGTILINGEDTSgmDTVTLRRNIGYVIQQIGLFPNMTIEENITVVPRMLGWDKARCK 116
Cdd:TIGR01187   1 LLGPSGCGKTTLLRLLAGFEQPDSGSIMLDGEDVT--NVPPHLRHINMVFQSYALFPHMTVEENVAFGLKMRKVPRAEIK 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556496326  117 TRAEELMDMVALDphKFLNRYPREMSGGQQQRIGVIRALAADPPVLLMDEPFGAVDPINREVIQNQFLEMQRKLKKTVML 196
Cdd:TIGR01187  79 PRVLEALRLVQLE--EFADRKPHQLSGGQQQRVALARALVFKPKILLLDEPLSALDKKLRDQMQLELKTIQEQLGITFVF 156

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 556496326  197 VSHDIDEALKLGDRIAVFRQGKIVQCASPDELLAKPANEFVGSFVGQ 243
Cdd:TIGR01187 157 VTHDQEEAMTMSDRIAIMRKGKIAQIGTPEEIYEEPANLFVARFIGE 203
ABC_HisP_GlnQ cd03262
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ...
 2-219 1.02e-63

ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ATP-binding components of the bacterial periplasmic histidine and glutamine permeases, respectively. Histidine permease is a multi-subunit complex containing the HisQ and HisM integral membrane subunits and two copies of HisP. HisP has properties intermediate between those of integral and peripheral membrane proteins and is accessible from both sides of the membrane, presumably by its interaction with HisQ and HisM. The two HisP subunits form a homodimer within the complex. The domain structure of the amino acid uptake systems is typical for prokaryotic extracellular solute binding protein-dependent uptake systems. All of the amino acid uptake systems also have at least one, and in a few cases, two extracellular solute binding proteins located in the periplasm of Gram-negative bacteria, or attached to the cell membrane of Gram-positive bacteria. The best-studied member of the PAAT (polar amino acid transport) family is the HisJQMP system of S. typhimurium, where HisJ is the extracellular solute binding proteins and HisP is the ABC protein.


Pssm-ID: 213229 [Multi-domain]  Cd Length: 213  Bit Score: 202.76  E-value: 1.02e-63
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556496326   2 IKLENLTKHFSQKHgqtfkAVDNVNLNVPEGEMCVLLGPSGCGKTTTLKMINRLITPSSGTILINGE--DTSGMDTVTLR 79
Cdd:cd03262    1 IEIKNLHKSFGDFH-----VLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIDGLklTDDKKNINELR 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556496326  80 RNIGYVIQQIGLFPNMTIEENITVVPR-MLGWDKARCKTRAEELMDMVALDPHKflNRYPREMSGGQQQRIGVIRALAAD 158
Cdd:cd03262   76 QKVGMVFQQFNLFPHLTVLENITLAPIkVKGMSKAEAEERALELLEKVGLADKA--DAYPAQLSGGQQQRVAIARALAMN 153

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 556496326 159 PPVLLMDEPFGAVDPinrEVIqNQFLEMQRKLKK---TVMLVSHDIDEALKLGDRIAVFRQGKI 219
Cdd:cd03262  154 PKVMLFDEPTSALDP---ELV-GEVLDVMKDLAEegmTMVVVTHEMGFAREVADRVIFMDDGRI 213
FtsE COG2884
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
1-220 6.62e-63

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


Pssm-ID: 442130 [Multi-domain]  Cd Length: 223  Bit Score: 200.66  E-value: 6.62e-63
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556496326   1 MIKLENLTKHFSQKHgqtfKAVDNVNLNVPEGEMCVLLGPSGCGKTTTLKMINRLITPSSGTILINGEDTSGMDTVT--- 77
Cdd:COG2884    1 MIRFENVSKRYPGGR----EALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLVNGQDLSRLKRREipy 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556496326  78 LRRNIGYVIQQIGLFPNMTIEENITVVPRMLGWDKARCKTRAEELMDMVALDpHKfLNRYPREMSGGQQQRIGVIRALAA 157
Cdd:COG2884   77 LRRRIGVVFQDFRLLPDRTVYENVALPLRVTGKSRKEIRRRVREVLDLVGLS-DK-AKALPHELSGGEQQRVAIARALVN 154

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 556496326 158 DPPVLLMDEPFGAVDPINREVIQNQFLEMQRkLKKTVMLVSHDIDEALKLGDRIAVFRQGKIV 220
Cdd:COG2884  155 RPELLLADEPTGNLDPETSWEIMELLEEINR-RGTTVLIATHDLELVDRMPKRVLELEDGRLV 216
PRK10851 PRK10851
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
2-243 1.44e-62

sulfate/thiosulfate ABC transporter ATP-binding protein CysA;


Pssm-ID: 182778 [Multi-domain]  Cd Length: 353  Bit Score: 204.16  E-value: 1.44e-62
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556496326   2 IKLENLTKHFsqkhGQTfKAVDNVNLNVPEGEMCVLLGPSGCGKTTTLKMINRLITPSSGTILINGEDTSGMDTvtLRRN 81
Cdd:PRK10851   3 IEIANIKKSF----GRT-QVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFHGTDVSRLHA--RDRK 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556496326  82 IGYVIQQIGLFPNMTIEENI----TVVPRMLGWDKARCKTRAEELMDMVALdPHkFLNRYPREMSGGQQQRIGVIRALAA 157
Cdd:PRK10851  76 VGFVFQHYALFRHMTVFDNIafglTVLPRRERPNAAAIKAKVTQLLEMVQL-AH-LADRYPAQLSGGQKQRVALARALAV 153

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556496326 158 DPPVLLMDEPFGAVDPINREVIQNQFLEMQRKLKKTVMLVSHDIDEALKLGDRIAVFRQGKIVQCASPDELLAKPANEFV 237
Cdd:PRK10851 154 EPQILLLDEPFGALDAQVRKELRRWLRQLHEELKFTSVFVTHDQEEAMEVADRVVVMSQGNIEQAGTPDQVWREPATRFV 233


                 ....*.
gi 556496326 238 GSFVGQ 243
Cdd:PRK10851 234 LEFMGE 239
DppF COG1124
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ...
 1-236 1.91e-62

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: 200.41  E-value: 1.91e-62
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556496326   1 MIKLENLTKHFSQKHGQTfKAVDNVNLNVPEGEmCV-LLGPSGCGKTTTLKMINRLITPSSGTILINGEDTSGMDTVTLR 79
Cdd:COG1124    1 MLEVRNLSVSYGQGGRRV-PVLKDVSLEVAPGE-SFgLVGESGSGKSTLLRALAGLERPWSGEVTFDGRPVTRRRRKAFR 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556496326  80 RNIGYVIQQIG--LFPNMTIEENITVVPRMLGwdKARCKTRAEELMDMVALDPHkFLNRYPREMSGGQQQRIGVIRALAA 157
Cdd:COG1124   79 RRVQMVFQDPYasLHPRHTVDRILAEPLRIHG--LPDREERIAELLEQVGLPPS-FLDRYPHQLSGGQRQRVAIARALIL 155

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 556496326 158 DPPVLLMDEPFGAVDPINREVIQNQFLEMQRKLKKTVMLVSHDIDEALKLGDRIAVFRQGKIVQCASPDELLAKPANEF 236
Cdd:COG1124  156 EPELLLLDEPTSALDVSVQAEILNLLKDLREERGLTYLFVSHDLAVVAHLCDRVAVMQNGRIVEELTVADLLAGPKHPY 234
ABC_PstB_phosphate_transporter cd03260
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ...
 2-228 4.42e-61

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: 196.25  E-value: 4.42e-61
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556496326   2 IKLENLTKHFSQKHgqtfkAVDNVNLNVPEGEMCVLLGPSGCGKTTTLKMINRLI-----TPSSGTILINGED--TSGMD 74
Cdd:cd03260    1 IELRDLNVYYGDKH-----ALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRLNdlipgAPDEGEVLLDGKDiyDLDVD 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556496326  75 TVTLRRNIGYVIQQIGLFPnMTIEENITVVPRMLG-WDKARCKTRAEELMDMVALDPHKFLNRYPREMSGGQQQRIGVIR 153
Cdd:cd03260   76 VLELRRRVGMVFQKPNPFP-GSIYDNVAYGLRLHGiKLKEELDERVEEALRKAALWDEVKDRLHALGLSGGQQQRLCLAR 154

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 556496326 154 ALAADPPVLLMDEPFGAVDPINREVIQNQFLEMQRKLkkTVMLVSHDIDEALKLGDRIAVFRQGKIVQCASPDEL 228
Cdd:cd03260  155 ALANEPEVLLLDEPTSALDPISTAKIEELIAELKKEY--TIVIVTHNMQQAARVADRTAFLLNGRLVEFGPTEQI 227
PhnC COG3638
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and ...
 1-228 4.72e-61

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


Pssm-ID: 442855 [Multi-domain]  Cd Length: 249  Bit Score: 196.82  E-value: 4.72e-61
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556496326   1 MIKLENLTKHFSqkhGQTfKAVDNVNLNVPEGEMCVLLGPSGCGKTTTLKMINRLITPSSGTILINGEDTSGMDTVTL-- 78
Cdd:COG3638    2 MLELRNLSKRYP---GGT-PALDDVSLEIERGEFVALIGPSGAGKSTLLRCLNGLVEPTSGEILVDGQDVTALRGRALrr 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556496326  79 -RRNIGYVIQQIGLFPNMTIEEN--------ITVVPRMLGWDKARCKTRAEELMDMVALDPHkfLNRYPREMSGGQQQRI 149
Cdd:COG3638   78 lRRRIGMIFQQFNLVPRLSVLTNvlagrlgrTSTWRSLLGLFPPEDRERALEALERVGLADK--AYQRADQLSGGQQQRV 155

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 556496326 150 GVIRALAADPPVLLMDEPFGAVDPINREVIQNQFLEMQRKLKKTVMLVSHDIDEALKLGDRIAVFRQGKIVQCASPDEL 228
Cdd:COG3638  156 AIARALVQEPKLILADEPVASLDPKTARQVMDLLRRIAREDGITVVVNLHQVDLARRYADRIIGLRDGRVVFDGPPAEL 234
CBS_pair_ABC_OpuCA_assoc cd04582
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains found associated with ...
 258-368 6.38e-61

Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains found associated with the ABC transporter OpuCA; This cd contains two tandem repeats of the cystathionine beta-synthase (CBS pair) domains found in association with the ABC transporter OpuCA. OpuCA is the ATP binding component of a bacterial solute transporter that serves a protective role to cells growing in a hyperosmolar environment but the function of the CBS domains in OpuCA remains unknown. In the related ABC transporter, OpuA, the tandem CBS domains have been shown to function as sensors for ionic strength, whereby they control the transport activity through an electronic switching mechanism. 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. They 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. The CBS domain, named after human CBS, is a small domain originally identified in cystathionine beta-synthase and is subsequently found in a wide range of different proteins. CBS domains usually occur in tandem repeats. They associate to form a so-called Bateman domain or a CBS pair based on crystallographic studies in bacteria. The CBS pair was used as a basis for this cd hierarchy since the human CBS proteins can adopt the typical core structure and form an intramolecular CBS pair. The interface between the two CBS domains forms a cleft that is a potential ligand binding site. The CBS pair coexists with a variety of other functional domains and this has been used to help in its classification here. It has been proposed that the CBS domain may play a regulatory role, although its exact function is unknown. Mutations of conserved residues within this domain are associated with a variety of human hereditary diseases, including congenital myotonia, idiopathic generalized epilepsy, hypercalciuric nephrolithiasis, and classic Bartter syndrome (CLC chloride channel family members), Wolff-Parkinson-White syndrome (gamma 2 subunit of AMP-activated protein kinase), retinitis pigmentosa (IMP dehydrogenase-1), and homocystinuria (cystathionine beta-synthase).


Pssm-ID: 341359 [Multi-domain]  Cd Length: 111  Bit Score: 191.83  E-value: 6.38e-61
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556496326 258 VTDQQPTITVRGSTPLPEAFATMDDNDIRAITVVDEHGKPLGFVKRREARNASGTCADILHPFRMTGKAEDNLRVVLSRL 337
Cdd:cd04582    1 EDAATPTPTVRPSTPLSDALGIMDDADSRYLVVVDADGRPLGYVTRRDARGASGTCGDFAHPFKATVPVDENLRVVLSRM 80

                         90       100       110
                 ....*....|....*....|....*....|.
gi 556496326 338 YESNTSWMPIVDEDGRYNGEISQDYIAEYLS 368
Cdd:cd04582   81 YEHNTSWLPVVDEDGRYAGEVTQDSIADYLS 111
ABC_DR_subfamily_A cd03230
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ...
 2-219 6.86e-61

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: 193.77  E-value: 6.86e-61
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556496326   2 IKLENLTKHFsqkhgQTFKAVDNVNLNVPEGEMCVLLGPSGCGKTTTLKMINRLITPSSGTILINGEDTSGmDTVTLRRN 81
Cdd:cd03230    1 IEVRNLSKRY-----GKKTALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVLGKDIKK-EPEEVKRR 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556496326  82 IGYVIQQIGLFPNMTIEENItvvprmlgwdkarcktraeelmdmvaldphkflnryprEMSGGQQQRIGVIRALAADPPV 161
Cdd:cd03230   75 IGYLPEEPSLYENLTVRENL--------------------------------------KLSGGMKQRLALAQALLHDPEL 116

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 556496326 162 LLMDEPFGAVDPINREVIQNQFLEMQRKlKKTVMLVSHDIDEALKLGDRIAVFRQGKI 219
Cdd:cd03230  117 LILDEPTSGLDPESRREFWELLRELKKE-GKTILLSSHILEEAERLCDRVAILNNGRI 173
TauB COG4525
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
1-226 1.77e-58

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


Pssm-ID: 443596 [Multi-domain]  Cd Length: 262  Bit Score: 190.84  E-value: 1.77e-58
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556496326   1 MIKLENLTKHFSqKHGQTFKAVDNVNLNVPEGEMCVLLGPSGCGKTTTLKMINRLITPSSGTILINGEDTSGMDTvtlRR 80
Cdd:COG4525    3 MLTVRHVSVRYP-GGGQPQPALQDVSLTIESGEFVVALGASGCGKTTLLNLIAGFLAPSSGEITLDGVPVTGPGA---DR 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556496326  81 niGYVIQQIGLFPNMTIEENITVVPRMLGWDKARCKTRAEELMDMVALDphKFLNRYPREMSGGQQQRIGVIRALAADPP 160
Cdd:COG4525   79 --GVVFQKDALLPWLNVLDNVAFGLRLRGVPKAERRARAEELLALVGLA--DFARRRIWQLSGGMRQRVGIARALAADPR 154

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 556496326 161 VLLMDEPFGAVDPINREVIQNQFLEMQRKLKKTVMLVSHDIDEALKLGDRIAVF--RQGKIVQCASPD 226
Cdd:COG4525  155 FLLMDEPFGALDALTREQMQELLLDVWQRTGKGVFLITHSVEEALFLATRLVVMspGPGRIVERLELD 222
ABC_subfamily_A cd03263
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ...
 2-228 2.00e-58

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: 189.25  E-value: 2.00e-58
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556496326   2 IKLENLTKHFSQKhgqTFKAVDNVNLNVPEGEMCVLLGPSGCGKTTTLKMINRLITPSSGTILINGEDTSgMDTVTLRRN 81
Cdd:cd03263    1 LQIRNLTKTYKKG---TKPAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYINGYSIR-TDRKAARQS 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556496326  82 IGYVIQQIGLFPNMTIEENITVVPRMLGWDKARCKTRAEELMDMVALDPHKflNRYPREMSGGQQQRIGVIRALAADPPV 161
Cdd:cd03263   77 LGYCPQFDALFDELTVREHLRFYARLKGLPKSEIKEEVELLLRVLGLTDKA--NKRARTLSGGMKRKLSLAIALIGGPSV 154

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 556496326 162 LLMDEPFGAVDPINREVIQNQFLEMQRklKKTVMLVSHDIDEALKLGDRIAVFRQGKIVQCASPDEL 228
Cdd:cd03263  155 LLLDEPTSGLDPASRRAIWDLILEVRK--GRSIILTTHSMDEAEALCDRIAIMSDGKLRCIGSPQEL 219
DppD COG0444
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ...
 1-233 3.73e-58

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: 191.81  E-value: 3.73e-58
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556496326   1 MIKLENLTKHFSQKHGqTFKAVDNVNLNVPEGEMCVLLGPSGCGKTTTLKMINRLITP---SSGTILINGEDTSGMDTVT 77
Cdd:COG0444    1 LLEVRNLKVYFPTRRG-VVKAVDGVSFDVRRGETLGLVGESGSGKSTLARAILGLLPPpgiTSGEILFDGEDLLKLSEKE 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556496326  78 LR----RNIGYVIQ--QIGLFPNMTIEENITVVPRM-LGWDKARCKTRAEELMDMVAL-DPHKFLNRYPREMSGGQQQRI 149
Cdd:COG0444   80 LRkirgREIQMIFQdpMTSLNPVMTVGDQIAEPLRIhGGLSKAEARERAIELLERVGLpDPERRLDRYPHELSGGMRQRV 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556496326 150 GVIRALAADPPVLLMDEPFGAVDPINREVIQNQFLEMQRKLKKTVMLVSHDIDEALKLGDRIAVFRQGKIVQCASPDELL 229
Cdd:COG0444  160 MIARALALEPKLLIADEPTTALDVTIQAQILNLLKDLQRELGLAILFITHDLGVVAEIADRVAVMYAGRIVEEGPVEELF 239


                 ....
gi 556496326 230 AKPA 233
Cdd:COG0444  240 ENPR 243
ABC_cobalt_CbiO_domain1 cd03225
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ...
 3-218 5.07e-58

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: 187.67  E-value: 5.07e-58
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556496326   3 KLENLTkhFSQKHGQTfKAVDNVNLNVPEGEMCVLLGPSGCGKTTTLKMINRLITPSSGTILINGEDTSGMDTVTLRRNI 82
Cdd:cd03225    1 ELKNLS--FSYPDGAR-PALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDLTKLSLKELRRKV 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556496326  83 GYVIQ----QigLFpNMTIEENITVVPRMLGWDKARCKTRAEELMDMVALDPhkFLNRYPREMSGGQQQRIGVIRALAAD 158
Cdd:cd03225   78 GLVFQnpddQ--FF-GPTVEEEVAFGLENLGLPEEEIEERVEEALELVGLEG--LRDRSPFTLSGGQKQRVAIAGVLAMD 152

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 556496326 159 PPVLLMDEPFGAVDPINREviqnQFLEMQRKLK---KTVMLVSHDIDEALKLGDRIAVFRQGK 218
Cdd:cd03225  153 PDILLLDEPTAGLDPAGRR----ELLELLKKLKaegKTIIIVTHDLDLLLELADRVIVLEDGK 211
ABC_PhnC_transporter cd03256
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ...
 2-228 7.52e-57

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: 185.85  E-value: 7.52e-57
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556496326   2 IKLENLTKHFsqkhGQTFKAVDNVNLNVPEGEMCVLLGPSGCGKTTTLKMINRLITPSSGTILINGEDTSGMDTVTL--- 78
Cdd:cd03256    1 IEVENLSKTY----PNGKKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGTDINKLKGKALrql 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556496326  79 RRNIGYVIQQIGLFPNMTIEENI--------TVVPRMLGWDKARCKTRAEELMDMVALDPHkfLNRYPREMSGGQQQRIG 150
Cdd:cd03256   77 RRQIGMIFQQFNLIERLSVLENVlsgrlgrrSTWRSLFGLFPKEEKQRALAALERVGLLDK--AYQRADQLSGGQQQRVA 154

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 556496326 151 VIRALAADPPVLLMDEPFGAVDPINREVIQNQFLEMQRKLKKTVMLVSHDIDEALKLGDRIAVFRQGKIVQCASPDEL 228
Cdd:cd03256  155 IARALMQQPKLILADEPVASLDPASSRQVMDLLKRINREEGITVIVSLHQVDLAREYADRIVGLKDGRIVFDGPPAEL 232
ECF_ATPase_2 TIGR04521
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ...
 2-232 1.41e-56

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: 186.50  E-value: 1.41e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556496326    2 IKLENLTkHFSQKhGQTF--KAVDNVNLNVPEGEMCVLLGPSGCGKTTTLKMINRLITPSSGTILINGEDTSGMDTVT-- 77
Cdd:TIGR04521   1 IKLKNVS-YIYQP-GTPFekKALDDVSLTIEDGEFVAIIGHTGSGKSTLIQHLNGLLKPTSGTVTIDGRDITAKKKKKlk 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556496326   78 -LRRNIGYVIQ----QigLFPNmTIEENITVVPRMLGWDKARCKTRAEELMDMVALDPhKFLNRYPREMSGGQQQRIGVI 152
Cdd:TIGR04521  79 dLRKKVGLVFQfpehQ--LFEE-TVYKDIAFGPKNLGLSEEEAEERVKEALELVGLDE-EYLERSPFELSGGQMRRVAIA 154

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556496326  153 RALAADPPVLLMDEPFGAVDPINREVIQNQFLEMQRKLKKTVMLVSHDIDEALKLGDRIAVFRQGKIVQCASPDELLAKP 232
Cdd:TIGR04521 155 GVLAMEPEVLILDEPTAGLDPKGRKEILDLFKRLHKEKGLTVILVTHSMEDVAEYADRVIVMHKGKIVLDGTPREVFSDV 234
PRK10070 PRK10070
proline/glycine betaine ABC transporter ATP-binding protein ProV;
21-367 1.63e-56

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


Pssm-ID: 182221 [Multi-domain]  Cd Length: 400  Bit Score: 189.86  E-value: 1.63e-56
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556496326  21 AVDNVNLNVPEGEMCVLLGPSGCGKTTTLKMINRLITPSSGTILINGEDTSGMDTVTLR----RNIGYVIQQIGLFPNMT 96
Cdd:PRK10070  43 GVKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAKISDAELRevrrKKIAMVFQSFALMPHMT 122

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556496326  97 IEENITVVPRMLGWDKARCKTRAEELMDMVALDphKFLNRYPREMSGGQQQRIGVIRALAADPPVLLMDEPFGAVDPINR 176
Cdd:PRK10070 123 VLDNTAFGMELAGINAEERREKALDALRQVGLE--NYAHSYPDELSGGMRQRVGLARALAINPDILLMDEAFSALDPLIR 200

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556496326 177 EVIQNQFLEMQRKLKKTVMLVSHDIDEALKLGDRIAVFRQGKIVQCASPDELLAKPANEFVGSFVgqdRTLKRLLLVSAG 256
Cdd:PRK10070 201 TEMQDELVKLQAKHQRTIVFISHDLDEAMRIGDRIAIMQNGEVVQVGTPDEILNNPANDYVRTFF---RGVDISQVFSAK 277

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556496326 257 DVTDQQPTITVRGSTPL--PEAFATMDDNDIRAITVVDEHGKPLGFVKRREARNASGTCADI---LHPFRMTGKAEDNLR 331
Cdd:PRK10070 278 DIARRTPNGLIRKTPGFgpRSALKLLQDEDREYGYVIERGNKFVGAVSIDSLKTALTQQQGLdaaLIDAPLAVDAQTPLS 357

                        330       340       350
                 ....*....|....*....|....*....|....*.
gi 556496326 332 VVLSRLYESNTSwMPIVDEDGRYNGEISQDYIAEYL 367
Cdd:PRK10070 358 ELLSHVGQAPCA-VPVVDEDQQYVGIISKGMLLRAL 392
metN PRK11153
DL-methionine transporter ATP-binding subunit; Provisional
 1-244 1.77e-56

DL-methionine transporter ATP-binding subunit; Provisional


Pssm-ID: 236863 [Multi-domain]  Cd Length: 343  Bit Score: 188.09  E-value: 1.77e-56
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556496326   1 MIKLENLTKHFSQKhGQTFKAVDNVNLNVPEGEMCVLLGPSGCGKTTTLKMINRLITPSSGTILINGEDTSGMDTVTL-- 78
Cdd:PRK11153   1 MIELKNISKVFPQG-GRTIHALNNVSLHIPAGEIFGVIGASGAGKSTLIRCINLLERPTSGRVLVDGQDLTALSEKELrk 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556496326  79 -RRNIGYVIQQIGLFPNMTIEENITVVPRMLGWDKARCKTRAEELMDMVALDPHKflNRYPREMSGGQQQRIGVIRALAA 157
Cdd:PRK11153  80 aRRQIGMIFQHFNLLSSRTVFDNVALPLELAGTPKAEIKARVTELLELVGLSDKA--DRYPAQLSGGQKQRVAIARALAS 157

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556496326 158 DPPVLLMDEPFGAVDPINREVIQNQFLEMQRKLKKTVMLVSHDIDEALKLGDRIAVFRQGKIVQCASPDELLAKP----A 233
Cdd:PRK11153 158 NPKVLLCDEATSALDPATTRSILELLKDINRELGLTIVLITHEMDVVKRICDRVAVIDAGRLVEQGTVSEVFSHPkhplT 237

                        250
                 ....*....|.
gi 556496326 234 NEFVGSFVGQD 244
Cdd:PRK11153 238 REFIQSTLHLD 248
AppF COG4608
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ...
 2-233 2.60e-56

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


Pssm-ID: 443658 [Multi-domain]  Cd Length: 329  Bit Score: 187.25  E-value: 2.60e-56
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556496326   2 IKLENLTKHFS------QKHGQTFKAVDNVNLNVPEGEMCVLLGPSGCGKTTTLKMINRLITPSSGTILINGEDTSGMDT 75
Cdd:COG4608    8 LEVRDLKKHFPvrgglfGRTVGVVKAVDGVSFDIRRGETLGLVGESGCGKSTLGRLLLRLEEPTSGEILFDGQDITGLSG 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556496326  76 ---VTLRRNIGYVIQ--QIGLFPNMTIEENITVVPRMLG-WDKARCKTRAEELMDMVALDPHkFLNRYPREMSGGQQQRI 149
Cdd:COG4608   88 relRPLRRRMQMVFQdpYASLNPRMTVGDIIAEPLRIHGlASKAERRERVAELLELVGLRPE-HADRYPHEFSGGQRQRI 166

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556496326 150 GVIRALAADPPVLLMDEPFGAVDpinreV-IQNQ----FLEMQRKLKKTVMLVSHDidealkLG------DRIAVFRQGK 218
Cdd:COG4608  167 GIARALALNPKLIVCDEPVSALD-----VsIQAQvlnlLEDLQDELGLTYLFISHD------LSvvrhisDRVAVMYLGK 235

                        250
                 ....*....|....*
gi 556496326 219 IVQCASPDELLAKPA 233
Cdd:COG4608  236 IVEIAPRDELYARPL 250
YhaQ COG4152
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ...
 1-291 5.45e-56

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


Pssm-ID: 443322 [Multi-domain]  Cd Length: 298  Bit Score: 185.31  E-value: 5.45e-56
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556496326   1 MIKLENLTKHFSqkhgqTFKAVDNVNLNVPEGEMCVLLGPSGCGKTTTLKMINRLITPSSGTILINGEDtsgmDTVTLRR 80
Cdd:COG4152    1 MLELKGLTKRFG-----DKTAVDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDSGEVLWDGEP----LDPEDRR 71

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556496326  81 NIGYVIQQIGLFPNMTIEENITVVPRMLGWDKARCKTRAEELMDMVALDPHKflNRYPREMSGGQQQRIGVIRALAADPP 160
Cdd:COG4152   72 RIGYLPEERGLYPKMKVGEQLVYLARLKGLSKAEAKRRADEWLERLGLGDRA--NKKVEELSKGNQQKVQLIAALLHDPE 149

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556496326 161 VLLMDEPFGAVDPINREVIQNQFLEMQRKlKKTVMLVSHDIDEALKLGDRIAVFRQGKIVQCASPDELLAK-PANEFVGS 239
Cdd:COG4152  150 LLILDEPFSGLDPVNVELLKDVIRELAAK-GTTVIFSSHQMELVEELCDRIVIINKGRKVLSGSVDEIRRQfGRNTLRLE 228

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|...
gi 556496326 240 FVGQDRTLKRLLLVSAGDVTDQQPTITVRGSTPLPEAFAT-MDDNDIRAITVV 291
Cdd:COG4152  229 ADGDAGWLRALPGVTVVEEDGDGAELKLEDGADAQELLRAlLARGPVREFEEV 281
potG PRK11607
putrescine ABC transporter ATP-binding subunit PotG;
1-242 9.10e-56

putrescine ABC transporter ATP-binding subunit PotG;


Pssm-ID: 183226 [Multi-domain]  Cd Length: 377  Bit Score: 187.35  E-value: 9.10e-56
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556496326   1 MIKLENLTKHFSQKHgqtfkAVDNVNLNVPEGEMCVLLGPSGCGKTTTLKMINRLITPSSGTILINGEDTSgmDTVTLRR 80
Cdd:PRK11607  19 LLEIRNLTKSFDGQH-----AVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVDLS--HVPPYQR 91

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556496326  81 NIGYVIQQIGLFPNMTIEENITVVPRMLGWDKARCKTRAEELMDMVALdpHKFLNRYPREMSGGQQQRIGVIRALAADPP 160
Cdd:PRK11607  92 PINMMFQSYALFPHMTVEQNIAFGLKQDKLPKAEIASRVNEMLGLVHM--QEFAKRKPHQLSGGQRQRVALARSLAKRPK 169

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556496326 161 VLLMDEPFGAVDPINREVIQNQFLEMQRKLKKTVMLVSHDIDEALKLGDRIAVFRQGKIVQCASPDELLAKPANEFVGSF 240
Cdd:PRK11607 170 LLLLDEPMGALDKKLRDRMQLEVVDILERVGVTCVMVTHDQEEAMTMAGRIAIMNRGKFVQIGEPEEIYEHPTTRYSAEF 249


                 ..
gi 556496326 241 VG 242
Cdd:PRK11607 250 IG 251
3a0107s01c2 TIGR00972
phosphate ABC transporter, ATP-binding protein; This model represents the ATP-binding protein ...
 2-235 2.26e-55

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: 182.11  E-value: 2.26e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556496326    2 IKLENLTKHFSQKHgqtfkAVDNVNLNVPEGEMCVLLGPSGCGKTTTLKMINRL--ITPS---SGTILINGED--TSGMD 74
Cdd:TIGR00972   2 IEIENLNLFYGEKE-----ALKNINLDIPKNQVTALIGPSGCGKSTLLRSLNRMndLVPGvriEGKVLFDGQDiyDKKID 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556496326   75 TVTLRRNIGYVIQQIGLFPnMTIEENITVVPRMLGW-DKARCKTRAEELMDMVAL-DPHK-FLNRYPREMSGGQQQRIGV 151
Cdd:TIGR00972  77 VVELRRRVGMVFQKPNPFP-MSIYDNIAYGPRLHGIkDKKELDEIVEESLKKAALwDEVKdRLHDSALGLSGGQQQRLCI 155

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556496326  152 IRALAADPPVLLMDEPFGAVDPINREVIQnqflEMQRKLKK--TVMLVSHDIDEALKLGDRIAVFRQGKIVQCASPDELL 229
Cdd:TIGR00972 156 ARALAVEPEVLLLDEPTSALDPIATGKIE----ELIQELKKkyTIVIVTHNMQQAARISDRTAFFYDGELVEYGPTEQIF 231


                  ....*.
gi 556496326  230 AKPANE 235
Cdd:TIGR00972 232 TNPKEK 237
FepC COG1120
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ...
 1-229 2.70e-55

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: 182.17  E-value: 2.70e-55
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556496326   1 MIKLENLTKHFSQKHgqtfkAVDNVNLNVPEGEMCVLLGPSGCGKTTTLKMINRLITPSSGTILINGEDTSGMDTVTLRR 80
Cdd:COG1120    1 MLEAENLSVGYGGRP-----VLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDGRDLASLSRRELAR 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556496326  81 NIGYVIQQIGLFPNMTIEEnitVV-----P--RMLGWDKARCKTRAEELMDMVALDPhkFLNRYPREMSGGQQQRIGVIR 153
Cdd:COG1120   76 RIAYVPQEPPAPFGLTVRE---LValgryPhlGLFGRPSAEDREAVEEALERTGLEH--LADRPVDELSGGERQRVLIAR 150

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 556496326 154 ALAADPPVLLMDEPFGAVDPINREVIQNQFLEMQRKLKKTVMLVSHDIDEALKLGDRIAVFRQGKIVQCASPDELL 229
Cdd:COG1120  151 ALAQEPPLLLLDEPTSHLDLAHQLEVLELLRRLARERGRTVVMVLHDLNLAARYADRLVLLKDGRIVAQGPPEEVL 226
ABC_DrrA cd03265
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ...
 2-228 3.51e-55

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: 181.03  E-value: 3.51e-55
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556496326   2 IKLENLTKHFSQkhgqtFKAVDNVNLNVPEGEMCVLLGPSGCGKTTTLKMINRLITPSSGTILINGEDTSgMDTVTLRRN 81
Cdd:cd03265    1 IEVENLVKKYGD-----FEAVRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATVAGHDVV-REPREVRRR 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556496326  82 IGYVIQQIGLFPNMTIEENITVVPRMLGWDKARCKTRAEELMDMVALdpHKFLNRYPREMSGGQQQRIGVIRALAADPPV 161
Cdd:cd03265   75 IGIVFQDLSVDDELTGWENLYIHARLYGVPGAERRERIDELLDFVGL--LEAADRLVKTYSGGMRRRLEIARSLVHRPEV 152

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 556496326 162 LLMDEPFGAVDPINREVIQNQFLEMQRKLKKTVMLVSHDIDEALKLGDRIAVFRQGKIVQCASPDEL 228
Cdd:cd03265  153 LFLDEPTIGLDPQTRAHVWEYIEKLKEEFGMTILLTTHYMEEAEQLCDRVAIIDHGRIIAEGTPEEL 219
GsiA COG1123
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ...
 1-269 5.64e-55

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: 188.57  E-value: 5.64e-55
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556496326   1 MIKLENLTKHFsqkHGQTFKAVDNVNLNVPEGEMCVLLGPSGCGKTTTLKMINRLITPS---SGTILINGEDTSGMDTVT 77
Cdd:COG1123    4 LLEVRDLSVRY---PGGDVPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGLLPHGgriSGEVLLDGRDLLELSEAL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556496326  78 LRRNIGYVIQQIG--LFPnMTIEENITVVPRMLGWDKARCKTRAEELMDMVALDphKFLNRYPREMSGGQQQRIGVIRAL 155
Cdd:COG1123   81 RGRRIGMVFQDPMtqLNP-VTVGDQIAEALENLGLSRAEARARVLELLEAVGLE--RRLDRYPHQLSGGQRQRVAIAMAL 157

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556496326 156 AADPPVLLMDEPFGAVDPINREVIQNQFLEMQRKLKKTVMLVSHDIDEALKLGDRIAVFRQGKIVQCASPDELLAKPANe 235
Cdd:COG1123  158 ALDPDLLIADEPTTALDVTTQAEILDLLRELQRERGTTVLLITHDLGVVAEIADRVVVMDDGRIVEDGPPEEILAAPQA- 236

                        250       260       270
                 ....*....|....*....|....*....|....
gi 556496326 236 fvgsfVGQDRTLKRLLLVSAGDVTDQQPTITVRG 269
Cdd:COG1123  237 -----LAAVPRLGAARGRAAPAAAAAEPLLEVRN 265
ABC_phnC TIGR02315
phosphonate ABC transporter, ATP-binding protein; Phosphonates are a class of ...
 1-228 5.96e-55

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: 180.96  E-value: 5.96e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556496326    1 MIKLENLTKHFSQKHgqtfKAVDNVNLNVPEGEMCVLLGPSGCGKTTTLKMINRLITPSSGTILINGED---TSGMDTVT 77
Cdd:TIGR02315   1 MLEVENLSKVYPNGK----QALKNINLNINPGEFVAIIGPSGAGKSTLLRCINRLVEPSSGSILLEGTDitkLRGKKLRK 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556496326   78 LRRNIGYVIQQIGLFPNMTIEENI--------TVVPRMLGWDKARCKTRAEELMDMVALDpHKFLNRyPREMSGGQQQRI 149
Cdd:TIGR02315  77 LRRRIGMIFQHYNLIERLTVLENVlhgrlgykPTWRSLLGRFSEEDKERALSALERVGLA-DKAYQR-ADQLSGGQQQRV 154

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 556496326  150 GVIRALAADPPVLLMDEPFGAVDPINREVIQNQFLEMQRKLKKTVMLVSHDIDEALKLGDRIAVFRQGKIVQCASPDEL 228
Cdd:TIGR02315 155 AIARALAQQPDLILADEPIASLDPKTSKQVMDYLKRINKEDGITVIINLHQVDLAKKYADRIVGLKAGEIVFDGAPSEL 233
glnQ PRK09493
glutamine ABC transporter ATP-binding protein GlnQ;
1-240 1.42e-54

glutamine ABC transporter ATP-binding protein GlnQ;


Pssm-ID: 181906 [Multi-domain]  Cd Length: 240  Bit Score: 179.90  E-value: 1.42e-54
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556496326   1 MIKLENLTKHFsqkhGQTfKAVDNVNLNVPEGEMCVLLGPSGCGKTTTLKMINRLITPSSGTILINGEDTSG--MDTVTL 78
Cdd:PRK09493   1 MIEFKNVSKHF----GPT-QVLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGLKVNDpkVDERLI 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556496326  79 RRNIGYVIQQIGLFPNMTIEENITVVP-RMLGWDKARCKTRAEELMDMVALDPHKflNRYPREMSGGQQQRIGVIRALAA 157
Cdd:PRK09493  76 RQEAGMVFQQFYLFPHLTALENVMFGPlRVRGASKEEAEKQARELLAKVGLAERA--HHYPSELSGGQQQRVAIARALAV 153

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556496326 158 DPPVLLMDEPFGAVDP-INREViqnqfLEMQRKLKK---TVMLVSHDIDEALKLGDRIAVFRQGKIVQCASPDELLAKPA 233
Cdd:PRK09493 154 KPKLMLFDEPTSALDPeLRHEV-----LKVMQDLAEegmTMVIVTHEIGFAEKVASRLIFIDKGRIAEDGDPQVLIKNPP 228


                 ....*..
gi 556496326 234 NEFVGSF 240
Cdd:PRK09493 229 SQRLQEF 235
SunT COG2274
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ...
 2-231 8.50e-54

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: 188.89  E-value: 8.50e-54
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556496326   2 IKLENLTKHFSqkhGQTFKAVDNVNLNVPEGEMCVLLGPSGCGKTTTLKMINRLITPSSGTILINGEDTSGMDTVTLRRN 81
Cdd:COG2274  474 IELENVSFRYP---GDSPPVLDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEPTSGRILIDGIDLRQIDPASLRRQ 550

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556496326  82 IGYVIQQIGLFpNMTIEENITVvprmlgWDKARCKTRAEELMDMVALdpHKFLNRYPR-------EM----SGGQQQRIG 150
Cdd:COG2274  551 IGVVLQDVFLF-SGTIRENITL------GDPDATDEEIIEAARLAGL--HDFIEALPMgydtvvgEGgsnlSGGQRQRLA 621

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556496326 151 VIRALAADPPVLLMDEPFGAVDPINREVIQNQFLEMQRklKKTVMLVSHDiDEALKLGDRIAVFRQGKIVQCASPDELLA 230
Cdd:COG2274  622 IARALLRNPRILILDEATSALDAETEAIILENLRRLLK--GRTVIIIAHR-LSTIRLADRIIVLDKGRIVEDGTHEELLA 698


                 .
gi 556496326 231 K 231
Cdd:COG2274  699 R 699
FetA COG4619
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
2-219 4.48e-53

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


Pssm-ID: 443661 [Multi-domain]  Cd Length: 209  Bit Score: 175.00  E-value: 4.48e-53
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556496326   2 IKLENLTKHFSQKHGqtfkaVDNVNLNVPEGEMCVLLGPSGCGKTTTLKMINRLITPSSGTILINGEDTSGMDTVTLRRN 81
Cdd:COG4619    1 LELEGLSFRVGGKPI-----LSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIYLDGKPLSAMPPPEWRRQ 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556496326  82 IGYVIQQIGLFPNmTIEENITVVPRMLgwDKARCKTRAEELMDMVALDPHkFLNRYPREMSGGQQQRIGVIRALAADPPV 161
Cdd:COG4619   76 VAYVPQEPALWGG-TVRDNLPFPFQLR--ERKFDRERALELLERLGLPPD-ILDKPVERLSGGERQRLALIRALLLQPDV 151

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 556496326 162 LLMDEPFGAVDPINREVIQNQFLEMQRKLKKTVMLVSHDIDEALKLGDRIAVFRQGKI 219
Cdd:COG4619  152 LLLDEPTSALDPENTRRVEELLREYLAEEGRAVLWVSHDPEQIERVADRVLTLEAGRL 209
PstB COG1117
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ...
 2-235 7.92e-53

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


Pssm-ID: 440734 [Multi-domain]  Cd Length: 258  Bit Score: 176.00  E-value: 7.92e-53
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556496326   2 IKLENLTKHFSQKHgqtfkAVDNVNLNVPEGEMCVLLGPSGCGKTTTLKMINRLI--TPS---SGTILINGED--TSGMD 74
Cdd:COG1117   12 IEVRNLNVYYGDKQ-----ALKDINLDIPENKVTALIGPSGCGKSTLLRCLNRMNdlIPGarvEGEILLDGEDiyDPDVD 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556496326  75 TVTLRRNIGYVIQQIGLFPnMTIEENITVVPRMLGW-DKARCKTRAEELMDMVAL-----DPhkfLNRYPREMSGGQQQR 148
Cdd:COG1117   87 VVELRRRVGMVFQKPNPFP-KSIYDNVAYGLRLHGIkSKSELDEIVEESLRKAALwdevkDR---LKKSALGLSGGQQQR 162

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556496326 149 IGVIRALAADPPVLLMDEPFGAVDPINREVIQNQFLEmqrkLKK--TVMLVSHDIDEALKLGDRIAVFRQGKIVQCASPD 226
Cdd:COG1117  163 LCIARALAVEPEVLLMDEPTSALDPISTAKIEELILE----LKKdyTIVIVTHNMQQAARVSDYTAFFYLGELVEFGPTE 238


                 ....*....
gi 556496326 227 ELLAKPANE 235
Cdd:COG1117  239 QIFTNPKDK 247
ZnuC COG1121
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ...
 1-229 4.20e-52

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


Pssm-ID: 440738 [Multi-domain]  Cd Length: 245  Bit Score: 173.74  E-value: 4.20e-52
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556496326   1 MIKLENLTKHFSQKhgqtfKAVDNVNLNVPEGEMCVLLGPSGCGKTTTLKMINRLITPSSGTILINGEDTSGMdtvtlRR 80
Cdd:COG1121    6 AIELENLTVSYGGR-----PVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLFGKPPRRA-----RR 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556496326  81 NIGYVIQQIGL---FPnMTIEEnitVVprMLGWD---------KARCKTRAEELMDMVALDphKFLNRYPREMSGGQQQR 148
Cdd:COG1121   76 RIGYVPQRAEVdwdFP-ITVRD---VV--LMGRYgrrglfrrpSRADREAVDEALERVGLE--DLADRPIGELSGGQQQR 147

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556496326 149 IGVIRALAADPPVLLMDEPFGAVDPINREVIQnQFLEMQRKLKKTVMLVSHDIDEALKLGDRIAVFRQGKIVQCaSPDEL 228
Cdd:COG1121  148 VLLARALAQDPDLLLLDEPFAGVDAATEEALY-ELLRELRREGKTILVVTHDLGAVREYFDRVLLLNRGLVAHG-PPEEV 225


                 .
gi 556496326 229 L 229
Cdd:COG1121  226 L 226
ABC_ModC_molybdenum_transporter cd03297
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ...
 20-221 5.21e-52

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: 172.48  E-value: 5.21e-52
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556496326  20 KAVDNVNLNVP---EGEMCVLLGPSGCGKTTTLKMINRLITPSSGTILINGE---DTS-GMDTVTLRRNIGYVIQQIGLF 92
Cdd:cd03297    8 KRLPDFTLKIDfdlNEEVTGIFGASGAGKSTLLRCIAGLEKPDGGTIVLNGTvlfDSRkKINLPPQQRKIGLVFQQYALF 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556496326  93 PNMTIEENITVVprMLGWDKARCKTRAEELMDMVALDPhkFLNRYPREMSGGQQQRIGVIRALAADPPVLLMDEPFGAVD 172
Cdd:cd03297   88 PHLNVRENLAFG--LKRKRNREDRISVDELLDLLGLDH--LLNRYPAQLSGGEKQRVALARALAAQPELLLLDEPFSALD 163

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 556496326 173 PINREVIQNQFLEMQRKLKKTVMLVSHDIDEALKLGDRIAVFRQGKIVQ 221
Cdd:cd03297  164 RALRLQLLPELKQIKKNLNIPVIFVTHDLSEAEYLADRIVVMEDGRLQY 212
LivG COG0411
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ...
 1-233 2.57e-51

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: 172.15  E-value: 2.57e-51
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556496326   1 MIKLENLTKHFsqkhGqTFKAVDNVNLNVPEGEMCVLLGPSGCGKTTTLKMINRLITPSSGTILINGEDTSGMDTVTL-R 79
Cdd:COG0411    4 LLEVRGLTKRF----G-GLVAVDDVSLEVERGEIVGLIGPNGAGKTTLFNLITGFYRPTSGRILFDGRDITGLPPHRIaR 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556496326  80 RNIGYVIQQIGLFPNMTIEENITV----------VPRMLGWDKAR-----CKTRAEELMDMVALDPHkfLNRYPREMSGG 144
Cdd:COG0411   79 LGIARTFQNPRLFPELTVLENVLVaaharlgrglLAALLRLPRARreereARERAEELLERVGLADR--ADEPAGNLSYG 156

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556496326 145 QQQRIGVIRALAADPPVLLMDEPFGAVDPINREVIQNQFLEMQRKLKKTVMLVSHDIDEALKLGDRIAVFRQGKIVQCAS 224
Cdd:COG0411  157 QQRRLEIARALATEPKLLLLDEPAAGLNPEETEELAELIRRLRDERGITILLIEHDMDLVMGLADRIVVLDFGRVIAEGT 236


                 ....*....
gi 556496326 225 PDELLAKPA 233
Cdd:COG0411  237 PAEVRADPR 245
ABCC_MRP_Like cd03228
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ...
 2-218 1.54e-50

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: 167.17  E-value: 1.54e-50
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556496326   2 IKLENLTKHFSqkhGQTFKAVDNVNLNVPEGEMCVLLGPSGCGKTTTLKMINRLITPSSGTILINGEDTSGMDTVTLRRN 81
Cdd:cd03228    1 IEFKNVSFSYP---GRPKPVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGVDLRDLDLESLRKN 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556496326  82 IGYVIQQIGLFpNMTIEENItvvprmlgwdkarcktraeelmdmvaldphkflnrypreMSGGQQQRIGVIRALAADPPV 161
Cdd:cd03228   78 IAYVPQDPFLF-SGTIRENI---------------------------------------LSGGQRQRIAIARALLRDPPI 117

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 556496326 162 LLMDEPFGAVDPINREVIQNQFLEMQRklKKTVMLVSHDIdEALKLGDRIAVFRQGK 218
Cdd:cd03228  118 LILDEATSALDPETEALILEALRALAK--GKTVIVIAHRL-STIRDADRIIVLDDGR 171
ABC_tran pfam00005
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ...
 22-168 2.57e-50

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: 165.90  E-value: 2.57e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556496326   22 VDNVNLNVPEGEMCVLLGPSGCGKTTTLKMINRLITPSSGTILINGEDTSGMDTVTLRRNIGYVIQQIGLFPNMTIEENI 101
Cdd:pfam00005   1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDLTDDERKSLRKEIGYVFQDPQLFPRLTVRENL 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 556496326  102 TVVPRMLGWDKARCKTRAEELMDMVAL--DPHKFLNRYPREMSGGQQQRIGVIRALAADPPVLLMDEPF 168
Cdd:pfam00005  81 RLGLLLKGLSKREKDARAEEALEKLGLgdLADRPVGERPGTLSGGQRQRVAIARALLTKPKLLLLDEPT 149
ABC_Mj1267_LivG_branched cd03219
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ...
 2-233 2.66e-50

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: 168.77  E-value: 2.66e-50
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556496326   2 IKLENLTKHFsqkhGQtFKAVDNVNLNVPEGEMCVLLGPSGCGKTTTLKMINRLITPSSGTILINGEDTSGMD-TVTLRR 80
Cdd:cd03219    1 LEVRGLTKRF----GG-LVALDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFDGEDITGLPpHEIARL 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556496326  81 NIGYVIQQIGLFPNMTIEENITVV------PRMLGWDKARCKT----RAEELMDMVALDPHkfLNRYPREMSGGQQQRIG 150
Cdd:cd03219   76 GIGRTFQIPRLFPELTVLENVMVAaqartgSGLLLARARREEReareRAEELLERVGLADL--ADRPAGELSYGQQRRLE 153

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556496326 151 VIRALAADPPVLLMDEPFGAVDPINREVIQNQFLEMqRKLKKTVMLVSHDIDEALKLGDRIAVFRQGKIVQCASPDELLA 230
Cdd:cd03219  154 IARALATDPKLLLLDEPAAGLNPEETEELAELIREL-RERGITVLLVEHDMDVVMSLADRVTVLDQGRVIAEGTPDEVRN 232


                 ...
gi 556496326 231 KPA 233
Cdd:cd03219  233 NPR 235
ugpC PRK11650
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
1-242 2.73e-50

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


Pssm-ID: 236947 [Multi-domain]  Cd Length: 356  Bit Score: 172.34  E-value: 2.73e-50
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556496326   1 MIKLENLTKHFSQKHgqtfKAVDNVNLNVPEGEMCVLLGPSGCGKTTTLKMINRLITPSSGTILINGEDTSGMDTVtlRR 80
Cdd:PRK11650   3 GLKLQAVRKSYDGKT----QVIKGIDLDVADGEFIVLVGPSGCGKSTLLRMVAGLERITSGEIWIGGRVVNELEPA--DR 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556496326  81 NIGYVIQQIGLFPNMTIEENITVVPRMLGWDKARCKTRAEELMDMVALDPhkFLNRYPREMSGGQQQRIGVIRALAADPP 160
Cdd:PRK11650  77 DIAMVFQNYALYPHMSVRENMAYGLKIRGMPKAEIEERVAEAARILELEP--LLDRKPRELSGGQRQRVAMGRAIVREPA 154

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556496326 161 VLLMDEPFGAVDPINREVIQNQFLEMQRKLKKTVMLVSHDIDEALKLGDRIAVFRQGKIVQCASPDELLAKPANEFVGSF 240
Cdd:PRK11650 155 VFLFDEPLSNLDAKLRVQMRLEIQRLHRRLKTTSLYVTHDQVEAMTLADRVVVMNGGVAEQIGTPVEVYEKPASTFVASF 234


                 ..
gi 556496326 241 VG 242
Cdd:PRK11650 235 IG 236
ArtP COG4161
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
2-221 4.34e-50

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


Pssm-ID: 443326 [Multi-domain]  Cd Length: 242  Bit Score: 168.27  E-value: 4.34e-50
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556496326   2 IKLENLTKHFSqkhgqTFKAVDNVNLNVPEGEMCVLLGPSGCGKTTTLKMINRLITPSSGTILINGEDTSGMDTVT---- 77
Cdd:COG4161    3 IQLKNINCFYG-----SHQALFDINLECPSGETLVLLGPSGAGKSSLLRVLNLLETPDSGQLNIAGHQFDFSQKPSekai 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556496326  78 --LRRNIGYVIQQIGLFPNMTIEENITVVP-RMLGWDKARCKTRAEELMDMVALDPhkFLNRYPREMSGGQQQRIGVIRA 154
Cdd:COG4161   78 rlLRQKVGMVFQQYNLWPHLTVMENLIEAPcKVLGLSKEQAREKAMKLLARLRLTD--KADRFPLHLSGGQQQRVAIARA 155

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556496326 155 LAADPPVLLMDEPFGAVDPinreVIQNQFLEMQRKLKK---TVMLVSHDIDEALKLGDRIAVFRQGKIVQ 221
Cdd:COG4161  156 LMMEPQVLLFDEPTAALDP----EITAQVVEIIRELSQtgiTQVIVTHEVEFARKVASQVVYMEKGRIIE 221
ThiQ COG3840
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
1-243 4.80e-50

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


Pssm-ID: 443051 [Multi-domain]  Cd Length: 232  Bit Score: 168.01  E-value: 4.80e-50
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556496326   1 MIKLENLTKHFsqkHGQTFKAvdnvNLNVPEGEMCVLLGPSGCGKTTTLKMINRLITPSSGTILINGEDTSgmDTVTLRR 80
Cdd:COG3840    1 MLRLDDLTYRY---GDFPLRF----DLTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILWNGQDLT--ALPPAER 71

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556496326  81 NIGYVIQQIGLFPNMTIEENITvvprmLGWDK-----ARCKTRAEELMDMVALDphKFLNRYPREMSGGQQQRIGVIRAL 155
Cdd:COG3840   72 PVSMLFQENNLFPHLTVAQNIG-----LGLRPglkltAEQRAQVEQALERVGLA--GLLDRLPGQLSGGQRQRVALARCL 144

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556496326 156 AADPPVLLMDEPFGAVDPINREviqnqflEM-------QRKLKKTVMLVSHDIDEALKLGDRIAVFRQGKIVQCASPDEL 228
Cdd:COG3840  145 VRKRPILLLDEPFSALDPALRQ-------EMldlvdelCRERGLTVLMVTHDPEDAARIADRVLLVADGRIAADGPTAAL 217

                        250
                 ....*....|....*
gi 556496326 229 LAKPANEFVGSFVGQ 243
Cdd:COG3840  218 LDGEPPPALAAYLGI 232
ABC_putative_ATPase cd03269
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ...
 2-220 2.00e-49

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: 165.53  E-value: 2.00e-49
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556496326   2 IKLENLTKHFSQKhgqtfKAVDNVNLNVPEGEMCVLLGPSGCGKTTTLKMINRLITPSSGTILINGEdtsGMDTVTlRRN 81
Cdd:cd03269    1 LEVENVTKRFGRV-----TALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDGK---PLDIAA-RNR 71

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556496326  82 IGYVIQQIGLFPNMTIEENITVVPRMLGWDKARCKTRAEELMDMVALDPHKflNRYPREMSGGQQQRIGVIRALAADPPV 161
Cdd:cd03269   72 IGYLPEERGLYPKMKVIDQLVYLAQLKGLKKEEARRRIDEWLERLELSEYA--NKRVEELSKGNQQKVQFIAAVIHDPEL 149

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 556496326 162 LLMDEPFGAVDPINREVIQNQFLEMQRKlKKTVMLVSHDIDEALKLGDRIAVFRQGKIV 220
Cdd:cd03269  150 LILDEPFSGLDPVNVELLKDVIRELARA-GKTVILSTHQMELVEELCDRVLLLNKGRAV 207
cbiO PRK13637
energy-coupling factor transporter ATPase;
2-227 2.35e-49

energy-coupling factor transporter ATPase;


Pssm-ID: 237455 [Multi-domain]  Cd Length: 287  Bit Score: 167.92  E-value: 2.35e-49
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556496326   2 IKLENLTKHFSQKHGQTFKAVDNVNLNVPEGEMCVLLGPSGCGKTTTLKMINRLITPSSGTILINGEDTS--GMDTVTLR 79
Cdd:PRK13637   3 IKIENLTHIYMEGTPFEKKALDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDGVDITdkKVKLSDIR 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556496326  80 RNIGYVIQ--QIGLFPNmTIEENITVVPRMLGWDKARCKTRAEELMDMVALDPHKFLNRYPREMSGGQQQRIGVIRALAA 157
Cdd:PRK13637  83 KKVGLVFQypEYQLFEE-TIEKDIAFGPINLGLSEEEIENRVKRAMNIVGLDYEDYKDKSPFELSGGQKRRVAIAGVVAM 161

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556496326 158 DPPVLLMDEPFGAVDPINREVIQNQFLEMQRKLKKTVMLVSHDIDEALKLGDRIAVFRQGKIVQCASPDE 227
Cdd:PRK13637 162 EPKILILDEPTAGLDPKGRDEILNKIKELHKEYNMTIILVSHSMEDVAKLADRIIVMNKGKCELQGTPRE 231
ModC COG4148
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ...
 24-233 2.46e-49

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: 169.90  E-value: 2.46e-49
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556496326  24 NVNLNVPEGEMCVLLGPSGCGKTTTLKMINRLITPSSGTILINGE----DTSGMDTVTLRRNIGYVIQQIGLFPNMTIEE 99
Cdd:COG4148   17 DVDFTLPGRGVTALFGPSGSGKTTLLRAIAGLERPDSGRIRLGGEvlqdSARGIFLPPHRRRIGYVFQEARLFPHLSVRG 96

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556496326 100 NITvvprmLGWDKARCKTRA---EELMDMVALDPHkfLNRYPREMSGGQQQRIGVIRALAADPPVLLMDEPFGAVD-PIN 175
Cdd:COG4148   97 NLL-----YGRKRAPRAERRisfDEVVELLGIGHL--LDRRPATLSGGERQRVAIGRALLSSPRLLLMDEPLAALDlARK 169

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 556496326 176 REVIqnQFLE-MQRKLKKTVMLVSHDIDEALKLGDRIAVFRQGKIVQCASPDELLAKPA 233
Cdd:COG4148  170 AEIL--PYLErLRDELDIPILYVSHSLDEVARLADHVVLLEQGRVVASGPLAEVLSRPD 226
CydC COG4987
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ...
 2-233 2.99e-49

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: 174.57  E-value: 2.99e-49
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556496326   2 IKLENLTKHFsqkHGQTFKAVDNVNLNVPEGEMCVLLGPSGCGKTTTLKMINRLITPSSGTILINGEDTSGMDTVTLRRN 81
Cdd:COG4987  334 LELEDVSFRY---PGAGRPVLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFLDPQSGSITLGGVDLRDLDEDDLRRR 410

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556496326  82 IGYVIQQIGLFpNMTIEENItvvprMLGWDKArckTRAE--ELMDMVALdpHKFLNRYP-----------REMSGGQQQR 148
Cdd:COG4987  411 IAVVPQRPHLF-DTTLRENL-----RLARPDA---TDEElwAALERVGL--GDWLAALPdgldtwlgeggRRLSGGERRR 479

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556496326 149 IGVIRALAADPPVLLMDEPFGAVDPIN-REVIQNQFLEMQRklkKTVMLVSHDIdEALKLGDRIAVFRQGKIVQCASPDE 227
Cdd:COG4987  480 LALARALLRDAPILLLDEPTEGLDAATeQALLADLLEALAG---RTVLLITHRL-AGLERMDRILVLEDGRIVEQGTHEE 555


                 ....*.
gi 556496326 228 LLAKPA 233
Cdd:COG4987  556 LLAQNG 561
artP PRK11124
arginine transporter ATP-binding subunit; Provisional
 2-221 1.56e-48

arginine transporter ATP-binding subunit; Provisional


Pssm-ID: 182980 [Multi-domain]  Cd Length: 242  Bit Score: 164.42  E-value: 1.56e-48
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556496326   2 IKLENLTKHFsqkhGQTfKAVDNVNLNVPEGEMCVLLGPSGCGKTTTLKMINRLITPSSGTILING------EDTSGMDT 75
Cdd:PRK11124   3 IQLNGINCFY----GAH-QALFDITLDCPQGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLNIAGnhfdfsKTPSDKAI 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556496326  76 VTLRRNIGYVIQQIGLFPNMTIEENITVVP-RMLGWDKARCKTRAEELMDMVALDPhkFLNRYPREMSGGQQQRIGVIRA 154
Cdd:PRK11124  78 RELRRNVGMVFQQYNLWPHLTVQQNLIEAPcRVLGLSKDQALARAEKLLERLRLKP--YADRFPLHLSGGQQQRVAIARA 155

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556496326 155 LAADPPVLLMDEPFGAVDPinreVIQNQFLEMQRKLKKT---VMLVSHDIDEALKLGDRIAVFRQGKIVQ 221
Cdd:PRK11124 156 LMMEPQVLLFDEPTAALDP----EITAQIVSIIRELAETgitQVIVTHEVEVARKTASRVVYMENGHIVE 221
PRK11000 PRK11000
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
2-242 3.85e-47

maltose/maltodextrin ABC transporter ATP-binding protein MalK;


Pssm-ID: 182893 [Multi-domain]  Cd Length: 369  Bit Score: 164.43  E-value: 3.85e-47
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556496326   2 IKLENLTKHFSQKHgqtfkAVDNVNLNVPEGEMCVLLGPSGCGKTTTLKMINRLITPSSGTILINGEDTSgmDTVTLRRN 81
Cdd:PRK11000   4 VTLRNVTKAYGDVV-----ISKDINLDIHEGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLFIGEKRMN--DVPPAERG 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556496326  82 IGYVIQQIGLFPNMTIEENITVVPRMLGWDKARCKTRAEELMDMVALDphKFLNRYPREMSGGQQQRIGVIRALAADPPV 161
Cdd:PRK11000  77 VGMVFQSYALYPHLSVAENMSFGLKLAGAKKEEINQRVNQVAEVLQLA--HLLDRKPKALSGGQRQRVAIGRTLVAEPSV 154

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556496326 162 LLMDEPFGAVDPINREVIQNQFLEMQRKLKKTVMLVSHDIDEALKLGDRIAVFRQGKIVQCASPDELLAKPANEFVGSFV 241
Cdd:PRK11000 155 FLLDEPLSNLDAALRVQMRIEISRLHKRLGRTMIYVTHDQVEAMTLADKIVVLDAGRVAQVGKPLELYHYPANRFVAGFI 234


                 .
gi 556496326 242 G 242
Cdd:PRK11000 235 G 235
ABC_ATPase cd00267
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ...
 3-218 4.24e-47

ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.


Pssm-ID: 213179 [Multi-domain]  Cd Length: 157  Bit Score: 157.79  E-value: 4.24e-47
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556496326   3 KLENLTKHFsqkhgQTFKAVDNVNLNVPEGEMCVLLGPSGCGKTTTLKMINRLITPSSGTILINGEDTSGMDTVTLRRNI 82
Cdd:cd00267    1 EIENLSFRY-----GGRTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGKDIAKLPLEELRRRI 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556496326  83 GYVIQqiglfpnmtieenitvvprmlgwdkarcktraeelmdmvaldphkflnrypreMSGGQQQRIGVIRALAADPPVL 162
Cdd:cd00267   76 GYVPQ-----------------------------------------------------LSGGQRQRVALARALLLNPDLL 102

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 556496326 163 LMDEPFGAVDPINREVIQNQFLEMQRKlKKTVMLVSHDIDEALKLGDRIAVFRQGK 218
Cdd:cd00267  103 LLDEPTSGLDPASRERLLELLRELAEE-GRTVIIVTHDPELAELAADRVIVLKDGK 157
MdlB COG1132
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
2-231 4.59e-47

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


Pssm-ID: 440747 [Multi-domain]  Cd Length: 579  Bit Score: 168.80  E-value: 4.59e-47
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556496326   2 IKLENLTkhFSqkHGQTFKAVDNVNLNVPEGEMCVLLGPSGCGKTTTLKMINRLITPSSGTILINGEDTSGMDTVTLRRN 81
Cdd:COG1132  340 IEFENVS--FS--YPGDRPVLKDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYDPTSGRILIDGVDIRDLTLESLRRQ 415

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556496326  82 IGYVIQQIGLFpNMTIEENITvvprmLGWDKArckTRAE--ELMDMVALdpHKFLNRYP-----------REMSGGQQQR 148
Cdd:COG1132  416 IGVVPQDTFLF-SGTIRENIR-----YGRPDA---TDEEveEAAKAAQA--HEFIEALPdgydtvvgergVNLSGGQRQR 484

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556496326 149 IGVIRALAADPPVLLMDEPFGAVDPINREVIQNQFLEMQRklKKTVMLVSHD---IDEAlklgDRIAVFRQGKIVQCASP 225
Cdd:COG1132  485 IAIARALLKDPPILILDEATSALDTETEALIQEALERLMK--GRTTIVIAHRlstIRNA----DRILVLDDGRIVEQGTH 558


                 ....*.
gi 556496326 226 DELLAK 231
Cdd:COG1132  559 EELLAR 564
CydD COG4988
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ...
 2-231 1.66e-46

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


Pssm-ID: 444012 [Multi-domain]  Cd Length: 563  Bit Score: 166.86  E-value: 1.66e-46
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556496326   2 IKLENLTkhFSqkHGQTFKAVDNVNLNVPEGEMCVLLGPSGCGKTTTLKMINRLITPSSGTILINGEDTSGMDTVTLRRN 81
Cdd:COG4988  337 IELEDVS--FS--YPGGRPALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPPYSGSILINGVDLSDLDPASWRRQ 412

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556496326  82 IGYVIQQIGLFPnMTIEENITvvprmLGWDKArckTRAE--ELMDMVALDphKFLNRYP-----------REMSGGQQQR 148
Cdd:COG4988  413 IAWVPQNPYLFA-GTIRENLR-----LGRPDA---SDEEleAALEAAGLD--EFVAALPdgldtplgeggRGLSGGQAQR 481

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556496326 149 IGVIRALAADPPVLLMDEPFGAVDPINREVIQNQFLEMQRklKKTVMLVSHDIdEALKLGDRIAVFRQGKIVQCASPDEL 228
Cdd:COG4988  482 LALARALLRDAPLLLLDEPTAHLDAETEAEILQALRRLAK--GRTVILITHRL-ALLAQADRILVLDDGRIVEQGTHEEL 558


                 ...
gi 556496326 229 LAK 231
Cdd:COG4988  559 LAK 561
ABC_NatA_sodium_exporter cd03266
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ...
 1-220 2.14e-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: 2.14e-46
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556496326   1 MIKLENLTKHFSQKHGqTFKAVDNVNLNVPEGEMCVLLGPSGCGKTTTLKMINRLITPSSGTILINGEDTSgMDTVTLRR 80
Cdd:cd03266    1 MITADALTKRFRDVKK-TVQAVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDGFDVV-KEPAEARR 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556496326  81 NIGYVIQQIGLFPNMTIEENITVVPRMLGWDKARCKTRAEELMDMvaLDPHKFLNRYPREMSGGQQQRIGVIRALAADPP 160
Cdd:cd03266   79 RLGFVSDSTGLYDRLTARENLEYFAGLYGLKGDELTARLEELADR--LGMEELLDRRVGGFSTGMRQKVAIARALVHDPP 156

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 556496326 161 VLLMDEPFGAVDPINREVIQnQFLEMQRKLKKTVMLVSHDIDEALKLGDRIAVFRQGKIV 220
Cdd:cd03266  157 VLLLDEPTTGLDVMATRALR-EFIRQLRALGKCILFSTHIMQEVERLCDRVVVLHRGRVV 215
tauB PRK11248
taurine ABC transporter ATP-binding subunit;
1-205 3.19e-46

taurine ABC transporter ATP-binding subunit;


Pssm-ID: 183056 [Multi-domain]  Cd Length: 255  Bit Score: 158.71  E-value: 3.19e-46
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556496326   1 MIKLENLTKHFSQKhgqtfKAVDNVNLNVPEGEMCVLLGPSGCGKTTTLKMINRLITPSSGTILINGEDTSGMDTvtlRR 80
Cdd:PRK11248   1 MLQISHLYADYGGK-----PALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDGKPVEGPGA---ER 72

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556496326  81 niGYVIQQIGLFPNMTIEENITVVPRMLGWDKARCKTRAEELMDMVALDphKFLNRYPREMSGGQQQRIGVIRALAADPP 160
Cdd:PRK11248  73 --GVVFQNEGLLPWRNVQDNVAFGLQLAGVEKMQRLEIAHQMLKKVGLE--GAEKRYIWQLSGGQRQRVGIARALAANPQ 148

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*
gi 556496326 161 VLLMDEPFGAVDPINREVIQNQFLEMQRKLKKTVMLVSHDIDEAL 205
Cdd:PRK11248 149 LLLLDEPFGALDAFTREQMQTLLLKLWQETGKQVLLITHDIEEAV 193
ABC_drug_resistance_like cd03264
ABC-type multidrug transport system, ATPase component; The biological function of this family ...
 2-222 3.21e-46

ABC-type multidrug transport system, ATPase component; The biological function of this family is not well characterized, but display ABC domains similar to members of ABCA subfamily. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.


Pssm-ID: 213231 [Multi-domain]  Cd Length: 211  Bit Score: 157.35  E-value: 3.21e-46
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556496326   2 IKLENLTKHFSQKHgqtfkAVDNVNLNVPEGeMCVLLGPSGCGKTTTLKMINRLITPSSGTILINGEDTSGMdTVTLRRN 81
Cdd:cd03264    1 LQLENLTKRYGKKR-----ALDGVSLTLGPG-MYGLLGPNGAGKTTLMRILATLTPPSSGTIRIDGQDVLKQ-PQKLRRR 73

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556496326  82 IGYVIQQIGLFPNMTIEENITVVPRMLGWDKARCKTRAEELMDMVALDPHKflNRYPREMSGGQQQRIGVIRALAADPPV 161
Cdd:cd03264   74 IGYLPQEFGVYPNFTVREFLDYIAWLKGIPSKEVKARVDEVLELVNLGDRA--KKKIGSLSGGMRRRVGIAQALVGDPSI 151

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 556496326 162 LLMDEPFGAVDPINREVIQNQFLEMQRklKKTVMLVSHDIDEALKLGDRIAVFRQGKIVQC 222
Cdd:cd03264  152 LIVDEPTAGLDPEERIRFRNLLSELGE--DRIVILSTHIVEDVESLCNQVAVLNKGKLVFE 210
ABC_Iron-Siderophores_B12_Hemin cd03214
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ...
 3-222 7.79e-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: 155.29  E-value: 7.79e-46
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556496326   3 KLENLTKHFSQKhgqtfKAVDNVNLNVPEGEMCVLLGPSGCGKTTTLKMINRLITPSSGTILINGEDTSGMDTVTLRRNI 82
Cdd:cd03214    1 EVENLSVGYGGR-----TVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDGKDLASLSPKELARKI 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556496326  83 GYVIQQIglfpnmtieenitvvprmlgwdkarcktraeELMDMVALdphkfLNRYPREMSGGQQQRIGVIRALAADPPVL 162
Cdd:cd03214   76 AYVPQAL-------------------------------ELLGLAHL-----ADRPFNELSGGERQRVLLARALAQEPPIL 119

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 556496326 163 LMDEPFGAVDPINreviQNQFLEMQRKLK----KTVMLVSHDIDEALKLGDRIAVFRQGKIVQC 222
Cdd:cd03214  120 LLDEPTSHLDIAH----QIELLELLRRLArergKTVVMVLHDLNLAARYADRVILLKDGRIVAQ 179
FtsE TIGR02673
cell division ATP-binding protein FtsE; This model describes FtsE, a member of the ABC ...
 1-218 8.51e-46

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: 156.25  E-value: 8.51e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556496326    1 MIKLENLTKHFsqkhGQTFKAVDNVNLNVPEGEMCVLLGPSGCGKTTTLKMINRLITPSSGTILINGEDTSGM---DTVT 77
Cdd:TIGR02673   1 MIEFHNVSKAY----PGGVAALHDVSLHIRKGEFLFLTGPSGAGKTTLLKLLYGALTPSRGQVRIAGEDVNRLrgrQLPL 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556496326   78 LRRNIGYVIQQIGLFPNMTIEENITVVPRMLGWDKARCKTRAEELMDMVALdPHKfLNRYPREMSGGQQQRIGVIRALAA 157
Cdd:TIGR02673  77 LRRRIGVVFQDFRLLPDRTVYENVALPLEVRGKKEREIQRRVGAALRQVGL-EHK-ADAFPEQLSGGEQQRVAIARAIVN 154

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 556496326  158 DPPVLLMDEPFGAVDPINREVIQNQFLEMQRkLKKTVMLVSHDIDEALKLGDRIAVFRQGK 218
Cdd:TIGR02673 155 SPPLLLADEPTGNLDPDLSERILDLLKRLNK-RGTTVIVATHDLSLVDRVAHRVIILDDGR 214
modC_ABC TIGR02142
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ...
 25-233 1.08e-45

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: 160.28  E-value: 1.08e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556496326   25 VNLNVPEGEMCVLLGPSGCGKTTTLKMINRLITPSSGTILINGE---DTS-GMDTVTLRRNIGYVIQQIGLFPNMTIEEN 100
Cdd:TIGR02142  16 ADFTLPGQGVTAIFGRSGSGKTTLIRLIAGLTRPDEGEIVLNGRtlfDSRkGIFLPPEKRRIGYVFQEARLFPHLSVRGN 95

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556496326  101 ItvvprMLGWDKARCKTRA---EELMDMVALDPhkFLNRYPREMSGGQQQRIGVIRALAADPPVLLMDEPFGAVD-PINR 176
Cdd:TIGR02142  96 L-----RYGMKRARPSERRisfERVIELLGIGH--LLGRLPGRLSGGEKQRVAIGRALLSSPRLLLMDEPLAALDdPRKY 168

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 556496326  177 EVIqnQFLE-MQRKLKKTVMLVSHDIDEALKLGDRIAVFRQGKIVQCASPDELLAKPA 233
Cdd:TIGR02142 169 EIL--PYLErLHAEFGIPILYVSHSLQEVLRLADRVVVLEDGRVAAAGPIAEVWASPD 224
LivF COG0410
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ...
 1-233 3.42e-45

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: 155.53  E-value: 3.42e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556496326   1 MIKLENLTKHFSQKHgqtfkAVDNVNLNVPEGEMCVLLGPSGCGKTTTLKMINRLITPSSGTILINGEDTSGMDTVTL-R 79
Cdd:COG0410    3 MLEVENLHAGYGGIH-----VLHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRSGSIRFDGEDITGLPPHRIaR 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556496326  80 RNIGYVIQQIGLFPNMTIEENItvvprMLGWDKARCKTRAEELMDMV-ALDP--HKFLNRYPREMSGGQQQRIGVIRALA 156
Cdd:COG0410   78 LGIGYVPEGRRIFPSLTVEENL-----LLGAYARRDRAEVRADLERVyELFPrlKERRRQRAGTLSGGEQQMLAIGRALM 152

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556496326 157 ADPPVLLMDEPFGAVDPinreVIQNQFLEMQRKLKK---TVMLVSHDIDEALKLGDRIAVFRQGKIVQCASPDELLAKPA 233
Cdd:COG0410  153 SRPKLLLLDEPSLGLAP----LIVEEIFEIIRRLNRegvTILLVEQNARFALEIADRAYVLERGRIVLEGTAAELLADPE 228
ABC_BcrA_bacitracin_resist cd03268
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ...
 2-220 4.26e-45

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: 154.30  E-value: 4.26e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556496326   2 IKLENLTKHFSQKHgqtfkAVDNVNLNVPEGEMCVLLGPSGCGKTTTLKMINRLITPSSGTILINGEDTSgmDTVTLRRN 81
Cdd:cd03268    1 LKTNDLTKTYGKKR-----VLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEITFDGKSYQ--KNIEALRR 73

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556496326  82 IGYVIQQIGLFPNMTIEENITVVPRMLGWDKARCktraEELMDMVALD--PHKFLNRYpremSGGQQQRIGVIRALAADP 159
Cdd:cd03268   74 IGALIEAPGFYPNLTARENLRLLARLLGIRKKRI----DEVLDVVGLKdsAKKKVKGF----SLGMKQRLGIALALLGNP 145

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 556496326 160 PVLLMDEPFGAVDPIN----REVIQNqflemQRKLKKTVMLVSHDIDEALKLGDRIAVFRQGKIV 220
Cdd:cd03268  146 DLLILDEPTNGLDPDGikelRELILS-----LRDQGITVLISSHLLSEIQKVADRIGIINKGKLI 205
ABC_TM1139_LivF_branched cd03224
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ...
 2-230 4.70e-45

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: 154.51  E-value: 4.70e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556496326   2 IKLENLTKHfsqkHGQtFKAVDNVNLNVPEGEMCVLLGPSGCGKTTTLKMINRLITPSSGTILINGEDTSGMDTVT-LRR 80
Cdd:cd03224    1 LEVENLNAG----YGK-SQILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDGRDITGLPPHErARA 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556496326  81 NIGYVIQQIGLFPNMTIEENItvvprMLGWdKARCKTRAEELMDMV-ALDP--HKFLNRYPREMSGGQQQRIGVIRALAA 157
Cdd:cd03224   76 GIGYVPEGRRIFPELTVEENL-----LLGA-YARRRAKRKARLERVyELFPrlKERRKQLAGTLSGGEQQMLAIARALMS 149

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 556496326 158 DPPVLLMDEPFGAVDPinreVIQNQFLEMQRKLKK---TVMLVSHDIDEALKLGDRIAVFRQGKIVQCASPDELLA 230
Cdd:cd03224  150 RPKLLLLDEPSEGLAP----KIVEEIFEAIRELRDegvTILLVEQNARFALEIADRAYVLERGRVVLEGTAAELLA 221
ABC_YhbG cd03218
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ...
 2-233 7.18e-45

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: 154.62  E-value: 7.18e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556496326   2 IKLENLTKHFSQKhgqtfKAVDNVNLNVPEGEMCVLLGPSGCGKTTTLKMINRLITPSSGTILINGEDTSG--MDTVTlR 79
Cdd:cd03218    1 LRAENLSKRYGKR-----KVVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDGQDITKlpMHKRA-R 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556496326  80 RNIGYVIQQIGLFPNMTIEENITVVPRMLGWDKARCKTRAEELMDMVALDphKFLNRYPREMSGGQQQRIGVIRALAADP 159
Cdd:cd03218   75 LGIGYLPQEASIFRKLTVEENILAVLEIRGLSKKEREEKLEELLEEFHIT--HLRKSKASSLSGGERRRVEIARALATNP 152

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 556496326 160 PVLLMDEPFGAVDPINREVIQNqfleMQRKLKKT---VMLVSHDIDEALKLGDRIAVFRQGKIVQCASPDELLAKPA 233
Cdd:cd03218  153 KFLLLDEPFAGVDPIAVQDIQK----IIKILKDRgigVLITDHNVRETLSITDRAYIIYEGKVLAEGTPEEIAANEL 225
PRK11264 PRK11264
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
 1-243 1.05e-44

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


Pssm-ID: 183063 [Multi-domain]  Cd Length: 250  Bit Score: 154.52  E-value: 1.05e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556496326   1 MIKLENLTKHFsqkHGQTfkAVDNVNLNVPEGEMCVLLGPSGCGKTTTLKMINRLITPSSGTILINGEDTSGMDTVT--- 77
Cdd:PRK11264   3 AIEVKNLVKKF---HGQT--VLHGIDLEVKPGEVVAIIGPSGSGKTTLLRCINLLEQPEAGTIRVGDITIDTARSLSqqk 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556496326  78 -----LRRNIGYVIQQIGLFPNMTIEENITVVPRML-GWDKARCKTRAEELMDMVALDPHKflNRYPREMSGGQQQRIGV 151
Cdd:PRK11264  78 glirqLRQHVGFVFQNFNLFPHRTVLENIIEGPVIVkGEPKEEATARARELLAKVGLAGKE--TSYPRRLSGGQQQRVAI 155

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556496326 152 IRALAADPPVLLMDEPFGAVDPinrEVIqNQFLEMQRKL---KKTVMLVSHDIDEALKLGDRIAVFRQGKIVQCASPDEL 228
Cdd:PRK11264 156 ARALAMRPEVILFDEPTSALDP---ELV-GEVLNTIRQLaqeKRTMVIVTHEMSFARDVADRAIFMDQGRIVEQGPAKAL 231

                        250
                 ....*....|....*....
gi 556496326 229 LAKPANE----FVGSFVGQ 243
Cdd:PRK11264 232 FADPQQPrtrqFLEKFLLQ 250
ABC_Metallic_Cations cd03235
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ...
 3-219 1.30e-44

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: 153.07  E-value: 1.30e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556496326   3 KLENLTKHFSQKHgqtfkAVDNVNLNVPEGEMCVLLGPSGCGKTTTLKMINRLITPSSGTILINGEDTSGMdtvtlRRNI 82
Cdd:cd03235    1 EVEDLTVSYGGHP-----VLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFGKPLEKE-----RKRI 70

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556496326  83 GYVIQQIGL---FPnMTIEEnitVV-------PRMLGWDKARCKTRAEELMDMVALDphKFLNRYPREMSGGQQQRIGVI 152
Cdd:cd03235   71 GYVPQRRSIdrdFP-ISVRD---VVlmglyghKGLFRRLSKADKAKVDEALERVGLS--ELADRQIGELSGGQQQRVLLA 144

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556496326 153 RALAADPPVLLMDEPFGAVDPINreviQNQFLEMQRKLK---KTVMLVSHDIDEALKLGDRIAVFRQGKI 219
Cdd:cd03235  145 RALVQDPDLLLLDEPFAGVDPKT----QEDIYELLRELRregMTILVVTHDLGLVLEYFDRVLLLNRTVV 210
PRK13651 PRK13651
cobalt transporter ATP-binding subunit; Provisional
 2-230 2.55e-44

cobalt transporter ATP-binding subunit; Provisional


Pssm-ID: 184210 [Multi-domain]  Cd Length: 305  Bit Score: 155.24  E-value: 2.55e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556496326   2 IKLENLTKHFSQKHGQTFKAVDNVNLNVPEGEMCVLLGPSGCGKTTTLKMINRLITPSSGTILINGED----------TS 71
Cdd:PRK13651   3 IKVKNIVKIFNKKLPTELKALDNVSVEINQGEFIAIIGQTGSGKTTFIEHLNALLLPDTGTIEWIFKDeknkkktkekEK 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556496326  72 GMDTVT--------------LRRNIGYVIQ--QIGLFPNmTIEENITVVPRMLGWDKARCKTRAEELMDMVALdPHKFLN 135
Cdd:PRK13651  83 VLEKLViqktrfkkikkikeIRRRVGVVFQfaEYQLFEQ-TIEKDIIFGPVSMGVSKEEAKKRAAKYIELVGL-DESYLQ 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556496326 136 RYPREMSGGQQQRIGVIRALAADPPVLLMDEPFGAVDPINREVIQNQFLEMQrKLKKTVMLVSHDIDEALKLGDRIAVFR 215
Cdd:PRK13651 161 RSPFELSGGQKRRVALAGILAMEPDFLVFDEPTAGLDPQGVKEILEIFDNLN-KQGKTIILVTHDLDNVLEWTKRTIFFK 239

                        250
                 ....*....|....*
gi 556496326 216 QGKIVQCASPDELLA 230
Cdd:PRK13651 240 DGKIIKDGDTYDILS 254
LptB COG1137
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ...
 1-232 4.83e-44

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


Pssm-ID: 440752 [Multi-domain]  Cd Length: 240  Bit Score: 152.49  E-value: 4.83e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556496326   1 MIKLENLTKHFSQKhgqtfKAVDNVNLNVPEGEMCVLLGPSGCGKTTTLKMINRLITPSSGTILINGEDtsgmdtVTL-- 78
Cdd:COG1137    3 TLEAENLVKSYGKR-----TVVKDVSLEVNQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGRIFLDGED------ITHlp 71

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556496326  79 -----RRNIGYVIQQIGLFPNMTIEENITVVPRMLGWDKARCKTRAEELMDMVALDPHKflNRYPREMSGGQQQRIGVIR 153
Cdd:COG1137   72 mhkraRLGIGYLPQEASIFRKLTVEDNILAVLELRKLSKKEREERLEELLEEFGITHLR--KSKAYSLSGGERRRVEIAR 149

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556496326 154 ALAADPPVLLMDEPFGAVDPINREVIQnqflEMQRKLKKT---VMLVSHDIDEALKLGDRIAVFRQGKIVQCASPDELLA 230
Cdd:COG1137  150 ALATNPKFILLDEPFAGVDPIAVADIQ----KIIRHLKERgigVLITDHNVRETLGICDRAYIISEGKVLAEGTPEEILN 225


                 ..
gi 556496326 231 KP 232
Cdd:COG1137  226 NP 227
CcmA COG4133
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ...
 1-210 1.96e-42

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: 147.24  E-value: 1.96e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556496326   1 MIKLENLTKHFSQKhgqtfKAVDNVNLNVPEGEMCVLLGPSGCGKTTTLKMINRLITPSSGTILINGEDTSgMDTVTLRR 80
Cdd:COG4133    2 MLEAENLSCRRGER-----LLFSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWNGEPIR-DAREDYRR 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556496326  81 NIGYVIQQIGLFPNMTIEENITVVPRMLGWDKARckTRAEELMDMVALDPHkfLNRYPREMSGGQQQRIGVIRALAADPP 160
Cdd:COG4133   76 RLAYLGHADGLKPELTVRENLRFWAALYGLRADR--EAIDEALEAVGLAGL--ADLPVRQLSAGQKRRVALARLLLSPAP 151

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 556496326 161 VLLMDEPFGAVDPINREVIQnQFLEMQRKLKKTVMLVSHDIDEA-----LKLGDR 210
Cdd:COG4133  152 LWLLDEPFTALDAAGVALLA-ELIAAHLARGGAVLLTTHQPLELaaarvLDLGDF 205
PRK14247 PRK14247
phosphate ABC transporter ATP-binding protein; Provisional
 20-241 5.87e-42

phosphate ABC transporter ATP-binding protein; Provisional


Pssm-ID: 172735 [Multi-domain]  Cd Length: 250  Bit Score: 147.37  E-value: 5.87e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556496326  20 KAVDNVNLNVPEGEMCVLLGPSGCGKTTTLKMINRLI-----TPSSGTILINGEDTSGMDTVTLRRNIGYVIQQIGLFPN 94
Cdd:PRK14247  17 EVLDGVNLEIPDNTITALMGPSGSGKSTLLRVFNRLIelypeARVSGEVYLDGQDIFKMDVIELRRRVQMVFQIPNPIPN 96

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556496326  95 MTIEENITVVPRM--LGWDKARCKTRAEELMDMVAL--DPHKFLNRYPREMSGGQQQRIGVIRALAADPPVLLMDEPFGA 170
Cdd:PRK14247  97 LSIFENVALGLKLnrLVKSKKELQERVRWALEKAQLwdEVKDRLDAPAGKLSGGQQQRLCIARALAFQPEVLLADEPTAN 176

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 556496326 171 VDPINREVIQNQFLEMQRKLkkTVMLVSHDIDEALKLGDRIAVFRQGKIVQCASPDELLAKPANEFVGSFV 241
Cdd:PRK14247 177 LDPENTAKIESLFLELKKDM--TIVLVTHFPQQAARISDYVAFLYKGQIVEWGPTREVFTNPRHELTEKYV 245
YejF COG4172
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ...
 2-235 6.10e-42

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: 154.07  E-value: 6.10e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556496326   2 IKLENLTKHFSQKHG------QTFKAVDNVNLNVPEGEMCVLLGPSGCGKTTTLKMINRLItPSSGTILINGEDTSGMDT 75
Cdd:COG4172  276 LEARDLKVWFPIKRGlfrrtvGHVKAVDGVSLTLRRGETLGLVGESGSGKSTLGLALLRLI-PSEGEIRFDGQDLDGLSR 354

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556496326  76 ---VTLRRNIgyviqQI-------GLFPNMTIEENIT---VVPRMlGWDKARCKTRAEELMDMVALDPhKFLNRYPREMS 142
Cdd:COG4172  355 ralRPLRRRM-----QVvfqdpfgSLSPRMTVGQIIAeglRVHGP-GLSAAERRARVAEALEEVGLDP-AARHRYPHEFS 427

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556496326 143 GGQQQRIGVIRALAADPPVLLMDEPFGAVDpinreV-IQNQFLEM----QRKLKKTVMLVSHDideaLK----LGDRIAV 213
Cdd:COG4172  428 GGQRQRIAIARALILEPKLLVLDEPTSALD-----VsVQAQILDLlrdlQREHGLAYLFISHD----LAvvraLAHRVMV 498

                        250       260
                 ....*....|....*....|..
gi 556496326 214 FRQGKIVQCASPDELLAKPANE 235
Cdd:COG4172  499 MKDGKVVEQGPTEQVFDAPQHP 520
L_ocin_972_ABC TIGR03608
putative bacteriocin export ABC transporter, lactococcin 972 group; A gene pair with a fairly ...
 4-211 6.16e-42

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


Pssm-ID: 188353 [Multi-domain]  Cd Length: 206  Bit Score: 145.84  E-value: 6.16e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556496326    4 LENLTKHFSQKHgqtfkAVDNVNLNVPEGEMCVLLGPSGCGKTTTLKMINRLITPSSGTILINGEDT---SGMDTVTLRR 80
Cdd:TIGR03608   1 LKNISKKFGDKV-----ILDDLNLTIEKGKMYAIIGESGSGKSTLLNIIGLLEKFDSGQVYLNGQETpplNSKKASKFRR 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556496326   81 N-IGYVIQQIGLFPNMTIEENITVVPRMLGWDKARCKTRAEELMDMVALDphKFLNRYPREMSGGQQQRIGVIRALAADP 159
Cdd:TIGR03608  76 EkLGYLFQNFALIENETVEENLDLGLKYKKLSKKEKREKKKEALEKVGLN--LKLKQKIYELSGGEQQRVALARAILKPP 153

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 556496326  160 PVLLMDEPFGAVDPINREVIQNQFLEMQRKlKKTVMLVSHDIdEALKLGDRI 211
Cdd:TIGR03608 154 PLILADEPTGSLDPKNRDEVLDLLLELNDE-GKTIIIVTHDP-EVAKQADRV 203
cbiO PRK13645
energy-coupling factor transporter ATPase;
2-230 6.83e-42

energy-coupling factor transporter ATPase;


Pssm-ID: 184204 [Multi-domain]  Cd Length: 289  Bit Score: 148.62  E-value: 6.83e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556496326   2 IKLENLTKHFSQKHGQTFKAVDNVNLNVPEGEMCVLLGPSGCGKTTTLKMINRLITPSSG-TILINGEDTSGMDTVT--- 77
Cdd:PRK13645   7 IILDNVSYTYAKKTPFEFKALNNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGLIISETGqTIVGDYAIPANLKKIKevk 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556496326  78 -LRRNIGYVIQ--QIGLFPNmTIEENITVVPRMLGWDKARCKTRAEELMDMVALdPHKFLNRYPREMSGGQQQRIGVIRA 154
Cdd:PRK13645  87 rLRKEIGLVFQfpEYQLFQE-TIEKDIAFGPVNLGENKQEAYKKVPELLKLVQL-PEDYVKRSPFELSGGQKRRVALAGI 164

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 556496326 155 LAADPPVLLMDEPFGAVDPINREVIQNQFLEMQRKLKKTVMLVSHDIDEALKLGDRIAVFRQGKIVQCASPDELLA 230
Cdd:PRK13645 165 IAMDGNTLVLDEPTGGLDPKGEEDFINLFERLNKEYKKRIIMVTHNMDQVLRIADEVIVMHEGKVISIGSPFEIFS 240
ABC_FtsE cd03292
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ...
 2-219 1.87e-41

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: 144.86  E-value: 1.87e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556496326   2 IKLENLTKhfsqKHGQTFKAVDNVNLNVPEGEMCVLLGPSGCGKTTTLKMINRLITPSSGTILINGEDTSGMD---TVTL 78
Cdd:cd03292    1 IEFINVTK----TYPNGTAALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQDVSDLRgraIPYL 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556496326  79 RRNIGYVIQQIGLFPNMTIEENITVVPRMLGWDKARCKTRAEELMDMVALDpHKfLNRYPREMSGGQQQRIGVIRALAAD 158
Cdd:cd03292   77 RRKIGVVFQDFRLLPDRNVYENVAFALEVTGVPPREIRKRVPAALELVGLS-HK-HRALPAELSGGEQQRVAIARAIVNS 154

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 556496326 159 PPVLLMDEPFGAVDPINREVIQNqFLEMQRKLKKTVMLVSHDIDEALKLGDRIAVFRQGKI 219
Cdd:cd03292  155 PTILIADEPTGNLDPDTTWEIMN-LLKKINKAGTTVVVATHAKELVDTTRHRVIALERGKL 214
ABC_ThiQ_thiamine_transporter cd03298
ATP-binding cassette domain of the thiamine transport system; Part of the ...
 27-220 2.96e-41

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: 144.56  E-value: 2.96e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556496326  27 LNVPEGEMCVLLGPSGCGKTTTLKMINRLITPSSGTILINGEDTSGMDTVtlRRNIGYVIQQIGLFPNMTIEENIT--VV 104
Cdd:cd03298   19 LTFAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLINGVDVTAAPPA--DRPVSMLFQENNLFAHLTVEQNVGlgLS 96

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556496326 105 PRM-LgwdKARCKTRAEELMDMVALDphKFLNRYPREMSGGQQQRIGVIRALAADPPVLLMDEPFGAVDPINREVIQNQF 183
Cdd:cd03298   97 PGLkL---TAEDRQAIEVALARVGLA--GLEKRLPGELSGGERQRVALARVLVRDKPVLLLDEPFAALDPALRAEMLDLV 171

                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 556496326 184 LEMQRKLKKTVMLVSHDIDEALKLGDRIAVFRQGKIV 220
Cdd:cd03298  172 LDLHAETKMTVLMVTHQPEDAKRLAQRVVFLDNGRIA 208
met_CoM_red_A2 TIGR03269
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ...
 1-230 3.12e-41

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: 151.88  E-value: 3.12e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556496326    1 MIKLENLTKHFSQKHGQTFKAVDNVNLNVPEGEMCVLLGPSGCGKTTTLKMINRLITPSSGTILIN-GEDTSGMDT--VT 77
Cdd:TIGR03269 279 IIKVRNVSKRYISVDRGVVKAVDNVSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGEVNVRvGDEWVDMTKpgPD 358

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556496326   78 LR----RNIGYVIQQIGLFPNMTIEENITV-----VPRMLGwdkarcKTRAEELMDMVALDPHK---FLNRYPREMSGGQ 145
Cdd:TIGR03269 359 GRgrakRYIGILHQEYDLYPHRTVLDNLTEaigleLPDELA------RMKAVITLKMVGFDEEKaeeILDKYPDELSEGE 432

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556496326  146 QQRIGVIRALAADPPVLLMDEPFGAVDPINREVIQNQFLEMQRKLKKTVMLVSHDIDEALKLGDRIAVFRQGKIVQCASP 225
Cdd:TIGR03269 433 RHRVALAQVLIKEPRIVILDEPTGTMDPITKVDVTHSILKAREEMEQTFIIVSHDMDFVLDVCDRAALMRDGKIVKIGDP 512


                  ....*
gi 556496326  226 DELLA 230
Cdd:TIGR03269 513 EEIVE 517
ntrCD TIGR01184
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ...
 22-217 7.05e-41

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: 144.15  E-value: 7.05e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556496326   22 VDNVNLNVPEGEMCVLLGPSGCGKTTTLKMINRLITPSSGTILINGE--DTSGMDTVTlrrnigyVIQQIGLFPNMTIEE 99
Cdd:TIGR01184   1 LKGVNLTIQQGEFISLIGHSGCGKSTLLNLISGLAQPTSGGVILEGKqiTEPGPDRMV-------VFQNYSLLPWLTVRE 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556496326  100 NITVVPRMLGWDKARCKTRA--EELMDMVALdpHKFLNRYPREMSGGQQQRIGVIRALAADPPVLLMDEPFGAVDPINRE 177
Cdd:TIGR01184  74 NIALAVDRVLPDLSKSERRAivEEHIALVGL--TEAADKRPGQLSGGMKQRVAIARALSIRPKVLLLDEPFGALDALTRG 151

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 556496326  178 VIQNQFLEMQRKLKKTVMLVSHDIDEALKLGDRIAVFRQG 217
Cdd:TIGR01184 152 NLQEELMQIWEEHRVTVLMVTHDVDEALLLSDRVVMLTNG 191
thiQ PRK10771
thiamine ABC transporter ATP-binding protein ThiQ;
1-235 1.06e-40

thiamine ABC transporter ATP-binding protein ThiQ;


Pssm-ID: 182716 [Multi-domain]  Cd Length: 232  Bit Score: 143.57  E-value: 1.06e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556496326   1 MIKLENLTKHFSQKHgQTFkavdnvNLNVPEGEMCVLLGPSGCGKTTTLKMINRLITPSSGTILINGEDTSgmDTVTLRR 80
Cdd:PRK10771   1 MLKLTDITWLYHHLP-MRF------DLTVERGERVAILGPSGAGKSTLLNLIAGFLTPASGSLTLNGQDHT--TTPPSRR 71

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556496326  81 NIGYVIQQIGLFPNMTIEENITvvprmLGWD-----KARCKTRAEELMDMVALDPhkFLNRYPREMSGGQQQRIGVIRAL 155
Cdd:PRK10771  72 PVSMLFQENNLFSHLTVAQNIG-----LGLNpglklNAAQREKLHAIARQMGIED--LLARLPGQLSGGQRQRVALARCL 144

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556496326 156 AADPPVLLMDEPFGAVDPINReviqNQFLEM------QRKLkkTVMLVSHDIDEALKLGDRIAVFRQGKIVQCASPDELL 229
Cdd:PRK10771 145 VREQPILLLDEPFSALDPALR----QEMLTLvsqvcqERQL--TLLMVSHSLEDAARIAPRSLVVADGRIAWDGPTDELL 218


                 ....*.
gi 556496326 230 AKPANE 235
Cdd:PRK10771 219 SGKASA 224
PRK15079 PRK15079
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
 1-232 4.18e-40

oligopeptide ABC transporter ATP-binding protein OppF; Provisional


Pssm-ID: 185037 [Multi-domain]  Cd Length: 331  Bit Score: 144.85  E-value: 4.18e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556496326   1 MIKLENLTKHFSQKHG--------QTFKAVDNVNLNVPEGEMCVLLGPSGCGKTTTLKMINRLITPSSGTILINGEDTSG 72
Cdd:PRK15079   8 LLEVADLKVHFDIKDGkqwfwqppKTLKAVDGVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGEVAWLGKDLLG 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556496326  73 MDTVTlRRNIGYVIQQI------GLFPNMTIEENI-----TVVPRMlgwDKARCKTRAEELMDMVALDPHkFLNRYPREM 141
Cdd:PRK15079  88 MKDDE-WRAVRSDIQMIfqdplaSLNPRMTIGEIIaeplrTYHPKL---SRQEVKDRVKAMMLKVGLLPN-LINRYPHEF 162

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556496326 142 SGGQQQRIGVIRALAADPPVLLMDEPFGAVD-PINREVIqNQFLEMQRKLKKTVMLVSHDIDEALKLGDRIAVFRQGKIV 220
Cdd:PRK15079 163 SGGQCQRIGIARALILEPKLIICDEPVSALDvSIQAQVV-NLLQQLQREMGLSLIFIAHDLAVVKHISDRVLVMYLGHAV 241

                        250
                 ....*....|..
gi 556496326 221 QCASPDELLAKP 232
Cdd:PRK15079 242 ELGTYDEVYHNP 253
PRK14246 PRK14246
phosphate ABC transporter ATP-binding protein; Provisional
 24-241 4.22e-40

phosphate ABC transporter ATP-binding protein; Provisional


Pssm-ID: 172734 [Multi-domain]  Cd Length: 257  Bit Score: 142.88  E-value: 4.22e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556496326  24 NVNLNVPEGEMCVLLGPSGCGKTTTLKMINRLI------TPSSGTILINGEDTSGMDTVTLRRNIGYVIQQIGLFPNMTI 97
Cdd:PRK14246  28 DITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLIeiydskIKVDGKVLYFGKDIFQIDAIKLRKEVGMVFQQPNPFPHLSI 107

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556496326  98 EENITVVPRMLGW-DKARCKTRAEELMDMVAL--DPHKFLNRYPREMSGGQQQRIGVIRALAADPPVLLMDEPFGAVDPI 174
Cdd:PRK14246 108 YDNIAYPLKSHGIkEKREIKKIVEECLRKVGLwkEVYDRLNSPASQLSGGQQQRLTIARALALKPKVLLMDEPTSMIDIV 187

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 556496326 175 NREVIQNQFLEMQRKLkkTVMLVSHDIDEALKLGDRIAVFRQGKIVQCASPDELLAKPANEFVGSFV 241
Cdd:PRK14246 188 NSQAIEKLITELKNEI--AIVIVSHNPQQVARVADYVAFLYNGELVEWGSSNEIFTSPKNELTEKYV 252
PRK14239 PRK14239
phosphate transporter ATP-binding protein; Provisional
 1-235 6.13e-40

phosphate transporter ATP-binding protein; Provisional


Pssm-ID: 184585 [Multi-domain]  Cd Length: 252  Bit Score: 142.22  E-value: 6.13e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556496326   1 MIKLENLTKHFSQKhgqtfKAVDNVNLNVPEGEMCVLLGPSGCGKTTTLKMINRL--ITPS---SGTILINGEDTSG--M 73
Cdd:PRK14239   5 ILQVSDLSVYYNKK-----KALNSVSLDFYPNEITALIGPSGSGKSTLLRSINRMndLNPEvtiTGSIVYNGHNIYSprT 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556496326  74 DTVTLRRNIGYVIQQIGLFPnMTIEENITVVPRMLGW-DKARCKTRAEELMDMVAL-DPHK-FLNRYPREMSGGQQQRIG 150
Cdd:PRK14239  80 DTVDLRKEIGMVFQQPNPFP-MSIYENVVYGLRLKGIkDKQVLDEAVEKSLKGASIwDEVKdRLHDSALGLSGGQQQRVC 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556496326 151 VIRALAADPPVLLMDEPFGAVDPINREVIQNQFLEMqrKLKKTVMLVSHDIDEALKLGDRIAVFRQGKIVQCASPDELLA 230
Cdd:PRK14239 159 IARVLATSPKIILLDEPTSALDPISAGKIEETLLGL--KDDYTMLLVTRSMQQASRISDRTGFFLDGDLIEYNDTKQMFM 236


                 ....*
gi 556496326 231 KPANE 235
Cdd:PRK14239 237 NPKHK 241
LPS_export_lptB TIGR04406
LPS export ABC transporter ATP-binding protein; Members of this fmaily are LptB, the ...
 2-232 6.24e-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: 6.24e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556496326    2 IKLENLTKHFSQKhgqtfKAVDNVNLNVPEGEMCVLLGPSGCGKTTTLKMINRLITPSSGTILINGEDTSGMDT-VTLRR 80
Cdd:TIGR04406   2 LVAENLIKSYKKR-----KVVNDVSLSVKSGEIVGLLGPNGAGKTTSFYMIVGLVRPDAGKILIDGQDITHLPMhERARL 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556496326   81 NIGYVIQQIGLFPNMTIEENI-TVVPRMLGWDKARCKTRAEELMDMVALDpHKFLNRYPrEMSGGQQQRIGVIRALAADP 159
Cdd:TIGR04406  77 GIGYLPQEASIFRKLTVEENImAVLEIRKDLDRAEREERLEALLEEFQIS-HLRDNKAM-SLSGGERRRVEIARALATNP 154

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 556496326  160 PVLLMDEPFGAVDPINREVIQNQFlemqRKLKKT---VMLVSHDIDEALKLGDRIAVFRQGKIVQCASPDELLAKP 232
Cdd:TIGR04406 155 KFILLDEPFAGVDPIAVGDIKKII----KHLKERgigVLITDHNVRETLDICDRAYIISDGKVLAEGTPAEIVANE 226
YbbA COG4181
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ...
 1-221 6.61e-40

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: 141.42  E-value: 6.61e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556496326   1 MIKLENLTKHFSQKHGQTfKAVDNVNLNVPEGEMCVLLGPSGCGKTTTLKMINRLITPSSGTILINGEDTSGMDT---VT 77
Cdd:COG4181    8 IIELRGLTKTVGTGAGEL-TILKGISLEVEAGESVAIVGASGSGKSTLLGLLAGLDRPTSGTVRLAGQDLFALDEdarAR 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556496326  78 LR-RNIGYVIQQIGLFPNMTIEENItvvprML-----GWDKARckTRAEELMDMVALDpHKfLNRYPREMSGGQQQRIGV 151
Cdd:COG4181   87 LRaRHVGFVFQSFQLLPTLTALENV-----MLplelaGRRDAR--ARARALLERVGLG-HR-LDHYPAQLSGGEQQRVAL 157

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556496326 152 IRALAADPPVLLMDEPFGAVDPINREVIQNQFLEMQRKLKKTVMLVSHDIDEALKLgDRIAVFRQGKIVQ 221
Cdd:COG4181  158 ARAFATEPAILFADEPTGNLDAATGEQIIDLLFELNRERGTTLVLVTHDPALAARC-DRVLRLRAGRLVE 226
ABCC_bacteriocin_exporters cd03245
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ...
 2-220 8.06e-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: 8.06e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556496326   2 IKLENLTKHFSqkhGQTFKAVDNVNLNVPEGEMCVLLGPSGCGKTTTLKMINRLITPSSGTILINGEDTSGMDTVTLRRN 81
Cdd:cd03245    3 IEFRNVSFSYP---NQEIPALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGTDIRQLDPADLRRN 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556496326  82 IGYVIQQIGLFpNMTIEENITVvprmlgwdkARCKTRAEELMDMVALDP-HKFLNRYP-----------REMSGGQQQRI 149
Cdd:cd03245   80 IGYVPQDVTLF-YGTLRDNITL---------GAPLADDERILRAAELAGvTDFVNKHPngldlqigergRGLSGGQRQAV 149

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 556496326 150 GVIRALAADPPVLLMDEPFGAVDpINREviqNQFLEMQRKLK--KTVMLVSHDIdEALKLGDRIAVFRQGKIV 220
Cdd:cd03245  150 ALARALLNDPPILLLDEPTSAMD-MNSE---ERLKERLRQLLgdKTLIIITHRP-SLLDLVDRIIVMDSGRIV 217
MglA COG1129
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
1-228 1.67e-39

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


Pssm-ID: 440745 [Multi-domain]  Cd Length: 497  Bit Score: 146.70  E-value: 1.67e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556496326   1 MIKLENLTKHFSqkhgqTFKAVDNVNLNVPEGEMCVLLGPSGCGKTTTLKMINRLITPSSGTILINGEDTSGMDTVTLRR 80
Cdd:COG1129    4 LLEMRGISKSFG-----GVKALDGVSLELRPGEVHALLGENGAGKSTLMKILSGVYQPDSGEILLDGEPVRFRSPRDAQA 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556496326  81 N-IGYVIQQIGLFPNMTIEENITV--VPRMLGW-DKARCKTRAEELMDMV--ALDPHKFLnrypREMSGGQQQRIGVIRA 154
Cdd:COG1129   79 AgIAIIHQELNLVPNLSVAENIFLgrEPRRGGLiDWRAMRRRARELLARLglDIDPDTPV----GDLSVAQQQLVEIARA 154

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 556496326 155 LAADPPVLLMDEPFGAVDPinREViqNQFLEMQRKLKK---TVMLVSHDIDEALKLGDRIAVFRQGKIVQCASPDEL 228
Cdd:COG1129  155 LSRDARVLILDEPTASLTE--REV--ERLFRIIRRLKAqgvAIIYISHRLDEVFEIADRVTVLRDGRLVGTGPVAEL 227
HisP COG4598
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism];
1-235 6.00e-39

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


Pssm-ID: 443652 [Multi-domain]  Cd Length: 259  Bit Score: 139.55  E-value: 6.00e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556496326   1 MIKLENLTKHFSQKhgQTFKAVDnvnLNVPEGEMCVLLGPSGCGKTTTLKMINRLITPSSGTILINGE------DTSGMD 74
Cdd:COG4598    8 ALEVRDLHKSFGDL--EVLKGVS---LTARKGDVISIIGSSGSGKSTFLRCINLLETPDSGEIRVGGEeirlkpDRDGEL 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556496326  75 TVT-------LRRNIGYVIQQIGLFPNMTIEENITVVP-RMLGWDKARCKTRAEELMDMVALdpHKFLNRYPREMSGGQQ 146
Cdd:COG4598   83 VPAdrrqlqrIRTRLGMVFQSFNLWSHMTVLENVIEAPvHVLGRPKAEAIERAEALLAKVGL--ADKRDAYPAHLSGGQQ 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556496326 147 QRIGVIRALAADPPVLLMDEPFGAVDP-INREViqnqfLEMQRKLK---KTVMLVSHDIDEALKLGDRIAVFRQGKIVQC 222
Cdd:COG4598  161 QRAAIARALAMEPEVMLFDEPTSALDPeLVGEV-----LKVMRDLAeegRTMLVVTHEMGFARDVSSHVVFLHQGRIEEQ 235

                        250
                 ....*....|...
gi 556496326 223 ASPDELLAKPANE 235
Cdd:COG4598  236 GPPAEVFGNPKSE 248
ABC_ATP_DarD NF038007
darobactin export ABC transporter ATP-binding protein;
1-219 6.64e-39

darobactin export ABC transporter ATP-binding protein;


Pssm-ID: 411600 [Multi-domain]  Cd Length: 218  Bit Score: 138.31  E-value: 6.64e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556496326   1 MIKLENLTKHFSQKHGQTfKAVDNVNLNVPEGEMCVLLGPSGCGKTTTLKMINRLITPSSGTILINGEDTSGM---DTVT 77
Cdd:NF038007   1 MLNMQNAEKCYITKTIKT-KVLNHLNFSVEKGDFVSIMGPSGSGKSTLLNIIGMFDSLDSGSLTLAGKEVTNLsysQKII 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556496326  78 LRRN-IGYVIQQIGLFPNMTIEENITVVPRMLGWDKARCKTRAEELMDMVALDPHKflNRYPREMSGGQQQRIGVIRALA 156
Cdd:NF038007  80 LRRElIGYIFQSFNLIPHLSIFDNVALPLKYRGVAKKERIERVNQVLNLFGIDNRR--NHKPMQLSGGQQQRVAIARAMV 157

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 556496326 157 ADPPVLLMDEPFGAVDPIN-REVIQNqfLEMQRKLKKTVMLVSHDiDEALKLGDRIAVFRQGKI 219
Cdd:NF038007 158 SNPALLLADEPTGNLDSKNaRAVLQQ--LKYINQKGTTIIMVTHS-DEASTYGNRIINMKDGKL 218
PhnL COG4778
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ...
 1-211 7.99e-39

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: 138.34  E-value: 7.99e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556496326   1 MIKLENLTKHFS--QKHGQTFKAVDNVNLNVPEGEMCVLLGPSGCGKTTTLKMINRLITPSSGTILINGEDtSGMDTVT- 77
Cdd:COG4778    4 LLEVENLSKTFTlhLQGGKRLPVLDGVSFSVAAGECVALTGPSGAGKSTLLKCIYGNYLPDSGSILVRHDG-GWVDLAQa 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556496326  78 -------LRRN-IGYVIQqiglFpnmtieenITVVPRM------------LGWDKARCKTRAEELMDMVALDPHKFlNRY 137
Cdd:COG4778   83 spreilaLRRRtIGYVSQ----F--------LRVIPRVsaldvvaeplleRGVDREEARARARELLARLNLPERLW-DLP 149

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 556496326 138 PREMSGGQQQRIGVIRALAADPPVLLMDEPFGAVDPINREVIqnqfLEMQRKLKK--TVML-VSHDIDEALKLGDRI 211
Cdd:COG4778  150 PATFSGGEQQRVNIARGFIADPPLLLLDEPTASLDAANRAVV----VELIEEAKArgTAIIgIFHDEEVREAVADRV 222
ABCC_Glucan_exporter_like cd03254
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ...
 2-231 9.49e-39

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: 138.13  E-value: 9.49e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556496326   2 IKLENLtkHFSQKHGQtfKAVDNVNLNVPEGEMCVLLGPSGCGKTTTLKMINRLITPSSGTILINGEDTSGMDTVTLRRN 81
Cdd:cd03254    3 IEFENV--NFSYDEKK--PVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGIDIRDISRKSLRSM 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556496326  82 IGYVIQQIGLFPNmTIEENITvvprmLGWDKArckTRAEELMDMVALDPHKFLNRYPR-----------EMSGGQQQRIG 150
Cdd:cd03254   79 IGVVLQDTFLFSG-TIMENIR-----LGRPNA---TDEEVIEAAKEAGAHDFIMKLPNgydtvlgenggNLSQGERQLLA 149

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556496326 151 VIRALAADPPVLLMDEPFGAVDPINREVIQNQFLEMQRklKKTVMLVSHDIDeALKLGDRIAVFRQGKIVQCASPDELLA 230
Cdd:cd03254  150 IARAMLRDPKILILDEATSNIDTETEKLIQEALEKLMK--GRTSIIIAHRLS-TIKNADKILVLDDGKIIEEGTHDELLA 226


                 .
gi 556496326 231 K 231
Cdd:cd03254  227 K 227
ModF COG1119
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ...
 22-229 1.72e-38

ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA [Inorganic ion transport and metabolism];


Pssm-ID: 440736 [Multi-domain]  Cd Length: 250  Bit Score: 138.29  E-value: 1.72e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556496326  22 VDNVNLNVPEGEMCVLLGPSGCGKTTTLKMINRLITPSSG-TILINGEDTSGMDTVTLRRNIGYV---IQQ--------- 88
Cdd:COG1119   19 LDDISWTVKPGEHWAILGPNGAGKSTLLSLITGDLPPTYGnDVRLFGERRGGEDVWELRKRIGLVspaLQLrfprdetvl 98

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556496326  89 ----------IGLFPNMTIEEnitvvprmlgwdkarcKTRAEELMDMVALDPHKflNRYPREMSGGQQQRIGVIRALAAD 158
Cdd:COG1119   99 dvvlsgffdsIGLYREPTDEQ----------------RERARELLELLGLAHLA--DRPFGTLSQGEQRRVLIARALVKD 160

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 556496326 159 PPVLLMDEPFGAVDPINREviqnQFLEMQRKL----KKTVMLVSHDIDEALKLGDRIAVFRQGKIVQCASPDELL 229
Cdd:COG1119  161 PELLILDEPTAGLDLGARE----LLLALLDKLaaegAPTLVLVTHHVEEIPPGITHVLLLKDGRVVAAGPKEEVL 231
cbiO PRK13634
cobalt transporter ATP-binding subunit; Provisional
 20-233 3.49e-38

cobalt transporter ATP-binding subunit; Provisional


Pssm-ID: 237454 [Multi-domain]  Cd Length: 290  Bit Score: 138.61  E-value: 3.49e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556496326  20 KAVDNVNLNVPEGEMCVLLGPSGCGKTTTLKMINRLITPSSGTILInGED-----TSGMDTVTLRRNIGYVIQqiglFPN 94
Cdd:PRK13634  21 RALYDVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVTI-GERvitagKKNKKLKPLRKKVGIVFQ----FPE 95

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556496326  95 M-----TIEENITVVPRMLGWDKARCKTRAEELMDMVALdPHKFLNRYPREMSGGQQQRIGVIRALAADPPVLLMDEPFG 169
Cdd:PRK13634  96 HqlfeeTVEKDICFGPMNFGVSEEDAKQKAREMIELVGL-PEELLARSPFELSGGQMRRVAIAGVLAMEPEVLVLDEPTA 174

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 556496326 170 AVDPINREVIQNQFLEMQRKLKKTVMLVSHDIDEALKLGDRIAVFRQGKIVQCASPDELLAKPA 233
Cdd:PRK13634 175 GLDPKGRKEMMEMFYKLHKEKGLTTVLVTHSMEDAARYADQIVVMHKGTVFLQGTPREIFADPD 238
ABC_MTABC3_MDL1_MDL2 cd03249
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ...
 20-231 3.83e-38

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: 136.90  E-value: 3.83e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556496326  20 KAVDNVNLNVPEGEMCVLLGPSGCGKTTTLKMINRLITPSSGTILINGEDTSGMDTVTLRRNIGYVIQQIGLFpNMTIEE 99
Cdd:cd03249   17 PILKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEILLDGVDIRDLNLRWLRSQIGLVSQEPVLF-DGTIAE 95

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556496326 100 NItvvprmlgwdkARCKTRAEELMDMVAL---DPHKFLNRYPR-----------EMSGGQQQRIGVIRALAADPPVLLMD 165
Cdd:cd03249   96 NI-----------RYGKPDATDEEVEEAAkkaNIHDFIMSLPDgydtlvgergsQLSGGQKQRIAIARALLRNPKILLLD 164

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 556496326 166 EPFGAVDPINREVIQNQfLEmQRKLKKTVMLVSHDIdEALKLGDRIAVFRQGKIVQCASPDELLAK 231
Cdd:cd03249  165 EATSALDAESEKLVQEA-LD-RAMKGRTTIVIAHRL-STIRNADLIAVLQNGQVVEQGTHDELMAQ 227
YnjD COG4136
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ...
 1-227 4.82e-38

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


Pssm-ID: 443311 [Multi-domain]  Cd Length: 211  Bit Score: 135.69  E-value: 4.82e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556496326   1 MIKLENLTKHfsqKHGQTFkaVDNVNLNVPEGEMCVLLGPSGCGKTTTLKMINRLITP---SSGTILINGEDtsgMDTV- 76
Cdd:COG4136    1 MLSLENLTIT---LGGRPL--LAPLSLTVAPGEILTLMGPSGSGKSTLLAAIAGTLSPafsASGEVLLNGRR---LTALp 72

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556496326  77 TLRRNIGYVIQQIGLFPNMTIEENITV-VPRMLGwdKARCKTRAEELMDMVALDphKFLNRYPREMSGGQQQRIGVIRAL 155
Cdd:COG4136   73 AEQRRIGILFQDDLLFPHLSVGENLAFaLPPTIG--RAQRRARVEQALEEAGLA--GFADRDPATLSGGQRARVALLRAL 148

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 556496326 156 AADPPVLLMDEPFGAVDPINREVIQNQFLEMQRKLKKTVMLVSHDIDEALKlgdriavfrQGKIVQCASPDE 227
Cdd:COG4136  149 LAEPRALLLDEPFSKLDAALRAQFREFVFEQIRQRGIPALLVTHDEEDAPA---------AGRVLDLGNWQH 211
nickel_nikE TIGR02769
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a ...
 1-221 1.46e-37

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: 136.47  E-value: 1.46e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556496326    1 MIKLENLTKHFsqKHGQTFKA------VDNVNLNVPEGEMCVLLGPSGCGKTTTLKMINRLITPSSGTILINGEDTSGMD 74
Cdd:TIGR02769   2 LLEVRDVTHTY--RTGGLFGAkqrapvLTNVSLSIEEGETVGLLGRSGCGKSTLARLLLGLEKPAQGTVSFRGQDLYQLD 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556496326   75 TVT---LRRNIGYVIQQ-IGLF-PNMTIEENITVVPR-MLGWDKARCKTRAEELMDMVALDPhKFLNRYPREMSGGQQQR 148
Cdd:TIGR02769  80 RKQrraFRRDVQLVFQDsPSAVnPRMTVRQIIGEPLRhLTSLDESEQKARIAELLDMVGLRS-EDADKLPRQLSGGQLQR 158

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 556496326  149 IGVIRALAADPPVLLMDEPFGAVDPINREVIQNQFLEMQRKLKKTVMLVSHDIDEALKLGDRIAVFRQGKIVQ 221
Cdd:TIGR02769 159 INIARALAVKPKLIVLDEAVSNLDMVLQAVILELLRKLQQAFGTAYLFITHDLRLVQSFCQRVAVMDKGQIVE 231
ABC_cobalt_CbiO_domain2 cd03226
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ...
 10-220 2.53e-37

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: 133.92  E-value: 2.53e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556496326  10 HFSQKHGQtfKAVDNVNLNVPEGEMCVLLGPSGCGKTTTLKMINRLITPSSGTILINGEDTSGMDtvtLRRNIGYVIQQI 89
Cdd:cd03226    6 SFSYKKGT--EILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLNGKPIKAKE---RRKSIGYVMQDV 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556496326  90 G--LFPNmTIEENITVVPRmlgwDKARCKTRAEELMDMvaLDPHKFLNRYPREMSGGQQQRIGVIRALAADPPVLLMDEP 167
Cdd:cd03226   81 DyqLFTD-SVREELLLGLK----ELDAGNEQAETVLKD--LDLYALKERHPLSLSGGQKQRLAIAAALLSGKDLLIFDEP 153

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 556496326 168 FGAVDPINREVIQNQFLEMQRKlKKTVMLVSHDIDEALKLGDRIAVFRQGKIV 220
Cdd:cd03226  154 TSGLDYKNMERVGELIRELAAQ-GKAVIVITHDYEFLAKVCDRVLLLANGAIV 205
fecE PRK11231
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
1-229 3.12e-37

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


Pssm-ID: 183044 [Multi-domain]  Cd Length: 255  Bit Score: 135.14  E-value: 3.12e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556496326   1 MIKLENLTKHFSQKhgqtfKAVDNVNLNVPEGEMCVLLGPSGCGKTTTLKMINRLITPSSGTILINGEDTSGMDTVTLRR 80
Cdd:PRK11231   2 TLRTENLTVGYGTK-----RILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDKPISMLSSRQLAR 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556496326  81 NIGYVIQQiglfpnMTIEENITV--------VP------RMLGWDKARCkTRAEELMDMVALdphkfLNRYPREMSGGQQ 146
Cdd:PRK11231  77 RLALLPQH------HLTPEGITVrelvaygrSPwlslwgRLSAEDNARV-NQAMEQTRINHL-----ADRRLTDLSGGQR 144

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556496326 147 QRIGVIRALAADPPVLLMDEPFGAVDpINREViqnQFLEMQRKLK---KTVMLVSHDIDEALKLGDRIAVFRQGKIVQCA 223
Cdd:PRK11231 145 QRAFLAMVLAQDTPVVLLDEPTTYLD-INHQV---ELMRLMRELNtqgKTVVTVLHDLNQASRYCDHLVVLANGHVMAQG 220


                 ....*.
gi 556496326 224 SPDELL 229
Cdd:PRK11231 221 TPEEVM 226
type_I_sec_LssB TIGR03375
type I secretion system ATPase, LssB family; Type I protein secretion is a system in some ...
 2-231 3.88e-37

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: 142.31  E-value: 3.88e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556496326    2 IKLENLTKHFSqkhGQTFKAVDNVNLNVPEGEMCVLLGPSGCGKTTTLKMINRLITPSSGTILINGEDTSGMDTVTLRRN 81
Cdd:TIGR03375 464 IEFRNVSFAYP---GQETPALDNVSLTIRPGEKVAIIGRIGSGKSTLLKLLLGLYQPTEGSVLLDGVDIRQIDPADLRRN 540

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556496326   82 IGYVIQQIGLFpNMTIEENITVvpRMLGWDKARCkTRAEE---LMDMVALDPHKF---LNRYPREMSGGQQQRIGVIRAL 155
Cdd:TIGR03375 541 IGYVPQDPRLF-YGTLRDNIAL--GAPYADDEEI-LRAAElagVTEFVRRHPDGLdmqIGERGRSLSGGQRQAVALARAL 616

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 556496326  156 AADPPVLLMDEPFGAVDpINREviqNQFLE-MQRKL-KKTVMLVSHDIdEALKLGDRIAVFRQGKIVQCASPDELLAK 231
Cdd:TIGR03375 617 LRDPPILLLDEPTSAMD-NRSE---ERFKDrLKRWLaGKTLVLVTHRT-SLLDLVDRIIVMDNGRIVADGPKDQVLEA 689
ABCC_MsbA cd03251
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ...
 20-231 5.61e-37

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: 133.90  E-value: 5.61e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556496326  20 KAVDNVNLNVPEGEMCVLLGPSGCGKTTTLKMINRLITPSSGTILINGEDTSGMDTVTLRRNIGYVIQQIGLFpNMTIEE 99
Cdd:cd03251   16 PVLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDGHDVRDYTLASLRRQIGLVSQDVFLF-NDTVAE 94

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556496326 100 NItvvprMLGWDKArckTRAEELMDMVALDPHKFLNRYPR-----------EMSGGQQQRIGVIRALAADPPVLLMDEPF 168
Cdd:cd03251   95 NI-----AYGRPGA---TREEVEEAARAANAHEFIMELPEgydtvigergvKLSGGQRQRIAIARALLKDPPILILDEAT 166

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 556496326 169 GAVDPINREVIQNQFLEMQRklKKTVMLVSH---DIDEAlklgDRIAVFRQGKIVQCASPDELLAK 231
Cdd:cd03251  167 SALDTESERLVQAALERLMK--NRTTFVIAHrlsTIENA----DRIVVLEDGKIVERGTHEELLAQ 226
YejF COG4172
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ...
 1-233 5.65e-37

ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites biosynthesis, transport and catabolism];


Pssm-ID: 443332 [Multi-domain]  Cd Length: 533  Bit Score: 140.20  E-value: 5.65e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556496326   1 MIKLENLTKHFSQkHGQTFKAVDNVNLNVPEGEMCVLLGPSGCGKTTTLKMINRLITPS----SGTILINGEDTSGMDTV 76
Cdd:COG4172    6 LLSVEDLSVAFGQ-GGGTVEAVKGVSFDIAAGETLALVGESGSGKSVTALSILRLLPDPaahpSGSILFDGQDLLGLSER 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556496326  77 TLRR----NIGYVIQQ--IGLFPNMTIEENITVVPRM-LGWDKARCKTRAEELMDMVAL-DPHKFLNRYPREMSGGQQQR 148
Cdd:COG4172   85 ELRRirgnRIAMIFQEpmTSLNPLHTIGKQIAEVLRLhRGLSGAAARARALELLERVGIpDPERRLDAYPHQLSGGQRQR 164

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556496326 149 IGVIRALAADPPVLLMDEPFGAVDpinreV-IQNQFL----EMQRKLKKTVMLVSHDIDEALKLGDRIAVFRQGKIVQCA 223
Cdd:COG4172  165 VMIAMALANEPDLLIADEPTTALD-----VtVQAQILdllkDLQRELGMALLLITHDLGVVRRFADRVAVMRQGEIVEQG 239

                        250
                 ....*....|
gi 556496326 224 SPDELLAKPA 233
Cdd:COG4172  240 PTAELFAAPQ 249
ABC_NatA_like cd03267
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ...
 4-220 1.88e-36

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: 132.46  E-value: 1.88e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556496326   4 LENLTKHFSQKHGQTFKAVDNVNLNVPEGEMCVLLGPSGCGKTTTLKMINRLITPSSGTILINGEDtSGMDTVTLRRNIG 83
Cdd:cd03267   19 LIGSLKSLFKRKYREVEALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRVAGLV-PWKRRKKFLRRIG 97

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556496326  84 YVI-QQIGLFPNMTIEENITVVPRMLGWDKARCKTRAEELMDMvaLDPHKFLNRYPREMSGGQQQRIGVIRALAADPPVL 162
Cdd:cd03267   98 VVFgQKTQLWWDLPVIDSFYLLAAIYDLPPARFKKRLDELSEL--LDLEELLDTPVRQLSLGQRMRAEIAAALLHEPEIL 175

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 556496326 163 LMDEPFGAVDPINREVIQNQFLEMQRKLKKTVMLVSHDIDEALKLGDRIAVFRQGKIV 220
Cdd:cd03267  176 FLDEPTIGLDVVAQENIRNFLKEYNRERGTTVLLTSHYMKDIEALARRVLVIDKGRLL 233
thiQ TIGR01277
thiamine ABC transporter, ATP-binding protein; This model describes the energy-transducing ...
 26-221 2.41e-36

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: 131.52  E-value: 2.41e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556496326   26 NLNVPEGEMCVLLGPSGCGKTTTLKMINRLITPSSGTILINGEDTSGmdTVTLRRNIGYVIQQIGLFPNMTIEENITvvp 105
Cdd:TIGR01277  18 DLNVADGEIVAIMGPSGAGKSTLLNLIAGFIEPASGSIKVNDQSHTG--LAPYQRPVSMLFQENNLFAHLTVRQNIG--- 92

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556496326  106 rmLGWdKARCKTRAEELMDMVALDPH----KFLNRYPREMSGGQQQRIGVIRALAADPPVLLMDEPFGAVDPINREVIQN 181
Cdd:TIGR01277  93 --LGL-HPGLKLNAEQQEKVVDAAQQvgiaDYLDRLPEQLSGGQRQRVALARCLVRPNPILLLDEPFSALDPLLREEMLA 169

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 556496326  182 QFLEMQRKLKKTVMLVSHDIDEALKLGDRIAVFRQGKIVQ 221
Cdd:TIGR01277 170 LVKQLCSERQRTLLMVTHHLSDARAIASQIAVVSQGKIKV 209
PRK10619 PRK10619
histidine ABC transporter ATP-binding protein HisP;
25-241 2.78e-36

histidine ABC transporter ATP-binding protein HisP;


Pssm-ID: 182592 [Multi-domain]  Cd Length: 257  Bit Score: 132.79  E-value: 2.78e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556496326  25 VNLNVPEGEMCVLLGPSGCGKTTTLKMINRLITPSSGTILINGE------DTSGMDTVT-------LRRNIGYVIQQIGL 91
Cdd:PRK10619  24 VSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNGQtinlvrDKDGQLKVAdknqlrlLRTRLTMVFQHFNL 103

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556496326  92 FPNMTIEENITVVP-RMLGWDKARCKTRAEELMDMVALDpHKFLNRYPREMSGGQQQRIGVIRALAADPPVLLMDEPFGA 170
Cdd:PRK10619 104 WSHMTVLENVMEAPiQVLGLSKQEARERAVKYLAKVGID-ERAQGKYPVHLSGGQQQRVSIARALAMEPEVLLFDEPTSA 182

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 556496326 171 VDPinrEVIqNQFLEMQRKLK---KTVMLVSHDIDEALKLGDRIAVFRQGKIVQCASPDELLAKPANEFVGSFV 241
Cdd:PRK10619 183 LDP---ELV-GEVLRIMQQLAeegKTMVVVTHEMGFARHVSSHVIFLHQGKIEEEGAPEQLFGNPQSPRLQQFL 252
PRK14267 PRK14267
phosphate ABC transporter ATP-binding protein; Provisional
 2-241 2.89e-36

phosphate ABC transporter ATP-binding protein; Provisional


Pssm-ID: 184596 [Multi-domain]  Cd Length: 253  Bit Score: 132.66  E-value: 2.89e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556496326   2 IKLENLTKHFSQKHgqtfkAVDNVNLNVPEGEMCVLLGPSGCGKTTTLKMINRLITPS-----SGTILINGED--TSGMD 74
Cdd:PRK14267   5 IETVNLRVYYGSNH-----VIKGVDLKIPQNGVFALMGPSGCGKSTLLRTFNRLLELNeearvEGEVRLFGRNiySPDVD 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556496326  75 TVTLRRNIGYVIQQIGLFPNMTIEENITVVPRMLGWDKARCK--TRAEELMDMVAL--DPHKFLNRYPREMSGGQQQRIG 150
Cdd:PRK14267  80 PIEVRREVGMVFQYPNPFPHLTIYDNVAIGVKLNGLVKSKKEldERVEWALKKAALwdEVKDRLNDYPSNLSGGQRQRLV 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556496326 151 VIRALAADPPVLLMDEPFGAVDPINREVIQNQFLEMQRKLkkTVMLVSHDIDEALKLGDRIAVFRQGKIVQCASPDELLA 230
Cdd:PRK14267 160 IARALAMKPKILLMDEPTANIDPVGTAKIEELLFELKKEY--TIVLVTHSPAQAARVSDYVAFLYLGKLIEVGPTRKVFE 237

                        250
                 ....*....|.
gi 556496326 231 KPANEFVGSFV 241
Cdd:PRK14267 238 NPEHELTEKYV 248
NupO COG3845
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ...
 1-227 4.76e-36

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


Pssm-ID: 443055 [Multi-domain]  Cd Length: 504  Bit Score: 137.47  E-value: 4.76e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556496326   1 MIKLENLTKHFSqkhgqTFKAVDNVNLNVPEGEMCVLLGPSGCGKTTTLKMINRLITPSSGTILINGEdtsgmdTVT--- 77
Cdd:COG3845    5 ALELRGITKRFG-----GVVANDDVSLTVRPGEIHALLGENGAGKSTLMKILYGLYQPDSGEILIDGK------PVRirs 73

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556496326  78 ----LRRNIGYVIQQIGLFPNMTIEENItvvprMLGW--------DKARCKTRAEELMDM--VALDPHkflnRYPREMSG 143
Cdd:COG3845   74 prdaIALGIGMVHQHFMLVPNLTVAENI-----VLGLeptkggrlDRKAARARIRELSERygLDVDPD----AKVEDLSV 144

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556496326 144 GQQQRIGVIRALAADPPVLLMDEPFGAVDPinREViqNQFLEMQRKLK---KTVMLVSHDIDEALKLGDRIAVFRQGKIV 220
Cdd:COG3845  145 GEQQRVEILKALYRGARILILDEPTAVLTP--QEA--DELFEILRRLAaegKSIIFITHKLREVMAIADRVTVLRRGKVV 220


                 ....*..
gi 556496326 221 QCASPDE 227
Cdd:COG3845  221 GTVDTAE 227
ABCC_Hemolysin cd03252
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ...
 21-231 4.78e-36

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: 131.45  E-value: 4.78e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556496326  21 AVDNVNLNVPEGEMCVLLGPSGCGKTTTLKMINRLITPSSGTILINGEDTSGMDTVTLRRNIGYVIQQIGLFpNMTIEEN 100
Cdd:cd03252   17 ILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGHDLALADPAWLRRQVGVVLQENVLF-NRSIRDN 95

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556496326 101 ITVVprmlgwDKARCKTRAEELMDMValDPHKFLNRYPR-----------EMSGGQQQRIGVIRALAADPPVLLMDEPFG 169
Cdd:cd03252   96 IALA------DPGMSMERVIEAAKLA--GAHDFISELPEgydtivgeqgaGLSGGQRQRIAIARALIHNPRILIFDEATS 167

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 556496326 170 AVDPINREVIQNQfleMQRKLK-KTVMLVSHDIdEALKLGDRIAVFRQGKIVQCASPDELLAK 231
Cdd:cd03252  168 ALDYESEHAIMRN---MHDICAgRTVIIIAHRL-STVKNADRIIVMEKGRIVEQGSHDELLAE 226
cbiO PRK13632
cobalt transporter ATP-binding subunit; Provisional
 1-229 5.00e-36

cobalt transporter ATP-binding subunit; Provisional


Pssm-ID: 237452 [Multi-domain]  Cd Length: 271  Bit Score: 132.42  E-value: 5.00e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556496326   1 MIKLENLTkhFSQKHGQTFkAVDNVNLNVPEGEMCVLLGPSGCGKTTTLKMINRLITPSSGTILINGEDTSGMDTVTLRR 80
Cdd:PRK13632   7 MIKVENVS--FSYPNSENN-ALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIDGITISKENLKEIRK 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556496326  81 NIGYVIQQ-----IGLfpnmTIE-------ENITVVPRMLgwdkarcKTRAEELMDMVALDphKFLNRYPREMSGGQQQR 148
Cdd:PRK13632  84 KIGIIFQNpdnqfIGA----TVEddiafglENKKVPPKKM-------KDIIDDLAKKVGME--DYLDKEPQNLSGGQKQR 150

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556496326 149 IGVIRALAADPPVLLMDEPFGAVDPINREVIQNQFLEMQRKLKKTVMLVSHDIDEALkLGDRIAVFRQGKIVQCASPDEL 228
Cdd:PRK13632 151 VAIASVLALNPEIIIFDESTSMLDPKGKREIKKIMVDLRKTRKKTLISITHDMDEAI-LADKVIVFSEGKLIAQGKPKEI 229


                 .
gi 556496326 229 L 229
Cdd:PRK13632 230 L 230
COG4586 COG4586
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ...
 1-293 5.23e-36

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


Pssm-ID: 443643 [Multi-domain]  Cd Length: 323  Bit Score: 133.67  E-value: 5.23e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556496326   1 MIKLENLTKHFSQKHGQ----------------TFKAVDNVNLNVPEGEMCVLLGPSGCGKTTTLKMINRLITPSSGTIL 64
Cdd:COG4586    1 IIEVENLSKTYRVYEKEpglkgalkglfrreyrEVEAVDDISFTIEPGEIVGFIGPNGAGKSTTIKMLTGILVPTSGEVR 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556496326  65 INGEDTSgMDTVTLRRNIGYVI---QQigLFPNMTIEENITVVPRMLGWDKARCKTRAEELMDMvaLDPHKFLNRYPREM 141
Cdd:COG4586   81 VLGYVPF-KRRKEFARRIGVVFgqrSQ--LWWDLPAIDSFRLLKAIYRIPDAEYKKRLDELVEL--LDLGELLDTPVRQL 155

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556496326 142 SGGQQQRIGVIRALAADPPVLLMDEPFGAVDPINREVIQnQFL-EMQRKLKKTVMLVSHDIDEALKLGDRIAVFRQGKIV 220
Cdd:COG4586  156 SLGQRMRCELAAALLHRPKILFLDEPTIGLDVVSKEAIR-EFLkEYNRERGTTILLTSHDMDDIEALCDRVIVIDHGRII 234

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556496326 221 QCASPDELLAKpanefvgsfVGQDRTLK--------RLLLVSAGDVTDQQP---TITVRGSTPLPEAFAT-MDDNDIRAI 288
Cdd:COG4586  235 YDGSLEELKER---------FGPYKTIVlelaepvpPLELPRGGEVIEREGnrvRLEVDPRESLAEVLARlLARYPVRDL 305


                 ....*
gi 556496326 289 TVVDE 293
Cdd:COG4586  306 TIEEP 310
PRK13633 PRK13633
energy-coupling factor transporter ATPase;
1-231 3.89e-35

energy-coupling factor transporter ATPase;


Pssm-ID: 237453 [Multi-domain]  Cd Length: 280  Bit Score: 130.21  E-value: 3.89e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556496326   1 MIKLENLTKHFSQKHGQTFK-AVDNVNLNVPEGEMCVLLGPSGCGKTTTLKMINRLITPSSGTILINGEDTSGMDTV-TL 78
Cdd:PRK13633   4 MIKCKNVSYKYESNEESTEKlALDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVYVDGLDTSDEENLwDI 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556496326  79 RRNIGYVIQQiglfPNMTI-----EENITVVPRMLGWDKARCKTRAEELMDMVALDPHKflnRY-PREMSGGQQQRIGVI 152
Cdd:PRK13633  84 RNKAGMVFQN----PDNQIvativEEDVAFGPENLGIPPEEIRERVDESLKKVGMYEYR---RHaPHLLSGGQKQRVAIA 156

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 556496326 153 RALAADPPVLLMDEPFGAVDPINREVIQNQFLEMQRKLKKTVMLVSHDIDEALKlGDRIAVFRQGKIVQCASPDELLAK 231
Cdd:PRK13633 157 GILAMRPECIIFDEPTAMLDPSGRREVVNTIKELNKKYGITIILITHYMEEAVE-ADRIIVMDSGKVVMEGTPKEIFKE 234
ABCC_ATM1_transporter cd03253
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ...
 2-231 3.96e-35

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: 128.89  E-value: 3.96e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556496326   2 IKLENLtkHFSqkHGQTFKAVDNVNLNVPEGEMCVLLGPSGCGKTTTLKMINRLITPSSGTILINGEDTSGMDTVTLRRN 81
Cdd:cd03253    1 IEFENV--TFA--YDPGRPVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDGQDIREVTLDSLRRA 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556496326  82 IGYVIQQIGLFpNMTIEENITVvprmlgwdkARCKTRAEELMDMV-ALDPHKFLNRYPR-----------EMSGGQQQRI 149
Cdd:cd03253   77 IGVVPQDTVLF-NDTIGYNIRY---------GRPDATDEEVIEAAkAAQIHDKIMRFPDgydtivgerglKLSGGEKQRV 146

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556496326 150 GVIRALAADPPVLLMDEPFGAVDPINREVIQNQFLEMQRklKKTVMLVSHDIDEALKlGDRIAVFRQGKIVQCASPDELL 229
Cdd:cd03253  147 AIARAILKNPPILLLDEATSALDTHTEREIQAALRDVSK--GRTTIVIAHRLSTIVN-ADKIIVLKDGRIVERGTHEELL 223


                 ..
gi 556496326 230 AK 231
Cdd:cd03253  224 AK 225
COG4559 COG4559
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism];
1-229 4.50e-35

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


Pssm-ID: 443620 [Multi-domain]  Cd Length: 258  Bit Score: 129.47  E-value: 4.50e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556496326   1 MIKLENLTKHFSQKhgqtfKAVDNVNLNVPEGEMCVLLGPSGCGKTTTLKMINRLITPSSGTILINGEDTSGMDTVTLRR 80
Cdd:COG4559    1 MLEAENLSVRLGGR-----TLLDDVSLTLRPGELTAIIGPNGAGKSTLLKLLTGELTPSSGEVRLNGRPLAAWSPWELAR 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556496326  81 NIGYVIQQIGL-FPnMTIEEnitVVprMLG-----WDKARCKTRAEELMDMVALDPhkFLNRYPREMSGGQQQRIGVIRA 154
Cdd:COG4559   76 RRAVLPQHSSLaFP-FTVEE---VV--ALGraphgSSAAQDRQIVREALALVGLAH--LAGRSYQTLSGGEQQRVQLARV 147

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556496326 155 LA-------ADPPVLLMDEPFGAVDPINreviQNQFLEMQRKLKK---TVMLVSHDIDEALKLGDRIAVFRQGKIVQCAS 224
Cdd:COG4559  148 LAqlwepvdGGPRWLFLDEPTSALDLAH----QHAVLRLARQLARrggGVVAVLHDLNLAAQYADRILLLHQGRLVAQGT 223


                 ....*
gi 556496326 225 PDELL 229
Cdd:COG4559  224 PEEVL 228
PRK14243 PRK14243
phosphate transporter ATP-binding protein; Provisional
 2-241 4.84e-35

phosphate transporter ATP-binding protein; Provisional


Pssm-ID: 184588 [Multi-domain]  Cd Length: 264  Bit Score: 129.52  E-value: 4.84e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556496326   2 IKLENLTKHFSqkhgqTFKAVDNVNLNVPEGEMCVLLGPSGCGKTTTLKMINRL--ITPS---SGTILINGED--TSGMD 74
Cdd:PRK14243  11 LRTENLNVYYG-----SFLAVKNVWLDIPKNQITAFIGPSGCGKSTILRCFNRLndLIPGfrvEGKVTFHGKNlyAPDVD 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556496326  75 TVTLRRNIGYVIQQIGLFPNmTIEENITVVPRMLGWdKARCKTRAEELMDMVAL-DPHK-FLNRYPREMSGGQQQRIGVI 152
Cdd:PRK14243  86 PVEVRRRIGMVFQKPNPFPK-SIYDNIAYGARINGY-KGDMDELVERSLRQAALwDEVKdKLKQSGLSLSGGQQQRLCIA 163

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556496326 153 RALAADPPVLLMDEPFGAVDPINREVIQnqflEMQRKLKK--TVMLVSHDIDEALKLGDRIAVF---------RQGKIVQ 221
Cdd:PRK14243 164 RAIAVQPEVILMDEPCSALDPISTLRIE----ELMHELKEqyTIIIVTHNMQQAARVSDMTAFFnveltegggRYGYLVE 239

                        250       260
                 ....*....|....*....|
gi 556496326 222 CASPDELLAKPANEFVGSFV 241
Cdd:PRK14243 240 FDRTEKIFNSPQQQATRDYV 259
ABCC_Protease_Secretion cd03246
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ...
 2-219 6.21e-35

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: 126.56  E-value: 6.21e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556496326   2 IKLENLtkhfSQKHGQTFKAV-DNVNLNVPEGEMCVLLGPSGCGKTTTLKMINRLITPSSGTILINGEDTSGMDTVTLRR 80
Cdd:cd03246    1 LEVENV----SFRYPGAEPPVlRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDGADISQWDPNELGD 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556496326  81 NIGYVIQQIGLFPNmTIEENItvvprmlgwdkarcktraeelmdmvaldphkflnrypreMSGGQQQRIGVIRALAADPP 160
Cdd:cd03246   77 HVGYLPQDDELFSG-SIAENI---------------------------------------LSGGQRQRLGLARALYGNPR 116

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 556496326 161 VLLMDEPFGAVDPINrEVIQNQFLEMQRKLKKTVMLVSHDIdEALKLGDRIAVFRQGKI 219
Cdd:cd03246  117 ILVLDEPNSHLDVEG-ERALNQAIAALKAAGATRIVIAHRP-ETLASADRILVLEDGRV 173
cbiO PRK13641
energy-coupling factor transporter ATPase;
2-232 8.68e-35

energy-coupling factor transporter ATPase;


Pssm-ID: 237456 [Multi-domain]  Cd Length: 287  Bit Score: 129.56  E-value: 8.68e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556496326   2 IKLENLTKHFSQKHGQTFKAVDNVNLNVPEGEMCVLLGPSGCGKTTTLKMINRLITPSSGTILINGE----DTSGMDTVT 77
Cdd:PRK13641   3 IKFENVDYIYSPGTPMEKKGLDNISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITIAGYhitpETGNKNLKK 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556496326  78 LRRNIGYVIQ--QIGLFPNmTIEENITVVPRMLGWDKARCKTRAEELMDMVALdPHKFLNRYPREMSGGQQQRIGVIRAL 155
Cdd:PRK13641  83 LRKKVSLVFQfpEAQLFEN-TVLKDVEFGPKNFGFSEDEAKEKALKWLKKVGL-SEDLISKSPFELSGGQMRRVAIAGVM 160

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 556496326 156 AADPPVLLMDEPFGAVDPINREVIQNQFLEMQRKlKKTVMLVSHDIDEALKLGDRIAVFRQGKIVQCASPDELLAKP 232
Cdd:PRK13641 161 AYEPEILCLDEPAAGLDPEGRKEMMQLFKDYQKA-GHTVILVTHNMDDVAEYADDVLVLEHGKLIKHASPKEIFSDK 236
PRK10895 PRK10895
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
 5-230 9.69e-35

lipopolysaccharide ABC transporter ATP-binding protein; Provisional


Pssm-ID: 182817 [Multi-domain]  Cd Length: 241  Bit Score: 128.09  E-value: 9.69e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556496326   5 ENLTKHFSQKhgqtfKAVDNVNLNVPEGEMCVLLGPSGCGKTTTLKMINRLITPSSGTILINGEDTSGMDT-VTLRRNIG 83
Cdd:PRK10895   7 KNLAKAYKGR-----RVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEDISLLPLhARARRGIG 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556496326  84 YVIQQIGLFPNMTIEENITVVPRML-GWDKARCKTRAEELMDMVALDphKFLNRYPREMSGGQQQRIGVIRALAADPPVL 162
Cdd:PRK10895  82 YLPQEASIFRRLSVYDNLMAVLQIRdDLSAEQREDRANELMEEFHIE--HLRDSMGQSLSGGERRRVEIARALAANPKFI 159

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 556496326 163 LMDEPFGAVDPINREVIQnQFLEMQRKLKKTVMLVSHDIDEALKLGDRIAVFRQGKIVQCASPDELLA 230
Cdd:PRK10895 160 LLDEPFAGVDPISVIDIK-RIIEHLRDSGLGVLITDHNVRETLAVCERAYIVSQGHLIAHGTPTEILQ 226
urea_trans_UrtE TIGR03410
urea ABC transporter, ATP-binding protein UrtE; Members of this protein family are ABC ...
 3-228 1.05e-34

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: 127.64  E-value: 1.05e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556496326    3 KLENLTKHFSQKHgqtfkAVDNVNLNVPEGEMCVLLGPSGCGKTTTLKMINRLITPSSGTILINGEDTSGMDTVTL-RRN 81
Cdd:TIGR03410   2 EVSNLNVYYGQSH-----ILRGVSLEVPKGEVTCVLGRNGVGKTTLLKTLMGLLPVKSGSIRLDGEDITKLPPHERaRAG 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556496326   82 IGYVIQQIGLFPNMTIEENItvvprMLGWD--KARCKTRAEELMDMV-ALdpHKFLNRYPREMSGGQQQRIGVIRALAAD 158
Cdd:TIGR03410  77 IAYVPQGREIFPRLTVEENL-----LTGLAalPRRSRKIPDEIYELFpVL--KEMLGRRGGDLSGGQQQQLAIARALVTR 149

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 556496326  159 PPVLLMDEPFGAVDPinrEVIQnqflEMQRKLKK-------TVMLVSHDIDEALKLGDRIAVFRQGKIVQCASPDEL 228
Cdd:TIGR03410 150 PKLLLLDEPTEGIQP---SIIK----DIGRVIRRlraeggmAILLVEQYLDFARELADRYYVMERGRVVASGAGDEL 219
ABC_Carb_Monos_I cd03216
First domain of the ATP-binding cassette component of monosaccharide transport system; This ...
 2-220 1.13e-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: 125.23  E-value: 1.13e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556496326   2 IKLENLTKHFSQkhgqtFKAVDNVNLNVPEGEMCVLLGPSGCGKTTTLKMINRLITPSSGTILINGEDTSGMDTV-TLRR 80
Cdd:cd03216    1 LELRGITKRFGG-----VKALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVDGKEVSFASPRdARRA 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556496326  81 NIGYVIQqiglfpnmtieenitvvprmlgwdkarcktraeelmdmvaldphkflnrypreMSGGQQQRIGVIRALAADPP 160
Cdd:cd03216   76 GIAMVYQ-----------------------------------------------------LSVGERQMVEIARALARNAR 102

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 556496326 161 VLLMDEPFGAVDPinREViqNQFLEMQRKLKK---TVMLVSHDIDEALKLGDRIAVFRQGKIV 220
Cdd:cd03216  103 LLILDEPTAALTP--AEV--ERLFKVIRRLRAqgvAVIFISHRLDEVFEIADRVTVLRDGRVV 161
type_I_sec_HlyB TIGR01846
type I secretion system ABC transporter, HlyB family; Type I protein secretion is a system in ...
 2-234 1.42e-34

type I secretion system ABC transporter, HlyB 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: 273831 [Multi-domain]  Cd Length: 694  Bit Score: 134.87  E-value: 1.42e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556496326    2 IKLENLTKHFSQkhgQTFKAVDNVNLNVPEGEMCVLLGPSGCGKTTTLKMINRLITPSSGTILINGEDTSGMDTVTLRRN 81
Cdd:TIGR01846 456 ITFENIRFRYAP---DSPEVLSNLNLDIKPGEFIGIVGPSGSGKSTLTKLLQRLYTPQHGQVLVDGVDLAIADPAWLRRQ 532

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556496326   82 IGYVIQQIGLFpNMTIEENItvvprmlgwdkARCKTRA--EELMDMVAL-DPHKFLNRYPR-----------EMSGGQQQ 147
Cdd:TIGR01846 533 MGVVLQENVLF-SRSIRDNI-----------ALCNPGApfEHVIHAAKLaGAHDFISELPQgyntevgekgaNLSGGQRQ 600

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556496326  148 RIGVIRALAADPPVLLMDEPFGAVDPINREVIQNQFLEMQRklKKTVMLVSHDIDeALKLGDRIAVFRQGKIVQCASPDE 227
Cdd:TIGR01846 601 RIAIARALVGNPRILIFDEATSALDYESEALIMRNMREICR--GRTVIIIAHRLS-TVRACDRIIVLEKGQIAESGRHEE 677


                  ....*..
gi 556496326  228 LLAKPAN 234
Cdd:TIGR01846 678 LLALQGL 684
PRK13537 PRK13537
nodulation factor ABC transporter ATP-binding protein NodI;
2-230 4.17e-34

nodulation factor ABC transporter ATP-binding protein NodI;


Pssm-ID: 237420 [Multi-domain]  Cd Length: 306  Bit Score: 128.38  E-value: 4.17e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556496326   2 IKLENLTKHFSQKhgqtfKAVDNVNLNVPEGEMCVLLGPSGCGKTTTLKMINRLITPSSGTILINGEDTSGMDTVTlRRN 81
Cdd:PRK13537   8 IDFRNVEKRYGDK-----LVVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCGEPVPSRARHA-RQR 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556496326  82 IGYVIQQIGLFPNMTIEENITVVPRMLGWDKARCKTRAEELMDMVALDPHKflNRYPREMSGGQQQRIGVIRALAADPPV 161
Cdd:PRK13537  82 VGVVPQFDNLDPDFTVRENLLVFGRYFGLSAAAARALVPPLLEFAKLENKA--DAKVGELSGGMKRRLTLARALVNDPDV 159

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 556496326 162 LLMDEPFGAVDPINREVIqnqfLEMQRKL---KKTVMLVSHDIDEALKLGDRIAVFRQGKIVQCASPDELLA 230
Cdd:PRK13537 160 LVLDEPTTGLDPQARHLM----WERLRSLlarGKTILLTTHFMEEAERLCDRLCVIEEGRKIAEGAPHALIE 227
btuD PRK09536
corrinoid ABC transporter ATPase; Reviewed
 1-335 4.80e-34

corrinoid ABC transporter ATPase; Reviewed


Pssm-ID: 236554 [Multi-domain]  Cd Length: 402  Bit Score: 130.35  E-value: 4.80e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556496326   1 MIKLENLTKHFsqkhGQTfKAVDNVNLNVPEGEMCVLLGPSGCGKTTTLKMINRLITPSSGTILINGEDTSGMDTVTLRR 80
Cdd:PRK09536   3 MIDVSDLSVEF----GDT-TVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGDDVEALSARAASR 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556496326  81 NIGYVIQQIGLFPNMTIEENITV-----VPRMLGWDKArcKTRA-EELMDMVALDphKFLNRYPREMSGGQQQRIGVIRA 154
Cdd:PRK09536  78 RVASVPQDTSLSFEFDVRQVVEMgrtphRSRFDTWTET--DRAAvERAMERTGVA--QFADRPVTSLSGGERQRVLLARA 153

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556496326 155 LAADPPVLLMDEPFGAVDpINREViqnQFLEMQRKL---KKTVMLVSHDIDEALKLGDRIAVFRQGKIVQCASPDELLAK 231
Cdd:PRK09536 154 LAQATPVLLLDEPTASLD-INHQV---RTLELVRRLvddGKTAVAAIHDLDLAARYCDELVLLADGRVRAAGPPADVLTA 229

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556496326 232 P-------ANEFVGS-----------FVGQDRT----LKRLLLVSAGdvtdqQPTITV------RGST----PLPE---A 276
Cdd:PRK09536 230 DtlraafdARTAVGTdpatgaptvtpLPDPDRTeaaaDTRVHVVGGG-----QPAARAvsrlvaAGASvsvgPVPEgdtA 304

                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 556496326 277 FATMDDNDIRAITVvdEHGKPLGFVKRREARNASGTCADILHPFRmTGKAEDNLRVVLS 335
Cdd:PRK09536 305 AETAARVGCEAVTV--PPFKPIEDSTRAEATDLIIAADAVVAAGV-AAAARSGVIGLLA 360
cbiO PRK13646
energy-coupling factor transporter ATPase;
2-231 4.90e-34

energy-coupling factor transporter ATPase;


Pssm-ID: 184205 [Multi-domain]  Cd Length: 286  Bit Score: 127.59  E-value: 4.90e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556496326   2 IKLENLTKHFSQKHGQTFKAVDNVNLNVPEGEMCVLLGPSGCGKTTTLKMINRLITPSSGTILING----EDTSGMDTVT 77
Cdd:PRK13646   3 IRFDNVSYTYQKGTPYEHQAIHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVDDititHKTKDKYIRP 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556496326  78 LRRNIGYVIQ--QIGLFPNmTIEENITVVPRMLGWDKARCKTRAEELMDMVALdPHKFLNRYPREMSGGQQQRIGVIRAL 155
Cdd:PRK13646  83 VRKRIGMVFQfpESQLFED-TVEREIIFGPKNFKMNLDEVKNYAHRLLMDLGF-SRDVMSQSPFQMSGGQMRKIAIVSIL 160

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 556496326 156 AADPPVLLMDEPFGAVDPINREVIQNQFLEMQRKLKKTVMLVSHDIDEALKLGDRIAVFRQGKIVQCASPDELLAK 231
Cdd:PRK13646 161 AMNPDIIVLDEPTAGLDPQSKRQVMRLLKSLQTDENKTIILVSHDMNEVARYADEVIVMKEGSIVSQTSPKELFKD 236
CydD TIGR02857
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ...
 20-213 9.92e-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: 131.25  E-value: 9.92e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556496326   20 KAVDNVNLNVPEGEMCVLLGPSGCGKTTTLKMINRLITPSSGTILINGEDTSGMDTVTLRRNIGYVIQQIGLFPNmTIEE 99
Cdd:TIGR02857 336 PALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSIAVNGVPLADADADSWRDQIAWVPQHPFLFAG-TIAE 414

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556496326  100 NITVVPRMLGWDKARCKTRAEELMDMVALDP---HKFLNRYPREMSGGQQQRIGVIRALAADPPVLLMDEPFGAVDPINr 176
Cdd:TIGR02857 415 NIRLARPDASDAEIREALERAGLDEFVAALPqglDTPIGEGGAGLSGGQAQRLALARAFLRDAPLLLLDEPTAHLDAET- 493

                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 556496326  177 eviQNQFLEMQRKLK--KTVMLVSHDiDEALKLGDRIAV 213
Cdd:TIGR02857 494 ---EAEVLEALRALAqgRTVLLVTHR-LALAALADRIVV 528
ABC_KpsT_Wzt cd03220
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ...
 2-222 1.21e-33

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: 124.57  E-value: 1.21e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556496326   2 IKLENLTKHFSQKHGQ-----------------TFKAVDNVNLNVPEGEMCVLLGPSGCGKTTTLKMINRLITPSSGTIL 64
Cdd:cd03220    1 IELENVSKSYPTYKGGssslkklgilgrkgevgEFWALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVT 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556496326  65 INGEDTSGMDtvtlrrnIGYviqqiGLFPNMTIEENITVVPRMLGWDKARCKTRAEELMDMVALDphKFLNRYPREMSGG 144
Cdd:cd03220   81 VRGRVSSLLG-------LGG-----GFNPELTGRENIYLNGRLLGLSRKEIDEKIDEIIEFSELG--DFIDLPVKTYSSG 146

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 556496326 145 QQQRIGVIRALAADPPVLLMDEPFGAVDPINREVIQNQFLEMQRKlKKTVMLVSHDIDEALKLGDRIAVFRQGKIVQC 222
Cdd:cd03220  147 MKARLAFAIATALEPDILLIDEVLAVGDAAFQEKCQRRLRELLKQ-GKTVILVSHDPSSIKRLCDRALVLEKGKIRFD 223
MsbA_rel TIGR02204
ABC transporter, permease/ATP-binding protein; This protein is related to a Proteobacterial ...
 2-231 3.63e-33

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: 130.21  E-value: 3.63e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556496326    2 IKLENLTKHFSQKHGQtfKAVDNVNLNVPEGEMCVLLGPSGCGKTTTLKMINRLITPSSGTILINGEDTSGMDTVTLRRN 81
Cdd:TIGR02204 338 IEFEQVNFAYPARPDQ--PALDGLNLTVRPGETVALVGPSGAGKSTLFQLLLRFYDPQSGRILLDGVDLRQLDPAELRAR 415

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556496326   82 IGYVIQQIGLFPNmTIEENITvvprmLGWDKArckTRAEELMDMVALDPHKFLNRYPR-----------EMSGGQQQRIG 150
Cdd:TIGR02204 416 MALVPQDPVLFAA-SVMENIR-----YGRPDA---TDEEVEAAARAAHAHEFISALPEgydtylgergvTLSGGQRQRIA 486

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556496326  151 VIRALAADPPVLLMDEPFGAVDPINREVIQnQFLE--MQrklKKTVMLVSHDIDEALKlGDRIAVFRQGKIVQCASPDEL 228
Cdd:TIGR02204 487 IARAILKDAPILLLDEATSALDAESEQLVQ-QALEtlMK---GRTTLIIAHRLATVLK-ADRIVVMDQGRIVAQGTHAEL 561


                  ...
gi 556496326  229 LAK 231
Cdd:TIGR02204 562 IAK 564
CeuD COG4604
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ...
 1-229 5.26e-33

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


Pssm-ID: 443654 [Multi-domain]  Cd Length: 252  Bit Score: 123.65  E-value: 5.26e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556496326   1 MIKLENLTKHFSQKhgqtfKAVDNVNLNVPEGEMCVLLGPSGCGKTTTLKMINRLITPSSGTILINGEDTSGMDTVTLRR 80
Cdd:COG4604    1 MIEIKNVSKRYGGK-----VVLDDVSLTIPKGGITALIGPNGAGKSTLLSMISRLLPPDSGEVLVDGLDVATTPSRELAK 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556496326  81 NIGYVIQQIGLFPNMTIEEnitVV-----PRMLGWDKARCKTRAEELMDMVALDP--HKFLNryprEMSGGQQQRIGVIR 153
Cdd:COG4604   76 RLAILRQENHINSRLTVRE---LVafgrfPYSKGRLTAEDREIIDEAIAYLDLEDlaDRYLD----ELSGGQRQRAFIAM 148

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 556496326 154 ALAADPPVLLMDEPFGAVDPINREVIQNQFLEMQRKLKKTVMLVSHDIDEALKLGDRIAVFRQGKIVQCASPDELL 229
Cdd:COG4604  149 VLAQDTDYVLLDEPLNNLDMKHSVQMMKLLRRLADELGKTVVIVLHDINFASCYADHIVAMKDGRVVAQGTPEEII 224
PRK13657 PRK13657
glucan ABC transporter ATP-binding protein/ permease;
21-231 7.93e-33

glucan ABC transporter ATP-binding protein/ permease;


Pssm-ID: 184214 [Multi-domain]  Cd Length: 588  Bit Score: 129.31  E-value: 7.93e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556496326  21 AVDNVNLNVPEGEMCVLLGPSGCGKTTTLKMINRLITPSSGTILINGEDTSGMDTVTLRRNIGYVIQQIGLFpNMTIEEN 100
Cdd:PRK13657 350 GVEDVSFEAKPGQTVAIVGPTGAGKSTLINLLQRVFDPQSGRILIDGTDIRTVTRASLRRNIAVVFQDAGLF-NRSIEDN 428

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556496326 101 ITVvprmlGWDKArckTRAEELMDMVALDPHKFLNRYP-----------REMSGGQQQRIGVIRALAADPPVLLMDEPFG 169
Cdd:PRK13657 429 IRV-----GRPDA---TDEEMRAAAERAQAHDFIERKPdgydtvvgergRQLSGGERQRLAIARALLKDPPILILDEATS 500

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 556496326 170 AVDpINREVIQNQFLEMQRKlKKTVMLVSH---DIDEAlklgDRIAVFRQGKIVQCASPDELLAK 231
Cdd:PRK13657 501 ALD-VETEAKVKAALDELMK-GRTTFIIAHrlsTVRNA----DRILVFDNGRVVESGSFDELVAR 559
modC PRK11144
molybdenum ABC transporter ATP-binding protein ModC;
7-220 9.41e-33

molybdenum ABC transporter ATP-binding protein ModC;


Pssm-ID: 182993 [Multi-domain]  Cd Length: 352  Bit Score: 125.76  E-value: 9.41e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556496326   7 LTKHFSQKHGQTFKavdNVNLNVPEGEMCVLLGPSGCGKTTTLKMINRLITPSSGTILING----EDTSGMDTVTLRRNI 82
Cdd:PRK11144   2 LELNFKQQLGDLCL---TVNLTLPAQGITAIFGRSGAGKTSLINAISGLTRPQKGRIVLNGrvlfDAEKGICLPPEKRRI 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556496326  83 GYVIQQIGLFPNMTIEENIT--VVPRMLG-WDKarcktraeeLMDMVALDPHkfLNRYPREMSGGQQQRIGVIRALAADP 159
Cdd:PRK11144  79 GYVFQDARLFPHYKVRGNLRygMAKSMVAqFDK---------IVALLGIEPL--LDRYPGSLSGGEKQRVAIGRALLTAP 147

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 556496326 160 PVLLMDEPFGAVD-PINREVIqnQFLEmqrKLKKTV---ML-VSHDIDEALKLGDRIAVFRQGKIV 220
Cdd:PRK11144 148 ELLLMDEPLASLDlPRKRELL--PYLE---RLAREInipILyVSHSLDEILRLADRVVVLEQGKVK 208
cbiO PRK13647
cobalt transporter ATP-binding subunit; Provisional
 2-233 2.38e-32

cobalt transporter ATP-binding subunit; Provisional


Pssm-ID: 237457 [Multi-domain]  Cd Length: 274  Bit Score: 122.54  E-value: 2.38e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556496326   2 IKLENLtkHFSQKHGQtfKAVDNVNLNVPEGEMCVLLGPSGCGKTTTLKMINRLITPSSGTILINGEDTSGMDTVTLRRN 81
Cdd:PRK13647   5 IEVEDL--HFRYKDGT--KALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGREVNAENEKWVRSK 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556496326  82 IGYVIQ----QIglFpNMTIEENITVVPRMLGWDKARCKTRAEELMDMVALdpHKFLNRYPREMSGGQQQRIGVIRALAA 157
Cdd:PRK13647  81 VGLVFQdpddQV--F-SSTVWDDVAFGPVNMGLDKDEVERRVEEALKAVRM--WDFRDKPPYHLSYGQKKRVAIAGVLAM 155

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 556496326 158 DPPVLLMDEPFGAVDPINREVIQnQFLEMQRKLKKTVMLVSHDIDEALKLGDRIAVFRQGKIVQCASPdELLAKPA 233
Cdd:PRK13647 156 DPDVIVLDEPMAYLDPRGQETLM-EILDRLHNQGKTVIVATHDVDLAAEWADQVIVLKEGRVLAEGDK-SLLTDED 229
PhnK COG1101
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ...
 1-220 4.64e-32

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


Pssm-ID: 440718 [Multi-domain]  Cd Length: 264  Bit Score: 121.35  E-value: 4.64e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556496326   1 MIKLENLTKHFSQKHGQTFKAVDNVNLNVPEGEMCVLLGPSGCGKTTTLKMINRLITPSSGTILINGEDTSGMDTVTLRR 80
Cdd:COG1101    1 MLELKNLSKTFNPGTVNEKRALDGLNLTIEEGDFVTVIGSNGAGKSTLLNAIAGSLPPDSGSILIDGKDVTKLPEYKRAK 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556496326  81 NIGYVIQ--QIGLFPNMTIEENITVV-----PRMLGWdkARCKTRAEELMDMVAL----------DPHKFLnrypremSG 143
Cdd:COG1101   81 YIGRVFQdpMMGTAPSMTIEENLALAyrrgkRRGLRR--GLTKKRRELFRELLATlglglenrldTKVGLL-------SG 151

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 556496326 144 GQQQRIGVIRALAADPPVLLMDEPFGAVDPINREVIQNQFLEMQRKLKKTVMLVSHDIDEALKLGDRIAVFRQGKIV 220
Cdd:COG1101  152 GQRQALSLLMATLTKPKLLLLDEHTAALDPKTAALVLELTEKIVEENNLTTLMVTHNMEQALDYGNRLIMMHEGRII 228
rim_protein TIGR01257
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ...
 4-225 7.51e-32

retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim protein) in eukaryotes. It is the member of ABC transporter superfamily. Rim protein is a membrane glycoprotein which is localized in the photoreceptor outer segment discs. Mutation/s in its genetic loci is implicated in the recessive Stargardt's disease. [Transport and binding proteins, Other]


Pssm-ID: 130324 [Multi-domain]  Cd Length: 2272  Bit Score: 127.82  E-value: 7.51e-32
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556496326     4 LENLTKHFsQKHGQtfKAVDNVNLNVPEGEMCVLLGPSGCGKTTTLKMINRLITPSSGTILINGEDT-SGMDTVtlRRNI 82
Cdd:TIGR01257  931 VKNLVKIF-EPSGR--PAVDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGKDIeTNLDAV--RQSL 1005

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556496326    83 GYVIQQIGLFPNMTIEENITVVPRMLG--WDKARCKTraEELMDMVALdpHKFLNRYPREMSGGQQQRIGVIRALAADPP 160
Cdd:TIGR01257 1006 GMCPQHNILFHHLTVAEHILFYAQLKGrsWEEAQLEM--EAMLEDTGL--HHKRNEEAQDLSGGMQRKLSVAIAFVGDAK 1081

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 556496326   161 VLLMDEPFGAVDPINREVIQNqfLEMQRKLKKTVMLVSHDIDEALKLGDRIAVFRQGKIVQCASP 225
Cdd:TIGR01257 1082 VVVLDEPTSGVDPYSRRSIWD--LLLKYRSGRTIIMSTHHMDEADLLGDRIAIISQGRLYCSGTP 1144
cbiO PRK13631
cobalt transporter ATP-binding subunit; Provisional
 1-233 9.50e-32

cobalt transporter ATP-binding subunit; Provisional


Pssm-ID: 237451 [Multi-domain]  Cd Length: 320  Bit Score: 122.27  E-value: 9.50e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556496326   1 MIKLENLTKHFSQKHGQTFKAVDNVNLNVPEGEMCVLLGPSGCGKTTTLKMINRLITPSSGTILI----NGEDTSGMDTV 76
Cdd:PRK13631  21 ILRVKNLYCVFDEKQENELVALNNISYTFEKNKIYFIIGNSGSGKSTLVTHFNGLIKSKYGTIQVgdiyIGDKKNNHELI 100

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556496326  77 T------------LRRNIGYVIQ--QIGLFPNmTIEENITVVPRMLGWDKARCKTRAEELMDMVALDpHKFLNRYPREMS 142
Cdd:PRK13631 101 TnpyskkiknfkeLRRRVSMVFQfpEYQLFKD-TIEKDIMFGPVALGVKKSEAKKLAKFYLNKMGLD-DSYLERSPFGLS 178

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556496326 143 GGQQQRIGVIRALAADPPVLLMDEPFGAVDPI-NREVIqnQFLEMQRKLKKTVMLVSHDIDEALKLGDRIAVFRQGKIVQ 221
Cdd:PRK13631 179 GGQKRRVAIAGILAIQPEILIFDEPTAGLDPKgEHEMM--QLILDAKANNKTVFVITHTMEHVLEVADEVIVMDKGKILK 256

                        250
                 ....*....|..
gi 556496326 222 CASPDELLAKPA 233
Cdd:PRK13631 257 TGTPYEIFTDQH 268
dppF PRK11308
dipeptide transporter ATP-binding subunit; Provisional
 6-232 5.90e-31

dipeptide transporter ATP-binding subunit; Provisional


Pssm-ID: 236898 [Multi-domain]  Cd Length: 327  Bit Score: 120.07  E-value: 5.90e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556496326   6 NLTKHFSQKHG-----QTFKAVDNVNLNVPEGEMCVLLGPSGCGKTTTLKMINRLITPSSGTILINGEDTSGMDTVT--- 77
Cdd:PRK11308  10 DLKKHYPVKRGlfkpeRLVKALDGVSFTLERGKTLAVVGESGCGKSTLARLLTMIETPTGGELYYQGQDLLKADPEAqkl 89

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556496326  78 LRRNIGYVIQQ--IGLFPNMTI----EENITVVPRMlgwDKARCKTRAEELMDMVALDPhKFLNRYPREMSGGQQQRIGV 151
Cdd:PRK11308  90 LRQKIQIVFQNpyGSLNPRKKVgqilEEPLLINTSL---SAAERREKALAMMAKVGLRP-EHYDRYPHMFSGGQRQRIAI 165

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556496326 152 IRALAADPPVLLMDEPFGAVDPINREVIQNQFLEMQRKLKKTVMLVSHDIDEALKLGDRIAVFRQGKIVQCASPDELLAK 231
Cdd:PRK11308 166 ARALMLDPDVVVADEPVSALDVSVQAQVLNLMMDLQQELGLSYVFISHDLSVVEHIADEVMVMYLGRCVEKGTKEQIFNN 245


                 .
gi 556496326 232 P 232
Cdd:PRK11308 246 P 246
PRK11160 PRK11160
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
 2-231 6.00e-31

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


Pssm-ID: 236865 [Multi-domain]  Cd Length: 574  Bit Score: 123.78  E-value: 6.00e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556496326   2 IKLENLtkHFSQkHGQTFKAVDNVNLNVPEGEMCVLLGPSGCGKTTTLKMINRLITPSSGTILINGEDTSGMDTVTLRRN 81
Cdd:PRK11160 339 LTLNNV--SFTY-PDQPQPVLKGLSLQIKAGEKVALLGRTGCGKSTLLQLLTRAWDPQQGEILLNGQPIADYSEAALRQA 415

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556496326  82 IGYVIQQIGLFpNMTIEENITvvprmLGWDKArcktRAEELMDMVA-------LDPHKFLNRY----PREMSGGQQQRIG 150
Cdd:PRK11160 416 ISVVSQRVHLF-SATLRDNLL-----LAAPNA----SDEALIEVLQqvgleklLEDDKGLNAWlgegGRQLSGGEQRRLG 485

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556496326 151 VIRALAADPPVLLMDEPFGAVDP-INREVIQNQFLEMQrklKKTVMLVSHDIdEALKLGDRIAVFRQGKIVQCASPDELL 229
Cdd:PRK11160 486 IARALLHDAPLLLLDEPTEGLDAeTERQILELLAEHAQ---NKTVLMITHRL-TGLEQFDRICVMDNGQIIEQGTHQELL 561


                 ..
gi 556496326 230 AK 231
Cdd:PRK11160 562 AQ 563
ssuB PRK11247
aliphatic sulfonates transport ATP-binding subunit; Provisional
 4-219 9.54e-31

aliphatic sulfonates transport ATP-binding subunit; Provisional


Pssm-ID: 183055 [Multi-domain]  Cd Length: 257  Bit Score: 117.86  E-value: 9.54e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556496326   4 LENLTKHFSQKhgqtfKAVDNVNLNVPEGEMCVLLGPSGCGKTTTLKMINRLITPSSGTILING-------EDTSGMdtv 76
Cdd:PRK11247  15 LNAVSKRYGER-----TVLNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAGELLAGTaplaearEDTRLM--- 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556496326  77 tlrrnigyvIQQIGLFPNMTIEENITvvprmLGWdKARCKTRAEELMDMVALDPHKflNRYPREMSGGQQQRIGVIRALA 156
Cdd:PRK11247  87 ---------FQDARLLPWKKVIDNVG-----LGL-KGQWRDAALQALAAVGLADRA--NEWPAALSGGQKQRVALARALI 149

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556496326 157 ADPPVLLMDEPFGAVDPINReviqnqfLEMQRKLKK-------TVMLVSHDIDEALKLGDRIAVFRQGKI 219
Cdd:PRK11247 150 HRPGLLLLDEPLGALDALTR-------IEMQDLIESlwqqhgfTVLLVTHDVSEAVAMADRVLLIEEGKI 212
ABCC_cytochrome_bd cd03247
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ...
 2-220 1.41e-30

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: 115.10  E-value: 1.41e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556496326   2 IKLENLtkHFSQKHgQTFKAVDNVNLNVPEGEMCVLLGPSGCGKTTTLKMINRLITPSSGTILINGEDTSGMDTvTLRRN 81
Cdd:cd03247    1 LSINNV--SFSYPE-QEQQVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDGVPVSDLEK-ALSSL 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556496326  82 IGYVIQQIGLFpNMTIEENITvvprmlgwdkarcktraeelmdmvaldphkflnrypREMSGGQQQRIGVIRALAADPPV 161
Cdd:cd03247   77 ISVLNQRPYLF-DTTLRNNLG------------------------------------RRFSGGERQRLALARILLQDAPI 119

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 556496326 162 LLMDEPFGAVDPINREVIQNQFLEMQRklKKTVMLVSHDIdEALKLGDRIAVFRQGKIV 220
Cdd:cd03247  120 VLLDEPTVGLDPITERQLLSLIFEVLK--DKTLIWITHHL-TGIEHMDKILFLENGKII 175
hmuV PRK13548
hemin importer ATP-binding subunit; Provisional
 1-229 1.73e-30

hemin importer ATP-binding subunit; Provisional


Pssm-ID: 237422 [Multi-domain]  Cd Length: 258  Bit Score: 117.18  E-value: 1.73e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556496326   1 MIKLENLTKHFSQKHgqtfkAVDNVNLNVPEGEMCVLLGPSGCGKTTTLKMINRLITPSSGTILINGEDTSGMDTVTLRR 80
Cdd:PRK13548   2 MLEARNLSVRLGGRT-----LLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLNGRPLADWSPAELAR 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556496326  81 NIGYVIQQIGL-FPnMTIEEnitVVpRM----LGWDKARCKTRAEELMDMVALDPhkFLNRYPREMSGGQQQRIGVIRAL 155
Cdd:PRK13548  77 RRAVLPQHSSLsFP-FTVEE---VV-AMgrapHGLSRAEDDALVAAALAQVDLAH--LAGRDYPQLSGGEQQRVQLARVL 149

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556496326 156 A------ADPPVLLMDEPFGAVDPINreviQNQFLEMQRKLKK----TVMLVSHDIDEALKLGDRIAVFRQGKIVQCASP 225
Cdd:PRK13548 150 AqlwepdGPPRWLLLDEPTSALDLAH----QHHVLRLARQLAHerglAVIVVLHDLNLAARYADRIVLLHQGRLVADGTP 225


                 ....
gi 556496326 226 DELL 229
Cdd:PRK13548 226 AEVL 229
PRK09984 PRK09984
phosphonate ABC transporter ATP-binding protein;
1-219 1.84e-30

phosphonate ABC transporter ATP-binding protein;


Pssm-ID: 182182 [Multi-domain]  Cd Length: 262  Bit Score: 117.42  E-value: 1.84e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556496326   1 MIKLENLTKHFSQKhgqtfKAVDNVNLNVPEGEMCVLLGPSGCGKTTTLKMINRLIT----PSSGTIL----INGEDTSG 72
Cdd:PRK09984   4 IIRVEKLAKTFNQH-----QALHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGLITgdksAGSHIELlgrtVQREGRLA 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556496326  73 MDTVTLRRNIGYVIQQIGLFPNMTIEENITV-----VP---RMLGWDKARCKTRAEELMDMVALdpHKFLNRYPREMSGG 144
Cdd:PRK09984  79 RDIRKSRANTGYIFQQFNLVNRLSVLENVLIgalgsTPfwrTCFSWFTREQKQRALQALTRVGM--VHFAHQRVSTLSGG 156

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 556496326 145 QQQRIGVIRALAADPPVLLMDEPFGAVDPINREVIQNQFLEMQRKLKKTVMLVSHDIDEALKLGDRIAVFRQGKI 219
Cdd:PRK09984 157 QQQRVAIARALMQQAKVILADEPIASLDPESARIVMDTLRDINQNDGITVVVTLHQVDYALRYCERIVALRQGHV 231
cbiO PRK13635
energy-coupling factor ABC transporter ATP-binding protein;
2-230 2.56e-30

energy-coupling factor ABC transporter ATP-binding protein;


Pssm-ID: 184195 [Multi-domain]  Cd Length: 279  Bit Score: 117.42  E-value: 2.56e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556496326   2 IKLENLTKHFSQkhgQTFKAVDNVNLNVPEGEMCVLLGPSGCGKTTTLKMINRLITPSSGTILINGEDTSgMDTV-TLRR 80
Cdd:PRK13635   6 IRVEHISFRYPD---AATYALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGGMVLS-EETVwDVRR 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556496326  81 NIGYVIQ----QiglFPNMTIE-------ENITVvPR--MLgwdkarckTRAEELMDMVALDPhkFLNRYPREMSGGQQQ 147
Cdd:PRK13635  82 QVGMVFQnpdnQ---FVGATVQddvafglENIGV-PReeMV--------ERVDQALRQVGMED--FLNREPHRLSGGQKQ 147

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556496326 148 RIGVIRALAADPPVLLMDEPFGAVDPINREviqnQFLEMQRKLKK----TVMLVSHDIDEALKlGDRIAVFRQGKIVQCA 223
Cdd:PRK13635 148 RVAIAGVLALQPDIIILDEATSMLDPRGRR----EVLETVRQLKEqkgiTVLSITHDLDEAAQ-ADRVIVMNKGEILEEG 222


                 ....*..
gi 556496326 224 SPDELLA 230
Cdd:PRK13635 223 TPEEIFK 229
PRK11831 PRK11831
phospholipid ABC transporter ATP-binding protein MlaF;
23-232 3.23e-30

phospholipid ABC transporter ATP-binding protein MlaF;


Pssm-ID: 236997 [Multi-domain]  Cd Length: 269  Bit Score: 116.79  E-value: 3.23e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556496326  23 DNVNLNVPEGEMCVLLGPSGCGKTTTLKMINRLITPSSGTILINGEDTSGMDTVTL---RRNIGYVIQQIGLFPNMTIEE 99
Cdd:PRK11831  24 DNISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEILFDGENIPAMSRSRLytvRKRMSMLFQSGALFTDMNVFD 103

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556496326 100 NI-------TVVPRMLgwdkarckTRAEELMDMVALDPHKFLNRYPREMSGGQQQRIGVIRALAADPPVLLMDEPFGAVD 172
Cdd:PRK11831 104 NVayplrehTQLPAPL--------LHSTVMMKLEAVGLRGAAKLMPSELSGGMARRAALARAIALEPDLIMFDEPFVGQD 175

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 556496326 173 PINREVIQNQFLEMQRKLKKTVMLVSHDIDEALKLGDRIAVFRQGKIVQCASPDELLAKP 232
Cdd:PRK11831 176 PITMGVLVKLISELNSALGVTCVVVSHDVPEVLSIADHAYIVADKKIVAHGSAQALQANP 235
cbiO PRK13642
energy-coupling factor transporter ATPase;
1-230 4.62e-30

energy-coupling factor transporter ATPase;


Pssm-ID: 184202 [Multi-domain]  Cd Length: 277  Bit Score: 116.73  E-value: 4.62e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556496326   1 MIKLENLTkhFSQKHGQTFKAVDNVNLNVPEGEMCVLLGPSGCGKTTTLKMINRLITPSSGTILINGEDTSGMDTVTLRR 80
Cdd:PRK13642   4 ILEVENLV--FKYEKESDVNQLNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDGELLTAENVWNLRR 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556496326  81 NIGYVIQQI-GLFPNMTIEENITVVPRMLGWDKARCKTRAEELMdmVALDPHKFLNRYPREMSGGQQQRIGVIRALAADP 159
Cdd:PRK13642  82 KIGMVFQNPdNQFVGATVEDDVAFGMENQGIPREEMIKRVDEAL--LAVNMLDFKTREPARLSGGQKQRVAVAGIIALRP 159

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 556496326 160 PVLLMDEPFGAVDPINREVIQNQFLEMQRKLKKTVMLVSHDIDEALKlGDRIAVFRQGKIVQCASPDELLA 230
Cdd:PRK13642 160 EIIILDESTSMLDPTGRQEIMRVIHEIKEKYQLTVLSITHDLDEAAS-SDRILVMKAGEIIKEAAPSELFA 229
ABC_Carb_Monos_II cd03215
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ...
 20-219 5.02e-30

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: 113.68  E-value: 5.02e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556496326  20 KAVDNVNLNVPEGEMCVLLGPSGCGKTTTLKMINRLITPSSGTILINGEDTSGMDTVTLRRN-IGYVI---QQIGLFPNM 95
Cdd:cd03215   14 GAVRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITLDGKPVTRRSPRDAIRAgIAYVPedrKREGLVLDL 93

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556496326  96 TIEENITVvPRMLgwdkarcktraeelmdmvaldphkflnrypremSGGQQQRIGVIRALAADPPVLLMDEPFGAVDPIN 175
Cdd:cd03215   94 SVAENIAL-SSLL---------------------------------SGGNQQKVVLARWLARDPRVLILDEPTRGVDVGA 139

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....
gi 556496326 176 REVIQNQFLEMQRKlKKTVMLVSHDIDEALKLGDRIAVFRQGKI 219
Cdd:cd03215  140 KAEIYRLIRELADA-GKAVLLISSELDELLGLCDRILVMYEGRI 182
TagH COG1134
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ...
 1-231 5.14e-30

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


Pssm-ID: 440749 [Multi-domain]  Cd Length: 245  Bit Score: 115.56  E-value: 5.14e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556496326   1 MIKLENLTKHF-----------------SQKHGQTFKAVDNVNLNVPEGEMCVLLGPSGCGKTTTLKMINRLITPSSGTI 63
Cdd:COG1134    4 MIEVENVSKSYrlyhepsrslkelllrrRRTRREEFWALKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTSGRV 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556496326  64 LINGEDTS------GMDtvtlrrnigyviqqiglfPNMTIEENITVVPRMLGWDKArcktRAEELMDMVA----LdpHKF 133
Cdd:COG1134   84 EVNGRVSAllelgaGFH------------------PELTGRENIYLNGRLLGLSRK----EIDEKFDEIVefaeL--GDF 139

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556496326 134 LN----RYpremSGGQQQRIGVIRALAADPPVLLMDEPFGAVDPINREVIQNQFLEMQRKlKKTVMLVSHDIDEALKLGD 209
Cdd:COG1134  140 IDqpvkTY----SSGMRARLAFAVATAVDPDILLVDEVLAVGDAAFQKKCLARIRELRES-GRTVIFVSHSMGAVRRLCD 214

                        250       260
                 ....*....|....*....|..
gi 556496326 210 RIAVFRQGKIVQCASPDELLAK 231
Cdd:COG1134  215 RAIWLEKGRLVMDGDPEEVIAA 236
cbiO PRK13650
energy-coupling factor transporter ATPase;
1-231 6.80e-30

energy-coupling factor transporter ATPase;


Pssm-ID: 184209 [Multi-domain]  Cd Length: 279  Bit Score: 115.98  E-value: 6.80e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556496326   1 MIKLENLTKHFSQKhgQTFKAVDNVNLNVPEGEMCVLLGPSGCGKTTTLKMINRLITPSSGTILINGEDTSGMDTVTLRR 80
Cdd:PRK13650   4 IIEVKNLTFKYKED--QEKYTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIIDGDLLTEENVWDIRH 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556496326  81 NIGYVIQQI-GLFPNMTIEENITVVPRMLGWDKARCKTRAEELMDMVALDphKFLNRYPREMSGGQQQRIGVIRALAADP 159
Cdd:PRK13650  82 KIGMVFQNPdNQFVGATVEDDVAFGLENKGIPHEEMKERVNEALELVGMQ--DFKEREPARLSGGQKQRVAIAGAVAMRP 159

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 556496326 160 PVLLMDEPFGAVDPINR-EVIQNqFLEMQRKLKKTVMLVSHDIDEaLKLGDRIAVFRQGKIVQCASPDELLAK 231
Cdd:PRK13650 160 KIIILDEATSMLDPEGRlELIKT-IKGIRDDYQMTVISITHDLDE-VALSDRVLVMKNGQVESTSTPRELFSR 230
nikE PRK10419
nickel ABC transporter ATP-binding protein NikE;
22-221 1.02e-29

nickel ABC transporter ATP-binding protein NikE;


Pssm-ID: 236689 [Multi-domain]  Cd Length: 268  Bit Score: 115.55  E-value: 1.02e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556496326  22 VDNVNLNVPEGEMCVLLGPSGCGKTTTLKMINRLITPSSGTILINGEDTSGMDTV---TLRRNIGYVIQQ-IGLF-PNMT 96
Cdd:PRK10419  28 LNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWRGEPLAKLNRAqrkAFRRDIQMVFQDsISAVnPRKT 107

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556496326  97 IEENITVVPR-MLGWDKARCKTRAEELMDMVALDPhKFLNRYPREMSGGQQQRIGVIRALAADPPVLLMDEpfgAVDPIN 175
Cdd:PRK10419 108 VREIIREPLRhLLSLDKAERLARASEMLRAVDLDD-SVLDKRPPQLSGGQLQRVCLARALAVEPKLLILDE---AVSNLD 183

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|
gi 556496326 176 ReVIQNQFL----EMQRKLKKTVMLVSHDIDEALKLGDRIAVFRQGKIVQ 221
Cdd:PRK10419 184 L-VLQAGVIrllkKLQQQFGTACLFITHDLRLVERFCQRVMVMDNGQIVE 232
PRK10261 PRK10261
glutathione transporter ATP-binding protein; Provisional
 21-221 2.04e-29

glutathione transporter ATP-binding protein; Provisional


Pssm-ID: 182342 [Multi-domain]  Cd Length: 623  Bit Score: 119.57  E-value: 2.04e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556496326  21 AVDNVNLNVPEGEMCVLLGPSGCGKTTTLKMINRLITPSSGTILINGE--DT-SGMDTVTLRRNIGYVIQQ--IGLFPNM 95
Cdd:PRK10261 339 AVEKVSFDLWPGETLSLVGESGSGKSTTGRALLRLVESQGGEIIFNGQriDTlSPGKLQALRRDIQFIFQDpyASLDPRQ 418

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556496326  96 TIEENIT---VVPRMLGWDKARckTRAEELMDMVALDPHKFLnRYPREMSGGQQQRIGVIRALAADPPVLLMDEPFGAVD 172
Cdd:PRK10261 419 TVGDSIMeplRVHGLLPGKAAA--ARVAWLLERVGLLPEHAW-RYPHEFSGGQRQRICIARALALNPKVIIADEAVSALD 495

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 556496326 173 PINREVIQNQFLEMQRKLKKTVMLVSHDIDEALKLGDRIAVFRQGKIVQ 221
Cdd:PRK10261 496 VSIRGQIINLLLDLQRDFGIAYLFISHDMAVVERISHRVAVMYLGQIVE 544
cbiO PRK13652
cobalt transporter ATP-binding subunit; Provisional
 8-232 2.35e-29

cobalt transporter ATP-binding subunit; Provisional


Pssm-ID: 172200 [Multi-domain]  Cd Length: 277  Bit Score: 114.51  E-value: 2.35e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556496326   8 TKHFSQKHGQTFKAVDNVNLNVPEGEMCVLLGPSGCGKTTTLKMINRLITPSSGTILINGEDTSGMDTVTLRRNIGYVIQ 87
Cdd:PRK13652   6 TRDLCYSYSGSKEALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIRGEPITKENIREVRKFVGLVFQ 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556496326  88 ----QIGlfpNMTIEENITVVPRMLGWDKARCKTRAEELMDMVALDphKFLNRYPREMSGGQQQRIGVIRALAADPPVLL 163
Cdd:PRK13652  86 npddQIF---SPTVEQDIAFGPINLGLDEETVAHRVSSALHMLGLE--ELRDRVPHHLSGGEKKRVAIAGVIAMEPQVLV 160

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 556496326 164 MDEPFGAVDPINREVIQNQFLEMQRKLKKTVMLVSHDIDEALKLGDRIAVFRQGKIVQCASPDELLAKP 232
Cdd:PRK13652 161 LDEPTAGLDPQGVKELIDFLNDLPETYGMTVIFSTHQLDLVPEMADYIYVMDKGRIVAYGTVEEIFLQP 229
cbiO PRK13643
energy-coupling factor transporter ATPase;
1-229 2.88e-29

energy-coupling factor transporter ATPase;


Pssm-ID: 184203 [Multi-domain]  Cd Length: 288  Bit Score: 114.83  E-value: 2.88e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556496326   1 MIKLENLTKHFSQKHGQTFKAVDNVNLNVPEGEMCVLLGPSGCGKTTTLKMINRLITPSSGTILING---EDTSGMDTVT 77
Cdd:PRK13643   1 MIKFEKVNYTYQPNSPFASRALFDIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVTVGDivvSSTSKQKEIK 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556496326  78 -LRRNIGYVIQqiglFPNM-----TIEENITVVPRMLGWDKARCKTRAEELMDMVALDpHKFLNRYPREMSGGQQQRIGV 151
Cdd:PRK13643  81 pVRKKVGVVFQ----FPESqlfeeTVLKDVAFGPQNFGIPKEKAEKIAAEKLEMVGLA-DEFWEKSPFELSGGQMRRVAI 155

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 556496326 152 IRALAADPPVLLMDEPFGAVDPINReVIQNQFLEMQRKLKKTVMLVSHDIDEALKLGDRIAVFRQGKIVQCASPDELL 229
Cdd:PRK13643 156 AGILAMEPEVLVLDEPTAGLDPKAR-IEMMQLFESIHQSGQTVVLVTHLMDDVADYADYVYLLEKGHIISCGTPSDVF 232
PRK14258 PRK14258
phosphate ABC transporter ATP-binding protein; Provisional
 2-242 4.08e-29

phosphate ABC transporter ATP-binding protein; Provisional


Pssm-ID: 184593 [Multi-domain]  Cd Length: 261  Bit Score: 113.59  E-value: 4.08e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556496326   2 IKLENLTKHFSqkhgqTFKAVDNVNLNVPEGEMCVLLGPSGCGKTTTLKMINRLITPSS-----GTILINGEDT--SGMD 74
Cdd:PRK14258   8 IKVNNLSFYYD-----TQKILEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLNRMNELESevrveGRVEFFNQNIyeRRVN 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556496326  75 TVTLRRNIGYVIQQIGLFPnMTIEENITVVPRMLGW-------DKARCKTRAEELMDMVAldpHKfLNRYPREMSGGQQQ 147
Cdd:PRK14258  83 LNRLRRQVSMVHPKPNLFP-MSVYDNVAYGVKIVGWrpkleidDIVESALKDADLWDEIK---HK-IHKSALDLSGGQQQ 157

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556496326 148 RIGVIRALAADPPVLLMDEPFGAVDPINREVIQNQFLEMQRKLKKTVMLVSHDIDEALKLGDRIAVF-----RQGKIVQC 222
Cdd:PRK14258 158 RLCIARALAVKPKVLLMDEPCFGLDPIASMKVESLIQSLRLRSELTMVIVSHNLHQVSRLSDFTAFFkgnenRIGQLVEF 237

                        250       260
                 ....*....|....*....|....
gi 556496326 223 ASPDELLAKPAN----EFVGSFVG 242
Cdd:PRK14258 238 GLTKKIFNSPHDsrtrEYVLSRLG 261
bacteriocin_ABC TIGR01193
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ...
 10-230 4.32e-29

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: 119.07  E-value: 4.32e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556496326   10 HFSQKHGQTFKAVDNVNLNVPEGEMCVLLGPSGCGKTTTLKMINRLITPSSGTILINGEDTSGMDTVTLRRNIGYVIQQI 89
Cdd:TIGR01193 478 DVSYSYGYGSNILSDISLTIKMNSKTTIVGMSGSGKSTLAKLLVGFFQARSGEILLNGFSLKDIDRHTLRQFINYLPQEP 557

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556496326   90 GLFPNmTIEENItvvprMLGwdkARCKTRAEELMDMVAL-----DPHKFLNRYPREM-------SGGQQQRIGVIRALAA 157
Cdd:TIGR01193 558 YIFSG-SILENL-----LLG---AKENVSQDEIWAACEIaeikdDIENMPLGYQTELseegssiSGGQKQRIALARALLT 628

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 556496326  158 DPPVLLMDEPFGAVDPINREVIQNQFLEMQrklKKTVMLVSHDIDEAlKLGDRIAVFRQGKIVQCASPDELLA 230
Cdd:TIGR01193 629 DSKVLILDESTSNLDTITEKKIVNNLLNLQ---DKTIIFVAHRLSVA-KQSDKIIVLDHGKIIEQGSHDELLD 697
livF PRK11614
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
1-233 7.33e-29

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


Pssm-ID: 183231 [Multi-domain]  Cd Length: 237  Bit Score: 112.28  E-value: 7.33e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556496326   1 MIKLENLTKHFSQkhgqtFKAVDNVNLNVPEGEMCVLLGPSGCGKTTTLKMINRLITPSSGTILINGEDTSGMDTV-TLR 79
Cdd:PRK11614   5 MLSFDKVSAHYGK-----IQALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDGKDITDWQTAkIMR 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556496326  80 RNIGYVIQQIGLFPNMTIEENITvvprMLGW--DKARCKTRAEELMDmvaLDPHKFLNRYPRE--MSGGQQQRIGVIRAL 155
Cdd:PRK11614  80 EAVAIVPEGRRVFSRMTVEENLA----MGGFfaERDQFQERIKWVYE---LFPRLHERRIQRAgtMSGGEQQMLAIGRAL 152

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556496326 156 AADPPVLLMDEPFGAVDPInreVIQNQF--LEMQRKLKKTVMLVSHDIDEALKLGDRIAVFRQGKIVQCASPDELLAKPA 233
Cdd:PRK11614 153 MSQPRLLLLDEPSLGLAPI---IIQQIFdtIEQLREQGMTIFLVEQNANQALKLADRGYVLENGHVVLEDTGDALLANEA 229
cbiO PRK13639
cobalt transporter ATP-binding subunit; Provisional
 21-232 7.39e-29

cobalt transporter ATP-binding subunit; Provisional


Pssm-ID: 184199 [Multi-domain]  Cd Length: 275  Bit Score: 113.25  E-value: 7.39e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556496326  21 AVDNVNLNVPEGEMCVLLGPSGCGKTTTLKMINRLITPSSGTILINGE--DTSGMDTVTLRRNIGYVIQQIG--LFPNmT 96
Cdd:PRK13639  17 ALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIKGEpiKYDKKSLLEVRKTVGIVFQNPDdqLFAP-T 95

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556496326  97 IEENITVVPRMLGWDKARCKTRAEELMDMVALDphKFLNRYPREMSGGQQQRIGVIRALAADPPVLLMDEPFGAVDPINR 176
Cdd:PRK13639  96 VEEDVAFGPLNLGLSKEEVEKRVKEALKAVGME--GFENKPPHHLSGGQKKRVAIAGILAMKPEIIVLDEPTSGLDPMGA 173

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 556496326 177 EVIQNQFLEMQRKlKKTVMLVSHDIDEALKLGDRIAVFRQGKIVQCASPDELLAKP 232
Cdd:PRK13639 174 SQIMKLLYDLNKE-GITIIISTHDVDLVPVYADKVYVMSDGKIIKEGTPKEVFSDI 228
PRK14271 PRK14271
phosphate ABC transporter ATP-binding protein; Provisional
 6-249 9.32e-29

phosphate ABC transporter ATP-binding protein; Provisional


Pssm-ID: 172759 [Multi-domain]  Cd Length: 276  Bit Score: 112.88  E-value: 9.32e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556496326   6 NLTKHFSQKhgqtfKAVDNVNLNVPEGEMCVLLGPSGCGKTTTLKMINRLITPSSG-----TILINGEDTSGM-DTVTLR 79
Cdd:PRK14271  26 NLTLGFAGK-----TVLDQVSMGFPARAVTSLMGPTGSGKTTFLRTLNRMNDKVSGyrysgDVLLGGRSIFNYrDVLEFR 100

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556496326  80 RNIGYVIQQIGLFPnMTIEENI-------TVVPRMLGWDKARCKTRAEELMDMVAldphKFLNRYPREMSGGQQQRIGVI 152
Cdd:PRK14271 101 RRVGMLFQRPNPFP-MSIMDNVlagvrahKLVPRKEFRGVAQARLTEVGLWDAVK----DRLSDSPFRLSGGQQQLLCLA 175

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556496326 153 RALAADPPVLLMDEPFGAVDPINREVIQNQFLEMQRKLkkTVMLVSHDIDEALKLGDRIAVFRQGKIVQCASPDELLAKP 232
Cdd:PRK14271 176 RTLAVNPEVLLLDEPTSALDPTTTEKIEEFIRSLADRL--TVIIVTHNLAQAARISDRAALFFDGRLVEEGPTEQLFSSP 253

                        250       260
                 ....*....|....*....|.
gi 556496326 233 AN----EFVGSFVGQDRTLKR 249
Cdd:PRK14271 254 KHaetaRYVAGLSGDVKDAKR 274
cbiO PRK13636
cobalt transporter ATP-binding subunit; Provisional
 8-231 2.20e-28

cobalt transporter ATP-binding subunit; Provisional


Pssm-ID: 184196 [Multi-domain]  Cd Length: 283  Bit Score: 112.25  E-value: 2.20e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556496326   8 TKHFSQKHGQTFKAVDNVNLNVPEGEMCVLLGPSGCGKTTTLKMINRLITPSSGTILINGE--DTSGMDTVTLRRNIGYV 85
Cdd:PRK13636   8 VEELNYNYSDGTHALKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGKpiDYSRKGLMKLRESVGMV 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556496326  86 IQQIG--LFpNMTIEENITVVPRMLGWDKARCKTRAEELMDMVALDPHKflNRYPREMSGGQQQRIGVIRALAADPPVLL 163
Cdd:PRK13636  88 FQDPDnqLF-SASVYQDVSFGAVNLKLPEDEVRKRVDNALKRTGIEHLK--DKPTHCLSFGQKKRVAIAGVLVMEPKVLV 164

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 556496326 164 MDEPFGAVDPINREVIQNQFLEMQRKLKKTVMLVSHDIDEALKLGDRIAVFRQGKIVQCASPDELLAK 231
Cdd:PRK13636 165 LDEPTAGLDPMGVSEIMKLLVEMQKELGLTIIIATHDIDIVPLYCDNVFVMKEGRVILQGNPKEVFAE 232
ArpD COG4618
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ...
 22-231 3.08e-28

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: 116.00  E-value: 3.08e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556496326  22 VDNVNLNVPEGEMCVLLGPSGCGKTTTLKMINRLITPSSGTILINGEDTSGMDTVTLRRNIGYVIQQIGLFPNmTIEENI 101
Cdd:COG4618  348 LRGVSFSLEPGEVLGVIGPSGSGKSTLARLLVGVWPPTAGSVRLDGADLSQWDREELGRHIGYLPQDVELFDG-TIAENI 426

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556496326 102 tvvprmlgwdkARcktraeelmdMVALDP------------HKFLNRYP-----------REMSGGQQQRIGVIRALAAD 158
Cdd:COG4618  427 -----------AR----------FGDADPekvvaaaklagvHEMILRLPdgydtrigeggARLSGGQRQRIGLARALYGD 485

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 556496326 159 PPVLLMDEPfgavdpiNR------EVIQNQFLEMQRKLKKTVMLVSHDIdEALKLGDRIAVFRQGKIVQCASPDELLAK 231
Cdd:COG4618  486 PRLVVLDEP-------NSnlddegEAALAAAIRALKARGATVVVITHRP-SLLAAVDKLLVLRDGRVQAFGPRDEVLAR 556
CydC TIGR02868
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ...
 8-200 4.57e-28

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: 115.15  E-value: 4.57e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556496326    8 TKHFSQKHGQTFKAVDNVNLNVPEGEMCVLLGPSGCGKTTTLKMINRLITPSSGTILINGEDTSGMDTVTLRRNIGYVIQ 87
Cdd:TIGR02868 337 LRDLSAGYPGAPPVLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPLQGEVTLDGVPVSSLDQDEVRRRVSVCAQ 416

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556496326   88 QIGLFpNMTIEENITVvprmlgwdkARCKTRAEELMDM---VALDPHkfLNRYP-----------REMSGGQQQRIGVIR 153
Cdd:TIGR02868 417 DAHLF-DTTVRENLRL---------ARPDATDEELWAAlerVGLADW--LRALPdgldtvlgeggARLSGGERQRLALAR 484

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 556496326  154 ALAADPPVLLMDEPFGAVDP-INREVIQNQFLEMQRklkKTVMLVSHD 200
Cdd:TIGR02868 485 ALLADAPILLLDEPTEHLDAeTADELLEDLLAALSG---RTVVLITHH 529
PRK10575 PRK10575
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
25-229 4.82e-28

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


Pssm-ID: 182561 [Multi-domain]  Cd Length: 265  Bit Score: 110.65  E-value: 4.82e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556496326  25 VNLNVPEGEMCVLLGPSGCGKTTTLKMINRLITPSSGTILINGEDTSGMDTVTLRRNIGYVIQQIGLFPNMTIEEnITVV 104
Cdd:PRK10575  30 LSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPLESWSSKAFARKVAYLPQQLPAAEGMTVRE-LVAI 108

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556496326 105 PR-----MLGWDKARCKTRAEELMDMVALDPhkFLNRYPREMSGGQQQRIGVIRALAADPPVLLMDEPFGAVDpINREV- 178
Cdd:PRK10575 109 GRypwhgALGRFGAADREKVEEAISLVGLKP--LAHRLVDSLSGGERQRAWIAMLVAQDSRCLLLDEPTSALD-IAHQVd 185

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 556496326 179 ----IQNqfLEMQRKLkkTVMLVSHDIDEALKLGDRIAVFRQGKIVQCASPDELL 229
Cdd:PRK10575 186 vlalVHR--LSQERGL--TVIAVLHDINMAARYCDYLVALRGGEMIAQGTPAELM 236
PRK10908 PRK10908
cell division ATP-binding protein FtsE;
1-220 5.93e-28

cell division ATP-binding protein FtsE;


Pssm-ID: 182829 [Multi-domain]  Cd Length: 222  Bit Score: 109.58  E-value: 5.93e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556496326   1 MIKLENLTKHFSQKHgqtfKAVDNVNLNVPEGEMCVLLGPSGCGKTTTLKMINRLITPSSGTILINGEDTSGM---DTVT 77
Cdd:PRK10908   1 MIRFEHVSKAYLGGR----QALQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDITRLknrEVPF 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556496326  78 LRRNIGYVIQQIGLFPNMTIEENITVVPRMLGWDKARCKTRAEELMDMVAL-DPHKflnRYPREMSGGQQQRIGVIRALA 156
Cdd:PRK10908  77 LRRQIGMIFQDHHLLMDRTVYDNVAIPLIIAGASGDDIRRRVSAALDKVGLlDKAK---NFPIQLSGGEQQRVGIARAVV 153

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 556496326 157 ADPPVLLMDEPFGAVDPINREVIQNQFLEMQRkLKKTVMLVSHDIDEALKLGDRIAVFRQGKIV 220
Cdd:PRK10908 154 NKPAVLLADEPTGNLDDALSEGILRLFEEFNR-VGVTVLMATHDIGLISRRSYRMLTLSDGHLH 216
ABC2_perm_RbbA NF033858
ribosome-associated ATPase/putative transporter RbbA;
2-231 9.22e-28

ribosome-associated ATPase/putative transporter RbbA;


Pssm-ID: 468210 [Multi-domain]  Cd Length: 907  Bit Score: 115.22  E-value: 9.22e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556496326   2 IKLENLTKHFSqkhgqTFKAVDNVNLNVPEGEMCVLLGPSGCGKTTTLKMINRLITPSSGTILINGE--DTSGMDTvtlR 79
Cdd:NF033858 267 IEARGLTMRFG-----DFTAVDHVSFRIRRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGEAWLFGQpvDAGDIAT---R 338

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556496326  80 RNIGYVIQQIGLFPNMTIEENITVVPRMLGWDKARCKTRAEELMDMVALDPHkfLNRYPREMSGGQQQRIgvirALAA-- 157
Cdd:NF033858 339 RRVGYMSQAFSLYGELTVRQNLELHARLFHLPAAEIAARVAEMLERFDLADV--ADALPDSLPLGIRQRL----SLAVav 412

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 556496326 158 --DPPVLLMDEPFGAVDPINREVIQNQFLEMQRKLKKTVMLVSHDIDEALKLgDRIAVFRQGKIVQCASPDELLAK 231
Cdd:NF033858 413 ihKPELLILDEPTSGVDPVARDMFWRLLIELSREDGVTIFISTHFMNEAERC-DRISLMHAGRVLASDTPAALVAA 487
lolD PRK11629
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
6-216 6.07e-27

lipoprotein-releasing ABC transporter ATP-binding protein LolD;


Pssm-ID: 183244 [Multi-domain]  Cd Length: 233  Bit Score: 106.82  E-value: 6.07e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556496326   6 NLTKHFSQKHGQTfKAVDNVNLNVPEGEMCVLLGPSGCGKTTTLKMINRLITPSSGTILINGEDTSGMDTVT---LR-RN 81
Cdd:PRK11629  10 NLCKRYQEGSVQT-DVLHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPMSKLSSAAkaeLRnQK 88

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556496326  82 IGYVIQQIGLFPNMTIEENITVvPRMLGWDK-ARCKTRAEELMDMVALDphKFLNRYPREMSGGQQQRIGVIRALAADPP 160
Cdd:PRK11629  89 LGFIYQFHHLLPDFTALENVAM-PLLIGKKKpAEINSRALEMLAAVGLE--HRANHRPSELSGGERQRVAIARALVNNPR 165

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 556496326 161 VLLMDEPFGAVDPINREVIQNQFLEMQRKLKKTVMLVSHDideaLKLGDRIAvfRQ 216
Cdd:PRK11629 166 LVLADEPTGNLDARNADSIFQLLGELNRLQGTAFLVVTHD----LQLAKRMS--RQ 215
ABCC_MRP_domain1 cd03250
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ...
 2-218 6.94e-27

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: 106.01  E-value: 6.94e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556496326   2 IKLENLTKHFSQKHGQTFKAVDNVNLNVPEGEMCVLLGPSGCGKTTTLKMINRLITPSSGTILINGedtsgmdtvtlrrN 81
Cdd:cd03250    1 ISVEDASFTWDSGEQETSFTLKDINLEVPKGELVAIVGPVGSGKSSLLSALLGELEKLSGSVSVPG-------------S 67

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556496326  82 IGYVIQQIGLFpNMTIEENITvvprmlgWDKARCKTRAEELMDMVALDPHkfLNRYPR-------E----MSGGQQQRIG 150
Cdd:cd03250   68 IAYVSQEPWIQ-NGTIRENIL-------FGKPFDEERYEKVIKACALEPD--LEILPDgdlteigEkginLSGGQKQRIS 137

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 556496326 151 VIRALAADPPVLLMDEPFGAVDP-INREVIQNQFLEMqRKLKKTVMLVSHDIdEALKLGDRIAVFRQGK 218
Cdd:cd03250  138 LARAVYSDADIYLLDDPLSAVDAhVGRHIFENCILGL-LLNNKTRILVTHQL-QLLPHADQIVVLDNGR 204
cbiO PRK13644
energy-coupling factor transporter ATPase;
1-238 7.27e-27

energy-coupling factor transporter ATPase;


Pssm-ID: 106587 [Multi-domain]  Cd Length: 274  Bit Score: 107.77  E-value: 7.27e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556496326   1 MIKLENLTkhFSQKHGQtfKAVDNVNLNVPEGEMCVLLGPSGCGKTTTLKMINRLITPSSGTILINGEDTSGMDTVT-LR 79
Cdd:PRK13644   1 MIRLENVS--YSYPDGT--PALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLVSGIDTGDFSKLQgIR 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556496326  80 RNIGYVIQQIGL-FPNMTIEENITVVPRMLGWDKARCKTRAEELMDMVALDphKFLNRYPREMSGGQQQRIGVIRALAAD 158
Cdd:PRK13644  77 KLVGIVFQNPETqFVGRTVEEDLAFGPENLCLPPIEIRKRVDRALAEIGLE--KYRHRSPKTLSGGQGQCVALAGILTME 154

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556496326 159 PPVLLMDEPFGAVDPINREVIQNQFLEMQRKlKKTVMLVSHDIDEaLKLGDRIAVFRQGKIVQCASPDELLAKPANEFVG 238
Cdd:PRK13644 155 PECLIFDEVTSMLDPDSGIAVLERIKKLHEK-GKTIVYITHNLEE-LHDADRIIVMDRGKIVLEGEPENVLSDVSLQTLG 232
cbiO PRK13649
energy-coupling factor transporter ATPase;
2-228 1.38e-26

energy-coupling factor transporter ATPase;


Pssm-ID: 184208 [Multi-domain]  Cd Length: 280  Bit Score: 107.14  E-value: 1.38e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556496326   2 IKLENLTkhFSQKHGQTF--KAVDNVNLNVPEGEMCVLLGPSGCGKTTTLKMINRLITPSSGTILINGE----DTSGMDT 75
Cdd:PRK13649   3 INLQNVS--YTYQAGTPFegRALFDVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDDTlitsTSKNKDI 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556496326  76 VTLRRNIGYVIQqiglFPNM-----TIEENITVVPRMLGWDKARCKTRAEELMDMVALDPHKFlNRYPREMSGGQQQRIG 150
Cdd:PRK13649  81 KQIRKKVGLVFQ----FPESqlfeeTVLKDVAFGPQNFGVSQEEAEALAREKLALVGISESLF-EKNPFELSGGQMRRVA 155

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 556496326 151 VIRALAADPPVLLMDEPFGAVDPINREVIQNQFLEMQRKlKKTVMLVSHDIDEALKLGDRIAVFRQGKIVQCASPDEL 228
Cdd:PRK13649 156 IAGILAMEPKILVLDEPTAGLDPKGRKELMTLFKKLHQS-GMTIVLVTHLMDDVANYADFVYVLEKGKLVLSGKPKDI 232
PRK13536 PRK13536
nodulation factor ABC transporter ATP-binding protein NodI;
2-229 1.64e-26

nodulation factor ABC transporter ATP-binding protein NodI;


Pssm-ID: 237419 [Multi-domain]  Cd Length: 340  Bit Score: 108.38  E-value: 1.64e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556496326   2 IKLENLTKHFSQKhgqtfKAVDNVNLNVPEGEMCVLLGPSGCGKTTTLKMINRLITPSSGTILINGEDTSGMDTVTlRRN 81
Cdd:PRK13536  42 IDLAGVSKSYGDK-----AVVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKITVLGVPVPARARLA-RAR 115

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556496326  82 IGYVIQQIGLFPNMTIEENITVVPRMLGWDKARCKTRAEELMDMVALDphKFLNRYPREMSGGQQQRIGVIRALAADPPV 161
Cdd:PRK13536 116 IGVVPQFDNLDLEFTVRENLLVFGRYFGMSTREIEAVIPSLLEFARLE--SKADARVSDLSGGMKRRLTLARALINDPQL 193

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 556496326 162 LLMDEPFGAVDPINREVIqnqfLEMQRKL---KKTVMLVSHDIDEALKLGDRIAVFRQGKIVQCASPDELL 229
Cdd:PRK13536 194 LILDEPTTGLDPHARHLI----WERLRSLlarGKTILLTTHFMEEAERLCDRLCVLEAGRKIAEGRPHALI 260
PRK10247 PRK10247
putative ABC transporter ATP-binding protein YbbL; Provisional
 20-203 2.53e-26

putative ABC transporter ATP-binding protein YbbL; Provisional


Pssm-ID: 182331 [Multi-domain]  Cd Length: 225  Bit Score: 105.18  E-value: 2.53e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556496326  20 KAVDNVNLNVPEGEMCVLLGPSGCGKTTTLKMINRLITPSSGTILINGEDTSGMDTVTLRRNIGYVIQQIGLFPNmTIEE 99
Cdd:PRK10247  21 KILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFEGEDISTLKPEIYRQQVSYCAQTPTLFGD-TVYD 99

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556496326 100 NItVVPRMLGWDKARCKTRAEELMDMvALdPHKFLNRYPREMSGGQQQRIGVIRALAADPPVLLMDEPFGAVDPINREVI 179
Cdd:PRK10247 100 NL-IFPWQIRNQQPDPAIFLDDLERF-AL-PDTILTKNIAELSGGEKQRISLIRNLQFMPKVLLLDEITSALDESNKHNV 176

                        170       180
                 ....*....|....*....|....
gi 556496326 180 QNQFLEMQRKLKKTVMLVSHDIDE 203
Cdd:PRK10247 177 NEIIHRYVREQNIAVLWVTHDKDE 200
PRK10535 PRK10535
macrolide ABC transporter ATP-binding protein/permease MacB;
1-220 2.91e-26

macrolide ABC transporter ATP-binding protein/permease MacB;


Pssm-ID: 182528 [Multi-domain]  Cd Length: 648  Bit Score: 110.58  E-value: 2.91e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556496326   1 MIKLENLTKHFSQKHGQTfKAVDNVNLNVPEGEMCVLLGPSGCGKTTTLKMINRLITPSSGTILINGEDTSGMDTVTL-- 78
Cdd:PRK10535   4 LLELKDIRRSYPSGEEQV-EVLKGISLDIYAGEMVAIVGASGSGKSTLMNILGCLDKPTSGTYRVAGQDVATLDADALaq 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556496326  79 --RRNIGYVIQQIGLFPNMTIEENITVVPRMLGWDKARCKTRAEELMDMVALDPHkfLNRYPREMSGGQQQRIGVIRALA 156
Cdd:PRK10535  83 lrREHFGFIFQRYHLLSHLTAAQNVEVPAVYAGLERKQRLLRAQELLQRLGLEDR--VEYQPSQLSGGQQQRVSIARALM 160

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 556496326 157 ADPPVLLMDEPFGAVDPINREVIQNqFLEMQRKLKKTVMLVSHDIDEALKlGDRIAVFRQGKIV 220
Cdd:PRK10535 161 NGGQVILADEPTGALDSHSGEEVMA-ILHQLRDRGHTVIIVTHDPQVAAQ-AERVIEIRDGEIV 222
PRK10584 PRK10584
putative ABC transporter ATP-binding protein YbbA; Provisional
 1-219 6.30e-26

putative ABC transporter ATP-binding protein YbbA; Provisional


Pssm-ID: 182569 [Multi-domain]  Cd Length: 228  Bit Score: 104.09  E-value: 6.30e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556496326   1 MIKLENLTKHFSQKHGQtFKAVDNVNLNVPEGEMCVLLGPSGCGKTTTLKMINRLITPSSGTILINGEDTSGMDT---VT 77
Cdd:PRK10584   6 IVEVHHLKKSVGQGEHE-LSILTGVELVVKRGETIALIGESGSGKSTLLAILAGLDDGSSGEVSLVGQPLHQMDEearAK 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556496326  78 LR-RNIGYVIQQIGLFPNMTIEENITVVPRMLGWDKARCKTRAEELMDMVALDphKFLNRYPREMSGGQQQRIGVIRALA 156
Cdd:PRK10584  85 LRaKHVGFVFQSFMLIPTLNALENVELPALLRGESSRQSRNGAKALLEQLGLG--KRLDHLPAQLSGGEQQRVALARAFN 162

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 556496326 157 ADPPVLLMDEPFGAVDPINREVIQNQFLEMQRKLKKTVMLVSHDIDEALKLGDRIAVfRQGKI 219
Cdd:PRK10584 163 GRPDVLFADEPTGNLDRQTGDKIADLLFSLNREHGTTLILVTHDLQLAARCDRRLRL-VNGQL 224
type_I_sec_PrtD TIGR01842
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in ...
 22-231 7.43e-26

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: 108.97  E-value: 7.43e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556496326   22 VDNVNLNVPEGEMCVLLGPSGCGKTTTLKMINRLITPSSGTILINGEDTSGMDTVTLRRNIGYVIQQIGLFPNmTIEENI 101
Cdd:TIGR01842 334 LRGISFSLQAGEALAIIGPSGSGKSTLARLIVGIWPPTSGSVRLDGADLKQWDRETFGKHIGYLPQDVELFPG-TVAENI 412

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556496326  102 TVVPRMLGWDKARCKTRAEELMDMVAldphKFLNRYPRE-------MSGGQQQRIGVIRALAADPPVLLMDEPFGAVDPI 174
Cdd:TIGR01842 413 ARFGENADPEKIIEAAKLAGVHELIL----RLPDGYDTVigpggatLSGGQRQRIALARALYGDPKLVVLDEPNSNLDEE 488

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 556496326  175 NREVIQNQFLEMQRKlKKTVMLVSHDIdEALKLGDRIAVFRQGKIVQCASPDELLAK 231
Cdd:TIGR01842 489 GEQALANAIKALKAR-GITVVVITHRP-SLLGCVDKILVLQDGRIARFGERDEVLAK 543
PRK09700 PRK09700
D-allose ABC transporter ATP-binding protein AlsA;
1-220 1.89e-25

D-allose ABC transporter ATP-binding protein AlsA;


Pssm-ID: 182036 [Multi-domain]  Cd Length: 510  Bit Score: 107.56  E-value: 1.89e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556496326   1 MIKLENLTKHFSQKHgqtfkAVDNVNLNVPEGEMCVLLGPSGCGKTTTLKMINRLITPSSGTILINGEDTSGMD-TVTLR 79
Cdd:PRK09700   5 YISMAGIGKSFGPVH-----ALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNINYNKLDhKLAAQ 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556496326  80 RNIGYVIQQIGLFPNMTIEENITV----VPRMLG---WDKARCKTRAEELMDMVALdpHKFLNRYPREMSGGQQQRIGVI 152
Cdd:PRK09700  80 LGIGIIYQELSVIDELTVLENLYIgrhlTKKVCGvniIDWREMRVRAAMMLLRVGL--KVDLDEKVANLSISHKQMLEIA 157

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 556496326 153 RALAADPPVLLMDEPFGAVdpINREV-----IQNQFlemqRKLKKTVMLVSHDIDEALKLGDRIAVFRQGKIV 220
Cdd:PRK09700 158 KTLMLDAKVIIMDEPTSSL--TNKEVdylflIMNQL----RKEGTAIVYISHKLAEIRRICDRYTVMKDGSSV 224
NupO COG3845
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ...
 21-228 1.95e-25

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


Pssm-ID: 443055 [Multi-domain]  Cd Length: 504  Bit Score: 107.42  E-value: 1.95e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556496326  21 AVDNVNLNVPEGEMCVLLGPSGCGKTTTLKMINRLITPSSGTILINGEDTSGMDTVTLRRN-IGYVI---QQIGLFPNMT 96
Cdd:COG3845  273 ALKDVSLEVRAGEILGIAGVAGNGQSELAEALAGLRPPASGSIRLDGEDITGLSPRERRRLgVAYIPedrLGRGLVPDMS 352

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556496326  97 IEENITV----VPRMLGW---DKARCKTRAEELMDmvaldphKFLNRYP------REMSGGQQQRIGVIRALAADPPVLL 163
Cdd:COG3845  353 VAENLILgryrRPPFSRGgflDRKAIRAFAEELIE-------EFDVRTPgpdtpaRSLSGGNQQKVILARELSRDPKLLI 425

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556496326 164 MDEP-----FGAVdpinrEVIQNQFLEMqRKLKKTVMLVSHDIDEALKLGDRIAVFRQGKIVQCASPDEL 228
Cdd:COG3845  426 AAQPtrgldVGAI-----EFIHQRLLEL-RDAGAAVLLISEDLDEILALSDRIAVMYEGRIVGEVPAAEA 489
AztA NF040873
zinc ABC transporter ATP-binding protein AztA;
21-205 2.13e-25

zinc ABC transporter ATP-binding protein AztA;


Pssm-ID: 468810 [Multi-domain]  Cd Length: 191  Bit Score: 101.54  E-value: 2.13e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556496326  21 AVDNVNLNVPEGEMCVLLGPSGCGKTTTLKMINRLITPSSGTIlingedtsgmdTVTLRRNIGYVIQQIGL---FPnMTI 97
Cdd:NF040873   7 VLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTV-----------RRAGGARVAYVPQRSEVpdsLP-LTV 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556496326  98 EENITV--VPRMLGWDKARCKTRAEELMDMVALDPHKFLNRYPREMSGGQQQRIGVIRALAADPPVLLMDEPFGAVDPIN 175
Cdd:NF040873  75 RDLVAMgrWARRGLWRRLTRDDRAAVDDALERVGLADLAGRQLGELSGGQRQRALLAQGLAQEADLLLLDEPTTGLDAES 154

                        170       180       190
                 ....*....|....*....|....*....|
gi 556496326 176 REVIqNQFLEMQRKLKKTVMLVSHDIDEAL 205
Cdd:NF040873 155 RERI-IALLAEEHARGATVVVVTHDLELVR 183
livG PRK11300
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
 21-232 3.54e-25

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


Pssm-ID: 183080 [Multi-domain]  Cd Length: 255  Bit Score: 102.76  E-value: 3.54e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556496326  21 AVDNVNLNVPEGEMCVLLGPSGCGKTTTLKMINRLITPSSGTILINGEDTSGM-DTVTLRRNIGYVIQQIGLFPNMTIEE 99
Cdd:PRK11300  20 AVNNVNLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTILLRGQHIEGLpGHQIARMGVVRTFQHVRLFREMTVIE 99

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556496326 100 NITVVP-RML------GWDKARCKTRAE-ELMDMVA--LDP---HKFLNRYPREMSGGQQQRIGVIRALAADPPVLLMDE 166
Cdd:PRK11300 100 NLLVAQhQQLktglfsGLLKTPAFRRAEsEALDRAAtwLERvglLEHANRQAGNLAYGQQRRLEIARCMVTQPEILMLDE 179

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 556496326 167 PFGAVDPINREVIQNQFLEMQRKLKKTVMLVSHDIDEALKLGDRIAVFRQGKIVQCASPDELLAKP 232
Cdd:PRK11300 180 PAAGLNPKETKELDELIAELRNEHNVTVLLIEHDMKLVMGISDRIYVVNQGTPLANGTPEEIRNNP 245
PRK11176 PRK11176
lipid A ABC transporter ATP-binding protein/permease MsbA;
21-231 1.09e-24

lipid A ABC transporter ATP-binding protein/permease MsbA;


Pssm-ID: 183016 [Multi-domain]  Cd Length: 582  Bit Score: 105.49  E-value: 1.09e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556496326  21 AVDNVNLNVPEGEMCVLLGPSGCGKTTTLKMINRLITPSSGTILINGEDTSGMDTVTLRRNIGYVIQQIGLFpNMTIEEN 100
Cdd:PRK11176 358 ALRNINFKIPAGKTVALVGRSGSGKSTIANLLTRFYDIDEGEILLDGHDLRDYTLASLRNQVALVSQNVHLF-NDTIANN 436

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556496326 101 ITVvprmlgwdkARCKTRAEELMDMVALDPH--KFLNRYPR-----------EMSGGQQQRIGVIRALAADPPVLLMDEP 167
Cdd:PRK11176 437 IAY---------ARTEQYSREQIEEAARMAYamDFINKMDNgldtvigengvLLSGGQRQRIAIARALLRDSPILILDEA 507

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 556496326 168 FGAVDPINREVIQNQFLEMQRklKKTVMLVSH---DIDEAlklgDRIAVFRQGKIVQCASPDELLAK 231
Cdd:PRK11176 508 TSALDTESERAIQAALDELQK--NRTSLVIAHrlsTIEKA----DEILVVEDGEIVERGTHAELLAQ 568
nikD PRK10418
nickel transporter ATP-binding protein NikD; Provisional
 22-254 1.29e-24

nickel transporter ATP-binding protein NikD; Provisional


Pssm-ID: 236688 [Multi-domain]  Cd Length: 254  Bit Score: 101.31  E-value: 1.29e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556496326  22 VDNVNLNVPEGEMCVLLGPSGCGKTTT----LKMINRLITPSSGTILINGEDTSGMDtvtLR-RNIGYVIQ--QIGLFPN 94
Cdd:PRK10418  19 VHGVSLTLQRGRVLALVGGSGSGKSLTcaaaLGILPAGVRQTAGRVLLDGKPVAPCA---LRgRKIATIMQnpRSAFNPL 95

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556496326  95 MTIEENITVVPRMLGwdKARCKTRAEELMDMVAL-DPHKFLNRYPREMSGGQQQRIGVIRALAADPPVLLMDEPFGAVDP 173
Cdd:PRK10418  96 HTMHTHARETCLALG--KPADDATLTAALEAVGLeNAARVLKLYPFEMSGGMLQRMMIALALLCEAPFIIADEPTTDLDV 173

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556496326 174 inreVIQNQFLEMQRKLKKT----VMLVSHDIDEALKLGDRIAVFRQGKIVQCASPDELLAKPANEFVGSFVGQDRTLKR 249
Cdd:PRK10418 174 ----VAQARILDLLESIVQKralgMLLVTHDMGVVARLADDVAVMSHGRIVEQGDVETLFNAPKHAVTRSLVSAHLALYG 249


                 ....*
gi 556496326 250 LLLVS 254
Cdd:PRK10418 250 MELAS 254
met_CoM_red_A2 TIGR03269
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ...
 2-231 1.98e-24

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: 104.50  E-value: 1.98e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556496326    2 IKLENLTKHFSQKhgqtfKAVDNVNLNVPEGEMCVLLGPSGCGKTTTLKMINRL--ITPSSGTILIN------------- 66
Cdd:TIGR03269   1 IEVKNLTKKFDGK-----EVLKNISFTIEEGEVLGILGRSGAGKSVLMHVLRGMdqYEPTSGRIIYHvalcekcgyverp 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556496326   67 ---GE-----------------DTSGMDTVTLRRNIGYVIQQ-IGLFPNMTIEENITVVPRMLGWDKARCKTRAEELMDM 125
Cdd:TIGR03269  76 skvGEpcpvcggtlepeevdfwNLSDKLRRRIRKRIAIMLQRtFALYGDDTVLDNVLEALEEIGYEGKEAVGRAVDLIEM 155

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556496326  126 VALDpHKFLNrYPREMSGGQQQRIGVIRALAADPPVLLMDEPFGAVDPINREVIQNQFLEMQRKLKKTVMLVSHDIDEAL 205
Cdd:TIGR03269 156 VQLS-HRITH-IARDLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALEEAVKASGISMVLTSHWPEVIE 233

                         250       260
                  ....*....|....*....|....*.
gi 556496326  206 KLGDRIAVFRQGKIVQCASPDELLAK 231
Cdd:TIGR03269 234 DLSDKAIWLENGEIKEEGTPDEVVAV 259
PRK15134 PRK15134
microcin C ABC transporter ATP-binding protein YejF; Provisional
 1-236 5.66e-24

microcin C ABC transporter ATP-binding protein YejF; Provisional


Pssm-ID: 237917 [Multi-domain]  Cd Length: 529  Bit Score: 103.25  E-value: 5.66e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556496326   1 MIKLENLTKHFSQKhGQTFKAVDNVNLNVPEGEMCVLLGPSGCGKTTTLKMINRLItPS------SGTILINGEDTSGMD 74
Cdd:PRK15134   5 LLAIENLSVAFRQQ-QTVRTVVNDVSLQIEAGETLALVGESGSGKSVTALSILRLL-PSppvvypSGDIRFHGESLLHAS 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556496326  75 TVTLRR----NIGYVIQQ--IGLFPNMTIEENITVV---PRMLGWDKARcktrAEEL--MDMVAL-DPHKFLNRYPREMS 142
Cdd:PRK15134  83 EQTLRGvrgnKIAMIFQEpmVSLNPLHTLEKQLYEVlslHRGMRREAAR----GEILncLDRVGIrQAAKRLTDYPHQLS 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556496326 143 GGQQQRIGVIRALAADPPVLLMDEPFGAVDPinreVIQNQFL----EMQRKLKKTVMLVSHDIDEALKLGDRIAVFRQGK 218
Cdd:PRK15134 159 GGERQRVMIAMALLTRPELLIADEPTTALDV----SVQAQILqllrELQQELNMGLLFITHNLSIVRKLADRVAVMQNGR 234

                        250
                 ....*....|....*...
gi 556496326 219 IVQCASPDELLAKPANEF 236
Cdd:PRK15134 235 CVEQNRAATLFSAPTHPY 252
PRK10253 PRK10253
iron-enterobactin ABC transporter ATP-binding protein;
5-229 1.05e-23

iron-enterobactin ABC transporter ATP-binding protein;


Pssm-ID: 182336 [Multi-domain]  Cd Length: 265  Bit Score: 98.91  E-value: 1.05e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556496326   5 ENLTKHFSQKhgqtfKAVDNVNLNVPEGEMCVLLGPSGCGKTTTLKMINRLITPSSGTILINGEDTSGMDTVTLRRNIGY 84
Cdd:PRK10253  11 EQLTLGYGKY-----TVAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIQHYASKEVARRIGL 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556496326  85 VIQQIGLFPNMTIEENITV-----VPRMLGWDK--ARCKTRAeelmdMVALDPHKFLNRYPREMSGGQQQRIGVIRALAA 157
Cdd:PRK10253  86 LAQNATTPGDITVQELVARgryphQPLFTRWRKedEEAVTKA-----MQATGITHLADQSVDTLSGGQRQRAWIAMVLAQ 160

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 556496326 158 DPPVLLMDEPFGAVDpINREVIQNQFL-EMQRKLKKTVMLVSHDIDEALKLGDRIAVFRQGKIVQCASPDELL 229
Cdd:PRK10253 161 ETAIMLLDEPTTWLD-ISHQIDLLELLsELNREKGYTLAAVLHDLNQACRYASHLIALREGKIVAQGAPKEIV 232
3a01208 TIGR00958
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
 24-232 3.10e-23

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


Pssm-ID: 273363 [Multi-domain]  Cd Length: 711  Bit Score: 101.72  E-value: 3.10e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556496326   24 NVNLNVPEGEMCVLLGPSGCGKTTTLKMINRLITPSSGTILINGEDTSGMDTVTLRRNIGYVIQQIGLFpNMTIEENITv 103
Cdd:TIGR00958 499 GLTFTLHPGEVVALVGPSGSGKSTVAALLQNLYQPTGGQVLLDGVPLVQYDHHYLHRQVALVGQEPVLF-SGSVRENIA- 576

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556496326  104 vprmLGWDKArckTRAEELMDMVALDPHKFLNRYPR-----------EMSGGQQQRIGVIRALAADPPVLLMDEPFGAVD 172
Cdd:TIGR00958 577 ----YGLTDT---PDEEIMAAAKAANAHDFIMEFPNgydtevgekgsQLSGGQKQRIAIARALVRKPRVLILDEATSALD 649

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 556496326  173 pinreVIQNQFLEMQRKLK-KTVMLVSHDIDEALKlGDRIAVFRQGKIVQCASPDELLAKP 232
Cdd:TIGR00958 650 -----AECEQLLQESRSRAsRTVLLIAHRLSTVER-ADQILVLKKGSVVEMGTHKQLMEDQ 704
MglA COG1129
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
20-228 3.87e-23

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


Pssm-ID: 440745 [Multi-domain]  Cd Length: 497  Bit Score: 100.48  E-value: 3.87e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556496326  20 KAVDNVNLNVPEGEMCVLLGPSGCGKTTTLKMINRLITPSSGTILINGEDTSGMDTVT-LRRNIGYVI---QQIGLFPNM 95
Cdd:COG1129  266 GVVRDVSFSVRAGEILGIAGLVGAGRTELARALFGADPADSGEIRLDGKPVRIRSPRDaIRAGIAYVPedrKGEGLVLDL 345

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556496326  96 TIEENIT--VVPRM--LGW-DKARCKTRAEELMDMVALdphkflnRYP------REMSGGQQQRIgVI-RALAADPPVLL 163
Cdd:COG1129  346 SIRENITlaSLDRLsrGGLlDRRRERALAEEYIKRLRI-------KTPspeqpvGNLSGGNQQKV-VLaKWLATDPKVLI 417

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556496326 164 MDEPFGAVDpIN--REVIQnqfleMQRKLK---KTVMLVSHDIDEALKLGDRIAVFRQGKIVQCASPDEL 228
Cdd:COG1129  418 LDEPTRGID-VGakAEIYR-----LIRELAaegKAVIVISSELPELLGLSDRILVMREGRIVGELDREEA 481
PRK15112 PRK15112
peptide ABC transporter ATP-binding protein SapF;
1-235 5.38e-23

peptide ABC transporter ATP-binding protein SapF;


Pssm-ID: 185067 [Multi-domain]  Cd Length: 267  Bit Score: 97.17  E-value: 5.38e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556496326   1 MIKLENLTKHFSQKHG----QTFKAVDNVNLNVPEGEMCVLLGPSGCGKTTTLKMINRLITPSSGTILINGEDTSGMDTV 76
Cdd:PRK15112   4 LLEVRNLSKTFRYRTGwfrrQTVEAVKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDHPLHFGDYS 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556496326  77 TLRRNIGYVIQ--QIGLFPNMTIEEnITVVPRMLGWD---KARCKtRAEELMDMVALDPHKfLNRYPREMSGGQQQRIGV 151
Cdd:PRK15112  84 YRSQRIRMIFQdpSTSLNPRQRISQ-ILDFPLRLNTDlepEQREK-QIIETLRQVGLLPDH-ASYYPHMLAPGQKQRLGL 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556496326 152 IRALAADPPVLLMDEPFGAVDPINREVIQNQFLEMQRKLKKTVMLVSHDIDEALKLGDRIAVFRQGKIVQCASPDELLAK 231
Cdd:PRK15112 161 ARALILRPKVIIADEALASLDMSMRSQLINLMLELQEKQGISYIYVTQHLGMMKHISDQVLVMHQGEVVERGSTADVLAS 240


                 ....
gi 556496326 232 PANE 235
Cdd:PRK15112 241 PLHE 244
NHLM_micro_ABC1 TIGR03796
NHLM bacteriocin system ABC transporter, peptidase/ATP-binding protein; This protein describes ...
 22-232 5.92e-23

NHLM bacteriocin system ABC transporter, peptidase/ATP-binding protein; This protein describes a multidomain ABC transporter subunit that is one of three protein families associated with some regularity with a distinctive family of putative bacteriocins. It includes a bacteriocin-processing peptidase domain at the N-terminus. Model TIGR03793 describes a conserved propeptide region for this bacteriocin family, unusual because it shows obvious homology a region of the enzyme nitrile hydratase up to the classic Gly-Gly cleavage motif. This family is therefore predicted to be a subunit of a bacteriocin processing and export system characteristic to this system that we designate NHLM, Nitrile Hydratase Leader Microcin. [Transport and binding proteins, Amino acids, peptides and amines, Cellular processes, Biosynthesis of natural products]


Pssm-ID: 274788 [Multi-domain]  Cd Length: 710  Bit Score: 100.79  E-value: 5.92e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556496326   22 VDNVNLNVPEGEMCVLLGPSGCGKTTTLKMINRLITPSSGTILINGEDTSGMDTVTLRRNIGYVIQQIGLFPNmTIEENI 101
Cdd:TIGR03796 495 IENFSLTLQPGQRVALVGGSGSGKSTIAKLVAGLYQPWSGEILFDGIPREEIPREVLANSVAMVDQDIFLFEG-TVRDNL 573

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556496326  102 TVvprmlgWDKarckTRAEELMDMVALDP--HKFLNRYP-----------REMSGGQQQRIGVIRALAADPPVLLMDEPF 168
Cdd:TIGR03796 574 TL------WDP----TIPDADLVRACKDAaiHDVITSRPggydaelaeggANLSGGQRQRLEIARALVRNPSILILDEAT 643

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 556496326  169 GAVDPI-NREVIQNqflemQRKLKKTVMLVSH------DIDEalklgdrIAVFRQGKIVQCASPDELLAKP 232
Cdd:TIGR03796 644 SALDPEtEKIIDDN-----LRRRGCTCIIVAHrlstirDCDE-------IIVLERGKVVQRGTHEELWAVG 702
PRK15134 PRK15134
microcin C ABC transporter ATP-binding protein YejF; Provisional
 21-236 8.79e-23

microcin C ABC transporter ATP-binding protein YejF; Provisional


Pssm-ID: 237917 [Multi-domain]  Cd Length: 529  Bit Score: 99.78  E-value: 8.79e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556496326  21 AVDNVNLNVPEGEMCVLLGPSGCGKTTTLKMINRLItPSSGTILINGEDTSGMD---TVTLRRNIGYVIQ--QIGLFPNM 95
Cdd:PRK15134 301 VVKNISFTLRPGETLGLVGESGSGKSTTGLALLRLI-NSQGEIWFDGQPLHNLNrrqLLPVRHRIQVVFQdpNSSLNPRL 379

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556496326  96 T----IEENITVVPRMLgwDKARCKTRAEELMDMVALDPHKfLNRYPREMSGGQQQRIGVIRALAADPPVLLMDEPFGAV 171
Cdd:PRK15134 380 NvlqiIEEGLRVHQPTL--SAAQREQQVIAVMEEVGLDPET-RHRYPAEFSGGQRQRIAIARALILKPSLIILDEPTSSL 456

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 556496326 172 DpinrEVIQNQFLEMQRKLKKTVML----VSHDIDEALKLGDRIAVFRQGKIVQCASPDELLAKPANEF 236
Cdd:PRK15134 457 D----KTVQAQILALLKSLQQKHQLaylfISHDLHVVRALCHQVIVLRQGEVVEQGDCERVFAAPQQEY 521
PRK10261 PRK10261
glutathione transporter ATP-binding protein; Provisional
 1-273 1.16e-22

glutathione transporter ATP-binding protein; Provisional


Pssm-ID: 182342 [Multi-domain]  Cd Length: 623  Bit Score: 99.54  E-value: 1.16e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556496326   1 MIKLENLTKHFSQKhGQTFKAVDNVNLNVPEGEMCVLLGPSGCGKTTTLKMINRLITPSSGTILINGE----------DT 70
Cdd:PRK10261  12 VLAVENLNIAFMQE-QQKIAAVRNLSFSLQRGETLAIVGESGSGKSVTALALMRLLEQAGGLVQCDKMllrrrsrqviEL 90

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556496326  71 SGMDTVTLRR----NIGYVIQQ--IGLFPNMTIEENITVVPRM-LGWDKARCKTRAEELMDMVAL-DPHKFLNRYPREMS 142
Cdd:PRK10261  91 SEQSAAQMRHvrgaDMAMIFQEpmTSLNPVFTVGEQIAESIRLhQGASREEAMVEAKRMLDQVRIpEAQTILSRYPHQLS 170

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556496326 143 GGQQQRIGVIRALAADPPVLLMDEPFGAVDPinreVIQNQFLE----MQRKLKKTVMLVSHDIDEALKLGDRIAVFRQGK 218
Cdd:PRK10261 171 GGMRQRVMIAMALSCRPAVLIADEPTTALDV----TIQAQILQlikvLQKEMSMGVIFITHDMGVVAEIADRVLVMYQGE 246

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 556496326 219 IVQCASPDELLAKPANEF----------VGSFVGQDRTlKRLLLVSAGDVTDQQPTI---TVRGSTPL 273
Cdd:PRK10261 247 AVETGSVEQIFHAPQHPYtrallaavpqLGAMKGLDYP-RRFPLISLEHPAKQEPPIeqdTVVDGEPI 313
ABCG_EPDR cd03213
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ...
 5-220 1.20e-22

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: 94.15  E-value: 1.20e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556496326   5 ENLTKHFSQKHGQTFKAV-DNVNLNVPEGEMCVLLGPSGCGKTTTLKMI-NRLITPS-SGTILINGEDtsgMDTVTLRRN 81
Cdd:cd03213    7 RNLTVTVKSSPSKSGKQLlKNVSGKAKPGELTAIMGPSGAGKSTLLNALaGRRTGLGvSGEVLINGRP---LDKRSFRKI 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556496326  82 IGYVIQQIGLFPNMTIEENITVVprmlgwdkARCktraeelmdmvaldphkflnrypREMSGGQQQRIGVIRALAADPPV 161
Cdd:cd03213   84 IGYVPQDDILHPTLTVRETLMFA--------AKL-----------------------RGLSGGERKRVSIALELVSNPSL 132

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 556496326 162 LLMDEPFGAVDPINreviQNQFLEMQRKLK---KTVMLVSHDI-DEALKLGDRIAVFRQGKIV 220
Cdd:cd03213  133 LFLDEPTSGLDSSS----ALQVMSLLRRLAdtgRTIICSIHQPsSEIFELFDKLLLLSQGRVI 191
SapD COG4170
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms];
6-232 1.60e-22

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


Pssm-ID: 443330 [Multi-domain]  Cd Length: 331  Bit Score: 96.90  E-value: 1.60e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556496326   6 NLTKHFSQKHGqTFKAVDNVNLNVPEGEMCVLLGPSGCGKTTTLKMINRlITPSSGTI-----LINGEDTSGMDTVTLR- 79
Cdd:COG4170    8 NLTIEIDTPQG-RVKAVDRVSLTLNEGEIRGLVGESGSGKSLIAKAICG-ITKDNWHVtadrfRWNGIDLLKLSPRERRk 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556496326  80 ---RNIGYVIQ--QIGLFPNMTI----EENI---TVVPRMLGWDKARcKTRAEELMDMVALDPHKF-LNRYPREMSGGQQ 146
Cdd:COG4170   86 iigREIAMIFQepSSCLDPSAKIgdqlIEAIpswTFKGKWWQRFKWR-KKRAIELLHRVGIKDHKDiMNSYPHELTEGEC 164

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556496326 147 QRIGVIRALAADPPVLLMDEPFGAVDPINreviQNQFLEMQRKLKK----TVMLVSHDIDEALKLGDRIAVFRQGKIVQC 222
Cdd:COG4170  165 QKVMIAMAIANQPRLLIADEPTNAMESTT----QAQIFRLLARLNQlqgtSILLISHDLESISQWADTITVLYCGQTVES 240

                        250
                 ....*....|
gi 556496326 223 ASPDELLAKP 232
Cdd:COG4170  241 GPTEQILKSP 250
ABCG_White cd03234
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ...
 13-222 3.22e-22

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: 93.87  E-value: 3.22e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556496326  13 QKHGQTFKAVDNVNLNVPEGEMCVLLGPSGCGKTTTLKMINRLITPS---SGTILINGEDtsgMDTVTLRRNIGYVIQQI 89
Cdd:cd03234   14 KNWNKYARILNDVSLHVESGQVMAILGSSGSGKTTLLDAISGRVEGGgttSGQILFNGQP---RKPDQFQKCVAYVRQDD 90

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556496326  90 GLFPNMTIEENITVVPRMLGWDKARCKTRAEELMDMVALDPH--KFLNRYPREMSGGQQQRIGVIRALAADPPVLLMDEP 167
Cdd:cd03234   91 ILLPGLTVRETLTYTAILRLPRKSSDAIRKKRVEDVLLRDLAltRIGGNLVKGISGGERRRVSIAVQLLWDPKVLILDEP 170

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 556496326 168 FGAVDPInrevIQNQFLEMQRKL---KKTVMLVSHDI-DEALKLGDRIAVFRQGKIVQC 222
Cdd:cd03234  171 TSGLDSF----TALNLVSTLSQLarrNRIVILTIHQPrSDLFRLFDRILLLSSGEIVYS 225
cbiO PRK13640
energy-coupling factor transporter ATPase;
9-232 4.32e-22

energy-coupling factor transporter ATPase;


Pssm-ID: 184200 [Multi-domain]  Cd Length: 282  Bit Score: 94.87  E-value: 4.32e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556496326   9 KHFSQKHGQTFK-AVDNVNLNVPEGEMCVLLGPSGCGKTTTLKMINRLITP---SSGTILINGEdTSGMDTV-TLRRNIG 83
Cdd:PRK13640   9 KHVSFTYPDSKKpALNDISFSIPRGSWTALIGHNGSGKSTISKLINGLLLPddnPNSKITVDGI-TLTAKTVwDIREKVG 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556496326  84 YVIQQI-GLFPNMTIEENITV------VPR--MLgwdkarcKTRAEELMDMVALDphkFLNRYPREMSGGQQQRIGVIRA 154
Cdd:PRK13640  88 IVFQNPdNQFVGATVGDDVAFglenraVPRpeMI-------KIVRDVLADVGMLD---YIDSEPANLSGGQKQRVAIAGI 157

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556496326 155 LAADPPVLLMDEPFGAVDPINREviqnQFLEMQRKLKK----TVMLVSHDIDEAlKLGDRIAVFRQGKIVQCASPDELLA 230
Cdd:PRK13640 158 LAVEPKIIILDESTSMLDPAGKE----QILKLIRKLKKknnlTVISITHDIDEA-NMADQVLVLDDGKLLAQGSPVEIFS 232


                 ..
gi 556496326 231 KP 232
Cdd:PRK13640 233 KV 234
PRK11174 PRK11174
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
 22-228 1.05e-21

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


Pssm-ID: 236870 [Multi-domain]  Cd Length: 588  Bit Score: 96.84  E-value: 1.05e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556496326  22 VDNVNLNVPEGEMCVLLGPSGCGKTTtlkMINRLI--TPSSGTILINGEDTSGMDTVTLRRNIGYVIQQIGLFPNmTIEE 99
Cdd:PRK11174 366 AGPLNFTLPAGQRIALVGPSGAGKTS---LLNALLgfLPYQGSLKINGIELRELDPESWRKHLSWVGQNPQLPHG-TLRD 441

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556496326 100 NITvvprmLGWDKARcktrAEELMDMVAL-DPHKFLNRYPR-----------EMSGGQQQRIGVIRALAADPPVLLMDEP 167
Cdd:PRK11174 442 NVL-----LGNPDAS----DEQLQQALENaWVSEFLPLLPQgldtpigdqaaGLSVGQAQRLALARALLQPCQLLLLDEP 512

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 556496326 168 FGAVDPINREVIQNQFLEMQRklKKTVMLVSHDIDEaLKLGDRIAVFRQGKIVQCASPDEL 228
Cdd:PRK11174 513 TASLDAHSEQLVMQALNAASR--RQTTLMVTHQLED-LAQWDQIWVMQDGQIVQQGDYAEL 570
dppD PRK11022
dipeptide transporter ATP-binding subunit; Provisional
 1-232 1.25e-21

dipeptide transporter ATP-binding subunit; Provisional


Pssm-ID: 182906 [Multi-domain]  Cd Length: 326  Bit Score: 94.42  E-value: 1.25e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556496326   1 MIKLENLTKHFSQKhGQTFKAVDNVNLNVPEGEMCVLLGPSGCGKTTTLKMINRLIT-P---SSGTILINGEDTSGMDTV 76
Cdd:PRK11022   3 LLNVDKLSVHFGDE-SAPFRAVDRISYSVKQGEVVGIVGESGSGKSVSSLAIMGLIDyPgrvMAEKLEFNGQDLQRISEK 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556496326  77 TLRRNIGYVIQQIGLFPNMTIEENITVVPRML-------GWDKARCKTRAEELMDMVAL-DPHKFLNRYPREMSGGQQQR 148
Cdd:PRK11022  82 ERRNLVGAEVAMIFQDPMTSLNPCYTVGFQIMeaikvhqGGNKKTRRQRAIDLLNQVGIpDPASRLDVYPHQLSGGMSQR 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556496326 149 IGVIRALAADPPVLLMDEPFGAVDPINREVIQNQFLEMQRKLKKTVMLVSHDIDEALKLGDRIAVFRQGKIVQCASPDEL 228
Cdd:PRK11022 162 VMIAMAIACRPKLLIADEPTTALDVTIQAQIIELLLELQQKENMALVLITHDLALVAEAAHKIIVMYAGQVVETGKAHDI 241


                 ....
gi 556496326 229 LAKP 232
Cdd:PRK11022 242 FRAP 245
phnK PRK11701
phosphonate C-P lyase system protein PhnK; Provisional
 1-232 1.42e-21

phosphonate C-P lyase system protein PhnK; Provisional


Pssm-ID: 183280 [Multi-domain]  Cd Length: 258  Bit Score: 92.68  E-value: 1.42e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556496326   1 MIKLENLTKHFSQKHGqtfkaVDNVNLNVPEGEMCVLLGPSGCGKTTTLKMINRLITPSSGTILINGEDTSGMDTVTL-- 78
Cdd:PRK11701   6 LLSVRGLTKLYGPRKG-----CRDVSFDLYPGEVLGIVGESGSGKTTLLNALSARLAPDAGEVHYRMRDGQLRDLYALse 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556496326  79 --RRNI-----GYVIQQI--GLFPNMTIEENITVVPRMLGWDK-ARCKTRAEELMDMVALDPHKfLNRYPREMSGGQQQR 148
Cdd:PRK11701  81 aeRRRLlrtewGFVHQHPrdGLRMQVSAGGNIGERLMAVGARHyGDIRATAGDWLERVEIDAAR-IDDLPTTFSGGMQQR 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556496326 149 IGVIRALAADPPVLLMDEPFGAVDpinreV-IQNQFLEMQRKLKKT----VMLVSHDIDEALKLGDRIAVFRQGKIVQCA 223
Cdd:PRK11701 160 LQIARNLVTHPRLVFMDEPTGGLD-----VsVQARLLDLLRGLVRElglaVVIVTHDLAVARLLAHRLLVMKQGRVVESG 234


                 ....*....
gi 556496326 224 SPDELLAKP 232
Cdd:PRK11701 235 LTDQVLDDP 243
araG PRK11288
L-arabinose ABC transporter ATP-binding protein AraG;
16-244 1.61e-21

L-arabinose ABC transporter ATP-binding protein AraG;


Pssm-ID: 183077 [Multi-domain]  Cd Length: 501  Bit Score: 95.75  E-value: 1.61e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556496326  16 GQTF---KAVDNVNLNVPEGEMCVLLGPSGCGKTTTLKMINRLITPSSGTILINGEDTSGMDTV-TLRRNIGYVIQQIGL 91
Cdd:PRK11288  11 GKTFpgvKALDDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSILIDGQEMRFASTTaALAAGVAIIYQELHL 90

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556496326  92 FPNMTIEENITV--VPRMLGW-DKARCKTRA-EELMDM-VALDPHKFLnrypREMSGGQQQRIGVIRALAADPPVLLMDE 166
Cdd:PRK11288  91 VPEMTVAENLYLgqLPHKGGIvNRRLLNYEArEQLEHLgVDIDPDTPL----KYLSIGQRQMVEIAKALARNARVIAFDE 166

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556496326 167 PFGAVDpiNREvIQNQFlEMQRKLK---KTVMLVSHDIDEALKLGDRIAVFRQGKIVqcASPDELLAKPANEFVGSFVGQ 243
Cdd:PRK11288 167 PTSSLS--ARE-IEQLF-RVIRELRaegRVILYVSHRMEEIFALCDAITVFKDGRYV--ATFDDMAQVDRDQLVQAMVGR 240


                 .
gi 556496326 244 D 244
Cdd:PRK11288 241 E 241
ATM1 COG5265
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ...
 23-231 1.85e-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: 96.04  E-value: 1.85e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556496326  23 DNVNLNVPEGEMCVLLGPSGCGKTTTLKMINRLITPSSGTILINGEDTSGMDTVTLRRNIGYVIQQIGLFpNMTIEENIT 102
Cdd:COG5265  375 KGVSFEVPAGKTVAIVGPSGAGKSTLARLLFRFYDVTSGRILIDGQDIRDVTQASLRAAIGIVPQDTVLF-NDTIAYNIA 453

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556496326 103 vvprmLGWDKArckTRAE--ELMDMVALdpHKFLNRYPR-----------EMSGGQQQRIGVIRALAADPPVLLMDEPFG 169
Cdd:COG5265  454 -----YGRPDA---SEEEveAAARAAQI--HDFIESLPDgydtrvgerglKLSGGEKQRVAIARTLLKNPPILIFDEATS 523

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 556496326 170 AVDPINREVIQNQFLEMQRklKKTVMLVSH---DIDEAlklgDRIAVFRQGKIVQCASPDELLAK 231
Cdd:COG5265  524 ALDSRTERAIQAALREVAR--GRTTLVIAHrlsTIVDA----DEILVLEAGRIVERGTHAELLAQ 582
ABC2_perm_RbbA NF033858
ribosome-associated ATPase/putative transporter RbbA;
2-231 5.18e-21

ribosome-associated ATPase/putative transporter RbbA;


Pssm-ID: 468210 [Multi-domain]  Cd Length: 907  Bit Score: 94.81  E-value: 5.18e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556496326   2 IKLENLTKHFsqkhGQTfKAVDNVNLNVPEGEMCVLLGPSGCGKTTTLKMIN--RLItpSSGTILINGEDtsgMDTVTLR 79
Cdd:NF033858   2 ARLEGVSHRY----GKT-VALDDVSLDIPAGCMVGLIGPDGVGKSSLLSLIAgaRKI--QQGRVEVLGGD---MADARHR 71

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556496326  80 RN----IGYVIQQIG--LFPNMTIEENITVVPRMLGWDKARCKTRAEELMDMVALDPhkFLNRYPREMSGGQQQRIGVIR 153
Cdd:NF033858  72 RAvcprIAYMPQGLGknLYPTLSVFENLDFFGRLFGQDAAERRRRIDELLRATGLAP--FADRPAGKLSGGMKQKLGLCC 149

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556496326 154 ALAADPPVLLMDEPFGAVDPINReviqNQFLEMQRKLKK-----TVMLVSHDIDEALKLgDRIAVFRQGKIVQCASPDEL 228
Cdd:NF033858 150 ALIHDPDLLILDEPTTGVDPLSR----RQFWELIDRIRAerpgmSVLVATAYMEEAERF-DWLVAMDAGRVLATGTPAEL 224


                 ...
gi 556496326 229 LAK 231
Cdd:NF033858 225 LAR 227
PRK15093 PRK15093
peptide ABC transporter ATP-binding protein SapD;
1-232 1.20e-20

peptide ABC transporter ATP-binding protein SapD;


Pssm-ID: 185049 [Multi-domain]  Cd Length: 330  Bit Score: 91.79  E-value: 1.20e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556496326   1 MIKLENLTKHFSQKHGQTfKAVDNVNLNVPEGEMCVLLGPSGCGKTTTLKMINRlITPSSGTILINGEDTSGMDTVTL-- 78
Cdd:PRK15093   3 LLDIRNLTIEFKTSDGWV-KAVDRVSMTLTEGEIRGLVGESGSGKSLIAKAICG-VTKDNWRVTADRMRFDDIDLLRLsp 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556496326  79 ---RRNIGYVIQQIGLFPNMTIE--ENI--TVVPRMLGWD-KARC-------KTRAEELMDMVALDPHKFLNR-YPREMS 142
Cdd:PRK15093  81 rerRKLVGHNVSMIFQEPQSCLDpsERVgrQLMQNIPGWTyKGRWwqrfgwrKRRAIELLHRVGIKDHKDAMRsFPYELT 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556496326 143 GGQQQRIGVIRALAADPPVLLMDEPFGAVDPINREVIQNQFLEMQRKLKKTVMLVSHDIDEALKLGDRIAVFRQGKIVQC 222
Cdd:PRK15093 161 EGECQKVMIAIALANQPRLLIADEPTNAMEPTTQAQIFRLLTRLNQNNNTTILLISHDLQMLSQWADKINVLYCGQTVET 240

                        250
                 ....*....|
gi 556496326 223 ASPDELLAKP 232
Cdd:PRK15093 241 APSKELVTTP 250
CP_lyasePhnK TIGR02323
phosphonate C-P lyase system protein PhnK; Members of this family are the PhnK protein of C-P ...
 20-232 3.61e-20

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: 88.73  E-value: 3.61e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556496326   20 KAVDNVNLNVPEGEMCVLLGPSGCGKTTTLKMINRLITPSSGTILINGEDTSGMDTVTL---------RRNIGYVIQQI- 89
Cdd:TIGR02323  17 KGCRDVSFDLYPGEVLGIVGESGSGKSTLLGCLAGRLAPDHGTATYIMRSGAELELYQLseaerrrlmRTEWGFVHQNPr 96

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556496326   90 -GLFPNMTIEENITVVPRMLGWDK-ARCKTRAEELMDMVALDPHKfLNRYPREMSGGQQQRIGVIRALAADPPVLLMDEP 167
Cdd:TIGR02323  97 dGLRMRVSAGANIGERLMAIGARHyGNIRATAQDWLEEVEIDPTR-IDDLPRAFSGGMQQRLQIARNLVTRPRLVFMDEP 175

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 556496326  168 FGAVDPinreVIQNQFLEMQRKLKK----TVMLVSHDIDEALKLGDRIAVFRQGKIVQCASPDELLAKP 232
Cdd:TIGR02323 176 TGGLDV----SVQARLLDLLRGLVRdlglAVIIVTHDLGVARLLAQRLLVMQQGRVVESGLTDQVLDDP 240
cbiO PRK13638
energy-coupling factor ABC transporter ATP-binding protein;
37-231 5.63e-20

energy-coupling factor ABC transporter ATP-binding protein;


Pssm-ID: 184198 [Multi-domain]  Cd Length: 271  Bit Score: 88.53  E-value: 5.63e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556496326  37 LLGPSGCGKTTTLKMINRLITPSSGTILINGE--DTSGMDTVTLRRNIGYVIQQiglfPNMTI-----EENITVVPRMLG 109
Cdd:PRK13638  32 LVGANGCGKSTLFMNLSGLLRPQKGAVLWQGKplDYSKRGLLALRQQVATVFQD----PEQQIfytdiDSDIAFSLRNLG 107

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556496326 110 WDKARCKTRAEELMDMValDPHKFLNRYPREMSGGQQQRIGVIRALAADPPVLLMDEPFGAVDPINReviqNQFLEMQRK 189
Cdd:PRK13638 108 VPEAEITRRVDEALTLV--DAQHFRHQPIQCLSHGQKKRVAIAGALVLQARYLLLDEPTAGLDPAGR----TQMIAIIRR 181

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*
gi 556496326 190 L---KKTVMLVSHDIDEALKLGDRIAVFRQGKIVQCASPDELLAK 231
Cdd:PRK13638 182 IvaqGNHVIISSHDIDLIYEISDAVYVLRQGQILTHGAPGEVFAC 226
PRK09700 PRK09700
D-allose ABC transporter ATP-binding protein AlsA;
16-221 6.60e-20

D-allose ABC transporter ATP-binding protein AlsA;


Pssm-ID: 182036 [Multi-domain]  Cd Length: 510  Bit Score: 91.00  E-value: 6.60e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556496326  16 GQTFKAVDNVNLNVPEGEMCVLLGPSGCGKTTTLKMINRLITPSSGTILINGED---TSGMDTVtlRRNIGYVIQ---QI 89
Cdd:PRK09700 273 SRDRKKVRDISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEIRLNGKDispRSPLDAV--KKGMAYITEsrrDN 350

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556496326  90 GLFPNMTIEENITVVP--RMLGW--------DKARCKTrAEELMDMVALDPHKfLNRYPREMSGGQQQRIGVIRALAADP 159
Cdd:PRK09700 351 GFFPNFSIAQNMAISRslKDGGYkgamglfhEVDEQRT-AENQRELLALKCHS-VNQNITELSGGNQQKVLISKWLCCCP 428

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 556496326 160 PVLLMDEPFGAVDPINREVIqnqfLEMQRKLK---KTVMLVSHDIDEALKLGDRIAVFRQGKIVQ 221
Cdd:PRK09700 429 EVIIFDEPTRGIDVGAKAEI----YKVMRQLAddgKVILMVSSELPEIITVCDRIAVFCEGRLTQ 489
ccmA TIGR01189
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ...
 24-173 7.48e-20

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: 86.64  E-value: 7.48e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556496326   24 NVNLNVPEGEMCVLLGPSGCGKTTTLKMINRLITPSSGTILINGEDtSGMDTVTLRRNIGYVIQQIGLFPNMTIEENITV 103
Cdd:TIGR01189  18 GLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRWNGTP-LAEQRDEPHENILYLGHLPGLKPELSALENLHF 96

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556496326  104 VPRMLGWDKARCktraEELMDMVALDPHKflNRYPREMSGGQQQRIGVIRALAADPPVLLMDEPFGAVDP 173
Cdd:TIGR01189  97 WAAIHGGAQRTI----EDALAAVGLTGFE--DLPAAQLSAGQQRRLALARLWLSRRPLWILDEPTTALDK 160
Uup COG0488
ATPase components of ABC transporters with duplicated ATPase domains [General function ...
 4-200 1.54e-19

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


Pssm-ID: 440254 [Multi-domain]  Cd Length: 520  Bit Score: 90.12  E-value: 1.54e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556496326   4 LENLTKHFSQKhgqtfKAVDNVNLNVPEGEmCV-LLGPSGCGKTTTLKMINRLITPSSGTILINGEDTsgmdtvtlrrnI 82
Cdd:COG0488    1 LENLSKSFGGR-----PLLDDVSLSINPGD-RIgLVGRNGAGKSTLLKILAGELEPDSGEVSIPKGLR-----------I 63

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556496326  83 GYVIQQIGLFPNMTIEENI-TVVPRMlgWDKARCKTRAEELMDMVALDPHKF---------------------------- 133
Cdd:COG0488   64 GYLPQEPPLDDDLTVLDTVlDGDAEL--RALEAELEELEAKLAEPDEDLERLaelqeefealggweaearaeeilsglgf 141

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556496326 134 ----LNRYPREMSGGQQQRIGVIRALAADPPVLLMDEPfgavdpinreviQN-----------QFLemqRKLKKTVMLVS 198
Cdd:COG0488  142 peedLDRPVSELSGGWRRRVALARALLSEPDLLLLDEP------------TNhldlesiewleEFL---KNYPGTVLVVS 206


                 ..
gi 556496326 199 HD 200
Cdd:COG0488  207 HD 208
ABCC_TAP cd03248
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ...
 2-219 1.78e-19

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: 86.37  E-value: 1.78e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556496326   2 IKLENLTkhFSQKHGQTFKAVDNVNLNVPEGEMCVLLGPSGCGKTTTLKMINRLITPSSGTILINGEDTSGMDTVTLRRN 81
Cdd:cd03248   12 VKFQNVT--FAYPTRPDTLVLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDGKPISQYEHKYLHSK 89

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556496326  82 IGYVIQQIGLFPNmTIEENI----TVVPRMLGWDKARcKTRAEELMDMVALDPHKFLNRYPREMSGGQQQRIGVIRALAA 157
Cdd:cd03248   90 VSLVGQEPVLFAR-SLQDNIayglQSCSFECVKEAAQ-KAHAHSFISELASGYDTEVGEKGSQLSGGQKQRVAIARALIR 167

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 556496326 158 DPPVLLMDEPFGAVDPINREVIQNQFLEMQRklKKTVMLVSHDIdEALKLGDRIAVFRQGKI 219
Cdd:cd03248  168 NPQVLILDEATSALDAESEQQVQQALYDWPE--RRTVLVIAHRL-STVERADQILVLDGGRI 226
PRK15439 PRK15439
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
 1-220 1.79e-19

autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional


Pssm-ID: 185336 [Multi-domain]  Cd Length: 510  Bit Score: 89.72  E-value: 1.79e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556496326   1 MIKLENLTKHFSQKhgQTFKAVDnvnLNVPEGEMCVLLGPSGCGKTTTLKMINRLITPSSGTILINGEDTSGMdTVTLRR 80
Cdd:PRK15439  11 LLCARSISKQYSGV--EVLKGID---FTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIGGNPCARL-TPAKAH 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556496326  81 NIG-YVI-QQIGLFPNMTIEENITV-VPRmlgwdKARCKTRAEELMDM--VALDPHkflnrypreMSGG-----QQQRIG 150
Cdd:PRK15439  85 QLGiYLVpQEPLLFPNLSVKENILFgLPK-----RQASMQKMKQLLAAlgCQLDLD---------SSAGslevaDRQIVE 150

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 556496326 151 VIRALAADPPVLLMDEPFGAVDPINREviqNQFLEMQRKLKKTVMLV--SHDIDEALKLGDRIAVFRQGKIV 220
Cdd:PRK15439 151 ILRGLMRDSRILILDEPTASLTPAETE---RLFSRIRELLAQGVGIVfiSHKLPEIRQLADRISVMRDGTIA 219
ABCC_MRP_domain2 cd03244
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ...
 9-225 8.18e-19

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: 84.08  E-value: 8.18e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556496326   9 KHFSQKHGQTFKAV-DNVNLNVPEGEMCVLLGPSGCGKTTTLKMINRLITPSSGTILINGEDTSGMDTVTLRRNIGYVIQ 87
Cdd:cd03244    6 KNVSLRYRPNLPPVlKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSILIDGVDISKIGLHDLRSRISIIPQ 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556496326  88 QIGLFPNmTIEENITvvPrmLG-------WD-------KARCKTRAEELMDMVALDPHKFlnrypremSGGQQQRIGVIR 153
Cdd:cd03244   86 DPVLFSG-TIRSNLD--P--FGeysdeelWQalervglKEFVESLPGGLDTVVEEGGENL--------SVGQRQLLCLAR 152

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 556496326 154 ALAADPPVLLMDEPFGAVDPINREVIQnQFLEMQRKlKKTVMLVSHDIDEALKLgDRIAVFRQGKIVQCASP 225
Cdd:cd03244  153 ALLRKSKILVLDEATASVDPETDALIQ-KTIREAFK-DCTVLTIAHRLDTIIDS-DRILVLDKGRVVEFDSP 221
cbiO PRK13648
cobalt transporter ATP-binding subunit; Provisional
 9-231 1.18e-18

cobalt transporter ATP-binding subunit; Provisional


Pssm-ID: 184207 [Multi-domain]  Cd Length: 269  Bit Score: 84.80  E-value: 1.18e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556496326   9 KHFS-QKHGQTFKAVDNVNLNVPEGEMCVLLGPSGCGKTTTLKMINRLITPSSGTILINGEDTSGMDTVTLRRNIGYVIQ 87
Cdd:PRK13648  11 KNVSfQYQSDASFTLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIFYNNQAITDDNFEKLRKHIGIVFQ 90

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556496326  88 Q---------------IGLFPNMTIEENI-TVVPRMLgwdkarcktraeELMDMVALDPHKflnryPREMSGGQQQRIGV 151
Cdd:PRK13648  91 NpdnqfvgsivkydvaFGLENHAVPYDEMhRRVSEAL------------KQVDMLERADYE-----PNALSGGQKQRVAI 153

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556496326 152 IRALAADPPVLLMDEPFGAVDPINREVIQNQFLEMQRKLKKTVMLVSHDIDEALKlGDRIAVFRQGKIVQCASPDELLAK 231
Cdd:PRK13648 154 AGVLALNPSVIILDEATSMLDPDARQNLLDLVRKVKSEHNITIISITHDLSEAME-ADHVIVMNKGTVYKEGTPTEIFDH 232
ABCC_SUR1_N cd03290
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ...
 16-217 1.96e-18

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: 83.15  E-value: 1.96e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556496326  16 GQTFKAVDNVNLNVPEGEMCVLLGPSGCGKTTTL-KMINRLITPSSGTILINGEDTSGMDTVTLRRN---IGYVIQQIGL 91
Cdd:cd03290   11 GSGLATLSNINIRIPTGQLTMIVGQVGCGKSSLLlAILGEMQTLEGKVHWSNKNESEPSFEATRSRNrysVAYAAQKPWL 90

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556496326  92 FpNMTIEENITvvprmlgWDKARCKTRAEELMDMVALDPHKFLNRYPRE---------MSGGQQQRIGVIRALAADPPVL 162
Cdd:cd03290   91 L-NATVEENIT-------FGSPFNKQRYKAVTDACSLQPDIDLLPFGDQteigerginLSGGQRQRICVARALYQNTNIV 162

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 556496326 163 LMDEPFGAVD-PINREVIQNQFLEMQRKLKKTVMLVSHDIdEALKLGDRIAVFRQG 217
Cdd:cd03290  163 FLDDPFSALDiHLSDHLMQEGILKFLQDDKRTLVLVTHKL-QYLPHADWIIAMKDG 217
ABCF_EF-3 cd03221
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ...
 2-218 2.14e-18

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: 80.96  E-value: 2.14e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556496326   2 IKLENLTKHFSQKhgQTFKavdNVNLNVPEGEMCVLLGPSGCGKTTTLKMINRLITPSSGTIlingedtsgmdTVTLRRN 81
Cdd:cd03221    1 IELENLSKTYGGK--LLLK---DISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIV-----------TWGSTVK 64

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556496326  82 IGYVIQqiglfpnmtieenitvvprmlgwdkarcktraeelmdmvaldphkflnrypreMSGGQQQRIGVIRALAADPPV 161
Cdd:cd03221   65 IGYFEQ-----------------------------------------------------LSGGEKMRLALAKLLLENPNL 91

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 556496326 162 LLMDEPFGAVDPINREVIQNQFlemqRKLKKTVMLVSHD---IDealKLGDRIAVFRQGK 218
Cdd:cd03221   92 LLLDEPTNHLDLESIEALEEAL----KEYPGTVILVSHDryfLD---QVATKIIELEDGK 144
Uup COG0488
ATPase components of ABC transporters with duplicated ATPase domains [General function ...
 1-220 2.15e-18

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


Pssm-ID: 440254 [Multi-domain]  Cd Length: 520  Bit Score: 86.66  E-value: 2.15e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556496326   1 MIKLENLTKHFSQKhgqtfKAVDNVNLNVPEGEMCVLLGPSGCGKTTTLKMINRLITPSSGTILInGEdtsgmdTVtlrr 80
Cdd:COG0488  315 VLELEGLSKSYGDK-----TLLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPDSGTVKL-GE------TV---- 378

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556496326  81 NIGYVIQ-QIGLFPNMTIEENItvvprmlgWDKARCKTRAeELMDMVAldphKFL------NRYPREMSGGQQQRIGVIR 153
Cdd:COG0488  379 KIGYFDQhQEELDPDKTVLDEL--------RDGAPGGTEQ-EVRGYLG----RFLfsgddaFKPVGVLSGGEKARLALAK 445

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556496326 154 ALAADPPVLLMDEPFGAVDPINREVIqNQFLEmqrKLKKTVMLVSHD---IDealKLGDRIAVFRQGKIV 220
Cdd:COG0488  446 LLLSPPNVLLLDEPTNHLDIETLEAL-EEALD---DFPGTVLLVSHDryfLD---RVATRILEFEDGGVR 508
rim_protein TIGR01257
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ...
 1-222 3.02e-18

retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim protein) in eukaryotes. It is the member of ABC transporter superfamily. Rim protein is a membrane glycoprotein which is localized in the photoreceptor outer segment discs. Mutation/s in its genetic loci is implicated in the recessive Stargardt's disease. [Transport and binding proteins, Other]


Pssm-ID: 130324 [Multi-domain]  Cd Length: 2272  Bit Score: 86.99  E-value: 3.02e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556496326     1 MIKLENLTKHFSqkhGQTFKAVDNVNLNVPEGEMCVLLGPSGCGKTTTLKMINRLITPSSGTILINGEdtSGMDTVT-LR 79
Cdd:TIGR01257 1937 ILRLNELTKVYS---GTSSPAVDRLCVGVRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAGK--SILTNISdVH 2011

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556496326    80 RNIGYVIQQIGLFPNMTIEENITVVPRMLGWDKARCKTRAEELMDMVALDphKFLNRYPREMSGGQQQRIGVIRALAADP 159
Cdd:TIGR01257 2012 QNMGYCPQFDAIDDLLTGREHLYLYARLRGVPAEEIEKVANWSIQSLGLS--LYADRLAGTYSGGNKRKLSTAIALIGCP 2089

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 556496326   160 PVLLMDEPFGAVDPINREVIQNQFLEMQRKlKKTVMLVSHDIDEALKLGDRIAVFRQGKIvQC 222
Cdd:TIGR01257 2090 PLVLLDEPTTGMDPQARRMLWNTIVSIIRE-GRAVVLTSHSMEECEALCTRLAIMVKGAF-QC 2150
ABC_RNaseL_inhibitor_domain2 cd03237
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ...
 31-249 1.18e-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: 81.69  E-value: 1.18e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556496326  31 EGEMCVLLGPSGCGKTTTLKMINRLITPSSGTILINGEDtsgmdtvtlrrnIGYVIQQIGLFPNMTIEENITVVPRMLGW 110
Cdd:cd03237   24 ESEVIGILGPNGIGKTTFIKMLAGVLKPDEGDIEIELDT------------VSYKPQYIKADYEGTVRDLLSSITKDFYT 91

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556496326 111 DkARCKTraeELMDMVALDPhkFLNRYPREMSGGQQQRIGVIRALAADPPVLLMDEPFGAVDPINR----EVIqNQFLEm 186
Cdd:cd03237   92 H-PYFKT---EIAKPLQIEQ--ILDREVPELSGGELQRVAIAACLSKDADIYLLDEPSAYLDVEQRlmasKVI-RRFAE- 163

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 556496326 187 qrKLKKTVMLVSHDIDEALKLGDRIAVFRQGKIVQC-ASPDELLAKPANEFVGSFvgqDRTLKR 249
Cdd:cd03237  164 --NNEKTAFVVEHDIIMIDYLADRLIVFEGEPSVNGvANPPQSLRSGMNRFLKNL---DITFRR 222
znuC PRK09544
high-affinity zinc transporter ATPase; Reviewed
 1-211 3.88e-17

high-affinity zinc transporter ATPase; Reviewed


Pssm-ID: 181939 [Multi-domain]  Cd Length: 251  Bit Score: 80.16  E-value: 3.88e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556496326   1 MIKLENLTKHFSQKhgqtfKAVDNVNLNVPEGEMCVLLGPSGCGKTTTLKMINRLITPSSGTILINGEdtsgmdtvtLRr 80
Cdd:PRK09544   4 LVSLENVSVSFGQR-----RVLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIKRNGK---------LR- 68

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556496326  81 nIGYVIQQIGLFPNMTIeenitVVPRMLgwdKARCKTRAEELMDMVALDPHKFLNRYP-REMSGGQQQRIGVIRALAADP 159
Cdd:PRK09544  69 -IGYVPQKLYLDTTLPL-----TVNRFL---RLRPGTKKEDILPALKRVQAGHLIDAPmQKLSGGETQRVLLARALLNRP 139

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 556496326 160 PVLLMDEPFGAVDPINREVIQNQFLEMQRKLKKTVMLVSHDI-------DEALKLGDRI 211
Cdd:PRK09544 140 QLLVLDEPTQGVDVNGQVALYDLIDQLRRELDCAVLMVSHDLhlvmaktDEVLCLNHHI 198
PRK13539 PRK13539
cytochrome c biogenesis protein CcmA; Provisional
 24-216 5.06e-17

cytochrome c biogenesis protein CcmA; Provisional


Pssm-ID: 237421 [Multi-domain]  Cd Length: 207  Bit Score: 78.76  E-value: 5.06e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556496326  24 NVNLNVPEGEMCVLLGPSGCGKTTTLKMINRLITPSSGTILINGEDTsgmDTVTLRRNIGYVIQQIGLFPNMTIEENITV 103
Cdd:PRK13539  20 GLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDGGDI---DDPDVAEACHYLGHRNAMKPALTVAENLEF 96

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556496326 104 VPRMLGWDkarcKTRAEELMDMVALDPhkFLNRYPREMSGGQQQRIGVIRALAADPPVLLMDEPFGAVDPINREVIQNqf 183
Cdd:PRK13539  97 WAAFLGGE----ELDIAAALEAVGLAP--LAHLPFGYLSAGQKRRVALARLLVSNRPIWILDEPTAALDAAAVALFAE-- 168

                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 556496326 184 lEMQRKLKK--TVMLVSH---DIDEALKLgdRIAVFRQ 216
Cdd:PRK13539 169 -LIRAHLAQggIVIAATHiplGLPGAREL--DLGPFAA 203
PTZ00265 PTZ00265
multidrug resistance protein (mdr1); Provisional
 59-230 6.75e-17

multidrug resistance protein (mdr1); Provisional


Pssm-ID: 240339 [Multi-domain]  Cd Length: 1466  Bit Score: 82.77  E-value: 6.75e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556496326   59 SSGTILINGEDTSGMDTVTLRRNIGYVIQQIGLFpNMTIEENITVVPRMLGWD--KARCKTRA-EELMDMValdPHKF-- 133
Cdd:PTZ00265 1275 NSGKILLDGVDICDYNLKDLRNLFSIVSQEPMLF-NMSIYENIKFGKEDATREdvKRACKFAAiDEFIESL---PNKYdt 1350

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556496326  134 -LNRYPREMSGGQQQRIGVIRALAADPPVLLMDEPFGAVDPINREVIQNQFLEMQRKLKKTVMLVSHDIdEALKLGDRIA 212
Cdd:PTZ00265 1351 nVGPYGKSLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDIKDKADKTIITIAHRI-ASIKRSDKIV 1429

                         170       180
                  ....*....|....*....|...
gi 556496326  213 VF----RQGKIVQC-ASPDELLA 230
Cdd:PTZ00265 1430 VFnnpdRTGSFVQAhGTHEELLS 1452
CBS_pair_SF cd02205
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains superfamily; The CBS ...
 262-363 1.23e-16

Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains superfamily; The CBS domain, named after human CBS, is a small domain originally identified in cystathionine beta-synthase and is subsequently found in a wide range of different proteins. CBS domains usually occur in tandem repeats. They associate to form a so-called Bateman domain or a CBS pair based on crystallographic studies in bacteria. The CBS pair was used as a basis for this cd hierarchy since the human CBS proteins can adopt the typical core structure and form an intramolecular CBS pair. The interface between the two CBS domains forms a cleft that is a potential ligand binding site. The CBS pair coexists with a variety of other functional domains and this has been used to help in its classification here. It has been proposed that the CBS domain may play a regulatory role, although its exact function is unknown. Mutations of conserved residues within this domain are associated with a variety of human hereditary diseases, including congenital myotonia, idiopathic generalized epilepsy, hypercalciuric nephrolithiasis, and classic Bartter syndrome (CLC chloride channel family members), Wolff-Parkinson-White syndrome (gamma 2 subunit of AMP-activated protein kinase), retinitis pigmentosa (IMP dehydrogenase-1), and homocystinuria (cystathionine beta-synthase).


Pssm-ID: 341358 [Multi-domain]  Cd Length: 113  Bit Score: 74.97  E-value: 1.23e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556496326 262 QPTITVRGSTPLPEAFATMDDNDIRAITVVDEHGKPLGFVKRREARNASG--------TCADILHPFRMTGKAEDNLRVV 333
Cdd:cd02205    2 RDVVTVDPDTTVREALELMAENGIGALPVVDDDGKLVGIVTERDILRALVegglaldtPVAEVMTPDVITVSPDTDLEEA 81

                         90       100       110
                 ....*....|....*....|....*....|
gi 556496326 334 LSRLYESNTSWMPIVDEDGRYNGEISQDYI 363
Cdd:cd02205   82 LELMLEHGIRRLPVVDDDGKLVGIVTRRDI 111
PRK13549 PRK13549
xylose transporter ATP-binding subunit; Provisional
 1-218 1.48e-16

xylose transporter ATP-binding subunit; Provisional


Pssm-ID: 184134 [Multi-domain]  Cd Length: 506  Bit Score: 81.13  E-value: 1.48e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556496326   1 MIKLENLTKHFSqkhgqTFKAVDNVNLNVPEGEMCVLLGPSGCGKTTTLKMINRlITPS---SGTILINGEdtsgmdtvT 77
Cdd:PRK13549   5 LLEMKNITKTFG-----GVKALDNVSLKVRAGEIVSLCGENGAGKSTLMKVLSG-VYPHgtyEGEIIFEGE--------E 70

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556496326  78 LR-RNI------GYVI--QQIGLFPNMTIEENI------TVVPRMlgwDKARCKTRAEELMDMVALDphkfLNRYPR--E 140
Cdd:PRK13549  71 LQaSNIrdteraGIAIihQELALVKELSVLENIflgneiTPGGIM---DYDAMYLRAQKLLAQLKLD----INPATPvgN 143

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556496326 141 MSGGQQQRIGVIRALAADPPVLLMDEPFGAVDPINREVIqnqfLEMQRKLKK---TVMLVSHDIDEALKLGDRIAVFRQG 217
Cdd:PRK13549 144 LGLGQQQLVEIAKALNKQARLLILDEPTASLTESETAVL----LDIIRDLKAhgiACIYISHKLNEVKAISDTICVIRDG 219


                 .
gi 556496326 218 K 218
Cdd:PRK13549 220 R 220
ABCC_NFT1 cd03369
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ...
 2-225 1.54e-16

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: 77.45  E-value: 1.54e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556496326   2 IKLENLTKHFSQkhgQTFKAVDNVNLNVPEGEMCVLLGPSGCGKTTTLKMINRLITPSSGTILINGEDTSGMDTVTLRRN 81
Cdd:cd03369    7 IEVENLSVRYAP---DLPPVLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDGIDISTIPLEDLRSS 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556496326  82 IGYVIQQIGLFPNmTIEENitvvprmlgwdkarcktraeelmdmvaLDPHkflNRYPRE--------------MSGGQQQ 147
Cdd:cd03369   84 LTIIPQDPTLFSG-TIRSN---------------------------LDPF---DEYSDEeiygalrvsegglnLSQGQRQ 132

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556496326 148 RIGVIRALAADPPVLLMDEPFGAVDPINREVIQnqflEMQRKL--KKTVMLVSHDIDEALKLgDRIAVFRQGKIVQCASP 225
Cdd:cd03369  133 LLCLARALLKRPRVLVLDEATASIDYATDALIQ----KTIREEftNSTILTIAHRLRTIIDY-DKILVMDAGEVKEYDHP 207
40850658_otr NF000106
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
2-231 1.68e-16

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


Pssm-ID: 411078 [Multi-domain]  Cd Length: 351  Bit Score: 79.78  E-value: 1.68e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556496326   2 IKLENLTKHFSQkhgqtFKAVDNVNLNVPEGEMCVLLGPSGCGKTttlkminRLITPSSgtilINGED---------TSG 72
Cdd:NF000106  14 VEVRGLVKHFGE-----VKAVDGVDLDVREGTVLGVLGP*GAA**-------RGALPAH----V*GPDagrrpwrf*TWC 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556496326  73 MDTVTLRRNIG-YVIQQIGLFPNMTIEENITVVPRMLGWDKARCKTRAEELMDMVALDphKFLNRYPREMSGGQQQRIGV 151
Cdd:NF000106  78 ANRRALRRTIG*HRPVR*GRRESFSGRENLYMIGR*LDLSRKDARARADELLERFSLT--EAAGRAAAKYSGGMRRRLDL 155

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556496326 152 IRALAADPPVLLMDEPFGAVDPINREVIQNQFLEMQRKlKKTVMLVSHDIDEALKLGDRIAVFRQGKIVQCASPDELLAK 231
Cdd:NF000106 156 AASMIGRPAVLYLDEPTTGLDPRTRNEVWDEVRSMVRD-GATVLLTTQYMEEAEQLAHELTVIDRGRVIADGKVDELKTK 234
PRK10522 PRK10522
multidrug transporter membrane component/ATP-binding component; Provisional
 2-219 2.26e-16

multidrug transporter membrane component/ATP-binding component; Provisional


Pssm-ID: 236707 [Multi-domain]  Cd Length: 547  Bit Score: 80.40  E-value: 2.26e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556496326   2 IKLENLTKHFsqkHGQTFkAVDNVNLNVPEGEMCVLLGPSGCGKTTTLKMINRLITPSSGTILINGEDTSGMDTVTLRRN 81
Cdd:PRK10522 323 LELRNVTFAY---QDNGF-SVGPINLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKPVTAEQPEDYRKL 398

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556496326  82 IGYVIQQIGLFPNMTIEENITVVPRMLGWDKARCKtraeeLMDMVALDPHKFLNrypREMSGGQQQRIGVIRALAADPPV 161
Cdd:PRK10522 399 FSAVFTDFHLFDQLLGPEGKPANPALVEKWLERLK-----MAHKLELEDGRISN---LKLSKGQKKRLALLLALAEERDI 470

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 556496326 162 LLMDEPFGAVDPINREVIQNQFLEMQRKLKKTVMLVSHDiDEALKLGDRIAVFRQGKI 219
Cdd:PRK10522 471 LLLDEWAADQDPHFRREFYQVLLPLLQEMGKTIFAISHD-DHYFIHADRLLEMRNGQL 527
PRK13540 PRK13540
cytochrome c biogenesis protein CcmA; Provisional
 22-199 2.51e-16

cytochrome c biogenesis protein CcmA; Provisional


Pssm-ID: 184127 [Multi-domain]  Cd Length: 200  Bit Score: 76.91  E-value: 2.51e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556496326  22 VDNVNLNVPEGEMCVLLGPSGCGKTTTLKMINRLITPSSGTILINGEDTSgMDTVTLRRNIGYVIQQIGLFPNMTIEENI 101
Cdd:PRK13540  17 LQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEILFERQSIK-KDLCTYQKQLCFVGHRSGINPYLTLRENC 95

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556496326 102 tvvprmlgWDKARCKTRAEELMDMVALDPHKFLNRYP-REMSGGQQQRIGVIRALAADPPVLLMDEPFGAVDPINREVIQ 180
Cdd:PRK13540  96 --------LYDIHFSPGAVGITELCRLFSLEHLIDYPcGLLSSGQKRQVALLRLWMSKAKLWLLDEPLVALDELSLLTII 167

                        170
                 ....*....|....*....
gi 556496326 181 NQfLEMQRKLKKTVMLVSH 199
Cdd:PRK13540 168 TK-IQEHRAKGGAVLLTSH 185
PRK15439 PRK15439
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
 2-219 2.62e-16

autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional


Pssm-ID: 185336 [Multi-domain]  Cd Length: 510  Bit Score: 80.09  E-value: 2.62e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556496326   2 IKLENLTkhfsqkhGQTFKavdNVNLNVPEGEMCVLLGPSGCGKTTTLKMINRLITPSSGTILINGEDTSGMDTVT-LRR 80
Cdd:PRK15439 269 LTVEDLT-------GEGFR---NISLEVRAGEILGLAGVVGAGRTELAETLYGLRPARGGRIMLNGKEINALSTAQrLAR 338

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556496326  81 NIGYVI---QQIGLFPNMTIEENIT--VVPRMLGW-DKARCKTRAEELMDMVALdphKF--LNRYPREMSGGQQQRIGVI 152
Cdd:PRK15439 339 GLVYLPedrQSSGLYLDAPLAWNVCalTHNRRGFWiKPARENAVLERYRRALNI---KFnhAEQAARTLSGGNQQKVLIA 415

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 556496326 153 RALAADPPVLLMDEPFGAVDPINREVIQnQFLEMQRKLKKTVMLVSHDIDEALKLGDRIAVFRQGKI 219
Cdd:PRK15439 416 KCLEASPQLLIVDEPTRGVDVSARNDIY-QLIRSIAAQNVAVLFISSDLEEIEQMADRVLVMHQGEI 481
PRK03695 PRK03695
vitamin B12-transporter ATPase; Provisional
 32-229 4.29e-16

vitamin B12-transporter ATPase; Provisional


Pssm-ID: 235150 [Multi-domain]  Cd Length: 248  Bit Score: 77.28  E-value: 4.29e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556496326  32 GEMCVLLGPSGCGKTTTLKMINRLiTPSSGTILINGEDTSGMDTVTLRRNIGYVIQQIGLFPNMTieenitvVPRML--- 108
Cdd:PRK03695  22 GEILHLVGPNGAGKSTLLARMAGL-LPGSGSIQFAGQPLEAWSAAELARHRAYLSQQQTPPFAMP-------VFQYLtlh 93

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556496326 109 ---GWDKARCKTRAEELMDMVALDPhkFLNRYPREMSGGQQQRI---GVI----RALAADPPVLLMDEPFGAVDpINREV 178
Cdd:PRK03695  94 qpdKTRTEAVASALNEVAEALGLDD--KLGRSVNQLSGGEWQRVrlaAVVlqvwPDINPAGQLLLLDEPMNSLD-VAQQA 170

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 556496326 179 IQNQFLEMQRKLKKTVMLVSHDIDEALKLGDRIAVFRQGKIVQCASPDELL 229
Cdd:PRK03695 171 ALDRLLSELCQQGIAVVMSSHDLNHTLRHADRVWLLKQGKLLASGRRDEVL 221
PvdE COG4615
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ...
 2-230 8.17e-16

ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion transport and metabolism];


Pssm-ID: 443659 [Multi-domain]  Cd Length: 547  Bit Score: 78.69  E-value: 8.17e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556496326   2 IKLENLTKHFSQKHGQTFKAVDNVNLNVPEGEMCVLLGPSGCGKTTTLKMINRLITPSSGTILINGEDTSGMDTVTLRRN 81
Cdd:COG4615  328 LELRGVTYRYPGEDGDEGFTLGPIDLTIRRGELVFIVGGNGSGKSTLAKLLTGLYRPESGEILLDGQPVTADNREAYRQL 407

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556496326  82 IGYVIQQIGLFPnmtieenitvvpRMLGWDKARCKTRAEELMDMVALDpHK-------FLNRyprEMSGGQQQRIGVIRA 154
Cdd:COG4615  408 FSAVFSDFHLFD------------RLLGLDGEADPARARELLERLELD-HKvsvedgrFSTT---DLSQGQRKRLALLVA 471

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 556496326 155 LAADPPVLLMDEpFGA-VDPINREVIQNQFLEMQRKLKKTVMLVSHDiDEALKLGDRIAVFRQGKIVQCASPDELLA 230
Cdd:COG4615  472 LLEDRPILVFDE-WAAdQDPEFRRVFYTELLPELKARGKTVIAISHD-DRYFDLADRVLKMDYGKLVELTGPAALAA 546
MK0520 COG2401
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ...
 2-221 1.20e-15

ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];


Pssm-ID: 441957 [Multi-domain]  Cd Length: 222  Bit Score: 75.38  E-value: 1.20e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556496326   2 IKLENLTKHFSQK------------------HGQTFKAVDNVNLNVPEGEMCVLLGPSGCGKTTTLKMINRLI--TPSSG 61
Cdd:COG2401    8 FVLMRVTKVYSSVldlservaivleafgvelRVVERYVLRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGALkgTPVAG 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556496326  62 TIlingedtsgmdtvtlrrnigyVIQQIGLFPNMTIEENItvvprmlgwDKARCKTRAEELMDMVAL-DPHKFLNRYpRE 140
Cdd:COG2401   88 CV---------------------DVPDNQFGREASLIDAI---------GRKGDFKDAVELLNAVGLsDAVLWLRRF-KE 136

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556496326 141 MSGGQQQRIGVIRALAADPPVLLMDEpFGAV-DPINREVIQNQFLEMQRKLKKTVMLVSH--DIDEALKlGDRIAVFRQG 217
Cdd:COG2401  137 LSTGQKFRFRLALLLAERPKLLVIDE-FCSHlDRQTAKRVARNLQKLARRAGITLVVATHhyDVIDDLQ-PDLLIFVGYG 214


                 ....
gi 556496326 218 KIVQ 221
Cdd:COG2401  215 GVPE 218
ABCG_PDR_domain1 cd03233
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ...
 11-220 1.42e-15

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: 74.61  E-value: 1.42e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556496326  11 FSQKHGQTFKAVDNVNLNVPEGEMCVLLGPSGCGKTTTLKMINRLITPS---SGTILINGEDTSGMDTvTLRRNIGYVIQ 87
Cdd:cd03233   12 TTGKGRSKIPILKDFSGVVKPGEMVLVLGRPGSGCSTLLKALANRTEGNvsvEGDIHYNGIPYKEFAE-KYPGEIIYVSE 90

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556496326  88 QIGLFPNMTIEENITVVPRMLGwdkarcktraeelmdmvaldphkflNRYPREMSGGQQQRIGVIRALAADPPVLLMDEP 167
Cdd:cd03233   91 EDVHFPTLTVRETLDFALRCKG-------------------------NEFVRGISGGERKRVSIAEALVSRASVLCWDNS 145

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 556496326 168 FGAVDPINREVIQNQFLEMQRKLKKTVML-VSHDIDEALKLGDRIAVFRQGKIV 220
Cdd:cd03233  146 TRGLDSSTALEILKCIRTMADVLKTTTFVsLYQASDEIYDLFDKVLVLYEGRQI 199
ABC_CcmA_heme_exporter cd03231
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ...
 25-172 3.91e-15

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: 73.30  E-value: 3.91e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556496326  25 VNLNVPEGEMCVLLGPSGCGKTTTLKMINRLITPSSGTILINGEDTsGMDTVTLRRNIGYVIQQIGLFPNMTIEENITvv 104
Cdd:cd03231   19 LSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNGGPL-DFQRDSIARGLLYLGHAPGIKTTLSVLENLR-- 95

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 556496326 105 prmlgWDKARCKTRA-EELMDMVALDphKFLNRYPREMSGGQQQRIGVIRALAADPPVLLMDEPFGAVD 172
Cdd:cd03231   96 -----FWHADHSDEQvEEALARVGLN--GFEDRPVAQLSAGQQRRVALARLLLSGRPLWILDEPTTALD 157
xylG TIGR02633
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ...
 1-220 5.83e-15

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: 76.02  E-value: 5.83e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556496326    1 MIKLENLTKHFSqkhgqTFKAVDNVNLNVPEGEMCVLLGPSGCGKTTTLKMINRlITPS---SGTILINGEDTSGMDTV- 76
Cdd:TIGR02633   1 LLEMKGIVKTFG-----GVKALDGIDLEVRPGECVGLCGENGAGKSTLMKILSG-VYPHgtwDGEIYWSGSPLKASNIRd 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556496326   77 TLRRNIGYVIQQIGLFPNMTIEENITV-------VPRMlgwDKARCKTRAEELMDMVALDPHKfLNRYPREMSGGQQQRI 149
Cdd:TIGR02633  75 TERAGIVIIHQELTLVPELSVAENIFLgneitlpGGRM---AYNAMYLRAKNLLRELQLDADN-VTRPVGDYGGGQQQLV 150

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 556496326  150 GVIRALAADPPVLLMDEPFGAVDPINREVIQNQFLEMQRKLKKTVMlVSHDIDEALKLGDRIAVFRQGKIV 220
Cdd:TIGR02633 151 EIAKALNKQARLLILDEPSSSLTEKETEILLDIIRDLKAHGVACVY-ISHKLNEVKAVCDTICVIRDGQHV 220
PRK10789 PRK10789
SmdA family multidrug ABC transporter permease/ATP-binding protein;
21-232 6.84e-15

SmdA family multidrug ABC transporter permease/ATP-binding protein;


Pssm-ID: 182732 [Multi-domain]  Cd Length: 569  Bit Score: 75.90  E-value: 6.84e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556496326  21 AVDNVNLNVPEGEMCVLLGPSGCGKTTTLKMINRLITPSSGTILINGEDTSGMDTVTLRRNIGYVIQQIGLFPNmTIEEN 100
Cdd:PRK10789 330 ALENVNFTLKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGDIRFHDIPLTKLQLDSWRSRLAVVSQTPFLFSD-TVANN 408

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556496326 101 ITvvprmLGwdkarCKTRAEELMDMVA--LDPHKFLNRYPR-----------EMSGGQQQRIGVIRALAADPPVLLMDEP 167
Cdd:PRK10789 409 IA-----LG-----RPDATQQEIEHVArlASVHDDILRLPQgydtevgergvMLSGGQKQRISIARALLLNAEILILDDA 478

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 556496326 168 FGAVD-PINREVIQNqfLEMQRKlKKTVMLVSHDIdEALKLGDRIAVFRQGKIVQCASPDELLAKP 232
Cdd:PRK10789 479 LSAVDgRTEHQILHN--LRQWGE-GRTVIISAHRL-SALTEASEILVMQHGHIAQRGNHDQLAQQS 540
ABCD_peroxisomal_ALDP cd03223
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ...
 2-199 1.20e-14

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: 71.03  E-value: 1.20e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556496326   2 IKLENLTkhFSQKHGQTFkaVDNVNLNVPEGEMCVLLGPSGCGKTTTLKMINRLITPSSGTILIngedtsgmdtvTLRRN 81
Cdd:cd03223    1 IELENLS--LATPDGRVL--LKDLSFEIKPGDRLLITGPSGTGKSSLFRALAGLWPWGSGRIGM-----------PEGED 65

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556496326  82 IGYVIQQiGLFPNMTIEENITvvprmlgwdkarcktraeelmdmvaldphkflnrYP--REMSGGQQQRIGVIRALAADP 159
Cdd:cd03223   66 LLFLPQR-PYLPLGTLREQLI----------------------------------YPwdDVLSGGEQQRLAFARLLLHKP 110

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|
gi 556496326 160 PVLLMDEPFGAVDPinrEViQNQFLEMQRKLKKTVMLVSH 199
Cdd:cd03223  111 KFVFLDEATSALDE---ES-EDRLYQLLKELGITVISVGH 146
YddA COG4178
ABC-type uncharacterized transport system, permease and ATPase components [General function ...
 1-199 2.09e-14

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


Pssm-ID: 443337 [Multi-domain]  Cd Length: 571  Bit Score: 74.46  E-value: 2.09e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556496326   1 MIKLENLTkhFSQKHGQTFkaVDNVNLNVPEGEMCVLLGPSGCGKTTTLKMINRLITPSSGTILI-NGEDT------SGM 73
Cdd:COG4178  362 ALALEDLT--LRTPDGRPL--LEDLSLSLKPGERLLITGPSGSGKSTLLRAIAGLWPYGSGRIARpAGARVlflpqrPYL 437

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556496326  74 DTVTLRRNIGYviqqiglfPNmtIEENITvvprmlgwdkarcKTRAEELMDMVALDphKFLNRY------PREMSGGQQQ 147
Cdd:COG4178  438 PLGTLREALLY--------PA--TAEAFS-------------DAELREALEAVGLG--HLAERLdeeadwDQVLSLGEQQ 492

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 556496326 148 RIGVIRALAADPPVLLMDEPFGAVDPINreviQNQFLEM-QRKLKK-TVMLVSH 199
Cdd:COG4178  493 RLAFARLLLHKPDWLFLDEATSALDEEN----EAALYQLlREELPGtTVISVGH 542
PTZ00265 PTZ00265
multidrug resistance protein (mdr1); Provisional
 2-199 2.95e-14

multidrug resistance protein (mdr1); Provisional


Pssm-ID: 240339 [Multi-domain]  Cd Length: 1466  Bit Score: 74.68  E-value: 2.95e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556496326    2 IKLENLTKHF-SQKHGQTFKavdNVNLNVPEGEMCVLLGPSGCGKTTTLKMINRLITPSSGTILINgeDTSGMDTVTL-- 78
Cdd:PTZ00265  383 IQFKNVRFHYdTRKDVEIYK---DLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIIIN--DSHNLKDINLkw 457

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556496326   79 -RRNIGYVIQQIGLFPNmTIEENITVVPRML-------------GWD-----------KARCK---------TRAEELM- 123
Cdd:PTZ00265  458 wRSKIGVVSQDPLLFSN-SIKNNIKYSLYSLkdlealsnyynedGNDsqenknkrnscRAKCAgdlndmsntTDSNELIe 536

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556496326  124 -----------DMVALDP----HKFLNRYP-----------REMSGGQQQRIGVIRALAADPPVLLMDEPFGAVDPINRE 177
Cdd:PTZ00265  537 mrknyqtikdsEVVDVSKkvliHDFVSALPdkyetlvgsnaSKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEY 616

                         250       260
                  ....*....|....*....|..
gi 556496326  178 VIQNQFLEMQRKLKKTVMLVSH 199
Cdd:PTZ00265  617 LVQKTINNLKGNENRITIIIAH 638
GguA NF040905
sugar ABC transporter ATP-binding protein;
18-221 3.47e-14

sugar ABC transporter ATP-binding protein;


Pssm-ID: 468840 [Multi-domain]  Cd Length: 500  Bit Score: 73.67  E-value: 3.47e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556496326  18 TF---KAVDNVNLNVPEGEMCVLLGPSGCGKTTTLKMINRlITPS---SGTILINGEdtsgmdtVTLRRNI------GYV 85
Cdd:NF040905  10 TFpgvKALDDVNLSVREGEIHALCGENGAGKSTLMKVLSG-VYPHgsyEGEILFDGE-------VCRFKDIrdsealGIV 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556496326  86 I--QQIGLFPNMTIEENItvvprMLG----------WDKARckTRAEELMDMVALDPHkflnryPREMSG----GQQQRI 149
Cdd:NF040905  82 IihQELALIPYLSIAENI-----FLGnerakrgvidWNETN--RRARELLAKVGLDES------PDTLVTdigvGKQQLV 148

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 556496326 150 GVIRALAADPPVLLMDEPFGAvdpINREVIQNqFLEMQRKLKK---TVMLVSHDIDEALKLGDRIAVFRQGKIVQ 221
Cdd:NF040905 149 EIAKALSKDVKLLILDEPTAA---LNEEDSAA-LLDLLLELKAqgiTSIIISHKLNEIRRVADSITVLRDGRTIE 219
PRK10762 PRK10762
D-ribose transporter ATP binding protein; Provisional
 1-223 5.70e-14

D-ribose transporter ATP binding protein; Provisional


Pssm-ID: 236755 [Multi-domain]  Cd Length: 501  Bit Score: 73.11  E-value: 5.70e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556496326   1 MIKLENLTKHFSqkhgqTFKAVDNVNLNVPEGEMCVLLGPSGCGKTTTLKMINRLITPSSGTILINGEDTS--------- 71
Cdd:PRK10762   4 LLQLKGIDKAFP-----GVKALSGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSILYLGKEVTfngpkssqe 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556496326  72 -GmdtvtlrrnIGYVIQQIGLFPNMTIEENI----TVVPRMLGWDKARCKTRAEELMDMVAL--DPHKFLNryprEMSGG 144
Cdd:PRK10762  79 aG---------IGIIHQELNLIPQLTIAENIflgrEFVNRFGRIDWKKMYAEADKLLARLNLrfSSDKLVG----ELSIG 145

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556496326 145 QQQRIGVIRALAADPPVLLMDEPFGAVDPINRE----VIqnqflemqRKLKKT---VMLVSHDIDEALKLGDRIAVFRQG 217
Cdd:PRK10762 146 EQQMVEIAKVLSFESKVIIMDEPTDALTDTETEslfrVI--------RELKSQgrgIVYISHRLKEIFEICDDVTVFRDG 217


                 ....*..
gi 556496326 218 K-IVQCA 223
Cdd:PRK10762 218 QfIAERE 224
MRP_assoc_pro TIGR00957
multi drug resistance-associated protein (MRP); This model describes multi drug ...
 2-231 6.05e-14

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: 73.83  E-value: 6.05e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556496326     2 IKLENLTKHFSQKHGQTFKAVDnvnLNVPEGEMCVLLGPSGCGKTTTLKminrlitpssgTILINGEDTSGmdTVTLRRN 81
Cdd:TIGR00957  637 ITVHNATFTWARDLPPTLNGIT---FSIPEGALVAVVGQVGCGKSSLLS-----------ALLAEMDKVEG--HVHMKGS 700

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556496326    82 IGYVIQQiGLFPNMTIEENItvvprMLGwdKARCKTRAEELMDMVALDPHkfLNRYPR-----------EMSGGQQQRIG 150
Cdd:TIGR00957  701 VAYVPQQ-AWIQNDSLRENI-----LFG--KALNEKYYQQVLEACALLPD--LEILPSgdrteigekgvNLSGGQKQRVS 770

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556496326   151 VIRALAADPPVLLMDEPFGAVDP-INREVIQNQFLEMQRKLKKTVMLVSHDIdEALKLGDRIAVFRQGKIVQCASPDELL 229
Cdd:TIGR00957  771 LARAVYSNADIYLFDDPLSAVDAhVGKHIFEHVIGPEGVLKNKTRILVTHGI-SYLPQVDVIIVMSGGKISEMGSYQELL 849


                   ..
gi 556496326   230 AK 231
Cdd:TIGR00957  850 QR 851
hmuV PRK13547
heme ABC transporter ATP-binding protein;
1-233 9.33e-14

heme ABC transporter ATP-binding protein;


Pssm-ID: 184132 [Multi-domain]  Cd Length: 272  Bit Score: 70.63  E-value: 9.33e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556496326   1 MIKLENLtkHFSQKHGqtfKAVDNVNLNVPEGEMCVLLGPSGCGKTTTLKMINRLITPS--------SGTILINGEDTSG 72
Cdd:PRK13547   1 MLTADHL--HVARRHR---AILRDLSLRIEPGRVTALLGRNGAGKSTLLKALAGDLTGGgaprgarvTGDVTLNGEPLAA 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556496326  73 MDTVTLRRNIGYVIQQ--------------IGLFPNMTIEENITVVPRMLGWdkarcktRAEELMDMVALDphkflNRYP 138
Cdd:PRK13547  76 IDAPRLARLRAVLPQAaqpafafsareivlLGRYPHARRAGALTHRDGEIAW-------QALALAGATALV-----GRDV 143

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556496326 139 REMSGGQQQRIGVIRALA---------ADPPVLLMDEPFGAVDPINreviQNQFLEMQRKLKKT----VMLVSHDIDEAL 205
Cdd:PRK13547 144 TTLSGGELARVQFARVLAqlwpphdaaQPPRYLLLDEPTAALDLAH----QHRLLDTVRRLARDwnlgVLAIVHDPNLAA 219

                        250       260
                 ....*....|....*....|....*...
gi 556496326 206 KLGDRIAVFRQGKIVQCASPDELLaKPA 233
Cdd:PRK13547 220 RHADRIAMLADGAIVAHGAPADVL-TPA 246
ABCC_CFTR1 cd03291
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ...
 24-217 1.10e-13

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: 70.66  E-value: 1.10e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556496326  24 NVNLNVPEGEMCVLLGPSGCGKTTTLKMINRLITPSSGTILINGEdtsgmdtvtlrrnIGYVIQQIGLFPNmTIEENITV 103
Cdd:cd03291   55 NINLKIEKGEMLAITGSTGSGKTSLLMLILGELEPSEGKIKHSGR-------------ISFSSQFSWIMPG-TIKENIIF 120

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556496326 104 vprMLGWDKARCKT--RAEELMDMVALDPHK---FLNRYPREMSGGQQQRIGVIRALAADPPVLLMDEPFGAVDPINREV 178
Cdd:cd03291  121 ---GVSYDEYRYKSvvKACQLEEDITKFPEKdntVLGEGGITLSGGQRARISLARAVYKDADLYLLDSPFGYLDVFTEKE 197

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 556496326 179 IqnqFLEMQRKL--KKTVMLVSHDIdEALKLGDRIAVFRQG 217
Cdd:cd03291  198 I---FESCVCKLmaNKTRILVTSKM-EHLKKADKILILHEG 234
BtuD COG4138
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ...
 22-234 1.13e-13

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


Pssm-ID: 443313 [Multi-domain]  Cd Length: 248  Bit Score: 70.25  E-value: 1.13e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556496326  22 VDNVNLNVPEGEMCVLLGPSGCGKTTTLKMINRLiTPSSGTILINGEDTSGMDTVTLRRNIGYVIQQIGLFPNMTIEENI 101
Cdd:COG4138   12 LGPISAQVNAGELIHLIGPNGAGKSTLLARMAGL-LPGQGEILLNGRPLSDWSAAELARHRAYLSQQQSPPFAMPVFQYL 90

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556496326 102 TV-VPRMLgwDKARCKTRAEELMDMVALDPhkFLNRYPREMSGGQQQRIGVIRAL-----AADPP--VLLMDEPFGAVDp 173
Cdd:COG4138   91 ALhQPAGA--SSEAVEQLLAQLAEALGLED--KLSRPLTQLSGGEWQRVRLAAVLlqvwpTINPEgqLLLLDEPMNSLD- 165

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 556496326 174 INREVIQNQFLEMQRKLKKTVMLVSHDIDEALKLGDRIAVFRQGKIVQCASPDELLaKPAN 234
Cdd:COG4138  166 VAQQAALDRLLRELCQQGITVVMSSHDLNHTLRHADRVWLLKQGKLVASGETAEVM-TPEN 225
3a01204 TIGR00955
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ...
 31-229 1.63e-13

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


Pssm-ID: 273361 [Multi-domain]  Cd Length: 617  Bit Score: 72.00  E-value: 1.63e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556496326   31 EGEMCVLLGPSGCGKTTTLKMINRLITPS---SGTILINGEDtsgMDTVTLRRNIGYVIQQIGLFPNMTIEENITV---- 103
Cdd:TIGR00955  50 PGELLAVMGSSGAGKTTLMNALAFRSPKGvkgSGSVLLNGMP---IDAKEMRAISAYVQQDDLFIPTLTVREHLMFqahl 126

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556496326  104 -VPRMLGWDKARckTRAEELMDMVAL-----------DPHKFLnrypremSGGQQQRIGVIRALAADPPVLLMDEPFGAV 171
Cdd:TIGR00955 127 rMPRRVTKKEKR--ERVDEVLQALGLrkcantrigvpGRVKGL-------SGGERKRLAFASELLTDPPLLFCDEPTSGL 197

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 556496326  172 DPIN-REVIQnQFLEMQRKLKKTVMLVSHDIDEALKLGDRIAVFRQGKIVQCASPDELL 229
Cdd:TIGR00955 198 DSFMaYSVVQ-VLKGLAQKGKTIICTIHQPSSELFELFDKIILMAEGRVAYLGSPDQAV 255
oppD PRK09473
oligopeptide transporter ATP-binding component; Provisional
 21-233 1.87e-13

oligopeptide transporter ATP-binding component; Provisional


Pssm-ID: 181888 [Multi-domain]  Cd Length: 330  Bit Score: 70.52  E-value: 1.87e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556496326  21 AVDNVNLNVPEGEMCVLLGPSGCGKTTTLKMINRLITPS---SGTILINGEDTSGMDTVTLRR----NIGYVIQQ--IGL 91
Cdd:PRK09473  31 AVNDLNFSLRAGETLGIVGESGSGKSQTAFALMGLLAANgriGGSATFNGREILNLPEKELNKlraeQISMIFQDpmTSL 110

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556496326  92 FPNMTIEENITVVpRML--GWDKARCKTRAEELMDMVAL-DPHKFLNRYPREMSGGQQQRIGVIRALAADPPVLLMDEPF 168
Cdd:PRK09473 111 NPYMRVGEQLMEV-LMLhkGMSKAEAFEESVRMLDAVKMpEARKRMKMYPHEFSGGMRQRVMIAMALLCRPKLLIADEPT 189

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 556496326 169 GAVDPinreVIQNQFLEMQRKLKK----TVMLVSHDIDEALKLGDRIAVFRQGKIVQCASPDELLAKPA 233
Cdd:PRK09473 190 TALDV----TVQAQIMTLLNELKRefntAIIMITHDLGVVAGICDKVLVMYAGRTMEYGNARDVFYQPS 254
PRK15056 PRK15056
manganese/iron ABC transporter ATP-binding protein;
14-201 2.10e-13

manganese/iron ABC transporter ATP-binding protein;


Pssm-ID: 185016 [Multi-domain]  Cd Length: 272  Bit Score: 69.91  E-value: 2.10e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556496326  14 KHGQTfkAVDNVNLNVPEGEMCVLLGPSGCGKTTTLKMINRLITPSSGTILINGEDTSGmdtvTLRRN-IGYVIQQIGL- 91
Cdd:PRK15056  17 RNGHT--ALRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKISILGQPTRQ----ALQKNlVAYVPQSEEVd 90

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556496326  92 --FPNMTieENITVVPRM--LGWDKaRCKTRAEELMD--MVALDPHKFLNRYPREMSGGQQQRIGVIRALAADPPVLLMD 165
Cdd:PRK15056  91 wsFPVLV--EDVVMMGRYghMGWLR-RAKKRDRQIVTaaLARVDMVEFRHRQIGELSGGQKKRVFLARAIAQQGQVILLD 167

                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 556496326 166 EPFGAVDpINREVIQNQFLEMQRKLKKTVMLVSHDI 201
Cdd:PRK15056 168 EPFTGVD-VKTEARIISLLRELRDEGKTMLVSTHNL 202
PRK13546 PRK13546
teichoic acids export ABC transporter ATP-binding subunit TagH;
2-240 5.04e-13

teichoic acids export ABC transporter ATP-binding subunit TagH;


Pssm-ID: 184131 [Multi-domain]  Cd Length: 264  Bit Score: 68.30  E-value: 5.04e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556496326   2 IKLENLTKHFS---------------QKHGQTFKAVDNVNLNVPEGEMCVLLGPSGCGKTTTLKMINRLITPSSGTILIN 66
Cdd:PRK13546   5 VNIKNVTKEYRiyrtnkermkdalipKHKNKTFFALDDISLKAYEGDVIGLVGINGSGKSTLSNIIGGSLSPTVGKVDRN 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556496326  67 GEdtsgmdtvtlrrnIGYVIQQIGLFPNMTIEENITVVPRMLGWDKARCKTRAEELMDMVALDphKFLNRYPREMSGGQQ 146
Cdd:PRK13546  85 GE-------------VSVIAISAGLSGQLTGIENIEFKMLCMGFKRKEIKAMTPKIIEFSELG--EFIYQPVKKYSSGMR 149

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556496326 147 QRIGVIRALAADPPVLLMDEPFGAVDPINREVIQNQFLEMQRKlKKTVMLVSHDIDEALKLGDRIAVFRQGKIVQCASPD 226
Cdd:PRK13546 150 AKLGFSINITVNPDILVIDEALSVGDQTFAQKCLDKIYEFKEQ-NKTIFFVSHNLGQVRQFCTKIAWIEGGKLKDYGELD 228

                        250
                 ....*....|....
gi 556496326 227 ELLAKpANEFVGSF 240
Cdd:PRK13546 229 DVLPK-YEAFLNDF 241
PRK10762 PRK10762
D-ribose transporter ATP binding protein; Provisional
 3-219 1.51e-12

D-ribose transporter ATP binding protein; Provisional


Pssm-ID: 236755 [Multi-domain]  Cd Length: 501  Bit Score: 68.49  E-value: 1.51e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556496326   3 KLENLTKHFSQKHGQ--------TFKAVDNVNLNVPEGEMCVLLGPSGCGKTTTLKMINRLITPSSGTILINGED---TS 71
Cdd:PRK10762 241 KLEDQYPRLDKAPGEvrlkvdnlSGPGVNDVSFTLRKGEILGVSGLMGAGRTELMKVLYGALPRTSGYVTLDGHEvvtRS 320

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556496326  72 GMDTvtLRRNIGYVIQQI---GLFPNMTIEENITVVP-RMLGWDKARCKTRAEELM--DMVALdphkFLNRYP------R 139
Cdd:PRK10762 321 PQDG--LANGIVYISEDRkrdGLVLGMSVKENMSLTAlRYFSRAGGSLKHADEQQAvsDFIRL----FNIKTPsmeqaiG 394

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556496326 140 EMSGGQQQRIGVIRALAADPPVLLMDEPFGAVD-PINREVIQ--NQFlemqRKLKKTVMLVSHDIDEALKLGDRIAVFRQ 216
Cdd:PRK10762 395 LLSGGNQQKVAIARGLMTRPKVLILDEPTRGVDvGAKKEIYQliNQF----KAEGLSIILVSSEMPEVLGMSDRILVMHE 470


                 ...
gi 556496326 217 GKI 219
Cdd:PRK10762 471 GRI 473
tagH PRK13545
teichoic acids export protein ATP-binding subunit; Provisional
 3-203 1.63e-12

teichoic acids export protein ATP-binding subunit; Provisional


Pssm-ID: 184130 [Multi-domain]  Cd Length: 549  Bit Score: 68.76  E-value: 1.63e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556496326   3 KLENLtkHFSQKHGQTFKAVDNVNLNVPEGEMCVLLGPSGCGKTTTLKMINRLITPSSGTILINGEDTsgmdtvtlrrni 82
Cdd:PRK13545  23 KLKDL--FFRSKDGEYHYALNNISFEVPEGEIVGIIGLNGSGKSTLSNLIAGVTMPNKGTVDIKGSAA------------ 88

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556496326  83 gYVIQQIGLFPNMTIEENITVVPRMLGWDKARCKTRAEELMDMValDPHKFLNRYPREMSGGQQQRIGVIRALAADPPVL 162
Cdd:PRK13545  89 -LIAISSGLNGQLTGIENIELKGLMMGLTKEKIKEIIPEIIEFA--DIGKFIYQPVKTYSSGMKSRLGFAISVHINPDIL 165

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....
gi 556496326 163 LMDEPFGAVDpinrEVIQNQFLEMQRKLK---KTVMLVSHDIDE 203
Cdd:PRK13545 166 VIDEALSVGD----QTFTKKCLDKMNEFKeqgKTIFFISHSLSQ 205
SufC COG0396
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, ...
 23-221 2.04e-12

Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 440165 [Multi-domain]  Cd Length: 245  Bit Score: 66.24  E-value: 2.04e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556496326  23 DNVNLNVPEGEMCVLLGPSGCGKTTTLKMI--NRLITPSSGTILINGEDTSGMDtVTLR--RNIGYVIQQIGLFPNMTIE 98
Cdd:COG0396   17 KGVNLTIKPGEVHAIMGPNGSGKSTLAKVLmgHPKYEVTSGSILLDGEDILELS-PDERarAGIFLAFQYPVEIPGVSVS 95

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556496326  99 E------NITVVPRMlgwDKARCKTRAEELMDMVALDPhKFLNRYPRE-MSGGQQQRIGVIRALAADPPVLLMDEP---- 167
Cdd:COG0396   96 NflrtalNARRGEEL---SAREFLKLLKEKMKELGLDE-DFLDRYVNEgFSGGEKKRNEILQMLLLEPKLAILDETdsgl 171

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 556496326 168 ----FGAVdpinREVIqNQFlemqRKLKKTVMLVSH-----DIDEAlklgDRIAVFRQGKIVQ 221
Cdd:COG0396  172 didaLRIV----AEGV-NKL----RSPDRGILIITHyqrilDYIKP----DFVHVLVDGRIVK 221
PRK10790 PRK10790
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
2-231 2.92e-12

SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;


Pssm-ID: 182733 [Multi-domain]  Cd Length: 592  Bit Score: 67.82  E-value: 2.92e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556496326   2 IKLENLTkhFSQKHGQtfKAVDNVNLNVPEGEMCVLLGPSGCGKTTTLKMINRLITPSSGTILINGEDTSGMDTVTLRRN 81
Cdd:PRK10790 341 IDIDNVS--FAYRDDN--LVLQNINLSVPSRGFVALVGHTGSGKSTLASLLMGYYPLTEGEIRLDGRPLSSLSHSVLRQG 416

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556496326  82 IGYVIQQI-----GLFPNMTIEENIT--VVPRMLgwdkarcktRAEELMDMVALDP---HKFLNRYPREMSGGQQQRIGV 151
Cdd:PRK10790 417 VAMVQQDPvvladTFLANVTLGRDISeeQVWQAL---------ETVQLAELARSLPdglYTPLGEQGNNLSVGQKQLLAL 487

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556496326 152 IRALAADPPVLLMDEPFGAVDPINREVIQnQFLEMQRKlKKTVMLVSH---DIDEAlklgDRIAVFRQGKIVQCASPDEL 228
Cdd:PRK10790 488 ARVLVQTPQILILDEATANIDSGTEQAIQ-QALAAVRE-HTTLVVIAHrlsTIVEA----DTILVLHRGQAVEQGTHQQL 561


                 ...
gi 556496326 229 LAK 231
Cdd:PRK10790 562 LAA 564
CFTR_protein TIGR01271
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ...
 24-217 2.97e-12

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: 68.40  E-value: 2.97e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556496326    24 NVNLNVPEGEMCVLLGPSGCGKTTTLKMINRLITPSSGTILINGEdtsgmdtvtlrrnIGYVIQQIGLFPNmTIEENITV 103
Cdd:TIGR01271  444 NISFKLEKGQLLAVAGSTGSGKSSLLMMIMGELEPSEGKIKHSGR-------------ISFSPQTSWIMPG-TIKDNIIF 509

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556496326   104 vprMLGWDKARCKT--RAEELMDMVALDPHK---FLNRYPREMSGGQQQRIGVIRALAADPPVLLMDEPFGAVDPINREV 178
Cdd:TIGR01271  510 ---GLSYDEYRYTSviKACQLEEDIALFPEKdktVLGEGGITLSGGQRARISLARAVYKDADLYLLDSPFTHLDVVTEKE 586

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|.
gi 556496326   179 IqnqFLEMQRKL--KKTVMLVSHDIdEALKLGDRIAVFRQG 217
Cdd:TIGR01271  587 I---FESCLCKLmsNKTRILVTSKL-EHLKKADKILLLHEG 623
PRK13538 PRK13538
cytochrome c biogenesis heme-transporting ATPase CcmA;
23-172 6.30e-12

cytochrome c biogenesis heme-transporting ATPase CcmA;


Pssm-ID: 184125 [Multi-domain]  Cd Length: 204  Bit Score: 64.05  E-value: 6.30e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556496326  23 DNVNLNVPEGEMCVLLGPSGCGKTTTLKMINRLITPSSGTILINGEDTSGMDTvTLRRNIGYVIQQIGLFPNMTIEENIT 102
Cdd:PRK13538  18 SGLSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVLWQGEPIRRQRD-EYHQDLLYLGHQPGIKTELTALENLR 96

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 556496326 103 VVPRMLGwdkarcKTRAEELMDmvALDphKF-LNRY---P-REMSGGQQQRIGVIRALAADPPVLLMDEPFGAVD 172
Cdd:PRK13538  97 FYQRLHG------PGDDEALWE--ALA--QVgLAGFedvPvRQLSAGQQRRVALARLWLTRAPLWILDEPFTAID 161
COG3448 COG3448
CBS-domain-containing membrane protein [Signal transduction mechanisms];
265-367 6.66e-12

CBS-domain-containing membrane protein [Signal transduction mechanisms];


Pssm-ID: 442671 [Multi-domain]  Cd Length: 136  Bit Score: 62.58  E-value: 6.66e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556496326 265 ITVRGSTPLPEAFATMDDNDIRAITVVDEHGKPLGFVKRREARNASG--------------TCADILHPFRMTGKAEDNL 330
Cdd:COG3448   13 VTVSPDTTLREALELMREHGIRGLPVVDEDGRLVGIVTERDLLRALLpdrldeleerlldlPVEDVMTRPVVTVTPDTPL 92

                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 556496326 331 RVVLSRLYESNTSWMPIVDEDGRYNGEISQDYIAEYL 367
Cdd:COG3448   93 EEAAELMLEHGIHRLPVVDDDGRLVGIVTRTDLLRAL 129
PRK13543 PRK13543
heme ABC exporter ATP-binding protein CcmA;
15-173 1.75e-11

heme ABC exporter ATP-binding protein CcmA;


Pssm-ID: 184129 [Multi-domain]  Cd Length: 214  Bit Score: 62.94  E-value: 1.75e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556496326  15 HGQTFKAVDN-----VNLNVPEGEMCVLLGPSGCGKTTTLKMINRLITPSSGTILINGEDTSGMDTVtlrRNIGYVIQQI 89
Cdd:PRK13543  15 HALAFSRNEEpvfgpLDFHVDAGEALLVQGDNGAGKTTLLRVLAGLLHVESGQIQIDGKTATRGDRS---RFMAYLGHLP 91

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556496326  90 GLFPNMTIEENITVVPRMLGWDKARCKTRAeelMDMVALDPHKflNRYPREMSGGQQQRIGVIRALAADPPVLLMDEPFG 169
Cdd:PRK13543  92 GLKADLSTLENLHFLCGLHGRRAKQMPGSA---LAIVGLAGYE--DTLVRQLSAGQKKRLALARLWLSPAPLWLLDEPYA 166


                 ....
gi 556496326 170 AVDP 173
Cdd:PRK13543 167 NLDL 170
PLN03232 PLN03232
ABC transporter C family member; Provisional
 2-228 2.02e-11

ABC transporter C family member; Provisional


Pssm-ID: 215640 [Multi-domain]  Cd Length: 1495  Bit Score: 65.77  E-value: 2.02e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556496326    2 IKLENltKHFSQKHGQTFKAVDNVNLNVPEGEMCVLLGPSGCGKTTtlkminrLITPSSGTiLINGEDTSgmdtVTLRRN 81
Cdd:PLN03232  615 ISIKN--GYFSWDSKTSKPTLSDINLEIPVGSLVAIVGGTGEGKTS-------LISAMLGE-LSHAETSS----VVIRGS 680

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556496326   82 IGYVIQQIGLFpNMTIEENItvvprMLGWDKArcKTRAEELMDMVAL--DPHKFLNRYPREM-------SGGQQQRIGVI 152
Cdd:PLN03232  681 VAYVPQVSWIF-NATVRENI-----LFGSDFE--SERYWRAIDVTALqhDLDLLPGRDLTEIgergvniSGGQKQRVSMA 752

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 556496326  153 RALAADPPVLLMDEPFGAVDP-INREVIQNQfleMQRKLK-KTVMLVSHDIdEALKLGDRIAVFRQGKIVQCASPDEL 228
Cdd:PLN03232  753 RAVYSNSDIYIFDDPLSALDAhVAHQVFDSC---MKDELKgKTRVLVTNQL-HFLPLMDRIILVSEGMIKEEGTFAEL 826
CBS COG0517
CBS domain [Signal transduction mechanisms];
253-367 3.60e-11

CBS domain [Signal transduction mechanisms];


Pssm-ID: 440283 [Multi-domain]  Cd Length: 128  Bit Score: 60.26  E-value: 3.60e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556496326 253 VSAGDVTDQQPtITVRGSTPLPEAFATMDDNDIRAITVVDEHGKPLGFVKRREARNA---------SGTCADILHPFRMT 323
Cdd:COG0517    1 MKVKDIMTTDV-VTVSPDATVREALELMSEKRIGGLPVVDEDGKLVGIVTDRDLRRAlaaegkdllDTPVSEVMTRPPVT 79

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 556496326 324 GKAEDNLRVVLSRLYESNTSWMPIVDEDGRYNGEISQDYIAEYL 367
Cdd:COG0517   80 VSPDTSLEEAAELMEEHKIRRLPVVDDDGRLVGIITIKDLLKAL 123
PRK10982 PRK10982
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
 20-220 3.75e-11

galactose/methyl galaxtoside transporter ATP-binding protein; Provisional


Pssm-ID: 182880 [Multi-domain]  Cd Length: 491  Bit Score: 64.37  E-value: 3.75e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556496326  20 KAVDNVNLNVPEGEMCVLLGPSGCGKTTTLKMINRLITPSSGTILINGEDTSGMDTV-TLRRNIGYVIQQIGLFPNMTIE 98
Cdd:PRK10982  12 KALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEIDFKSSKeALENGISMVHQELNLVLQRSVM 91

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556496326  99 ENITV--VPR---MLGWDKARCKTRA--EELMdmVALDPHKFLNryprEMSGGQQQRIGVIRALAADPPVLLMDEPFGAV 171
Cdd:PRK10982  92 DNMWLgrYPTkgmFVDQDKMYRDTKAifDELD--IDIDPRAKVA----TLSVSQMQMIEIAKAFSYNAKIVIMDEPTSSL 165

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 556496326 172 DpiNREViqNQFLEMQRKLKKT---VMLVSHDIDEALKLGDRIAVFRQGKIV 220
Cdd:PRK10982 166 T--EKEV--NHLFTIIRKLKERgcgIVYISHKMEEIFQLCDEITILRDGQWI 213
ABCG_PDR_domain2 cd03232
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ...
 16-167 4.16e-11

Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding cassette transporters; The pleiotropic drug resistance (PDR) is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. This PDR subfamily represents domain I of its (ABC-IM)2 organization. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds including sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.


Pssm-ID: 213199 [Multi-domain]  Cd Length: 192  Bit Score: 61.49  E-value: 4.16e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556496326  16 GQTFKAVDNVNLNVPEGEMCVLLGPSGCGKTTTLKMI-NRLITPS-SGTILINGEDTsgmdTVTLRRNIGYVIQQIGLFP 93
Cdd:cd03232   17 GGKRQLLNNISGYVKPGTLTALMGESGAGKTTLLDVLaGRKTAGViTGEILINGRPL----DKNFQRSTGYVEQQDVHSP 92

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 556496326  94 NMTIEEnitvvprmlgwdkarcktraeelmdmvALDPHKFLnrypREMSGGQQQR--IGVirALAADPPVLLMDEP 167
Cdd:cd03232   93 NLTVRE---------------------------ALRFSALL----RGLSVEQRKRltIGV--ELAAKPSILFLDEP 135
PLN03211 PLN03211
ABC transporter G-25; Provisional
 32-172 4.28e-11

ABC transporter G-25; Provisional


Pssm-ID: 215634 [Multi-domain]  Cd Length: 659  Bit Score: 64.52  E-value: 4.28e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556496326  32 GEMCVLLGPSGCGKTTTLKMINRLITPSS--GTILINGedtsGMDTVTLRRNIGYVIQQIGLFPNMTIEENITVV----- 104
Cdd:PLN03211  94 GEILAVLGPSGSGKSTLLNALAGRIQGNNftGTILANN----RKPTKQILKRTGFVTQDDILYPHLTVRETLVFCsllrl 169

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 556496326 105 PRMLGWDKarcKTR-AEELMDMVALDPHK---FLNRYPREMSGGQQQRIGVIRALAADPPVLLMDEPFGAVD 172
Cdd:PLN03211 170 PKSLTKQE---KILvAESVISELGLTKCEntiIGNSFIRGISGGERKRVSIAHEMLINPSLLILDEPTSGLD 238
PLN03232 PLN03232
ABC transporter C family member; Provisional
 15-236 7.21e-11

ABC transporter C family member; Provisional


Pssm-ID: 215640 [Multi-domain]  Cd Length: 1495  Bit Score: 64.23  E-value: 7.21e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556496326   15 HGQTFKavdnvnlnVPEGEMCVLLGPSGCGKTTTLKMINRLITPSSGTILINGEDTSGMDTVTLRRNIGYVIQQIGLFPN 94
Cdd:PLN03232 1253 HGLSFF--------VSPSEKVGVVGRTGAGKSSMLNALFRIVELEKGRIMIDDCDVAKFGLTDLRRVLSIIPQSPVLFSG 1324

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556496326   95 mTIEENITVVPRMLGWDKARCKTRAeELMDMVALDPHKF---LNRYPREMSGGQQQRIGVIRALAADPPVLLMDEPFGAV 171
Cdd:PLN03232 1325 -TVRFNIDPFSEHNDADLWEALERA-HIKDVIDRNPFGLdaeVSEGGENFSVGQRQLLSLARALLRRSKILVLDEATASV 1402

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 556496326  172 DPINREVIQNQFLEMQRKLkkTVMLVSHDIDEALKLgDRIAVFRQGKIVQCASPDELLAKPANEF 236
Cdd:PLN03232 1403 DVRTDSLIQRTIREEFKSC--TMLVIAHRLNTIIDC-DKILVLSSGQVLEYDSPQELLSRDTSAF 1464
ABC_FeS_Assembly cd03217
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ...
 22-229 7.39e-11

ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of iron-sulfur clusters (Fe-S) depends on multi-protein systems. The SUF system of E. coli and Erwinia chrysanthemi is important for Fe-S biogenesis under stressful conditions. The SUF system is made of six proteins: SufC is an atypical cytoplasmic ABC-ATPase, which forms a complex with SufB and SufD; SufA plays the role of a scaffold protein for assembly of iron-sulfur clusters and delivery to target proteins; SufS is a cysteine desulfurase which mobilizes the sulfur atom from cysteine and provides it to the cluster; SufE has no associated function yet.


Pssm-ID: 213184 [Multi-domain]  Cd Length: 200  Bit Score: 61.00  E-value: 7.39e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556496326  22 VDNVNLNVPEGEMCVLLGPSGCGKTTTLKMI--NRLITPSSGTILINGEDTSGMdTVTLRRNIGyviqqIGLFPNMTIEe 99
Cdd:cd03217   16 LKGVNLTIKKGEVHALMGPNGSGKSTLAKTImgHPKYEVTEGEILFKGEDITDL-PPEERARLG-----IFLAFQYPPE- 88

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556496326 100 nitvvprmlgwdkarcktraeelMDMVALDphKFLnRYPRE-MSGGQQQRIGVIRALAADPPVLLMDEPFGAVDPINREV 178
Cdd:cd03217   89 -----------------------IPGVKNA--DFL-RYVNEgFSGGEKKRNEILQLLLLEPDLAILDEPDSGLDIDALRL 142

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 556496326 179 IQNQFLEMqRKLKKTVMLVSH--DIDEALKlGDRIAVFRQGKIVqCASPDELL 229
Cdd:cd03217  143 VAEVINKL-REEGKSVLIITHyqRLLDYIK-PDRVHVLYDGRIV-KSGDKELA 192
PTZ00243 PTZ00243
ABC transporter; Provisional
 24-220 8.55e-11

ABC transporter; Provisional


Pssm-ID: 240327 [Multi-domain]  Cd Length: 1560  Bit Score: 63.64  E-value: 8.55e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556496326   24 NVNLNVPEGEMCVLLGPSGCGKTTTLkminrlitpssGTILINGEDTSGmdTVTLRRNIGYVIQQIGLFpNMTIEENItv 103
Cdd:PTZ00243  678 DVSVSVPRGKLTVVLGATGSGKSTLL-----------QSLLSQFEISEG--RVWAERSIAYVPQQAWIM-NATVRGNI-- 741

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556496326  104 vprmLGWDkarcKTRAEELMDMV---------ALDP--------HKFLNrypreMSGGQQQRIGVIRALAADPPVLLMDE 166
Cdd:PTZ00243  742 ----LFFD----EEDAARLADAVrvsqleadlAQLGggleteigEKGVN-----LSGGQKARVSLARAVYANRDVYLLDD 808

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 556496326  167 PFGAVDP-INREVIQNQFLemQRKLKKTVMLVSHDIdEALKLGDRIAVFRQGKIV 220
Cdd:PTZ00243  809 PLSALDAhVGERVVEECFL--GALAGKTRVLATHQV-HVVPRADYVVALGDGRVE 860
PLN03130 PLN03130
ABC transporter C family member; Provisional
 24-230 1.79e-10

ABC transporter C family member; Provisional


Pssm-ID: 215595 [Multi-domain]  Cd Length: 1622  Bit Score: 62.83  E-value: 1.79e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556496326   24 NVNLNVPEGEMCVLLGPSGCGKTTTLK-MINRLITPSSGTILINGedtsgmdtvtlrrNIGYVIQQIGLFpNMTIEENIt 102
Cdd:PLN03130  635 NINLDVPVGSLVAIVGSTGEGKTSLISaMLGELPPRSDASVVIRG-------------TVAYVPQVSWIF-NATVRDNI- 699

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556496326  103 vvprMLGWDKARckTRAEELMDMVALdpHKFLNRYPR-----------EMSGGQQQRIGVIRALAADPPVLLMDEPFGAV 171
Cdd:PLN03130  700 ----LFGSPFDP--ERYERAIDVTAL--QHDLDLLPGgdlteigergvNISGGQKQRVSMARAVYSNSDVYIFDDPLSAL 771

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 556496326  172 DP-INREVIQNQFLEMQRklKKTVMLVSHDIdEALKLGDRIAVFRQGKIVQCASPDELLA 230
Cdd:PLN03130  772 DAhVGRQVFDKCIKDELR--GKTRVLVTNQL-HFLSQVDRIILVHEGMIKEEGTYEELSN 828
araG PRK11288
L-arabinose ABC transporter ATP-binding protein AraG;
25-235 2.78e-10

L-arabinose ABC transporter ATP-binding protein AraG;


Pssm-ID: 183077 [Multi-domain]  Cd Length: 501  Bit Score: 61.47  E-value: 2.78e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556496326  25 VNLNVPEGEMCVLLGPSGCGKTTTLKMINRLITPSSGTILINGEdtsgmdTVTLRRNIGYVIQQI----------GLFPN 94
Cdd:PRK11288 272 ISFSVRAGEIVGLFGLVGAGRSELMKLLYGATRRTAGQVYLDGK------PIDIRSPRDAIRAGImlcpedrkaeGIIPV 345

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556496326  95 MTIEENITVVPR-------ML---GWDKA---------RCKTR-AEELMdmvaldphkflnrypREMSGGQQQRIGVIRA 154
Cdd:PRK11288 346 HSVADNINISARrhhlragCLinnRWEAEnadrfirslNIKTPsREQLI---------------MNLSGGNQQKAILGRW 410

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556496326 155 LAADPPVLLMDEPFGAVDPINREVIQNQFLEMQRKlKKTVMLVSHDIDEALKLGDRIAVFRQGKIVqcaspDELLAKPAN 234
Cdd:PRK11288 411 LSEDMKVILLDEPTRGIDVGAKHEIYNVIYELAAQ-GVAVLFVSSDLPEVLGVADRIVVMREGRIA-----GELAREQAT 484


                 .
gi 556496326 235 E 235
Cdd:PRK11288 485 E 485
PRK13409 PRK13409
ribosome biogenesis/translation initiation ATPase RLI;
31-214 3.98e-10

ribosome biogenesis/translation initiation ATPase RLI;


Pssm-ID: 184037 [Multi-domain]  Cd Length: 590  Bit Score: 61.36  E-value: 3.98e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556496326  31 EGEMCVLLGPSGCGKTTTLKMINRLITPSSGTILIngedtsgmdtvTLRrnIGYVIQQIGLFPNMTIEENITVVPRMLG- 109
Cdd:PRK13409 364 EGEVIGIVGPNGIGKTTFAKLLAGVLKPDEGEVDP-----------ELK--ISYKPQYIKPDYDGTVEDLLRSITDDLGs 430

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556496326 110 -WDKarcktraEELMDMVALdpHKFLNRYPREMSGGQQQRIGVIRALAADPPVLLMDEPFGAVDPINR----EVIQNqfl 184
Cdd:PRK13409 431 sYYK-------SEIIKPLQL--ERLLDKNVKDLSGGELQRVAIAACLSRDADLYLLDEPSAHLDVEQRlavaKAIRR--- 498

                        170       180       190
                 ....*....|....*....|....*....|...
gi 556496326 185 eMQRKLKKTVMLVSHDI---DealKLGDRIAVF 214
Cdd:PRK13409 499 -IAEEREATALVVDHDIymiD---YISDRLMVF 527
AAA smart00382
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ...
 32-216 6.57e-10

ATPases associated with a variety of cellular activities; AAA - ATPases associated with a variety of cellular activities. This profile/alignment only detects a fraction of this vast family. The poorly conserved N-terminal helix is missing from the alignment.


Pssm-ID: 214640 [Multi-domain]  Cd Length: 148  Bit Score: 57.00  E-value: 6.57e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556496326    32 GEMCVLLGPSGCGKTTTLKMINRLITPSSGT-ILINGEDTSGMDTVTLRrnigyviqqiglfpnmtieenitvvprmlgw 110
Cdd:smart00382   2 GEVILIVGPPGSGKTTLARALARELGPPGGGvIYIDGEDILEEVLDQLL------------------------------- 50

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556496326   111 dkarcktraeelmdmvaldpHKFLNRYPREMSGGQQQRIGVIRALAADPPVLLMDEPFGAVDPINREVIQ-----NQFLE 185
Cdd:smart00382  51 --------------------LIIVGGKKASGSGELRLRLALALARKLKPDVLILDEITSLLDAEQEALLLlleelRLLLL 110

                          170       180       190
                   ....*....|....*....|....*....|.
gi 556496326   186 MQRKLKKTVMLVSHDIDEALKLGDRIAVFRQ 216
Cdd:smart00382 111 LKSEKNLTVILTTNDEKDLGPALLRRRFDRR 141
PLN03130 PLN03130
ABC transporter C family member; Provisional
 37-238 9.57e-10

ABC transporter C family member; Provisional


Pssm-ID: 215595 [Multi-domain]  Cd Length: 1622  Bit Score: 60.52  E-value: 9.57e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556496326   37 LLGPSGCGKTTTLKMINRLITPSSGTILINGEDTSGMDTVTLRRNIGYVIQQIGLFPNmTIEENITVVPRMLGWDKARCK 116
Cdd:PLN03130 1270 IVGRTGAGKSSMLNALFRIVELERGRILIDGCDISKFGLMDLRKVLGIIPQAPVLFSG-TVRFNLDPFNEHNDADLWESL 1348

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556496326  117 TRAEeLMDMVALDPhKFLNRYPRE----MSGGQQQRIGVIRALAADPPVLLMDEPFGAVDPINREVIQNQFLEmqrKLKK 192
Cdd:PLN03130 1349 ERAH-LKDVIRRNS-LGLDAEVSEagenFSVGQRQLLSLARALLRRSKILVLDEATAAVDVRTDALIQKTIRE---EFKS 1423

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 556496326  193 TVMLV-SHDIDEALKLgDRIAVFRQGKIVQCASPDELLAKPANEFVG 238
Cdd:PLN03130 1424 CTMLIiAHRLNTIIDC-DRILVLDAGRVVEFDTPENLLSNEGSAFSK 1469
ABCC_SUR2 cd03288
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The ...
 2-245 1.27e-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: 58.38  E-value: 1.27e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556496326   2 IKLENLTKHFSQKHGQTFKavdNVNLNVPEGEMCVLLGPSGCGKTTTLKMINRLITPSSGTILINGEDTSGMDTVTLRRN 81
Cdd:cd03288   20 IKIHDLCVRYENNLKPVLK---HVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVIDGIDISKLPLHTLRSR 96

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556496326  82 IGYVIQQIGLFPNmTIEENITvvPRMLGWDKARCKT-RAEELMDMVALDP---HKFLNRYPREMSGGQQQRIGVIRALAA 157
Cdd:cd03288   97 LSIILQDPILFSG-SIRFNLD--PECKCTDDRLWEAlEIAQLKNMVKSLPgglDAVVTEGGENFSVGQRQLFCLARAFVR 173

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556496326 158 DPPVLLMDEPFGAVDPINREVIQNqfLEMQRKLKKTVMLVSHDIDEALKlGDRIAVFRQGKIVQCASPDELLAKPANEFv 237
Cdd:cd03288  174 KSSILIMDEATASIDMATENILQK--VVMTAFADRTVVTIAHRVSTILD-ADLVLVLSRGILVECDTPENLLAQEDGVF- 249


                 ....*...
gi 556496326 238 GSFVGQDR 245
Cdd:cd03288  250 ASLVRTDK 257
PRK10938 PRK10938
putative molybdenum transport ATP-binding protein ModF; Provisional
 23-204 1.38e-09

putative molybdenum transport ATP-binding protein ModF; Provisional


Pssm-ID: 182852 [Multi-domain]  Cd Length: 490  Bit Score: 59.64  E-value: 1.38e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556496326  23 DNVNLNVPEGEMCVLLGPSGCGKTTTLKminrLIT---P---SSGTILINGEDTSGMDTVTLRRNIGYVIQQI------- 89
Cdd:PRK10938 277 HNLSWQVNPGEHWQIVGPNGAGKSTLLS----LITgdhPqgySNDLTLFGRRRGSGETIWDIKKHIGYVSSSLhldyrvs 352

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556496326  90 ---------GLFPNMTIEENITVVPRMLgwdkarcktrAEELMDMVALDphKFLNRYP-REMSGGQQQRIGVIRALAADP 159
Cdd:PRK10938 353 tsvrnvilsGFFDSIGIYQAVSDRQQKL----------AQQWLDILGID--KRTADAPfHSLSWGQQRLALIVRALVKHP 420

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*.
gi 556496326 160 PVLLMDEPFGAVDPINREVIQnQFLEMQRKLKKTVML-VSHDIDEA 204
Cdd:PRK10938 421 TLLILDEPLQGLDPLNRQLVR-RFVDVLISEGETQLLfVSHHAEDA 465
ABC_ABC_ChvD TIGR03719
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ...
 2-167 2.53e-09

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: 58.79  E-value: 2.53e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556496326    2 IKLENLTKHFSQKhgqtfKAVDNVNLNVPEGEMCVLLGPSGCGKTTTLKMINRLITPSSGTILINgedtsgmDTVTLrrn 81
Cdd:TIGR03719 323 IEAENLTKAFGDK-----LLIDDLSFKLPPGGIVGVIGPNGAGKSTLFRMITGQEQPDSGTIEIG-------ETVKL--- 387

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556496326   82 iGYVIQQ-IGLFPNMTIEENITVVPRMLGWDKARCKTRAeelmdMVAL------DPHKFLNryprEMSGGQQQRIGVIRA 154
Cdd:TIGR03719 388 -AYVDQSrDALDPNKTVWEEISGGLDIIKLGKREIPSRA-----YVGRfnfkgsDQQKKVG----QLSGGERNRVHLAKT 457

                         170
                  ....*....|...
gi 556496326  155 LAADPPVLLMDEP 167
Cdd:TIGR03719 458 LKSGGNVLLLDEP 470
Rli1 COG1245
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ...
 31-214 2.93e-09

Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ribosomal structure and biogenesis];


Pssm-ID: 440858 [Multi-domain]  Cd Length: 592  Bit Score: 58.64  E-value: 2.93e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556496326  31 EGEMCVLLGPSGCGKTTTLKMINRLITPSSGTIlingedtsgmdTVTLRrnIGYVIQQIGLFPNMTIEENI-TVVPRMLG 109
Cdd:COG1245  365 EGEVLGIVGPNGIGKTTFAKILAGVLKPDEGEV-----------DEDLK--ISYKPQYISPDYDGTVEEFLrSANTDDFG 431

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556496326 110 --WDKarcktraEELMDMVALdpHKFLNRYPREMSGGQQQRIGVIRALAADPPVLLMDEPFGAVDPINR----EVIQNqf 183
Cdd:COG1245  432 ssYYK-------TEIIKPLGL--EKLLDKNVKDLSGGELQRVAIAACLSRDADLYLLDEPSAHLDVEQRlavaKAIRR-- 500

                        170       180       190
                 ....*....|....*....|....*....|....
gi 556496326 184 leMQRKLKKTVMLVSHDI---DealKLGDRIAVF 214
Cdd:COG1245  501 --FAENRGKTAMVVDHDIyliD---YISDRLMVF 529
PRK13549 PRK13549
xylose transporter ATP-binding subunit; Provisional
 20-219 5.85e-09

xylose transporter ATP-binding subunit; Provisional


Pssm-ID: 184134 [Multi-domain]  Cd Length: 506  Bit Score: 57.63  E-value: 5.85e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556496326  20 KAVDNVNLNVPEGEMCVLLGPSGCGKTTTLKMI-----NRlitpSSGTILINGEDtsgmdtVTLRR-------NIGYVIQ 87
Cdd:PRK13549 276 KRVDDVSFSLRRGEILGIAGLVGAGRTELVQCLfgaypGR----WEGEIFIDGKP------VKIRNpqqaiaqGIAMVPE 345

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556496326  88 ---QIGLFPNMTIEENIT--VVPRMLGW---DKARCKTRAEELMDMVALD-PHKFLnRYPReMSGGQQQRIGVIRALAAD 158
Cdd:PRK13549 346 drkRDGIVPVMGVGKNITlaALDRFTGGsriDDAAELKTILESIQRLKVKtASPEL-AIAR-LSGGNQQKAVLAKCLLLN 423

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 556496326 159 PPVLLMDEPFGAVD-----PINRevIQNQFLEMQrklkKTVMLVSHDIDEALKLGDRIAVFRQGKI 219
Cdd:PRK13549 424 PKILILDEPTRGIDvgakyEIYK--LINQLVQQG----VAIIVISSELPEVLGLSDRVLVMHEGKL 483
CBS_pair_bact_arch cd17775
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains present in bacteria ...
 262-367 7.51e-09

Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains present in bacteria and archaea; The CBS domain, named after human CBS, is a small domain originally identified in cystathionine beta-synthase and is subsequently found in a wide range of different proteins. CBS domains usually occur in tandem repeats. They associate to form a so-called Bateman domain or a CBS pair based on crystallographic studies in bacteria. The CBS pair was used as a basis for this cd hierarchy since the human CBS proteins can adopt the typical core structure and form an intramolecular CBS pair. The interface between the two CBS domains forms a cleft that is a potential ligand binding site. The CBS pair coexists with a variety of other functional domains and this has been used to help in its classification here. It has been proposed that the CBS domain may play a regulatory role, although its exact function is unknown. Mutations of conserved residues within this domain are associated with a variety of human hereditary diseases, including congenital myotonia, idiopathic generalized epilepsy, hypercalciuric nephrolithiasis, and classic Bartter syndrome (CLC chloride channel family members), Wolff-Parkinson-White syndrome (gamma 2 subunit of AMP-activated protein kinase), retinitis pigmentosa (IMP dehydrogenase-1), and homocystinuria (cystathionine beta-synthase).


Pssm-ID: 341411 [Multi-domain]  Cd Length: 117  Bit Score: 53.31  E-value: 7.51e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556496326 262 QPTITVRGSTPLPEAFATMDDNDIRAITVVDEHGKPLGFVKRRE------ARN---ASGTCADILHPFRMTGKAEDNLRV 332
Cdd:cd17775    3 REVVTASPDTSVLEAARLMRDHHVGSVVVVEEDGKPVGIVTDRDivvevvAKGldpKDVTVGDIMSADLITAREDDGLFE 82

                         90       100       110
                 ....*....|....*....|....*....|....*
gi 556496326 333 VLSRLYESNTSWMPIVDEDGRYNGEISQDYIAEYL 367
Cdd:cd17775   83 ALERMREKGVRRLPVVDDDGELVGIVTLDDILELL 117
PRK13541 PRK13541
cytochrome c biogenesis protein CcmA; Provisional
 39-199 1.04e-08

cytochrome c biogenesis protein CcmA; Provisional


Pssm-ID: 184128 [Multi-domain]  Cd Length: 195  Bit Score: 54.49  E-value: 1.04e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556496326  39 GPSGCGKTTTLKMINRLITPSSGTILINGEDTSGMDTVTLrrniGYVIQQIGLFPNMTIEENITVvprmlgWdkarcktr 118
Cdd:PRK13541  33 GANGCGKSSLLRMIAGIMQPSSGNIYYKNCNINNIAKPYC----TYIGHNLGLKLEMTVFENLKF------W-------- 94

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556496326 119 aEELMDMVALDP--------HKFLNRYPREMSGGQQQRIGVIRALAADPPVLLMDEPFGAVDPINREVIQNqFLEMQRKL 190
Cdd:PRK13541  95 -SEIYNSAETLYaaihyfklHDLLDEKCYSLSSGMQKIVAIARLIACQSDLWLLDEVETNLSKENRDLLNN-LIVMKANS 172


                 ....*....
gi 556496326 191 KKTVMLVSH 199
Cdd:PRK13541 173 GGIVLLSSH 181
PRK15064 PRK15064
ABC transporter ATP-binding protein; Provisional
 4-220 1.71e-08

ABC transporter ATP-binding protein; Provisional


Pssm-ID: 237894 [Multi-domain]  Cd Length: 530  Bit Score: 56.05  E-value: 1.71e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556496326   4 LENLTKHFSQkhGQTFKavdNVNLNVPEGEMCVLLGPSGCGKTTTLKMINRLITPSSGTIlingedtsgmdTVTLRRNIG 83
Cdd:PRK15064 322 VENLTKGFDN--GPLFK---NLNLLLEAGERLAIIGENGVGKTTLLRTLVGELEPDSGTV-----------KWSENANIG 385

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556496326  84 YVIQ--------QIGLFPNM----TIEENITVVPRMLGwdkaRCKTRAEElmdmvaldphkfLNRYPREMSGGQQQRIGV 151
Cdd:PRK15064 386 YYAQdhaydfenDLTLFDWMsqwrQEGDDEQAVRGTLG----RLLFSQDD------------IKKSVKVLSGGEKGRMLF 449

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 556496326 152 IRALAADPPVLLMDEPFGAVDpinREVIQ--NQFLEmqrKLKKTVMLVSHDIDEALKLGDRIAVFRQGKIV 220
Cdd:PRK15064 450 GKLMMQKPNVLVMDEPTNHMD---MESIEslNMALE---KYEGTLIFVSHDREFVSSLATRIIEITPDGVV 514
ABC_RNaseL_inhibitor cd03222
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ...
 29-240 1.98e-08

ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI's are not transport proteins, and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLI's have an N-terminal Fe-S domain and two nucleotide-binding domains, which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.


Pssm-ID: 213189 [Multi-domain]  Cd Length: 177  Bit Score: 53.34  E-value: 1.98e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556496326  29 VPEGEMCVLLGPSGCGKTTTLKMInrlitpsSGTILINGEDTSgmdtvtlrrnigyviqqiglfpnmtieenitvvprml 108
Cdd:cd03222   22 VKEGEVIGIVGPNGTGKTTAVKIL-------AGQLIPNGDNDE------------------------------------- 57

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556496326 109 gWDKARcktraeelmdmVALDPHKFlnryprEMSGGQQQRIGVIRALAADPPVLLMDEPFGAVDPINREVIQNQFLEMQR 188
Cdd:cd03222   58 -WDGIT-----------PVYKPQYI------DLSGGELQRVAIAAALLRNATFYLFDEPSAYLDIEQRLNAARAIRRLSE 119

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 556496326 189 KLKKTVMLVSHDIDEALKLGDRIAVFR-QGKIVQCASPDELLAKPANEFVGSF 240
Cdd:cd03222  120 EGKKTALVVEHDLAVLDYLSDRIHVFEgEPGVYGIASQPKGTREGINRFLRGY 172
xylG TIGR02633
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ...
 20-219 2.06e-08

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: 55.99  E-value: 2.06e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556496326   20 KAVDNVNLNVPEGEMCVLLGPSGCGKTTTLKMI-NRLITPSSGTILINGEDtsgMDTVTLRRNIGYVIQQI-------GL 91
Cdd:TIGR02633 274 KRVDDVSFSLRRGEILGVAGLVGAGRTELVQALfGAYPGKFEGNVFINGKP---VDIRNPAQAIRAGIAMVpedrkrhGI 350

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556496326   92 FPNMTIEENITVVPRMLGWDKARCKTRAEELMDMVALDPHKFLNRYP----REMSGGQQQRIGVIRALAADPPVLLMDEP 167
Cdd:TIGR02633 351 VPILGVGKNITLSVLKSFCFKMRIDAAAELQIIGSAIQRLKVKTASPflpiGRLSGGNQQKAVLAKMLLTNPRVLILDEP 430

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 556496326  168 FGAVD-PINREVIQNQFLEMQRKLkkTVMLVSHDIDEALKLGDRIAVFRQGKI 219
Cdd:TIGR02633 431 TRGVDvGAKYEIYKLINQLAQEGV--AIIVVSSELAEVLGLSDRVLVIGEGKL 481
3a01205 TIGR00956
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
 7-245 3.67e-08

Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]


Pssm-ID: 273362 [Multi-domain]  Cd Length: 1394  Bit Score: 55.50  E-value: 3.67e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556496326     7 LTKHFSQKHGQTFKAVDNVNLNVPEGEMCVLLGPSGCGKTTTLKMINRLITPS----SGTILINGEDTSGMDTvTLRRNI 82
Cdd:TIGR00956   62 FRKLKKFRDTKTFDILKPMDGLIKPGELTVVLGRPGSGCSTLLKTIASNTDGFhigvEGVITYDGITPEEIKK-HYRGDV 140

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556496326    83 GYVIQQIGLFPNMTIEENITVVprmlgwdkARCKT------------RAEELMDMVA----LDpH----KFLNRYPREMS 142
Cdd:TIGR00956  141 VYNAETDVHFPHLTVGETLDFA--------ARCKTpqnrpdgvsreeYAKHIADVYMatygLS-HtrntKVGNDFVRGVS 211

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556496326   143 GGQQQRIGVIRALAADPPVLLMDEpfgavdpINREVIQNQFLEMQRKLK------KTVMLVS--HDIDEALKLGDRIAVF 214
Cdd:TIGR00956  212 GGERKRVSIAEASLGGAKIQCWDN-------ATRGLDSATALEFIRALKtsanilDTTPLVAiyQCSQDAYELFDKVIVL 284

                          250       260       270
                   ....*....|....*....|....*....|.
gi 556496326   215 RQGKIVQCASPDEllAKPANEFVGsFVGQDR 245
Cdd:TIGR00956  285 YEGYQIYFGPADK--AKQYFEKMG-FKCPDR 312
CBS_pair_arch cd09836
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains; The CBS domain, ...
 263-368 3.92e-08

Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains; The CBS domain, named after human CBS, is a small domain originally identified in cystathionine beta-synthase and is subsequently found in a wide range of different proteins. CBS domains usually occur in tandem repeats. They associate to form a so-called Bateman domain or a CBS pair based on crystallographic studies in bacteria. The CBS pair was used as a basis for this cd hierarchy since the human CBS proteins can adopt the typical core structure and form an intramolecular CBS pair. The interface between the two CBS domains forms a cleft that is a potential ligand binding site. The CBS pair coexists with a variety of other functional domains and this has been used to help in its classification here. It has been proposed that the CBS domain may play a regulatory role, although its exact function is unknown. Mutations of conserved residues within this domain are associated with a variety of human hereditary diseases, including congenital myotonia, idiopathic generalized epilepsy, hypercalciuric nephrolithiasis, and classic Bartter syndrome (CLC chloride channel family members), Wolff-Parkinson-White syndrome (gamma 2 subunit of AMP-activated protein kinase), retinitis pigmentosa (IMP dehydrogenase-1), and homocystinuria (cystathionine beta-synthase).


Pssm-ID: 341405 [Multi-domain]  Cd Length: 116  Bit Score: 50.98  E-value: 3.92e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556496326 263 PTITVRGSTPLPEAFATMDDNDIRAITVVDEHGKPLGFVKRREARNASGTCADILHPFR--MTG-----KAEDNLRVVLS 335
Cdd:cd09836    4 PVVTVPPETTIREAAKLMAENNIGSVVVVDDDGKPVGIVTERDIVRAVAEGIDLDTPVEeiMTKnlvtvSPDESIYEAAE 83

                         90       100       110
                 ....*....|....*....|....*....|...
gi 556496326 336 RLYESNTSWMPIVDEDGRYNGEISQDYIAEYLS 368
Cdd:cd09836   84 LMREHNIRHLPVVDGGGKLVGVISIRDLARELS 116
COG2524 COG2524
Predicted transcriptional regulator, contains C-terminal CBS domains [Transcription];
241-367 5.20e-08

Predicted transcriptional regulator, contains C-terminal CBS domains [Transcription];


Pssm-ID: 442013 [Multi-domain]  Cd Length: 206  Bit Score: 52.96  E-value: 5.20e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556496326 241 VGQDRTLKRLLLVSAGDVTDQQPtITVRGSTPLPEAFATMDDNDIRAITVVDEhGKPLGFVKRREARNA--------SGT 312
Cdd:COG2524   74 VVAEKELGLVLKMKVKDIMTKDV-ITVSPDTTLEEALELMLEKGISGLPVVDD-GKLVGIITERDLLKAlaegrdllDAP 151

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 556496326 313 CADILHPFRMTGKAEDNLRVVLSRLYESNTSWMPIVDEDGRYNGEISQDYIAEYL 367
Cdd:COG2524  152 VSDIMTRDVVTVSEDDSLEEALRLMLEHGIGRLPVVDDDGKLVGIITRTDILRAL 206
CFTR_protein TIGR01271
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ...
 9-206 1.25e-07

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: 53.76  E-value: 1.25e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556496326     9 KHFSQKHGQTFKAV-DNVNLNVPEGEMCVLLGPSGCGKTTTLKMINRLITpSSGTILINGEDTSGMDTVTLRRNIGYVIQ 87
Cdd:TIGR01271 1221 QGLTAKYTEAGRAVlQDLSFSVEGGQRVGLLGRTGSGKSTLLSALLRLLS-TEGEIQIDGVSWNSVTLQTWRKAFGVIPQ 1299

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556496326    88 QIGLFPNmTIEENITVVPRmlgWDKARCKTRAEE--LMDMVALDPHKF---LNRYPREMSGGQQQRIGVIRALAADPPVL 162
Cdd:TIGR01271 1300 KVFIFSG-TFRKNLDPYEQ---WSDEEIWKVAEEvgLKSVIEQFPDKLdfvLVDGGYVLSNGHKQLMCLARSILSKAKIL 1375

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*....
gi 556496326   163 LMDEPFGAVDPINREVIqnqflemQRKLKK-----TVMLVSHDIDEALK 206
Cdd:TIGR01271 1376 LLDEPSAHLDPVTLQII-------RKTLKQsfsncTVILSEHRVEALLE 1417
PRK11819 PRK11819
putative ABC transporter ATP-binding protein; Reviewed
 2-101 1.62e-07

putative ABC transporter ATP-binding protein; Reviewed


Pssm-ID: 236992 [Multi-domain]  Cd Length: 556  Bit Score: 53.20  E-value: 1.62e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556496326   2 IKLENLTKHFSQKhgqtfKAVDNVNLNVPEGEMCVLLGPSGCGKTTTLKMINRLITPSSGTILInGEdtsgmdTVTLrrn 81
Cdd:PRK11819 325 IEAENLSKSFGDR-----LLIDDLSFSLPPGGIVGIIGPNGAGKSTLFKMITGQEQPDSGTIKI-GE------TVKL--- 389

                         90       100
                 ....*....|....*....|.
gi 556496326  82 iGYVIQQ-IGLFPNMTIEENI 101
Cdd:PRK11819 390 -AYVDQSrDALDPNKTVWEEI 409
PRK11147 PRK11147
ABC transporter ATPase component; Reviewed
 23-220 1.86e-07

ABC transporter ATPase component; Reviewed


Pssm-ID: 236861 [Multi-domain]  Cd Length: 635  Bit Score: 53.03  E-value: 1.86e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556496326  23 DNVNLNVPEGEMCVLLGPSGCGKTTTLKMINRLITPSSGTILINGedtsgmDTVTLR------RNIG-----YV---IQQ 88
Cdd:PRK11147  20 DNAELHIEDNERVCLVGRNGAGKSTLMKILNGEVLLDDGRIIYEQ------DLIVARlqqdppRNVEgtvydFVaegIEE 93

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556496326  89 IG-----------LFPNMTIEENITVVPRML-------GWdkaRCKTRAEELMDMVALDPHKFLNryprEMSGGQQQRIG 150
Cdd:PRK11147  94 QAeylkryhdishLVETDPSEKNLNELAKLQeqldhhnLW---QLENRINEVLAQLGLDPDAALS----SLSGGWLRKAA 166

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 556496326 151 VIRALAADPPVLLMDEPFGAVDPinrEVIQ--NQFLemqRKLKKTVMLVSHDIDEALKLGDRIAVFRQGKIV 220
Cdd:PRK11147 167 LGRALVSNPDVLLLDEPTNHLDI---ETIEwlEGFL---KTFQGSIIFISHDRSFIRNMATRIVDLDRGKLV 232
COG2905 COG2905
Signal-transduction protein containing cAMP-binding, CBS, and nucleotidyltransferase domains ...
 265-369 2.62e-07

Signal-transduction protein containing cAMP-binding, CBS, and nucleotidyltransferase domains [Signal transduction mechanisms];


Pssm-ID: 442149 [Multi-domain]  Cd Length: 124  Bit Score: 49.06  E-value: 2.62e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556496326 265 ITVRGSTPLPEAFATMDDNDIRAITVVDEHGKPLGFVKRREARNA---------SGTCADILHPFRMTGKAEDNLRVVLS 335
Cdd:COG2905   10 VTVSPDATVREAARLMTEKGVGSLVVVDDDGRLVGIITDRDLRRRvlaegldplDTPVSEVMTRPPITVSPDDSLAEALE 89

                         90       100       110
                 ....*....|....*....|....*....|....
gi 556496326 336 RLYESNTSWMPIVDeDGRYNGEISQDYIAEYLSS 369
Cdd:COG2905   90 LMEEHRIRHLPVVD-DGKLVGIVSITDLLRALSE 122
MRP_assoc_pro TIGR00957
multi drug resistance-associated protein (MRP); This model describes multi drug ...
 24-231 3.49e-07

multi drug resistance-associated protein (MRP); This model describes multi drug resistance-associated protein (MRP) in eukaryotes. The multidrug resistance-associated protein is an integral membrane protein that causes multidrug resistance when overexpressed in mammalian cells. It belongs to ABC transporter superfamily. The protein topology and function was experimentally demonstrated by epitope tagging and immunofluorescence. Insertion of tags in the critical regions associated with drug efflux, abrogated its function. The C-terminal domain seem to highly conserved. [Transport and binding proteins, Other]


Pssm-ID: 188098 [Multi-domain]  Cd Length: 1522  Bit Score: 52.26  E-value: 3.49e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556496326    24 NVNLNVPEGEMCVLLGPSGCGKTTTLKMINRLITPSSGTILINGEDTSGMDTVTLRRNIGYVIQQIGLFP---NMTIEEN 100
Cdd:TIGR00957 1304 HINVTIHGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGLNIAKIGLHDLRFKITIIPQDPVLFSgslRMNLDPF 1383

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556496326   101 ITVVPRMLGWdkarcKTRAEELMDMVALDPHKfLNRYPRE----MSGGQQQRIGVIRALAADPPVLLMDEPFGAVDPINR 176
Cdd:TIGR00957 1384 SQYSDEEVWW-----ALELAHLKTFVSALPDK-LDHECAEggenLSVGQRQLVCLARALLRKTKILVLDEATAAVDLETD 1457

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 556496326   177 EVIQ----NQFLEMqrklkkTVMLVSHDIDEALKLgDRIAVFRQGKIVQCASPDELLAK 231
Cdd:TIGR00957 1458 NLIQstirTQFEDC------TVLTIAHRLNTIMDY-TRVIVLDKGEVAEFGAPSNLLQQ 1509
ABCC_CFTR2 cd03289
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ...
 22-229 5.18e-07

ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator (CFTR), the product of the gene mutated in patients with cystic fibrosis, has adapted the ABC transporter structural motif to form a tightly regulated anion channel at the apical surface of many epithelia. Use of the term assembly of a functional ion channel implies the coming together of subunits or at least smaller not-yet functional components of the active whole. In fact, on the basis of current knowledge only the CFTR polypeptide itself is required to form an ATP- and protein kinase A-dependent low-conductance chloride channel of the type present in the apical membrane of many epithelial cells. CFTR displays the typical organization (IM-ABC)2 and carries a characteristic hydrophilic R-domain that separates IM1-ABC1 from IM2-ABC2.


Pssm-ID: 213256 [Multi-domain]  Cd Length: 275  Bit Score: 50.62  E-value: 5.18e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556496326  22 VDNVNLNVPEGEMCVLLGPSGCGKTTTLKMINRLITpSSGTILINGEDTSGMDTVTLRRNIGYVIQQIGLFPNmTIEENI 101
Cdd:cd03289   20 LENISFSISPGQRVGLLGRTGSGKSTLLSAFLRLLN-TEGDIQIDGVSWNSVPLQKWRKAFGVIPQKVFIFSG-TFRKNL 97

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556496326 102 TVVPRmlgWDKARCKTRAEEL------------MDMVALDPHKFLnrypremSGGQQQRIGVIRALAADPPVLLMDEPFG 169
Cdd:cd03289   98 DPYGK---WSDEEIWKVAEEVglksvieqfpgqLDFVLVDGGCVL-------SHGHKQLMCLARSVLSKAKILLLDEPSA 167

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 556496326 170 AVDPINREVIqnqflemQRKLKK-----TVMLVSHDIdEALKLGDRIAVFRQGKIVQCASPDELL 229
Cdd:cd03289  168 HLDPITYQVI-------RKTLKQafadcTVILSEHRI-EAMLECQRFLVIEENKVRQYDSIQKLL 224
Rli1 COG1245
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ...
 26-201 5.98e-07

Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ribosomal structure and biogenesis];


Pssm-ID: 440858 [Multi-domain]  Cd Length: 592  Bit Score: 51.32  E-value: 5.98e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556496326  26 NLNVP-EGEMCVLLGPSGCGKTTTLKMINRLITPSSGtiliNGEDTSGMDTVtLRRNIGYVIQQiglFPNMTIEENITVV 104
Cdd:COG1245   92 GLPVPkKGKVTGILGPNGIGKSTALKILSGELKPNLG----DYDEEPSWDEV-LKRFRGTELQD---YFKKLANGEIKVA 163

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556496326 105 ---------PRMLG------WDKARCKTRAEELMDMVALDPhkFLNRYPREMSGGQQQRIGVIRALAADPPVLLMDEPFG 169
Cdd:COG1245  164 hkpqyvdliPKVFKgtvrelLEKVDERGKLDELAEKLGLEN--ILDRDISELSGGELQRVAIAAALLRDADFYFFDEPSS 241

                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 556496326 170 AVDPINR----EVIQnqflEMQRKlKKTVMLVSHDI 201
Cdd:COG1245  242 YLDIYQRlnvaRLIR----ELAEE-GKYVLVVEHDL 272
CBS pfam00571
CBS domain; CBS domains are small intracellular modules that pair together to form a stable ...
 255-309 9.36e-07

CBS domain; CBS domains are small intracellular modules that pair together to form a stable globular domain. This family represents a single CBS domain. Pairs of these domains have been termed a Bateman domain. CBS domains have been shown to bind ligands with an adenosyl group such as AMP, ATP and S-AdoMet. CBS domains are found attached to a wide range of other protein domains suggesting that CBS domains may play a regulatory role making proteins sensitive to adenosyl carrying ligands. The region containing the CBS domains in Cystathionine-beta synthase is involved in regulation by S-AdoMet. CBS domain pairs from AMPK bind AMP or ATP. The CBS domains from IMPDH and the chloride channel CLC2 bind ATP.


Pssm-ID: 425756 [Multi-domain]  Cd Length: 57  Bit Score: 45.67  E-value: 9.36e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 556496326  255 AGDVTDQQPtITVRGSTPLPEAFATMDDNDIRAITVVDEHGKPLGFVKRREARNA 309
Cdd:pfam00571   1 VKDIMTKDV-VTVSPDTTLEEALELMREHGISRLPVVDEDGKLVGIVTLKDLLRA 54
CBS smart00116
Domain in cystathionine beta-synthase and other proteins; Domain present in all 3 forms of ...
 263-304 1.38e-06

Domain in cystathionine beta-synthase and other proteins; Domain present in all 3 forms of cellular life. Present in two copies in inosine monophosphate dehydrogenase, of which one is disordered in the crystal structure. A number of disease states are associated with CBS-containing proteins including homocystinuria, Becker's and Thomsen disease.


Pssm-ID: 214522 [Multi-domain]  Cd Length: 49  Bit Score: 44.81  E-value: 1.38e-06
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|..
gi 556496326   263 PTITVRGSTPLPEAFATMDDNDIRAITVVDEHGKPLGFVKRR 304
Cdd:smart00116   1 DVVTVSPDTTLEEALELLRENGIRRLPVVDEEGRLVGIVTRR 42
PRK11147 PRK11147
ABC transporter ATPase component; Reviewed
 4-200 1.57e-06

ABC transporter ATPase component; Reviewed


Pssm-ID: 236861 [Multi-domain]  Cd Length: 635  Bit Score: 49.95  E-value: 1.57e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556496326   4 LENLTKHFSQKhgqtfKAVDNVNLNVPEGEMCVLLGPSGCGKTTTLK-MINRLiTPSSGTIlingedtsgmdTVTLRRNI 82
Cdd:PRK11147 322 MENVNYQIDGK-----QLVKDFSAQVQRGDKIALIGPNGCGKTTLLKlMLGQL-QADSGRI-----------HCGTKLEV 384

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556496326  83 GYVIQ-QIGLFPNMTIEEN-------ITV--VPR-MLGWdkarcktraeeLMD-----MVALDPHKFLnrypremSGGQQ 146
Cdd:PRK11147 385 AYFDQhRAELDPEKTVMDNlaegkqeVMVngRPRhVLGY-----------LQDflfhpKRAMTPVKAL-------SGGER 446

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 556496326 147 QRIGVIRALAADPPVLLMDEPFGAVDPINREVIQnqflEMQRKLKKTVMLVSHD 200
Cdd:PRK11147 447 NRLLLARLFLKPSNLLILDEPTNDLDVETLELLE----ELLDSYQGTVLLVSHD 496
CBS_pair_inorgPPase cd04597
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with ...
 265-359 2.52e-06

Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with family II inorganic pyrophosphatase; This cd contains two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with a subgroup of family II inorganic pyrophosphatases (PPases) that also contain a DRTGG domain. The homolog from Clostridium has been shown to be inhibited by AMP and activated by a novel effector, diadenosine 5',5-P1,P4-tetraphosphate (AP(4)A), which has been shown to bind to the CBS domain. The CBS domain, named after human CBS, is a small domain originally identified in cystathionine beta-synthase and is subsequently found in a wide range of different proteins. CBS domains usually occur in tandem repeats. They associate to form a so-called Bateman domain or a CBS pair based on crystallographic studies in bacteria. The CBS pair was used as a basis for this cd hierarchy since the human CBS proteins can adopt the typical core structure and form an intramolecular CBS pair. The interface between the two CBS domains forms a cleft that is a potential ligand binding site. The CBS pair coexists with a variety of other functional domains and this has been used to help in its classification here.


Pssm-ID: 341372 [Multi-domain]  Cd Length: 106  Bit Score: 45.80  E-value: 2.52e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556496326 265 ITVRGSTPLPEAFATMDDNDIRAITVVDEHGKPLGFVKRRE-ARNASG--TCADILhpfrmTGKAEDNLRVVLSRLYESN 341
Cdd:cd04597    8 EPLSPETSIKDAWNLMDENNLKTLPVTDDNGKLIGLLSISDiARTVDYimTKDNLI-----VFKEDDYLDEVKEIMLNTN 82

                         90
                 ....*....|....*...
gi 556496326 342 TSWMPIVDEDGRYNGEIS 359
Cdd:cd04597   83 FRNYPVVDENNKFLGTIS 100
GguA NF040905
sugar ABC transporter ATP-binding protein;
20-220 3.30e-06

sugar ABC transporter ATP-binding protein;


Pssm-ID: 468840 [Multi-domain]  Cd Length: 500  Bit Score: 49.02  E-value: 3.30e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556496326  20 KAVDNVNLNVPEGEMCVLLGPSGCGKTTtLKM------INRLItpsSGTILINGEDtsgMDTVTLRRNIG----YVIQ-- 87
Cdd:NF040905 274 KVVDDVSLNVRRGEIVGIAGLMGAGRTE-LAMsvfgrsYGRNI---SGTVFKDGKE---VDVSTVSDAIDaglaYVTEdr 346

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556496326  88 -QIGLFPNMTIEENITVvPRMLGWDKARCKTRAEELMdmVALDPHKFLN-RYP------REMSGGQQQRIGVIRALAADP 159
Cdd:NF040905 347 kGYGLNLIDDIKRNITL-ANLGKVSRRGVIDENEEIK--VAEEYRKKMNiKTPsvfqkvGNLSGGNQQKVVLSKWLFTDP 423

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556496326 160 PVLLMDEPFGAVDP---------INREVIQNqflemqrklkKTVMLVSHDIDEALKLGDRIAVFRQGKIV 220
Cdd:NF040905 424 DVLILDEPTRGIDVgakyeiytiINELAAEG----------KGVIVISSELPELLGMCDRIYVMNEGRIT 483
PRK13409 PRK13409
ribosome biogenesis/translation initiation ATPase RLI;
19-201 6.45e-06

ribosome biogenesis/translation initiation ATPase RLI;


Pssm-ID: 184037 [Multi-domain]  Cd Length: 590  Bit Score: 47.88  E-value: 6.45e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556496326  19 FKAVDNVNLnvPE--GEMCV-----------------------LLGPSGCGKTTTLKMINRLITPSSGtiliNGEDTSGM 73
Cdd:PRK13409  63 FDAISIVNL--PEelEEEPVhrygvngfklyglpipkegkvtgILGPNGIGKTTAVKILSGELIPNLG----DYEEEPSW 136

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556496326  74 DTVtLRRNIGYVIQQigLFPNMtIEENITVV---------PRML-G-----WDKARCKTRAEELMDMVALDPhkFLNRYP 138
Cdd:PRK13409 137 DEV-LKRFRGTELQN--YFKKL-YNGEIKVVhkpqyvdliPKVFkGkvrelLKKVDERGKLDEVVERLGLEN--ILDRDI 210

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 556496326 139 REMSGGQQQRIGVIRALAADPPVLLMDEP---------FGAVDPInREVIQNqflemqrklkKTVMLVSHDI 201
Cdd:PRK13409 211 SELSGGELQRVAIAAALLRDADFYFFDEPtsyldirqrLNVARLI-RELAEG----------KYVLVVEHDL 271
YtoI COG4109
Predicted transcriptional regulator containing CBS domains [Transcription];
245-367 1.07e-05

Predicted transcriptional regulator containing CBS domains [Transcription];


Pssm-ID: 443285 [Multi-domain]  Cd Length: 135  Bit Score: 44.52  E-value: 1.07e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556496326 245 RTLKRLLLVsaGDVTDQQPTITVRGSTPLPEAFATMDDNDIRAITVVDEHGKPLGFVKRREARNASGT--CADIL--HPF 320
Cdd:COG4109   10 DTFKEILLV--EDIMTLEDVATLSEDDTVEDALELLEKTGHSRFPVVDENGRLVGIVTSKDILGKDDDtpIEDVMtkNPI 87

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 556496326 321 rmTGKAEDNLRVVLSRLYESNTSWMPIVDEDGRYNGEIS-QDYIAEYL 367
Cdd:COG4109   88 --TVTPDTSLASAAHKMIWEGIELLPVVDDDGRLLGIISrQDVLKALQ 133
PRK10982 PRK10982
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
 21-219 2.10e-05

galactose/methyl galaxtoside transporter ATP-binding protein; Provisional


Pssm-ID: 182880 [Multi-domain]  Cd Length: 491  Bit Score: 46.26  E-value: 2.10e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556496326  21 AVDNVNLNVPEGEMCVLLGPSGCGKTTTLKMINRLITPSSGTILINGED----------TSGMDTVTLRRnigyviQQIG 90
Cdd:PRK10982 263 SIRDVSFDLHKGEILGIAGLVGAKRTDIVETLFGIREKSAGTITLHGKKinnhnaneaiNHGFALVTEER------RSTG 336

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556496326  91 LFPNMTIEEN--ITVVPRMLG----WDKARCKTRAEELMDM--VALDPHKflnRYPREMSGGQQQRIGVIRALAADPPVL 162
Cdd:PRK10982 337 IYAYLDIGFNslISNIRNYKNkvglLDNSRMKSDTQWVIDSmrVKTPGHR---TQIGSLSGGNQQKVIIGRWLLTQPEIL 413

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 556496326 163 LMDEPFGAVDPINREVIQNQFLEMQRKlKKTVMLVSHDIDEALKLGDRIAVFRQGKI 219
Cdd:PRK10982 414 MLDEPTRGIDVGAKFEIYQLIAELAKK-DKGIIIISSEMPELLGITDRILVMSNGLV 469
CBS_pair_ABC_OpuCA_assoc cd04583
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains found associated with ...
 265-353 2.49e-05

Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains found associated with the ABC transporter OpuCA; This cd contains two tandem repeats of the cystathionine beta-synthase (CBS pair) domains found in association with the ABC transporter OpuCA. OpuCA is the ATP binding component of a bacterial solute transporter that serves a protective role to cells growing in a hyperosmolar environment but the function of the CBS domains in OpuCA remains unknown. In the related ABC transporter, OpuA, the tandem CBS domains have been shown to function as sensors for ionic strength, whereby they control the transport activity through an electronic switching mechanism. 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. They 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. The CBS domain, named after human CBS, is a small domain originally identified in cystathionine beta-synthase and is subsequently found in a wide range of different proteins. CBS domains usually occur in tandem repeats. They associate to form a so-called Bateman domain or a CBS pair based on crystallographic studies in bacteria. The CBS pair was used as a basis for this cd hierarchy since the human CBS proteins can adopt the typical core structure and form an intramolecular CBS pair. The interface between the two CBS domains forms a cleft that is a potential ligand binding site. The CBS pair coexists with a variety of other functional domains and this has been used to help in its classification here. It has been proposed that the CBS domain may play a regulatory role, although its exact function is unknown. Mutations of conserved residues within this domain are associated with a variety of human hereditary diseases, including congenital myotonia, idiopathic generalized epilepsy, hypercalciuric nephrolithiasis, and classic Bartter syndrome (CLC chloride channel family members), Wolff-Parkinson-White syndrome (gamma 2 subunit of AMP-activated protein kinase), retinitis pigmentosa (IMP dehydrogenase-1), and homocystinuria (cystathionine beta-synthase).


Pssm-ID: 341360 [Multi-domain]  Cd Length: 110  Bit Score: 42.89  E-value: 2.49e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556496326 265 ITVRGSTPLPEAFATMDDNDIRAITVVDEHGKPLGFVKRRE---ARNASGTCADILHPFRMTGKAEDNLRVVLSRLYESN 341
Cdd:cd04583    5 VTITPERTLAQAIEIMREKRVDSLLVVDKDNVLLGIVDIEDinrNYRKAKKVGEIMERDVFTVKEDSLLRDTVDRILKRG 84

                         90
                 ....*....|..
gi 556496326 342 TSWMPIVDEDGR 353
Cdd:cd04583   85 LKYVPVVDEQGR 96
3a01205 TIGR00956
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
 23-172 2.64e-05

Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]


Pssm-ID: 273362 [Multi-domain]  Cd Length: 1394  Bit Score: 46.26  E-value: 2.64e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556496326    23 DNVNLNVPEGEMCVLLGPSGCGKTTTLKMINRLITP---SSGTILINGEdtsGMDTvTLRRNIGYVIQQIGLFPNMTIEE 99
Cdd:TIGR00956  780 NNVDGWVKPGTLTALMGASGAGKTTLLNVLAERVTTgviTGGDRLVNGR---PLDS-SFQRSIGYVQQQDLHLPTSTVRE 855

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556496326   100 NITVVPRMLGWDKARCKTR---AEELMDMVALDPHK-FLNRYPRE-MSGGQQQR--IGVirALAADPPVLL-MDEPFGAV 171
Cdd:TIGR00956  856 SLRFSAYLRQPKSVSKSEKmeyVEEVIKLLEMESYAdAVVGVPGEgLNVEQRKRltIGV--ELVAKPKLLLfLDEPTSGL 933


                   .
gi 556496326   172 D 172
Cdd:TIGR00956  934 D 934
COG3448 COG3448
CBS-domain-containing membrane protein [Signal transduction mechanisms];
244-305 4.93e-05

CBS-domain-containing membrane protein [Signal transduction mechanisms];


Pssm-ID: 442671 [Multi-domain]  Cd Length: 136  Bit Score: 42.93  E-value: 4.93e-05
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 556496326 244 DRTLKRLLLVSAGDVTdQQPTITVRGSTPLPEAFATMDDNDIRAITVVDEHGKPLGFVKRRE 305
Cdd:COG3448   64 DELEERLLDLPVEDVM-TRPVVTVTPDTPLEEAAELMLEHGIHRLPVVDDDGRLVGIVTRTD 124
ABC_UvrA cd03238
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ...
 24-211 5.66e-05

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: 43.47  E-value: 5.66e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556496326  24 NVNLNVPEGEMCVLLGPSGCGKTTTLKMInrlitpssgtILINGEDTSGMDTVTLRRNIGYVIQQIGLFpnmtIEENITV 103
Cdd:cd03238   13 NLDVSIPLNVLVVVTGVSGSGKSTLVNEG----------LYASGKARLISFLPKFSRNKLIFIDQLQFL----IDVGLGY 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556496326 104 VPrmlgwdkarcktraeelmdmvaldphkfLNRYPREMSGGQQQRIGVIRALAADPP--VLLMDEPFGAVDPInrevIQN 181
Cdd:cd03238   79 LT----------------------------LGQKLSTLSGGELQRVKLASELFSEPPgtLFILDEPSTGLHQQ----DIN 126

                        170       180       190
                 ....*....|....*....|....*....|...
gi 556496326 182 QFLEMQRKL---KKTVMLVSHDiDEALKLGDRI 211
Cdd:cd03238  127 QLLEVIKGLidlGNTVILIEHN-LDVLSSADWI 158
PRK14869 PRK14869
putative manganese-dependent inorganic diphosphatase;
256-301 7.08e-05

putative manganese-dependent inorganic diphosphatase;


Pssm-ID: 237843 [Multi-domain]  Cd Length: 546  Bit Score: 44.82  E-value: 7.08e-05
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*.
gi 556496326 256 GDVTDQQPtITVRGSTPLPEAFATMDDNDIRAITVVDEHGKPLGFV 301
Cdd:PRK14869  71 RDLEIDKP-VTVSPDTSLKEAWNLMDENNVKTLPVVDEEGKLLGLV 115
CBS_pair_ABC_Gly_Pro_assoc cd09831
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains found associated with ...
 260-360 4.33e-04

Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains found associated with the glycine betaine/L-proline ABC transporter; This cd contains two tandem repeats of the cystathionine beta-synthase (CBS pair) domains found in association with the ABC transporter OpuCA. OpuCA is the ATP binding component of a bacterial solute transporter that serves a protective role to cells growing in a hyperosmolar environment but the function of the CBS domains in OpuCA remains unknown. In the related ABC transporter, OpuA, the tandem CBS domains have been shown to function as sensors for ionic strength, whereby they control the transport activity through an electronic switching mechanism. 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. They 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. The CBS domain, named after human CBS, is a small domain originally identified in cystathionine beta-synthase and is subsequently found in a wide range of different proteins. CBS domains usually occur in tandem repeats. They associate to form a so-called Bateman domain or a CBS pair based on crystallographic studies in bacteria. The CBS pair was used as a basis for this cd hierarchy since the human CBS proteins can adopt the typical core structure and form an intramolecular CBS pair. The interface between the two CBS domains forms a cleft that is a potential ligand binding site. The CBS pair coexists with a variety of other functional domains and this has been used to help in its classification here. It has been proposed that the CBS domain may play a regulatory role, although its exact function is unknown. Mutations of conserved residues within this domain are associated with a variety of human hereditary diseases, including congenital myotonia, idiopathic generalized epilepsy, hypercalciuric nephrolithiasis, and classic Bartter syndrome (CLC chloride channel family members), Wolff-Parkinson-White syndrome (gamma 2 subunit of AMP-activated protein kinase), retinitis pigmentosa (IMP dehydrogenase-1), and homocystinuria (cystathionine beta-synthase).


Pssm-ID: 341402 [Multi-domain]  Cd Length: 116  Bit Score: 39.47  E-value: 4.33e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556496326 260 DQQPTITVRGSTPLPEAFATMDDNDIRAITVVDEHGKPLGFVKRREARNA----SGTCADILHPFRMTGKAEDNLRVVLS 335
Cdd:cd09831    5 KTQVTVIEKTGDGPRAALQLLREHDREYGYVVDKKRRFLGVVSVDSLRAAlkenAQSLEDAFLTDVETVPADTSLSDILG 84

                         90       100
                 ....*....|....*....|....*
gi 556496326 336 RLYESNTSwMPIVDEDGRYNGEISQ 360
Cdd:cd09831   85 LVASAPCP-LPVVDEDGRYLGVISK 108
uvra TIGR00630
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ...
 116-247 5.06e-04

excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of proteins of which all members for which functions are known except the UvrA proteins are involved in the transport of material through membranes. UvrA orthologs are involved in the recognition of DNA damage as a step in nucleotide excision repair. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]


Pssm-ID: 273184 [Multi-domain]  Cd Length: 925  Bit Score: 42.31  E-value: 5.06e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556496326  116 KTRAEELMDmVALDpHKFLNRYPREMSGGQQQRIGVIRALAAD-PPVL-LMDEP-FGAVDPINREVIQNqfLEMQRKLKK 192
Cdd:TIGR00630 466 RERLGFLID-VGLD-YLSLSRAAGTLSGGEAQRIRLATQIGSGlTGVLyVLDEPsIGLHQRDNRRLINT--LKRLRDLGN 541

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 556496326  193 TVMLVSHDiDEALKLGDRI------AVFRQGKIVQCASPDELLAKPaNEFVGSFVGQDRTL 247
Cdd:TIGR00630 542 TLIVVEHD-EDTIRAADYVidigpgAGEHGGEVVASGTPEEILANP-DSLTGQYLSGRKKI 600
CBS_pair_plant_CBSX cd17789
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains from plant CBSX ...
 201-303 8.71e-04

Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains from plant CBSX proteins; This cd contains two tandem repeats of the cystathionine beta-synthase (CBS pair) domains of plant single cystathionine beta-synthase (CBS) pair proteins (CBSX). CBSX1 and CBSX2 have been identified as redox regulators of the thioredoxin (Trx) system. The CBS domain, named after human CBS, is a small domain originally identified in cystathionine beta-synthase and is subsequently found in a wide range of different proteins. CBS domains usually occur in tandem repeats. They associate to form a so-called Bateman domain or a CBS pair based on crystallographic studies in bacteria. The CBS pair was used as a basis for this cd hierarchy since the human CBS proteins can adopt the typical core structure and form an intramolecular CBS pair. The interface between the two CBS domains forms a cleft that is a potential ligand binding site. The CBS pair coexists with a variety of other functional domains and this has been used to help in its classification here. It has been proposed that the CBS domain may play a regulatory role, although its exact function is unknown. Mutations of conserved residues within this domain are associated with a variety of human hereditary diseases, including congenital myotonia, idiopathic generalized epilepsy, hypercalciuric nephrolithiasis, and classic Bartter syndrome (CLC chloride channel family members), Wolff-Parkinson-White syndrome (gamma 2 subunit of AMP-activated protein kinase), retinitis pigmentosa (IMP dehydrogenase-1), and homocystinuria (cystathionine beta-synthase).


Pssm-ID: 341425 [Multi-domain]  Cd Length: 141  Bit Score: 39.38  E-value: 8.71e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556496326 201 IDEALKL--GDRIAVF----RQGKIVQCASPDELLAKPA----NEFVGSFVGQDRT------LKRLLLVSAG----DVTD 260
Cdd:cd17789   14 VDEALELlvENRITGLpvidEDWRLVGVVSDYDLLALDSisgrSQTDNNFPPADSTwktfneVQKLLSKTNGkvvgDVMT 93

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 556496326 261 QQPtITVRGSTPLPEAFATMDDNDIRAITVVDEHGKPLGFVKR 303
Cdd:cd17789   94 PSP-LVVREKTNLEDAARILLETKFRRLPVVDSDGKLVGIITR 135
CBS_pair_BON_assoc cd04586
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with the ...
 265-301 1.13e-03

Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with the BON (bacterial OsmY and nodulation domain) domain; This cd contains two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with the BON (bacterial OsmY and nodulation domain) domain. BON is a putative phospholipid-binding domain found in a family of osmotic shock protection proteins. It is also found in some secretins and a group of potential haemolysins. Its likely function is attachment to phospholipid membranes. The CBS domain, named after human CBS, is a small domain originally identified in cystathionine beta-synthase and is subsequently found in a wide range of different proteins. CBS domains usually occur in tandem repeats. They associate to form a so-called Bateman domain or a CBS pair based on crystallographic studies in bacteria. The CBS pair was used as a basis for this cd hierarchy since the human CBS proteins can adopt the typical core structure and form an intramolecular CBS pair. The interface between the two CBS domains forms a cleft that is a potential ligand binding site. The CBS pair coexists with a variety of other functional domains and this has been used to help in its classification here. It has been proposed that the CBS domain may play a regulatory role, although its exact function is unknown. Mutations of conserved residues within this domain are associated with a variety of human hereditary diseases, including congenital myotonia, idiopathic generalized epilepsy, hypercalciuric nephrolithiasis, and classic Bartter syndrome (CLC chloride channel family members), Wolff-Parkinson-White syndrome (gamma 2 subunit of AMP-activated protein kinase), retinitis pigmentosa (IMP dehydrogenase-1), and homocystinuria (cystathionine beta-synthase).


Pssm-ID: 341362 [Multi-domain]  Cd Length: 137  Bit Score: 38.95  E-value: 1.13e-03
                         10        20        30
                 ....*....|....*....|....*....|....*..
gi 556496326 265 ITVRGSTPLPEAFATMDDNDIRAITVVDEHGKPLGFV 301
Cdd:cd04586    6 VTVTPDTSVREAARLLLEHRISGLPVVDDDGKLVGIV 42
AdhP COG1064
D-arabinose 1-dehydrogenase, Zn-dependent alcohol dehydrogenase family [Carbohydrate transport ...
 197-292 1.76e-03

D-arabinose 1-dehydrogenase, Zn-dependent alcohol dehydrogenase family [Carbohydrate transport and metabolism];


Pssm-ID: 440684 [Multi-domain]  Cd Length: 332  Bit Score: 40.10  E-value: 1.76e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556496326 197 VSHDIDEALKLgdriaVFRQGKIVQCASPDELLAKPAN-------EFVGSFVGQDRTLKRLL-LVSAGDVTdqqPTITVR 268
Cdd:COG1064  237 APATVNAALAL-----LRRGGRLVLVGLPGGPIPLPPFdlilkerSIRGSLIGTRADLQEMLdLAAEGKIK---PEVETI 308

                         90       100
                 ....*....|....*....|....*..
gi 556496326 269 gstPL---PEAFATMDDNDIRAITVVD 292
Cdd:COG1064  309 ---PLeeaNEALERLRAGKVRGRAVLD 332
CBS_pair_bac_arch cd17785
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains present in bacteria ...
 263-299 3.21e-03

Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains present in bacteria and archaea; The CBS domain, named after human CBS, is a small domain originally identified in cystathionine beta-synthase and is subsequently found in a wide range of different proteins. CBS domains usually occur in tandem repeats. They associate to form a so-called Bateman domain or a CBS pair based on crystallographic studies in bacteria. The CBS pair was used as a basis for this cd hierarchy since the human CBS proteins can adopt the typical core structure and form an intramolecular CBS pair. The interface between the two CBS domains forms a cleft that is a potential ligand binding site. The CBS pair coexists with a variety of other functional domains and this has been used to help in its classification here. It has been proposed that the CBS domain may play a regulatory role, although its exact function is unknown. Mutations of conserved residues within this domain are associated with a variety of human hereditary diseases, including congenital myotonia, idiopathic generalized epilepsy, hypercalciuric nephrolithiasis, and classic Bartter syndrome (CLC chloride channel family members), Wolff-Parkinson-White syndrome (gamma 2 subunit of AMP-activated protein kinase), retinitis pigmentosa (IMP dehydrogenase-1), and homocystinuria (cystathionine beta-synthase).


Pssm-ID: 341421 [Multi-domain]  Cd Length: 136  Bit Score: 37.64  E-value: 3.21e-03
                         10        20        30
                 ....*....|....*....|....*....|....*..
gi 556496326 263 PTITVRGSTPLPEAFATMDDNDIRAITVVDEHGKPLG 299
Cdd:cd17785   91 SPIYVKKEDTLEEALELMVKNRLQELPVVDENGKVIG 127
CBS_pair_bac cd04629
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains present in bacteria; ...
 265-301 4.31e-03

Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains present in bacteria; The CBS domain, named after human CBS, is a small domain originally identified in cystathionine beta-synthase and is subsequently found in a wide range of different proteins. CBS domains usually occur in tandem repeats. They associate to form a so-called Bateman domain or a CBS pair based on crystallographic studies in bacteria. The CBS pair was used as a basis for this cd hierarchy since the human CBS proteins can adopt the typical core structure and form an intramolecular CBS pair. The interface between the two CBS domains forms a cleft that is a potential ligand binding site. The CBS pair coexists with a variety of other functional domains and this has been used to help in its classification here. It has been proposed that the CBS domain may play a regulatory role, although its exact function is unknown. Mutations of conserved residues within this domain are associated with a variety of human hereditary diseases, including congenital myotonia, idiopathic generalized epilepsy, hypercalciuric nephrolithiasis, and classic Bartter syndrome (CLC chloride channel family members), Wolff-Parkinson-White syndrome (gamma 2 subunit of AMP-activated protein kinase), retinitis pigmentosa (IMP dehydrogenase-1), and homocystinuria (cystathionine beta-synthase).


Pssm-ID: 341392 [Multi-domain]  Cd Length: 116  Bit Score: 36.65  E-value: 4.31e-03
                         10        20        30
                 ....*....|....*....|....*....|....*..
gi 556496326 265 ITVRGSTPLPEAFATMDDNDIRAITVVDEHGKPLGFV 301
Cdd:cd04629    6 VTLTPDTSILEAVELLLEHKISGAPVVDEQGRLVGFL 42
ABC_UvrA_I cd03270
ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair ...
 24-211 4.35e-03

ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins, and UvrB having one ATP binding site that is structurally related to that of helicases.


Pssm-ID: 213237 [Multi-domain]  Cd Length: 226  Bit Score: 38.39  E-value: 4.35e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556496326  24 NVNLNVPEGEMCVLLGPSGCGKTTtLKMinrlitpssGTILINGEDTSgMDTVT--LRRNIG-----YVIQQIGLFPNMT 96
Cdd:cd03270   13 NVDVDIPRNKLVVITGVSGSGKSS-LAF---------DTIYAEGQRRY-VESLSayARQFLGqmdkpDVDSIEGLSPAIA 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556496326  97 IEENITVV-PRM-------------LGWDKARCKTRAEELMDmVALDpHKFLNRYPREMSGGQQQRIGVIRALAADPPVL 162
Cdd:cd03270   82 IDQKTTSRnPRStvgtvteiydylrLLFARVGIRERLGFLVD-VGLG-YLTLSRSAPTLSGGEAQRIRLATQIGSGLTGV 159

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 556496326 163 L--MDEPFGAVDPI-NREVIQNqfLEMQRKLKKTVMLVSHDiDEALKLGDRI 211
Cdd:cd03270  160 LyvLDEPSIGLHPRdNDRLIET--LKRLRDLGNTVLVVEHD-EDTIRAADHV 208
CBS_pair_CAP-ED_NT_Pol-beta-like_DUF294_assoc cd17771
CBS domain protein; This cd contains two tandem repeats of the cystathionine beta-synthase ...
 265-307 4.40e-03

CBS domain protein; This cd contains two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with the bacterial CAP_ED (cAMP receptor protein effector domain) family of transcription factors, the NT_Pol-beta-like domain, and the DUF294 domain. Members of CAP_ED, include CAP which binds cAMP, FNR (fumarate and nitrate reductase) which uses an iron-sulfur cluster to sense oxygen, and CooA a heme containing CO sensor. In all cases binding of the effector leads to conformational changes and the ability to activate transcription. The NT_Pol-beta-like domain includes the Nucleotidyltransferase (NT) domains of DNA polymerase beta and other family X DNA polymerases, as well as the NT domains of class I and class II CCA-adding enzymes, RelA- and SpoT-like ppGpp synthetases and hydrolases, 2'5'-oligoadenylate (2-5A)synthetases, Escherichia coli adenylyltransferase (GlnE), Escherichia coli uridylyl transferase (GlnD), poly (A) polymerases, terminal uridylyl transferases, Staphylococcus aureus kanamycin nucleotidyltransferase, and similar proteins. DUF294 is a putative nucleotidyltransferase with a conserved DxD motif. CBS is a small domain originally identified in cystathionine beta-synthase and subsequently found in a wide range of different proteins. The CBS domain, named after human CBS, is a small domain originally identified in cystathionine beta-synthase and is subsequently found in a wide range of different proteins. CBS domains usually occur in tandem repeats. They associate to form a so-called Bateman domain or a CBS pair based on crystallographic studies in bacteria. The CBS pair was used as a basis for this cd hierarchy since the human CBS proteins can adopt the typical core structure and form an intramolecular CBS pair. The interface between the two CBS domains forms a cleft that is a potential ligand binding site. The CBS pair coexists with a variety of other functional domains and this has been used to help in its classification here. It has been proposed that the CBS domain may play a regulatory role, although its exact function is unknown. Mutations of conserved residues within this domain are associated with a variety of human hereditary diseases, including congenital myotonia, idiopathic generalized epilepsy, hypercalciuric nephrolithiasis, and classic Bartter syndrome (CLC chloride channel family members), Wolff-Parkinson-White syndrome (gamma 2 subunit of AMP-activated protein kinase), retinitis pigmentosa (IMP dehydrogenase-1), and homocystinuria (cystathionine beta-synthase).


Pssm-ID: 341407 [Multi-domain]  Cd Length: 115  Bit Score: 36.53  E-value: 4.40e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|...
gi 556496326 265 ITVRGSTPLPEAFATMDDNDIRAITVVDEHGKPLGFVKRREAR 307
Cdd:cd17771    7 VTCSPDTPLRAALETMHERRVGSMVVVDANRRPVGIFTLRDLL 49
CBS_pair_IMPDH cd04601
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains in the inosine 5' ...
 265-353 5.25e-03

Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains in the inosine 5' monophosphate dehydrogenase (IMPDH) protein; This cd contains two tandem repeats of the cystathionine beta-synthase (CBS pair) domains in the inosine 5' monophosphate dehydrogenase (IMPDH) protein. IMPDH is an essential enzyme that catalyzes the first step unique to GTP synthesis, playing a key role in the regulation of cell proliferation and differentiation. The CBS domain, named after human CBS, is a small domain originally identified in cystathionine beta-synthase and is subsequently found in a wide range of different proteins. CBS domains usually occur in tandem repeats. They associate to form a so-called Bateman domain or a CBS pair based on crystallographic studies in bacteria. The CBS pair was used as a basis for this cd hierarchy since the human CBS proteins can adopt the typical core structure and form an intramolecular CBS pair. The interface between the two CBS domains forms a cleft that is a potential ligand binding site. The CBS pair coexists with a variety of other functional domains and this has been used to help in its classification here. It has been proposed that the CBS domain may play a regulatory role, although its exact function is unknown. Mutations of conserved residues within this domain are associated with a variety of human hereditary diseases, including congenital myotonia, idiopathic generalized epilepsy, hypercalciuric nephrolithiasis, and classic Bartter syndrome (CLC chloride channel family members), Wolff-Parkinson-White syndrome (gamma 2 subunit of AMP-activated protein kinase), retinitis pigmentosa (IMP dehydrogenase-1), and homocystinuria (cystathionine beta-synthase).


Pssm-ID: 341376 [Multi-domain]  Cd Length: 110  Bit Score: 36.24  E-value: 5.25e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556496326 265 ITVRGSTPLPEAFATMDDNDIRAITVVDEHGKPLGFVKRRE---ARNASGTCADILHPFRM--TGKAEDNLRVVLSRLYE 339
Cdd:cd04601    5 VTLSPDATVADVLELKAEYGISGVPVTEDGGKLVGIVTSRDirfETDLSTPVSEVMTPDERlvTAPEGITLEEAKEILHK 84

                         90
                 ....*....|....
gi 556496326 340 SNTSWMPIVDEDGR 353
Cdd:cd04601   85 HKIEKLPIVDDNGE 98
CBS_pair_AcuB_like cd04584
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with the ...
 265-310 5.95e-03

Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with the ACT domain; The putative Acetoin Utilization Protein (Acub) from Vibrio Cholerae contains a CBS pair domain. The acetoin utilization protein plays a role in growth and sporulation on acetoin or butanediol for use as a carbon source. Acetoin is an important physiological metabolite excreted by many microorganisms. It is used as an external energy store by a number of fermentive bacteria. Acetoin is produced by the decarboxylation of alpha-acetolactate. Once superior carbon sources are exhausted, and the culture enters stationary phase, acetoin can be utilised in order to maintain the culture density. The conversion of acetoin into acetyl-CoA or 2,3-butanediol is catalysed by the acetoin dehydrogenase complex and acetoin reductase/2,3-butanediol dehydrogenase, respectively. Acetoin utilization proteins, acetylpolyamine amidohydrolases, and histone deacetylases are members of an ancient protein superfamily.This cd contains two tandem repeats of the cystathionine beta-synthase (CBS pair) domains in the acetoin utilization proteins in bacteria. Acetoin is a product of fermentative metabolism in many prokaryotic and eukaryotic microorganisms. They produce acetoin as an external carbon storage compound and then later reuse it as a carbon and energy source during their stationary phase and sporulation. In addition these CBS domains are associated with a downstream ACT (aspartate kinase/chorismate mutase/TyrA) domain, which is linked to a wide range of metabolic enzymes that are regulated by amino acid concentration. Pairs of ACT domains bind specifically to a particular amino acid leading to regulation of the linked enzyme. The CBS domain, named after human CBS, is a small domain originally identified in cystathionine beta-synthase and is subsequently found in a wide range of different proteins. CBS domains usually occur in tandem repeats. They associate to form a so-called Bateman domain or a CBS pair based on crystallographic studies in bacteria. The CBS pair was used as a basis for this cd hierarchy since the human CBS proteins can adopt the typical core structure and form an intramolecular CBS pair. The interface between the two CBS domains forms a cleft that is a potential ligand binding site. The CBS pair coexists with a variety of other functional domains and this has been used to help in its classification here. It has been proposed that the CBS domain may play a regulatory role, although its exact function is unknown. Mutations of conserved residues within this domain are associated with a variety of human hereditary diseases, including congenital myotonia, idiopathic generalized epilepsy, hypercalciuric nephrolithiasis, and classic Bartter syndrome (CLC chloride channel family members), Wolff-Parkinson-White syndrome (gamma 2 subunit of AMP-activated protein kinase), retinitis pigmentosa (IMP dehydrogenase-1), and homocystinuria (cystathionine beta-synthase).


Pssm-ID: 341361 [Multi-domain]  Cd Length: 130  Bit Score: 36.63  E-value: 5.95e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*.
gi 556496326 265 ITVRGSTPLPEAFATMDDNDIRAITVVDEhGKPLGFVKRREARNAS 310
Cdd:cd04584   11 VTVTPDTSLAEARELMKEHKIRHLPVVDD-GKLVGIVTDRDLLRAS 55
AAA_22 pfam13401
AAA domain;
34-82 5.97e-03

AAA domain;


Pssm-ID: 379165 [Multi-domain]  Cd Length: 129  Bit Score: 36.55  E-value: 5.97e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 556496326   34 MCVLLGPSGCGKTTTLKMI-NRLITPSSGTILIngEDTSGMDTVTLRRNI 82
Cdd:pfam13401   7 ILVLTGESGTGKTTLLRRLlEQLPEVRDSVVFV--DLPSGTSPKDLLRAL 54
CBS pfam00571
CBS domain; CBS domains are small intracellular modules that pair together to form a stable ...
 325-369 6.53e-03

CBS domain; CBS domains are small intracellular modules that pair together to form a stable globular domain. This family represents a single CBS domain. Pairs of these domains have been termed a Bateman domain. CBS domains have been shown to bind ligands with an adenosyl group such as AMP, ATP and S-AdoMet. CBS domains are found attached to a wide range of other protein domains suggesting that CBS domains may play a regulatory role making proteins sensitive to adenosyl carrying ligands. The region containing the CBS domains in Cystathionine-beta synthase is involved in regulation by S-AdoMet. CBS domain pairs from AMPK bind AMP or ATP. The CBS domains from IMPDH and the chloride channel CLC2 bind ATP.


Pssm-ID: 425756 [Multi-domain]  Cd Length: 57  Bit Score: 34.50  E-value: 6.53e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 556496326  325 KAEDNLRVVLSRLYESNTSWMPIVDEDGRYNGEISQDYIAEYLSS 369
Cdd:pfam00571  13 SPDTTLEEALELMREHGISRLPVVDEDGKLVGIVTLKDLLRALLG 57
CBS_pair_NTP_transferase_assoc cd04607
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domain associated with the ...
 265-353 6.54e-03

Two tandem repeats of the cystathionine beta-synthase (CBS pair) domain associated with the NTP (Nucleotidyl transferase) domain; This cd contains two tandem repeats of the cystathionine beta-synthase (CBS pair) domain associated with the NTP (Nucleotidyl transferase) domain downstream. The CBS domain, named after human CBS, is a small domain originally identified in cystathionine beta-synthase and is subsequently found in a wide range of different proteins. CBS domains usually occur in tandem repeats. They associate to form a so-called Bateman domain or a CBS pair based on crystallographic studies in bacteria. The CBS pair was used as a basis for this cd hierarchy since the human CBS proteins can adopt the typical core structure and form an intramolecular CBS pair. The interface between the two CBS domains forms a cleft that is a potential ligand binding site. The CBS pair coexists with a variety of other functional domains and this has been used to help in its classification here. It has been proposed that the CBS domain may play a regulatory role, although its exact function is unknown. Mutations of conserved residues within this domain are associated with a variety of human hereditary diseases, including congenital myotonia, idiopathic generalized epilepsy, hypercalciuric nephrolithiasis, and classic Bartter syndrome (CLC chloride channel family members), Wolff-Parkinson-White syndrome (gamma 2 subunit of AMP-activated protein kinase), retinitis pigmentosa (IMP dehydrogenase-1), and homocystinuria (cystathionine beta-synthase).


Pssm-ID: 341381 [Multi-domain]  Cd Length: 112  Bit Score: 36.27  E-value: 6.54e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556496326 265 ITVRGSTPLPEAFATMDDNDIRAITVVDEHGKPLGFVK----RReA--RNAS--GTCADILHPFRMTGKAEDNLRVVLSR 336
Cdd:cd04607    5 VLVSPDTTIREAIEVIDKGALQIALVVDENRKLLGTVTdgdiRR-GllKGLSldAPVEEVMNKNPITASPSTSREELLAL 83

                         90
                 ....*....|....*..
gi 556496326 337 LYESNTSWMPIVDEDGR 353
Cdd:cd04607   84 MRAKKILQLPIVDEQGR 100
 
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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