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Conserved domains on  [gi|1037402861|gb|ANM26269|]
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sugar ABC transporter ATP-binding protein (plasmid) [Rhizobium sp. N941]

Protein Classification

ABC transporter ATP-binding protein( domain architecture ID 11467400)

ABC transporter ATP-binding protein is the ATPase catalytic subunit of an ABC transporter complex and is responsible for coupling the energy of ATP hydrolysis to the import of one or more from a variety of substrates including sugars or polysaccharides, such as sn-glycerol-3-phosphate, trehalose, or maltose/maltodextrin

CATH:  3.40.50.300
Gene Ontology:  GO:0042626|GO:0140359|GO:0016887|GO:0005524
PubMed:  11421270|25750732|24638992
SCOP:  4003976
TCDB:  3.A.1

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
MalK COG3839
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ...
 1-359 0e+00

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


:

Pssm-ID: 443050 [Multi-domain]  Cd Length: 352  Bit Score: 581.65  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037402861   1 MAELSLSNIVKRFGGFEIIHGANLEVKDGEFVVFVGPSGCGKSTLLRMIAGLEDITSGELQIGGRVVNDVEPADRGIAMV 80
Cdd:COG3839     1 MASLELENVSKSYGGVEALKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAGLEDPTSGEILIGGRDVTDLPPKDRNIAMV 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037402861  81 FQSYALYPHLTVEENLSFGLRMNGNPKADTERRVSHVAEILQITELMKRRPKQLSGGQRQRVAIGRAIVREPEVFLFDEP 160
Cdd:COG3839    81 FQSYALYPHMTVYENIAFPLKLRKVPKAEIDRRVREAAELLGLEDLLDRKPKQLSGGQRQRVALGRALVREPKVFLLDEP 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037402861 161 LSNLDAELRVQMRVEISRLHKKLGTTMIYVTHDQTEAMTLADRIVVLRAGNIEQIGAPLDLYDDPANQFVAGFVGSPKMN 240
Cdd:COG3839   161 LSNLDAKLRVEMRAEIKRLHRRLGTTTIYVTHDQVEAMTLADRIAVMNDGRIQQVGTPEELYDRPANLFVAGFIGSPPMN 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037402861 241 FLKAVVVEaqpGRAVIalesdANMRLPLPVAAPIETGAKVTLGIRPEHFVDAGMGDADLTVAIDVAEHLGNTSYIYAAIG 320
Cdd:COG3839   241 LLPGTVEG---GGVRL-----GGVRLPLPAALAAAAGGEVTLGIRPEHLRLADEGDGGLEATVEVVEPLGSETLVHVRLG 312

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|
gi 1037402861 321 SEQLIIERPESRTAGNRETLTVGLPARHTFLFDGA-GKRL 359
Cdd:COG3839   313 GQELVARVPGDTRLRPGDTVRLAFDPERLHLFDAEtGRRL 352
 
Name Accession Description Interval E-value
MalK COG3839
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ...
 1-359 0e+00

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


Pssm-ID: 443050 [Multi-domain]  Cd Length: 352  Bit Score: 581.65  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037402861   1 MAELSLSNIVKRFGGFEIIHGANLEVKDGEFVVFVGPSGCGKSTLLRMIAGLEDITSGELQIGGRVVNDVEPADRGIAMV 80
Cdd:COG3839     1 MASLELENVSKSYGGVEALKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAGLEDPTSGEILIGGRDVTDLPPKDRNIAMV 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037402861  81 FQSYALYPHLTVEENLSFGLRMNGNPKADTERRVSHVAEILQITELMKRRPKQLSGGQRQRVAIGRAIVREPEVFLFDEP 160
Cdd:COG3839    81 FQSYALYPHMTVYENIAFPLKLRKVPKAEIDRRVREAAELLGLEDLLDRKPKQLSGGQRQRVALGRALVREPKVFLLDEP 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037402861 161 LSNLDAELRVQMRVEISRLHKKLGTTMIYVTHDQTEAMTLADRIVVLRAGNIEQIGAPLDLYDDPANQFVAGFVGSPKMN 240
Cdd:COG3839   161 LSNLDAKLRVEMRAEIKRLHRRLGTTTIYVTHDQVEAMTLADRIAVMNDGRIQQVGTPEELYDRPANLFVAGFIGSPPMN 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037402861 241 FLKAVVVEaqpGRAVIalesdANMRLPLPVAAPIETGAKVTLGIRPEHFVDAGMGDADLTVAIDVAEHLGNTSYIYAAIG 320
Cdd:COG3839   241 LLPGTVEG---GGVRL-----GGVRLPLPAALAAAAGGEVTLGIRPEHLRLADEGDGGLEATVEVVEPLGSETLVHVRLG 312

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|
gi 1037402861 321 SEQLIIERPESRTAGNRETLTVGLPARHTFLFDGA-GKRL 359
Cdd:COG3839   313 GQELVARVPGDTRLRPGDTVRLAFDPERLHLFDAEtGRRL 352
ugpC PRK11650
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
1-358 0e+00

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


Pssm-ID: 236947 [Multi-domain]  Cd Length: 356  Bit Score: 530.57  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037402861   1 MAELSLSNIVKRF-GGFEIIHGANLEVKDGEFVVFVGPSGCGKSTLLRMIAGLEDITSGELQIGGRVVNDVEPADRGIAM 79
Cdd:PRK11650    1 MAGLKLQAVRKSYdGKTQVIKGIDLDVADGEFIVLVGPSGCGKSTLLRMVAGLERITSGEIWIGGRVVNELEPADRDIAM 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037402861  80 VFQSYALYPHLTVEENLSFGLRMNGNPKADTERRVSHVAEILQITELMKRRPKQLSGGQRQRVAIGRAIVREPEVFLFDE 159
Cdd:PRK11650   81 VFQNYALYPHMSVRENMAYGLKIRGMPKAEIEERVAEAARILELEPLLDRKPRELSGGQRQRVAMGRAIVREPAVFLFDE 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037402861 160 PLSNLDAELRVQMRVEISRLHKKLGTTMIYVTHDQTEAMTLADRIVVLRAGNIEQIGAPLDLYDDPANQFVAGFVGSPKM 239
Cdd:PRK11650  161 PLSNLDAKLRVQMRLEIQRLHRRLKTTSLYVTHDQVEAMTLADRVVVMNGGVAEQIGTPVEVYEKPASTFVASFIGSPAM 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037402861 240 NFLkavvvEAQPGRAVIALESDANMRLPLPVAAPIETGAKVTLGIRPEHFVDAGmGDADLTVAIDVAEHLGNTSYIYAAI 319
Cdd:PRK11650  241 NLL-----DGRVSADGAAFELAGGIALPLGGGYRQYAGRKLTLGIRPEHIALSS-AEGGVPLTVDTVELLGADNLAHGRW 314

                         330       340       350
                  ....*....|....*....|....*....|....*....
gi 1037402861 320 GSEQLIIERPESRTAGNRETLTVGLPARHTFLFDGAGKR 358
Cdd:PRK11650  315 GGQPLVVRLPHQERPAAGSTLWLHLPANQLHLFDADTGR 353
ABC_MalK_N cd03301
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ...
 4-216 3.05e-132

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: 376.21  E-value: 3.05e-132
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037402861   4 LSLSNIVKRFGGFEIIHGANLEVKDGEFVVFVGPSGCGKSTLLRMIAGLEDITSGELQIGGRVVNDVEPADRGIAMVFQS 83
Cdd:cd03301     1 VELENVTKRFGNVTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGRDVTDLPPKDRDIAMVFQN 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037402861  84 YALYPHLTVEENLSFGLRMNGNPKADTERRVSHVAEILQITELMKRRPKQLSGGQRQRVAIGRAIVREPEVFLFDEPLSN 163
Cdd:cd03301    81 YALYPHMTVYDNIAFGLKLRKVPKDEIDERVREVAELLQIEHLLDRKPKQLSGGQRQRVALGRAIVREPKVFLMDEPLSN 160

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1037402861 164 LDAELRVQMRVEISRLHKKLGTTMIYVTHDQTEAMTLADRIVVLRAGNIEQIG 216
Cdd:cd03301   161 LDAKLRVQMRAELKRLQQRLGTTTIYVTHDQVEAMTMADRIAVMNDGQIQQIG 213
PhnT2 TIGR03265
putative 2-aminoethylphosphonate ABC transporter, ATP-binding protein; This ABC transporter ...
 1-312 1.30e-105

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: 313.90  E-value: 1.30e-105
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037402861   1 MAELSLSNIVKRFGGFEIIHGANLEVKDGEFVVFVGPSGCGKSTLLRMIAGLEDITSGELQIGGRVVNDVEPADRGIAMV 80
Cdd:TIGR03265   2 SPYLSIDNIRKRFGAFTALKDISLSVKKGEFVCLLGPSGCGKTTLLRIIAGLERQTAGTIYQGGRDITRLPPQKRDYGIV 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037402861  81 FQSYALYPHLTVEENLSFGLRMNGNPKADTERRVSHVAEILQITELMKRRPKQLSGGQRQRVAIGRAIVREPEVFLFDEP 160
Cdd:TIGR03265  82 FQSYALFPNLTVADNIAYGLKNRGMGRAEVAERVAELLDLVGLPGSERKYPGQLSGGQQQRVALARALATSPGLLLLDEP 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037402861 161 LSNLDAELRVQMRVEISRLHKKLGTTMIYVTHDQTEAMTLADRIVVLRAGNIEQIGAPLDLYDDPANQFVAGFVGspKMN 240
Cdd:TIGR03265 162 LSALDARVREHLRTEIRQLQRRLGVTTIMVTHDQEEALSMADRIVVMNHGVIEQVGTPQEIYRHPATPFVADFVG--EVN 239

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1037402861 241 FLKAVVveAQPGRAVIAlesDANMRLPLPVAAPietGAKVTLGIRPEHFVDAGMGDADLTVAIDVAEH--LGNT 312
Cdd:TIGR03265 240 WLPGTR--GGGSRARVG---GLTLACAPGLAQP---GASVRLAVRPEDIRVSPAGNAANLLLARVEDMefLGAF 305
ABC_arch_GlcV NF040933
glucose ABC transporter ATP-binding protein GlcV;
2-287 8.85e-98

glucose ABC transporter ATP-binding protein GlcV;


Pssm-ID: 468866 [Multi-domain]  Cd Length: 357  Bit Score: 294.21  E-value: 8.85e-98
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037402861   2 AELSLSNIVKRFG-GFEIIH---GANLEVKDGEFVVFVGPSGCGKSTLLRMIAGLEDITSGELQIGGRVVND-----VEP 72
Cdd:NF040933    1 VTVRVENVTKIFKkGKKEVValdNVNLEIKSGEFFGILGPSGHGKTTFLRIIAGLEVPTDGEIYFDDKLVASpgkiiVPP 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037402861  73 ADRGIAMVFQSYALYPHLTVEENLSFGLRMNGNPKADTERRVSHVAEILQITELMKRRPKQLSGGQRQRVAIGRAIVREP 152
Cdd:NF040933   81 EDRNIGMVFQNWALYPNMTVFDNIAFPLKIKKVPKDEIEKKVKEVAEILGISEVLDRYPRELSGGQQQRVALARALVKNP 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037402861 153 EVFLFDEPLSNLDAELRVQMRVEISRLHKKLGTTMIYVTHDQTEAMTLADRIVVLRAGNIEQIGAPLDLYDDPANQFVAG 232
Cdd:NF040933  161 QVLLLDEPFSNLDARIRDSARALVKKIQRELKITTIIVSHDPADIFSLADRAGVINNGKFQQVGKPEEIYDNPANIFVAR 240

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1037402861 233 FVGspKMNFLKAVVVEAQpgravialESDANMrLPLPVAAPIETGAKVTLGIRPE 287
Cdd:NF040933  241 LIG--DINLLEGKVEEEG--------LVDGND-LKIPLPNPKLEAGEVIIGIRPE 284
tungstate_WtpC NF040840
tungstate ABC transporter ATP-binding protein WtpC;
4-287 3.39e-82

tungstate ABC transporter ATP-binding protein WtpC;


Pssm-ID: 468779 [Multi-domain]  Cd Length: 347  Bit Score: 253.84  E-value: 3.39e-82
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037402861   4 LSLSNIVKRFGGFEIiHGANLEVKDGEFVVFVGPSGCGKSTLLRMIAGLEDITSGELQIGGRVVNDVEPADRGIAMVFQS 83
Cdd:NF040840    2 IRIENLSKDWKEFKL-RDISLEVKEGEYFIILGPSGAGKTVLLELIAGIWPPDSGKIYLDGKDITNLPPEKRGIAYVYQN 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037402861  84 YALYPHLTVEENLSFGLRMNGNPKADTERRVSHVAEILQITELMKRRPKQLSGGQRQRVAIGRAIVREPEVFLFDEPLSN 163
Cdd:NF040840   81 YMLFPHKTVFENIAFGLKLRKVPKEEIERKVKEIMELLGISHLLHRKPRTLSGGEQQRVALARALIIEPKLLLLDEPLSA 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037402861 164 LDAELRVQMRVEISRLHKKLGTTMIYVTHDQTEAMTLADRIVVLRAGNIEQIGAPLDLYDDPANQFVAGFVGSPkmNFLK 243
Cdd:NF040840  161 LDVQTRDELIREMKRWHREFGFTAIHVTHNFEEALSLADRVGIMLNGRLSQVGDVREVFRRPKNEFVARFVGFE--NIIE 238

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....
gi 1037402861 244 AVVVEAQPGRAVIAlesdANMRlplpVAAPIETGAKVTLGIRPE 287
Cdd:NF040840  239 GVAEKGGEGTILDT----GNIK----IELPEEKKGKVRIGIRPE 274
ABC_tran pfam00005
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ...
 19-162 1.67e-44

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: 150.11  E-value: 1.67e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037402861  19 IHGANLEVKDGEFVVFVGPSGCGKSTLLRMIAGLEDITSGELQIGGRVVNDVEPAD--RGIAMVFQSYALYPHLTVEENL 96
Cdd:pfam00005   1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDLTDDERKSlrKEIGYVFQDPQLFPRLTVRENL 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037402861  97 SFGLRMNGNPKADTERRVSHVAEILQITELMKRR----PKQLSGGQRQRVAIGRAIVREPEVFLFDEPLS 162
Cdd:pfam00005  81 RLGLLLKGLSKREKDARAEEALEKLGLGDLADRPvgerPGTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
AztA NF040873
zinc ABC transporter ATP-binding protein AztA;
12-207 4.48e-33

zinc ABC transporter ATP-binding protein AztA;


Pssm-ID: 468810 [Multi-domain]  Cd Length: 191  Bit Score: 121.57  E-value: 4.48e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037402861  12 RFGGFEIIHGANLEVKDGEFVVFVGPSGCGKSTLLRMIAGLEDITSGELQIGGrvvndvepaDRGIAMVFQSYAL---YP 88
Cdd:NF040873    1 GYGGRPVLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTVRRAG---------GARVAYVPQRSEVpdsLP 71

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037402861  89 hLTVEENLSFGL----RMNGNPKADTERRVSHVAEILQITELMKRRPKQLSGGQRQRVAIGRAIVREPEVFLFDEPLSNL 164
Cdd:NF040873   72 -LTVRDLVAMGRwarrGLWRRLTRDDRAAVDDALERVGLADLAGRQLGELSGGQRQRALLAQGLAQEADLLLLDEPTTGL 150

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 1037402861 165 DAELRVQMRVEISRLHKKlGTTMIYVTHDQTEAMtLADRIVVL 207
Cdd:NF040873  151 DAESRERIIALLAEEHAR-GATVVVVTHDLELVR-RADPCVLL 191
ABC2_perm_RbbA NF033858
ribosome-associated ATPase/putative transporter RbbA;
8-221 1.92e-20

ribosome-associated ATPase/putative transporter RbbA;


Pssm-ID: 468210 [Multi-domain]  Cd Length: 907  Bit Score: 92.88  E-value: 1.92e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037402861   8 NIVKRFGGFEIIHGANLEVKDGEFVVFVGPSGCGKSTLLRMIAGLEDITSGELQIGGRVV--NDVEpADRGIAMVFQSYA 85
Cdd:NF033858  271 GLTMRFGDFTAVDHVSFRIRRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGEAWLFGQPVdaGDIA-TRRRVGYMSQAFS 349

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037402861  86 LYPHLTVEENLSFGLRMNGNPKADTERRVSHVAEILQITELMKRRPKQLSGGQRQRVAIGRAIVREPEVFLFDEPLSNLD 165
Cdd:NF033858  350 LYGELTVRQNLELHARLFHLPAAEIAARVAEMLERFDLADVADALPDSLPLGIRQRLSLAVAVIHKPELLILDEPTSGVD 429

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037402861 166 AELR---VQMRVEISRlhkKLGTTmIYV-THDQTEAMtLADRIVVLRAGNIEQIGAPLDL 221
Cdd:NF033858  430 PVARdmfWRLLIELSR---EDGVT-IFIsTHFMNEAE-RCDRISLMHAGRVLASDTPAAL 484
ABC2_perm_RbbA NF033858
ribosome-associated ATPase/putative transporter RbbA;
5-160 4.89e-13

ribosome-associated ATPase/putative transporter RbbA;


Pssm-ID: 468210 [Multi-domain]  Cd Length: 907  Bit Score: 70.15  E-value: 4.89e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037402861   5 SLSNIVKRFGGFEIIHGANLEVKDGEFVVFVGPSGCGKSTLLRMIAGLEDITSGELQI-GGrvvnDVepADRG------- 76
Cdd:NF033858    3 RLEGVSHRYGKTVALDDVSLDIPAGCMVGLIGPDGVGKSSLLSLIAGARKIQQGRVEVlGG----DM--ADARhrravcp 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037402861  77 -IAMVFQSYA--LYPHLTVEENLSFGLRMNGNPKADTERRvshVAEILQITEL--MKRRP-KQLSGGQRQRVAIGRAIVR 150
Cdd:NF033858   77 rIAYMPQGLGknLYPTLSVFENLDFFGRLFGQDAAERRRR---IDELLRATGLapFADRPaGKLSGGMKQKLGLCCALIH 153

                         170
                  ....*....|
gi 1037402861 151 EPEVFLFDEP 160
Cdd:NF033858  154 DPDLLILDEP 163
GguA NF040905
sugar ABC transporter ATP-binding protein;
4-235 8.44e-13

sugar ABC transporter ATP-binding protein;


Pssm-ID: 468840 [Multi-domain]  Cd Length: 500  Bit Score: 69.05  E-value: 8.44e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037402861   4 LSLSNIVKRFGGFEIIHGANLEVKDGEFVVFVGPSGCGKSTLLRMIAGLEDITS--GELQIGGRVV-----NDVEpaDRG 76
Cdd:NF040905    2 LEMRGITKTFPGVKALDDVNLSVREGEIHALCGENGAGKSTLMKVLSGVYPHGSyeGEILFDGEVCrfkdiRDSE--ALG 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037402861  77 IAMVFQSYALYPHLTVEENLSFglrmnGNPKA--------DTERRVshvaeilqiTELMKR---------RPKQLSGGQR 139
Cdd:NF040905   80 IVIIHQELALIPYLSIAENIFL-----GNERAkrgvidwnETNRRA---------RELLAKvgldespdtLVTDIGVGKQ 145

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037402861 140 QRVAIGRAIVREPEVFLFDEP-----------LSNLDAELRVQmrveisrlhkklGTTMIYVTHDQTEAMTLADRIVVLR 208
Cdd:NF040905  146 QLVEIAKALSKDVKLLILDEPtaalneedsaaLLDLLLELKAQ------------GITSIIISHKLNEIRRVADSITVLR 213

                         250       260       270
                  ....*....|....*....|....*....|
gi 1037402861 209 AGN-IEQigapLDLYDDPANQ--FVAGFVG 235
Cdd:NF040905  214 DGRtIET----LDCRADEVTEdrIIRGMVG 239
40850658_otr NF000106
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
4-212 1.16e-09

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


Pssm-ID: 411078 [Multi-domain]  Cd Length: 351  Bit Score: 58.98  E-value: 1.16e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037402861   4 LSLSNIVKRFGGFEIIHGANLEVKDGEFVVFVGPSGCG--KSTLLRMIAGLE--------DITSGELQIGGRVVNDVEPA 73
Cdd:NF000106   14 VEVRGLVKHFGEVKAVDGVDLDVREGTVLGVLGP*GAA**RGALPAHV*GPDagrrpwrf*TWCANRRALRRTIG*HRPV 93

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037402861  74 DRGIAMVFQSyalyphltvEENLSFGLRMNGNPKADTERRVSHVAEILQITELMKRRPKQLSGGQRQRVAIGRAIVREPE 153
Cdd:NF000106   94 R*GRRESFSG---------RENLYMIGR*LDLSRKDARARADELLERFSLTEAAGRAAAKYSGGMRRRLDLAASMIGRPA 164

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1037402861 154 VFLFDEPLSNLDAELRVQMRVEISRLHKKlGTTMIYVTHDQTEAMTLADRIVVLRAGNI 212
Cdd:NF000106  165 VLYLDEPTTGLDPRTRNEVWDEVRSMVRD-GATVLLTTQYMEEAEQLAHELTVIDRGRV 222
AAA smart00382
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ...
 29-219 1.42e-07

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


Pssm-ID: 214640 [Multi-domain]  Cd Length: 148  Bit Score: 50.45  E-value: 1.42e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037402861   29 GEFVVFVGPSGCGKSTLLRMIAGLEDITSGELqiggrvvndvepadrgiamvfqsyalyphltveenlsfgLRMNGNPKA 108
Cdd:smart00382   2 GEVILIVGPPGSGKTTLARALARELGPPGGGV---------------------------------------IYIDGEDIL 42

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037402861  109 DTERRVSHVaeilqitELMKRRPKQLSGGQRQRVAIGRAIVREPEVFLFDEPLSNLDAELRVQMRVEIS-----RLHKKL 183
Cdd:smart00382  43 EEVLDQLLL-------IIVGGKKASGSGELRLRLALALARKLKPDVLILDEITSLLDAEQEALLLLLEElrlllLLKSEK 115

                          170       180       190
                   ....*....|....*....|....*....|....*.
gi 1037402861  184 GTTMIYVTHDQTeamTLADRIVVLRAGNIEQIGAPL 219
Cdd:smart00382 116 NLTVILTTNDEK---DLGPALLRRRFDRRIVLLLIL 148
 
Name Accession Description Interval E-value
MalK COG3839
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ...
 1-359 0e+00

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


Pssm-ID: 443050 [Multi-domain]  Cd Length: 352  Bit Score: 581.65  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037402861   1 MAELSLSNIVKRFGGFEIIHGANLEVKDGEFVVFVGPSGCGKSTLLRMIAGLEDITSGELQIGGRVVNDVEPADRGIAMV 80
Cdd:COG3839     1 MASLELENVSKSYGGVEALKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAGLEDPTSGEILIGGRDVTDLPPKDRNIAMV 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037402861  81 FQSYALYPHLTVEENLSFGLRMNGNPKADTERRVSHVAEILQITELMKRRPKQLSGGQRQRVAIGRAIVREPEVFLFDEP 160
Cdd:COG3839    81 FQSYALYPHMTVYENIAFPLKLRKVPKAEIDRRVREAAELLGLEDLLDRKPKQLSGGQRQRVALGRALVREPKVFLLDEP 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037402861 161 LSNLDAELRVQMRVEISRLHKKLGTTMIYVTHDQTEAMTLADRIVVLRAGNIEQIGAPLDLYDDPANQFVAGFVGSPKMN 240
Cdd:COG3839   161 LSNLDAKLRVEMRAEIKRLHRRLGTTTIYVTHDQVEAMTLADRIAVMNDGRIQQVGTPEELYDRPANLFVAGFIGSPPMN 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037402861 241 FLKAVVVEaqpGRAVIalesdANMRLPLPVAAPIETGAKVTLGIRPEHFVDAGMGDADLTVAIDVAEHLGNTSYIYAAIG 320
Cdd:COG3839   241 LLPGTVEG---GGVRL-----GGVRLPLPAALAAAAGGEVTLGIRPEHLRLADEGDGGLEATVEVVEPLGSETLVHVRLG 312

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|
gi 1037402861 321 SEQLIIERPESRTAGNRETLTVGLPARHTFLFDGA-GKRL 359
Cdd:COG3839   313 GQELVARVPGDTRLRPGDTVRLAFDPERLHLFDAEtGRRL 352
ugpC PRK11650
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
1-358 0e+00

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


Pssm-ID: 236947 [Multi-domain]  Cd Length: 356  Bit Score: 530.57  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037402861   1 MAELSLSNIVKRF-GGFEIIHGANLEVKDGEFVVFVGPSGCGKSTLLRMIAGLEDITSGELQIGGRVVNDVEPADRGIAM 79
Cdd:PRK11650    1 MAGLKLQAVRKSYdGKTQVIKGIDLDVADGEFIVLVGPSGCGKSTLLRMVAGLERITSGEIWIGGRVVNELEPADRDIAM 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037402861  80 VFQSYALYPHLTVEENLSFGLRMNGNPKADTERRVSHVAEILQITELMKRRPKQLSGGQRQRVAIGRAIVREPEVFLFDE 159
Cdd:PRK11650   81 VFQNYALYPHMSVRENMAYGLKIRGMPKAEIEERVAEAARILELEPLLDRKPRELSGGQRQRVAMGRAIVREPAVFLFDE 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037402861 160 PLSNLDAELRVQMRVEISRLHKKLGTTMIYVTHDQTEAMTLADRIVVLRAGNIEQIGAPLDLYDDPANQFVAGFVGSPKM 239
Cdd:PRK11650  161 PLSNLDAKLRVQMRLEIQRLHRRLKTTSLYVTHDQVEAMTLADRVVVMNGGVAEQIGTPVEVYEKPASTFVASFIGSPAM 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037402861 240 NFLkavvvEAQPGRAVIALESDANMRLPLPVAAPIETGAKVTLGIRPEHFVDAGmGDADLTVAIDVAEHLGNTSYIYAAI 319
Cdd:PRK11650  241 NLL-----DGRVSADGAAFELAGGIALPLGGGYRQYAGRKLTLGIRPEHIALSS-AEGGVPLTVDTVELLGADNLAHGRW 314

                         330       340       350
                  ....*....|....*....|....*....|....*....
gi 1037402861 320 GSEQLIIERPESRTAGNRETLTVGLPARHTFLFDGAGKR 358
Cdd:PRK11650  315 GGQPLVVRLPHQERPAAGSTLWLHLPANQLHLFDADTGR 353
PRK11000 PRK11000
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
1-359 0e+00

maltose/maltodextrin ABC transporter ATP-binding protein MalK;


Pssm-ID: 182893 [Multi-domain]  Cd Length: 369  Bit Score: 519.59  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037402861   1 MAELSLSNIVKRFGGFEIIHGANLEVKDGEFVVFVGPSGCGKSTLLRMIAGLEDITSGELQIGGRVVNDVEPADRGIAMV 80
Cdd:PRK11000    1 MASVTLRNVTKAYGDVVISKDINLDIHEGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLFIGEKRMNDVPPAERGVGMV 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037402861  81 FQSYALYPHLTVEENLSFGLRMNGNPKADTERRVSHVAEILQITELMKRRPKQLSGGQRQRVAIGRAIVREPEVFLFDEP 160
Cdd:PRK11000   81 FQSYALYPHLSVAENMSFGLKLAGAKKEEINQRVNQVAEVLQLAHLLDRKPKALSGGQRQRVAIGRTLVAEPSVFLLDEP 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037402861 161 LSNLDAELRVQMRVEISRLHKKLGTTMIYVTHDQTEAMTLADRIVVLRAGNIEQIGAPLDLYDDPANQFVAGFVGSPKMN 240
Cdd:PRK11000  161 LSNLDAALRVQMRIEISRLHKRLGRTMIYVTHDQVEAMTLADKIVVLDAGRVAQVGKPLELYHYPANRFVAGFIGSPKMN 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037402861 241 FLKAVVVEAQPGRAVIALESDANMRLPLPvAAPIETGAKVTLGIRPEHFVDAGMGDADLTVAIDVAEHLGNTSYIYAAI- 319
Cdd:PRK11000  241 FLPVKVTATAIEQVQVELPNRQQVWLPVE-GRGVQVGANMSLGIRPEHLLPSDIADVTLEGEVQVVEQLGNETQIHIQIp 319

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....
gi 1037402861 320 GSEQLIIER-PESRTAGNRETLTVGLPARHTFLF--DG-AGKRL 359
Cdd:PRK11000  320 AIRQNLVYRqNDVVLVEEGATFAIGLPPERCHLFreDGtACRRL 363
PotA COG3842
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ...
 1-352 3.65e-156

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


Pssm-ID: 443052 [Multi-domain]  Cd Length: 353  Bit Score: 442.23  E-value: 3.65e-156
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037402861   1 MAELSLSNIVKRFGGFEIIHGANLEVKDGEFVVFVGPSGCGKSTLLRMIAGLEDITSGELQIGGRVVNDVEPADRGIAMV 80
Cdd:COG3842     3 MPALELENVSKRYGDVTALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRILLDGRDVTGLPPEKRNVGMV 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037402861  81 FQSYALYPHLTVEENLSFGLRMNGNPKADTERRVSHVAEILQITELMKRRPKQLSGGQRQRVAIGRAIVREPEVFLFDEP 160
Cdd:COG3842    83 FQDYALFPHLTVAENVAFGLRMRGVPKAEIRARVAELLELVGLEGLADRYPHQLSGGQQQRVALARALAPEPRVLLLDEP 162

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037402861 161 LSNLDAELRVQMRVEISRLHKKLGTTMIYVTHDQTEAMTLADRIVVLRAGNIEQIGAPLDLYDDPANQFVAGFVGspKMN 240
Cdd:COG3842   163 LSALDAKLREEMREELRRLQRELGITFIYVTHDQEEALALADRIAVMNDGRIEQVGTPEEIYERPATRFVADFIG--EAN 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037402861 241 FLKAVVVEAQPGRAVIalesdANMRLPLPVAAPIETGAKVTLGIRPEHF-VDAGMGDADLTVAIDVAEHLGNTSYIYAAI 319
Cdd:COG3842   241 LLPGTVLGDEGGGVRT-----GGRTLEVPADAGLAAGGPVTVAIRPEDIrLSPEGPENGLPGTVEDVVFLGSHVRYRVRL 315

                         330       340       350
                  ....*....|....*....|....*....|....*.
gi 1037402861 320 GS-EQLIIERPESRTAGNR--ETLTVGLPARHTFLF 352
Cdd:COG3842   316 GDgQELVVRVPNRAALPLEpgDRVGLSWDPEDVVVL 351
ABC_MalK_N cd03301
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ...
 4-216 3.05e-132

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: 376.21  E-value: 3.05e-132
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037402861   4 LSLSNIVKRFGGFEIIHGANLEVKDGEFVVFVGPSGCGKSTLLRMIAGLEDITSGELQIGGRVVNDVEPADRGIAMVFQS 83
Cdd:cd03301     1 VELENVTKRFGNVTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGRDVTDLPPKDRDIAMVFQN 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037402861  84 YALYPHLTVEENLSFGLRMNGNPKADTERRVSHVAEILQITELMKRRPKQLSGGQRQRVAIGRAIVREPEVFLFDEPLSN 163
Cdd:cd03301    81 YALYPHMTVYDNIAFGLKLRKVPKDEIDERVREVAELLQIEHLLDRKPKQLSGGQRQRVALGRAIVREPKVFLMDEPLSN 160

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1037402861 164 LDAELRVQMRVEISRLHKKLGTTMIYVTHDQTEAMTLADRIVVLRAGNIEQIG 216
Cdd:cd03301   161 LDAKLRVQMRAELKRLQQRLGTTTIYVTHDQVEAMTMADRIAVMNDGQIQQIG 213
CysA COG1118
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ...
 3-347 6.70e-117

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


Pssm-ID: 440735 [Multi-domain]  Cd Length: 348  Bit Score: 342.51  E-value: 6.70e-117
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037402861   3 ELSLSNIVKRFGGFEIIHGANLEVKDGEFVVFVGPSGCGKSTLLRMIAGLEDITSGELQIGGRVVN-DVEPADRGIAMVF 81
Cdd:COG1118     2 SIEVRNISKRFGSFTLLDDVSLEIASGELVALLGPSGSGKTTLLRIIAGLETPDSGRIVLNGRDLFtNLPPRERRVGFVF 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037402861  82 QSYALYPHLTVEENLSFGLRMNGNPKADTERRVSHVAEILQITELMKRRPKQLSGGQRQRVAIGRAIVREPEVFLFDEPL 161
Cdd:COG1118    82 QHYALFPHMTVAENIAFGLRVRPPSKAEIRARVEELLELVQLEGLADRYPSQLSGGQRQRVALARALAVEPEVLLLDEPF 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037402861 162 SNLDAELRVQMRVEISRLHKKLGTTMIYVTHDQTEAMTLADRIVVLRAGNIEQIGAPLDLYDDPANQFVAGFVGSpkMNF 241
Cdd:COG1118   162 GALDAKVRKELRRWLRRLHDELGGTTVFVTHDQEEALELADRVVVMNQGRIEQVGTPDEVYDRPATPFVARFLGC--VNV 239

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037402861 242 LKAVVVEAQpgraviaLESDAnmrLPLPVAAPIETGAkVTLGIRPEH--FVDAGMGDADLTVAIDVAEHLGNTSYIYAAI 319
Cdd:COG1118   240 LRGRVIGGQ-------LEADG---LTLPVAEPLPDGP-AVAGVRPHDieVSREPEGENTFPATVARVSELGPEVRVELKL 308

                         330       340
                  ....*....|....*....|....*....
gi 1037402861 320 -GSEQLIIERPESRTAGNRETLTVGLPAR 347
Cdd:COG1118   309 eDGEGQPLEAEVTKEAWAELGLAPGDPVY 337
ABC_PotA_N cd03300
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ...
 4-235 1.27e-115

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: 334.98  E-value: 1.27e-115
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037402861   4 LSLSNIVKRFGGFEIIHGANLEVKDGEFVVFVGPSGCGKSTLLRMIAGLEDITSGELQIGGRVVNDVEPADRGIAMVFQS 83
Cdd:cd03300     1 IELENVSKFYGGFVALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGKDITNLPPHKRPVNTVFQN 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037402861  84 YALYPHLTVEENLSFGLRMNGNPKADTERRVSHVAEILQITELMKRRPKQLSGGQRQRVAIGRAIVREPEVFLFDEPLSN 163
Cdd:cd03300    81 YALFPHLTVFENIAFGLRLKKLPKAEIKERVAEALDLVQLEGYANRKPSQLSGGQQQRVAIARALVNEPKVLLLDEPLGA 160

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1037402861 164 LDAELRVQMRVEISRLHKKLGTTMIYVTHDQTEAMTLADRIVVLRAGNIEQIGAPLDLYDDPANQFVAGFVG 235
Cdd:cd03300   161 LDLKLRKDMQLELKRLQKELGITFVFVTHDQEEALTMSDRIAVMNKGKIQQIGTPEEIYEEPANRFVADFIG 232
potA PRK09452
spermidine/putrescine ABC transporter ATP-binding protein PotA;
4-287 5.03e-114

spermidine/putrescine ABC transporter ATP-binding protein PotA;


Pssm-ID: 236523 [Multi-domain]  Cd Length: 375  Bit Score: 336.15  E-value: 5.03e-114
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037402861   4 LSLSNIVKRFGGFEIIHGANLEVKDGEFVVFVGPSGCGKSTLLRMIAGLEDITSGELQIGGRVVNDVEPADRGIAMVFQS 83
Cdd:PRK09452   15 VELRGISKSFDGKEVISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLDGQDITHVPAENRHVNTVFQS 94

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037402861  84 YALYPHLTVEENLSFGLRMNGNPKADTERRVSHVAEILQITELMKRRPKQLSGGQRQRVAIGRAIVREPEVFLFDEPLSN 163
Cdd:PRK09452   95 YALFPHMTVFENVAFGLRMQKTPAAEITPRVMEALRMVQLEEFAQRKPHQLSGGQQQRVAIARAVVNKPKVLLLDESLSA 174

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037402861 164 LDAELRVQMRVEISRLHKKLGTTMIYVTHDQTEAMTLADRIVVLRAGNIEQIGAPLDLYDDPANQFVAGFVGspKMNFLK 243
Cdd:PRK09452  175 LDYKLRKQMQNELKALQRKLGITFVFVTHDQEEALTMSDRIVVMRDGRIEQDGTPREIYEEPKNLFVARFIG--EINIFD 252

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....
gi 1037402861 244 AVVVEAQPGRAVIAleSDANMRLPLPVAAPIETGAKVTLGIRPE 287
Cdd:PRK09452  253 ATVIERLDEQRVRA--NVEGRECNIYVNFAVEPGQKLHVLLRPE 294
ABC_Carb_Solutes_like cd03259
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ...
 4-216 1.29e-110

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: 321.39  E-value: 1.29e-110
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037402861   4 LSLSNIVKRFGGFEIIHGANLEVKDGEFVVFVGPSGCGKSTLLRMIAGLEDITSGELQIGGRVVNDVEPADRGIAMVFQS 83
Cdd:cd03259     1 LELKGLSKTYGSVRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDGRDVTGVPPERRNIGMVFQD 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037402861  84 YALYPHLTVEENLSFGLRMNGNPKADTERRVSHVAEILQITELMKRRPKQLSGGQRQRVAIGRAIVREPEVFLFDEPLSN 163
Cdd:cd03259    81 YALFPHLTVAENIAFGLKLRGVPKAEIRARVRELLELVGLEGLLNRYPHELSGGQQQRVALARALAREPSLLLLDEPLSA 160

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1037402861 164 LDAELRVQMRVEISRLHKKLGTTMIYVTHDQTEAMTLADRIVVLRAGNIEQIG 216
Cdd:cd03259   161 LDAKLREELREELKELQRELGITTIYVTHDQEEALALADRIAVMNEGRIVQVG 213
PhnT2 TIGR03265
putative 2-aminoethylphosphonate ABC transporter, ATP-binding protein; This ABC transporter ...
 1-312 1.30e-105

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: 313.90  E-value: 1.30e-105
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037402861   1 MAELSLSNIVKRFGGFEIIHGANLEVKDGEFVVFVGPSGCGKSTLLRMIAGLEDITSGELQIGGRVVNDVEPADRGIAMV 80
Cdd:TIGR03265   2 SPYLSIDNIRKRFGAFTALKDISLSVKKGEFVCLLGPSGCGKTTLLRIIAGLERQTAGTIYQGGRDITRLPPQKRDYGIV 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037402861  81 FQSYALYPHLTVEENLSFGLRMNGNPKADTERRVSHVAEILQITELMKRRPKQLSGGQRQRVAIGRAIVREPEVFLFDEP 160
Cdd:TIGR03265  82 FQSYALFPNLTVADNIAYGLKNRGMGRAEVAERVAELLDLVGLPGSERKYPGQLSGGQQQRVALARALATSPGLLLLDEP 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037402861 161 LSNLDAELRVQMRVEISRLHKKLGTTMIYVTHDQTEAMTLADRIVVLRAGNIEQIGAPLDLYDDPANQFVAGFVGspKMN 240
Cdd:TIGR03265 162 LSALDARVREHLRTEIRQLQRRLGVTTIMVTHDQEEALSMADRIVVMNHGVIEQVGTPQEIYRHPATPFVADFVG--EVN 239

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1037402861 241 FLKAVVveAQPGRAVIAlesDANMRLPLPVAAPietGAKVTLGIRPEHFVDAGMGDADLTVAIDVAEH--LGNT 312
Cdd:TIGR03265 240 WLPGTR--GGGSRARVG---GLTLACAPGLAQP---GASVRLAVRPEDIRVSPAGNAANLLLARVEDMefLGAF 305
ABC_arch_GlcV NF040933
glucose ABC transporter ATP-binding protein GlcV;
2-287 8.85e-98

glucose ABC transporter ATP-binding protein GlcV;


Pssm-ID: 468866 [Multi-domain]  Cd Length: 357  Bit Score: 294.21  E-value: 8.85e-98
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037402861   2 AELSLSNIVKRFG-GFEIIH---GANLEVKDGEFVVFVGPSGCGKSTLLRMIAGLEDITSGELQIGGRVVND-----VEP 72
Cdd:NF040933    1 VTVRVENVTKIFKkGKKEVValdNVNLEIKSGEFFGILGPSGHGKTTFLRIIAGLEVPTDGEIYFDDKLVASpgkiiVPP 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037402861  73 ADRGIAMVFQSYALYPHLTVEENLSFGLRMNGNPKADTERRVSHVAEILQITELMKRRPKQLSGGQRQRVAIGRAIVREP 152
Cdd:NF040933   81 EDRNIGMVFQNWALYPNMTVFDNIAFPLKIKKVPKDEIEKKVKEVAEILGISEVLDRYPRELSGGQQQRVALARALVKNP 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037402861 153 EVFLFDEPLSNLDAELRVQMRVEISRLHKKLGTTMIYVTHDQTEAMTLADRIVVLRAGNIEQIGAPLDLYDDPANQFVAG 232
Cdd:NF040933  161 QVLLLDEPFSNLDARIRDSARALVKKIQRELKITTIIVSHDPADIFSLADRAGVINNGKFQQVGKPEEIYDNPANIFVAR 240

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1037402861 233 FVGspKMNFLKAVVVEAQpgravialESDANMrLPLPVAAPIETGAKVTLGIRPE 287
Cdd:NF040933  241 LIG--DINLLEGKVEEEG--------LVDGND-LKIPLPNPKLEAGEVIIGIRPE 284
ABC_CysA_sulfate_importer cd03296
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ...
 3-236 2.21e-95

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: 283.85  E-value: 2.21e-95
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037402861   3 ELSLSNIVKRFGGFEIIHGANLEVKDGEFVVFVGPSGCGKSTLLRMIAGLEDITSGELQIGGRVVNDVEPADRGIAMVFQ 82
Cdd:cd03296     2 SIEVRNVSKRFGDFVALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGGEDATDVPVQERNVGFVFQ 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037402861  83 SYALYPHLTVEENLSFGLRM----NGNPKADTERRVSHVAEILQITELMKRRPKQLSGGQRQRVAIGRAIVREPEVFLFD 158
Cdd:cd03296    82 HYALFRHMTVFDNVAFGLRVkprsERPPEAEIRAKVHELLKLVQLDWLADRYPAQLSGGQRQRVALARALAVEPKVLLLD 161

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1037402861 159 EPLSNLDAELRVQMRVEISRLHKKLGTTMIYVTHDQTEAMTLADRIVVLRAGNIEQIGAPLDLYDDPANQFVAGFVGS 236
Cdd:cd03296   162 EPFGALDAKVRKELRRWLRRLHDELHVTTVFVTHDQEEALEVADRVVVMNKGRIEQVGTPDEVYDHPASPFVYSFLGE 239
potA TIGR01187
spermidine/putrescine ABC transporter ATP-binding subunit; This model describes spermidine ...
 35-287 1.23e-93

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: 282.46  E-value: 1.23e-93
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037402861  35 VGPSGCGKSTLLRMIAGLEDITSGELQIGGRVVNDVEPADRGIAMVFQSYALYPHLTVEENLSFGLRMNGNPKADTERRV 114
Cdd:TIGR01187   2 LGPSGCGKTTLLRLLAGFEQPDSGSIMLDGEDVTNVPPHLRHINMVFQSYALFPHMTVEENVAFGLKMRKVPRAEIKPRV 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037402861 115 SHVAEILQITELMKRRPKQLSGGQRQRVAIGRAIVREPEVFLFDEPLSNLDAELRVQMRVEISRLHKKLGTTMIYVTHDQ 194
Cdd:TIGR01187  82 LEALRLVQLEEFADRKPHQLSGGQQQRVALARALVFKPKILLLDEPLSALDKKLRDQMQLELKTIQEQLGITFVFVTHDQ 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037402861 195 TEAMTLADRIVVLRAGNIEQIGAPLDLYDDPANQFVAGFVGSpkMNFLKAVVVEAQPGRAVIAleSDANMRLPLPVAAPI 274
Cdd:TIGR01187 162 EEAMTMSDRIAIMRKGKIAQIGTPEEIYEEPANLFVARFIGE--INVFEATVIERKSEQVVLA--GVEGRRCDIYTDVPV 237

                         250
                  ....*....|...
gi 1037402861 275 ETGAKVTLGIRPE 287
Cdd:TIGR01187 238 EKDQPLHVVLRPE 250
fbpC PRK11432
ferric ABC transporter ATP-binding protein;
4-327 8.88e-92

ferric ABC transporter ATP-binding protein;


Pssm-ID: 183133 [Multi-domain]  Cd Length: 351  Bit Score: 278.53  E-value: 8.88e-92
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037402861   4 LSLSNIVKRFGGFEIIHGANLEVKDGEFVVFVGPSGCGKSTLLRMIAGLEDITSGELQIGGRVVNDVEPADRGIAMVFQS 83
Cdd:PRK11432    7 VVLKNITKRFGSNTVIDNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIFIDGEDVTHRSIQQRDICMVFQS 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037402861  84 YALYPHLTVEENLSFGLRMNGNPKADTERRVSHVAEILQITELMKRRPKQLSGGQRQRVAIGRAIVREPEVFLFDEPLSN 163
Cdd:PRK11432   87 YALFPHMSLGENVGYGLKMLGVPKEERKQRVKEALELVDLAGFEDRYVDQISGGQQQRVALARALILKPKVLLFDEPLSN 166

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037402861 164 LDAELRVQMRVEISRLHKKLGTTMIYVTHDQTEAMTLADRIVVLRAGNIEQIGAPLDLYDDPANQFVAGFVGspkmnflK 243
Cdd:PRK11432  167 LDANLRRSMREKIRELQQQFNITSLYVTHDQSEAFAVSDTVIVMNKGKIMQIGSPQELYRQPASRFMASFMG-------D 239

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037402861 244 AVVVEAQPGRAVIALEsdaNMRLPLPVA-APIETGAKVTLGIRPEHFVDAGMGDADLTVAIDVAEHLGNTSYIYAAIGSE 322
Cdd:PRK11432  240 ANIFPATLSGDYVDIY---GYRLPRPAAfAFNLPDGECTVGVRPEAITLSEQGEESQRCTIKHVAYMGPQYEVTVDWHGQ 316


                  ....*
gi 1037402861 323 QLIIE 327
Cdd:PRK11432  317 ELLLQ 321
3a0106s01 TIGR00968
sulfate ABC transporter, ATP-binding protein; [Transport and binding proteins, Anions]
 6-235 2.62e-91

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


Pssm-ID: 130041 [Multi-domain]  Cd Length: 237  Bit Score: 273.21  E-value: 2.62e-91
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037402861   6 LSNIVKRFGGFEIIHGANLEVKDGEFVVFVGPSGCGKSTLLRMIAGLEDITSGELQIGGRVVNDVEPADRGIAMVFQSYA 85
Cdd:TIGR00968   3 IANISKRFGSFQALDDVNLEVPTGSLVALLGPSGSGKSTLLRIIAGLEQPDSGRIRLNGQDATRVHARDRKIGFVFQHYA 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037402861  86 LYPHLTVEENLSFGLRMNGNPKADTERRVSHVAEILQITELMKRRPKQLSGGQRQRVAIGRAIVREPEVFLFDEPLSNLD 165
Cdd:TIGR00968  83 LFKHLTVRDNIAFGLEIRKHPKAKIKARVEELLELVQLEGLGDRYPNQLSGGQRQRVALARALAVEPQVLLLDEPFGALD 162

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037402861 166 AELRVQMRVEISRLHKKLGTTMIYVTHDQTEAMTLADRIVVLRAGNIEQIGAPLDLYDDPANQFVAGFVG 235
Cdd:TIGR00968 163 AKVRKELRSWLRKLHDEVHVTTVFVTHDQEEAMEVADRIVVMSNGKIEQIGSPDEVYDHPANPFVMSFLG 232
TauB COG1116
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ...
 1-210 8.44e-90

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


Pssm-ID: 440733 [Multi-domain]  Cd Length: 260  Bit Score: 270.04  E-value: 8.44e-90
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037402861   1 MAELSLSNIVKRF----GGFEIIHGANLEVKDGEFVVFVGPSGCGKSTLLRMIAGLEDITSGELQIGGRvvnDVEPADRG 76
Cdd:COG1116     5 APALELRGVSKRFptggGGVTALDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPTSGEVLVDGK---PVTGPGPD 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037402861  77 IAMVFQSYALYPHLTVEENLSFGLRMNGNPKADTERRVSHVAEILQITELMKRRPKQLSGGQRQRVAIGRAIVREPEVFL 156
Cdd:COG1116    82 RGVVFQEPALLPWLTVLDNVALGLELRGVPKAERRERARELLELVGLAGFEDAYPHQLSGGMRQRVAIARALANDPEVLL 161

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1037402861 157 FDEPLSNLDAELRVQMRVEISRLHKKLGTTMIYVTHDQTEAMTLADRIVVLRAG 210
Cdd:COG1116   162 MDEPFGALDALTRERLQDELLRLWQETGKTVLFVTHDVDEAVFLADRVVVLSAR 215
ABC_NrtD_SsuB_transporters cd03293
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ...
 4-209 6.11e-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: 261.64  E-value: 6.11e-87
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037402861   4 LSLSNIVKRFGG----FEIIHGANLEVKDGEFVVFVGPSGCGKSTLLRMIAGLEDITSGELQIGGRVVNDVEPAdrgIAM 79
Cdd:cd03293     1 LEVRNVSKTYGGgggaVTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVDGEPVTGPGPD---RGY 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037402861  80 VFQSYALYPHLTVEENLSFGLRMNGNPKADTERRVSHVAEILQITELMKRRPKQLSGGQRQRVAIGRAIVREPEVFLFDE 159
Cdd:cd03293    78 VFQQDALLPWLTVLDNVALGLELQGVPKAEARERAEELLELVGLSGFENAYPHQLSGGMRQRVALARALAVDPDVLLLDE 157

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 1037402861 160 PLSNLDAELRVQMRVEISRLHKKLGTTMIYVTHDQTEAMTLADRIVVLRA 209
Cdd:cd03293   158 PFSALDALTREQLQEELLDIWRETGKTVLLVTHDIDEAVFLADRVVVLSA 207
tungstate_WtpC NF040840
tungstate ABC transporter ATP-binding protein WtpC;
4-287 3.39e-82

tungstate ABC transporter ATP-binding protein WtpC;


Pssm-ID: 468779 [Multi-domain]  Cd Length: 347  Bit Score: 253.84  E-value: 3.39e-82
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037402861   4 LSLSNIVKRFGGFEIiHGANLEVKDGEFVVFVGPSGCGKSTLLRMIAGLEDITSGELQIGGRVVNDVEPADRGIAMVFQS 83
Cdd:NF040840    2 IRIENLSKDWKEFKL-RDISLEVKEGEYFIILGPSGAGKTVLLELIAGIWPPDSGKIYLDGKDITNLPPEKRGIAYVYQN 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037402861  84 YALYPHLTVEENLSFGLRMNGNPKADTERRVSHVAEILQITELMKRRPKQLSGGQRQRVAIGRAIVREPEVFLFDEPLSN 163
Cdd:NF040840   81 YMLFPHKTVFENIAFGLKLRKVPKEEIERKVKEIMELLGISHLLHRKPRTLSGGEQQRVALARALIIEPKLLLLDEPLSA 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037402861 164 LDAELRVQMRVEISRLHKKLGTTMIYVTHDQTEAMTLADRIVVLRAGNIEQIGAPLDLYDDPANQFVAGFVGSPkmNFLK 243
Cdd:NF040840  161 LDVQTRDELIREMKRWHREFGFTAIHVTHNFEEALSLADRVGIMLNGRLSQVGDVREVFRRPKNEFVARFVGFE--NIIE 238

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....
gi 1037402861 244 AVVVEAQPGRAVIAlesdANMRlplpVAAPIETGAKVTLGIRPE 287
Cdd:NF040840  239 GVAEKGGEGTILDT----GNIK----IELPEEKKGKVRIGIRPE 274
potG PRK11607
putrescine ABC transporter ATP-binding subunit PotG;
4-325 2.75e-81

putrescine ABC transporter ATP-binding subunit PotG;


Pssm-ID: 183226 [Multi-domain]  Cd Length: 377  Bit Score: 252.83  E-value: 2.75e-81
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037402861   4 LSLSNIVKRFGGFEIIHGANLEVKDGEFVVFVGPSGCGKSTLLRMIAGLEDITSGELQIGGRVVNDVEPADRGIAMVFQS 83
Cdd:PRK11607   20 LEIRNLTKSFDGQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVDLSHVPPYQRPINMMFQS 99

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037402861  84 YALYPHLTVEENLSFGLRMNGNPKADTERRVSHVAEILQITELMKRRPKQLSGGQRQRVAIGRAIVREPEVFLFDEPLSN 163
Cdd:PRK11607  100 YALFPHMTVEQNIAFGLKQDKLPKAEIASRVNEMLGLVHMQEFAKRKPHQLSGGQRQRVALARSLAKRPKLLLLDEPMGA 179

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037402861 164 LDAELRVQMRVEISRLHKKLGTTMIYVTHDQTEAMTLADRIVVLRAGNIEQIGAPLDLYDDPANQFVAGFVGSpkMNFLK 243
Cdd:PRK11607  180 LDKKLRDRMQLEVVDILERVGVTCVMVTHDQEEAMTMAGRIAIMNRGKFVQIGEPEEIYEHPTTRYSAEFIGS--VNVFE 257

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037402861 244 AVVVEAQPGRAVIalESDAnMRLPLPV--AAPIETGAKVTLGIRPEHFVDAGMGDAD-LTVAIDVAEH---LGNTSYIYA 317
Cdd:PRK11607  258 GVLKERQEDGLVI--DSPG-LVHPLKVdaDASVVDNVPVHVALRPEKIMLCEEPPADgCNFAVGEVIHiayLGDLSIYHV 334


                  ....*...
gi 1037402861 318 AIGSEQLI 325
Cdd:PRK11607  335 RLKSGQMI 342
PRK10851 PRK10851
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
6-286 4.45e-81

sulfate/thiosulfate ABC transporter ATP-binding protein CysA;


Pssm-ID: 182778 [Multi-domain]  Cd Length: 353  Bit Score: 251.16  E-value: 4.45e-81
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037402861   6 LSNIVKRFGGFEIIHGANLEVKDGEFVVFVGPSGCGKSTLLRMIAGLEDITSGELQIGGRVVNDVEPADRGIAMVFQSYA 85
Cdd:PRK10851    5 IANIKKSFGRTQVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFHGTDVSRLHARDRKVGFVFQHYA 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037402861  86 LYPHLTVEENLSFGLRM---NGNP-KADTERRVSHVAEILQITELMKRRPKQLSGGQRQRVAIGRAIVREPEVFLFDEPL 161
Cdd:PRK10851   85 LFRHMTVFDNIAFGLTVlprRERPnAAAIKAKVTQLLEMVQLAHLADRYPAQLSGGQKQRVALARALAVEPQILLLDEPF 164

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037402861 162 SNLDAELRVQMRVEISRLHKKLGTTMIYVTHDQTEAMTLADRIVVLRAGNIEQIGAPLDLYDDPANQFVAGFVGspKMNF 241
Cdd:PRK10851  165 GALDAQVRKELRRWLRQLHEELKFTSVFVTHDQEEAMEVADRVVVMSQGNIEQAGTPDQVWREPATRFVLEFMG--EVNR 242

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*
gi 1037402861 242 LKAVVVEAQpgraviaLESDANmRLPLPVaAPIETGaKVTLGIRP 286
Cdd:PRK10851  243 LQGTIRGGQ-------FHVGAH-RWPLGY-TPAYQG-PVDLFLRP 277
OpuBA COG1125
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and ...
 6-236 4.54e-81

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


Pssm-ID: 440742 [Multi-domain]  Cd Length: 306  Bit Score: 249.62  E-value: 4.54e-81
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037402861   6 LSNIVKRF-GGFEIIHGANLEVKDGEFVVFVGPSGCGKSTLLRMIAGLEDITSGELQIGGRVVNDVEPAD--RGIAMVFQ 82
Cdd:COG1125     4 FENVTKRYpDGTVAVDDLSLTIPAGEFTVLVGPSGCGKTTTLRMINRLIEPTSGRILIDGEDIRDLDPVElrRRIGYVIQ 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037402861  83 SYALYPHLTVEENLSFGLRMNGNPKADTERRVSHVAEILQI--TELMKRRPKQLSGGQRQRVAIGRAIVREPEVFLFDEP 160
Cdd:COG1125    84 QIGLFPHMTVAENIATVPRLLGWDKERIRARVDELLELVGLdpEEYRDRYPHELSGGQQQRVGVARALAADPPILLMDEP 163

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1037402861 161 LSNLDAELRVQMRVEISRLHKKLGTTMIYVTHDQTEAMTLADRIVVLRAGNIEQIGAPLDLYDDPANQFVAGFVGS 236
Cdd:COG1125   164 FGALDPITREQLQDELLRLQRELGKTIVFVTHDIDEALKLGDRIAVMREGRIVQYDTPEEILANPANDFVADFVGA 239
ABC_ModC_like cd03299
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ...
 4-235 6.42e-81

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: 246.86  E-value: 6.42e-81
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037402861   4 LSLSNIVKRFGGFEIiHGANLEVKDGEFVVFVGPSGCGKSTLLRMIAGLEDITSGELQIGGRVVNDVEPADRGIAMVFQS 83
Cdd:cd03299     1 LKVENLSKDWKEFKL-KNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNGKDITNLPPEKRDISYVPQN 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037402861  84 YALYPHLTVEENLSFGLRMNGNPKADTERRVSHVAEILQITELMKRRPKQLSGGQRQRVAIGRAIVREPEVFLFDEPLSN 163
Cdd:cd03299    80 YALFPHMTVYKNIAYGLKKRKVDKKEIERKVLEIAEMLGIDHLLNRKPETLSGGEQQRVAIARALVVNPKILLLDEPFSA 159

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1037402861 164 LDAELRVQMRVEISRLHKKLGTTMIYVTHDQTEAMTLADRIVVLRAGNIEQIGAPLDLYDDPANQFVAGFVG 235
Cdd:cd03299   160 LDVRTKEKLREELKKIRKEFGVTVLHVTHDFEEAWALADKVAIMLNGKLIQVGKPEEVFKKPKNEFVAEFLG 231
ABC_OpuCA_Osmoprotection cd03295
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ...
 4-238 3.26e-75

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: 232.58  E-value: 3.26e-75
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037402861   4 LSLSNIVKRF-GGFEIIHGANLEVKDGEFVVFVGPSGCGKSTLLRMIAGLEDITSGELQIGGRVVNDVEPAD--RGIAMV 80
Cdd:cd03295     1 IEFENVTKRYgGGKKAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGEDIREQDPVElrRKIGYV 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037402861  81 FQSYALYPHLTVEENLSFGLRMNGNPKADTERRVSHVAEI--LQITELMKRRPKQLSGGQRQRVAIGRAIVREPEVFLFD 158
Cdd:cd03295    81 IQQIGLFPHMTVEENIALVPKLLKWPKEKIRERADELLALvgLDPAEFADRYPHELSGGQQQRVGVARALAADPPLLLMD 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037402861 159 EPLSNLDAELRVQMRVEISRLHKKLGTTMIYVTHDQTEAMTLADRIVVLRAGNIEQIGAPLDLYDDPANQFVAGFVGSPK 238
Cdd:cd03295   161 EPFGALDPITRDQLQEEFKRLQQELGKTIVFVTHDIDEAFRLADRIAIMKNGEIVQVGTPDEILRSPANDFVAEFVGADR 240
ABC_Class3 cd03229
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ...
 4-210 2.12e-74

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: 227.84  E-value: 2.12e-74
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037402861   4 LSLSNIVKRFGGFEIIHGANLEVKDGEFVVFVGPSGCGKSTLLRMIAGLEDITSGELQIGGRVVND----VEPADRGIAM 79
Cdd:cd03229     1 LELKNVSKRYGQKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGEDLTDledeLPPLRRRIGM 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037402861  80 VFQSYALYPHLTVEENLSFGlrmngnpkadterrvshvaeilqitelmkrrpkqLSGGQRQRVAIGRAIVREPEVFLFDE 159
Cdd:cd03229    81 VFQDFALFPHLTVLENIALG----------------------------------LSGGQQQRVALARALAMDPDVLLLDE 126

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1037402861 160 PLSNLDAELRVQMRVEISRLHKKLGTTMIYVTHDQTEAMTLADRIVVLRAG 210
Cdd:cd03229   127 PTSALDPITRREVRALLKSLQAQLGITVVLVTHDLDEAARLADRVVVLRDG 177
ABC_MJ0796_LolCDE_FtsE cd03255
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ...
 4-212 8.77e-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: 227.76  E-value: 8.77e-74
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037402861   4 LSLSNIVKRFGG----FEIIHGANLEVKDGEFVVFVGPSGCGKSTLLRMIAGLEDITSGELQIGGRVVNDVEPADRG--- 76
Cdd:cd03255     1 IELKNLSKTYGGggekVQALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRVDGTDISKLSEKELAafr 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037402861  77 ---IAMVFQSYALYPHLTVEENLSFGLRMNGNPKADTERRVSHVAEILQITELMKRRPKQLSGGQRQRVAIGRAIVREPE 153
Cdd:cd03255    81 rrhIGFVFQSFNLLPDLTALENVELPLLLAGVPKKERRERAEELLERVGLGDRLNHYPSELSGGQQQRVAIARALANDPK 160

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1037402861 154 VFLFDEPLSNLDAELRVQMRVEISRLHKKLGTTMIYVTHDQTEAMtLADRIVVLRAGNI 212
Cdd:cd03255   161 IILADEPTGNLDSETGKEVMELLRELNKEAGTTIVVVTHDPELAE-YADRIIELRDGKI 218
ABC_ModC_molybdenum_transporter cd03297
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ...
 9-216 9.75e-72

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


Pssm-ID: 213264 [Multi-domain]  Cd Length: 214  Bit Score: 222.56  E-value: 9.75e-72
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037402861   9 IVKRFGGFeiihgaNLEVK---DGEFVVFVGPSGCGKSTLLRMIAGLEDITSGELQIGGRVVNDVE------PADRGIAM 79
Cdd:cd03297     6 IEKRLPDF------TLKIDfdlNEEVTGIFGASGAGKSTLLRCIAGLEKPDGGTIVLNGTVLFDSRkkinlpPQQRKIGL 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037402861  80 VFQSYALYPHLTVEENLSFGLRMngnpKADTERRVShVAEI---LQITELMKRRPKQLSGGQRQRVAIGRAIVREPEVFL 156
Cdd:cd03297    80 VFQQYALFPHLNVRENLAFGLKR----KRNREDRIS-VDELldlLGLDHLLNRYPAQLSGGEKQRVALARALAAQPELLL 154

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037402861 157 FDEPLSNLDAELRVQMRVEISRLHKKLGTTMIYVTHDQTEAMTLADRIVVLRAGNIEQIG 216
Cdd:cd03297   155 LDEPFSALDRALRLQLLPELKQIKKNLNIPVIFVTHDLSEAEYLADRIVVMEDGRLQYIG 214
ModC COG4148
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ...
 8-285 2.19e-71

ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and metabolism]; ABC-type molybdate transport system, ATPase component ModC is part of the Pathway/BioSystem: Molybdopterin biosynthesis


Pssm-ID: 443319 [Multi-domain]  Cd Length: 358  Bit Score: 226.52  E-value: 2.19e-71
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037402861   8 NIVKRFGGFEIihGANLEVKDGEFVVFVGPSGCGKSTLLRMIAGLEDITSGELQIGGRVVND------VEPADRGIAMVF 81
Cdd:COG4148     6 DFRLRRGGFTL--DVDFTLPGRGVTALFGPSGSGKTTLLRAIAGLERPDSGRIRLGGEVLQDsargifLPPHRRRIGYVF 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037402861  82 QSYALYPHLTVEENLSFGLRMNgnPKADTERRVSHVAEILQITELMKRRPKQLSGGQRQRVAIGRAIVREPEVFLFDEPL 161
Cdd:COG4148    84 QEARLFPHLSVRGNLLYGRKRA--PRAERRISFDEVVELLGIGHLLDRRPATLSGGERQRVAIGRALLSSPRLLLMDEPL 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037402861 162 SNLDAELRVQMRVEISRLHKKLGTTMIYVTHDQTEAMTLADRIVVLRAGNIEQIGAPLDLYDDPANQFVAGfvGSPKMNF 241
Cdd:COG4148   162 AALDLARKAEILPYLERLRDELDIPILYVSHSLDEVARLADHVVLLEQGRVVASGPLAEVLSRPDLLPLAG--GEEAGSV 239

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....
gi 1037402861 242 LKAVVVEAQPGRAVIALESDANmRLPLPvAAPIETGAKVTLGIR 285
Cdd:COG4148   240 LEATVAAHDPDYGLTRLALGGG-RLWVP-RLDLPPGTRVRVRIR 281
ABC_Pro_Gly_Betaine cd03294
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ...
 9-234 2.20e-70

ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This family comprises the glycine betaine/L-proline ATP binding subunit in bacteria and its equivalents in archaea. This transport system belong to the larger ATP-Binding Cassette (ABC) transporter superfamily. The characteristic feature of these transporters is the obligatory coupling of ATP hydrolysis to substrate translocation. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.


Pssm-ID: 213261 [Multi-domain]  Cd Length: 269  Bit Score: 220.98  E-value: 2.20e-70
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037402861   9 IVKRFGGFEIIHGANLEVKDGEFVVFVGPSGCGKSTLLRMIAGLEDITSGELQIGGRVVNDVEPAD------RGIAMVFQ 82
Cdd:cd03294    30 ILKKTGQTVGVNDVSLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGKVLIDGQDIAAMSRKElrelrrKKISMVFQ 109

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037402861  83 SYALYPHLTVEENLSFGLRMNGNPKADTERRVSHVAEILQITELMKRRPKQLSGGQRQRVAIGRAIVREPEVFLFDEPLS 162
Cdd:cd03294   110 SFALLPHRTVLENVAFGLEVQGVPRAEREERAAEALELVGLEGWEHKYPDELSGGMQQRVGLARALAVDPDILLMDEAFS 189

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1037402861 163 NLDAELRVQMRVEISRLHKKLGTTMIYVTHDQTEAMTLADRIVVLRAGNIEQIGAPLDLYDDPANQFVAGFV 234
Cdd:cd03294   190 ALDPLIRREMQDELLRLQAELQKTIVFITHDLDEALRLGDRIAIMKDGRLVQVGTPEEILTNPANDYVREFF 261
LolD COG1136
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
4-213 9.19e-70

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


Pssm-ID: 440751 [Multi-domain]  Cd Length: 227  Bit Score: 217.99  E-value: 9.19e-70
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037402861   4 LSLSNIVKRFG----GFEIIHGANLEVKDGEFVVFVGPSGCGKSTLLRMIAGLEDITSGELQIGGRVVNDVEPADRG--- 76
Cdd:COG1136     5 LELRNLTKSYGtgegEVTALRGVSLSIEAGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVLIDGQDISSLSERELArlr 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037402861  77 ---IAMVFQSYALYPHLTVEENLSFGLRMNGNPKADTERRVSHVAEILQITELMKRRPKQLSGGQRQRVAIGRAIVREPE 153
Cdd:COG1136    85 rrhIGFVFQFFNLLPELTALENVALPLLLAGVSRKERRERARELLERVGLGDRLDHRPSQLSGGQQQRVAIARALVNRPK 164

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037402861 154 VFLFDEPLSNLDAELRVQMRVEISRLHKKLGTTMIYVTHDQtEAMTLADRIVVLRAGNIE 213
Cdd:COG1136   165 LILADEPTGNLDSKTGEEVLELLRELNRELGTTIVMVTHDP-ELAARADRVIRLRDGRIV 223
ThiQ COG3840
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
4-235 1.35e-68

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


Pssm-ID: 443051 [Multi-domain]  Cd Length: 232  Bit Score: 215.00  E-value: 1.35e-68
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037402861   4 LSLSNIVKRFGGFEIihGANLEVKDGEFVVFVGPSGCGKSTLLRMIAGLEDITSGELQIGGRVVNDVEPADRGIAMVFQS 83
Cdd:COG3840     2 LRLDDLTYRYGDFPL--RFDLTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILWNGQDLTALPPAERPVSMLFQE 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037402861  84 YALYPHLTVEENLSFGLRMNGNPKADTERRVSHVAEILQITELMKRRPKQLSGGQRQRVAIGRAIVREPEVFLFDEPLSN 163
Cdd:COG3840    80 NNLFPHLTVAQNIGLGLRPGLKLTAEQRAQVEQALERVGLAGLLDRLPGQLSGGQRQRVALARCLVRKRPILLLDEPFSA 159

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1037402861 164 LDAELRVQMRVEISRLHKKLGTTMIYVTHDQTEAMTLADRIVVLRAGNIEQIGAPLDLYDDPANQFVAGFVG 235
Cdd:COG3840   160 LDPALRQEMLDLVDELCRERGLTVLMVTHDPEDAARIADRVLLVADGRIAADGPTAALLDGEPPPALAAYLG 231
CcmA COG1131
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
4-221 1.16e-67

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


Pssm-ID: 440746 [Multi-domain]  Cd Length: 236  Bit Score: 212.62  E-value: 1.16e-67
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037402861   4 LSLSNIVKRFGGFEIIHGANLEVKDGEFVVFVGPSGCGKSTLLRMIAGLEDITSGELQIGGR-VVNDVEPADRGIAMVFQ 82
Cdd:COG1131     1 IEVRGLTKRYGDKTALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRVLGEdVARDPAEVRRRIGYVPQ 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037402861  83 SYALYPHLTVEENLSFGLRMNGNPKADTERRVSHVAEILQITELMKRRPKQLSGGQRQRVAIGRAIVREPEVFLFDEPLS 162
Cdd:COG1131    81 EPALYPDLTVRENLRFFARLYGLPRKEARERIDELLELFGLTDAADRKVGTLSGGMKQRLGLALALLHDPELLILDEPTS 160

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1037402861 163 NLDAELRVQMRVEISRLHKKlGTTMIYVTHDQTEAMTLADRIVVLRAGNIEQIGAPLDL 221
Cdd:COG1131   161 GLDPEARRELWELLRELAAE-GKTVLLSTHYLEEAERLCDRVAIIDKGRIVADGTPDEL 218
GlnQ COG1126
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ...
 4-228 1.57e-67

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


Pssm-ID: 440743 [Multi-domain]  Cd Length: 239  Bit Score: 212.55  E-value: 1.57e-67
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037402861   4 LSLSNIVKRFGGFEIIHGANLEVKDGEFVVFVGPSGCGKSTLLRMIAGLEDITSGELQIGGRVVN----DVEPADRGIAM 79
Cdd:COG1126     2 IEIENLHKSFGDLEVLKGISLDVEKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTITVDGEDLTdskkDINKLRRKVGM 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037402861  80 VFQSYALYPHLTVEENLSFGLRM-NGNPKADTERRVSHVAEILQITELMKRRPKQLSGGQRQRVAIGRAIVREPEVFLFD 158
Cdd:COG1126    82 VFQQFNLFPHLTVLENVTLAPIKvKKMSKAEAEERAMELLERVGLADKADAYPAQLSGGQQQRVAIARALAMEPKVMLFD 161

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1037402861 159 EPLSNLDAE-----LRVqMRveisRLhKKLGTTMIYVTHDQTEAMTLADRIVVLRAGNIEQIGAPLDLYDDPANQ 228
Cdd:COG1126   162 EPTSALDPElvgevLDV-MR----DL-AKEGMTMVVVTHEMGFAREVADRVVFMDGGRIVEEGPPEEFFENPQHE 230
proV TIGR01186
glycine betaine/L-proline transport ATP binding subunit; This model describes the glycine ...
 11-235 9.19e-66

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: 212.40  E-value: 9.19e-66
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037402861  11 KRFGGFEIIHGANLEVKDGEFVVFVGPSGCGKSTLLRMIAGLEDITSGELQIGGRVVNDVEPAD------RGIAMVFQSY 84
Cdd:TIGR01186   1 KKTGGKKGVNDADLAIAKGEIFVIMGLSGSGKSTTVRMLNRLIEPTAGQIFIDGENIMKQSPVElrevrrKKIGMVFQQF 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037402861  85 ALYPHLTVEENLSFGLRMNGNPKADTERRVSHVAEILQITELMKRRPKQLSGGQRQRVAIGRAIVREPEVFLFDEPLSNL 164
Cdd:TIGR01186  81 ALFPHMTILQNTSLGPELLGWPEQERKEKALELLKLVGLEEYEHRYPDELSGGMQQRVGLARALAAEPDILLMDEAFSAL 160

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1037402861 165 DAELRVQMRVEISRLHKKLGTTMIYVTHDQTEAMTLADRIVVLRAGNIEQIGAPLDLYDDPANQFVAGFVG 235
Cdd:TIGR01186 161 DPLIRDSMQDELKKLQATLQKTIVFITHDLDEAIRIGDRIVIMKAGEIVQVGTPDEILRNPANEYVEEFIG 231
MlaF COG1127
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ...
 4-230 2.10e-64

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: 204.44  E-value: 2.10e-64
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037402861   4 LSLSNIVKRFGGFEIIHGANLEVKDGEFVVFVGPSGCGKSTLLRMIAGLEDITSGELQIGGRVVNDVEPAD-----RGIA 78
Cdd:COG1127     6 IEVRNLTKSFGDRVVLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEILVDGQDITGLSEKElyelrRRIG 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037402861  79 MVFQSYALYPHLTVEENLSFGLRMNGN-PKADTERRVSHVAEILQITELMKRRPKQLSGGQRQRVAIGRAIVREPEVFLF 157
Cdd:COG1127    86 MLFQGGALFDSLTVFENVAFPLREHTDlSEAEIRELVLEKLELVGLPGAADKMPSELSGGMRKRVALARALALDPEILLY 165

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037402861 158 DEPLSNLD-------AELrvqmrveISRLHKKLGTTMIYVTHDQTEAMTLADRIVVLRAGNIEQIGAPLDLY--DDPA-N 227
Cdd:COG1127   166 DEPTAGLDpitsaviDEL-------IRELRDELGLTSVVVTHDLDSAFAIADRVAVLADGKIIAEGTPEELLasDDPWvR 238


                  ...
gi 1037402861 228 QFV 230
Cdd:COG1127   239 QFL 241
EcfA2 COG1122
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ...
 14-225 2.55e-63

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: 201.41  E-value: 2.55e-63
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037402861  14 GGFEIIHGANLEVKDGEFVVFVGPSGCGKSTLLRMIAGLEDITSGELQIGGRVVNDVEPAD--RGIAMVFQsyalYP--- 88
Cdd:COG1122    12 GGTPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVDGKDITKKNLRElrRKVGLVFQ----NPddq 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037402861  89 --HLTVEENLSFGLRMNGNPKADTERRVSHVAEILQITELMKRRPKQLSGGQRQRVAIGRAIVREPEVFLFDEPLSNLDA 166
Cdd:COG1122    88 lfAPTVEEDVAFGPENLGLPREEIRERVEEALELVGLEHLADRPPHELSGGQKQRVAIAGVLAMEPEVLVLDEPTAGLDP 167

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1037402861 167 ELRVQMRVEISRLHKKlGTTMIYVTHDQTEAMTLADRIVVLRAGNIEQIGAPLDLYDDP 225
Cdd:COG1122   168 RGRRELLELLKRLNKE-GKTVIIVTHDLDLVAELADRVIVLDDGRIVADGTPREVFSDY 225
DppF COG1124
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ...
 4-227 4.03e-63

ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid transport and metabolism, Inorganic ion transport and metabolism];


Pssm-ID: 440741 [Multi-domain]  Cd Length: 248  Bit Score: 201.57  E-value: 4.03e-63
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037402861   4 LSLSNIVKRFG----GFEIIHGANLEVKDGEFVVFVGPSGCGKSTLLRMIAGLEDITSGELQIGGRVVNDVEPAD--RGI 77
Cdd:COG1124     2 LEVRNLSVSYGqggrRVPVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVTFDGRPVTRRRRKAfrRRV 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037402861  78 AMVFQSY--ALYPHLTVEENLSFGLRMNGNPkaDTERRVSHVAEILQIT-ELMKRRPKQLSGGQRQRVAIGRAIVREPEV 154
Cdd:COG1124    82 QMVFQDPyaSLHPRHTVDRILAEPLRIHGLP--DREERIAELLEQVGLPpSFLDRYPHQLSGGQRQRVAIARALILEPEL 159

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1037402861 155 FLFDEPLSNLDAELRVQMRVEISRLHKKLGTTMIYVTHDQTEAMTLADRIVVLRAGNIEQIGAPLDLYDDPAN 227
Cdd:COG1124   160 LLLDEPTSALDVSVQAEILNLLKDLREERGLTYLFVSHDLAVVAHLCDRVAVMQNGRIVEELTVADLLAGPKH 232
glnQ PRK09493
glutamine ABC transporter ATP-binding protein GlnQ;
6-233 2.02e-62

glutamine ABC transporter ATP-binding protein GlnQ;


Pssm-ID: 181906 [Multi-domain]  Cd Length: 240  Bit Score: 199.55  E-value: 2.02e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037402861   6 LSNIVKRFGGFEIIHGANLEVKDGEFVVFVGPSGCGKSTLLRMIAGLEDITSGELQIGGRVVNDVEPADRGI----AMVF 81
Cdd:PRK09493    4 FKNVSKHFGPTQVLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGLKVNDPKVDERLIrqeaGMVF 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037402861  82 QSYALYPHLTVEENLSFG-LRMNGNPKADTERRVSHVAEILQITELMKRRPKQLSGGQRQRVAIGRAIVREPEVFLFDEP 160
Cdd:PRK09493   84 QQFYLFPHLTALENVMFGpLRVRGASKEEAEKQARELLAKVGLAERAHHYPSELSGGQQQRVAIARALAVKPKLMLFDEP 163

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1037402861 161 LSNLDAELrvqmRVEISRLHKKL---GTTMIYVTHDQTEAMTLADRIVVLRAGNIEQIGAPLDLYDDPANQFVAGF 233
Cdd:PRK09493  164 TSALDPEL----RHEVLKVMQDLaeeGMTMVIVTHEIGFAEKVASRLIFIDKGRIAEDGDPQVLIKNPPSQRLQEF 235
ABC_cobalt_CbiO_domain1 cd03225
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ...
 5-210 2.65e-62

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: 198.07  E-value: 2.65e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037402861   5 SLSNIVKRFGGFE--IIHGANLEVKDGEFVVFVGPSGCGKSTLLRMIAGLEDITSGELQIGGRVVNDVEPADRG--IAMV 80
Cdd:cd03225     1 ELKNLSFSYPDGArpALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDLTKLSLKELRrkVGLV 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037402861  81 FQsyalYP-----HLTVEENLSFGLRMNGNPKADTERRVSHVAEILQITELMKRRPKQLSGGQRQRVAIGRAIVREPEVF 155
Cdd:cd03225    81 FQ----NPddqffGPTVEEEVAFGLENLGLPEEEIEERVEEALELVGLEGLRDRSPFTLSGGQKQRVAIAGVLAMDPDIL 156

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1037402861 156 LFDEPLSNLDAELRVQMRVEISRLHKKlGTTMIYVTHDQTEAMTLADRIVVLRAG 210
Cdd:cd03225   157 LLDEPTAGLDPAGRRELLELLKKLKAE-GKTIIIVTHDLDLLLELADRVIVLEDG 210
ABC_HisP_GlnQ cd03262
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ...
 4-212 4.69e-62

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: 197.75  E-value: 4.69e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037402861   4 LSLSNIVKRFGGFEIIHGANLEVKDGEFVVFVGPSGCGKSTLLRMIAGLEDITSGELQIGGRVVNDVEPA----DRGIAM 79
Cdd:cd03262     1 IEIKNLHKSFGDFHVLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIDGLKLTDDKKNinelRQKVGM 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037402861  80 VFQSYALYPHLTVEENLSFGLR-MNGNPKADTERRVSHVAEILQITELMKRRPKQLSGGQRQRVAIGRAIVREPEVFLFD 158
Cdd:cd03262    81 VFQQFNLFPHLTVLENITLAPIkVKGMSKAEAEERALELLEKVGLADKADAYPAQLSGGQQQRVAIARALAMNPKVMLFD 160

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1037402861 159 EPLSNLDAELrVQMRVEISRLHKKLGTTMIYVTHDQTEAMTLADRIVVLRAGNI 212
Cdd:cd03262   161 EPTSALDPEL-VGEVLDVMKDLAEEGMTMVVVTHEMGFAREVADRVIFMDDGRI 213
FtsE COG2884
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
4-212 4.49e-60

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


Pssm-ID: 442130 [Multi-domain]  Cd Length: 223  Bit Score: 192.96  E-value: 4.49e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037402861   4 LSLSNIVKRF-GGFEIIHGANLEVKDGEFVVFVGPSGCGKSTLLRMIAGLEDITSGELQIGGRVVNDVEPAD-----RGI 77
Cdd:COG2884     2 IRFENVSKRYpGGREALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLVNGQDLSRLKRREipylrRRI 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037402861  78 AMVFQSYALYPHLTVEENLSFGLRMNGNPKADTERRVSHVAEILQITELMKRRPKQLSGGQRQRVAIGRAIVREPEVFLF 157
Cdd:COG2884    82 GVVFQDFRLLPDRTVYENVALPLRVTGKSRKEIRRRVREVLDLVGLSDKAKALPHELSGGEQQRVAIARALVNRPELLLA 161

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1037402861 158 DEPLSNLDAELRVQ-MRV--EISRlhkkLGTTMIYVTHDQTEAMTLADRIVVLRAGNI 212
Cdd:COG2884   162 DEPTGNLDPETSWEiMELleEINR----RGTTVLIATHDLELVDRMPKRVLELEDGRL 215
ABC_Org_Solvent_Resistant cd03261
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ...
 4-229 2.58e-59

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: 191.18  E-value: 2.58e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037402861   4 LSLSNIVKRFGGFEIIHGANLEVKDGEFVVFVGPSGCGKSTLLRMIAGLEDITSGELQIGGRVVNDVEPAD-----RGIA 78
Cdd:cd03261     1 IELRGLTKSFGGRTVLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGEDISGLSEAElyrlrRRMG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037402861  79 MVFQSYALYPHLTVEENLSFGLRMNGN-PKADTERRVSHVAEILQITELMKRRPKQLSGGQRQRVAIGRAIVREPEVFLF 157
Cdd:cd03261    81 MLFQSGALFDSLTVFENVAFPLREHTRlSEEEIREIVLEKLEAVGLRGAEDLYPAELSGGMKKRVALARALALDPELLLY 160

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1037402861 158 DEPLSNLD---AELRVQMrveISRLHKKLGTTMIYVTHDQTEAMTLADRIVVLRAGNIEQIGAPLDLY--DDPA-NQF 229
Cdd:cd03261   161 DEPTAGLDpiaSGVIDDL---IRSLKKELGLTSIMVTHDLDTAFAIADRIAVLYDGKIVAEGTPEELRasDDPLvRQF 235
GsiA COG1123
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ...
 4-225 7.34e-59

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: 198.20  E-value: 7.34e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037402861   4 LSLSNIVKRF-----GGFEIIHGANLEVKDGEFVVFVGPSGCGKSTLLRMIAGLEDITSGELQIGGRVVNDVEPAD---- 74
Cdd:COG1123   261 LEVRNLSKRYpvrgkGGVRAVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRPTSGSILFDGKDLTKLSRRSlrel 340

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037402861  75 -RGIAMVFQ--SYALYPHLTVEENLSFGLRMNGN-PKADTERRvshVAEILQI----TELMKRRPKQLSGGQRQRVAIGR 146
Cdd:COG1123   341 rRRVQMVFQdpYSSLNPRMTVGDIIAEPLRLHGLlSRAERRER---VAELLERvglpPDLADRYPHELSGGQRQRVAIAR 417

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1037402861 147 AIVREPEVFLFDEPLSNLDAELRVQMRVEISRLHKKLGTTMIYVTHDQTEAMTLADRIVVLRAGNIEQIGAPLDLYDDP 225
Cdd:COG1123   418 ALALEPKLLILDEPTSALDVSVQAQILNLLRDLQRELGLTYLFISHDLAVVRYIADRVAVMYDGRIVEDGPTEEVFANP 496
FetA COG4619
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
4-212 4.28e-58

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


Pssm-ID: 443661 [Multi-domain]  Cd Length: 209  Bit Score: 187.33  E-value: 4.28e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037402861   4 LSLSNIVKRFGGFEIIHGANLEVKDGEFVVFVGPSGCGKSTLLRMIAGLEDITSGELQIGGRVVNDVEPAD--RGIAMVF 81
Cdd:COG4619     1 LELEGLSFRVGGKPILSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIYLDGKPLSAMPPPEwrRQVAYVP 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037402861  82 QSYALYPHlTVEENLSFGLRMNGnpKADTERRVSHVAEILQITE-LMKRRPKQLSGGQRQRVAIGRAIVREPEVFLFDEP 160
Cdd:COG4619    81 QEPALWGG-TVRDNLPFPFQLRE--RKFDRERALELLERLGLPPdILDKPVERLSGGERQRLALIRALLLQPDVLLLDEP 157

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1037402861 161 LSNLDAELRVqmRVE--ISRLHKKLGTTMIYVTHDQTEAMTLADRIVVLRAGNI 212
Cdd:COG4619   158 TSALDPENTR--RVEelLREYLAEEGRAVLWVSHDPEQIERVADRVLTLEAGRL 209
TauB COG4525
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
1-232 2.41e-57

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


Pssm-ID: 443596 [Multi-domain]  Cd Length: 262  Bit Score: 186.99  E-value: 2.41e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037402861   1 MAELSLSNIVKRFGGF----EIIHGANLEVKDGEFVVFVGPSGCGKSTLLRMIAGLEDITSGELQIGGRVVNDveP-ADR 75
Cdd:COG4525     1 MSMLTVRHVSVRYPGGgqpqPALQDVSLTIESGEFVVALGASGCGKTTLLNLIAGFLAPSSGEITLDGVPVTG--PgADR 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037402861  76 GIamVFQSYALYPHLTVEENLSFGLRMNGNPKADTERRVSHVAEILQITELMKRRPKQLSGGQRQRVAIGRAIVREPEVF 155
Cdd:COG4525    79 GV--VFQKDALLPWLNVLDNVAFGLRLRGVPKAERRARAEELLALVGLADFARRRIWQLSGGMRQRVGIARALAADPRFL 156

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1037402861 156 LFDEPLSNLDAELRVQMRVEISRLHKKLGTTMIYVTHDQTEAMTLADRIVVLrAGNIEQIGAPLDLydDPANQFVAG 232
Cdd:COG4525   157 LMDEPFGALDALTREQMQELLLDVWQRTGKGVFLITHSVEEALFLATRLVVM-SPGPGRIVERLEL--DFSRRFLAG 230
PhnC COG3638
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and ...
 4-229 2.61e-57

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


Pssm-ID: 442855 [Multi-domain]  Cd Length: 249  Bit Score: 186.42  E-value: 2.61e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037402861   4 LSLSNIVKRF-GGFEIIHGANLEVKDGEFVVFVGPSGCGKSTLLRMIAGLEDITSGELQIGGRVVNDVEPAD-----RGI 77
Cdd:COG3638     3 LELRNLSKRYpGGTPALDDVSLEIERGEFVALIGPSGAGKSTLLRCLNGLVEPTSGEILVDGQDVTALRGRAlrrlrRRI 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037402861  78 AMVFQSYALYPHLTVEENLSFGL--RMNG-------NPKADTERrvshVAEILQ---ITELMKRRPKQLSGGQRQRVAIG 145
Cdd:COG3638    83 GMIFQQFNLVPRLSVLTNVLAGRlgRTSTwrsllglFPPEDRER----ALEALErvgLADKAYQRADQLSGGQQQRVAIA 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037402861 146 RAIVREPEVFLFDEPLSNLDAEL-RVQMRVeISRLHKKLGTTMIYVTHDQTEAMTLADRIVVLRAGNIeqigapldLYDD 224
Cdd:COG3638   159 RALVQEPKLILADEPVASLDPKTaRQVMDL-LRRIAREDGITVVVNLHQVDLARRYADRIIGLRDGRV--------VFDG 229


                  ....*
gi 1037402861 225 PANQF 229
Cdd:COG3638   230 PPAEL 234
FepC COG1120
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ...
 4-218 2.71e-57

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: 186.79  E-value: 2.71e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037402861   4 LSLSNIVKRFGGFEIIHGANLEVKDGEFVVFVGPSGCGKSTLLRMIAGLEDITSGELQIGGRVVNDVEPADRG--IAMVF 81
Cdd:COG1120     2 LEAENLSVGYGGRPVLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDGRDLASLSRRELArrIAYVP 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037402861  82 QSYALYPHLTVEENLSFG----LRMNGNPKADTERRVSHVAEILQITELMKRRPKQLSGGQRQRVAIGRAIVREPEVFLF 157
Cdd:COG1120    82 QEPPAPFGLTVRELVALGryphLGLFGRPSAEDREAVEEALERTGLEHLADRPVDELSGGERQRVLIARALAQEPPLLLL 161

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1037402861 158 DEPLSNLDaeLRVQMRV--EISRLHKKLGTTMIYVTHDQTEAMTLADRIVVLRAGNIEQIGAP 218
Cdd:COG1120   162 DEPTSHLD--LAHQLEVleLLRRLARERGRTVVMVLHDLNLAARYADRLVLLKDGRIVAQGPP 222
NatA COG4555
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ...
 4-249 3.10e-57

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


Pssm-ID: 443618 [Multi-domain]  Cd Length: 243  Bit Score: 186.22  E-value: 3.10e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037402861   4 LSLSNIVKRFGGFEIIHGANLEVKDGEFVVFVGPSGCGKSTLLRMIAGLEDITSGELQIGGR-VVNDVEPADRGIAMVFQ 82
Cdd:COG4555     2 IEVENLSKKYGKVPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIDGEdVRKEPREARRQIGVLPD 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037402861  83 SYALYPHLTVEENLSFGLRMNGNPKADTERRVSHVAEILQITELMKRRPKQLSGGQRQRVAIGRAIVREPEVFLFDEPLS 162
Cdd:COG4555    82 ERGLYDRLTVRENIRYFAELYGLFDEELKKRIEELIELLGLEEFLDRRVGELSTGMKKKVALARALVHDPKVLLLDEPTN 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037402861 163 NLDAELRVQMRvEISRLHKKLGTTMIYVTHDQTEAMTLADRIVVLRAGNIeqigapldLYDDPANQFVAGFVGSPkmnfL 242
Cdd:COG4555   162 GLDVMARRLLR-EILRALKKEGKTVLFSSHIMQEVEALCDRVVILHKGKV--------VAQGSLDELREEIGEEN----L 228


                  ....*..
gi 1037402861 243 KAVVVEA 249
Cdd:COG4555   229 EDAFVAL 235
ABC_NikE_OppD_transporters cd03257
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ...
 4-216 4.85e-57

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: 185.40  E-value: 4.85e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037402861   4 LSLSNIVKRF----GGFEIIHGANLEVKDGEFVVFVGPSGCGKSTLLRMIAGLEDITSGELQIGGRVVNDVEPADRG--- 76
Cdd:cd03257     2 LEVKNLSVSFptggGSVKALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGKDLLKLSRRLRKirr 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037402861  77 --IAMVFQSY--ALYPHLTVEENLSFGLRMNGNPKADTERRVSHVAEILQI---TELMKRRPKQLSGGQRQRVAIGRAIV 149
Cdd:cd03257    82 keIQMVFQDPmsSLNPRMTIGEQIAEPLRIHGKLSKKEARKEAVLLLLVGVglpEEVLNRYPHELSGGQRQRVAIARALA 161

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1037402861 150 REPEVFLFDEPLSNLDAELRVQMRVEISRLHKKLGTTMIYVTHDQTEAMTLADRIVVLRAGNIEQIG 216
Cdd:cd03257   162 LNPKLLIADEPTSALDVSVQAQILDLLKKLQEELGLTLLFITHDLGVVAKIADRVAVMYAGKIVEEG 228
modC_ABC TIGR02142
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ...
 8-258 7.86e-54

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: 181.08  E-value: 7.86e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037402861   8 NIVKRFGGFEIihGANLEVKDGEFVVFVGPSGCGKSTLLRMIAGLEDITSGELQIGGRVVNDVE------PADRGIAMVF 81
Cdd:TIGR02142   4 RFSKRLGDFSL--DADFTLPGQGVTAIFGRSGSGKTTLIRLIAGLTRPDEGEIVLNGRTLFDSRkgiflpPEKRRIGYVF 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037402861  82 QSYALYPHLTVEENLSFGLRmngnpKAD-TERRVS--HVAEILQITELMKRRPKQLSGGQRQRVAIGRAIVREPEVFLFD 158
Cdd:TIGR02142  82 QEARLFPHLSVRGNLRYGMK-----RARpSERRISfeRVIELLGIGHLLGRLPGRLSGGEKQRVAIGRALLSSPRLLLMD 156

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037402861 159 EPLSNLDAELRVQMRVEISRLHKKLGTTMIYVTHDQTEAMTLADRIVVLRAGNIEQIGAPLDLYDDPANQFVAgfvGSPK 238
Cdd:TIGR02142 157 EPLAALDDPRKYEILPYLERLHAEFGIPILYVSHSLQEVLRLADRVVVLEDGRVAAAGPIAEVWASPDLPWLA---REDQ 233

                         250       260
                  ....*....|....*....|
gi 1037402861 239 MNFLKAVVVEAQPGRAVIAL 258
Cdd:TIGR02142 234 GSLIEGVVAEHDQHYGLTAL 253
ABC_DR_subfamily_A cd03230
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ...
 4-212 6.91e-53

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: 172.58  E-value: 6.91e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037402861   4 LSLSNIVKRFGGFEIIHGANLEVKDGEFVVFVGPSGCGKSTLLRMIAGLEDITSGELQI-GGRVVNDVEPADRGIAMVFQ 82
Cdd:cd03230     1 IEVRNLSKRYGKKTALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVlGKDIKKEPEEVKRRIGYLPE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037402861  83 SYALYPHLTVEENLsfglrmngnpkadterrvshvaeilqitelmkrrpkQLSGGQRQRVAIGRAIVREPEVFLFDEPLS 162
Cdd:cd03230    81 EPSLYENLTVRENL------------------------------------KLSGGMKQRLALAQALLHDPELLILDEPTS 124

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 1037402861 163 NLDAELRVQMRVEISRLHKKlGTTMIYVTHDQTEAMTLADRIVVLRAGNI 212
Cdd:cd03230   125 GLDPESRREFWELLRELKKE-GKTILLSSHILEEAERLCDRVAILNNGRI 173
AbcC COG1135
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
4-237 1.00e-52

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


Pssm-ID: 440750 [Multi-domain]  Cd Length: 339  Bit Score: 177.58  E-value: 1.00e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037402861   4 LSLSNIVKRF----GGFEIIHGANLEVKDGEfvVF--VGPSGCGKSTLLRMIAGLEDITSGELQIGGRVVNDVEPAD--- 74
Cdd:COG1135     2 IELENLSKTFptkgGPVTALDDVSLTIEKGE--IFgiIGYSGAGKSTLIRCINLLERPTSGSVLVDGVDLTALSERElra 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037402861  75 --RGIAMVFQSYALYPHLTVEENLSFGLRMNGNPKADTERRVshvAEILQITEL---MKRRPKQLSGGQRQRVAIGRAIV 149
Cdd:COG1135    80 arRKIGMIFQHFNLLSSRTVAENVALPLEIAGVPKAEIRKRV---AELLELVGLsdkADAYPSQLSGGQKQRVGIARALA 156

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037402861 150 REPEVFLFDEPLSNLDAE-----LRVqmrveISRLHKKLGTTMIYVTHDqteaM----TLADRIVVLRAGNIEQIGAPLD 220
Cdd:COG1135   157 NNPKVLLCDEATSALDPEttrsiLDL-----LKDINRELGLTIVLITHE----MdvvrRICDRVAVLENGRIVEQGPVLD 227

                         250
                  ....*....|....*..
gi 1037402861 221 LYDDPANQFVAGFVGSP 237
Cdd:COG1135   228 VFANPQSELTRRFLPTV 244
GsiA COG1123
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ...
 4-226 1.67e-52

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: 181.25  E-value: 1.67e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037402861   4 LSLSNIVKRF--GGFEIIHGANLEVKDGEFVVFVGPSGCGKSTLLRMIAGLEDIT---SGELQIGGRVVNDVEPADRG-- 76
Cdd:COG1123     5 LEVRDLSVRYpgGDVPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGLLPHGgriSGEVLLDGRDLLELSEALRGrr 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037402861  77 IAMVFQS--YALYPhLTVEENLSFGLRMNGNPKADTERRVSHVAEILQITELMKRRPKQLSGGQRQRVAIGRAIVREPEV 154
Cdd:COG1123    85 IGMVFQDpmTQLNP-VTVGDQIAEALENLGLSRAEARARVLELLEAVGLERRLDRYPHQLSGGQRQRVAIAMALALDPDL 163

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1037402861 155 FLFDEPLSNLDAELRVQMRVEISRLHKKLGTTMIYVTHDQTEAMTLADRIVVLRAGNIEQIGAPLDLYDDPA 226
Cdd:COG1123   164 LIADEPTTALDVTTQAEILDLLRELQRERGTTVLLITHDLGVVAEIADRVVVMDDGRIVEDGPPEEILAAPQ 235
ABC_ThiQ_thiamine_transporter cd03298
ATP-binding cassette domain of the thiamine transport system; Part of the ...
 24-212 2.46e-52

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: 172.68  E-value: 2.46e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037402861  24 LEVKDGEFVVFVGPSGCGKSTLLRMIAGLEDITSGELQIGGRVVNDVEPADRGIAMVFQSYALYPHLTVEENLSFGLRMN 103
Cdd:cd03298    19 LTFAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLINGVDVTAAPPADRPVSMLFQENNLFAHLTVEQNVGLGLSPG 98

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037402861 104 GNPKADTERRVSHVAEILQITELMKRRPKQLSGGQRQRVAIGRAIVREPEVFLFDEPLSNLDAELRVQMRVEISRLHKKL 183
Cdd:cd03298    99 LKLTAEDRQAIEVALARVGLAGLEKRLPGELSGGERQRVALARVLVRDKPVLLLDEPFAALDPALRAEMLDLVLDLHAET 178

                         170       180
                  ....*....|....*....|....*....
gi 1037402861 184 GTTMIYVTHDQTEAMTLADRIVVLRAGNI 212
Cdd:cd03298   179 KMTVLMVTHQPEDAKRLAQRVVFLDNGRI 207
ABC_PstB_phosphate_transporter cd03260
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ...
 4-216 9.22e-52

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: 171.59  E-value: 9.22e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037402861   4 LSLSNIVKRFGGFEIIHGANLEVKDGEFVVFVGPSGCGKSTLLRMIAGLEDI-----TSGELQIGGRVVNDVEPAD---- 74
Cdd:cd03260     1 IELRDLNVYYGDKHALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRLNDLipgapDEGEVLLDGKDIYDLDVDVlelr 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037402861  75 RGIAMVFQSYALYPhLTVEENLSFGLRMNG-NPKADTERRVSHVAEILQITELMKRR--PKQLSGGQRQRVAIGRAIVRE 151
Cdd:cd03260    81 RRVGMVFQKPNPFP-GSIYDNVAYGLRLHGiKLKEELDERVEEALRKAALWDEVKDRlhALGLSGGQQQRLCLARALANE 159

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1037402861 152 PEVFLFDEPLSNLDAELRvqMRVE--ISRLHKKlgTTMIYVTHDQTEAMTLADRIVVLRAGNIEQIG 216
Cdd:cd03260   160 PEVLLLDEPTSALDPIST--AKIEelIAELKKE--YTIVIVTHNMQQAARVADRTAFLLNGRLVEFG 222
FtsE TIGR02673
cell division ATP-binding protein FtsE; This model describes FtsE, a member of the ABC ...
 1-210 2.09e-51

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: 170.12  E-value: 2.09e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037402861   1 MAELSlsNIVKRF-GGFEIIHGANLEVKDGEFVVFVGPSGCGKSTLLRMIAGLEDITSGELQIGGRVVNDVEPAD----- 74
Cdd:TIGR02673   1 MIEFH--NVSKAYpGGVAALHDVSLHIRKGEFLFLTGPSGAGKTTLLKLLYGALTPSRGQVRIAGEDVNRLRGRQlpllr 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037402861  75 RGIAMVFQSYALYPHLTVEENLSFGLRMNGNPKADTERRVSHVAEILQITELMKRRPKQLSGGQRQRVAIGRAIVREPEV 154
Cdd:TIGR02673  79 RRIGVVFQDFRLLPDRTVYENVALPLEVRGKKEREIQRRVGAALRQVGLEHKADAFPEQLSGGEQQRVAIARAIVNSPPL 158

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1037402861 155 FLFDEPLSNLDAELRVQ-MRVeISRLHkKLGTTMIYVTHDQTEAMTLADRIVVLRAG 210
Cdd:TIGR02673 159 LLADEPTGNLDPDLSERiLDL-LKRLN-KRGTTVIVATHDLSLVDRVAHRVIILDDG 213
ABC_PhnC_transporter cd03256
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ...
 4-224 3.04e-51

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: 170.83  E-value: 3.04e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037402861   4 LSLSNIVKRFG-GFEIIHGANLEVKDGEFVVFVGPSGCGKSTLLRMIAGLEDITSGELQIGGRVVNDVEPAD-----RGI 77
Cdd:cd03256     1 IEVENLSKTYPnGKKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGTDINKLKGKAlrqlrRQI 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037402861  78 AMVFQSYALYPHLTVEENLSFGL--RMN-------GNPKADTErRVSHVAEILQITELMKRRPKQLSGGQRQRVAIGRAI 148
Cdd:cd03256    81 GMIFQQFNLIERLSVLENVLSGRlgRRStwrslfgLFPKEEKQ-RALAALERVGLLDKAYQRADQLSGGQQQRVAIARAL 159

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1037402861 149 VREPEVFLFDEPLSNLDAELRVQ-MRVeISRLHKKLGTTMIYVTHDQTEAMTLADRIVVLRAGNIEQIGAPLDLYDD 224
Cdd:cd03256   160 MQQPKLILADEPVASLDPASSRQvMDL-LKRINREEGITVIVSLHQVDLAREYADRIVGLKDGRIVFDGPPAELTDE 235
HisP COG4598
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism];
4-232 5.00e-51

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


Pssm-ID: 443652 [Multi-domain]  Cd Length: 259  Bit Score: 170.75  E-value: 5.00e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037402861   4 LSLSNIVKRFGGFEIIHGANLEVKDGEFVVFVGPSGCGKSTLLRMIAGLEDITSGELQIGGRVV-------NDVEPADR- 75
Cdd:COG4598     9 LEVRDLHKSFGDLEVLKGVSLTARKGDVISIIGSSGSGKSTFLRCINLLETPDSGEIRVGGEEIrlkpdrdGELVPADRr 88

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037402861  76 -------GIAMVFQSYALYPHLTVEENLSFG-LRMNGNPKADTERRVSHVAEILQITELMKRRPKQLSGGQRQRVAIGRA 147
Cdd:COG4598    89 qlqrirtRLGMVFQSFNLWSHMTVLENVIEApVHVLGRPKAEAIERAEALLAKVGLADKRDAYPAHLSGGQQQRAAIARA 168

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037402861 148 IVREPEVFLFDEPLSNLDAELrVQmrvEISRLHKKL---GTTMIYVTHDQTEAMTLADRIVVLRAGNIEQIGAPLDLYDD 224
Cdd:COG4598   169 LAMEPEVMLFDEPTSALDPEL-VG---EVLKVMRDLaeeGRTMLVVTHEMGFARDVSSHVVFLHQGRIEEQGPPAEVFGN 244

                         250
                  ....*....|..
gi 1037402861 225 PAN----QFVAG 232
Cdd:COG4598   245 PKSerlrQFLSS 256
ArtP COG4161
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
3-212 1.40e-50

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


Pssm-ID: 443326 [Multi-domain]  Cd Length: 242  Bit Score: 169.04  E-value: 1.40e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037402861   3 ELSLSNIVKRFGGFEIIHGANLEVKDGEFVVFVGPSGCGKSTLLRMIAGLEDITSGELQIGGRVVNDVEPAD-------- 74
Cdd:COG4161     2 SIQLKNINCFYGSHQALFDINLECPSGETLVLLGPSGAGKSSLLRVLNLLETPDSGQLNIAGHQFDFSQKPSekairllr 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037402861  75 RGIAMVFQSYALYPHLTVEENLSFG-LRMNGNPKADTERRVSHVAEILQITELMKRRPKQLSGGQRQRVAIGRAIVREPE 153
Cdd:COG4161    82 QKVGMVFQQYNLWPHLTVMENLIEApCKVLGLSKEQAREKAMKLLARLRLTDKADRFPLHLSGGQQQRVAIARALMMEPQ 161

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1037402861 154 VFLFDEPLSNLDAELRVQMrVEISRLHKKLGTTMIYVTHDQTEAMTLADRIVVLRAGNI 212
Cdd:COG4161   162 VLLFDEPTAALDPEITAQV-VEIIRELSQTGITQVIVTHEVEFARKVASQVVYMEKGRI 219
thiQ TIGR01277
thiamine ABC transporter, ATP-binding protein; This model describes the energy-transducing ...
 23-216 1.87e-50

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: 167.73  E-value: 1.87e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037402861  23 NLEVKDGEFVVFVGPSGCGKSTLLRMIAGLEDITSGELQIGGRVVNDVEPADRGIAMVFQSYALYPHLTVEENLSFGLRM 102
Cdd:TIGR01277  18 DLNVADGEIVAIMGPSGAGKSTLLNLIAGFIEPASGSIKVNDQSHTGLAPYQRPVSMLFQENNLFAHLTVRQNIGLGLHP 97

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037402861 103 NGNPKADTERRVSHVAEILQITELMKRRPKQLSGGQRQRVAIGRAIVREPEVFLFDEPLSNLDAELRVQMRVEISRLHKK 182
Cdd:TIGR01277  98 GLKLNAEQQEKVVDAAQQVGIADYLDRLPEQLSGGQRQRVALARCLVRPNPILLLDEPFSALDPLLREEMLALVKQLCSE 177

                         170       180       190
                  ....*....|....*....|....*....|....
gi 1037402861 183 LGTTMIYVTHDQTEAMTLADRIVVLRAGNIEQIG 216
Cdd:TIGR01277 178 RQRTLLMVTHHLSDARAIASQIAVVSQGKIKVVS 211
ABC_MetN_methionine_transporter cd03258
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ...
 4-225 3.93e-50

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: 167.37  E-value: 3.93e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037402861   4 LSLSNIVKRFGG----FEIIHGANLEVKDGEFVVFVGPSGCGKSTLLRMIAGLEDITSGELQIGGRVVNDVEPAD----- 74
Cdd:cd03258     2 IELKNVSKVFGDtggkVTALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGSVLVDGTDLTLLSGKElrkar 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037402861  75 RGIAMVFQSYALYPHLTVEENLSFGLRMNGNPKADTERRVSHVAEILQITELMKRRPKQLSGGQRQRVAIGRAIVREPEV 154
Cdd:cd03258    82 RRIGMIFQHFNLLSSRTVFENVALPLEIAGVPKAEIEERVLELLELVGLEDKADAYPAQLSGGQKQRVGIARALANNPKV 161

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1037402861 155 FLFDEPLSNLDAELRVQMRVEISRLHKKLGTTMIYVTHDQTEAMTLADRIVVLRAGNIEQIGAPLDLYDDP 225
Cdd:cd03258   162 LLCDEATSALDPETTQSILALLRDINRELGLTIVLITHEMEVVKRICDRVAVMEKGEVVEEGTVEEVFANP 232
artP PRK11124
arginine transporter ATP-binding subunit; Provisional
 4-216 8.90e-50

arginine transporter ATP-binding subunit; Provisional


Pssm-ID: 182980 [Multi-domain]  Cd Length: 242  Bit Score: 167.11  E-value: 8.90e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037402861   4 LSLSNIVKRFGGFEIIHGANLEVKDGEFVVFVGPSGCGKSTLLRMIAGLEDITSGELQIGGRVVNDVEPAD--------R 75
Cdd:PRK11124    3 IQLNGINCFYGAHQALFDITLDCPQGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLNIAGNHFDFSKTPSdkairelrR 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037402861  76 GIAMVFQSYALYPHLTVEENL-SFGLRMNGNPKADTERRVSHVAEILQITELMKRRPKQLSGGQRQRVAIGRAIVREPEV 154
Cdd:PRK11124   83 NVGMVFQQYNLWPHLTVQQNLiEAPCRVLGLSKDQALARAEKLLERLRLKPYADRFPLHLSGGQQQRVAIARALMMEPQV 162

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1037402861 155 FLFDEPLSNLDAELRVQMrVEISRLHKKLGTTMIYVTHDQTEAMTLADRIVVLRAGNIEQIG 216
Cdd:PRK11124  163 LLFDEPTAALDPEITAQI-VSIIRELAETGITQVIVTHEVEVARKTASRVVYMENGHIVEQG 223
ECF_ATPase_2 TIGR04521
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ...
 19-225 2.79e-49

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: 166.86  E-value: 2.79e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037402861  19 IHGANLEVKDGEFVVFVGPSGCGKSTLLRMIAGLEDITSGELQIGGRVVN-----DVEPADRGIAMVFQsyalYPH---- 89
Cdd:TIGR04521  21 LDDVSLTIEDGEFVAIIGHTGSGKSTLIQHLNGLLKPTSGTVTIDGRDITakkkkKLKDLRKKVGLVFQ----FPEhqlf 96

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037402861  90 -LTVEENLSFGLRMNGNPKADTERRVSHVAEILQITE-LMKRRPKQLSGGQRQRVAIGRAIVREPEVFLFDEPLSNLDAE 167
Cdd:TIGR04521  97 eETVYKDIAFGPKNLGLSEEEAEERVKEALELVGLDEeYLERSPFELSGGQMRRVAIAGVLAMEPEVLILDEPTAGLDPK 176

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1037402861 168 LRVQMRVEISRLHKKLGTTMIYVTHDQTEAMTLADRIVVLRAGNIEQIGAPLDLYDDP 225
Cdd:TIGR04521 177 GRKEILDLFKRLHKEKGLTVILVTHSMEDVAEYADRVIVMHKGKIVLDGTPREVFSDV 234
thiQ PRK10771
thiamine ABC transporter ATP-binding protein ThiQ;
23-232 1.93e-48

thiamine ABC transporter ATP-binding protein ThiQ;


Pssm-ID: 182716 [Multi-domain]  Cd Length: 232  Bit Score: 163.21  E-value: 1.93e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037402861  23 NLEVKDGEFVVFVGPSGCGKSTLLRMIAGLEDITSGELQIGGRVVNDVEPADRGIAMVFQSYALYPHLTVEENLSFG--- 99
Cdd:PRK10771   19 DLTVERGERVAILGPSGAGKSTLLNLIAGFLTPASGSLTLNGQDHTTTPPSRRPVSMLFQENNLFSHLTVAQNIGLGlnp 98

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037402861 100 -LRMNgnpkADTERRVSHVAEILQITELMKRRPKQLSGGQRQRVAIGRAIVREPEVFLFDEPLSNLDAELRVQMRVEISR 178
Cdd:PRK10771   99 gLKLN----AAQREKLHAIARQMGIEDLLARLPGQLSGGQRQRVALARCLVREQPILLLDEPFSALDPALRQEMLTLVSQ 174

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1037402861 179 LHKKLGTTMIYVTHDQTEAMTLADRIVVLRAGNIeqigapldLYDDPANQFVAG 232
Cdd:PRK10771  175 VCQERQLTLLMVSHSLEDAARIAPRSLVVADGRI--------AWDGPTDELLSG 220
SunT COG2274
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ...
 3-221 2.85e-48

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: 173.10  E-value: 2.85e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037402861   3 ELSLSNIVKRFGGFE--IIHGANLEVKDGEFVVFVGPSGCGKSTLLRMIAGLEDITSGELQIGGRVVNDVEPAD--RGIA 78
Cdd:COG2274   473 DIELENVSFRYPGDSppVLDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEPTSGRILIDGIDLRQIDPASlrRQIG 552

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037402861  79 MVFQSYALYpHLTVEENLSFglrmnGNPKADTErRVSHVAEILQITELMKRRPK-----------QLSGGQRQRVAIGRA 147
Cdd:COG2274   553 VVLQDVFLF-SGTIRENITL-----GDPDATDE-EIIEAARLAGLHDFIEALPMgydtvvgeggsNLSGGQRQRLAIARA 625

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1037402861 148 IVREPEVFLFDEPLSNLDA--ELRVQMRveISRLHKklGTTMIYVTHDqTEAMTLADRIVVLRAGNIEQIGAPLDL 221
Cdd:COG2274   626 LLRNPRILILDEATSALDAetEAIILEN--LRRLLK--GRTVIIIAHR-LSTIRLADRIIVLDKGRIVEDGTHEEL 696
ntrCD TIGR01184
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ...
 19-221 1.67e-47

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: 160.71  E-value: 1.67e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037402861  19 IHGANLEVKDGEFVVFVGPSGCGKSTLLRMIAGLEDITSGELQIGGRVVNDVEPaDRGIamVFQSYALYPHLTVEENLSF 98
Cdd:TIGR01184   1 LKGVNLTIQQGEFISLIGHSGCGKSTLLNLISGLAQPTSGGVILEGKQITEPGP-DRMV--VFQNYSLLPWLTVRENIAL 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037402861  99 GLR--MNGNPKADTERRVSHVAEILQITELMKRRPKQLSGGQRQRVAIGRAIVREPEVFLFDEPLSNLDAELRVQMRVEI 176
Cdd:TIGR01184  78 AVDrvLPDLSKSERRAIVEEHIALVGLTEAADKRPGQLSGGMKQRVAIARALSIRPKVLLLDEPFGALDALTRGNLQEEL 157

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 1037402861 177 SRLHKKLGTTMIYVTHDQTEAMTLADRIVVLRAGNIEQIGAPLDL 221
Cdd:TIGR01184 158 MQIWEEHRVTVLMVTHDVDEALLLSDRVVMLTNGPAANIGQILEV 202
ABC_subfamily_A cd03263
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ...
 4-221 1.84e-47

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: 160.36  E-value: 1.84e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037402861   4 LSLSNIVKRFGGFE--IIHGANLEVKDGEFVVFVGPSGCGKSTLLRMIAGLEDITSGELQIGGR-VVNDVEPADRGIAMV 80
Cdd:cd03263     1 LQIRNLTKTYKKGTkpAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYINGYsIRTDRKAARQSLGYC 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037402861  81 FQSYALYPHLTVEENLSFGLRMNGNPKADTERRVSHVAEILQITELMKRRPKQLSGGQRQRVAIGRAIVREPEVFLFDEP 160
Cdd:cd03263    81 PQFDALFDELTVREHLRFYARLKGLPKSEIKEEVELLLRVLGLTDKANKRARTLSGGMKRKLSLAIALIGGPSVLLLDEP 160

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1037402861 161 LSNLDAELRVQMRVEISRLhkKLGTTMIYVTHDQTEAMTLADRIVVLRAGNIEQIGAPLDL 221
Cdd:cd03263   161 TSGLDPASRRAIWDLILEV--RKGRSIILTTHSMDEAEALCDRIAIMSDGKLRCIGSPQEL 219
ssuB PRK11247
aliphatic sulfonates transport ATP-binding subunit; Provisional
 4-248 1.90e-47

aliphatic sulfonates transport ATP-binding subunit; Provisional


Pssm-ID: 183055 [Multi-domain]  Cd Length: 257  Bit Score: 161.38  E-value: 1.90e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037402861   4 LSLSNIVKRFGGFEIIHGANLEVKDGEFVVFVGPSGCGKSTLLRMIAGLEDITSGELQIGGRVVNDVEPADRgiaMVFQS 83
Cdd:PRK11247   13 LLLNAVSKRYGERTVLNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAGELLAGTAPLAEAREDTR---LMFQD 89

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037402861  84 YALYPHLTVEENLSFGLRMNGNPKAdterrvshvAEILQITELMKRR---PKQLSGGQRQRVAIGRAIVREPEVFLFDEP 160
Cdd:PRK11247   90 ARLLPWKKVIDNVGLGLKGQWRDAA---------LQALAAVGLADRAnewPAALSGGQKQRVALARALIHRPGLLLLDEP 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037402861 161 LSNLDAELRVQMRVEISRLHKKLGTTMIYVTHDQTEAMTLADRIVVLRAGnieQIGapLDLYDDPANQFVagfVGSPKMN 240
Cdd:PRK11247  161 LGALDALTRIEMQDLIESLWQQHGFTVLLVTHDVSEAVAMADRVLLIEEG---KIG--LDLTVDLPRPRR---RGSARLA 232


                  ....*...
gi 1037402861 241 FLKAVVVE 248
Cdd:PRK11247  233 ELEAEVLQ 240
ABC_phnC TIGR02315
phosphonate ABC transporter, ATP-binding protein; Phosphonates are a class of ...
 4-228 5.10e-47

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: 159.77  E-value: 5.10e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037402861   4 LSLSNIVKRFG-GFEIIHGANLEVKDGEFVVFVGPSGCGKSTLLRMIAGLEDITSGELQIGGRVVNDVEPAD-----RGI 77
Cdd:TIGR02315   2 LEVENLSKVYPnGKQALKNINLNINPGEFVAIIGPSGAGKSTLLRCINRLVEPSSGSILLEGTDITKLRGKKlrklrRRI 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037402861  78 AMVFQSYALYPHLTVEENLSFGlRMNGNP----------KADTERRVSHVAEiLQITELMKRRPKQLSGGQRQRVAIGRA 147
Cdd:TIGR02315  82 GMIFQHYNLIERLTVLENVLHG-RLGYKPtwrsllgrfsEEDKERALSALER-VGLADKAYQRADQLSGGQQQRVAIARA 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037402861 148 IVREPEVFLFDEPLSNLDAELRVQMRVEISRLHKKLGTTMIYVTHDQTEAMTLADRIVVLRAGNIEQIGAPLDLYDDPAN 227
Cdd:TIGR02315 160 LAQQPDLILADEPIASLDPKTSKQVMDYLKRINKEDGITVIINLHQVDLAKKYADRIVGLKAGEIVFDGAPSELDDEVLR 239


                  .
gi 1037402861 228 Q 228
Cdd:TIGR02315 240 H 240
L_ocin_972_ABC TIGR03608
putative bacteriocin export ABC transporter, lactococcin 972 group; A gene pair with a fairly ...
 6-207 2.47e-46

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: 156.62  E-value: 2.47e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037402861   6 LSNIVKRFGGFEIIHGANLEVKDGEFVVFVGPSGCGKSTLLRMIAGLEDITSGELQIGG---RVVNDVEPAD---RGIAM 79
Cdd:TIGR03608   1 LKNISKKFGDKVILDDLNLTIEKGKMYAIIGESGSGKSTLLNIIGLLEKFDSGQVYLNGqetPPLNSKKASKfrrEKLGY 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037402861  80 VFQSYALYPHLTVEENLSFGLRMNGNPKADTERRVSHVAEILQITELMKRRPKQLSGGQRQRVAIGRAIVREPEVFLFDE 159
Cdd:TIGR03608  81 LFQNFALIENETVEENLDLGLKYKKLSKKEKREKKKEALEKVGLNLKLKQKIYELSGGEQQRVALARAILKPPPLILADE 160

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 1037402861 160 PLSNLDAELRvQMRVEISRLHKKLGTTMIYVTHDqTEAMTLADRIVVL 207
Cdd:TIGR03608 161 PTGSLDPKNR-DEVLDLLLELNDEGKTIIIVTHD-PEVAKQADRVIEL 206
YnjD COG4136
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ...
 4-209 5.42e-46

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


Pssm-ID: 443311 [Multi-domain]  Cd Length: 211  Bit Score: 156.10  E-value: 5.42e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037402861   4 LSLSNIVKRFGGFEIIHGANLEVKDGEFVVFVGPSGCGKSTLLRMIAG-LEDI--TSGELQIGGRVVNDVEPADRGIAMV 80
Cdd:COG4136     2 LSLENLTITLGGRPLLAPLSLTVAPGEILTLMGPSGSGKSTLLAAIAGtLSPAfsASGEVLLNGRRLTALPAEQRRIGIL 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037402861  81 FQSYALYPHLTVEENLSFGLRmNGNPKADTERRVSHVAEILQITELMKRRPKQLSGGQRQRVAIGRAIVREPEVFLFDEP 160
Cdd:COG4136    82 FQDDLLFPHLSVGENLAFALP-PTIGRAQRRARVEQALEEAGLAGFADRDPATLSGGQRARVALLRALLAEPRALLLDEP 160

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 1037402861 161 LSNLDAELRVQMRVEISRLHKKLGTTMIYVTHDQTEAMtLADRIVVLRA 209
Cdd:COG4136   161 FSKLDAALRAQFREFVFEQIRQRGIPALLVTHDEEDAP-AAGRVLDLGN 208
ECF_ATPase_1 TIGR04520
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ...
 18-222 6.54e-46

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


Pssm-ID: 275313 [Multi-domain]  Cd Length: 268  Bit Score: 157.59  E-value: 6.54e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037402861  18 IIHGANLEVKDGEFVVFVGPSGCGKSTLLRMIAGLEDITSGELQIGGRVVNDVE---PADRGIAMVFQSyalyPH----- 89
Cdd:TIGR04520  17 ALKNVSLSIEKGEFVAIIGHNGSGKSTLAKLLNGLLLPTSGKVTVDGLDTLDEEnlwEIRKKVGMVFQN----PDnqfvg 92

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037402861  90 LTVEENLSFGLRMNGNPKADTERRVSHVAEILQITELMKRRPKQLSGGQRQRVAIGRAIVREPEVFLFDEPLSNLDAELR 169
Cdd:TIGR04520  93 ATVEDDVAFGLENLGVPREEMRKRVDEALKLVGMEDFRDREPHLLSGGQKQRVAIAGVLAMRPDIIILDEATSMLDPKGR 172

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1037402861 170 VQMRVEISRLHKKLGTTMIYVTHDQTEAmTLADRIVVLRAGNIEQIGAPLDLY 222
Cdd:TIGR04520 173 KEVLETIRKLNKEEGITVISITHDMEEA-VLADRVIVMNKGKIVAEGTPREIF 224
LivG COG0411
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ...
 1-226 1.74e-45

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: 156.35  E-value: 1.74e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037402861   1 MAELSLSNIVKRFGGFEIIHGANLEVKDGEFVVFVGPSGCGKSTLLRMIAGLEDITSGELQIGGRVVNDVEP---ADRGI 77
Cdd:COG0411     2 DPLLEVRGLTKRFGGLVAVDDVSLEVERGEIVGLIGPNGAGKTTLFNLITGFYRPTSGRILFDGRDITGLPPhriARLGI 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037402861  78 AMVFQSYALYPHLTVEENL---------------SFGLRMNGNPKADTERRVSHVAEILQITELMKRRPKQLSGGQRQRV 142
Cdd:COG0411    82 ARTFQNPRLFPELTVLENVlvaaharlgrgllaaLLRLPRARREEREARERAEELLERVGLADRADEPAGNLSYGQQRRL 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037402861 143 AIGRAIVREPEVFLFDEPLSNLDAELRVQMRVEISRLHKKLGTTMIYVTHDQTEAMTLADRIVVLRAGniEQI--GAPLD 220
Cdd:COG0411   162 EIARALATEPKLLLLDEPAAGLNPEETEELAELIRRLRDERGITILLIEHDMDLVMGLADRIVVLDFG--RVIaeGTPAE 239


                  ....*.
gi 1037402861 221 LYDDPA 226
Cdd:COG0411   240 VRADPR 245
ABC_ATPase cd00267
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ...
 5-210 1.77e-45

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: 152.78  E-value: 1.77e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037402861   5 SLSNIVKRFGGFEIIHGANLEVKDGEFVVFVGPSGCGKSTLLRMIAGLEDITSGELQIGGRVVNDVEP--ADRGIAMVFQ 82
Cdd:cd00267     1 EIENLSFRYGGRTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGKDIAKLPLeeLRRRIGYVPQ 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037402861  83 syalyphltveenlsfglrmngnpkadterrvshvaeilqitelmkrrpkqLSGGQRQRVAIGRAIVREPEVFLFDEPLS 162
Cdd:cd00267    81 ---------------------------------------------------LSGGQRQRVALARALLLNPDLLLLDEPTS 109

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 1037402861 163 NLDAELRVQMRVEISRLHKKlGTTMIYVTHDQTEAMTLADRIVVLRAG 210
Cdd:cd00267   110 GLDPASRERLLELLRELAEE-GRTVIIVTHDPELAELAADRVIVLKDG 156
CydD COG4988
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ...
 2-222 2.73e-45

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: 163.01  E-value: 2.73e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037402861   2 AELSLSNIVKRF-GGFEIIHGANLEVKDGEFVVFVGPSGCGKSTLLRMIAGLEDITSGELQIGGRVVNDVEPAD--RGIA 78
Cdd:COG4988   335 PSIELEDVSFSYpGGRPALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPPYSGSILINGVDLSDLDPASwrRQIA 414

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037402861  79 MVFQSyalyPHL---TVEENLSFglrmnGNPKAdTERRVSHVAEILQITELMKRRPK-----------QLSGGQRQRVAI 144
Cdd:COG4988   415 WVPQN----PYLfagTIRENLRL-----GRPDA-SDEELEAALEAAGLDEFVAALPDgldtplgeggrGLSGGQAQRLAL 484

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1037402861 145 GRAIVREPEVFLFDEPLSNLDAELRVQMRVEISRLHKklGTTMIYVTHDqTEAMTLADRIVVLRAGNIEQIGAPLDLY 222
Cdd:COG4988   485 ARALLRDAPLLLLDEPTAHLDAETEAEILQALRRLAK--GRTVILITHR-LALLAQADRILVLDDGRIVEQGTHEELL 559
DppD COG0444
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ...
 4-226 3.23e-45

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: 157.52  E-value: 3.23e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037402861   4 LSLSNIVKRF----GGFEIIHGANLEVKDGEFVVFVGPSGCGKSTLLRMIAGLED---ITSGELQIGGRVVNDVEPAD-- 74
Cdd:COG0444     2 LEVRNLKVYFptrrGVVKAVDGVSFDVRRGETLGLVGESGSGKSTLARAILGLLPppgITSGEILFDGEDLLKLSEKElr 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037402861  75 ----RGIAMVFQ-SY-ALYPHLTVEENLSFGLRMNGN-PKADTERRVSHVAEILQIT---ELMKRRPKQLSGGQRQRVAI 144
Cdd:COG0444    82 kirgREIQMIFQdPMtSLNPVMTVGDQIAEPLRIHGGlSKAEARERAIELLERVGLPdpeRRLDRYPHELSGGMRQRVMI 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037402861 145 GRAIVREPEVFLFDEPLSNLDAELRVQMRVEISRLHKKLGTTMIYVTHDQTEAMTLADRIVVLRAGNIEQIGAPLDLYDD 224
Cdd:COG0444   162 ARALALEPKLLIADEPTTALDVTIQAQILNLLKDLQRELGLAILFITHDLGVVAEIADRVAVMYAGRIVEEGPVEELFEN 241


                  ..
gi 1037402861 225 PA 226
Cdd:COG0444   242 PR 243
YbbA COG4181
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ...
 4-214 3.72e-45

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: 154.51  E-value: 3.72e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037402861   4 LSLSNIVKRFGGFE----IIHGANLEVKDGEFVVFVGPSGCGKSTLLRMIAGLEDITSGELQIGGRvvnDVEPAD----- 74
Cdd:COG4181     9 IELRGLTKTVGTGAgeltILKGISLEVEAGESVAIVGASGSGKSTLLGLLAGLDRPTSGTVRLAGQ---DLFALDedara 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037402861  75 ----RGIAMVFQSYALYPHLTVEENLSFGLRMNGNPKAdtERRVSHVAEILQITELMKRRPKQLSGGQRQRVAIGRAIVR 150
Cdd:COG4181    86 rlraRHVGFVFQSFQLLPTLTALENVMLPLELAGRRDA--RARARALLERVGLGHRLDHYPAQLSGGEQQRVALARAFAT 163

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1037402861 151 EPEVFLFDEPLSNLDAELRVQMRVEISRLHKKLGTTMIYVTHDQteamTLA---DRIVVLRAGNIEQ 214
Cdd:COG4181   164 EPAILFADEPTGNLDAATGEQIIDLLFELNRERGTTLVLVTHDP----ALAarcDRVLRLRAGRLVE 226
ZnuC COG1121
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ...
 1-207 7.93e-45

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


Pssm-ID: 440738 [Multi-domain]  Cd Length: 245  Bit Score: 154.09  E-value: 7.93e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037402861   1 MAELSLSNIVKRFGGFEIIHGANLEVKDGEFVVFVGPSGCGKSTLLRMIAGLEDITSGELQIGGRvvnDVEPADRGIAMV 80
Cdd:COG1121     4 MPAIELENLTVSYGGRPVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLFGK---PPRRARRRIGYV 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037402861  81 FQSYALYPH--LTVEENLSFGL----RMNGNPKADTERRVSHVAEILQITELMKRRPKQLSGGQRQRVAIGRAIVREPEV 154
Cdd:COG1121    81 PQRAEVDWDfpITVRDVVLMGRygrrGLFRRPSRADREAVDEALERVGLEDLADRPIGELSGGQQQRVLLARALAQDPDL 160

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1037402861 155 FLFDEPLSNLDAELRVQ-MRVeISRLHKKlGTTMIYVTHDQTEAMTLADRIVVL 207
Cdd:COG1121   161 LLLDEPFAGVDAATEEAlYEL-LRELRRE-GKTILVVTHDLGAVREYFDRVLLL 212
ABC_Mj1267_LivG_branched cd03219
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ...
 4-212 9.56e-45

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: 153.75  E-value: 9.56e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037402861   4 LSLSNIVKRFGGFEIIHGANLEVKDGEFVVFVGPSGCGKSTLLRMIAGLEDITSGELQIGGRVVNDVEP---ADRGIAMV 80
Cdd:cd03219     1 LEVRGLTKRFGGLVALDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFDGEDITGLPPheiARLGIGRT 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037402861  81 FQSYALYPHLTVEENL----------SFGLRMNGNPKADTERRVSHVAEILQITELMKRRPKQLSGGQRQRVAIGRAIVR 150
Cdd:cd03219    81 FQIPRLFPELTVLENVmvaaqartgsGLLLARARREEREARERAEELLERVGLADLADRPAGELSYGQQRRLEIARALAT 160

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1037402861 151 EPEVFLFDEPLSNLDAELRVQMRVEISRLhKKLGTTMIYVTHDQTEAMTLADRIVVLRAGNI 212
Cdd:cd03219   161 DPKLLLLDEPAAGLNPEETEELAELIREL-RERGITVLLVEHDMDVVMSLADRVTVLDQGRV 221
CcmA COG4133
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ...
 4-209 1.00e-44

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


Pssm-ID: 443308 [Multi-domain]  Cd Length: 206  Bit Score: 152.63  E-value: 1.00e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037402861   4 LSLSNIVKRFGGFEIIHGANLEVKDGEFVVFVGPSGCGKSTLLRMIAGLEDITSGELQIGGRVVNDVEPADRG-IAMVFQ 82
Cdd:COG4133     3 LEAENLSCRRGERLLFSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWNGEPIRDAREDYRRrLAYLGH 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037402861  83 SYALYPHLTVEENLSFGLRMNGNPkaDTERRVSHVAEILQITELMKRRPKQLSGGQRQRVAIGRAIVREPEVFLFDEPLS 162
Cdd:COG4133    83 ADGLKPELTVRENLRFWAALYGLR--ADREAIDEALEAVGLAGLADLPVRQLSAGQKRRVALARLLLSPAPLWLLDEPFT 160

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 1037402861 163 NLDAElRVQMRVEISRLHKKLGTTMIYVTHDQTEAmtLADRIVVLRA 209
Cdd:COG4133   161 ALDAA-GVALLAELIAAHLARGGAVLLTTHQPLEL--AAARVLDLGD 204
PRK11264 PRK11264
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
 1-235 1.33e-44

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


Pssm-ID: 183063 [Multi-domain]  Cd Length: 250  Bit Score: 153.75  E-value: 1.33e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037402861   1 MAELSLSNIVKRFGGFEIIHGANLEVKDGEFVVFVGPSGCGKSTLLRMIAGLEDITSGELQIGGRVVNDVEP--ADRG-- 76
Cdd:PRK11264    1 MSAIEVKNLVKKFHGQTVLHGIDLEVKPGEVVAIIGPSGSGKTTLLRCINLLEQPEAGTIRVGDITIDTARSlsQQKGli 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037402861  77 ------IAMVFQSYALYPHLTVEENLSFG-LRMNGNPKADTERRVSHVAEILQITELMKRRPKQLSGGQRQRVAIGRAIV 149
Cdd:PRK11264   81 rqlrqhVGFVFQNFNLFPHRTVLENIIEGpVIVKGEPKEEATARARELLAKVGLAGKETSYPRRLSGGQQQRVAIARALA 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037402861 150 REPEVFLFDEPLSNLDAELRVQMRVEISRLHKKlGTTMIYVTHDQTEAMTLADRIVVLRAGNIEQIGAPLDLYDDP---- 225
Cdd:PRK11264  161 MRPEVILFDEPTSALDPELVGEVLNTIRQLAQE-KRTMVIVTHEMSFARDVADRAIFMDQGRIVEQGPAKALFADPqqpr 239

                         250
                  ....*....|
gi 1037402861 226 ANQFVAGFVG 235
Cdd:PRK11264  240 TRQFLEKFLL 249
ABC_tran pfam00005
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ...
 19-162 1.67e-44

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: 150.11  E-value: 1.67e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037402861  19 IHGANLEVKDGEFVVFVGPSGCGKSTLLRMIAGLEDITSGELQIGGRVVNDVEPAD--RGIAMVFQSYALYPHLTVEENL 96
Cdd:pfam00005   1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDLTDDERKSlrKEIGYVFQDPQLFPRLTVRENL 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037402861  97 SFGLRMNGNPKADTERRVSHVAEILQITELMKRR----PKQLSGGQRQRVAIGRAIVREPEVFLFDEPLS 162
Cdd:pfam00005  81 RLGLLLKGLSKREKDARAEEALEKLGLGDLADRPvgerPGTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
ABC_FtsE cd03292
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ...
 8-212 3.08e-44

Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where FtsE is the ATPase and the membrane subunit FtsX resembles a permease subunit. But rather than transporting any substrate, the complex acts in cell division by undergoing conformational changes that alter the activity of cell wall hydrolases located outside the plasma membrane. The complex is widely conserved in bacteria, but also extremely divergent in sequence between different lineages


Pssm-ID: 213259 [Multi-domain]  Cd Length: 214  Bit Score: 151.79  E-value: 3.08e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037402861   8 NIVKRF-GGFEIIHGANLEVKDGEFVVFVGPSGCGKSTLLRMIAGLEDITSGELQIGGRVVND-----VEPADRGIAMVF 81
Cdd:cd03292     5 NVTKTYpNGTAALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQDVSDlrgraIPYLRRKIGVVF 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037402861  82 QSYALYPHLTVEENLSFGLRMNGNPKADTERRVSHVAEILQITELMKRRPKQLSGGQRQRVAIGRAIVREPEVFLFDEPL 161
Cdd:cd03292    85 QDFRLLPDRNVYENVAFALEVTGVPPREIRKRVPAALELVGLSHKHRALPAELSGGEQQRVAIARAIVNSPTILIADEPT 164

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1037402861 162 SNLDAElrvqMRVEISRLHKKL---GTTMIYVTHDQTEAMTLADRIVVLRAGNI 212
Cdd:cd03292   165 GNLDPD----TTWEIMNLLKKInkaGTTVVVATHAKELVDTTRHRVIALERGKL 214
tauB PRK11248
taurine ABC transporter ATP-binding subunit;
4-210 1.07e-43

taurine ABC transporter ATP-binding subunit;


Pssm-ID: 183056 [Multi-domain]  Cd Length: 255  Bit Score: 151.39  E-value: 1.07e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037402861   4 LSLSNIVKRFGGFEIIHGANLEVKDGEFVVFVGPSGCGKSTLLRMIAGLEDITSGELQIGGRVVNDvEPADRGIamVFQS 83
Cdd:PRK11248    2 LQISHLYADYGGKPALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDGKPVEG-PGAERGV--VFQN 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037402861  84 YALYPHLTVEENLSFGLRMNGNPKADTERRVSHVAEILQITELMKRRPKQLSGGQRQRVAIGRAIVREPEVFLFDEPLSN 163
Cdd:PRK11248   79 EGLLPWRNVQDNVAFGLQLAGVEKMQRLEIAHQMLKKVGLEGAEKRYIWQLSGGQRQRVGIARALAANPQLLLLDEPFGA 158

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 1037402861 164 LDAELRVQMRVEISRLHKKLGTTMIYVTHDQTEAMTLADRIVVLRAG 210
Cdd:PRK11248  159 LDAFTREQMQTLLLKLWQETGKQVLLITHDIEEAVFMATELVLLSPG 205
ABC_TM1139_LivF_branched cd03224
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ...
 4-224 1.11e-43

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: 150.28  E-value: 1.11e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037402861   4 LSLSNIVKRFGGFEIIHGANLEVKDGEFVVFVGPSGCGKSTLLRMIAGLEDITSGELQIGGRVVNDVEPADR---GIAMV 80
Cdd:cd03224     1 LEVENLNAGYGKSQILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDGRDITGLPPHERaraGIGYV 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037402861  81 FQSYALYPHLTVEENLSFGLRmnGNPKADTERRVSHVAEILQI-TELMKRRPKQLSGGQRQRVAIGRAIVREPEVFLFDE 159
Cdd:cd03224    81 PEGRRIFPELTVEENLLLGAY--ARRRAKRKARLERVYELFPRlKERRKQLAGTLSGGEQQMLAIARALMSRPKLLLLDE 158

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1037402861 160 PLSNLdAELRVQMRVEISRLHKKLGTTMIYVTHDQTEAMTLADRIVVLRAGNIEQIGAPLDLYDD 224
Cdd:cd03224   159 PSEGL-APKIVEEIFEAIRELRDEGVTILLVEQNARFALEIADRAYVLERGRVVLEGTAAELLAD 222
ABC_DrrA cd03265
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ...
 7-221 1.58e-43

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: 149.83  E-value: 1.58e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037402861   7 SNIVKRFGGFEIIHGANLEVKDGEFVVFVGPSGCGKSTLLRMIAGLEDITSGELQIGGR-VVNDVEPADRGIAMVFQSYA 85
Cdd:cd03265     4 ENLVKKYGDFEAVRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATVAGHdVVREPREVRRRIGIVFQDLS 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037402861  86 LYPHLTVEENLSFGLRMNGNPKADTERRVSHVAEILQITELMKRRPKQLSGGQRQRVAIGRAIVREPEVFLFDEPLSNLD 165
Cdd:cd03265    84 VDDELTGWENLYIHARLYGVPGAERRERIDELLDFVGLLEAADRLVKTYSGGMRRRLEIARSLVHRPEVLFLDEPTIGLD 163

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1037402861 166 AELRVQMRVEISRLHKKLGTTMIYVTHDQTEAMTLADRIVVLRAGNIEQIGAPLDL 221
Cdd:cd03265   164 PQTRAHVWEYIEKLKEEFGMTILLTTHYMEEAEQLCDRVAIIDHGRIIAEGTPEEL 219
ABC_Metallic_Cations cd03235
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ...
 5-207 1.99e-43

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: 149.61  E-value: 1.99e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037402861   5 SLSNIVKRFGGFEIIHGANLEVKDGEFVVFVGPSGCGKSTLLRMIAGLEDITSGELQIGGRvvnDVEPADRGIAMVFQSY 84
Cdd:cd03235     1 EVEDLTVSYGGHPVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFGK---PLEKERKRIGYVPQRR 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037402861  85 AL---YPhLTVEENLSFGL----RMNGNPKADTERRVSHVAEILQITELMKRRPKQLSGGQRQRVAIGRAIVREPEVFLF 157
Cdd:cd03235    78 SIdrdFP-ISVRDVVLMGLyghkGLFRRLSKADKAKVDEALERVGLSELADRQIGELSGGQQQRVLLARALVQDPDLLLL 156

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 1037402861 158 DEPLSNLDAELRVQMRVEISRLHKKlGTTMIYVTHDQTEAMTLADRIVVL 207
Cdd:cd03235   157 DEPFAGVDPKTQEDIYELLRELRRE-GMTILVVTHDLGLVLEYFDRVLLL 205
MdlB COG1132
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
14-216 2.31e-43

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


Pssm-ID: 440747 [Multi-domain]  Cd Length: 579  Bit Score: 158.02  E-value: 2.31e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037402861  14 GGFEIIHGANLEVKDGEFVVFVGPSGCGKSTLLRMIAGLEDITSGELQIGGRVVNDVEPAD--RGIAMVFQSYALYpHLT 91
Cdd:COG1132   351 GDRPVLKDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYDPTSGRILIDGVDIRDLTLESlrRQIGVVPQDTFLF-SGT 429

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037402861  92 VEENLSFglrmnGNPKADTErRVSHVAEILQITELMKRRPK-----------QLSGGQRQRVAIGRAIVREPEVFLFDEP 160
Cdd:COG1132   430 IRENIRY-----GRPDATDE-EVEEAAKAAQAHEFIEALPDgydtvvgergvNLSGGQRQRIAIARALLKDPPILILDEA 503

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1037402861 161 LSNLDA--ELRVQMRveISRLHKklGTTMIYVTHdQTEAMTLADRIVVLRAGNIEQIG 216
Cdd:COG1132   504 TSALDTetEALIQEA--LERLMK--GRTTIVIAH-RLSTIRNADRILVLDDGRIVEQG 556
ABCC_MRP_Like cd03228
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ...
 4-210 4.39e-43

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: 147.14  E-value: 4.39e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037402861   4 LSLSNIVKRFGGF--EIIHGANLEVKDGEFVVFVGPSGCGKSTLLRMIAGLEDITSGELQIGGRVVNDVEPAD--RGIAM 79
Cdd:cd03228     1 IEFKNVSFSYPGRpkPVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGVDLRDLDLESlrKNIAY 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037402861  80 VFQSYALYpHLTVEENLsfglrmngnpkadterrvshvaeilqitelmkrrpkqLSGGQRQRVAIGRAIVREPEVFLFDE 159
Cdd:cd03228    81 VPQDPFLF-SGTIRENI-------------------------------------LSGGQRQRIAIARALLRDPPILILDE 122

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1037402861 160 PLSNLDAELRVQMRVEISRLHKklGTTMIYVTHDqTEAMTLADRIVVLRAG 210
Cdd:cd03228   123 ATSALDPETEALILEALRALAK--GKTVIVIAHR-LSTIRDADRIIVLDDG 170
AppF COG4608
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ...
 4-226 6.12e-43

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


Pssm-ID: 443658 [Multi-domain]  Cd Length: 329  Bit Score: 151.81  E-value: 6.12e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037402861   4 LSLSNIVKRF---GGF-----EIIH---GANLEVKDGEFVVFVGPSGCGKSTLLRMIAGLEDITSGELQIGGRVVNDVEP 72
Cdd:COG4608     8 LEVRDLKKHFpvrGGLfgrtvGVVKavdGVSFDIRRGETLGLVGESGCGKSTLGRLLLRLEEPTSGEILFDGQDITGLSG 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037402861  73 AD-----RGIAMVFQ-SYA-LYPHLTVEENLSFGLRMNG-NPKADTERRvshVAEILQI----TELMKRRPKQLSGGQRQ 140
Cdd:COG4608    88 RElrplrRRMQMVFQdPYAsLNPRMTVGDIIAEPLRIHGlASKAERRER---VAELLELvglrPEHADRYPHEFSGGQRQ 164

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037402861 141 RVAIGRAIVREPEVFLFDEPLSNLDAELRVQ----MRveisRLHKKLGTTMIYVTHDQTEAMTLADRIVVLRAGNIEQIG 216
Cdd:COG4608   165 RIGIARALALNPKLIVCDEPVSALDVSIQAQvlnlLE----DLQDELGLTYLFISHDLSVVRHISDRVAVMYLGKIVEIA 240

                         250
                  ....*....|
gi 1037402861 217 APLDLYDDPA 226
Cdd:COG4608   241 PRDELYARPL 250
ABC_Iron-Siderophores_B12_Hemin cd03214
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ...
 5-216 1.54e-42

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: 146.04  E-value: 1.54e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037402861   5 SLSNIVKRFGGFEIIHGANLEVKDGEFVVFVGPSGCGKSTLLRMIAGLEDITSGELQIGGRVVNDVEPADRG--IAMVFQ 82
Cdd:cd03214     1 EVENLSVGYGGRTVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDGKDLASLSPKELArkIAYVPQ 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037402861  83 syalyphltveenlsfglrmngnpkadterrvshVAEILQITELMKRRPKQLSGGQRQRVAIGRAIVREPEVFLFDEPLS 162
Cdd:cd03214    81 ----------------------------------ALELLGLAHLADRPFNELSGGERQRVLLARALAQEPPILLLDEPTS 126

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1037402861 163 NLDaeLRVQMRV--EISRLHKKLGTTMIYVTHDQTEAMTLADRIVVLRAGNIEQIG 216
Cdd:cd03214   127 HLD--IAHQIELleLLRRLARERGKTVVMVLHDLNLAARYADRVILLKDGRIVAQG 180
ABC_BcrA_bacitracin_resist cd03268
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ...
 4-212 3.98e-42

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: 145.82  E-value: 3.98e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037402861   4 LSLSNIVKRFGGFEIIHGANLEVKDGEFVVFVGPSGCGKSTLLRMIAGLEDITSGELQIGGRVVNDVEPADRGIAMVFQS 83
Cdd:cd03268     1 LKTNDLTKTYGKKRVLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEITFDGKSYQKNIEALRRIGALIEA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037402861  84 YALYPHLTVEENLSFGLRMNGNPKADTERrvshVAEILQITELMKRRPKQLSGGQRQRVAIGRAIVREPEVFLFDEPLSN 163
Cdd:cd03268    81 PGFYPNLTARENLRLLARLLGIRKKRIDE----VLDVVGLKDSAKKKVKGFSLGMKQRLGIALALLGNPDLLILDEPTNG 156

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 1037402861 164 LDAELRVQMRvEISRLHKKLGTTMIYVTHDQTEAMTLADRIVVLRAGNI 212
Cdd:cd03268   157 LDPDGIKELR-ELILSLRDQGITVLISSHLLSEIQKVADRIGIINKGKL 204
PRK10070 PRK10070
proline/glycine betaine ABC transporter ATP-binding protein ProV;
4-233 6.76e-42

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


Pssm-ID: 182221 [Multi-domain]  Cd Length: 400  Bit Score: 150.95  E-value: 6.76e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037402861   4 LSLSNIVKRFGGFEIIHGANLEVKDGEFVVFVGPSGCGKSTLLRMIAGLEDITSGELQIGGRVVNDVEPAD------RGI 77
Cdd:PRK10070   29 LSKEQILEKTGLSLGVKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAKISDAElrevrrKKI 108

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037402861  78 AMVFQSYALYPHLTVEENLSFGLRMNGNPKADTERRVSHVAEILQITELMKRRPKQLSGGQRQRVAIGRAIVREPEVFLF 157
Cdd:PRK10070  109 AMVFQSFALMPHMTVLDNTAFGMELAGINAEERREKALDALRQVGLENYAHSYPDELSGGMRQRVGLARALAINPDILLM 188

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1037402861 158 DEPLSNLDAELRVQMRVEISRLHKKLGTTMIYVTHDQTEAMTLADRIVVLRAGNIEQIGAPLDLYDDPANQFVAGF 233
Cdd:PRK10070  189 DEAFSALDPLIRTEMQDELVKLQAKHQRTIVFISHDLDEAMRIGDRIAIMQNGEVVQVGTPDEILNNPANDYVRTF 264
ABC_Carb_Monos_I cd03216
First domain of the ATP-binding cassette component of monosaccharide transport system; This ...
 4-210 1.15e-41

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: 143.34  E-value: 1.15e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037402861   4 LSLSNIVKRFGGFEIIHGANLEVKDGEFVVFVGPSGCGKSTLLRMIAGLEDITSGELQIGGRVVNDVEPAD---RGIAMV 80
Cdd:cd03216     1 LELRGITKRFGGVKALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVDGKEVSFASPRDarrAGIAMV 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037402861  81 FqsyalyphltveenlsfglrmngnpkadterrvshvaeilqitelmkrrpkQLSGGQRQRVAIGRAIVREPEVFLFDEP 160
Cdd:cd03216    81 Y---------------------------------------------------QLSVGERQMVEIARALARNARLLILDEP 109

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 1037402861 161 LSNLDAELRVQMRVEISRLhKKLGTTMIYVTHDQTEAMTLADRIVVLRAG 210
Cdd:cd03216   110 TAALTPAEVERLFKVIRRL-RAQGVAVIFISHRLDEVFEIADRVTVLRDG 158
MglA COG1129
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
4-210 6.07e-41

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


Pssm-ID: 440745 [Multi-domain]  Cd Length: 497  Bit Score: 150.17  E-value: 6.07e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037402861   4 LSLSNIVKRFGGFEIIHGANLEVKDGEFVVFVGPSGCGKSTLLRMIAGLEDITSGELQIGGRVVNDVEPAD---RGIAMV 80
Cdd:COG1129     5 LEMRGISKSFGGVKALDGVSLELRPGEVHALLGENGAGKSTLMKILSGVYQPDSGEILLDGEPVRFRSPRDaqaAGIAII 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037402861  81 FQSYALYPHLTVEENLSFGLRMNGNP---KADTERRVSHVAEILQITELMKRRPKQLSGGQRQRVAIGRAIVREPEVFLF 157
Cdd:COG1129    85 HQELNLVPNLSVAENIFLGREPRRGGlidWRAMRRRARELLARLGLDIDPDTPVGDLSVAQQQLVEIARALSRDARVLIL 164

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1037402861 158 DEPLSNLDAElrvqmrvEISRLH------KKLGTTMIYVTHDQTEAMTLADRIVVLRAG 210
Cdd:COG1129   165 DEPTASLTER-------EVERLFriirrlKAQGVAIIYISHRLDEVFEIADRVTVLRDG 216
LivF COG0410
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ...
 1-226 1.17e-40

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: 142.81  E-value: 1.17e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037402861   1 MAELSLSNIVKRFGGFEIIHGANLEVKDGEFVVFVGPSGCGKSTLLRMIAGLEDITSGELQIGGRVVNDVEP---ADRGI 77
Cdd:COG0410     1 MPMLEVENLHAGYGGIHVLHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRSGSIRFDGEDITGLPPhriARLGI 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037402861  78 AMVFQSYALYPHLTVEENLSFGLRmNGNPKADTERRVSHVAE---ILQitELMKRRPKQLSGGQRQRVAIGRAIVREPEV 154
Cdd:COG0410    81 GYVPEGRRIFPSLTVEENLLLGAY-ARRDRAEVRADLERVYElfpRLK--ERRRQRAGTLSGGEQQMLAIGRALMSRPKL 157

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1037402861 155 FLFDEPLSNLdAELRVQMRVEISRLHKKLGTTMIYVTHDQTEAMTLADRIVVLRAGNIEQIGAPLDLYDDPA 226
Cdd:COG0410   158 LLLDEPSLGL-APLIVEEIFEIIRRLNREGVTILLVEQNARFALEIADRAYVLERGRIVLEGTAAELLADPE 228
ABC_NatA_sodium_exporter cd03266
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ...
 4-212 5.29e-40

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: 140.58  E-value: 5.29e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037402861   4 LSLSNIVKRF----GGFEIIHGANLEVKDGEFVVFVGPSGCGKSTLLRMIAGLEDITSGELQIGG-RVVNDVEPADRGIA 78
Cdd:cd03266     2 ITADALTKRFrdvkKTVQAVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDGfDVVKEPAEARRRLG 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037402861  79 MVFQSYALYPHLTVEENLSFGLRMNGNPKADTERRVSHVAEILQITELMKRRPKQLSGGQRQRVAIGRAIVREPEVFLFD 158
Cdd:cd03266    82 FVSDSTGLYDRLTARENLEYFAGLYGLKGDELTARLEELADRLGMEELLDRRVGGFSTGMRQKVAIARALVHDPPVLLLD 161

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1037402861 159 EPLSNLDAeLRVQMRVEISRLHKKLGTTMIYVTHDQTEAMTLADRIVVLRAGNI 212
Cdd:cd03266   162 EPTTGLDV-MATRALREFIRQLRALGKCILFSTHIMQEVERLCDRVVVLHRGRV 214
CeuD COG4604
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ...
 5-221 6.06e-40

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


Pssm-ID: 443654 [Multi-domain]  Cd Length: 252  Bit Score: 141.37  E-value: 6.06e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037402861   5 SLSNIVKRFGGFEIIHGANLEVKDGEFVVFVGPSGCGKSTLLRMIAGLEDITSGELQIGGRVVNDVEPAD--RGIAMVFQ 82
Cdd:COG4604     3 EIKNVSKRYGGKVVLDDVSLTIPKGGITALIGPNGAGKSTLLSMISRLLPPDSGEVLVDGLDVATTPSRElaKRLAILRQ 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037402861  83 SYALYPHLTVEENLSFGlRM---NGNPKADTERRVSHVAEILQITELMKRRPKQLSGGQRQRVAIGRAIVREPEVFLFDE 159
Cdd:COG4604    83 ENHINSRLTVRELVAFG-RFpysKGRLTAEDREIIDEAIAYLDLEDLADRYLDELSGGQRQRAFIAMVLAQDTDYVLLDE 161

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1037402861 160 PLSNLDAELRVQMRVEISRLHKKLGTTMIYVTHDQTEAMTLADRIVVLRAGNIEQIGAPLDL 221
Cdd:COG4604   162 PLNNLDMKHSVQMMKLLRRLADELGKTVVIVLHDINFASCYADHIVAMKDGRVVAQGTPEEI 223
PRK10619 PRK10619
histidine ABC transporter ATP-binding protein HisP;
1-232 1.10e-39

histidine ABC transporter ATP-binding protein HisP;


Pssm-ID: 182592 [Multi-domain]  Cd Length: 257  Bit Score: 141.26  E-value: 1.10e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037402861   1 MAE--LSLSNIVKRFGGFEIIHGANLEVKDGEFVVFVGPSGCGKSTLLRMIAGLEDITSGELQIGGRVVNDVEPAD---- 74
Cdd:PRK10619    1 MSEnkLNVIDLHKRYGEHEVLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNGQTINLVRDKDgqlk 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037402861  75 -----------RGIAMVFQSYALYPHLTVEEN-LSFGLRMNGNPKADTERRVSHVAEILQITELMKRR-PKQLSGGQRQR 141
Cdd:PRK10619   81 vadknqlrllrTRLTMVFQHFNLWSHMTVLENvMEAPIQVLGLSKQEARERAVKYLAKVGIDERAQGKyPVHLSGGQQQR 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037402861 142 VAIGRAIVREPEVFLFDEPLSNLDAELrvqmRVEISRLHKKL---GTTMIYVTHDQTEAMTLADRIVVLRAGNIEQIGAP 218
Cdd:PRK10619  161 VSIARALAMEPEVLLFDEPTSALDPEL----VGEVLRIMQQLaeeGKTMVVVTHEMGFARHVSSHVIFLHQGKIEEEGAP 236

                         250
                  ....*....|....*...
gi 1037402861 219 LDLYDDPAN----QFVAG 232
Cdd:PRK10619  237 EQLFGNPQSprlqQFLKG 254
CydC COG4987
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ...
 2-226 7.62e-39

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: 145.29  E-value: 7.62e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037402861   2 AELSLSNIVKRF--GGFEIIHGANLEVKDGEFVVFVGPSGCGKSTLLRMIAGLEDITSGELQIGGRVVNDVEPAD--RGI 77
Cdd:COG4987   332 PSLELEDVSFRYpgAGRPVLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFLDPQSGSITLGGVDLRDLDEDDlrRRI 411

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037402861  78 AMVFQSyalyPHL---TVEENLSFglrmnGNPKAdTERRVSHVAEILQITELMKRRPK-----------QLSGGQRQRVA 143
Cdd:COG4987   412 AVVPQR----PHLfdtTLRENLRL-----ARPDA-TDEELWAALERVGLGDWLAALPDgldtwlgeggrRLSGGERRRLA 481

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037402861 144 IGRAIVREPEVFLFDEPLSNLDAELRVQMRVEISRLHKklGTTMIYVTHDQTeAMTLADRIVVLRAGNIEQIGAPLDLYD 223
Cdd:COG4987   482 LARALLRDAPILLLDEPTEGLDAATEQALLADLLEALA--GRTVLLITHRLA-GLERMDRILVLEDGRIVEQGTHEELLA 558


                  ...
gi 1037402861 224 DPA 226
Cdd:COG4987   559 QNG 561
YhaQ COG4152
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ...
 4-262 1.21e-38

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


Pssm-ID: 443322 [Multi-domain]  Cd Length: 298  Bit Score: 139.47  E-value: 1.21e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037402861   4 LSLSNIVKRFGGFEIIHGANLEVKDGEFVVFVGPSGCGKSTLLRMIAGLEDITSGELQIGGRVVNDVE-------PADRG 76
Cdd:COG4152     2 LELKGLTKRFGDKTAVDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDSGEVLWDGEPLDPEDrrrigylPEERG 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037402861  77 iamvfqsyaLYPHLTVEENLSFGLRMNGNPKADTERRVSHVAEILQITELMKRRPKQLSGGQRQRVAIGRAIVREPEVFL 156
Cdd:COG4152    82 ---------LYPKMKVGEQLVYLARLKGLSKAEAKRRADEWLERLGLGDRANKKVEELSKGNQQKVQLIAALLHDPELLI 152

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037402861 157 FDEPLSNLD---AELrvqMRVEISRLHKKlGTTMIYVTHDQTEAMTLADRIVVLRAGNIEQIGAPLDLYDD-PANQFVAG 232
Cdd:COG4152   153 LDEPFSGLDpvnVEL---LKDVIRELAAK-GTTVIFSSHQMELVEELCDRIVIINKGRKVLSGSVDEIRRQfGRNTLRLE 228

                         250       260       270
                  ....*....|....*....|....*....|....
gi 1037402861 233 FVGSPKmnFLKAV----VVEAQPGRAVIALESDA 262
Cdd:COG4152   229 ADGDAG--WLRALpgvtVVEEDGDGAELKLEDGA 260
modC PRK11144
molybdenum ABC transporter ATP-binding protein ModC;
36-258 1.34e-38

molybdenum ABC transporter ATP-binding protein ModC;


Pssm-ID: 182993 [Multi-domain]  Cd Length: 352  Bit Score: 140.78  E-value: 1.34e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037402861  36 GPSGCGKSTLLRMIAGLEDITSGELQIGGRVVNDVE------PADRGIAMVFQSYALYPHLTVEENLSFGLRMNGNPKAD 109
Cdd:PRK11144   31 GRSGAGKTSLINAISGLTRPQKGRIVLNGRVLFDAEkgiclpPEKRRIGYVFQDARLFPHYKVRGNLRYGMAKSMVAQFD 110

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037402861 110 TerrvshVAEILQITELMKRRPKQLSGGQRQRVAIGRAIVREPEVFLFDEPLSNLDAELRVQMRVEISRLHKKLGTTMIY 189
Cdd:PRK11144  111 K------IVALLGIEPLLDRYPGSLSGGEKQRVAIGRALLTAPELLLMDEPLASLDLPRKRELLPYLERLAREINIPILY 184

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1037402861 190 VTHDQTEAMTLADRIVVLRAGNIEQIGAPLDLYDDPAnqFVAGFVGSPKMNFLKAVVVEAQPGRAVIAL 258
Cdd:PRK11144  185 VSHSLDEILRLADRVVVLEQGKVKAFGPLEEVWASSA--MRPWLPKEEQSSILKVTVLEHHPHYAMTAL 251
cbiO PRK13632
cobalt transporter ATP-binding subunit; Provisional
 23-224 2.50e-38

cobalt transporter ATP-binding subunit; Provisional


Pssm-ID: 237452 [Multi-domain]  Cd Length: 271  Bit Score: 137.81  E-value: 2.50e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037402861  23 NLEVKDGEFVVFVGPSGCGKSTLLRMIAGLEDITSGELQIGGRVVND--VEPADRGIAMVFQSyalyPH-----LTVEEN 95
Cdd:PRK13632   29 SFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIDGITISKenLKEIRKKIGIIFQN----PDnqfigATVEDD 104

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037402861  96 LSFGLRMNGNPKADTERRVSHVAEILQITELMKRRPKQLSGGQRQRVAIGRAIVREPEVFLFDEPLSNLDAELRVQMRVE 175
Cdd:PRK13632  105 IAFGLENKKVPPKKMKDIIDDLAKKVGMEDYLDKEPQNLSGGQKQRVAIASVLALNPEIIIFDESTSMLDPKGKREIKKI 184

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 1037402861 176 ISRLHKKLGTTMIYVTHDQTEAmTLADRIVVLRAGNIEQIGAPLDLYDD 224
Cdd:PRK13632  185 MVDLRKTRKKTLISITHDMDEA-ILADKVIVFSEGKLIAQGKPKEILNN 232
NupO COG3845
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ...
 4-210 3.74e-38

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


Pssm-ID: 443055 [Multi-domain]  Cd Length: 504  Bit Score: 142.47  E-value: 3.74e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037402861   4 LSLSNIVKRFGGFEIIHGANLEVKDGEFVVFVGPSGCGKSTLLRMIAGLEDITSGELQIGGRVVNDVEPAD---RGIAMV 80
Cdd:COG3845     6 LELRGITKRFGGVVANDDVSLTVRPGEIHALLGENGAGKSTLMKILYGLYQPDSGEILIDGKPVRIRSPRDaiaLGIGMV 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037402861  81 FQSYALYPHLTVEENLSFGLRMNGNPKADTERrvshVAEilQITELMKR---------RPKQLSGGQRQRVAIGRAIVRE 151
Cdd:COG3845    86 HQHFMLVPNLTVAENIVLGLEPTKGGRLDRKA----ARA--RIRELSERygldvdpdaKVEDLSVGEQQRVEILKALYRG 159

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1037402861 152 PEVFLFDEPLSNLD----AELRVQMRveisRLhKKLGTTMIYVTHDQTEAMTLADRIVVLRAG 210
Cdd:COG3845   160 ARILILDEPTAVLTpqeaDELFEILR----RL-AAEGKSIIFITHKLREVMAIADRVTVLRRG 217
cbiO PRK13637
energy-coupling factor transporter ATPase;
23-222 5.40e-38

energy-coupling factor transporter ATPase;


Pssm-ID: 237455 [Multi-domain]  Cd Length: 287  Bit Score: 137.49  E-value: 5.40e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037402861  23 NLEVKDGEFVVFVGPSGCGKSTLLRMIAGLEDITSGELqiggrVVNDVEPADRGIAM---------VFQ--SYALYPHlT 91
Cdd:PRK13637   27 NIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKI-----IIDGVDITDKKVKLsdirkkvglVFQypEYQLFEE-T 100

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037402861  92 VEENLSFGLRMNGNPKADTERRVSHVAEI--LQITELMKRRPKQLSGGQRQRVAIGRAIVREPEVFLFDEPLSNLDAELR 169
Cdd:PRK13637  101 IEKDIAFGPINLGLSEEEIENRVKRAMNIvgLDYEDYKDKSPFELSGGQKRRVAIAGVVAMEPKILILDEPTAGLDPKGR 180

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1037402861 170 VQMRVEISRLHKKLGTTMIYVTHDQTEAMTLADRIVVLRAGNIEQIGAPLDLY 222
Cdd:PRK13637  181 DEILNKIKELHKEYNMTIILVSHSMEDVAKLADRIIVMNKGKCELQGTPREVF 233
nikE PRK10419
nickel ABC transporter ATP-binding protein NikE;
1-228 6.39e-38

nickel ABC transporter ATP-binding protein NikE;


Pssm-ID: 236689 [Multi-domain]  Cd Length: 268  Bit Score: 136.74  E-value: 6.39e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037402861   1 MAELSLSNIVKRFGGF---------EIIHGANLEVKDGEFVVFVGPSGCGKSTLLRMIAGLEDITSGELQIGGRVVNDVE 71
Cdd:PRK10419    1 MTLLNVSGLSHHYAHGglsgkhqhqTVLNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWRGEPLAKLN 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037402861  72 PAD-----RGIAMVFQSY--ALYPHLTVEENLSFGLR-MNGNPKADTERRVSHVAEILQIT-ELMKRRPKQLSGGQRQRV 142
Cdd:PRK10419   81 RAQrkafrRDIQMVFQDSisAVNPRKTVREIIREPLRhLLSLDKAERLARASEMLRAVDLDdSVLDKRPPQLSGGQLQRV 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037402861 143 AIGRAIVREPEVFLFDEPLSNLDAELRVQMRVEISRLHKKLGTTMIYVTHDQTEAMTLADRIVVLRAGNI--EQIGAPLD 220
Cdd:PRK10419  161 CLARALAVEPKLLILDEAVSNLDLVLQAGVIRLLKKLQQQFGTACLFITHDLRLVERFCQRVMVMDNGQIveTQPVGDKL 240


                  ....*...
gi 1037402861 221 LYDDPANQ 228
Cdd:PRK10419  241 TFSSPAGR 248
ABC_drug_resistance_like cd03264
ABC-type multidrug transport system, ATPase component; The biological function of this family ...
 4-216 9.51e-38

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: 134.63  E-value: 9.51e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037402861   4 LSLSNIVKRFGGFEIIHGANLEVKDGEFVVfVGPSGCGKSTLLRMIAGLEDITSGELQIGGR-VVNDVEPADRGIAMVFQ 82
Cdd:cd03264     1 LQLENLTKRYGKKRALDGVSLTLGPGMYGL-LGPNGAGKTTLMRILATLTPPSSGTIRIDGQdVLKQPQKLRRRIGYLPQ 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037402861  83 SYALYPHLTVEENLSFGLRMNGNPKADTERRVSHVAEILQITELMKRRPKQLSGGQRQRVAIGRAIVREPEVFLFDEPLS 162
Cdd:cd03264    80 EFGVYPNFTVREFLDYIAWLKGIPSKEVKARVDEVLELVNLGDRAKKKIGSLSGGMRRRVGIAQALVGDPSILIVDEPTA 159

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1037402861 163 NLDAELRVQMRVEISRLHKklGTTMIYVTHDQTEAMTLADRIVVLRAGNIEQIG 216
Cdd:cd03264   160 GLDPEERIRFRNLLSELGE--DRIVILSTHIVEDVESLCNQVAVLNKGKLVFEG 211
cbiO PRK13634
cobalt transporter ATP-binding subunit; Provisional
 23-226 1.15e-37

cobalt transporter ATP-binding subunit; Provisional


Pssm-ID: 237454 [Multi-domain]  Cd Length: 290  Bit Score: 136.69  E-value: 1.15e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037402861  23 NLEVKDGEFVVFVGPSGCGKSTLLRMIAGLEDITSGELQIGGRVVN------DVEPADRGIAMVFQ--SYALYPHlTVEE 94
Cdd:PRK13634   27 NVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVTIGERVITagkknkKLKPLRKKVGIVFQfpEHQLFEE-TVEK 105

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037402861  95 NLSFGlRMN-GNPKADTERRVSHVAEILQITE-LMKRRPKQLSGGQRQRVAIGRAIVREPEVFLFDEPLSNLDAELRVQM 172
Cdd:PRK13634  106 DICFG-PMNfGVSEEDAKQKAREMIELVGLPEeLLARSPFELSGGQMRRVAIAGVLAMEPEVLVLDEPTAGLDPKGRKEM 184

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1037402861 173 RVEISRLHKKLGTTMIYVTHDQTEAMTLADRIVVLRAGNIEQIGAPLDLYDDPA 226
Cdd:PRK13634  185 MEMFYKLHKEKGLTTVLVTHSMEDAARYADQIVVMHKGTVFLQGTPREIFADPD 238
cbiO PRK13635
energy-coupling factor ABC transporter ATP-binding protein;
1-218 1.29e-37

energy-coupling factor ABC transporter ATP-binding protein;


Pssm-ID: 184195 [Multi-domain]  Cd Length: 279  Bit Score: 136.30  E-value: 1.29e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037402861   1 MAE--LSLSNIVKRFGGFE--IIHGANLEVKDGEFVVFVGPSGCGKSTLLRMIAGLEDITSGELQIGGRVVND--VEPAD 74
Cdd:PRK13635    1 MKEeiIRVEHISFRYPDAAtyALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGGMVLSEetVWDVR 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037402861  75 RGIAMVFQSyalyPH-----LTVEENLSFGLRMNGNPKADTERRVSHVAEILQITELMKRRPKQLSGGQRQRVAIGRAIV 149
Cdd:PRK13635   81 RQVGMVFQN----PDnqfvgATVQDDVAFGLENIGVPREEMVERVDQALRQVGMEDFLNREPHRLSGGQKQRVAIAGVLA 156

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1037402861 150 REPEVFLFDEPLSNLDAELRVQMRVEISRLHKKLGTTMIYVTHDQTEAMTlADRIVVLRAGNIEQIGAP 218
Cdd:PRK13635  157 LQPDIIILDEATSMLDPRGRREVLETVRQLKEQKGITVLSITHDLDEAAQ-ADRVIVMNKGEILEEGTP 224
nickel_nikE TIGR02769
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a ...
 4-256 1.31e-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: 135.70  E-value: 1.31e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037402861   4 LSLSNIVKRF--GGF-------EIIHGANLEVKDGEFVVFVGPSGCGKSTLLRMIAGLEDITSGELQIGGRVVNDVEPAD 74
Cdd:TIGR02769   3 LEVRDVTHTYrtGGLfgakqraPVLTNVSLSIEEGETVGLLGRSGCGKSTLARLLLGLEKPAQGTVSFRGQDLYQLDRKQ 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037402861  75 -----RGIAMVFQ-SY-ALYPHLTVEENLSFGLR-MNGNPKADTERRVSHVAEILQI-TELMKRRPKQLSGGQRQRVAIG 145
Cdd:TIGR02769  83 rrafrRDVQLVFQdSPsAVNPRMTVRQIIGEPLRhLTSLDESEQKARIAELLDMVGLrSEDADKLPRQLSGGQLQRINIA 162

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037402861 146 RAIVREPEVFLFDEPLSNLDAELRVQMRVEISRLHKKLGTTMIYVTHDQTEAMTLADRIVVLRAGNI--EQIGAPLDLYD 223
Cdd:TIGR02769 163 RALAVKPKLIVLDEAVSNLDMVLQAVILELLRKLQQAFGTAYLFITHDLRLVQSFCQRVAVMDKGQIveECDVAQLLSFK 242

                         250       260       270
                  ....*....|....*....|....*....|...
gi 1037402861 224 DPANQfvagfvgspkmnFLKAVVVEAQPGRAVI 256
Cdd:TIGR02769 243 HPAGR------------NLQSAVLPEHPVRRSI 263
metN PRK11153
DL-methionine transporter ATP-binding subunit; Provisional
 6-236 1.96e-37

DL-methionine transporter ATP-binding subunit; Provisional


Pssm-ID: 236863 [Multi-domain]  Cd Length: 343  Bit Score: 137.24  E-value: 1.96e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037402861   6 LSNIVKRFGG----FEIIHGANLEVKDGEFVVFVGPSGCGKSTLLRMIAGLEDITSGELQIGGRVV-----NDVEPADRG 76
Cdd:PRK11153    4 LKNISKVFPQggrtIHALNNVSLHIPAGEIFGVIGASGAGKSTLIRCINLLERPTSGRVLVDGQDLtalseKELRKARRQ 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037402861  77 IAMVFQSYALYPHLTVEENLSFGLRMNGNPKADTERRVSHVAEILQITELMKRRPKQLSGGQRQRVAIGRAIVREPEVFL 156
Cdd:PRK11153   84 IGMIFQHFNLLSSRTVFDNVALPLELAGTPKAEIKARVTELLELVGLSDKADRYPAQLSGGQKQRVAIARALASNPKVLL 163

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037402861 157 FDEPLSNLDAELRVQMRVEISRLHKKLGTTMIYVTHDQTEAMTLADRIVVLRAGNIEQIGAPLDLYDDPANQFVAGFVGS 236
Cdd:PRK11153  164 CDEATSALDPATTRSILELLKDINRELGLTIVLITHEMDVVKRICDRVAVIDAGRLVEQGTVSEVFSHPKHPLTREFIQS 243
PRK14247 PRK14247
phosphate ABC transporter ATP-binding protein; Provisional
 1-234 3.80e-37

phosphate ABC transporter ATP-binding protein; Provisional


Pssm-ID: 172735 [Multi-domain]  Cd Length: 250  Bit Score: 134.27  E-value: 3.80e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037402861   1 MAELSLSNIVKRFGGFEIIHGANLEVKDGEFVVFVGPSGCGKSTLLRMIAGL-----EDITSGELQIGGRVV--NDVEPA 73
Cdd:PRK14247    1 MNKIEIRDLKVSFGQVEVLDGVNLEIPDNTITALMGPSGSGKSTLLRVFNRLielypEARVSGEVYLDGQDIfkMDVIEL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037402861  74 DRGIAMVFQSYALYPHLTVEENLSFGLRMN--GNPKADTERRVSHVAEILQITELMKRR----PKQLSGGQRQRVAIGRA 147
Cdd:PRK14247   81 RRRVQMVFQIPNPIPNLSIFENVALGLKLNrlVKSKKELQERVRWALEKAQLWDEVKDRldapAGKLSGGQQQRLCIARA 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037402861 148 IVREPEVFLFDEPLSNLDAELRVQMRVEISRLHKKLgtTMIYVTHDQTEAMTLADRIVVLRAGNIEQIGAPLDLYDDPAN 227
Cdd:PRK14247  161 LAFQPEVLLADEPTANLDPENTAKIESLFLELKKDM--TIVLVTHFPQQAARISDYVAFLYKGQIVEWGPTREVFTNPRH 238


                  ....*..
gi 1037402861 228 QFVAGFV 234
Cdd:PRK14247  239 ELTEKYV 245
LolD_lipo_ex TIGR02211
lipoprotein releasing system, ATP-binding protein; This model represents LolD, a member of the ...
 4-212 9.03e-37

lipoprotein releasing system, ATP-binding protein; This model represents LolD, a member of the ABC transporter family (pfam00005). LolD is involved in localization of lipoproteins in some bacteria. It works with a transmembrane protein LolC, which in some species is a paralogous pair LolC and LolE. Depending on whether the residue immediately following the new, modified N-terminal Cys residue, the nascent lipoprotein may be carried further by LolA and LolB to the outer membrane, or remain at the inner membrane. The top scoring proteins excluded by this model include homologs from the archaeal genus Methanosarcina. [Protein fate, Protein and peptide secretion and trafficking]


Pssm-ID: 131266 [Multi-domain]  Cd Length: 221  Bit Score: 132.48  E-value: 9.03e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037402861   4 LSLSNIVKRF--GGFEII--HGANLEVKDGEFVVFVGPSGCGKSTLLRMIAGLEDITSGELQIGGRVVNDVEPADRG--- 76
Cdd:TIGR02211   2 LKCENLGKRYqeGKLDTRvlKGVSLSIGKGEIVAIVGSSGSGKSTLLHLLGGLDNPTSGEVLFNGQSLSKLSSNERAklr 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037402861  77 ---IAMVFQSYALYPHLTVEENLSFGLRMNGNPKADTERRVshvAEILQITELMKR---RPKQLSGGQRQRVAIGRAIVR 150
Cdd:TIGR02211  82 nkkLGFIYQFHHLLPDFTALENVAMPLLIGKKSVKEAKERA---YEMLEKVGLEHRinhRPSELSGGERQRVAIARALVN 158

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1037402861 151 EPEVFLFDEPLSNLDAELRVQMRVEISRLHKKLGTTMIYVTHDQTEAMTLaDRIVVLRAGNI 212
Cdd:TIGR02211 159 QPSLVLADEPTGNLDNNNAKIIFDLMLELNRELNTSFLVVTHDLELAKKL-DRVLEMKDGQL 219
ABCC_ATM1_transporter cd03253
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ...
 15-221 1.51e-36

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: 132.35  E-value: 1.51e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037402861  15 GFEIIHGANLEVKDGEFVVFVGPSGCGKSTLLRMIAGLEDITSGELQIGGRVVNDV--EPADRGIAMVFQSYALYpHLTV 92
Cdd:cd03253    13 GRPVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDGQDIREVtlDSLRRAIGVVPQDTVLF-NDTI 91

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037402861  93 EENLSFglrmnGNPKAdTERRVSHVAEILQITELMKRRPKQ-----------LSGGQRQRVAIGRAIVREPEVFLFDEPL 161
Cdd:cd03253    92 GYNIRY-----GRPDA-TDEEVIEAAKAAQIHDKIMRFPDGydtivgerglkLSGGEKQRVAIARAILKNPPILLLDEAT 165

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037402861 162 SNLDAELRVQMRVEISRLHKklGTTMIYVTHDQTEAMTlADRIVVLRAGNIEQIGAPLDL 221
Cdd:cd03253   166 SALDTHTEREIQAALRDVSK--GRTTIVIAHRLSTIVN-ADKIIVLKDGRIVERGTHEEL 222
ModF COG1119
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ...
 4-212 2.45e-36

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: 132.13  E-value: 2.45e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037402861   4 LSLSNIVKRFGGFEIIHGANLEVKDGEFVVFVGPSGCGKSTLLRMIAGLEDITSG-ELQIGGRVVNDVEPAD--RGIAMV 80
Cdd:COG1119     4 LELRNVTVRRGGKTILDDISWTVKPGEHWAILGPNGAGKSTLLSLITGDLPPTYGnDVRLFGERRGGEDVWElrKRIGLV 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037402861  81 fqSYAL----YPHLTVEENL------SFGLRMNgnPKADTERRVSHVAEILQITELMKRRPKQLSGGQRQRVAIGRAIVR 150
Cdd:COG1119    84 --SPALqlrfPRDETVLDVVlsgffdSIGLYRE--PTDEQRERARELLELLGLAHLADRPFGTLSQGEQRRVLIARALVK 159

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1037402861 151 EPEVFLFDEPLSNLDAELRVQMRVEISRLHKKLGTTMIYVTHDQTEAMTLADRIVVLRAGNI 212
Cdd:COG1119   160 DPELLILDEPTAGLDLGARELLLALLDKLAAEGAPTLVLVTHHVEEIPPGITHVLLLKDGRV 221
urea_trans_UrtE TIGR03410
urea ABC transporter, ATP-binding protein UrtE; Members of this protein family are ABC ...
 4-231 3.02e-36

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: 131.11  E-value: 3.02e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037402861   4 LSLSNIVKRFGGFEIIHGANLEVKDGEFVVFVGPSGCGKSTLLRMIAGLEDITSGELQIGGRVVNDVEP---ADRGIAMV 80
Cdd:TIGR03410   1 LEVSNLNVYYGQSHILRGVSLEVPKGEVTCVLGRNGVGKTTLLKTLMGLLPVKSGSIRLDGEDITKLPPherARAGIAYV 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037402861  81 FQSYALYPHLTVEENLSFGLrmngNPKADTERRVshVAEILQI----TELMKRRPKQLSGGQRQRVAIGRAIVREPEVFL 156
Cdd:TIGR03410  81 PQGREIFPRLTVEENLLTGL----AALPRRSRKI--PDEIYELfpvlKEMLGRRGGDLSGGQQQQLAIARALVTRPKLLL 154

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1037402861 157 FDEPLSNLDAELRVQMRVEISRLHKKLGTTMIYVTHDQTEAMTLADRIVVLRAGNIEQIGAPLDLYDDPANQFVA 231
Cdd:TIGR03410 155 LDEPTEGIQPSIIKDIGRVIRRLRAEGGMAILLVEQYLDFARELADRYYVMERGRVVASGAGDELDEDKVRRYLA 229
YejF COG4172
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ...
 11-225 4.58e-36

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


Pssm-ID: 443332 [Multi-domain]  Cd Length: 533  Bit Score: 137.12  E-value: 4.58e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037402861  11 KRFGGFEIIHGANLEVKDGEFVVFVGPSGCGKSTLLRMIAGLEDiTSGELQIGGRVVNDVEPAD-----RGIAMVFQS-Y 84
Cdd:COG4172   294 RTVGHVKAVDGVSLTLRRGETLGLVGESGSGKSTLGLALLRLIP-SEGEIRFDGQDLDGLSRRAlrplrRRMQVVFQDpF 372

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037402861  85 A-LYPHLTVEENLSFGLRMNGNPKADTERRvSHVAEILQITEL----MKRRPKQLSGGQRQRVAIGRAIVREPEVFLFDE 159
Cdd:COG4172   373 GsLSPRMTVGQIIAEGLRVHGPGLSAAERR-ARVAEALEEVGLdpaaRHRYPHEFSGGQRQRIAIARALILEPKLLVLDE 451

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1037402861 160 PLSNLDAELRVQMrVEI-SRLHKKLGTTMIYVTHDQTEAMTLADRIVVLRAGNI-EQiGAPLDLYDDP 225
Cdd:COG4172   452 PTSALDVSVQAQI-LDLlRDLQREHGLAYLFISHDLAVVRALAHRVMVMKDGKVvEQ-GPTEQVFDAP 517
ABC_putative_ATPase cd03269
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ...
 4-210 1.21e-35

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: 128.94  E-value: 1.21e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037402861   4 LSLSNIVKRFGGFEIIHGANLEVKDGEFVVFVGPSGCGKSTLLRMIAGLEDITSGELQIGGRVVNDVE-------PADRG 76
Cdd:cd03269     1 LEVENVTKRFGRVTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDGKPLDIAArnrigylPEERG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037402861  77 iamvfqsyaLYPHLTVEENLSFGLRMNGNPKADTERRVSHVAEILQITELMKRRPKQLSGGQRQRVAIGRAIVREPEVFL 156
Cdd:cd03269    81 ---------LYPKMKVIDQLVYLAQLKGLKKEEARRRIDEWLERLELSEYANKRVEELSKGNQQKVQFIAAVIHDPELLI 151

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1037402861 157 FDEPLSNLDAELRVQMRVEISRLHKKlGTTMIYVTHDQTEAMTLADRIVVLRAG 210
Cdd:cd03269   152 LDEPFSGLDPVNVELLKDVIRELARA-GKTVILSTHQMELVEELCDRVLLLNKG 204
ABC_YhbG cd03218
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ...
 4-226 5.30e-35

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: 128.04  E-value: 5.30e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037402861   4 LSLSNIVKRFGGFEIIHGANLEVKDGEFVVFVGPSGCGKSTLLRMIAGLEDITSGELQIGGRVVNDVEP---ADRGIAMV 80
Cdd:cd03218     1 LRAENLSKRYGKRKVVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDGQDITKLPMhkrARLGIGYL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037402861  81 FQSYALYPHLTVEENLSFGLRMNGNPKADTERRVSHVAEILQITELMKRRPKQLSGGQRQRVAIGRAIVREPEVFLFDEP 160
Cdd:cd03218    81 PQEASIFRKLTVEENILAVLEIRGLSKKEREEKLEELLEEFHITHLRKSKASSLSGGERRRVEIARALATNPKFLLLDEP 160

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1037402861 161 LSNLDAeLRVQmrvEISRLHKKLGTTMIYV---THDQTEAMTLADRIVVLRAGNIEQIGAPLDLYDDPA 226
Cdd:cd03218   161 FAGVDP-IAVQ---DIQKIIKILKDRGIGVlitDHNVRETLSITDRAYIIYEGKVLAEGTPEEIAANEL 225
cbiO PRK13650
energy-coupling factor transporter ATPase;
26-222 6.15e-35

energy-coupling factor transporter ATPase;


Pssm-ID: 184209 [Multi-domain]  Cd Length: 279  Bit Score: 129.08  E-value: 6.15e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037402861  26 VKDGEFVVFVGPSGCGKSTLLRMIAGLEDITSGELQIGGRVV--NDVEPADRGIAMVFQSyalyPH-----LTVEENLSF 98
Cdd:PRK13650   30 VKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIIDGDLLteENVWDIRHKIGMVFQN----PDnqfvgATVEDDVAF 105

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037402861  99 GLRMNGNPKADTERRVSHVAEILQITELMKRRPKQLSGGQRQRVAIGRAIVREPEVFLFDEPLSNLDAELRVQMRVEISR 178
Cdd:PRK13650  106 GLENKGIPHEEMKERVNEALELVGMQDFKEREPARLSGGQKQRVAIAGAVAMRPKIIILDEATSMLDPEGRLELIKTIKG 185

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 1037402861 179 LHKKLGTTMIYVTHDQTEaMTLADRIVVLRAGNIEQIGAPLDLY 222
Cdd:PRK13650  186 IRDDYQMTVISITHDLDE-VALSDRVLVMKNGQVESTSTPRELF 228
ABC_cobalt_CbiO_domain2 cd03226
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ...
 5-212 7.44e-35

Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of the ABC component of a cobalt transport family found in bacteria, archaea, and eukaryota. The transition metal cobalt is an essential component of many enzymes and must be transported into cells in appropriate amounts when needed. The CbiMNQO family ABC transport system is involved in cobalt transport in association with the cobalamin (vitamin B12) biosynthetic pathways. Most cobalt (Cbi) transport systems possess a separate CbiN component, the cobalt-binding periplasmic protein, and they are encoded by the conserved gene cluster cbiMNQO. Both the CbiM and CbiQ proteins are integral cytoplasmic membrane proteins, and the CbiO protein has the linker peptide and the Walker A and B motifs commonly found in the ATPase components of the ABC-type transport systems.


Pssm-ID: 213193 [Multi-domain]  Cd Length: 205  Bit Score: 126.60  E-value: 7.44e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037402861   5 SLSNIVKRFG-GFEIIHGANLEVKDGEFVVFVGPSGCGKSTLLRMIAGLEDITSGELQIGGRVVNDVEPAdRGIAMVFQS 83
Cdd:cd03226     1 RIENISFSYKkGTEILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLNGKPIKAKERR-KSIGYVMQD 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037402861  84 --YALYPHlTVEENLSFGLRmngnPKADTERRVSHVAEILQITELMKRRPKQLSGGQRQRVAIGRAIVREPEVFLFDEPL 161
Cdd:cd03226    80 vdYQLFTD-SVREELLLGLK----ELDAGNEQAETVLKDLDLYALKERHPLSLSGGQKQRLAIAAALLSGKDLLIFDEPT 154

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1037402861 162 SNLDAElrvQMRvEISRLHKKL---GTTMIYVTHDQTEAMTLADRIVVLRAGNI 212
Cdd:cd03226   155 SGLDYK---NME-RVGELIRELaaqGKAVIVITHDYEFLAKVCDRVLLLANGAI 204
PRK14267 PRK14267
phosphate ABC transporter ATP-binding protein; Provisional
 13-234 1.00e-34

phosphate ABC transporter ATP-binding protein; Provisional


Pssm-ID: 184596 [Multi-domain]  Cd Length: 253  Bit Score: 128.04  E-value: 1.00e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037402861  13 FGGFEIIHGANLEVKDGEFVVFVGPSGCGKSTLLRMIAGLEDIT-----SGELQIGGRVV--NDVEPAD--RGIAMVFQS 83
Cdd:PRK14267   14 YGSNHVIKGVDLKIPQNGVFALMGPSGCGKSTLLRTFNRLLELNeearvEGEVRLFGRNIysPDVDPIEvrREVGMVFQY 93

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037402861  84 YALYPHLTVEENLSFGLRMNG--NPKADTERRVSHVAEILQITELMKRR----PKQLSGGQRQRVAIGRAIVREPEVFLF 157
Cdd:PRK14267   94 PNPFPHLTIYDNVAIGVKLNGlvKSKKELDERVEWALKKAALWDEVKDRlndyPSNLSGGQRQRLVIARALAMKPKILLM 173

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1037402861 158 DEPLSNLDAELRVQMRVEISRLHKKLgtTMIYVTHDQTEAMTLADRIVVLRAGNIEQIGAPLDLYDDPANQFVAGFV 234
Cdd:PRK14267  174 DEPTANIDPVGTAKIEELLFELKKEY--TIVLVTHSPAQAARVSDYVAFLYLGKLIEVGPTRKVFENPEHELTEKYV 248
ABC_MTABC3_MDL1_MDL2 cd03249
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ...
 17-222 1.07e-34

ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 (also known as ABCB6) is a mitochondrial ATP-binding cassette protein involved in iron homeostasis and one of four ABC transporters expressed in the mitochondrial inner membrane, the other three being MDL1(ABC7), MDL2, and ATM1. In fact, the yeast MDL1 (multidrug resistance-like protein 1) and MDL2 (multidrug resistance-like protein 2) transporters are also included in this CD. MDL1 is an ATP-dependent permease that acts as a high-copy suppressor of ATM1 and is thought to have a role in resistance to oxidative stress. Interestingly, subfamily B is more closely related to the carboxyl-terminal component of subfamily C than the two halves of ABCC molecules are with one another.


Pssm-ID: 213216 [Multi-domain]  Cd Length: 238  Bit Score: 127.27  E-value: 1.07e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037402861  17 EIIHGANLEVKDGEFVVFVGPSGCGKSTLLRMIAGLEDITSGELQIGGRVVNDVEPAD--RGIAMVFQSYALYPhLTVEE 94
Cdd:cd03249    17 PILKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEILLDGVDIRDLNLRWlrSQIGLVSQEPVLFD-GTIAE 95

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037402861  95 NLSFGLRmngNPKADTERRVSHVAEILQ-ITELMKR-------RPKQLSGGQRQRVAIGRAIVREPEVFLFDEPLSNLDA 166
Cdd:cd03249    96 NIRYGKP---DATDEEVEEAAKKANIHDfIMSLPDGydtlvgeRGSQLSGGQKQRIAIARALLRNPKILLLDEATSALDA 172

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037402861 167 --ELRVQMRVEisRLHKklGTTMIYVTHDQTeamTL--ADRIVVLRAGNIEQIGAPLDLY 222
Cdd:cd03249   173 esEKLVQEALD--RAMK--GRTTIVIAHRLS---TIrnADLIAVLQNGQVVEQGTHDELM 225
ABCC_bacteriocin_exporters cd03245
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ...
 3-212 1.16e-34

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: 126.55  E-value: 1.16e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037402861   3 ELSLSNIVKRFGGFEI--IHGANLEVKDGEFVVFVGPSGCGKSTLLRMIAGLEDITSGELQIGGRVVNDVEPAD--RGIA 78
Cdd:cd03245     2 RIEFRNVSFSYPNQEIpaLDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGTDIRQLDPADlrRNIG 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037402861  79 MVFQSyalyPHL---TVEENLSFGlrmngNPKADTERrVSHVAEILQITELMKRRPK-----------QLSGGQRQRVAI 144
Cdd:cd03245    82 YVPQD----VTLfygTLRDNITLG-----APLADDER-ILRAAELAGVTDFVNKHPNgldlqigergrGLSGGQRQAVAL 151

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1037402861 145 GRAIVREPEVFLFDEPLSNLD--AELRVqmrveISRLHKKLGT-TMIYVTHdQTEAMTLADRIVVLRAGNI 212
Cdd:cd03245   152 ARALLNDPPILLLDEPTSAMDmnSEERL-----KERLRQLLGDkTLIIITH-RPSLLDLVDRIIVMDSGRI 216
ABCC_MsbA cd03251
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ...
 4-224 1.48e-34

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


Pssm-ID: 213218 [Multi-domain]  Cd Length: 234  Bit Score: 126.96  E-value: 1.48e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037402861   4 LSLSNIVKRFGGFE--IIHGANLEVKDGEFVVFVGPSGCGKSTLLRMIAGLEDITSGELQIGGRVVNDVEPAD--RGIAM 79
Cdd:cd03251     1 VEFKNVTFRYPGDGppVLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDGHDVRDYTLASlrRQIGL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037402861  80 VFQSYALYpHLTVEENLSFGlrmngNPKAdTERRVSHVAEILQITELMKRRPK-----------QLSGGQRQRVAIGRAI 148
Cdd:cd03251    81 VSQDVFLF-NDTVAENIAYG-----RPGA-TREEVEEAARAANAHEFIMELPEgydtvigergvKLSGGQRQRIAIARAL 153

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1037402861 149 VREPEVFLFDEPLSNLDAELRVQMRVEISRLHKklGTTMIYVTHDQTEAMTlADRIVVLRAGNIEQIGAPLDLYDD 224
Cdd:cd03251   154 LKDPPILILDEATSALDTESERLVQAALERLMK--NRTTFVIAHRLSTIEN-ADRIVVLEDGKIVERGTHEELLAQ 226
ABC_NatA_like cd03267
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ...
 5-224 5.97e-34

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: 125.52  E-value: 5.97e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037402861   5 SLSNIVKR-FGGFEIIHGANLEVKDGEFVVFVGPSGCGKSTLLRMIAGLEDITSGELQIGGRVvndvePADRG------I 77
Cdd:cd03267    22 SLKSLFKRkYREVEALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRVAGLV-----PWKRRkkflrrI 96

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037402861  78 AMVF-QSYALYPHLTVEENLSFGLRMNGNPKADTERRVSHVAEILQITELMKRRPKQLSGGQRQRVAIGRAIVREPEVFL 156
Cdd:cd03267    97 GVVFgQKTQLWWDLPVIDSFYLLAAIYDLPPARFKKRLDELSELLDLEELLDTPVRQLSLGQRMRAEIAAALLHEPEILF 176

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1037402861 157 FDEPLSNLDAELRVQMRVEISRLHKKLGTTMIYVTHDQTEAMTLADRIVVLRAGNIeqigapldLYDD 224
Cdd:cd03267   177 LDEPTIGLDVVAQENIRNFLKEYNRERGTTVLLTSHYMKDIEALARRVLVIDKGRL--------LYDG 236
AztA NF040873
zinc ABC transporter ATP-binding protein AztA;
12-207 4.48e-33

zinc ABC transporter ATP-binding protein AztA;


Pssm-ID: 468810 [Multi-domain]  Cd Length: 191  Bit Score: 121.57  E-value: 4.48e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037402861  12 RFGGFEIIHGANLEVKDGEFVVFVGPSGCGKSTLLRMIAGLEDITSGELQIGGrvvndvepaDRGIAMVFQSYAL---YP 88
Cdd:NF040873    1 GYGGRPVLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTVRRAG---------GARVAYVPQRSEVpdsLP 71

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037402861  89 hLTVEENLSFGL----RMNGNPKADTERRVSHVAEILQITELMKRRPKQLSGGQRQRVAIGRAIVREPEVFLFDEPLSNL 164
Cdd:NF040873   72 -LTVRDLVAMGRwarrGLWRRLTRDDRAAVDDALERVGLADLAGRQLGELSGGQRQRALLAQGLAQEADLLLLDEPTTGL 150

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 1037402861 165 DAELRVQMRVEISRLHKKlGTTMIYVTHDQTEAMtLADRIVVL 207
Cdd:NF040873  151 DAESRERIIALLAEEHAR-GATVVVVTHDLELVR-RADPCVLL 191
PstB COG1117
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ...
 13-228 4.56e-33

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


Pssm-ID: 440734 [Multi-domain]  Cd Length: 258  Bit Score: 123.61  E-value: 4.56e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037402861  13 FGGFEIIHGANLEVKDGEFVVFVGPSGCGKSTLLRMIAGLEDI-----TSGELQIGGRVVND--VEPAD--RGIAMVFQS 83
Cdd:COG1117    21 YGDKQALKDINLDIPENKVTALIGPSGCGKSTLLRCLNRMNDLipgarVEGEILLDGEDIYDpdVDVVElrRRVGMVFQK 100

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037402861  84 YALYPHlTVEENLSFGLRMNG-NPKADTERRVSHVaeiLQITEL---MKRRPKQ----LSGGQRQRVAIGRAIVREPEVF 155
Cdd:COG1117   101 PNPFPK-SIYDNVAYGLRLHGiKSKSELDEIVEES---LRKAALwdeVKDRLKKsalgLSGGQQQRLCIARALAVEPEVL 176

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1037402861 156 LFDEPLSNLD--AElrvqMRVE--ISRLHKKLgtTMIYVTHDQTEAMTLADRIVVLRAGNIEQIGAPLDLYDDPANQ 228
Cdd:COG1117   177 LMDEPTSALDpiST----AKIEelILELKKDY--TIVIVTHNMQQAARVSDYTAFFYLGELVEFGPTEQIFTNPKDK 247
type_I_sec_LssB TIGR03375
type I secretion system ATPase, LssB family; Type I protein secretion is a system in some ...
 19-212 6.84e-33

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: 129.60  E-value: 6.84e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037402861  19 IHGANLEVKDGEFVVFVGPSGCGKSTLLRMIAGLEDITSGELQIGGRVVNDVEPAD--RGIAMVFQSYALYpHLTVEENL 96
Cdd:TIGR03375 481 LDNVSLTIRPGEKVAIIGRIGSGKSTLLKLLLGLYQPTEGSVLLDGVDIRQIDPADlrRNIGYVPQDPRLF-YGTLRDNI 559

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037402861  97 SFGlrmngNPKADtERRVSHVAEILQITELMKRRPK-----------QLSGGQRQRVAIGRAIVREPEVFLFDEPLSNLD 165
Cdd:TIGR03375 560 ALG-----APYAD-DEEILRAAELAGVTEFVRRHPDgldmqigergrSLSGGQRQAVALARALLRDPPILLLDEPTSAMD 633

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 1037402861 166 AelRVQMRVeISRLHKKL-GTTMIYVTHdQTEAMTLADRIVVLRAGNI 212
Cdd:TIGR03375 634 N--RSEERF-KDRLKRWLaGKTLVLVTH-RTSLLDLVDRIIVMDNGRI 677
ABCG_EPDR cd03213
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ...
 1-212 7.51e-33

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: 121.12  E-value: 7.51e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037402861   1 MAELSLSNI---VKRF---GGFEIIHGANLEVKDGEFVVFVGPSGCGKSTLLRMIAGLED--ITSGELQIGGRVVNDVEP 72
Cdd:cd03213     1 GVTLSFRNLtvtVKSSpskSGKQLLKNVSGKAKPGELTAIMGPSGAGKSTLLNALAGRRTglGVSGEVLINGRPLDKRSF 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037402861  73 ADRgIAMVFQSYALYPHLTVEENLSFGLRMngnpkadterrvshvaeilqitelmkrrpKQLSGGQRQRVAIGRAIVREP 152
Cdd:cd03213    81 RKI-IGYVPQDDILHPTLTVRETLMFAAKL-----------------------------RGLSGGERKRVSIALELVSNP 130

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1037402861 153 EVFLFDEPLSNLDAELRVQMRVEISRLhKKLGTTMIYVTHD-QTEAMTLADRIVVLRAGNI 212
Cdd:cd03213   131 SLLFLDEPTSGLDSSSALQVMSLLRRL-ADTGRTIICSIHQpSSEIFELFDKLLLLSQGRV 190
met_CoM_red_A2 TIGR03269
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ...
 4-218 9.54e-33

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: 128.00  E-value: 9.54e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037402861   4 LSLSNIVKRF-----GGFEIIHGANLEVKDGEFVVFVGPSGCGKSTLLRMIAGLEDITSGEL--QIGGRVVNDVEP---- 72
Cdd:TIGR03269 280 IKVRNVSKRYisvdrGVVKAVDNVSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGEVnvRVGDEWVDMTKPgpdg 359

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037402861  73 ---ADRGIAMVFQSYALYPHLTVEENL--SFGLRMngnPKADTERRVSHVAEILQITE-----LMKRRPKQLSGGQRQRV 142
Cdd:TIGR03269 360 rgrAKRYIGILHQEYDLYPHRTVLDNLteAIGLEL---PDELARMKAVITLKMVGFDEekaeeILDKYPDELSEGERHRV 436

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1037402861 143 AIGRAIVREPEVFLFDEPLSNLDAELRVQMRVEISRLHKKLGTTMIYVTHDQTEAMTLADRIVVLRAGNIEQIGAP 218
Cdd:TIGR03269 437 ALAQVLIKEPRIVILDEPTGTMDPITKVDVTHSILKAREEMEQTFIIVSHDMDFVLDVCDRAALMRDGKIVKIGDP 512
COG4559 COG4559
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism];
4-218 1.08e-32

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


Pssm-ID: 443620 [Multi-domain]  Cd Length: 258  Bit Score: 122.53  E-value: 1.08e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037402861   4 LSLSNIVKRFGGFEIIHGANLEVKDGEFVVFVGPSGCGKSTLLRMIAGLEDITSGELQIGGRVVNDVEPAD--RGIAMVF 81
Cdd:COG4559     2 LEAENLSVRLGGRTLLDDVSLTLRPGELTAIIGPNGAGKSTLLKLLTGELTPSSGEVRLNGRPLAAWSPWElaRRRAVLP 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037402861  82 QSYALYPHLTVEENLSFGLRMNGNPKADTERRVSHVAEILQITELMKRRPKQLSGGQRQRVAIGRAI------VREPEVF 155
Cdd:COG4559    82 QHSSLAFPFTVEEVVALGRAPHGSSAAQDRQIVREALALVGLAHLAGRSYQTLSGGEQQRVQLARVLaqlwepVDGGPRW 161

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1037402861 156 LF-DEPLSNLDaeLRVQMRV-EISRLHKKLGTTMIYVTHDQTEAMTLADRIVVLRAGNIEQIGAP 218
Cdd:COG4559   162 LFlDEPTSALD--LAHQHAVlRLARQLARRGGGVVAVLHDLNLAAQYADRILLLHQGRLVAQGTP 224
hmuV PRK13548
hemin importer ATP-binding subunit; Provisional
 4-218 6.96e-32

hemin importer ATP-binding subunit; Provisional


Pssm-ID: 237422 [Multi-domain]  Cd Length: 258  Bit Score: 120.26  E-value: 6.96e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037402861   4 LSLSNIVKRFGGFEIIHGANLEVKDGEFVVFVGPSGCGKSTLLRMIAGLEDITSGELQIGGRVVNDVEPAD--RGIAMVF 81
Cdd:PRK13548    3 LEARNLSVRLGGRTLLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLNGRPLADWSPAElaRRRAVLP 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037402861  82 QSYAL-YPhLTVEENLSFGLRMNGNPKADTERRVSHVAEILQITELMKRRPKQLSGGQRQRVAIGRAIVR------EPEV 154
Cdd:PRK13548   83 QHSSLsFP-FTVEEVVAMGRAPHGLSRAEDDALVAAALAQVDLAHLAGRDYPQLSGGEQQRVQLARVLAQlwepdgPPRW 161

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1037402861 155 FLFDEPLSNLDaeLRVQMRV-EISR-LHKKLGTTMIYVTHDQTEAMTLADRIVVLRAGNIEQIGAP 218
Cdd:PRK13548  162 LLLDEPTSALD--LAHQHHVlRLARqLAHERGLAVIVVLHDLNLAARYADRIVLLHQGRLVADGTP 225
ABCC_Glucan_exporter_like cd03254
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ...
 18-221 9.17e-32

ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan exporter ATP-binding protein. In A. tumefaciens cyclic beta-1, 2-glucan must be transported into the periplasmic space to exert its action as a virulence factor. This subfamily belongs to the MRP-like family and is involved in drug, peptide, and lipid export. The MRP-like family, similar to all ABC proteins, have a common four-domain core structure constituted by two membrane-spanning domains each composed of six transmembrane (TM) helices and two nucleotide-binding domains (NBD). ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.


Pssm-ID: 213221 [Multi-domain]  Cd Length: 229  Bit Score: 119.25  E-value: 9.17e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037402861  18 IIHGANLEVKDGEFVVFVGPSGCGKSTLLRMIAGLEDITSGELQIGGRVVNDVEPAD--RGIAMVFQSYALYPHlTVEEN 95
Cdd:cd03254    18 VLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGIDIRDISRKSlrSMIGVVLQDTFLFSG-TIMEN 96

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037402861  96 LSFglrmnGNPKAdTERRVSHVAEILQITELMKRRPK-----------QLSGGQRQRVAIGRAIVREPEVFLFDEPLSNL 164
Cdd:cd03254    97 IRL-----GRPNA-TDEEVIEAAKEAGAHDFIMKLPNgydtvlgenggNLSQGERQLLAIARAMLRDPKILILDEATSNI 170

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1037402861 165 D--AELRVQMRVEisRLHKklGTTMIYVTHDQTeamTL--ADRIVVLRAGNIEQIGAPLDL 221
Cdd:cd03254   171 DteTEKLIQEALE--KLMK--GRTSIIIAHRLS---TIknADKILVLDDGKIIEEGTHDEL 224
lolD PRK11629
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
17-214 1.19e-31

lipoprotein-releasing ABC transporter ATP-binding protein LolD;


Pssm-ID: 183244 [Multi-domain]  Cd Length: 233  Bit Score: 119.15  E-value: 1.19e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037402861  17 EIIHGANLEVKDGEFVVFVGPSGCGKSTLLRMIAGLEDITSGELQIGGRVVNDVEPA------DRGIAMVFQSYALYPHL 90
Cdd:PRK11629   23 DVLHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPMSKLSSAakaelrNQKLGFIYQFHHLLPDF 102

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037402861  91 TVEENLSFGLRMNGNPKADTERRVShvaEILQITELMKR---RPKQLSGGQRQRVAIGRAIVREPEVFLFDEPLSNLDAE 167
Cdd:PRK11629  103 TALENVAMPLLIGKKKPAEINSRAL---EMLAAVGLEHRanhRPSELSGGERQRVAIARALVNNPRLVLADEPTGNLDAR 179

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 1037402861 168 LRVQMRVEISRLHKKLGTTMIYVTHDqteaMTLADRI---VVLRAGNIEQ 214
Cdd:PRK11629  180 NADSIFQLLGELNRLQGTAFLVVTHD----LQLAKRMsrqLEMRDGRLTA 225
LptB COG1137
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ...
 1-225 1.27e-31

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


Pssm-ID: 440752 [Multi-domain]  Cd Length: 240  Bit Score: 119.36  E-value: 1.27e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037402861   1 MAELSLSNIVKRFGGFEIIHGANLEVKDGEFVVFVGPSGCGKSTLLRMIAGLEDITSGELQIGGRVVNDVeP----ADRG 76
Cdd:COG1137     1 MMTLEAENLVKSYGKRTVVKDVSLEVNQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGRIFLDGEDITHL-PmhkrARLG 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037402861  77 I------AMVFQsyalypHLTVEENLSFGLRMNGNPKADTERRVSHVAEILQITELMKRRPKQLSGGQRQRVAIGRAIVR 150
Cdd:COG1137    80 IgylpqeASIFR------KLTVEDNILAVLELRKLSKKEREERLEELLEEFGITHLRKSKAYSLSGGERRRVEIARALAT 153

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037402861 151 EPEVFLFDEPLSNLD----AELRvQMrveISRLHKK-LGttmIYVT-HDQTEAMTLADRIVVLRAGNIEQIGAPLDLYDD 224
Cdd:COG1137   154 NPKFILLDEPFAGVDpiavADIQ-KI---IRHLKERgIG---VLITdHNVRETLGICDRAYIISEGKVLAEGTPEEILNN 226


                  .
gi 1037402861 225 P 225
Cdd:COG1137   227 P 227
ABCC_Protease_Secretion cd03246
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ...
 4-212 1.70e-31

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: 116.93  E-value: 1.70e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037402861   4 LSLSNIVKRFGGFE--IIHGANLEVKDGEFVVFVGPSGCGKSTLLRMIAGLEDITSGELQIGGRVVNDVEPADRG--IAM 79
Cdd:cd03246     1 LEVENVSFRYPGAEppVLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDGADISQWDPNELGdhVGY 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037402861  80 VFQSYALYPHlTVEENLsfglrmngnpkadterrvshvaeilqitelmkrrpkqLSGGQRQRVAIGRAIVREPEVFLFDE 159
Cdd:cd03246    81 LPQDDELFSG-SIAENI-------------------------------------LSGGQRQRLGLARALYGNPRILVLDE 122

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1037402861 160 PLSNLDAELRVQMRVEISRLhKKLGTTMIYVTHdQTEAMTLADRIVVLRAGNI 212
Cdd:cd03246   123 PNSHLDVEGERALNQAIAAL-KAAGATRIVIAH-RPETLASADRILVLEDGRV 173
ABC_KpsT_Wzt cd03220
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ...
 10-216 2.03e-31

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: 118.40  E-value: 2.03e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037402861  10 VKRFGGFEIIHGANLEVKDGEFVVFVGPSGCGKSTLLRMIAGLEDITSGELQIGGRVVndvepadrgiAMVFQSYALYPH 89
Cdd:cd03220    29 KGEVGEFWALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVTVRGRVS----------SLLGLGGGFNPE 98

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037402861  90 LTVEENLSFGLRMNGNPKADTERRvshVAEILQITEL---MKRRPKQLSGGQRQRVAIGRAIVREPEVFLFDEPLSNLDA 166
Cdd:cd03220    99 LTGRENIYLNGRLLGLSRKEIDEK---IDEIIEFSELgdfIDLPVKTYSSGMKARLAFAIATALEPDILLIDEVLAVGDA 175

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 1037402861 167 ELRVQMRVEISRLHKKlGTTMIYVTHDQTEAMTLADRIVVLRAGNIEQIG 216
Cdd:cd03220   176 AFQEKCQRRLRELLKQ-GKTVILVSHDPSSIKRLCDRALVLEKGKIRFDG 224
CydD TIGR02857
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ...
 3-207 7.50e-31

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: 122.40  E-value: 7.50e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037402861   3 ELSLSNIVKRFGG-FEIIHGANLEVKDGEFVVFVGPSGCGKSTLLRMIAGLEDITSGELQIGGRVVNDVEPAD--RGIAM 79
Cdd:TIGR02857 321 SLEFSGVSVAYPGrRPALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSIAVNGVPLADADADSwrDQIAW 400

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037402861  80 VFQSYALYPHlTVEENLSFGLRmngNPKADTERRVSHVAEILQITE--------LMKRRPKQLSGGQRQRVAIGRAIVRE 151
Cdd:TIGR02857 401 VPQHPFLFAG-TIAENIRLARP---DASDAEIREALERAGLDEFVAalpqgldtPIGEGGAGLSGGQAQRLALARAFLRD 476

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1037402861 152 PEVFLFDEPLSNLDAELRVQMRVEISRLHKklGTTMIYVTHDqTEAMTLADRIVVL 207
Cdd:TIGR02857 477 APLLLLDEPTAHLDAETEAEVLEALRALAQ--GRTVLLVTHR-LALAALADRIVVL 529
TagH COG1134
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ...
 11-222 1.06e-30

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


Pssm-ID: 440749 [Multi-domain]  Cd Length: 245  Bit Score: 116.72  E-value: 1.06e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037402861  11 KRFGGFEIIHGANLEVKDGEFVVFVGPSGCGKSTLLRMIAGLEDITSGELQIGGRVVNDVEpadrgIAMVFQsyalyPHL 90
Cdd:COG1134    34 TRREEFWALKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTSGRVEVNGRVSALLE-----LGAGFH-----PEL 103

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037402861  91 TVEENLSFGLRMNGNPKADTERRVSHVAEILQITELMKRRPKQLSGGQRQRVAIGRAIVREPEVFLFDEPLSNLDAELRV 170
Cdd:COG1134   104 TGRENIYLNGRLLGLSRKEIDEKFDEIVEFAELGDFIDQPVKTYSSGMRARLAFAVATAVDPDILLVDEVLAVGDAAFQK 183

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1037402861 171 QMRVEISRLHKKlGTTMIYVTHDQTEAMTLADRIVVLRAGNIEQIGAP---LDLY 222
Cdd:COG1134   184 KCLARIRELRES-GRTVIFVSHSMGAVRRLCDRAIWLEKGRLVMDGDPeevIAAY 237
cbiO PRK13642
energy-coupling factor transporter ATPase;
19-222 1.67e-30

energy-coupling factor transporter ATPase;


Pssm-ID: 184202 [Multi-domain]  Cd Length: 277  Bit Score: 117.50  E-value: 1.67e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037402861  19 IHGANLEVKDGEFVVFVGPSGCGKSTLLRMIAGLEDITSGELQIGGR--VVNDVEPADRGIAMVFQSY-ALYPHLTVEEN 95
Cdd:PRK13642   23 LNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDGEllTAENVWNLRRKIGMVFQNPdNQFVGATVEDD 102

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037402861  96 LSFGLRMNGNPKADTERRVSHVAEILQITELMKRRPKQLSGGQRQRVAIGRAIVREPEVFLFDEPLSNLDAELRVQMRVE 175
Cdd:PRK13642  103 VAFGMENQGIPREEMIKRVDEALLAVNMLDFKTREPARLSGGQKQRVAVAGIIALRPEIIILDESTSMLDPTGRQEIMRV 182

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 1037402861 176 ISRLHKKLGTTMIYVTHDQTEAMTlADRIVVLRAGNIEQIGAPLDLY 222
Cdd:PRK13642  183 IHEIKEKYQLTVLSITHDLDEAAS-SDRILVMKAGEIIKEAAPSELF 228
PhnK COG1101
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ...
 4-212 1.76e-30

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


Pssm-ID: 440718 [Multi-domain]  Cd Length: 264  Bit Score: 116.72  E-value: 1.76e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037402861   4 LSLSNIVKRFG-GF----EIIHGANLEVKDGEFVVFVGPSGCGKSTLLRMIAGLEDITSGELQIGGRVVNDVEPADRG-- 76
Cdd:COG1101     2 LELKNLSKTFNpGTvnekRALDGLNLTIEEGDFVTVIGSNGAGKSTLLNAIAGSLPPDSGSILIDGKDVTKLPEYKRAky 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037402861  77 IAMVFQSYAL--YPHLTVEENLS--------FGLRMnGNPKADTErrvsHVAEILQITEL-----MKRRPKQLSGGQRQR 141
Cdd:COG1101    82 IGRVFQDPMMgtAPSMTIEENLAlayrrgkrRGLRR-GLTKKRRE----LFRELLATLGLglenrLDTKVGLLSGGQRQA 156

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1037402861 142 VAIGRAIVREPEVFLFDEPLSNLD---AELRVQMRVEISRLHkKLGTTMiyVTHDQTEAMTLADRIVVLRAGNI 212
Cdd:COG1101   157 LSLLMATLTKPKLLLLDEHTAALDpktAALVLELTEKIVEEN-NLTTLM--VTHNMEQALDYGNRLIMMHEGRI 227
nickel_nikD TIGR02770
nickel import ATP-binding protein NikD; This family represents the NikD subunit of a ...
 18-227 3.71e-30

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


Pssm-ID: 131817 [Multi-domain]  Cd Length: 230  Bit Score: 115.16  E-value: 3.71e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037402861  18 IIHGANLEVKDGEFVVFVGPSGCGKSTLLRMIAGLED----ITSGELQIGGRVVNDVEPADRGIAMVFQS--YALYPHLT 91
Cdd:TIGR02770   1 LVQDLNLSLKRGEVLALVGESGSGKSLTCLAILGLLPpgltQTSGEILLDGRPLLPLSIRGRHIATIMQNprTAFNPLFT 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037402861  92 VEENLSFGLRMNGNPKADTERRVSHVAE---ILQITELMKRRPKQLSGGQRQRVAIGRAIVREPEVFLFDEPLSNLDAEL 168
Cdd:TIGR02770  81 MGNHAIETLRSLGKLSKQARALILEALEavgLPDPEEVLKKYPFQLSGGMLQRVMIALALLLEPPFLIADEPTTDLDVVN 160

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1037402861 169 RVQMRVEISRLHKKLGTTMIYVTHDQTEAMTLADRIVVLRAGNIEQIGAPLDLYDDPAN 227
Cdd:TIGR02770 161 QARVLKLLRELRQLFGTGILLITHDLGVVARIADEVAVMDDGRIVERGTVKEIFYNPKH 219
PRK10584 PRK10584
putative ABC transporter ATP-binding protein YbbA; Provisional
 18-214 4.09e-30

putative ABC transporter ATP-binding protein YbbA; Provisional


Pssm-ID: 182569 [Multi-domain]  Cd Length: 228  Bit Score: 114.88  E-value: 4.09e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037402861  18 IIHGANLEVKDGEFVVFVGPSGCGKSTLLRMIAGLEDITSGELQIGGRVVNDVEPADRG------IAMVFQSYALYPHLT 91
Cdd:PRK10584   25 ILTGVELVVKRGETIALIGESGSGKSTLLAILAGLDDGSSGEVSLVGQPLHQMDEEARAklrakhVGFVFQSFMLIPTLN 104

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037402861  92 VEENLSFGLRMNGNPKADTERRVSHVAEILQITELMKRRPKQLSGGQRQRVAIGRAIVREPEVFLFDEPLSNLDAELRVQ 171
Cdd:PRK10584  105 ALENVELPALLRGESSRQSRNGAKALLEQLGLGKRLDHLPAQLSGGEQQRVALARAFNGRPDVLFADEPTGNLDRQTGDK 184

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 1037402861 172 MRVEISRLHKKLGTTMIYVTHDQTEAMTlADRIVVLRAGNIEQ 214
Cdd:PRK10584  185 IADLLFSLNREHGTTLILVTHDLQLAAR-CDRRLRLVNGQLQE 226
cbiO PRK13643
energy-coupling factor transporter ATPase;
23-238 5.51e-30

energy-coupling factor transporter ATPase;


Pssm-ID: 184203 [Multi-domain]  Cd Length: 288  Bit Score: 116.37  E-value: 5.51e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037402861  23 NLEVKDGEFVVFVGPSGCGKSTLLRMIAGLEDITSGELQIGGRVVN------DVEPADRGIAMVFQ--SYALYPHlTVEE 94
Cdd:PRK13643   26 DLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVTVGDIVVSstskqkEIKPVRKKVGVVFQfpESQLFEE-TVLK 104

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037402861  95 NLSFGLRMNGNPKADTERRVSHVAEILQIT-ELMKRRPKQLSGGQRQRVAIGRAIVREPEVFLFDEPLSNLDAELRVQMR 173
Cdd:PRK13643  105 DVAFGPQNFGIPKEKAEKIAAEKLEMVGLAdEFWEKSPFELSGGQMRRVAIAGILAMEPEVLVLDEPTAGLDPKARIEMM 184

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1037402861 174 VEISRLHKKlGTTMIYVTHDQTEAMTLADRIVVLRAGNIEQIGAPLDLYDDpANQFVAGFVGSPK 238
Cdd:PRK13643  185 QLFESIHQS-GQTVVLVTHLMDDVADYADYVYLLEKGHIISCGTPSDVFQE-VDFLKAHELGVPK 247
PRK10908 PRK10908
cell division ATP-binding protein FtsE;
13-212 6.22e-30

cell division ATP-binding protein FtsE;


Pssm-ID: 182829 [Multi-domain]  Cd Length: 222  Bit Score: 114.20  E-value: 6.22e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037402861  13 FGGFEIIHGANLEVKDGEFVVFVGPSGCGKSTLLRMIAGLEDITSGELQIGGRVVNDVEPAD-----RGIAMVFQSYALY 87
Cdd:PRK10908   12 LGGRQALQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDITRLKNREvpflrRQIGMIFQDHHLL 91

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037402861  88 PHLTVEENLSFGLRMNGNPKADTERRVSHVAEILQITELMKRRPKQLSGGQRQRVAIGRAIVREPEVFLFDEPLSNLDAE 167
Cdd:PRK10908   92 MDRTVYDNVAIPLIIAGASGDDIRRRVSAALDKVGLLDKAKNFPIQLSGGEQQRVGIARAVVNKPAVLLADEPTGNLDDA 171

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 1037402861 168 LrvqmRVEISRLHK---KLGTTMIYVTHDQTEAMTLADRIVVLRAGNI 212
Cdd:PRK10908  172 L----SEGILRLFEefnRVGVTVLMATHDIGLISRRSYRMLTLSDGHL 215
PRK15079 PRK15079
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
 21-225 6.57e-30

oligopeptide ABC transporter ATP-binding protein OppF; Provisional


Pssm-ID: 185037 [Multi-domain]  Cd Length: 331  Bit Score: 117.11  E-value: 6.57e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037402861  21 GANLEVKDGEFVVFVGPSGCGKSTLLRMIAGLEDITSGELQIGGRVVNDVEPADR-----GIAMVFQS--YALYPHLTVE 93
Cdd:PRK15079   39 GVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGEVAWLGKDLLGMKDDEWravrsDIQMIFQDplASLNPRMTIG 118

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037402861  94 ENLSFGLRMNgNPKADTERRVSHVAEILQ----ITELMKRRPKQLSGGQRQRVAIGRAIVREPEVFLFDEPLSNLDAELR 169
Cdd:PRK15079  119 EIIAEPLRTY-HPKLSRQEVKDRVKAMMLkvglLPNLINRYPHEFSGGQCQRIGIARALILEPKLIICDEPVSALDVSIQ 197

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1037402861 170 VQMRVEISRLHKKLGTTMIYVTHDQTEAMTLADRIVVLRAGNIEQIGAPLDLYDDP 225
Cdd:PRK15079  198 AQVVNLLQQLQREMGLSLIFIAHDLAVVKHISDRVLVMYLGHAVELGTYDEVYHNP 253
anch_rpt_ABC TIGR03771
anchored repeat-type ABC transporter, ATP-binding subunit; This protein family is the ...
 24-223 1.00e-29

anchored repeat-type ABC transporter, ATP-binding subunit; This protein family is the ATP-binding cassette subunit of binding protein-dependent ABC transporter complex that strictly co-occurs with TIGR03769. TIGRFAMs model TIGR03769 describes a protein domain that occurs singly or as one of up to three repeats in proteins of a number of Actinobacteria, including Propionibacterium acnes KPA171202. The TIGR03769 domain occurs both in an adjacent gene for the substrate-binding protein and in additional (often nearby) proteins, often with LPXTG-like sortase recognition signals. Homologous ATP-binding subunits outside the scope of this family include manganese transporter MntA in Synechocystis sp. PCC 6803 and chelated iron transporter subunits. The function of this transporter complex is unknown. [Transport and binding proteins, Unknown substrate]


Pssm-ID: 163483 [Multi-domain]  Cd Length: 223  Bit Score: 113.79  E-value: 1.00e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037402861  24 LEVKDGEFVVFVGPSGCGKSTLLRMIAGLEDITSGELQIGGRvvnDVEPADRGIAMVFQSYAL---YPHLTVEENLSFGL 100
Cdd:TIGR03771   1 LSADKGELLGLLGPNGAGKTTLLRAILGLIPPAKGTVKVAGA---SPGKGWRHIGYVPQRHEFawdFPISVAHTVMSGRT 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037402861 101 RMNG---NPKADTERRVSHVAEILQITELMKRRPKQLSGGQRQRVAIGRAIVREPEVFLFDEPLSNLD---AELRVQMRV 174
Cdd:TIGR03771  78 GHIGwlrRPCVADFAAVRDALRRVGLTELADRPVGELSGGQRQRVLVARALATRPSVLLLDEPFTGLDmptQELLTELFI 157

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 1037402861 175 EISrlhkKLGTTMIYVTHDQTEAMTLADRIVVLRaGNIEQIGAPLDLYD 223
Cdd:TIGR03771 158 ELA----GAGTAILMTTHDLAQAMATCDRVVLLN-GRVIADGTPQQLQD 201
dppF PRK11308
dipeptide transporter ATP-binding subunit; Provisional
 10-225 2.78e-29

dipeptide transporter ATP-binding subunit; Provisional


Pssm-ID: 236898 [Multi-domain]  Cd Length: 327  Bit Score: 115.06  E-value: 2.78e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037402861  10 VKRFGG--FEIIHGANLEVkdgefvvfVGPSGCGKSTLLRMIAGLEDITSGELQIGGRVVNDVEPAD-----RGIAMVFQ 82
Cdd:PRK11308   28 VKALDGvsFTLERGKTLAV--------VGESGCGKSTLARLLTMIETPTGGELYYQGQDLLKADPEAqkllrQKIQIVFQ 99

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037402861  83 S-YA-LYPHLTVEENLSFGLRMNGNPKAdTERRvSHVAEILQI----TELMKRRPKQLSGGQRQRVAIGRAIVREPEVFL 156
Cdd:PRK11308  100 NpYGsLNPRKKVGQILEEPLLINTSLSA-AERR-EKALAMMAKvglrPEHYDRYPHMFSGGQRQRIAIARALMLDPDVVV 177

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1037402861 157 FDEPLSNLDAELRVQMRVEISRLHKKLGTTMIYVTHDQTEAMTLADRIVVLRAGNIEQIGAPLDLYDDP 225
Cdd:PRK11308  178 ADEPVSALDVSVQAQVLNLMMDLQQELGLSYVFISHDLSVVEHIADEVMVMYLGRCVEKGTKEQIFNNP 246
fecE PRK11231
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
18-218 5.07e-29

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


Pssm-ID: 183044 [Multi-domain]  Cd Length: 255  Bit Score: 112.80  E-value: 5.07e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037402861  18 IIHGANLEVKDGEFVVFVGPSGCGKSTLLRMIAGLEDITSGELQIGGRVVNDVepADRGIAmvfQSYALYP--HLT---- 91
Cdd:PRK11231   17 ILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDKPISML--SSRQLA---RRLALLPqhHLTpegi 91

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037402861  92 -VEENLSFG----LRMNGNPKADTERRVSHVAEILQITELMKRRPKQLSGGQRQRVAIGRAIVREPEVFLFDEPLSNLDa 166
Cdd:PRK11231   92 tVRELVAYGrspwLSLWGRLSAEDNARVNQAMEQTRINHLADRRLTDLSGGQRQRAFLAMVLAQDTPVVLLDEPTTYLD- 170

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1037402861 167 elrVQMRVEISRLHKKL---GTTMIYVTHDQTEAMTLADRIVVLRAGNIEQIGAP 218
Cdd:PRK11231  171 ---INHQVELMRLMRELntqGKTVVTVLHDLNQASRYCDHLVVLANGHVMAQGTP 222
ArpD COG4618
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ...
 2-217 6.56e-29

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: 117.16  E-value: 6.56e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037402861   2 AELSLSNIVKRFGGFE--IIHGANLEVKDGEFVVFVGPSGCGKSTLLRMIAGLEDITSGELQIGGRVVNDVEPADRG--I 77
Cdd:COG4618   329 GRLSVENLTVVPPGSKrpILRGVSFSLEPGEVLGVIGPSGSGKSTLARLLVGVWPPTAGSVRLDGADLSQWDREELGrhI 408

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037402861  78 AMVFQSYALYPHlTVEENLSfglRMngnPKADTErRVSHVAEILQITELMKRRPK-----------QLSGGQRQRVAIGR 146
Cdd:COG4618   409 GYLPQDVELFDG-TIAENIA---RF---GDADPE-KVVAAAKLAGVHEMILRLPDgydtrigeggaRLSGGQRQRIGLAR 480

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1037402861 147 AIVREPEVFLFDEPLSNLDAELRVQMRVEISRLhKKLGTTMIYVTHDQTeAMTLADRIVVLRAGNIEQIGA 217
Cdd:COG4618   481 ALYGDPRLVVLDEPNSNLDDEGEAALAAAIRAL-KARGATVVVITHRPS-LLAAVDKLLVLRDGRVQAFGP 549
cbiO PRK13644
energy-coupling factor transporter ATPase;
23-230 9.41e-29

energy-coupling factor transporter ATPase;


Pssm-ID: 106587 [Multi-domain]  Cd Length: 274  Bit Score: 112.39  E-value: 9.41e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037402861  23 NLEVKDGEFVVFVGPSGCGKSTLLRMIAGLEDITSGELQIGGRVVND---VEPADRGIAMVFQS-YALYPHLTVEENLSF 98
Cdd:PRK13644   22 NLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLVSGIDTGDfskLQGIRKLVGIVFQNpETQFVGRTVEEDLAF 101

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037402861  99 GLRMNGNPKADTERRVSHVAEILQITELMKRRPKQLSGGQRQRVAIGRAIVREPEVFLFDEPLSNLDAELRVQMRVEISR 178
Cdd:PRK13644  102 GPENLCLPPIEIRKRVDRALAEIGLEKYRHRSPKTLSGGQGQCVALAGILTMEPECLIFDEVTSMLDPDSGIAVLERIKK 181

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1037402861 179 LHKKlGTTMIYVTHDqTEAMTLADRIVVLRAGNIEQIGAPLDLYDDPANQFV 230
Cdd:PRK13644  182 LHEK-GKTIVYITHN-LEELHDADRIIVMDRGKIVLEGEPENVLSDVSLQTL 231
PRK10535 PRK10535
macrolide ABC transporter ATP-binding protein/permease MacB;
2-233 1.19e-28

macrolide ABC transporter ATP-binding protein/permease MacB;


Pssm-ID: 182528 [Multi-domain]  Cd Length: 648  Bit Score: 117.13  E-value: 1.19e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037402861   2 AELSLSNIVKRF----GGFEIIHGANLEVKDGEFVVFVGPSGCGKSTLLRMIAGLEDITSGELQIGGRVVNDVEPADRGI 77
Cdd:PRK10535    3 ALLELKDIRRSYpsgeEQVEVLKGISLDIYAGEMVAIVGASGSGKSTLMNILGCLDKPTSGTYRVAGQDVATLDADALAQ 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037402861  78 ------AMVFQSYALYPHLTVEENLSFGLRMNGNPKADTERRVSHVAEILQITELMKRRPKQLSGGQRQRVAIGRAIVRE 151
Cdd:PRK10535   83 lrrehfGFIFQRYHLLSHLTAAQNVEVPAVYAGLERKQRLLRAQELLQRLGLEDRVEYQPSQLSGGQQQRVSIARALMNG 162

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037402861 152 PEVFLFDEPLSNLDAELRVQMRVEISRLHKKlGTTMIYVTHDQTEAMTlADRIVVLRAGNI----------EQIGAPLDL 221
Cdd:PRK10535  163 GQVILADEPTGALDSHSGEEVMAILHQLRDR-GHTVIIVTHDPQVAAQ-AERVIEIRDGEIvrnppaqekvNVAGGTEPV 240

                         250
                  ....*....|....
gi 1037402861 222 YDDPA--NQFVAGF 233
Cdd:PRK10535  241 VNTASgwRQFVSGF 254
cbiO PRK13645
energy-coupling factor transporter ATPase;
16-224 2.48e-28

energy-coupling factor transporter ATPase;


Pssm-ID: 184204 [Multi-domain]  Cd Length: 289  Bit Score: 111.64  E-value: 2.48e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037402861  16 FEIIHGANLEVKDGEFVVFVGPSGCGKSTLLRMIAGLEDITSGELQIGG-------RVVNDVEPADRGIAMVFQ--SYAL 86
Cdd:PRK13645   24 FKALNNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGLIISETGQTIVGDyaipanlKKIKEVKRLRKEIGLVFQfpEYQL 103

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037402861  87 YPHlTVEENLSFGLRMNGNPKADTERRVSHVAEILQI-TELMKRRPKQLSGGQRQRVAIGRAIVREPEVFLFDEPLSNLD 165
Cdd:PRK13645  104 FQE-TIEKDIAFGPVNLGENKQEAYKKVPELLKLVQLpEDYVKRSPFELSGGQKRRVALAGIIAMDGNTLVLDEPTGGLD 182

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1037402861 166 AELRVQMRVEISRLHKKLGTTMIYVTHDQTEAMTLADRIVVLRAGNIEQIGAPLDLYDD 224
Cdd:PRK13645  183 PKGEEDFINLFERLNKEYKKRIIMVTHNMDQVLRIADEVIVMHEGKVISIGSPFEIFSN 241
ABCC_MRP_domain1 cd03250
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ...
 18-210 2.71e-28

ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This subfamily is also known as MRP (multidrug resistance-associated protein). Some of the MRP members have five additional transmembrane segments in their N-terminus, but the function of these additional membrane-spanning domains is not clear. The MRP was found in the multidrug-resisting lung cancer cell in which p-glycoprotein was not overexpressed. MRP exports glutathione by drug stimulation, as well as, certain substrates in conjugated forms with anions, such as glutathione, glucuronate, and sulfate.


Pssm-ID: 213217 [Multi-domain]  Cd Length: 204  Bit Score: 109.48  E-value: 2.71e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037402861  18 IIHGANLEVKDGEFVVFVGPSGCGKSTLLRMIAGLEDITSGELQIGGRvvndvepadrgIAMVFQSyalyPHL---TVEE 94
Cdd:cd03250    20 TLKDINLEVPKGELVAIVGPVGSGKSSLLSALLGELEKLSGSVSVPGS-----------IAYVSQE----PWIqngTIRE 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037402861  95 NLSFGLRMNgnpkadtERRVSHVAEILQITELMKRRPKQ-----------LSGGQRQRVAIGRAIVREPEVFLFDEPLSN 163
Cdd:cd03250    85 NILFGKPFD-------EERYEKVIKACALEPDLEILPDGdlteigekginLSGGQKQRISLARAVYSDADIYLLDDPLSA 157

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 1037402861 164 LDAELRVQMRVEISRLHKKLGTTMIYVTHdQTEAMTLADRIVVLRAG 210
Cdd:cd03250   158 VDAHVGRHIFENCILGLLLNNKTRILVTH-QLQLLPHADQIVVLDNG 203
PRK14243 PRK14243
phosphate transporter ATP-binding protein; Provisional
 13-202 4.17e-28

phosphate transporter ATP-binding protein; Provisional


Pssm-ID: 184588 [Multi-domain]  Cd Length: 264  Bit Score: 110.64  E-value: 4.17e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037402861  13 FGGFEIIHGANLEVKDGEFVVFVGPSGCGKSTLLRMIAGLEDITSGeLQIGGRVV--------NDVEPAD--RGIAMVFQ 82
Cdd:PRK14243   20 YGSFLAVKNVWLDIPKNQITAFIGPSGCGKSTILRCFNRLNDLIPG-FRVEGKVTfhgknlyaPDVDPVEvrRRIGMVFQ 98

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037402861  83 SYALYPHlTVEENLSFGLRMNGNpKAD----TERRVSHVAEILQITELMKRRPKQLSGGQRQRVAIGRAIVREPEVFLFD 158
Cdd:PRK14243   99 KPNPFPK-SIYDNIAYGARINGY-KGDmdelVERSLRQAALWDEVKDKLKQSGLSLSGGQQQRLCIARAIAVQPEVILMD 176

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 1037402861 159 EPLSNLD--AELRVQmrveisRLHKKLGT--TMIYVTHDQTEAMTLAD 202
Cdd:PRK14243  177 EPCSALDpiSTLRIE------ELMHELKEqyTIIIVTHNMQQAARVSD 218
COG4586 COG4586
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ...
 19-233 5.50e-28

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


Pssm-ID: 443643 [Multi-domain]  Cd Length: 323  Bit Score: 111.33  E-value: 5.50e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037402861  19 IHGANLEVKDGEFVVFVGPSGCGKSTLLRMIAGLEDITSGELQIGGRVvndvePAD------RGIAMVF-QSYALYPHLT 91
Cdd:COG4586    38 VDDISFTIEPGEIVGFIGPNGAGKSTTIKMLTGILVPTSGEVRVLGYV-----PFKrrkefaRRIGVVFgQRSQLWWDLP 112

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037402861  92 VEEnlSFGL--RMNGNPKADTERRVSHVAEILQITELMKRRPKQLSGGQRQRVAIGRAIVREPEVFLFDEPLSNLDAELR 169
Cdd:COG4586   113 AID--SFRLlkAIYRIPDAEYKKRLDELVELLDLGELLDTPVRQLSLGQRMRCELAAALLHRPKILFLDEPTIGLDVVSK 190

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1037402861 170 VQMRVEISRLHKKLGTTMIYVTHDQTEAMTLADRIVVLRAGNIeqigapldLYDDPANQFVAGF 233
Cdd:COG4586   191 EAIREFLKEYNRERGTTILLTSHDMDDIEALCDRVIVIDHGRI--------IYDGSLEELKERF 246
PRK14239 PRK14239
phosphate transporter ATP-binding protein; Provisional
 4-228 7.63e-28

phosphate transporter ATP-binding protein; Provisional


Pssm-ID: 184585 [Multi-domain]  Cd Length: 252  Bit Score: 109.48  E-value: 7.63e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037402861   4 LSLSNIVKRFGGFEIIHGANLEVKDGEFVVFVGPSGCGKSTLLRMIAGLEDI-----TSGELQIGGRVV----NDVEPAD 74
Cdd:PRK14239    6 LQVSDLSVYYNKKKALNSVSLDFYPNEITALIGPSGSGKSTLLRSINRMNDLnpevtITGSIVYNGHNIysprTDTVDLR 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037402861  75 RGIAMVFQSYALYPhLTVEENLSFGLRMNG-NPKADTERRVSHVAEILQITELMKRRPKQ----LSGGQRQRVAIGRAIV 149
Cdd:PRK14239   86 KEIGMVFQQPNPFP-MSIYENVVYGLRLKGiKDKQVLDEAVEKSLKGASIWDEVKDRLHDsalgLSGGQQQRVCIARVLA 164

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1037402861 150 REPEVFLFDEPLSNLDAelRVQMRVEISRLHKKLGTTMIYVTHDQTEAMTLADRIVVLRAGNIEQIGAPLDLYDDPANQ 228
Cdd:PRK14239  165 TSPKIILLDEPTSALDP--ISAGKIEETLLGLKDDYTMLLVTRSMQQASRISDRTGFFLDGDLIEYNDTKQMFMNPKHK 241
btuD PRK09536
corrinoid ABC transporter ATPase; Reviewed
 1-306 9.24e-28

corrinoid ABC transporter ATPase; Reviewed


Pssm-ID: 236554 [Multi-domain]  Cd Length: 402  Bit Score: 112.24  E-value: 9.24e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037402861   1 MAELSLSNIVKRFGGFEIIHGANLEVKDGEFVVFVGPSGCGKSTLLRMIAGLEDITSGELQIGGRVVN--DVEPADRGIA 78
Cdd:PRK09536    1 MPMIDVSDLSVEFGDTTVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGDDVEalSARAASRRVA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037402861  79 MVFQSYALYPHLTVEENLSFGL-----RMNGNPKADtERRVSHVAEILQITELMKRRPKQLSGGQRQRVAIGRAIVREPE 153
Cdd:PRK09536   81 SVPQDTSLSFEFDVRQVVEMGRtphrsRFDTWTETD-RAAVERAMERTGVAQFADRPVTSLSGGERQRVLLARALAQATP 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037402861 154 VFLFDEPLSNLDAELRVQMRVEISRLHKKlGTTMIYVTHDQTEAMTLADRIVVLRAGNIEQIGAPLDLYDDP-------A 226
Cdd:PRK09536  160 VLLLDEPTASLDINHQVRTLELVRRLVDD-GKTAVAAIHDLDLAARYCDELVLLADGRVRAAGPPADVLTADtlraafdA 238

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037402861 227 NQFVAG--FVGSPKMNFLKAVVVEAQPGRAVIALESDANMRLPLpVAAPIETGAKVTLGIRPEhfvdagmGDADLTVAID 304
Cdd:PRK09536  239 RTAVGTdpATGAPTVTPLPDPDRTEAAADTRVHVVGGGQPAARA-VSRLVAAGASVSVGPVPE-------GDTAAETAAR 310


                  ..
gi 1037402861 305 VA 306
Cdd:PRK09536  311 VG 312
cbiO PRK13648
cobalt transporter ATP-binding subunit; Provisional
 29-224 1.06e-27

cobalt transporter ATP-binding subunit; Provisional


Pssm-ID: 184207 [Multi-domain]  Cd Length: 269  Bit Score: 109.46  E-value: 1.06e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037402861  29 GEFVVFVGPSGCGKSTLLRMIAGLEDITSGELQIGGRVVNDVEPAD--RGIAMVFQSyalyPH-----LTVEENLSFGLR 101
Cdd:PRK13648   35 GQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIFYNNQAITDDNFEKlrKHIGIVFQN----PDnqfvgSIVKYDVAFGLE 110

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037402861 102 MNGNPKADTERRVSHVAEILQITELMKRRPKQLSGGQRQRVAIGRAIVREPEVFLFDEPLSNLDAELRVQMRVEISRLHK 181
Cdd:PRK13648  111 NHAVPYDEMHRRVSEALKQVDMLERADYEPNALSGGQKQRVAIAGVLALNPSVIILDEATSMLDPDARQNLLDLVRKVKS 190

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 1037402861 182 KLGTTMIYVTHDQTEAMTlADRIVVLRAGNIEQIGAPLDLYDD 224
Cdd:PRK13648  191 EHNITIISITHDLSEAME-ADHVIVMNKGTVYKEGTPTEIFDH 232
PRK09984 PRK09984
phosphonate ABC transporter ATP-binding protein;
4-229 1.15e-27

phosphonate ABC transporter ATP-binding protein;


Pssm-ID: 182182 [Multi-domain]  Cd Length: 262  Bit Score: 109.33  E-value: 1.15e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037402861   4 LSLSNIVKRFGGFEIIHGANLEVKDGEFVVFVGPSGCGKSTLLRMIAGL--EDITSGE--------LQIGGRVVNDVEPA 73
Cdd:PRK09984    5 IRVEKLAKTFNQHQALHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGLitGDKSAGShiellgrtVQREGRLARDIRKS 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037402861  74 DRGIAMVFQSYALYPHLTVEENLSFGlRMNGNPKADT---------ERRVSHVAEILQITELMKRRPKQLSGGQRQRVAI 144
Cdd:PRK09984   85 RANTGYIFQQFNLVNRLSVLENVLIG-ALGSTPFWRTcfswftreqKQRALQALTRVGMVHFAHQRVSTLSGGQQQRVAI 163

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037402861 145 GRAIVREPEVFLFDEPLSNLDAE-LRVQMRVeISRLHKKLGTTMIYVTHDQTEAMTLADRIVVLRAGNIeqigapldLYD 223
Cdd:PRK09984  164 ARALMQQAKVILADEPIASLDPEsARIVMDT-LRDINQNDGITVVVTLHQVDYALRYCERIVALRQGHV--------FYD 234


                  ....*.
gi 1037402861 224 DPANQF 229
Cdd:PRK09984  235 GSSQQF 240
araG PRK11288
L-arabinose ABC transporter ATP-binding protein AraG;
1-210 1.32e-27

L-arabinose ABC transporter ATP-binding protein AraG;


Pssm-ID: 183077 [Multi-domain]  Cd Length: 501  Bit Score: 113.08  E-value: 1.32e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037402861   1 MAELSLSNIVKRFGGFEIIHGANLEVKDGEFVVFVGPSGCGKSTLLRMIAGLEDITSGELQIGGRVV---NDVEPADRGI 77
Cdd:PRK11288    2 SPYLSFDGIGKTFPGVKALDDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSILIDGQEMrfaSTTAALAAGV 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037402861  78 AMVFQSYALYPHLTVEENL-------SFGLRMNGNPKADTERRVSHVAEilqitELMKRRP-KQLSGGQRQRVAIGRAIV 149
Cdd:PRK11288   82 AIIYQELHLVPEMTVAENLylgqlphKGGIVNRRLLNYEAREQLEHLGV-----DIDPDTPlKYLSIGQRQMVEIAKALA 156

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1037402861 150 REPEVFLFDEPLSNLDA-ELRVQMRVeISRLHKKlGTTMIYVTHDQTEAMTLADRIVVLRAG 210
Cdd:PRK11288  157 RNARVIAFDEPTSSLSArEIEQLFRV-IRELRAE-GRVILYVSHRMEEIFALCDAITVFKDG 216
ABCG_White cd03234
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ...
 18-212 3.78e-27

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: 106.97  E-value: 3.78e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037402861  18 IIHGANLEVKDGEFVVFVGPSGCGKSTLLRMIAGLED---ITSGELQIGGRVVNDVEPADRgIAMVFQSYALYPHLTVEE 94
Cdd:cd03234    22 ILNDVSLHVESGQVMAILGSSGSGKTTLLDAISGRVEgggTTSGQILFNGQPRKPDQFQKC-VAYVRQDDILLPGLTVRE 100

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037402861  95 NLSFGLRM-NGNPKADTERRVSHVAEILQ---ITELMKRRPKQLSGGQRQRVAIGRAIVREPEVFLFDEPLSNLDAELRV 170
Cdd:cd03234   101 TLTYTAILrLPRKSSDAIRKKRVEDVLLRdlaLTRIGGNLVKGISGGERRRVSIAVQLLWDPKVLILDEPTSGLDSFTAL 180

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 1037402861 171 QMRVEISRLHKKLGTTMIYVTHDQTEAMTLADRIVVLRAGNI 212
Cdd:cd03234   181 NLVSTLSQLARRNRIVILTIHQPRSDLFRLFDRILLLSSGEI 222
PRK13633 PRK13633
energy-coupling factor transporter ATPase;
23-224 3.95e-27

energy-coupling factor transporter ATPase;


Pssm-ID: 237453 [Multi-domain]  Cd Length: 280  Bit Score: 108.25  E-value: 3.95e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037402861  23 NLEVKDGEFVVFVGPSGCGKSTLLRMIAGLEDITSGELQIGGRVVNDVE---PADRGIAMVFQSyalyPH-----LTVEE 94
Cdd:PRK13633   30 NLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVYVDGLDTSDEEnlwDIRNKAGMVFQN----PDnqivaTIVEE 105

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037402861  95 NLSFGLRMNGNPKADTERRVSHVAEILQITELMKRRPKQLSGGQRQRVAIGRAIVREPEVFLFDEPLSNLDAELRVQMRV 174
Cdd:PRK13633  106 DVAFGPENLGIPPEEIRERVDESLKKVGMYEYRRHAPHLLSGGQKQRVAIAGILAMRPECIIFDEPTAMLDPSGRREVVN 185

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 1037402861 175 EISRLHKKLGTTMIYVTHDQTEAMTlADRIVVLRAGNIEQIGAPLDLYDD 224
Cdd:PRK13633  186 TIKELNKKYGITIILITHYMEEAVE-ADRIIVMDSGKVVMEGTPKEIFKE 234
cbiO PRK13649
energy-coupling factor transporter ATPase;
21-224 4.52e-27

energy-coupling factor transporter ATPase;


Pssm-ID: 184208 [Multi-domain]  Cd Length: 280  Bit Score: 107.91  E-value: 4.52e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037402861  21 GANLEVKDGEFVVFVGPSGCGKSTLLRMIAGLEDITSGELQIGGRVVN------DVEPADRGIAMVFQsyalYPHL---- 90
Cdd:PRK13649   25 DVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDDTLITstsknkDIKQIRKKVGLVFQ----FPESqlfe 100

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037402861  91 -TVEENLSFGLRMNGNPKADTERRVSHVAEILQITE-LMKRRPKQLSGGQRQRVAIGRAIVREPEVFLFDEPLSNLDAEL 168
Cdd:PRK13649  101 eTVLKDVAFGPQNFGVSQEEAEALAREKLALVGISEsLFEKNPFELSGGQMRRVAIAGILAMEPKILVLDEPTAGLDPKG 180

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1037402861 169 RVQMRVEISRLHKKlGTTMIYVTHDQTEAMTLADRIVVLRAGNIEQIGAPLDLYDD 224
Cdd:PRK13649  181 RKELMTLFKKLHQS-GMTIVLVTHLMDDVANYADFVYVLEKGKLVLSGKPKDIFQD 235
PRK10253 PRK10253
iron-enterobactin ABC transporter ATP-binding protein;
13-218 6.43e-27

iron-enterobactin ABC transporter ATP-binding protein;


Pssm-ID: 182336 [Multi-domain]  Cd Length: 265  Bit Score: 107.38  E-value: 6.43e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037402861  13 FGGFEIIHGANLEVKDGEFVVFVGPSGCGKSTLLRMIAGLEDITSGELQIGGRVVNDVEPAD--RGIAMVFQSYALYPHL 90
Cdd:PRK10253   17 YGKYTVAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIQHYASKEvaRRIGLLAQNATTPGDI 96

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037402861  91 TVEENLSFGlRMNGNP-----KADTERRVSHVAEILQITELMKRRPKQLSGGQRQRVAIGRAIVREPEVFLFDEPLSNLD 165
Cdd:PRK10253   97 TVQELVARG-RYPHQPlftrwRKEDEEAVTKAMQATGITHLADQSVDTLSGGQRQRAWIAMVLAQETAIMLLDEPTTWLD 175

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1037402861 166 AELRVQMRVEISRLHKKLGTTMIYVTHDQTEAMTLADRIVVLRAGNIEQIGAP 218
Cdd:PRK10253  176 ISHQIDLLELLSELNREKGYTLAAVLHDLNQACRYASHLIALREGKIVAQGAP 228
PRK10247 PRK10247
putative ABC transporter ATP-binding protein YbbL; Provisional
 4-214 8.14e-27

putative ABC transporter ATP-binding protein YbbL; Provisional


Pssm-ID: 182331 [Multi-domain]  Cd Length: 225  Bit Score: 105.95  E-value: 8.14e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037402861   4 LSLSNIVKRFGGFEIIHGANLEVKDGEFVVFVGPSGCGKSTLLRMIAGLEDITSGELQIGGRVVNDVEPAD--RGIAMVF 81
Cdd:PRK10247    8 LQLQNVGYLAGDAKILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFEGEDISTLKPEIyrQQVSYCA 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037402861  82 QSYALYPHlTVEENLSFGLRMNgNPKADTERRVSHVAEILQITELMKRRPKQLSGGQRQRVAIGRAIVREPEVFLFDEPL 161
Cdd:PRK10247   88 QTPTLFGD-TVYDNLIFPWQIR-NQQPDPAIFLDDLERFALPDTILTKNIAELSGGEKQRISLIRNLQFMPKVLLLDEIT 165

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1037402861 162 SNLDAELRVQMRVEISRLHKKLGTTMIYVTHDQTEaMTLADRIVVL--RAGNIEQ 214
Cdd:PRK10247  166 SALDESNKHNVNEIIHRYVREQNIAVLWVTHDKDE-INHADKVITLqpHAGEMQE 219
type_I_sec_PrtD TIGR01842
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in ...
 3-216 1.01e-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: 110.90  E-value: 1.01e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037402861   3 ELSLSNIVKRFGGFE--IIHGANLEVKDGEFVVFVGPSGCGKSTLLRMIAGLEDITSGELQIGGRVVNDVEPADRG--IA 78
Cdd:TIGR01842 316 HLSVENVTIVPPGGKkpTLRGISFSLQAGEALAIIGPSGSGKSTLARLIVGIWPPTSGSVRLDGADLKQWDRETFGkhIG 395

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037402861  79 MVFQSYALYPHlTVEENLSfglRMNGNPKAdteRRVSHVAEILQITELMKRRPK-----------QLSGGQRQRVAIGRA 147
Cdd:TIGR01842 396 YLPQDVELFPG-TVAENIA---RFGENADP---EKIIEAAKLAGVHELILRLPDgydtvigpggaTLSGGQRQRIALARA 468

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1037402861 148 IVREPEVFLFDEPLSNLDAELRVQMRVEISRLhKKLGTTMIYVTHdQTEAMTLADRIVVLRAGNIEQIG 216
Cdd:TIGR01842 469 LYGDPKLVVLDEPNSNLDEEGEQALANAIKAL-KARGITVVVITH-RPSLLGCVDKILVLQDGRIARFG 535
YejF COG4172
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ...
 4-226 1.26e-26

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: 110.54  E-value: 1.26e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037402861   4 LSLSNIVKRFGG----FEIIHGANLEVKDGEFVVFVGPSGCGKS----TLLRMIAGLEDITSGELQIGGRVVNDVEPAD- 74
Cdd:COG4172     7 LSVEDLSVAFGQgggtVEAVKGVSFDIAAGETLALVGESGSGKSvtalSILRLLPDPAAHPSGSILFDGQDLLGLSEREl 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037402861  75 ---RG--IAMVFQ--SYALYPHLTVEENLSFGLRM-NGNPKADTERRVshvAEILQITEL------MKRRPKQLSGGQRQ 140
Cdd:COG4172    87 rriRGnrIAMIFQepMTSLNPLHTIGKQIAEVLRLhRGLSGAAARARA---LELLERVGIpdperrLDAYPHQLSGGQRQ 163

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037402861 141 RVAIGRAIVREPEVFLFDEPLSNLDAELRVQMRVEISRLHKKLGTTMIYVTHDQTEAMTLADRIVVLRAGNIEQIGAPLD 220
Cdd:COG4172   164 RVMIAMALANEPDLLIADEPTTALDVTVQAQILDLLKDLQRELGMALLLITHDLGVVRRFADRVAVMRQGEIVEQGPTAE 243


                  ....*.
gi 1037402861 221 LYDDPA 226
Cdd:COG4172   244 LFAAPQ 249
cbiO PRK13639
cobalt transporter ATP-binding subunit; Provisional
 15-225 1.29e-26

cobalt transporter ATP-binding subunit; Provisional


Pssm-ID: 184199 [Multi-domain]  Cd Length: 275  Bit Score: 106.70  E-value: 1.29e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037402861  15 GFEIIHGANLEVKDGEFVVFVGPSGCGKSTLLRMIAGLEDITSGELQIGGRVVN----DVEPADRGIAMVFQS-----YA 85
Cdd:PRK13639   14 GTEALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIKGEPIKydkkSLLEVRKTVGIVFQNpddqlFA 93

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037402861  86 lyPhlTVEENLSFGLRMNGNPKADTERRVSHVAEILQITELMKRRPKQLSGGQRQRVAIGRAIVREPEVFLFDEPLSNLD 165
Cdd:PRK13639   94 --P--TVEEDVAFGPLNLGLSKEEVEKRVKEALKAVGMEGFENKPPHHLSGGQKKRVAIAGILAMKPEIIVLDEPTSGLD 169

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037402861 166 AELRVQMRVEISRLHKKlGTTMIYVTHDQTEAMTLADRIVVLRAGNIEQIGAPLDLYDDP 225
Cdd:PRK13639  170 PMGASQIMKLLYDLNKE-GITIIISTHDVDLVPVYADKVYVMSDGKIIKEGTPKEVFSDI 228
cbiO PRK13640
energy-coupling factor transporter ATPase;
23-225 1.32e-26

energy-coupling factor transporter ATPase;


Pssm-ID: 184200 [Multi-domain]  Cd Length: 282  Bit Score: 106.81  E-value: 1.32e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037402861  23 NLEVKDGEFVVFVGPSGCGKSTLLRMIAGL--------EDITSGELQIGGRVVNDVEpaDRgIAMVFQSyalyPH----- 89
Cdd:PRK13640   27 SFSIPRGSWTALIGHNGSGKSTISKLINGLllpddnpnSKITVDGITLTAKTVWDIR--EK-VGIVFQN----PDnqfvg 99

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037402861  90 LTVEENLSFGLRMNGNPKADTERRVSHVAEILQITELMKRRPKQLSGGQRQRVAIGRAIVREPEVFLFDEPLSNLDAELR 169
Cdd:PRK13640  100 ATVGDDVAFGLENRAVPRPEMIKIVRDVLADVGMLDYIDSEPANLSGGQKQRVAIAGILAVEPKIIILDESTSMLDPAGK 179

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1037402861 170 VQMRVEISRLHKKLGTTMIYVTHDQTEAmTLADRIVVLRAGNIEQIGAPLDLYDDP 225
Cdd:PRK13640  180 EQILKLIRKLKKKNNLTVISITHDIDEA-NMADQVLVLDDGKLLAQGSPVEIFSKV 234
PRK13651 PRK13651
cobalt transporter ATP-binding subunit; Provisional
 6-229 1.67e-26

cobalt transporter ATP-binding subunit; Provisional


Pssm-ID: 184210 [Multi-domain]  Cd Length: 305  Bit Score: 107.09  E-value: 1.67e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037402861   6 LSNIVKRFGG-----FEIIHGANLEVKDGEFVVFVGPSGCGKSTLLRMIAGLEDITSGELQI------------------ 62
Cdd:PRK13651    5 VKNIVKIFNKklpteLKALDNVSVEINQGEFIAIIGQTGSGKTTFIEHLNALLLPDTGTIEWifkdeknkkktkekekvl 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037402861  63 --------GGRVVNDVEPADRGIAMVFQ--SYALYPHlTVEENLSFGLRMNGNPKADTERRVSHVAEILQITE-LMKRRP 131
Cdd:PRK13651   85 eklviqktRFKKIKKIKEIRRRVGVVFQfaEYQLFEQ-TIEKDIIFGPVSMGVSKEEAKKRAAKYIELVGLDEsYLQRSP 163

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037402861 132 KQLSGGQRQRVAIGRAIVREPEVFLFDEPLSNLDAELRVQMRVEISRLHKKlGTTMIYVTHDQTEAMTLADRIVVLRAGN 211
Cdd:PRK13651  164 FELSGGQKRRVALAGILAMEPDFLVFDEPTAGLDPQGVKEILEIFDNLNKQ-GKTIILVTHDLDNVLEWTKRTIFFKDGK 242

                         250
                  ....*....|....*...
gi 1037402861 212 IEQIGAPLDLYDDpaNQF 229
Cdd:PRK13651  243 IIKDGDTYDILSD--NKF 258
PRK11831 PRK11831
phospholipid ABC transporter ATP-binding protein MlaF;
14-237 2.17e-26

phospholipid ABC transporter ATP-binding protein MlaF;


Pssm-ID: 236997 [Multi-domain]  Cd Length: 269  Bit Score: 106.00  E-value: 2.17e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037402861  14 GGFEIIHGANLEVKDGEFVVFVGPSGCGKSTLLRMIAGLEDITSGELQIGGRVV-----NDVEPADRGIAMVFQSYALYP 88
Cdd:PRK11831   18 GNRCIFDNISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEILFDGENIpamsrSRLYTVRKRMSMLFQSGALFT 97

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037402861  89 HLTVEENLSFGLRMNGN-PkadterrvshvAEILQITELMKRR-----------PKQLSGGQRQRVAIGRAIVREPEVFL 156
Cdd:PRK11831   98 DMNVFDNVAYPLREHTQlP-----------APLLHSTVMMKLEavglrgaaklmPSELSGGMARRAALARAIALEPDLIM 166

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037402861 157 FDEPLSNLDAelrVQMRV---EISRLHKKLGTTMIYVTHDQTEAMTLADRIVVLRAGNIEQIGAPLDLYDDP---ANQFV 230
Cdd:PRK11831  167 FDEPFVGQDP---ITMGVlvkLISELNSALGVTCVVVSHDVPEVLSIADHAYIVADKKIVAHGSAQALQANPdprVRQFL 243


                  ....*..
gi 1037402861 231 AGFVGSP 237
Cdd:PRK11831  244 DGIADGP 250
ATM1 COG5265
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ...
 17-214 5.03e-26

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: 109.14  E-value: 5.03e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037402861  17 EIIHGANLEVKDGEFVVFVGPSGCGKSTLLRMIAGLEDITSGELQIGGRVVNDVEPAD--RGIAMVFQSYALYpHLTVEE 94
Cdd:COG5265   372 PILKGVSFEVPAGKTVAIVGPSGAGKSTLARLLFRFYDVTSGRILIDGQDIRDVTQASlrAAIGIVPQDTVLF-NDTIAY 450

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037402861  95 NLSFglrmnGNPKAdTERRVSHVAEILQITELMKRRPKQ-----------LSGGQRQRVAIGRAIVREPEVFLFDEPLSN 163
Cdd:COG5265   451 NIAY-----GRPDA-SEEEVEAAARAAQIHDFIESLPDGydtrvgerglkLSGGEKQRVAIARTLLKNPPILIFDEATSA 524

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1037402861 164 LD--------AELRvqmrvEISRlhkklGTTMIYVTH------DqteamtlADRIVVLRAGNI-EQ 214
Cdd:COG5265   525 LDsrteraiqAALR-----EVAR-----GRTTLVIAHrlstivD-------ADEILVLEAGRIvER 573
PRK15439 PRK15439
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
 4-224 5.48e-26

autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional


Pssm-ID: 185336 [Multi-domain]  Cd Length: 510  Bit Score: 108.60  E-value: 5.48e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037402861   4 LSLSNIVKRFGGFEIIHGANLEVKDGEFVVFVGPSGCGKSTLLRMIAGLEDITSGELQIGGRVVNDVEPADR---GIAMV 80
Cdd:PRK15439   12 LCARSISKQYSGVEVLKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIGGNPCARLTPAKAhqlGIYLV 91

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037402861  81 FQSYALYPHLTVEENLSFGLrmngnPK-ADTERRVSHVAEILQITELMKRRPKQLSGGQRQRVAIGRAIVREPEVFLFDE 159
Cdd:PRK15439   92 PQEPLLFPNLSVKENILFGL-----PKrQASMQKMKQLLAALGCQLDLDSSAGSLEVADRQIVEILRGLMRDSRILILDE 166

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1037402861 160 PLSNLDAelrvqmrVEISRLHKKL------GTTMIYVTHDQTEAMTLADRIVVLRAGNIEQIGAPLDLYDD 224
Cdd:PRK15439  167 PTASLTP-------AETERLFSRIrellaqGVGIVFISHKLPEIRQLADRISVMRDGTIALSGKTADLSTD 230
Uup COG0488
ATPase components of ABC transporters with duplicated ATPase domains [General function ...
 6-193 7.88e-26

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


Pssm-ID: 440254 [Multi-domain]  Cd Length: 520  Bit Score: 108.23  E-value: 7.88e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037402861   6 LSNIVKRFGGFEIIHGANLEVKDGEFVVFVGPSGCGKSTLLRMIAGLEDITSGELQIGGRVVndvepadrgIAMVFQSYA 85
Cdd:COG0488     1 LENLSKSFGGRPLLDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEVSIPKGLR---------IGYLPQEPP 71

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037402861  86 LYPHLTVEENLSFGL--------RMN------GNPKADTER------------------RVSHVAEILQITELMKRRP-K 132
Cdd:COG0488    72 LDDDLTVLDTVLDGDaelraleaELEeleaklAEPDEDLERlaelqeefealggweaeaRAEEILSGLGFPEEDLDRPvS 151

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1037402861 133 QLSGGQRQRVAIGRAIVREPEVFLFDEPLSNLDAElrvqmrvEISRLH---KKLGTTMIYVTHD 193
Cdd:COG0488   152 ELSGGWRRRVALARALLSEPDLLLLDEPTNHLDLE-------SIEWLEeflKNYPGTVLVVSHD 208
cbiO PRK13646
energy-coupling factor transporter ATPase;
16-224 7.95e-26

energy-coupling factor transporter ATPase;


Pssm-ID: 184205 [Multi-domain]  Cd Length: 286  Bit Score: 104.86  E-value: 7.95e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037402861  16 FEIIHGANLEVKDGEFVVFVGPSGCGKSTLLRMIAGLEDITSGELQIGGRVVND------VEPADRGIAMVFQsyalYPH 89
Cdd:PRK13646   20 HQAIHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVDDITITHktkdkyIRPVRKRIGMVFQ----FPE 95

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037402861  90 L-----TVEENLSFGLRmngNPKADTERRVSHVAEILQ----ITELMKRRPKQLSGGQRQRVAIGRAIVREPEVFLFDEP 160
Cdd:PRK13646   96 SqlfedTVEREIIFGPK---NFKMNLDEVKNYAHRLLMdlgfSRDVMSQSPFQMSGGQMRKIAIVSILAMNPDIIVLDEP 172

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1037402861 161 LSNLDAELRVQMRVEISRLHKKLGTTMIYVTHDQTEAMTLADRIVVLRAGNIEQIGAPLDLYDD 224
Cdd:PRK13646  173 TAGLDPQSKRQVMRLLKSLQTDENKTIILVSHDMNEVARYADEVIVMKEGSIVSQTSPKELFKD 236
cbiO PRK13647
cobalt transporter ATP-binding subunit; Provisional
 15-224 1.10e-25

cobalt transporter ATP-binding subunit; Provisional


Pssm-ID: 237457 [Multi-domain]  Cd Length: 274  Bit Score: 104.05  E-value: 1.10e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037402861  15 GFEIIHGANLEVKDGEFVVFVGPSGCGKSTLLRMIAGLEDITSGELQIGGRVVN-DVEPADRG-IAMVFQSyalyPH--- 89
Cdd:PRK13647   17 GTKALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGREVNaENEKWVRSkVGLVFQD----PDdqv 92

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037402861  90 --LTVEENLSFGLRMNGNPKADTERRVSHVAEILQITELMKRRPKQLSGGQRQRVAIGRAIVREPEVFLFDEPLSNLDAE 167
Cdd:PRK13647   93 fsSTVWDDVAFGPVNMGLDKDEVERRVEEALKAVRMWDFRDKPPYHLSYGQKKRVAIAGVLAMDPDVIVLDEPMAYLDPR 172

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1037402861 168 LRVQMRVEISRLHKKlGTTMIYVTHDQTEAMTLADRIVVLRAGNIEQIGAPLDLYDD 224
Cdd:PRK13647  173 GQETLMEILDRLHNQ-GKTVIVATHDVDLAAEWADQVIVLKEGRVLAEGDKSLLTDE 228
livF PRK11614
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
1-219 1.12e-25

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


Pssm-ID: 183231 [Multi-domain]  Cd Length: 237  Bit Score: 103.42  E-value: 1.12e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037402861   1 MAELSLSNIVKRFGGFEIIHGANLEVKDGEFVVFVGPSGCGKSTLLRMIAGLEDITSGELQIGGRVVNDVEPAD---RGI 77
Cdd:PRK11614    3 KVMLSFDKVSAHYGKIQALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDGKDITDWQTAKimrEAV 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037402861  78 AMVFQSYALYPHLTVEENLSFGLRMngNPKADTERRVSHVAEIL-QITELMKRRPKQLSGGQRQRVAIGRAIVREPEVFL 156
Cdd:PRK11614   83 AIVPEGRRVFSRMTVEENLAMGGFF--AERDQFQERIKWVYELFpRLHERRIQRAGTMSGGEQQMLAIGRALMSQPRLLL 160

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1037402861 157 FDEPLSNLDAELRVQMRVEISRLHKKlGTTMIYVTHDQTEAMTLADRIVVLRAGNI--EQIGAPL 219
Cdd:PRK11614  161 LDEPSLGLAPIIIQQIFDTIEQLREQ-GMTIFLVEQNANQALKLADRGYVLENGHVvlEDTGDAL 224
PhnL COG4778
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ...
 4-210 1.79e-25

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: 102.51  E-value: 1.79e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037402861   4 LSLSNIVKRF-----GGFEI--IHGANLEVKDGEFVVFVGPSGCGKSTLLRMIAGLEDITSGELQI--GGRVVNDVEPAD 74
Cdd:COG4778     5 LEVENLSKTFtlhlqGGKRLpvLDGVSFSVAAGECVALTGPSGAGKSTLLKCIYGNYLPDSGSILVrhDGGWVDLAQASP 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037402861  75 RGIAMVFQSYALY--------PHLTVEENLSFGLRMNGNPKADTERRVSHVAEILQITE-LMKRRPKQLSGGQRQRVAIG 145
Cdd:COG4778    85 REILALRRRTIGYvsqflrviPRVSALDVVAEPLLERGVDREEARARARELLARLNLPErLWDLPPATFSGGEQQRVNIA 164

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1037402861 146 RAIVREPEVFLFDEPLSNLDAELRvqmRVEISRLHKKL--GTTMIYVTHDqTEAM-TLADRIVVLRAG 210
Cdd:COG4778   165 RGFIADPPLLLLDEPTASLDAANR---AVVVELIEEAKarGTAIIGIFHD-EEVReAVADRVVDVTPF 228
PRK13537 PRK13537
nodulation factor ABC transporter ATP-binding protein NodI;
2-223 1.81e-25

nodulation factor ABC transporter ATP-binding protein NodI;


Pssm-ID: 237420 [Multi-domain]  Cd Length: 306  Bit Score: 104.12  E-value: 1.81e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037402861   2 AELSLSNIVKRFGGFEIIHGANLEVKDGEFVVFVGPSGCGKSTLLRMIAGLEDITSGELQIGGRVVNDVEP-ADRGIAMV 80
Cdd:PRK13537    6 APIDFRNVEKRYGDKLVVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCGEPVPSRARhARQRVGVV 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037402861  81 FQSYALYPHLTVEENLSFGLRMNGNPKADTERRVSHVAEILQITELMKRRPKQLSGGQRQRVAIGRAIVREPEVFLFDEP 160
Cdd:PRK13537   86 PQFDNLDPDFTVRENLLVFGRYFGLSAAAARALVPPLLEFAKLENKADAKVGELSGGMKRRLTLARALVNDPDVLVLDEP 165

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1037402861 161 LSNLDAELRVQMRVEISRLHKKlGTTMIYVTHDQTEAMTLADRIVVLRAGNIEQIGAPLDLYD 223
Cdd:PRK13537  166 TTGLDPQARHLMWERLRSLLAR-GKTILLTTHFMEEAERLCDRLCVIEEGRKIAEGAPHALIE 227
cbiO PRK13641
energy-coupling factor transporter ATPase;
23-225 1.97e-25

energy-coupling factor transporter ATPase;


Pssm-ID: 237456 [Multi-domain]  Cd Length: 287  Bit Score: 103.76  E-value: 1.97e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037402861  23 NLEVKDGEFVVFVGPSGCGKSTLLRMIAGLEDITSGELQIGGRVVN------DVEPADRGIAMVFQsyalYPHL-----T 91
Cdd:PRK13641   27 SFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITIAGYHITpetgnkNLKKLRKKVSLVFQ----FPEAqlfenT 102

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037402861  92 VEENLSFGLRMNGnpKADTERRVSHVAEILQI---TELMKRRPKQLSGGQRQRVAIGRAIVREPEVFLFDEPLSNLDAEL 168
Cdd:PRK13641  103 VLKDVEFGPKNFG--FSEDEAKEKALKWLKKVglsEDLISKSPFELSGGQMRRVAIAGVMAYEPEILCLDEPAAGLDPEG 180

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1037402861 169 RVQMrVEISRLHKKLGTTMIYVTHDQTEAMTLADRIVVLRAGNIEQIGAPLDLYDDP 225
Cdd:PRK13641  181 RKEM-MQLFKDYQKAGHTVILVTHNMDDVAEYADDVLVLEHGKLIKHASPKEIFSDK 236
cbiO PRK13631
cobalt transporter ATP-binding subunit; Provisional
 35-226 2.50e-25

cobalt transporter ATP-binding subunit; Provisional


Pssm-ID: 237451 [Multi-domain]  Cd Length: 320  Bit Score: 104.16  E-value: 2.50e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037402861  35 VGPSGCGKSTLLRMIAGL----------EDITSGELQIGGRVVNDVEPAD--------RGIAMVFQ--SYALYPHlTVEE 94
Cdd:PRK13631   58 IGNSGSGKSTLVTHFNGLikskygtiqvGDIYIGDKKNNHELITNPYSKKiknfkelrRRVSMVFQfpEYQLFKD-TIEK 136

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037402861  95 NLSFGLRMNGNPKADTERRVSHVAEILQITE-LMKRRPKQLSGGQRQRVAIGRAIVREPEVFLFDEPLSNLDAELRVQMr 173
Cdd:PRK13631  137 DIMFGPVALGVKKSEAKKLAKFYLNKMGLDDsYLERSPFGLSGGQKRRVAIAGILAIQPEILIFDEPTAGLDPKGEHEM- 215

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1037402861 174 VEISRLHKKLGTTMIYVTHDQTEAMTLADRIVVLRAGNIEQIGAPLDLYDDPA 226
Cdd:PRK13631  216 MQLILDAKANNKTVFVITHTMEHVLEVADEVIVMDKGKILKTGTPYEIFTDQH 268
PRK14258 PRK14258
phosphate ABC transporter ATP-binding protein; Provisional
 17-234 3.01e-25

phosphate ABC transporter ATP-binding protein; Provisional


Pssm-ID: 184593 [Multi-domain]  Cd Length: 261  Bit Score: 102.81  E-value: 3.01e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037402861  17 EIIHGANLEVKDGEFVVFVGPSGCGKSTLLRMIAGLEDItSGELQIGGRV-----------VNdVEPADRGIAMVFQSYA 85
Cdd:PRK14258   21 KILEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLNRMNEL-ESEVRVEGRVeffnqniyerrVN-LNRLRRQVSMVHPKPN 98

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037402861  86 LYPhLTVEENLSFGLRMNG-NPKADTERRVSHV---AEIL-QITELMKRRPKQLSGGQRQRVAIGRAIVREPEVFLFDEP 160
Cdd:PRK14258   99 LFP-MSVYDNVAYGVKIVGwRPKLEIDDIVESAlkdADLWdEIKHKIHKSALDLSGGQQQRLCIARALAVKPKVLLMDEP 177

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037402861 161 LSNLD--AELRVQMRVEISRLHKKLgtTMIYVTHDQTEAMTLADRIVVL-----RAGNIEQIGAPLDLYDDPANQFVAGF 233
Cdd:PRK14258  178 CFGLDpiASMKVESLIQSLRLRSEL--TMVIVSHNLHQVSRLSDFTAFFkgnenRIGQLVEFGLTKKIFNSPHDSRTREY 255


                  .
gi 1037402861 234 V 234
Cdd:PRK14258  256 V 256
PRK14246 PRK14246
phosphate ABC transporter ATP-binding protein; Provisional
 18-234 3.44e-25

phosphate ABC transporter ATP-binding protein; Provisional


Pssm-ID: 172734 [Multi-domain]  Cd Length: 257  Bit Score: 102.43  E-value: 3.44e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037402861  18 IIHGANLEVKDGEFVVFVGPSGCGKSTLLRMIAGLEDITSGELQIGGRVV---NDVEPAD-----RGIAMVFQSYALYPH 89
Cdd:PRK14246   25 ILKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLIEIYDSKIKVDGKVLyfgKDIFQIDaiklrKEVGMVFQQPNPFPH 104

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037402861  90 LTVEENLSFGLRMNG-----NPKADTERRVSHVAEILQITELMKRRPKQLSGGQRQRVAIGRAIVREPEVFLFDEPLSNL 164
Cdd:PRK14246  105 LSIYDNIAYPLKSHGikekrEIKKIVEECLRKVGLWKEVYDRLNSPASQLSGGQQQRLTIARALALKPKVLLMDEPTSMI 184

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037402861 165 DAELRVQMRVEISRLHKKLgtTMIYVTHDQTEAMTLADRIVVLRAGNIEQIGAPLDLYDDPANQFVAGFV 234
Cdd:PRK14246  185 DIVNSQAIEKLITELKNEI--AIVIVSHNPQQVARVADYVAFLYNGELVEWGSSNEIFTSPKNELTEKYV 252
cbiO PRK13652
cobalt transporter ATP-binding subunit; Provisional
 14-225 4.47e-25

cobalt transporter ATP-binding subunit; Provisional


Pssm-ID: 172200 [Multi-domain]  Cd Length: 277  Bit Score: 102.57  E-value: 4.47e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037402861  14 GGFEIIHGANLEVKDGEFVVFVGPSGCGKSTLLRMIAGLEDITSGELQIGGRVVN--DVEPADRGIAMVFQS---YALYP 88
Cdd:PRK13652   15 GSKEALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIRGEPITkeNIREVRKFVGLVFQNpddQIFSP 94

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037402861  89 hlTVEENLSFGLRMNGNPKADTERRVSHVAEILQITELMKRRPKQLSGGQRQRVAIGRAIVREPEVFLFDEPLSNLDAEL 168
Cdd:PRK13652   95 --TVEQDIAFGPINLGLDEETVAHRVSSALHMLGLEELRDRVPHHLSGGEKKRVAIAGVIAMEPQVLVLDEPTAGLDPQG 172

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1037402861 169 RVQMRVEISRLHKKLGTTMIYVTHDQTEAMTLADRIVVLRAGNIEQIGAPLDLYDDP 225
Cdd:PRK13652  173 VKELIDFLNDLPETYGMTVIFSTHQLDLVPEMADYIYVMDKGRIVAYGTVEEIFLQP 229
PRK13536 PRK13536
nodulation factor ABC transporter ATP-binding protein NodI;
4-224 8.27e-25

nodulation factor ABC transporter ATP-binding protein NodI;


Pssm-ID: 237419 [Multi-domain]  Cd Length: 340  Bit Score: 102.99  E-value: 8.27e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037402861   4 LSLSNIVKRFGGFEIIHGANLEVKDGEFVVFVGPSGCGKSTLLRMIAGLEDITSGELQI-GGRVVNDVEPADRGIAMVFQ 82
Cdd:PRK13536   42 IDLAGVSKSYGDKAVVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKITVlGVPVPARARLARARIGVVPQ 121

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037402861  83 SYALYPHLTVEENLSFGLRMNGNPKADTERRVSHVAEILQITELMKRRPKQLSGGQRQRVAIGRAIVREPEVFLFDEPLS 162
Cdd:PRK13536  122 FDNLDLEFTVRENLLVFGRYFGMSTREIEAVIPSLLEFARLESKADARVSDLSGGMKRRLTLARALINDPQLLILDEPTT 201

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1037402861 163 NLDAELRvQMRVEISRLHKKLGTTMIYVTHDQTEAMTLADRIVVLRAGNIEQIGAPLDLYDD 224
Cdd:PRK13536  202 GLDPHAR-HLIWERLRSLLARGKTILLTTHFMEEAERLCDRLCVLEAGRKIAEGRPHALIDE 262
Rli1 COG1245
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ...
 4-206 1.66e-24

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: 104.48  E-value: 1.66e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037402861   4 LSLSNIVKRFGGF--EIIHGanlEVKDGEFVVFVGPSGCGKSTLLRMIAGLEDITSGELQIGGRVvndvepadrgiamvf 81
Cdd:COG1245   342 VEYPDLTKSYGGFslEVEGG---EIREGEVLGIVGPNGIGKTTFAKILAGVLKPDEGEVDEDLKI--------------- 403

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037402861  82 qSY------ALYPhLTVEENLsfglRMNGNPKADTERRVSHVAEILQITELMKRRPKQLSGGQRQRVAIGRAIVREPEVF 155
Cdd:COG1245   404 -SYkpqyisPDYD-GTVEEFL----RSANTDDFGSSYYKTEIIKPLGLEKLLDKNVKDLSGGELQRVAIAACLSRDADLY 477

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1037402861 156 LFDEPLSNLDAELRVQMRVEISRLHKKLGTTMIYVTHDQTEAMTLADRIVV 206
Cdd:COG1245   478 LLDEPSAHLDVEQRLAVAKAIRRFAENRGKTAMVVDHDIYLIDYISDRLMV 528
MsbA_lipidA TIGR02203
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ...
 4-223 2.13e-24

lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide chain transporter in the ATP-binding cassette (ABC) transporter family, MsbA, which exports lipid A. It may also act in multidrug resistance. Lipid A, a part of lipopolysaccharide, is found in the outer leaflet of the outer membrane of most Gram-negative bacteria. Members of this family are restricted to the Proteobacteria (although lipid A is more broadly distributed) and often are clustered with lipid A biosynthesis genes. [Cell envelope, Biosynthesis and degradation of surface polysaccharides and lipopolysaccharides, Transport and binding proteins, Other]


Pssm-ID: 131258 [Multi-domain]  Cd Length: 571  Bit Score: 104.41  E-value: 2.13e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037402861   4 LSLSNIVKRFGGFEI--IHGANLEVKDGEFVVFVGPSGCGKSTLLRMIAGLEDITSGELQIGGRVVNDVEPAD--RGIAM 79
Cdd:TIGR02203 331 VEFRNVTFRYPGRDRpaLDSISLVIEPGETVALVGRSGSGKSTLVNLIPRFYEPDSGQILLDGHDLADYTLASlrRQVAL 410

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037402861  80 VFQSYALYPHlTVEENLSFGlRMNGNPKADTERrvshVAEILQITELMKRRPK-----------QLSGGQRQRVAIGRAI 148
Cdd:TIGR02203 411 VSQDVVLFND-TIANNIAYG-RTEQADRAEIER----ALAAAYAQDFVDKLPLgldtpigengvLLSGGQRQRLAIARAL 484

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1037402861 149 VREPEVFLFDEPLSNLDAELRVQMRVEISRLHKklGTTMIYVTHDQTeAMTLADRIVVLRAGNIEQIGAPLDLYD 223
Cdd:TIGR02203 485 LKDAPILILDEATSALDNESERLVQAALERLMQ--GRTTLVIAHRLS-TIEKADRIVVMDDGRIVERGTHNELLA 556
ABCC_Hemolysin cd03252
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ...
 17-216 2.33e-24

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: 99.48  E-value: 2.33e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037402861  17 EIIHGANLEVKDGEFVVFVGPSGCGKSTLLRMIAGLEDITSGELQIGGRVVNDVEPA--DRGIAMVFQSYALYpHLTVEE 94
Cdd:cd03252    16 VILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGHDLALADPAwlRRQVGVVLQENVLF-NRSIRD 94

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037402861  95 NLSFGlrmngNPKADTERrVSHVAE-------ILQITE----LMKRRPKQLSGGQRQRVAIGRAIVREPEVFLFDEPLSN 163
Cdd:cd03252    95 NIALA-----DPGMSMER-VIEAAKlagahdfISELPEgydtIVGEQGAGLSGGQRQRIAIARALIHNPRILIFDEATSA 168

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1037402861 164 LDAElrvQMRVEISRLHKKL-GTTMIYVTHDQTEAMTlADRIVVLRAGNIEQIG 216
Cdd:cd03252   169 LDYE---SEHAIMRNMHDICaGRTVIIIAHRLSTVKN-ADRIIVMEKGRIVEQG 218
met_CoM_red_A2 TIGR03269
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ...
 4-221 7.80e-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: 102.19  E-value: 7.80e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037402861   4 LSLSNIVKRFGGFEIIHGANLEVKDGEFVVFVGPSGCGKSTLLRMIAGLEDI--TSGEL--------------------- 60
Cdd:TIGR03269   1 IEVKNLTKKFDGKEVLKNISFTIEEGEVLGILGRSGAGKSVLMHVLRGMDQYepTSGRIiyhvalcekcgyverpskvge 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037402861  61 ---QIGGR----VVNDVEPAD-------RGIAMVFQ-SYALYPHLTVEENLSFGLRMNGNPKADTERRVSHVAEILQITE 125
Cdd:TIGR03269  81 pcpVCGGTlepeEVDFWNLSDklrrrirKRIAIMLQrTFALYGDDTVLDNVLEALEEIGYEGKEAVGRAVDLIEMVQLSH 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037402861 126 LMKRRPKQLSGGQRQRVAIGRAIVREPEVFLFDEPLSNLDAELRVQMRVEISRLHKKLGTTMIYVTHdQTEAMT-LADRI 204
Cdd:TIGR03269 161 RITHIARDLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALEEAVKASGISMVLTSH-WPEVIEdLSDKA 239

                         250
                  ....*....|....*..
gi 1037402861 205 VVLRAGNIEQIGAPLDL 221
Cdd:TIGR03269 240 IWLENGEIKEEGTPDEV 256
xylG TIGR02633
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ...
 4-210 9.12e-24

D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose isomerase and xylulokinase enzymes for xylose utilization. Members of this protein family are the ATP-binding cassette (ABC) subunit of the known or predicted high-affinity xylose ABC transporter for xylose import. These genes, which closely resemble other sugar transport ABC transporter genes, typically are encoded near xylose utilization enzymes and regulatory proteins. Note that this form of the transporter contains two copies of the ABC transporter domain (pfam00005). [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]


Pssm-ID: 131681 [Multi-domain]  Cd Length: 500  Bit Score: 102.21  E-value: 9.12e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037402861   4 LSLSNIVKRFGGFEIIHGANLEVKDGEFVVFVGPSGCGKSTLLRMIAGLE-------DITSGELQIGGRVVNDVEPAdrG 76
Cdd:TIGR02633   2 LEMKGIVKTFGGVKALDGIDLEVRPGECVGLCGENGAGKSTLMKILSGVYphgtwdgEIYWSGSPLKASNIRDTERA--G 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037402861  77 IAMVFQSYALYPHLTVEENLSFG--LRMNGNPKADTE--RRVSHVAEILQITELMKRRP-KQLSGGQRQRVAIGRAIVRE 151
Cdd:TIGR02633  80 IVIIHQELTLVPELSVAENIFLGneITLPGGRMAYNAmyLRAKNLLRELQLDADNVTRPvGDYGGGQQQLVEIAKALNKQ 159

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1037402861 152 PEVFLFDEPLSNLdAELRVQMRVEISRLHKKLGTTMIYVTHDQTEAMTLADRIVVLRAG 210
Cdd:TIGR02633 160 ARLLILDEPSSSL-TEKETEILLDIIRDLKAHGVACVYISHKLNEVKAVCDTICVIRDG 217
ABC_RNaseL_inhibitor_domain2 cd03237
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ...
 7-206 9.73e-24

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: 98.25  E-value: 9.73e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037402861   7 SNIVKRFGGF--EIIHGanlEVKDGEFVVFVGPSGCGKSTLLRMIAGLEDITSGELQIggrVVNDVEPADRGIAMVFQSy 84
Cdd:cd03237     4 PTMKKTLGEFtlEVEGG---SISESEVIGILGPNGIGKTTFIKMLAGVLKPDEGDIEI---ELDTVSYKPQYIKADYEG- 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037402861  85 alyphlTVEENLSFGLRMNGN-PKADTErrvshVAEILQITELMKRRPKQLSGGQRQRVAIGRAIVREPEVFLFDEPLSN 163
Cdd:cd03237    77 ------TVRDLLSSITKDFYThPYFKTE-----IAKPLQIEQILDREVPELSGGELQRVAIAACLSKDADIYLLDEPSAY 145

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 1037402861 164 LDAELRVQMRVEISRLHKKLGTTMIYVTHDQTEAMTLADRIVV 206
Cdd:cd03237   146 LDVEQRLMASKVIRRFAENNEKTAFVVEHDIIMIDYLADRLIV 188
ABCG_PDR_domain1 cd03233
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ...
 1-212 9.78e-24

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: 96.95  E-value: 9.78e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037402861   1 MAELSLSNIV----KRFGGFEIIHGANLEVKDGEFVVFVGPSGCGKSTLLRMIAGledITSGELQIGGRVVNDVEPADrG 76
Cdd:cd03233     1 ASTLSWRNISfttgKGRSKIPILKDFSGVVKPGEMVLVLGRPGSGCSTLLKALAN---RTEGNVSVEGDIHYNGIPYK-E 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037402861  77 IAMVFQSYALY--------PHLTVEENLSFGLRMNGNpkadterrvshvaEILqitelmkrrpKQLSGGQRQRVAIGRAI 148
Cdd:cd03233    77 FAEKYPGEIIYvseedvhfPTLTVRETLDFALRCKGN-------------EFV----------RGISGGERKRVSIAEAL 133

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1037402861 149 VREPEVFLFDEPLSNLDAELRVQMRVEISRLHKKLG-TTMIYVTHDQTEAMTLADRIVVLRAGNI 212
Cdd:cd03233   134 VSRASVLCWDNSTRGLDSSTALEILKCIRTMADVLKtTTFVSLYQASDEIYDLFDKVLVLYEGRQ 198
PRK11174 PRK11174
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
 23-216 1.06e-23

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


Pssm-ID: 236870 [Multi-domain]  Cd Length: 588  Bit Score: 102.23  E-value: 1.06e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037402861  23 NLEVKDGEFVVFVGPSGCGKSTLLRMIAGLEDITsGELQIGGRVVNDVEPAD--RGIAMVFQSYALyPHLTVEENLSFGl 100
Cdd:PRK11174  370 NFTLPAGQRIALVGPSGAGKTSLLNALLGFLPYQ-GSLKINGIELRELDPESwrKHLSWVGQNPQL-PHGTLRDNVLLG- 446

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037402861 101 rmngNPKAdTERRVSHVAEILQITELMKRRPK-----------QLSGGQRQRVAIGRAIVREPEVFLFDEPLSNLDA--E 167
Cdd:PRK11174  447 ----NPDA-SDEQLQQALENAWVSEFLPLLPQgldtpigdqaaGLSVGQAQRLALARALLQPCQLLLLDEPTASLDAhsE 521

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1037402861 168 LRVQMRVEisrlHKKLGTTMIYVTH--DQTEAMtlaDRIVVLRAGNIEQIG 216
Cdd:PRK11174  522 QLVMQALN----AASRRQTTLMVTHqlEDLAQW---DQIWVMQDGQIVQQG 565
type_I_sec_HlyB TIGR01846
type I secretion system ABC transporter, HlyB family; Type I protein secretion is a system in ...
 4-216 1.22e-23

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: 102.13  E-value: 1.22e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037402861   4 LSLSNIVKRFG--GFEIIHGANLEVKDGEFVVFVGPSGCGKSTLLRMIAGLEDITSGELQIGGRVVNDVEPA--DRGIAM 79
Cdd:TIGR01846 456 ITFENIRFRYApdSPEVLSNLNLDIKPGEFIGIVGPSGSGKSTLTKLLQRLYTPQHGQVLVDGVDLAIADPAwlRRQMGV 535

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037402861  80 VFQSYALYPHlTVEENLSFGlrmngNPKADTERrVSHVAEILQITELMKRRPK-----------QLSGGQRQRVAIGRAI 148
Cdd:TIGR01846 536 VLQENVLFSR-SIRDNIALC-----NPGAPFEH-VIHAAKLAGAHDFISELPQgyntevgekgaNLSGGQRQRIAIARAL 608

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1037402861 149 VREPEVFLFDEPLSNLDAE----LRVQMRvEISRlhkklGTTMIYVTHdQTEAMTLADRIVVLRAGNIEQIG 216
Cdd:TIGR01846 609 VGNPRILIFDEATSALDYEsealIMRNMR-EICR-----GRTVIIIAH-RLSTVRACDRIIVLEKGQIAESG 673
ccmA TIGR01189
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ...
 4-192 1.42e-23

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


Pssm-ID: 273491 [Multi-domain]  Cd Length: 198  Bit Score: 96.27  E-value: 1.42e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037402861   4 LSLSNIVKRFGGFEIIHGANLEVKDGEFVVFVGPSGCGKSTLLRMIAGLEDITSGELQIGGRVVNDVEPA-DRGIAMVFQ 82
Cdd:TIGR01189   1 LAARNLACSRGERMLFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRWNGTPLAEQRDEpHENILYLGH 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037402861  83 SYALYPHLTVEENLSFGLRMNGnpkaDTERRVSHVAEILQITELMKRRPKQLSGGQRQRVAIGRAIVREPEVFLFDEPLS 162
Cdd:TIGR01189  81 LPGLKPELSALENLHFWAAIHG----GAQRTIEDALAAVGLTGFEDLPAAQLSAGQQRRLALARLWLSRRPLWILDEPTT 156

                         170       180       190
                  ....*....|....*....|....*....|
gi 1037402861 163 NLDAElRVQMRVEISRLHKKLGTTMIYVTH 192
Cdd:TIGR01189 157 ALDKA-GVALLAGLLRAHLARGGIVLLTTH 185
cbiO PRK13636
cobalt transporter ATP-binding subunit; Provisional
 15-224 2.37e-23

cobalt transporter ATP-binding subunit; Provisional


Pssm-ID: 184196 [Multi-domain]  Cd Length: 283  Bit Score: 98.00  E-value: 2.37e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037402861  15 GFEIIHGANLEVKDGEFVVFVGPSGCGKSTLLRMIAGLEDITSGELQIGGRVVN----DVEPADRGIAMVFQS--YALYP 88
Cdd:PRK13636   18 GTHALKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGKPIDysrkGLMKLRESVGMVFQDpdNQLFS 97

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037402861  89 hLTVEENLSFGLRMNGNPKADTERRVSHVAEILQITELMKRRPKQLSGGQRQRVAIGRAIVREPEVFLFDEPLSNLDAEL 168
Cdd:PRK13636   98 -ASVYQDVSFGAVNLKLPEDEVRKRVDNALKRTGIEHLKDKPTHCLSFGQKKRVAIAGVLVMEPKVLVLDEPTAGLDPMG 176

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1037402861 169 RVQMRVEISRLHKKLGTTMIYVTHDQTEAMTLADRIVVLRAGNIEQIGAPLDLYDD 224
Cdd:PRK13636  177 VSEIMKLLVEMQKELGLTIIIATHDIDIVPLYCDNVFVMKEGRVILQGNPKEVFAE 232
ABCF_EF-3 cd03221
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ...
 4-210 2.71e-23

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: 94.05  E-value: 2.71e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037402861   4 LSLSNIVKRFGGFEIIHGANLEVKDGEFVVFVGPSGCGKSTLLRMIAGLEDITSGELQIGGRVvndvepadrgiamvfqs 83
Cdd:cd03221     1 IELENLSKTYGGKLLLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIVTWGSTV----------------- 63

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037402861  84 yalyphltveenlsfglrmngnpkadterRVSHVAeilqitelmkrrpkQLSGGQRQRVAIGRAIVREPEVFLFDEPLSN 163
Cdd:cd03221    64 -----------------------------KIGYFE--------------QLSGGEKMRLALAKLLLENPNLLLLDEPTNH 100

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 1037402861 164 LDAELRVQMRVEISRLHKklgtTMIYVTHDQTEAMTLADRIVVLRAG 210
Cdd:cd03221   101 LDLESIEALEEALKEYPG----TVILVSHDRYFLDQVATKIIELEDG 143
livG PRK11300
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
 4-225 2.83e-23

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


Pssm-ID: 183080 [Multi-domain]  Cd Length: 255  Bit Score: 96.98  E-value: 2.83e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037402861   4 LSLSNIVKRFGGFEIIHGANLEVKDGEFVVFVGPSGCGKSTLLRMIAGLEDITSGELQIGGRVVN---DVEPADRGIAMV 80
Cdd:PRK11300    6 LSVSGLMMRFGGLLAVNNVNLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTILLRGQHIEglpGHQIARMGVVRT 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037402861  81 FQSYALYPHLTVEENLSFG--LRMNGN--------P---KADTE--RRVSHVAEILQITELMKRRPKQLSGGQRQRVAIG 145
Cdd:PRK11300   86 FQHVRLFREMTVIENLLVAqhQQLKTGlfsgllktPafrRAESEalDRAATWLERVGLLEHANRQAGNLAYGQQRRLEIA 165

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037402861 146 RAIVREPEVFLFDEPLSNLDAELRVQMRVEISRLHKKLGTTMIYVTHDQTEAMTLADRIVVLRAGNIEQIGAPLDLYDDP 225
Cdd:PRK11300  166 RCMVTQPEILMLDEPAAGLNPKETKELDELIAELRNEHNVTVLLIEHDMKLVMGISDRIYVVNQGTPLANGTPEEIRNNP 245
NHLM_micro_ABC2 TIGR03797
NHLM bacteriocin system ABC transporter, ATP-binding protein; Members of this protein family ...
 18-221 3.62e-23

NHLM bacteriocin system ABC transporter, ATP-binding protein; Members of this protein family are ABC transporter ATP-binding subunits, part of a three-gene putative bacteriocin transport operon. The other subunits include another ATP-binding subunit (TIGR03796), which has an N-terminal leader sequence cleavage domain, and an HlyD homolog (TIGR03794). In a number of genomes, members of protein families related to nitrile hydratase alpha subunit or to nif11 have undergone paralogous family expansions, with members possessing a putative bacteriocin cleavage region ending with a classic Gly-Gly motif. Those sets of putative bacteriocins, members of this protein family and its partners TIGR03794 and TIGR03796, and cyclodehydratase/docking scaffold fusion proteins of thiazole/oxazole biosynthesis frequently show correlated species distribution and co-clustering within many of those genomes. [Transport and binding proteins, Amino acids, peptides and amines, Cellular processes, Biosynthesis of natural products]


Pssm-ID: 274789 [Multi-domain]  Cd Length: 686  Bit Score: 100.80  E-value: 3.62e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037402861  18 IIHGANLEVKDGEFVVFVGPSGCGKSTLLRMIAGLEDITSGELQIGGRVVN--DVEPADRGIAMVFQSYALYPHlTVEEN 95
Cdd:TIGR03797 468 ILDDVSLQIEPGEFVAIVGPSGSGKSTLLRLLLGFETPESGSVFYDGQDLAglDVQAVRRQLGVVLQNGRLMSG-SIFEN 546

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037402861  96 LSFGLRMngnpkadTERRVSHVAEILQITELMKRRPKQ-----------LSGGQRQRVAIGRAIVREPEVFLFDEPLSNL 164
Cdd:TIGR03797 547 IAGGAPL-------TLDEAWEAARMAGLAEDIRAMPMGmhtvisegggtLSGGQRQRLLIARALVRKPRILLFDEATSAL 619

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1037402861 165 DAelRVQMRVEISRlhKKLGTTMIYVTHDQTEAMTlADRIVVLRAGNIEQIGAPLDL 221
Cdd:TIGR03797 620 DN--RTQAIVSESL--ERLKVTRIVIAHRLSTIRN-ADRIYVLDAGRVVQQGTYDEL 671
ABC_Carb_Monos_II cd03215
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ...
 19-212 3.63e-23

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


Pssm-ID: 213182 [Multi-domain]  Cd Length: 182  Bit Score: 94.81  E-value: 3.63e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037402861  19 IHGANLEVKDGEFVVFVGPSGCGKSTLLRMIAGLEDITSGELQIGGRVVNDVEPADR---GIAMV---FQSYALYPHLTV 92
Cdd:cd03215    16 VRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITLDGKPVTRRSPRDAiraGIAYVpedRKREGLVLDLSV 95

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037402861  93 EENLSFGLrmngnpkadterrvshvaeilqitelmkrrpkQLSGGQRQRVAIGRAIVREPEVFLFDEPLSNLDAELRVQM 172
Cdd:cd03215    96 AENIALSS--------------------------------LLSGGNQQKVVLARWLARDPRVLILDEPTRGVDVGAKAEI 143

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 1037402861 173 RVEISRLHKKlGTTMIYVTHDQTEAMTLADRIVVLRAGNI 212
Cdd:cd03215   144 YRLIRELADA-GKAVLLISSELDELLGLCDRILVMYEGRI 182
3a01208 TIGR00958
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
 18-225 4.06e-23

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


Pssm-ID: 273363 [Multi-domain]  Cd Length: 711  Bit Score: 100.57  E-value: 4.06e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037402861  18 IIHGANLEVKDGEFVVFVGPSGCGKSTLLRMIAGLEDITSGELQIGGRVVNDVEPA--DRGIAMVFQSYALYPHlTVEEN 95
Cdd:TIGR00958 496 VLKGLTFTLHPGEVVALVGPSGSGKSTVAALLQNLYQPTGGQVLLDGVPLVQYDHHylHRQVALVGQEPVLFSG-SVREN 574

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037402861  96 LSFGLRMNGNPKADTERRVSHVAEIlqITELMK-------RRPKQLSGGQRQRVAIGRAIVREPEVFLFDEPLSNLDAEl 168
Cdd:TIGR00958 575 IAYGLTDTPDEEIMAAAKAANAHDF--IMEFPNgydtevgEKGSQLSGGQKQRIAIARALVRKPRVLILDEATSALDAE- 651

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1037402861 169 rVQMRVEISRlhKKLGTTMIYVTHdQTEAMTLADRIVVLRAGNIEQIGAPLDLYDDP 225
Cdd:TIGR00958 652 -CEQLLQESR--SRASRTVLLIAH-RLSTVERADQILVLKKGSVVEMGTHKQLMEDQ 704
MglA COG1129
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
10-212 6.67e-23

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


Pssm-ID: 440745 [Multi-domain]  Cd Length: 497  Bit Score: 99.32  E-value: 6.67e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037402861  10 VKRFGGFEIIHGANLEVKDGEFVVFVGPSGCGKSTLLRMIAGLEDITSGELQIGGRVVNDVEPAD---RGIAMV---FQS 83
Cdd:COG1129   259 VEGLSVGGVVRDVSFSVRAGEILGIAGLVGAGRTELARALFGADPADSGEIRLDGKPVRIRSPRDairAGIAYVpedRKG 338

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037402861  84 YALYPHLTVEENLSFG----LRMNG--NPKAdtERRVS-HVAEILQI-TELMKRRPKQLSGGQRQRVAIGRAIVREPEVF 155
Cdd:COG1129   339 EGLVLDLSIRENITLAsldrLSRGGllDRRR--ERALAeEYIKRLRIkTPSPEQPVGNLSGGNQQKVVLAKWLATDPKVL 416

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037402861 156 LFDEPLSNLDaelrVQMRVEISRLHKKL---GTTMIYVTHDQTEAMTLADRIVVLRAGNI 212
Cdd:COG1129   417 ILDEPTRGID----VGAKAEIYRLIRELaaeGKAVIVISSELPELLGLSDRILVMREGRI 472
PRK10261 PRK10261
glutathione transporter ATP-binding protein; Provisional
 29-253 7.37e-23

glutathione transporter ATP-binding protein; Provisional


Pssm-ID: 182342 [Multi-domain]  Cd Length: 623  Bit Score: 99.93  E-value: 7.37e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037402861  29 GEFVVFVGPSGCGKSTLLRMIAGLEDITSGELQIGGRVVN-----DVEPADRGIAMVFQS-YA-LYPHLTVEENLSFGLR 101
Cdd:PRK10261  350 GETLSLVGESGSGKSTTGRALLRLVESQGGEIIFNGQRIDtlspgKLQALRRDIQFIFQDpYAsLDPRQTVGDSIMEPLR 429

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037402861 102 MNGNPKADTERRvsHVAEILQITELMK----RRPKQLSGGQRQRVAIGRAIVREPEVFLFDEPLSNLDAELRVQMRVEIS 177
Cdd:PRK10261  430 VHGLLPGKAAAA--RVAWLLERVGLLPehawRYPHEFSGGQRQRICIARALALNPKVIIADEAVSALDVSIRGQIINLLL 507

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1037402861 178 RLHKKLGTTMIYVTHDQTEAMTLADRIVVLRAGNIEQIGAPLDLYDDPANqfvagfvgsPKMNFLKAVVVEAQPGR 253
Cdd:PRK10261  508 DLQRDFGIAYLFISHDMAVVERISHRVAVMYLGQIVEIGPRRAVFENPQH---------PYTRKLMAAVPVADPSR 574
PRK13409 PRK13409
ribosome biogenesis/translation initiation ATPase RLI;
4-206 7.50e-23

ribosome biogenesis/translation initiation ATPase RLI;


Pssm-ID: 184037 [Multi-domain]  Cd Length: 590  Bit Score: 99.88  E-value: 7.50e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037402861   4 LSLSNIVKRFGGF--EIIHGanlEVKDGEFVVFVGPSGCGKSTLLRMIAGLEDITSGELQIGGRVvndvepadrgiamvf 81
Cdd:PRK13409  341 VEYPDLTKKLGDFslEVEGG---EIYEGEVIGIVGPNGIGKTTFAKLLAGVLKPDEGEVDPELKI--------------- 402

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037402861  82 qSY------ALYPhLTVEENLSfglrmNGNPKADTERRVSHVAEILQITELMKRRPKQLSGGQRQRVAIGRAIVREPEVF 155
Cdd:PRK13409  403 -SYkpqyikPDYD-GTVEDLLR-----SITDDLGSSYYKSEIIKPLQLERLLDKNVKDLSGGELQRVAIAACLSRDADLY 475

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1037402861 156 LFDEPLSNLDAELRVQMRVEISRLHKKLGTTMIYVTHDQTEAMTLADRIVV 206
Cdd:PRK13409  476 LLDEPSAHLDVEQRLAVAKAIRRIAEEREATALVVDHDIYMIDYISDRLMV 526
SufC COG0396
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, ...
 4-218 8.88e-23

Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 440165 [Multi-domain]  Cd Length: 245  Bit Score: 95.52  E-value: 8.88e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037402861   4 LSLSNIVKRFGGFEIIHGANLEVKDGEFVVFVGPSGCGKSTLLRMIAGLED--ITSGELQIGGRVVNDVEPADR---GIA 78
Cdd:COG0396     1 LEIKNLHVSVEGKEILKGVNLTIKPGEVHAIMGPNGSGKSTLAKVLMGHPKyeVTSGSILLDGEDILELSPDERaraGIF 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037402861  79 MVFQsyalYPhltVE----ENLSFgLRMNGNPKADTE-------RRVSHVAEILQITELMKRRP--KQLSGGQRQRVAIG 145
Cdd:COG0396    81 LAFQ----YP---VEipgvSVSNF-LRTALNARRGEElsareflKLLKEKMKELGLDEDFLDRYvnEGFSGGEKKRNEIL 152

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1037402861 146 RAIVREPEVFLFDEPLSNLDAE-LRVqMRVEISRLHKKlGTTMIYVTHDQteamTL-----ADRIVVLRAGNIEQIGAP 218
Cdd:COG0396   153 QMLLLEPKLAILDETDSGLDIDaLRI-VAEGVNKLRSP-DRGILIITHYQ----RIldyikPDFVHVLVDGRIVKSGGK 225
YddA COG4178
ABC-type uncharacterized transport system, permease and ATPase components [General function ...
 18-210 1.37e-22

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


Pssm-ID: 443337 [Multi-domain]  Cd Length: 571  Bit Score: 98.73  E-value: 1.37e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037402861  18 IIHGANLEVKDGEFVVFVGPSGCGKSTLLRMIAGLEDITSGELQIggrvvndvePADRGIAMVFQ-SY--------AL-Y 87
Cdd:COG4178   378 LLEDLSLSLKPGERLLITGPSGSGKSTLLRAIAGLWPYGSGRIAR---------PAGARVLFLPQrPYlplgtlreALlY 448

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037402861  88 PHLtveenlsfglrmngnPKADTERRVSHVAEILQITELMKR------RPKQLSGGQRQRVAIGRAIVREPEVFLFDEPL 161
Cdd:COG4178   449 PAT---------------AEAFSDAELREALEAVGLGHLAERldeeadWDQVLSLGEQQRLAFARLLLHKPDWLFLDEAT 513

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 1037402861 162 SNLDAELRVQMrveISRLHKKL-GTTMIYVTHdQTEAMTLADRIVVLRAG 210
Cdd:COG4178   514 SALDEENEAAL---YQLLREELpGTTVISVGH-RSTLAAFHDRVLELTGD 559
PRK15112 PRK15112
peptide ABC transporter ATP-binding protein SapF;
26-225 1.53e-22

peptide ABC transporter ATP-binding protein SapF;


Pssm-ID: 185067 [Multi-domain]  Cd Length: 267  Bit Score: 95.24  E-value: 1.53e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037402861  26 VKDGEFVVFVGPSGCGKSTLLRMIAGLEDITSGELQIGGRVVN--DVEPADRGIAMVFQ--SYALYPHLTVEENLSFGLR 101
Cdd:PRK15112   36 LREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDHPLHfgDYSYRSQRIRMIFQdpSTSLNPRQRISQILDFPLR 115

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037402861 102 MNgnPKADTERRVSHVAEILQITELMKRR----PKQLSGGQRQRVAIGRAIVREPEVFLFDEPLSNLDAELRVQMRVEIS 177
Cdd:PRK15112  116 LN--TDLEPEQREKQIIETLRQVGLLPDHasyyPHMLAPGQKQRLGLARALILRPKVIIADEALASLDMSMRSQLINLML 193

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 1037402861 178 RLHKKLGTTMIYVTHDQTEAMTLADRIVVLRAGNIEQIGAPLDLYDDP 225
Cdd:PRK15112  194 ELQEKQGISYIYVTQHLGMMKHISDQVLVMHQGEVVERGSTADVLASP 241
PRK13539 PRK13539
cytochrome c biogenesis protein CcmA; Provisional
 4-192 1.64e-22

cytochrome c biogenesis protein CcmA; Provisional


Pssm-ID: 237421 [Multi-domain]  Cd Length: 207  Bit Score: 93.79  E-value: 1.64e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037402861   4 LSLSNIVKRFGGFEIIHGANLEVKDGEFVVFVGPSGCGKSTLLRMIAGLEDITSGELQIGGRVVNDVEPADRgIAMVFQS 83
Cdd:PRK13539    3 LEGEDLACVRGGRVLFSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDGGDIDDPDVAEA-CHYLGHR 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037402861  84 YALYPHLTVEENLSFGLRMNGNPkadtERRVSHVAEILQITELMKRRPKQLSGGQRQRVAIGRAIVREPEVFLFDEPLSN 163
Cdd:PRK13539   82 NAMKPALTVAENLEFWAAFLGGE----ELDIAAALEAVGLAPLAHLPFGYLSAGQKRRVALARLLVSNRPIWILDEPTAA 157

                         170       180
                  ....*....|....*....|....*....
gi 1037402861 164 LDAElRVQMRVEISRLHKKLGTTMIYVTH 192
Cdd:PRK13539  158 LDAA-AVALFAELIRAHLAQGGIVIAATH 185
ABCC_cytochrome_bd cd03247
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ...
 4-216 1.68e-22

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


Pssm-ID: 213214 [Multi-domain]  Cd Length: 178  Bit Score: 93.15  E-value: 1.68e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037402861   4 LSLSNIVKRFGGFE--IIHGANLEVKDGEFVVFVGPSGCGKSTLLRMIAGLEDITSGELQIGGRVVNDVEPADRG-IAMV 80
Cdd:cd03247     1 LSINNVSFSYPEQEqqVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDGVPVSDLEKALSSlISVL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037402861  81 FQSyalyPHL---TVEENLSfglrmngnpkadterrvshvaeilqitelmkrrpKQLSGGQRQRVAIGRAIVREPEVFLF 157
Cdd:cd03247    81 NQR----PYLfdtTLRNNLG----------------------------------RRFSGGERQRLALARILLQDAPIVLL 122

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037402861 158 DEPLSNLDAELRVQ-MRVEISRLHKKlgtTMIYVTHDQTeAMTLADRIVVLRAGNIEQIG 216
Cdd:cd03247   123 DEPTVGLDPITERQlLSLIFEVLKDK---TLIWITHHLT-GIEHMDKILFLENGKIIMQG 178
ABC_FeS_Assembly cd03217
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ...
 4-224 2.03e-22

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: 93.36  E-value: 2.03e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037402861   4 LSLSNIVKRFGGFEIIHGANLEVKDGEFVVFVGPSGCGKSTLLRMIAGLED--ITSGELQIGGRVVNDVEPADR---GIA 78
Cdd:cd03217     1 LEIKDLHVSVGGKEILKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMGHPKyeVTEGEILFKGEDITDLPPEERarlGIF 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037402861  79 MVFQSYALYPHLTVEENLsfglrmngnpkadteRRVShvaeilqitelmkrrpKQLSGGQRQRVAIGRAIVREPEVFLFD 158
Cdd:cd03217    81 LAFQYPPEIPGVKNADFL---------------RYVN----------------EGFSGGEKKRNEILQLLLLEPDLAILD 129

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1037402861 159 EPLSNLDAE-LRVQMRVeISRLHKKlGTTMIYVTHDQTEAMTL-ADRIVVLRAGNIEQIGaPLDLYDD 224
Cdd:cd03217   130 EPDSGLDIDaLRLVAEV-INKLREE-GKSVLIITHYQRLLDYIkPDRVHVLYDGRIVKSG-DKELALE 194
PRK09700 PRK09700
D-allose ABC transporter ATP-binding protein AlsA;
4-210 2.41e-22

D-allose ABC transporter ATP-binding protein AlsA;


Pssm-ID: 182036 [Multi-domain]  Cd Length: 510  Bit Score: 97.93  E-value: 2.41e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037402861   4 LSLSNIVKRFGGFEIIHGANLEVKDGEFVVFVGPSGCGKSTLLRMIAGLEDITSGELQIGGRVVNDVEP---ADRGIAMV 80
Cdd:PRK09700    6 ISMAGIGKSFGPVHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNINYNKLDHklaAQLGIGII 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037402861  81 FQSYALYPHLTVEENLSFGL----RMNGNPKADTERRVSHVAEILQITELmKRRPKQ----LSGGQRQRVAIGRAIVREP 152
Cdd:PRK09700   86 YQELSVIDELTVLENLYIGRhltkKVCGVNIIDWREMRVRAAMMLLRVGL-KVDLDEkvanLSISHKQMLEIAKTLMLDA 164

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1037402861 153 EVFLFDEPLSNLDAELRVQMRVEISRLhKKLGTTMIYVTHDQTEAMTLADRIVVLRAG 210
Cdd:PRK09700  165 KVIIMDEPTSSLTNKEVDYLFLIMNQL-RKEGTAIVYISHKLAEIRRICDRYTVMKDG 221
Uup COG0488
ATPase components of ABC transporters with duplicated ATPase domains [General function ...
 4-213 3.14e-22

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


Pssm-ID: 440254 [Multi-domain]  Cd Length: 520  Bit Score: 97.44  E-value: 3.14e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037402861   4 LSLSNIVKRFGGFEIIHGANLEVKDGEFVVFVGPSGCGKSTLLRMIAGLEDITSGELQIGGRVVndvepadrgIAMVFQS 83
Cdd:COG0488   316 LELEGLSKSYGDKTLLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPDSGTVKLGETVK---------IGYFDQH 386

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037402861  84 YA-LYPHLTVEENLSfglrmNGNPKAdTERRVSHVAEILQITELMKRRP-KQLSGGQRQRVAIGRAIVREPEVFLFDEPL 161
Cdd:COG0488   387 QEeLDPDKTVLDELR-----DGAPGG-TEQEVRGYLGRFLFSGDDAFKPvGVLSGGEKARLALAKLLLSPPNVLLLDEPT 460

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1037402861 162 SNLDAELRvqmrvEIsrLHKKLGT---TMIYVTHDQTEAMTLADRIVVLRAGNIE 213
Cdd:COG0488   461 NHLDIETL-----EA--LEEALDDfpgTVLLVSHDRYFLDRVATRILEFEDGGVR 508
PRK15134 PRK15134
microcin C ABC transporter ATP-binding protein YejF; Provisional
 29-229 3.90e-22

microcin C ABC transporter ATP-binding protein YejF; Provisional


Pssm-ID: 237917 [Multi-domain]  Cd Length: 529  Bit Score: 97.47  E-value: 3.90e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037402861  29 GEFVVFVGPSGCGKST----LLRMIAGLEDITSGELQIGGRVVNDVEPADRGIAMVFQ--SYALYPHLTVEENLSFGLRM 102
Cdd:PRK15134  312 GETLGLVGESGSGKSTtglaLLRLINSQGEIWFDGQPLHNLNRRQLLPVRHRIQVVFQdpNSSLNPRLNVLQIIEEGLRV 391

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037402861 103 NgNPKADTERRVSHVAEILQIT----ELMKRRPKQLSGGQRQRVAIGRAIVREPEVFLFDEPLSNLDAELRVQMRVEISR 178
Cdd:PRK15134  392 H-QPTLSAAQREQQVIAVMEEVgldpETRHRYPAEFSGGQRQRIAIARALILKPSLIILDEPTSSLDKTVQAQILALLKS 470

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1037402861 179 LHKKLGTTMIYVTHDQTEAMTLADRIVVLRAGNIEQIGAPLDLYDDPANQF 229
Cdd:PRK15134  471 LQQKHQLAYLFISHDLHVVRALCHQVIVLRQGEVVEQGDCERVFAAPQQEY 521
ABCC_TAP cd03248
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ...
 18-212 5.87e-22

ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; TAP (Transporter Associated with Antigen Processing) is essential for peptide delivery from the cytosol into the lumen of the endoplasmic reticulum (ER), where these peptides are loaded on major histocompatibility complex (MHC) I molecules. Loaded MHC I leave the ER and display their antigenic cargo on the cell surface to cytotoxic T cells. Subsequently, virus-infected or malignantly transformed cells can be eliminated. TAP belongs to the large family of ATP-binding cassette (ABC) transporters, which translocate a vast variety of solutes across membranes.


Pssm-ID: 213215 [Multi-domain]  Cd Length: 226  Bit Score: 92.92  E-value: 5.87e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037402861  18 IIHGANLEVKDGEFVVFVGPSGCGKSTLLRMIAGLEDITSGELQIGGRVVNDVEPA--DRGIAMVFQSYALYPHlTVEEN 95
Cdd:cd03248    29 VLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDGKPISQYEHKylHSKVSLVGQEPVLFAR-SLQDN 107

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037402861  96 LSFGLR-------MNGNPKADTERRVSHVAeiLQITELMKRRPKQLSGGQRQRVAIGRAIVREPEVFLFDEPLSNLDAEL 168
Cdd:cd03248   108 IAYGLQscsfecvKEAAQKAHAHSFISELA--SGYDTEVGEKGSQLSGGQKQRVAIARALIRNPQVLILDEATSALDAES 185

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 1037402861 169 RVQMRVEISRLHKKlgTTMIYVTHdQTEAMTLADRIVVLRAGNI 212
Cdd:cd03248   186 EQQVQQALYDWPER--RTVLVIAH-RLSTVERADQILVLDGGRI 226
cbiO PRK13638
energy-coupling factor ABC transporter ATP-binding protein;
4-222 6.29e-22

energy-coupling factor ABC transporter ATP-binding protein;


Pssm-ID: 184198 [Multi-domain]  Cd Length: 271  Bit Score: 93.92  E-value: 6.29e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037402861   4 LSLSNIVKRFGGFEIIHGANLEVKDGEFVVFVGPSGCGKSTLLRMIAGLEDITSGELQIGGRVVNdvePADRG------- 76
Cdd:PRK13638    2 LATSDLWFRYQDEPVLKGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLRPQKGAVLWQGKPLD---YSKRGllalrqq 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037402861  77 IAMVFQSYALYPHLT-VEENLSFGLRMNGNPKADTERRVSHvAEILQITELMKRRPKQ-LSGGQRQRVAIGRAIVREPEV 154
Cdd:PRK13638   79 VATVFQDPEQQIFYTdIDSDIAFSLRNLGVPEAEITRRVDE-ALTLVDAQHFRHQPIQcLSHGQKKRVAIAGALVLQARY 157

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1037402861 155 FLFDEPLSNLDAELRVQMRVEISRLHKKlGTTMIYVTHDQTEAMTLADRIVVLRAGNIEQIGAPLDLY 222
Cdd:PRK13638  158 LLLDEPTAGLDPAGRTQMIAIIRRIVAQ-GNHVIISSHDIDLIYEISDAVYVLRQGQILTHGAPGEVF 224
PRK13549 PRK13549
xylose transporter ATP-binding subunit; Provisional
 4-210 8.27e-22

xylose transporter ATP-binding subunit; Provisional


Pssm-ID: 184134 [Multi-domain]  Cd Length: 506  Bit Score: 96.15  E-value: 8.27e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037402861   4 LSLSNIVKRFGGFEIIHGANLEVKDGEFVVFVGPSGCGKSTLLRMIAGL--EDITSGELQIGG-----RVVNDVEPAdrG 76
Cdd:PRK13549    6 LEMKNITKTFGGVKALDNVSLKVRAGEIVSLCGENGAGKSTLMKVLSGVypHGTYEGEIIFEGeelqaSNIRDTERA--G 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037402861  77 IAMVFQSYALYPHLTVEENLSFGLRMNGNPKADTERRVSHVAEILQITEL---MKRRPKQLSGGQRQRVAIGRAIVREPE 153
Cdd:PRK13549   84 IAIIHQELALVKELSVLENIFLGNEITPGGIMDYDAMYLRAQKLLAQLKLdinPATPVGNLGLGQQQLVEIAKALNKQAR 163

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1037402861 154 VFLFDEPLSNL-DAELRVQMrvEISRLHKKLGTTMIYVTHDQTEAMTLADRIVVLRAG 210
Cdd:PRK13549  164 LLILDEPTASLtESETAVLL--DIIRDLKAHGIACIYISHKLNEVKAISDTICVIRDG 219
bacteriocin_ABC TIGR01193
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ...
 15-223 8.46e-22

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: 96.73  E-value: 8.46e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037402861  15 GFEIIHGANLEVKDGEFVVFVGPSGCGKSTLLRMIAGLEDITSGELQIGGRVVNDVepaDRGIAMVFQSY-ALYPHL--- 90
Cdd:TIGR01193 486 GSNILSDISLTIKMNSKTTIVGMSGSGKSTLAKLLVGFFQARSGEILLNGFSLKDI---DRHTLRQFINYlPQEPYIfsg 562

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037402861  91 TVEENLSFGlrmnGNPKAdTERRVSHVAEILQITELMKRRPK-----------QLSGGQRQRVAIGRAIVREPEVFLFDE 159
Cdd:TIGR01193 563 SILENLLLG----AKENV-SQDEIWAACEIAEIKDDIENMPLgyqtelseegsSISGGQKQRIALARALLTDSKVLILDE 637

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1037402861 160 PLSNLDAELRVQMrveISRLHKKLGTTMIYVTHDQTEAmTLADRIVVLRAGNIEQIGAPLDLYD 223
Cdd:TIGR01193 638 STSNLDTITEKKI---VNNLLNLQDKTIIFVAHRLSVA-KQSDKIIVLDHGKIIEQGSHDELLD 697
PRK13657 PRK13657
glucan ABC transporter ATP-binding protein/ permease;
19-216 9.49e-22

glucan ABC transporter ATP-binding protein/ permease;


Pssm-ID: 184214 [Multi-domain]  Cd Length: 588  Bit Score: 96.57  E-value: 9.49e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037402861  19 IHGANLEVKDGEFVVFVGPSGCGKSTLLRMIAGLEDITSGELQIGGRVVNDVEPAD--RGIAMVFQSYALYPHlTVEENL 96
Cdd:PRK13657  351 VEDVSFEAKPGQTVAIVGPTGAGKSTLINLLQRVFDPQSGRILIDGTDIRTVTRASlrRNIAVVFQDAGLFNR-SIEDNI 429

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037402861  97 SFGlrmngnpKAD-TERRVSHVAEILQITELMKRRPK-----------QLSGGQRQRVAIGRAIVREPEVFLFDEPLSNL 164
Cdd:PRK13657  430 RVG-------RPDaTDEEMRAAAERAQAHDFIERKPDgydtvvgergrQLSGGERQRLAIARALLKDPPILILDEATSAL 502

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1037402861 165 DAELRVQMRVEISRLHKklGTTMIYVTHdQTEAMTLADRIVVLRAGNIEQIG 216
Cdd:PRK13657  503 DVETEAKVKAALDELMK--GRTTFIIAH-RLSTVRNADRILVFDNGRVVESG 551
PRK10895 PRK10895
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
 1-224 1.52e-21

lipopolysaccharide ABC transporter ATP-binding protein; Provisional


Pssm-ID: 182817 [Multi-domain]  Cd Length: 241  Bit Score: 91.88  E-value: 1.52e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037402861   1 MAELSLSNIVKRFGGFEIIHGANLEVKDGEFVVFVGPSGCGKSTLLRMIAGLEDITSGELQIGGRVVNDV---EPADRGI 77
Cdd:PRK10895    1 MATLTAKNLAKAYKGRRVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEDISLLplhARARRGI 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037402861  78 AMVFQSYALYPHLTVEENLSFGLRMNGNPKADT-ERRVSHVAEILQITELMKRRPKQLSGGQRQRVAIGRAIVREPEVFL 156
Cdd:PRK10895   81 GYLPQEASIFRRLSVYDNLMAVLQIRDDLSAEQrEDRANELMEEFHIEHLRDSMGQSLSGGERRRVEIARALAANPKFIL 160

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1037402861 157 FDEPLSNLDAELRVQMRVEISRLhKKLGTTMIYVTHDQTEAMTLADRIVVLRAGNIEQIGAPLDLYDD 224
Cdd:PRK10895  161 LDEPFAGVDPISVIDIKRIIEHL-RDSGLGVLITDHNVRETLAVCERAYIVSQGHLIAHGTPTEILQD 227
3a01204 TIGR00955
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ...
 17-218 2.02e-21

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


Pssm-ID: 273361 [Multi-domain]  Cd Length: 617  Bit Score: 95.50  E-value: 2.02e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037402861  17 EIIHGANLEVKDGEFVVFVGPSGCGKSTLLRMIAGLediTSGELQIGGRVVNDVEPAD----RGI-AMVFQSYALYPHLT 91
Cdd:TIGR00955  39 HLLKNVSGVAKPGELLAVMGSSGAGKTTLMNALAFR---SPKGVKGSGSVLLNGMPIDakemRAIsAYVQQDDLFIPTLT 115

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037402861  92 VEENLSFG--LRMNGNPKADTerRVSHVAEILQITELMK---------RRPKQLSGGQRQRVAIGRAIVREPEVFLFDEP 160
Cdd:TIGR00955 116 VREHLMFQahLRMPRRVTKKE--KRERVDEVLQALGLRKcantrigvpGRVKGLSGGERKRLAFASELLTDPPLLFCDEP 193

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1037402861 161 LSNLDAelrvQMRVEISRLHKKL---GTTMIYVTHDQT-EAMTLADRIVVLRAGNIEQIGAP 218
Cdd:TIGR00955 194 TSGLDS----FMAYSVVQVLKGLaqkGKTIICTIHQPSsELFELFDKIILMAEGRVAYLGSP 251
NHLM_micro_ABC1 TIGR03796
NHLM bacteriocin system ABC transporter, peptidase/ATP-binding protein; This protein describes ...
 18-216 3.51e-21

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: 95.01  E-value: 3.51e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037402861  18 IIHGANLEVKDGEFVVFVGPSGCGKSTLLRMIAGLEDITSGELQIGGRVVNDVEPA--DRGIAMVFQSYALYPHlTVEEN 95
Cdd:TIGR03796 494 LIENFSLTLQPGQRVALVGGSGSGKSTIAKLVAGLYQPWSGEILFDGIPREEIPREvlANSVAMVDQDIFLFEG-TVRDN 572

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037402861  96 LSfgLRMNGNPKADTERrvshVAEILQITELMKRRP-----------KQLSGGQRQRVAIGRAIVREPEVFLFDEPLSNL 164
Cdd:TIGR03796 573 LT--LWDPTIPDADLVR----ACKDAAIHDVITSRPggydaelaeggANLSGGQRQRLEIARALVRNPSILILDEATSAL 646

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1037402861 165 DAELRVQmrveISRLHKKLGTTMIYVTHdQTEAMTLADRIVVLRAGNIEQIG 216
Cdd:TIGR03796 647 DPETEKI----IDDNLRRRGCTCIIVAH-RLSTIRDCDEIIVLERGKVVQRG 693
PRK14271 PRK14271
phosphate ABC transporter ATP-binding protein; Provisional
 8-238 6.62e-21

phosphate ABC transporter ATP-binding protein; Provisional


Pssm-ID: 172759 [Multi-domain]  Cd Length: 276  Bit Score: 90.93  E-value: 6.62e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037402861   8 NIVKRFGGFEIIHGANLEVKDGEFVVFVGPSGCGKSTLLRMIAGLEDITSG-----ELQIGGRVV---NDVEPADRGIAM 79
Cdd:PRK14271   26 NLTLGFAGKTVLDQVSMGFPARAVTSLMGPTGSGKTTFLRTLNRMNDKVSGyrysgDVLLGGRSIfnyRDVLEFRRRVGM 105

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037402861  80 VFQSYALYPhLTVEENLSFGLRMNG-NPKAD----TERRVSHVAEILQITELMKRRPKQLSGGQRQRVAIGRAIVREPEV 154
Cdd:PRK14271  106 LFQRPNPFP-MSIMDNVLAGVRAHKlVPRKEfrgvAQARLTEVGLWDAVKDRLSDSPFRLSGGQQQLLCLARTLAVNPEV 184

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037402861 155 FLFDEPLSNLDAELRVQMRVEISRLHKKLgtTMIYVTHDQTEAMTLADRIVVLRAGNIEQIGAPLDLYDDPAN----QFV 230
Cdd:PRK14271  185 LLLDEPTSALDPTTTEKIEEFIRSLADRL--TVIIVTHNLAQAARISDRAALFFDGRLVEEGPTEQLFSSPKHaetaRYV 262


                  ....*...
gi 1037402861 231 AGFVGSPK 238
Cdd:PRK14271  263 AGLSGDVK 270
PRK11160 PRK11160
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
 2-212 7.15e-21

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


Pssm-ID: 236865 [Multi-domain]  Cd Length: 574  Bit Score: 93.74  E-value: 7.15e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037402861   2 AELSLSNIVKRF--GGFEIIHGANLEVKDGEFVVFVGPSGCGKSTLLRMIAGLEDITSGELQIGGRVVNDV-EPADR-GI 77
Cdd:PRK11160  337 VSLTLNNVSFTYpdQPQPVLKGLSLQIKAGEKVALLGRTGCGKSTLLQLLTRAWDPQQGEILLNGQPIADYsEAALRqAI 416

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037402861  78 AMVFQSYALYPHlTVEENLSFglrmnGNPKADTERrvshVAEILQITELMK----------------RrpkQLSGGQRQR 141
Cdd:PRK11160  417 SVVSQRVHLFSA-TLRDNLLL-----AAPNASDEA----LIEVLQQVGLEKlleddkglnawlgeggR---QLSGGEQRR 483

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1037402861 142 VAIGRAIVREPEVFLFDEPLSNLDAELRVQMrVEISRLHKKlGTTMIYVTHDQTeAMTLADRIVVLRAGNI 212
Cdd:PRK11160  484 LGIARALLHDAPLLLLDEPTEGLDAETERQI-LELLAEHAQ-NKTVLMITHRLT-GLEQFDRICVMDNGQI 551
ABC2_perm_RbbA NF033858
ribosome-associated ATPase/putative transporter RbbA;
8-221 1.92e-20

ribosome-associated ATPase/putative transporter RbbA;


Pssm-ID: 468210 [Multi-domain]  Cd Length: 907  Bit Score: 92.88  E-value: 1.92e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037402861   8 NIVKRFGGFEIIHGANLEVKDGEFVVFVGPSGCGKSTLLRMIAGLEDITSGELQIGGRVV--NDVEpADRGIAMVFQSYA 85
Cdd:NF033858  271 GLTMRFGDFTAVDHVSFRIRRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGEAWLFGQPVdaGDIA-TRRRVGYMSQAFS 349

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037402861  86 LYPHLTVEENLSFGLRMNGNPKADTERRVSHVAEILQITELMKRRPKQLSGGQRQRVAIGRAIVREPEVFLFDEPLSNLD 165
Cdd:NF033858  350 LYGELTVRQNLELHARLFHLPAAEIAARVAEMLERFDLADVADALPDSLPLGIRQRLSLAVAVIHKPELLILDEPTSGVD 429

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037402861 166 AELR---VQMRVEISRlhkKLGTTmIYV-THDQTEAMtLADRIVVLRAGNIEQIGAPLDL 221
Cdd:NF033858  430 PVARdmfWRLLIELSR---EDGVT-IFIsTHFMNEAE-RCDRISLMHAGRVLASDTPAAL 484
phnK PRK11701
phosphonate C-P lyase system protein PhnK; Provisional
 4-225 2.05e-20

phosphonate C-P lyase system protein PhnK; Provisional


Pssm-ID: 183280 [Multi-domain]  Cd Length: 258  Bit Score: 89.21  E-value: 2.05e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037402861   4 LSLSNIVKRFGGFEIIHGANLEVKDGEFVVFVGPSGCGKSTLLRMIAGLEDITSGELQIGGRVVNDVEPADRGIA---MV 80
Cdd:PRK11701    7 LSVRGLTKLYGPRKGCRDVSFDLYPGEVLGIVGESGSGKTTLLNALSARLAPDAGEVHYRMRDGQLRDLYALSEAerrRL 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037402861  81 FQSYALYphltVEENLSFGLRMNGNPKADTERR-----VSHVAEI-------LQITELMKRR----PKQLSGGQRQRVAI 144
Cdd:PRK11701   87 LRTEWGF----VHQHPRDGLRMQVSAGGNIGERlmavgARHYGDIratagdwLERVEIDAARiddlPTTFSGGMQQRLQI 162

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037402861 145 GRAIVREPEVFLFDEPLSNLDaeLRVQMRV--EISRLHKKLGTTMIYVTHDQTEAMTLADRIVVLRAGNIEQIGAPLDLY 222
Cdd:PRK11701  163 ARNLVTHPRLVFMDEPTGGLD--VSVQARLldLLRGLVRELGLAVVIVTHDLAVARLLAHRLLVMKQGRVVESGLTDQVL 240


                  ...
gi 1037402861 223 DDP 225
Cdd:PRK11701  241 DDP 243
rim_protein TIGR01257
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ...
 6-233 3.58e-20

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


Pssm-ID: 130324 [Multi-domain]  Cd Length: 2272  Bit Score: 92.38  E-value: 3.58e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037402861    6 LSNIVKRF--GGFEIIHGANLEVKDGEFVVFVGPSGCGKSTLLRMIAGLEDITSGELQIGGR-VVNDVEPADRGIAMVFQ 82
Cdd:TIGR01257  931 VKNLVKIFepSGRPAVDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGKdIETNLDAVRQSLGMCPQ 1010

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037402861   83 SYALYPHLTVEENLSFGLRMNGNPKADTERRVSHVAEILQITELMKRRPKQLSGGQRQRVAIGRAIVREPEVFLFDEPLS 162
Cdd:TIGR01257 1011 HNILFHHLTVAEHILFYAQLKGRSWEEAQLEMEAMLEDTGLHHKRNEEAQDLSGGMQRKLSVAIAFVGDAKVVVLDEPTS 1090

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1037402861  163 NLDAELRVQMRVEIsrLHKKLGTTMIYVTHDQTEAMTLADRIVVLRAGNIEQIGAPLDLyddpANQFVAGF 233
Cdd:TIGR01257 1091 GVDPYSRRSIWDLL--LKYRSGRTIIMSTHHMDEADLLGDRIAIISQGRLYCSGTPLFL----KNCFGTGF 1155
BtuD COG4138
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ...
 4-212 5.10e-20

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


Pssm-ID: 443313 [Multi-domain]  Cd Length: 248  Bit Score: 87.97  E-value: 5.10e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037402861   4 LSLSNIV--KRFGGFeiihgaNLEVKDGEFVVFVGPSGCGKSTLLRMIAGLEDiTSGELQIGGRVVNDVEPAD--RGIAM 79
Cdd:COG4138     1 LQLNDVAvaGRLGPI------SAQVNAGELIHLIGPNGAGKSTLLARMAGLLP-GQGEILLNGRPLSDWSAAElaRHRAY 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037402861  80 VFQSYALYPHLTVEENLSFGLRMNGNPKAdTERRVSHVAEILQITELMKRRPKQLSGGQRQRVAIGRAIVR-------EP 152
Cdd:COG4138    74 LSQQQSPPFAMPVFQYLALHQPAGASSEA-VEQLLAQLAEALGLEDKLSRPLTQLSGGEWQRVRLAAVLLQvwptinpEG 152

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1037402861 153 EVFLFDEPLSNLDaelrVQMRVEISRLHKKL---GTTMIYVTHDQTEAMTLADRIVVLRAGNI 212
Cdd:COG4138   153 QLLLLDEPMNSLD----VAQQAALDRLLRELcqqGITVVMSSHDLNHTLRHADRVWLLKQGKL 211
CydC TIGR02868
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ...
 14-193 1.57e-19

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: 89.73  E-value: 1.57e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037402861  14 GGFEIIHGANLEVKDGEFVVFVGPSGCGKSTLLRMIAGLEDITSGELQIGGRVVNDVEPADRGIAMVFqsYALYPHL--- 90
Cdd:TIGR02868 346 GAPPVLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPLQGEVTLDGVPVSSLDQDEVRRRVSV--CAQDAHLfdt 423

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037402861  91 TVEENLSFGlrmngNPKAdTERRVSHVAEILQITELMKRRP-----------KQLSGGQRQRVAIGRAIVREPEVFLFDE 159
Cdd:TIGR02868 424 TVRENLRLA-----RPDA-TDEELWAALERVGLADWLRALPdgldtvlgeggARLSGGERQRLALARALLADAPILLLDE 497

                         170       180       190
                  ....*....|....*....|....*....|....*
gi 1037402861 160 PLSNLDAELRVQMrveISRLHKKL-GTTMIYVTHD 193
Cdd:TIGR02868 498 PTEHLDAETADEL---LEDLLAALsGRTVVLITHH 529
PRK15134 PRK15134
microcin C ABC transporter ATP-binding protein YejF; Provisional
 17-214 3.99e-19

microcin C ABC transporter ATP-binding protein YejF; Provisional


Pssm-ID: 237917 [Multi-domain]  Cd Length: 529  Bit Score: 88.61  E-value: 3.99e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037402861  17 EIIHGANLEVKDGEFVVFVGPSGCGKS----TLLRMIAGLEDI-TSGELQIGGR-VVNDVEPADRG-----IAMVFQS-- 83
Cdd:PRK15134   23 TVVNDVSLQIEAGETLALVGESGSGKSvtalSILRLLPSPPVVyPSGDIRFHGEsLLHASEQTLRGvrgnkIAMIFQEpm 102

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037402861  84 YALYPHLTVEENLSFGLRMNGNPKADTERrvshvAEILQITELM-----KRR----PKQLSGGQRQRVAIGRAIVREPEV 154
Cdd:PRK15134  103 VSLNPLHTLEKQLYEVLSLHRGMRREAAR-----GEILNCLDRVgirqaAKRltdyPHQLSGGERQRVMIAMALLTRPEL 177

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1037402861 155 FLFDEPLSNLDAELRVQMRVEISRLHKKLGTTMIYVTHDQTEAMTLADRIVVLRAGN-IEQ 214
Cdd:PRK15134  178 LIADEPTTALDVSVQAQILQLLRELQQELNMGLLFITHNLSIVRKLADRVAVMQNGRcVEQ 238
PRK13538 PRK13538
cytochrome c biogenesis heme-transporting ATPase CcmA;
20-167 4.01e-19

cytochrome c biogenesis heme-transporting ATPase CcmA;


Pssm-ID: 184125 [Multi-domain]  Cd Length: 204  Bit Score: 84.47  E-value: 4.01e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037402861  20 HGANLEVKDGEFVVFVGPSGCGKSTLLRMIAGLEDITSGELQIGGRVVNDVEPAdrgiamvFQSYALY--------PHLT 91
Cdd:PRK13538   18 SGLSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVLWQGEPIRRQRDE-------YHQDLLYlghqpgikTELT 90

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1037402861  92 VEENLSFGLRMNGNPKADTerrvshVAEILQITELMKRR--P-KQLSGGQRQRVAIGRAIVREPEVFLFDEPLSNLDAE 167
Cdd:PRK13538   91 ALENLRFYQRLHGPGDDEA------LWEALAQVGLAGFEdvPvRQLSAGQQRRVALARLWLTRAPLWILDEPFTAIDKQ 163
CP_lyasePhnK TIGR02323
phosphonate C-P lyase system protein PhnK; Members of this family are the PhnK protein of C-P ...
 4-236 4.29e-19

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: 85.65  E-value: 4.29e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037402861   4 LSLSNIVKRFGGFEIIHGANLEVKDGEFVVFVGPSGCGKSTLLRMIAGLEDITSGELQIGGRvvndvepaDRGIAMVFQ- 82
Cdd:TIGR02323   4 LQVSGLSKSYGGGKGCRDVSFDLYPGEVLGIVGESGSGKSTLLGCLAGRLAPDHGTATYIMR--------SGAELELYQl 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037402861  83 SYALYPHLT------VEENLSFGLRMNGNPKADTERR-----VSHVAEI-------LQITELMKRR----PKQLSGGQRQ 140
Cdd:TIGR02323  76 SEAERRRLMrtewgfVHQNPRDGLRMRVSAGANIGERlmaigARHYGNIrataqdwLEEVEIDPTRiddlPRAFSGGMQQ 155

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037402861 141 RVAIGRAIVREPEVFLFDEPLSNLDAELRVQMRVEISRLHKKLGTTMIYVTHDQTEAMTLADRIVVLRAGNIEQIGAPLD 220
Cdd:TIGR02323 156 RLQIARNLVTRPRLVFMDEPTGGLDVSVQARLLDLLRGLVRDLGLAVIIVTHDLGVARLLAQRLLVMQQGRVVESGLTDQ 235

                         250
                  ....*....|....*.
gi 1037402861 221 LYDDPANQFVAGFVGS 236
Cdd:TIGR02323 236 VLDDPQHPYTQLLVSS 251
PRK03695 PRK03695
vitamin B12-transporter ATPase; Provisional
 23-218 9.56e-19

vitamin B12-transporter ATPase; Provisional


Pssm-ID: 235150 [Multi-domain]  Cd Length: 248  Bit Score: 84.21  E-value: 9.56e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037402861  23 NLEVKDGEFVVFVGPSGCGKSTLLRMIAGLEDiTSGELQIGGRVVNDVEPAD----RG---------IAM-VFQSYALYp 88
Cdd:PRK03695   16 SAEVRAGEILHLVGPNGAGKSTLLARMAGLLP-GSGSIQFAGQPLEAWSAAElarhRAylsqqqtppFAMpVFQYLTLH- 93

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037402861  89 hltveenlsfglRMNGNPKADTERRVSHVAEILQITELMKRRPKQLSGGQRQRV-------AIGRAIVREPEVFLFDEPL 161
Cdd:PRK03695   94 ------------QPDKTRTEAVASALNEVAEALGLDDKLGRSVNQLSGGEWQRVrlaavvlQVWPDINPAGQLLLLDEPM 161

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037402861 162 SNLDaelrVQMRVEISRLHKKL---GTTMIYVTHDQTEAMTLADRIVVLRAGNIEQIGAP 218
Cdd:PRK03695  162 NSLD----VAQQAALDRLLSELcqqGIAVVMSSHDLNHTLRHADRVWLLKQGKLLASGRR 217
PRK10261 PRK10261
glutathione transporter ATP-binding protein; Provisional
 4-229 3.11e-18

glutathione transporter ATP-binding protein; Provisional


Pssm-ID: 182342 [Multi-domain]  Cd Length: 623  Bit Score: 86.06  E-value: 3.11e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037402861   4 LSLSNIVKRF----GGFEIIHGANLEVKDGEFVVFVGPSGCGKSTLLRMIAGLEDITSGELQIGG--------RVVNDVE 71
Cdd:PRK10261   13 LAVENLNIAFmqeqQKIAAVRNLSFSLQRGETLAIVGESGSGKSVTALALMRLLEQAGGLVQCDKmllrrrsrQVIELSE 92

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037402861  72 PAD------RG--IAMVFQS--YALYPHLTVEENLSFGLRMN---GNPKADTE-RRVSHVAEILQITELMKRRPKQLSGG 137
Cdd:PRK10261   93 QSAaqmrhvRGadMAMIFQEpmTSLNPVFTVGEQIAESIRLHqgaSREEAMVEaKRMLDQVRIPEAQTILSRYPHQLSGG 172

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037402861 138 QRQRVAIGRAIVREPEVFLFDEPLSNLDAELRVQMRVEISRLHKKLGTTMIYVTHDQTEAMTLADRIVVLRAGNIEQIGA 217
Cdd:PRK10261  173 MRQRVMIAMALSCRPAVLIADEPTTALDVTIQAQILQLIKVLQKEMSMGVIFITHDMGVVAEIADRVLVMYQGEAVETGS 252

                         250
                  ....*....|..
gi 1037402861 218 PLDLYDDPANQF 229
Cdd:PRK10261  253 VEQIFHAPQHPY 264
PRK10575 PRK10575
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
5-221 4.21e-18

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


Pssm-ID: 182561 [Multi-domain]  Cd Length: 265  Bit Score: 82.91  E-value: 4.21e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037402861   5 SLSNIVKRFGGFEIIHGANLEVKDGEFVVFVGPSGCGKSTLLRMIAGLEDITSGELQIGGRVVN--DVEPADRGIAMVFQ 82
Cdd:PRK10575   13 ALRNVSFRVPGRTLLHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPLEswSSKAFARKVAYLPQ 92

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037402861  83 SYALYPHLTVEENLSFGlRMN-----GNPKADTERRVSHVAEILQITELMKRRPKQLSGGQRQRVAIGRAIVREPEVFLF 157
Cdd:PRK10575   93 QLPAAEGMTVRELVAIG-RYPwhgalGRFGAADREKVEEAISLVGLKPLAHRLVDSLSGGERQRAWIAMLVAQDSRCLLL 171

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1037402861 158 DEPLSNLDAELRVQMRVEISRLHKKLGTTMIYVTHDQTEAMTLADRIVVLRAGNIEQIGAPLDL 221
Cdd:PRK10575  172 DEPTSALDIAHQVDVLALVHRLSQERGLTVIAVLHDINMAARYCDYLVALRGGEMIAQGTPAEL 235
ABCD_peroxisomal_ALDP cd03223
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ...
 23-195 5.90e-18

ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding cassette transporter (Pat) is involved in the import of very long-chain fatty acids (VLCFA) into the peroxisome. The peroxisomal membrane forms a permeability barrier for a wide variety of metabolites required for and formed during fatty acid beta-oxidation. To communicate with the cytoplasm and mitochondria, peroxisomes need dedicated proteins to transport such hydrophilic molecules across their membranes. X-linked adrenoleukodystrophy (X-ALD) is caused by mutations in the ALD gene, which encodes ALDP (adrenoleukodystrophy protein ), a peroxisomal integral membrane protein that is a member of the ATP-binding cassette (ABC) transporter protein family. The disease is characterized by a striking and unpredictable variation in phenotypic expression. Phenotypes include the rapidly progressive childhood cerebral form (CCALD), the milder adult form, adrenomyeloneuropathy (AMN), and variants without neurologic involvement (i.e. asymptomatic).


Pssm-ID: 213190 [Multi-domain]  Cd Length: 166  Bit Score: 80.28  E-value: 5.90e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037402861  23 NLEVKDGEFVVFVGPSGCGKSTLLRMIAGLEDITSGELQIggrvvndvePADRGIAMVFQ-SYalyphltveenLSFG-L 100
Cdd:cd03223    21 SFEIKPGDRLLITGPSGTGKSSLFRALAGLWPWGSGRIGM---------PEGEDLLFLPQrPY-----------LPLGtL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037402861 101 RmngnpkadterrvshvaEILqitelmkRRP--KQLSGGQRQRVAIGRAIVREPEVFLFDEPLSNLDAELRVQMRveisR 178
Cdd:cd03223    81 R-----------------EQL-------IYPwdDVLSGGEQQRLAFARLLLHKPKFVFLDEATSALDEESEDRLY----Q 132

                         170
                  ....*....|....*..
gi 1037402861 179 LHKKLGTTMIYVTHDQT 195
Cdd:cd03223   133 LLKELGITVISVGHRPS 149
araG PRK11288
L-arabinose ABC transporter ATP-binding protein AraG;
22-212 9.33e-18

L-arabinose ABC transporter ATP-binding protein AraG;


Pssm-ID: 183077 [Multi-domain]  Cd Length: 501  Bit Score: 84.19  E-value: 9.33e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037402861  22 ANLEVKDGEFVVFVGPSGCGKSTLLRMIAGLEDITSGELQIGGRVVNDVEPAD---RGIAMV---FQSYALYPHLTVEEN 95
Cdd:PRK11288  272 ISFSVRAGEIVGLFGLVGAGRSELMKLLYGATRRTAGQVYLDGKPIDIRSPRDairAGIMLCpedRKAEGIIPVHSVADN 351

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037402861  96 LS---------FGLRMNGNPKADTERRvshvaeilQITELMKRRP------KQLSGGQRQRVAIGRAIVREPEVFLFDEP 160
Cdd:PRK11288  352 INisarrhhlrAGCLINNRWEAENADR--------FIRSLNIKTPsreqliMNLSGGNQQKAILGRWLSEDMKVILLDEP 423

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1037402861 161 LSNLDaelrVQMRVEISRLHKKL---GTTMIYVTHDQTEAMTLADRIVVLRAGNI 212
Cdd:PRK11288  424 TRGID----VGAKHEIYNVIYELaaqGVAVLFVSSDLPEVLGVADRIVVMREGRI 474
ABC_CcmA_heme_exporter cd03231
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ...
 14-192 9.75e-18

Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the bacterial CcmAB transporter. The CCM family is involved in bacterial cytochrome c biogenesis. Cytochrome c maturation in E. coli requires the ccm operon, which encodes eight membrane proteins (CcmABCDEFGH). CcmE is a periplasmic heme chaperon that binds heme covalently and transfers it onto apocytochrome c in the presence of CcmF, CcmG, and CcmH. The CcmAB proteins represent an ABC transporter and the CcmCD proteins participate in heme transfer to CcmE.


Pssm-ID: 213198 [Multi-domain]  Cd Length: 201  Bit Score: 80.61  E-value: 9.75e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037402861  14 GGFEIIHGANLEVKDGEFVVFVGPSGCGKSTLLRMIAGLEDITSGELQIGGRVVNDVEPA-DRGIAMVFQSYALYPHLTV 92
Cdd:cd03231    11 DGRALFSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNGGPLDFQRDSiARGLLYLGHAPGIKTTLSV 90

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037402861  93 EENLSFGLRMNGnpkadTERRVSHVAEIlQITELMKRRPKQLSGGQRQRVAIGRAIVREPEVFLFDEPLSNLDAElRVQM 172
Cdd:cd03231    91 LENLRFWHADHS-----DEQVEEALARV-GLNGFEDRPVAQLSAGQQRRVALARLLLSGRPLWILDEPTTALDKA-GVAR 163

                         170       180
                  ....*....|....*....|
gi 1037402861 173 RVEISRLHKKLGTTMIYVTH 192
Cdd:cd03231   164 FAEAMAGHCARGGMVVLTTH 183
PRK10789 PRK10789
SmdA family multidrug ABC transporter permease/ATP-binding protein;
18-216 1.41e-17

SmdA family multidrug ABC transporter permease/ATP-binding protein;


Pssm-ID: 182732 [Multi-domain]  Cd Length: 569  Bit Score: 83.99  E-value: 1.41e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037402861  18 IIHGANLEVKDGEFVVFVGPSGCGKSTLLRMIAGLEDITSGELQIGGRVVNDVEPAD-RG-IAMVFQSYALYPHlTVEEN 95
Cdd:PRK10789  330 ALENVNFTLKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGDIRFHDIPLTKLQLDSwRSrLAVVSQTPFLFSD-TVANN 408

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037402861  96 LSFGlrmngNPKAdTERRVSHVAEILQITELMKRRPK-----------QLSGGQRQRVAIGRAIVREPEVFLFDEPLSNL 164
Cdd:PRK10789  409 IALG-----RPDA-TQQEIEHVARLASVHDDILRLPQgydtevgergvMLSGGQKQRISIARALLLNAEILILDDALSAV 482

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1037402861 165 DAELRVQMRVEISRLHKklGTTMIYVTHdQTEAMTLADRIVVLRAGNIEQIG 216
Cdd:PRK10789  483 DGRTEHQILHNLRQWGE--GRTVIISAH-RLSALTEASEILVMQHGHIAQRG 531
MRP_assoc_pro TIGR00957
multi drug resistance-associated protein (MRP); This model describes multi drug ...
 19-223 1.43e-17

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: 84.23  E-value: 1.43e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037402861   19 IHGANLEVKDGEFVVFVGPSGCGKSTLLRMIAGLEDITSGELQIGGRVvndvepadrgiAMVFQSyALYPHLTVEENLSF 98
Cdd:TIGR00957  654 LNGITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVHMKGSV-----------AYVPQQ-AWIQNDSLRENILF 721

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037402861   99 GLRMNGNPKADTERRVSHVA--EIL---QITELmKRRPKQLSGGQRQRVAIGRAIVREPEVFLFDEPLSNLDAELRVQMR 173
Cdd:TIGR00957  722 GKALNEKYYQQVLEACALLPdlEILpsgDRTEI-GEKGVNLSGGQKQRVSLARAVYSNADIYLFDDPLSAVDAHVGKHIF 800

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|.
gi 1037402861  174 VEISRLHKKL-GTTMIYVTHDQTeAMTLADRIVVLRAGNIEQIGAPLDLYD 223
Cdd:TIGR00957  801 EHVIGPEGVLkNKTRILVTHGIS-YLPQVDVIIVMSGGKISEMGSYQELLQ 850
dppD PRK11022
dipeptide transporter ATP-binding subunit; Provisional
 1-225 1.69e-17

dipeptide transporter ATP-binding subunit; Provisional


Pssm-ID: 182906 [Multi-domain]  Cd Length: 326  Bit Score: 82.10  E-value: 1.69e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037402861   1 MAELSLSNIVKRFGG----FEIIHGANLEVKDGEFVVFVGPSGCGKSTLLRMIAGLED----ITSGELQIGGRVVNDVEP 72
Cdd:PRK11022    1 MALLNVDKLSVHFGDesapFRAVDRISYSVKQGEVVGIVGESGSGKSVSSLAIMGLIDypgrVMAEKLEFNGQDLQRISE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037402861  73 ADR------GIAMVFQS--YALYPHLTVEENLSFGLRMN--GNPKADTERRVShVAEILQITELMKR---RPKQLSGGQR 139
Cdd:PRK11022   81 KERrnlvgaEVAMIFQDpmTSLNPCYTVGFQIMEAIKVHqgGNKKTRRQRAID-LLNQVGIPDPASRldvYPHQLSGGMS 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037402861 140 QRVAIGRAIVREPEVFLFDEPLSNLDAELRVQMRVEISRLHKKLGTTMIYVTHDQTEAMTLADRIVVLRAGNIEQIGAPL 219
Cdd:PRK11022  160 QRVMIAMAIACRPKLLIADEPTTALDVTIQAQIIELLLELQQKENMALVLITHDLALVAEAAHKIIVMYAGQVVETGKAH 239


                  ....*.
gi 1037402861 220 DLYDDP 225
Cdd:PRK11022  240 DIFRAP 245
PRK09700 PRK09700
D-allose ABC transporter ATP-binding protein AlsA;
26-215 4.58e-17

D-allose ABC transporter ATP-binding protein AlsA;


Pssm-ID: 182036 [Multi-domain]  Cd Length: 510  Bit Score: 82.14  E-value: 4.58e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037402861  26 VKDGEFVVFVGPSGCGKSTLLRMIAGLEDITSGELQIGGRVVNDVEPAD---RGIAMVFQSY---ALYPHLTVEENLSFG 99
Cdd:PRK09700  286 VCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEIRLNGKDISPRSPLDavkKGMAYITESRrdnGFFPNFSIAQNMAIS 365

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037402861 100 --LRMNG--------NPKadTERRVSHVA-EILQIT-ELMKRRPKQLSGGQRQRVAIGRAIVREPEVFLFDEPLSNLDae 167
Cdd:PRK09700  366 rsLKDGGykgamglfHEV--DEQRTAENQrELLALKcHSVNQNITELSGGNQQKVLISKWLCCCPEVIIFDEPTRGID-- 441

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1037402861 168 lrVQMRVEISRLHKKL---GTTMIYVTHDQTEAMTLADRIVVLRAGNIEQI 215
Cdd:PRK09700  442 --VGAKAEIYKVMRQLaddGKVILMVSSELPEIITVCDRIAVFCEGRLTQI 490
nikD PRK10418
nickel transporter ATP-binding protein NikD; Provisional
 17-226 4.93e-17

nickel transporter ATP-binding protein NikD; Provisional


Pssm-ID: 236688 [Multi-domain]  Cd Length: 254  Bit Score: 79.74  E-value: 4.93e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037402861  17 EIIHGANLEVKDGEFVVFVGPSGCGKStlLRMIAGLEDITSGELQIGGRVVND---VEPAD---RGIAMVFQS--YALYP 88
Cdd:PRK10418   17 PLVHGVSLTLQRGRVLALVGGSGSGKS--LTCAAALGILPAGVRQTAGRVLLDgkpVAPCAlrgRKIATIMQNprSAFNP 94

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037402861  89 HLTVEENLSFGLRMNGnpKADTERRVSHVAEILQITE---LMKRRPKQLSGGQRQRVAIGRAIVREPEVFLFDEPLSNLD 165
Cdd:PRK10418   95 LHTMHTHARETCLALG--KPADDATLTAALEAVGLENaarVLKLYPFEMSGGMLQRMMIALALLCEAPFIIADEPTTDLD 172

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1037402861 166 aeLRVQMRV--EISRLHKKLGTTMIYVTHDQTEAMTLADRIVVLRAGNIEQIGAPLDLYDDPA 226
Cdd:PRK10418  173 --VVAQARIldLLESIVQKRALGMLLVTHDMGVVARLADDVAVMSHGRIVEQGDVETLFNAPK 233
oppD PRK09473
oligopeptide transporter ATP-binding component; Provisional
 23-240 5.94e-17

oligopeptide transporter ATP-binding component; Provisional


Pssm-ID: 181888 [Multi-domain]  Cd Length: 330  Bit Score: 80.54  E-value: 5.94e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037402861  23 NLEVKDGEFVVFVGPSGCGKSTLLRMIAGL---EDITSGELQIGGR-VVNDVEPA-----DRGIAMVFQS--YALYPHLT 91
Cdd:PRK09473   36 NFSLRAGETLGIVGESGSGKSQTAFALMGLlaaNGRIGGSATFNGReILNLPEKElnklrAEQISMIFQDpmTSLNPYMR 115

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037402861  92 VEENLSFGLRMN-GNPKADTERRVSHVAEILQITELMKRR---PKQLSGGQRQRVAIGRAIVREPEVFLFDEPLSNLDAE 167
Cdd:PRK09473  116 VGEQLMEVLMLHkGMSKAEAFEESVRMLDAVKMPEARKRMkmyPHEFSGGMRQRVMIAMALLCRPKLLIADEPTTALDVT 195

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1037402861 168 LRVQMRVEISRLHKKLGTTMIYVTHDQTEAMTLADRIVVLRAGNIEQIGAPLDLYDDPANQFVAGFVGS-PKMN 240
Cdd:PRK09473  196 VQAQIMTLLNELKREFNTAIIMITHDLGVVAGICDKVLVMYAGRTMEYGNARDVFYQPSHPYSIGLLNAvPRLD 269
MK0520 COG2401
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ...
 16-194 6.77e-17

ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];


Pssm-ID: 441957 [Multi-domain]  Cd Length: 222  Bit Score: 78.46  E-value: 6.77e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037402861  16 FEIIHGANLEVKDGEFVVFVGPSGCGKSTLLRMIAGLEDITSGELQIggrvvndvepadrgiamVFQSYALYPHLTVEEN 95
Cdd:COG2401    43 RYVLRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGALKGTPVAGCV-----------------DVPDNQFGREASLIDA 105

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037402861  96 LSfglrMNGNPKAdterrvshVAEILQITEL-----MKRRPKQLSGGQRQRVAIGRAIVREPEVFLFDEPLSNLDAELRV 170
Cdd:COG2401   106 IG----RKGDFKD--------AVELLNAVGLsdavlWLRRFKELSTGQKFRFRLALLLAERPKLLVIDEFCSHLDRQTAK 173

                         170       180
                  ....*....|....*....|....
gi 1037402861 171 QMRVEISRLHKKLGTTMIYVTHDQ 194
Cdd:COG2401   174 RVARNLQKLARRAGITLVVATHHY 197
PRK10790 PRK10790
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
18-214 7.84e-17

SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;


Pssm-ID: 182733 [Multi-domain]  Cd Length: 592  Bit Score: 81.69  E-value: 7.84e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037402861  18 IIHGANLEVKDGEFVVFVGPSGCGKSTLLRMIAGLEDITSGELQIGGRVVNDVEPA--DRGIAMVFQ-----SYALYPHL 90
Cdd:PRK10790  356 VLQNINLSVPSRGFVALVGHTGSGKSTLASLLMGYYPLTEGEIRLDGRPLSSLSHSvlRQGVAMVQQdpvvlADTFLANV 435

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037402861  91 TVEENLSfglrmngnpkadtERRVSHVAEILQITELMKRRPK-----------QLSGGQRQRVAIGRAIVREPEVFLFDE 159
Cdd:PRK10790  436 TLGRDIS-------------EEQVWQALETVQLAELARSLPDglytplgeqgnNLSVGQKQLLALARVLVQTPQILILDE 502

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1037402861 160 PLSNLDA--ELRVQMRVEISRLHkklgTTMIYVTHdQTEAMTLADRIVVLRAGN-IEQ 214
Cdd:PRK10790  503 ATANIDSgtEQAIQQALAAVREH----TTLVVIAH-RLSTIVEADTILVLHRGQaVEQ 555
PTZ00243 PTZ00243
ABC transporter; Provisional
 17-220 8.64e-17

ABC transporter; Provisional


Pssm-ID: 240327 [Multi-domain]  Cd Length: 1560  Bit Score: 82.13  E-value: 8.64e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037402861   17 EIIHGANLEVKDGEFVVFVGPSGCGKSTLLRMIAGLEDITSGELQiggrvvndvepADRGIAMVFQSyALYPHLTVEENL 96
Cdd:PTZ00243   674 VLLRDVSVSVPRGKLTVVLGATGSGKSTLLQSLLSQFEISEGRVW-----------AERSIAYVPQQ-AWIMNATVRGNI 741

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037402861   97 SFGLRMNGNPKADTERRVSHVAEILQI-----TELmKRRPKQLSGGQRQRVAIGRAIVREPEVFLFDEPLSNLDAEL--R 169
Cdd:PTZ00243   742 LFFDEEDAARLADAVRVSQLEADLAQLgggleTEI-GEKGVNLSGGQKARVSLARAVYANRDVYLLDDPLSALDAHVgeR 820

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|.
gi 1037402861  170 VQMRVEISRLHkklGTTMIYVTHdQTEAMTLADRIVVLRAGNIEQIGAPLD 220
Cdd:PTZ00243   821 VVEECFLGALA---GKTRVLATH-QVHVVPRADYVVALGDGRVEFSGSSAD 867
PRK10762 PRK10762
D-ribose transporter ATP binding protein; Provisional
 4-210 1.35e-16

D-ribose transporter ATP binding protein; Provisional


Pssm-ID: 236755 [Multi-domain]  Cd Length: 501  Bit Score: 80.82  E-value: 1.35e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037402861   4 LSLSNIVKRFGGFEIIHGANLEVKDGEFVVFVGPSGCGKSTLLRMIAGLEDITSGELQIGGRVVNDVEPADR---GIAMV 80
Cdd:PRK10762    5 LQLKGIDKAFPGVKALSGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSILYLGKEVTFNGPKSSqeaGIGII 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037402861  81 FQSYALYPHLTVEENL--------SFGL----RMNGNPKADTERrvshvaeiLQITELMKRRPKQLSGGQRQRVAIGRAI 148
Cdd:PRK10762   85 HQELNLIPQLTIAENIflgrefvnRFGRidwkKMYAEADKLLAR--------LNLRFSSDKLVGELSIGEQQMVEIAKVL 156

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1037402861 149 VREPEVFLFDEPLSNL-DAELRVQMRVeISRLhKKLGTTMIYVTHDQTEAMTLADRIVVLRAG 210
Cdd:PRK10762  157 SFESKVIIMDEPTDALtDTETESLFRV-IREL-KSQGRGIVYISHRLKEIFEICDDVTVFRDG 217
PLN03211 PLN03211
ABC transporter G-25; Provisional
 18-210 1.96e-16

ABC transporter G-25; Provisional


Pssm-ID: 215634 [Multi-domain]  Cd Length: 659  Bit Score: 80.69  E-value: 1.96e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037402861  18 IIHGANLEVKDGEFVVFVGPSGCGKSTLLRMIAGLediTSGELQIGGRVVNDVEPAD---RGIAMVFQSYALYPHLTVEE 94
Cdd:PLN03211   83 ILNGVTGMASPGEILAVLGPSGSGKSTLLNALAGR---IQGNNFTGTILANNRKPTKqilKRTGFVTQDDILYPHLTVRE 159

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037402861  95 NLSFG--LRMngnPKADTERRVSHVAEILqITELMKRRPKQ----------LSGGQRQRVAIGRAIVREPEVFLFDEPLS 162
Cdd:PLN03211  160 TLVFCslLRL---PKSLTKQEKILVAESV-ISELGLTKCENtiignsfirgISGGERKRVSIAHEMLINPSLLILDEPTS 235

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 1037402861 163 NLDAELRVQMRVEISRLHKKlGTTMIYVTHD-QTEAMTLADRIVVLRAG 210
Cdd:PLN03211  236 GLDATAAYRLVLTLGSLAQK-GKTIVTSMHQpSSRVYQMFDSVLVLSEG 283
PRK10762 PRK10762
D-ribose transporter ATP binding protein; Provisional
 19-212 2.05e-16

D-ribose transporter ATP binding protein; Provisional


Pssm-ID: 236755 [Multi-domain]  Cd Length: 501  Bit Score: 80.05  E-value: 2.05e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037402861  19 IHGANLEVKDGEFVVFVGPSGCGKSTLLRMIAGLEDITSGELQIGGRVVNDVEPAD---RGIAMVFQSY---ALYPHLTV 92
Cdd:PRK10762  268 VNDVSFTLRKGEILGVSGLMGAGRTELMKVLYGALPRTSGYVTLDGHEVVTRSPQDglaNGIVYISEDRkrdGLVLGMSV 347

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037402861  93 EENLSF-GLR----MNGNPKADTERR-VSHVAEILQI-TELMKRRPKQLSGGQRQRVAIGRAIVREPEVFLFDEPLSNLD 165
Cdd:PRK10762  348 KENMSLtALRyfsrAGGSLKHADEQQaVSDFIRLFNIkTPSMEQAIGLLSGGNQQKVAIARGLMTRPKVLILDEPTRGVD 427

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 1037402861 166 aelrVQMRVEISRL---HKKLGTTMIYVTHDQTEAMTLADRIVVLRAGNI 212
Cdd:PRK10762  428 ----VGAKKEIYQLinqFKAEGLSIILVSSEMPEVLGMSDRILVMHEGRI 473
PRK10982 PRK10982
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
 6-250 2.83e-16

galactose/methyl galaxtoside transporter ATP-binding protein; Provisional


Pssm-ID: 182880 [Multi-domain]  Cd Length: 491  Bit Score: 79.77  E-value: 2.83e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037402861   6 LSNIVKRFGGFEIIHGANLEVKDGEFVVFVGPSGCGKSTLLRMIAGLEDITSGELQIGGRVVN---DVEPADRGIAMVFQ 82
Cdd:PRK10982    1 MSNISKSFPGVKALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEIDfksSKEALENGISMVHQ 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037402861  83 SYALYPHLTVEENLSFGLRMNGNPKADTERRVSHVAEI---LQITELMKRRPKQLSGGQRQRVAIGRAIVREPEVFLFDE 159
Cdd:PRK10982   81 ELNLVLQRSVMDNMWLGRYPTKGMFVDQDKMYRDTKAIfdeLDIDIDPRAKVATLSVSQMQMIEIAKAFSYNAKIVIMDE 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037402861 160 PLSNLdAELRVQMRVEISRLHKKLGTTMIYVTHDQTEAMTLADRIVVLRAGnieQIGAPLDLYDDPANQFVAGFVGS--- 236
Cdd:PRK10982  161 PTSSL-TEKEVNHLFTIIRKLKERGCGIVYISHKMEEIFQLCDEITILRDG---QWIATQPLAGLTMDKIIAMMVGRslt 236

                         250
                  ....*....|....*...
gi 1037402861 237 ----PKMNFLKAVVVEAQ 250
Cdd:PRK10982  237 qrfpDKENKPGEVILEVR 254
ycf16 CHL00131
sulfate ABC transporter protein; Validated
 4-216 3.04e-16

sulfate ABC transporter protein; Validated


Pssm-ID: 214372 [Multi-domain]  Cd Length: 252  Bit Score: 77.37  E-value: 3.04e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037402861   4 LSLSNIVKRFGGFEIIHGANLEVKDGEFVVFVGPSGCGKSTLLRMIAGLE--DITSGELQIGGRVVNDVEPADR---GIA 78
Cdd:CHL00131    8 LEIKNLHASVNENEILKGLNLSINKGEIHAIMGPNGSGKSTLSKVIAGHPayKILEGDILFKGESILDLEPEERahlGIF 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037402861  79 MVFQsyalYPhltVE----ENLSFgLRM--------NGNPKADTERRVSHVAEILQITELmkrRPKQL--------SGGQ 138
Cdd:CHL00131   88 LAFQ----YP---IEipgvSNADF-LRLaynskrkfQGLPELDPLEFLEIINEKLKLVGM---DPSFLsrnvnegfSGGE 156

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037402861 139 RQRVAIGRAIVREPEVFLFDEPLSNLDAELRVQMRVEISRLhKKLGTTMIYVTHDQteamTLADRIV-----VLRAGNIE 213
Cdd:CHL00131  157 KKRNEILQMALLDSELAILDETDSGLDIDALKIIAEGINKL-MTSENSIILITHYQ----RLLDYIKpdyvhVMQNGKII 231


                  ...
gi 1037402861 214 QIG 216
Cdd:CHL00131  232 KTG 234
ABCC_MRP_domain2 cd03244
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ...
 18-218 6.88e-16

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: 75.61  E-value: 6.88e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037402861  18 IIHGANLEVKDGEFVVFVGPSGCGKST----LLRMIagleDITSGELQIGGRVVNDVEPAD--RGIAMVFQSyalyPHL- 90
Cdd:cd03244    19 VLKNISFSIKPGEKVGIVGRTGSGKSSlllaLFRLV----ELSSGSILIDGVDISKIGLHDlrSRISIIPQD----PVLf 90

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037402861  91 --TVEENL-SFGLRmngnpkadTERRVSHVAEILQITELMKRRPKQL-----------SGGQRQRVAIGRAIVREPEVFL 156
Cdd:cd03244    91 sgTIRSNLdPFGEY--------SDEELWQALERVGLKEFVESLPGGLdtvveeggenlSVGQRQLLCLARALLRKSKILV 162

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1037402861 157 FDEPLSNLDAELRVQMRvEISRLHKKlGTTMIYVTHdQTEAMTLADRIVVLRAGNIEQIGAP 218
Cdd:cd03244   163 LDEATASVDPETDALIQ-KTIREAFK-DCTVLTIAH-RLDTIIDSDRILVLDKGRVVEFDSP 221
NupO COG3845
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ...
 4-212 1.27e-15

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


Pssm-ID: 443055 [Multi-domain]  Cd Length: 504  Bit Score: 77.76  E-value: 1.27e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037402861   4 LSLSNI-VKRFGGFEIIHGANLEVKDGEFVVFVGPSGCGKSTLLRMIAGLEDITSGELQIGGRVVNDVEPADR---GIAM 79
Cdd:COG3845   258 LEVENLsVRDDRGVPALKDVSLEVRAGEILGIAGVAGNGQSELAEALAGLRPPASGSIRLDGEDITGLSPRERrrlGVAY 337

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037402861  80 V---FQSYALYPHLTVEENLSFGL----RMNGNPKADTERRVSHVAEilqiteLMKR---RP-------KQLSGGQRQRV 142
Cdd:COG3845   338 IpedRLGRGLVPDMSVAENLILGRyrrpPFSRGGFLDRKAIRAFAEE------LIEEfdvRTpgpdtpaRSLSGGNQQKV 411

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1037402861 143 AIGRAIVREPEVFLFDEPLSNLD--AelrvqmrveISRLHKKL------GTTMIYVTHDQTEAMTLADRIVVLRAGNI 212
Cdd:COG3845   412 ILARELSRDPKLLIAAQPTRGLDvgA---------IEFIHQRLlelrdaGAAVLLISEDLDEILALSDRIAVMYEGRI 480
PRK15056 PRK15056
manganese/iron ABC transporter ATP-binding protein;
15-208 1.96e-15

manganese/iron ABC transporter ATP-binding protein;


Pssm-ID: 185016 [Multi-domain]  Cd Length: 272  Bit Score: 75.30  E-value: 1.96e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037402861  15 GFEIIHGANLEVKDGEFVVFVGPSGCGKSTLLRMIAGLEDITSGELQIGGRVVNDVEPADRgIAMVFQSYAL---YPHLt 91
Cdd:PRK15056   19 GHTALRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKISILGQPTRQALQKNL-VAYVPQSEEVdwsFPVL- 96

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037402861  92 VEENLSFG----LRMNGNPKADTERRVSHVAEILQITELMKRRPKQLSGGQRQRVAIGRAIVREPEVFLFDEPLSNLDae 167
Cdd:PRK15056   97 VEDVVMMGryghMGWLRRAKKRDRQIVTAALARVDMVEFRHRQIGELSGGQKKRVFLARAIAQQGQVILLDEPFTGVD-- 174

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 1037402861 168 lrVQMRVEISRLHKKL---GTTMIYVTHDQTEAMTLADRIVVLR 208
Cdd:PRK15056  175 --VKTEARIISLLRELrdeGKTMLVSTHNLGSVTEFCDYTVMVK 216
znuC PRK09544
high-affinity zinc transporter ATPase; Reviewed
 4-207 3.00e-15

high-affinity zinc transporter ATPase; Reviewed


Pssm-ID: 181939 [Multi-domain]  Cd Length: 251  Bit Score: 74.38  E-value: 3.00e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037402861   4 LSLSNIVKRFGGFEIIHGANLEVKDGEFVVFVGPSGCGKSTLLRMIAGLEDITSGELQiggrvvndvEPADRGIAMVFQS 83
Cdd:PRK09544    5 VSLENVSVSFGQRRVLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIK---------RNGKLRIGYVPQK 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037402861  84 YALYPH--LTVEEnlsFGLRMNGNPKADTERRVSHVaeilQITELMKRRPKQLSGGQRQRVAIGRAIVREPEVFLFDEPL 161
Cdd:PRK09544   76 LYLDTTlpLTVNR---FLRLRPGTKKEDILPALKRV----QAGHLIDAPMQKLSGGETQRVLLARALLNRPQLLVLDEPT 148

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 1037402861 162 SNLDAELRVQMRVEISRLHKKLGTTMIYVTHDQTEAMTLADRIVVL 207
Cdd:PRK09544  149 QGVDVNGQVALYDLIDQLRRELDCAVLMVSHDLHLVMAKTDEVLCL 194
PLN03130 PLN03130
ABC transporter C family member; Provisional
 5-216 3.92e-15

ABC transporter C family member; Provisional


Pssm-ID: 215595 [Multi-domain]  Cd Length: 1622  Bit Score: 77.09  E-value: 3.92e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037402861    5 SLSNIvkrfggfeiihgaNLEVKDGEFVVFVGPSGCGKSTLLR-MIAGLEDITSGELQIGGRVvndvepadrgiAMVFQS 83
Cdd:PLN03130   632 TLSNI-------------NLDVPVGSLVAIVGSTGEGKTSLISaMLGELPPRSDASVVIRGTV-----------AYVPQV 687

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037402861   84 YALYpHLTVEENLSFGLRMNgnpkADTERRVSHVAEILQITELMK--------RRPKQLSGGQRQRVAIGRAIVREPEVF 155
Cdd:PLN03130   688 SWIF-NATVRDNILFGSPFD----PERYERAIDVTALQHDLDLLPggdlteigERGVNISGGQKQRVSMARAVYSNSDVY 762

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1037402861  156 LFDEPLSNLDAElrVQMRVEISRLHKKL-GTTMIYVThDQTEAMTLADRIVVLRAGNIEQIG 216
Cdd:PLN03130   763 IFDDPLSALDAH--VGRQVFDKCIKDELrGKTRVLVT-NQLHFLSQVDRIILVHEGMIKEEG 821
cyc_pep_trnsptr TIGR01194
cyclic peptide transporter; This model describes cyclic peptide transporter in bacteria. ...
 23-212 3.97e-15

cyclic peptide transporter; This model describes cyclic peptide transporter in bacteria. Bacteria have elaborate pathways for the production of toxins and secondary metabolites. Many such compounds, including syringomycin and pyoverdine are synthesized on non-ribosomal templates consisting of a multienzyme complex. On several occasions the proteins of the complex and transporter protein are present on the same operon. Often times these compounds cross the biological membrane by specific transporters. Syringomycin is an amphipathic, cylclic lipodepsipeptide when inserted into host causes formation of channels, permeable to variety of cations. On the other hand, pyoverdine is a cyclic octa-peptidyl dihydroxyquinoline, which is efficient in sequestering iron for uptake. [Transport and binding proteins, Amino acids, peptides and amines, Transport and binding proteins, Other]


Pssm-ID: 130262 [Multi-domain]  Cd Length: 555  Bit Score: 76.53  E-value: 3.97e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037402861  23 NLEVKDGEFVVFVGPSGCGKSTLLRMIAGLEDITSGELQIGGRVVNDVEPAD--RGIAMVFQSYALYPHLTveenlsfGL 100
Cdd:TIGR01194 362 DLRIAQGDIVFIVGENGCGKSTLAKLFCGLYIPQEGEILLDGAAVSADSRDDyrDLFSAIFADFHLFDDLI-------GP 434

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037402861 101 RMNGNPKADTERRVSHVAEI---LQITELMKRRPKQLSGGQRQRVAIGRAIVREPEVFLFDEPLSNLDAELRVQMRVEIS 177
Cdd:TIGR01194 435 DEGEHASLDNAQQYLQRLEIadkVKIEDGGFSTTTALSTGQQKRLALICAWLEDRPILLFDEWAADQDPAFKRFFYEELL 514

                         170       180       190
                  ....*....|....*....|....*....|....*
gi 1037402861 178 RLHKKLGTTMIYVTHDQtEAMTLADRIVVLRAGNI 212
Cdd:TIGR01194 515 PDLKRQGKTIIIISHDD-QYFELADQIIKLAAGCI 548
Rli1 COG1245
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ...
 3-207 4.50e-15

Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ribosomal structure and biogenesis];


Pssm-ID: 440858 [Multi-domain]  Cd Length: 592  Bit Score: 76.36  E-value: 4.50e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037402861   3 ELSlSNIVKRFG--GFEIIhgaNLEV-KDGEFVVFVGPSGCGKSTLLRMIAG---------------------------- 51
Cdd:COG1245    74 ELE-EDPVHRYGenGFRLY---GLPVpKKGKVTGILGPNGIGKSTALKILSGelkpnlgdydeepswdevlkrfrgtelq 149

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037402861  52 --LEDITSGELqiggRVVNDVEPADRgIAMVFQSyalyphlTVEENLSfglrmngnpKADTERRVSHVAEILQITELMKR 129
Cdd:COG1245   150 dyFKKLANGEI----KVAHKPQYVDL-IPKVFKG-------TVRELLE---------KVDERGKLDELAEKLGLENILDR 208

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037402861 130 RPKQLSGGQRQRVAIGRAIVREPEVFLFDEPLSNLDaelrVQMRVEISRLHKKL---GTTMIYVTHDQTEAMTLADRIVV 206
Cdd:COG1245   209 DISELSGGELQRVAIAAALLRDADFYFFDEPSSYLD----IYQRLNVARLIRELaeeGKYVLVVEHDLAILDYLADYVHI 284


                  .
gi 1037402861 207 L 207
Cdd:COG1245   285 L 285
ABC_RNaseL_inhibitor cd03222
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ...
 9-207 5.41e-15

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: 72.22  E-value: 5.41e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037402861   9 IVKRFGGFEIIHGANlEVKDGEFVVFVGPSGCGKSTLLRMIAGLEDITSGELQIGGrvvndvepadrgiamvfqsyalyp 88
Cdd:cd03222     6 CVKRYGVFFLLVELG-VVKEGEVIGIVGPNGTGKTTAVKILAGQLIPNGDNDEWDG------------------------ 60

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037402861  89 hltveenlsfglrmngnpkadterrvshvaeilqITELMKRRPKQLSGGQRQRVAIGRAIVREPEVFLFDEPLSNLDAEL 168
Cdd:cd03222    61 ----------------------------------ITPVYKPQYIDLSGGELQRVAIAAALLRNATFYLFDEPSAYLDIEQ 106

                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 1037402861 169 RVQMRVEISRLHKKLGTTMIYVTHDQTEAMTLADRIVVL 207
Cdd:cd03222   107 RLNAARAIRRLSEEGKKTALVVEHDLAVLDYLSDRIHVF 145
PRK13543 PRK13543
heme ABC exporter ATP-binding protein CcmA;
23-167 7.64e-15

heme ABC exporter ATP-binding protein CcmA;


Pssm-ID: 184129 [Multi-domain]  Cd Length: 214  Bit Score: 72.57  E-value: 7.64e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037402861  23 NLEVKDGEFVVFVGPSGCGKSTLLRMIAGLEDITSGELQIGGRVVNDVEPAdRGIAMVFQSYALYPHLTVEENLSFglrM 102
Cdd:PRK13543   31 DFHVDAGEALLVQGDNGAGKTTLLRVLAGLLHVESGQIQIDGKTATRGDRS-RFMAYLGHLPGLKADLSTLENLHF---L 106

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1037402861 103 NGNPKADTERRVSHVAEILQITELMKRRPKQLSGGQRQRVAIGRAIVREPEVFLFDEPLSNLDAE 167
Cdd:PRK13543  107 CGLHGRRAKQMPGSALAIVGLAGYEDTLVRQLSAGQKKRLALARLWLSPAPLWLLDEPYANLDLE 171
PRK13409 PRK13409
ribosome biogenesis/translation initiation ATPase RLI;
26-207 8.42e-15

ribosome biogenesis/translation initiation ATPase RLI;


Pssm-ID: 184037 [Multi-domain]  Cd Length: 590  Bit Score: 75.62  E-value: 8.42e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037402861  26 VKDGEFVVFVGPSGCGKSTLLRMIAG------------------------------LEDITSGELqiggRVVNDVEPADR 75
Cdd:PRK13409   96 PKEGKVTGILGPNGIGKTTAVKILSGelipnlgdyeeepswdevlkrfrgtelqnyFKKLYNGEI----KVVHKPQYVDL 171

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037402861  76 gIAMVFQSyalyphlTVEENLSfglrmngnpKADTERRVSHVAEILQITELMKRRPKQLSGGQRQRVAIGRAIVREPEVF 155
Cdd:PRK13409  172 -IPKVFKG-------KVRELLK---------KVDERGKLDEVVERLGLENILDRDISELSGGELQRVAIAAALLRDADFY 234

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1037402861 156 LFDEPLSNLDaelrVQMRVEISRLHKKL--GTTMIYVTHDQTEAMTLADRIVVL 207
Cdd:PRK13409  235 FFDEPTSYLD----IRQRLNVARLIRELaeGKYVLVVEHDLAVLDYLADNVHIA 284
ABC_RNaseL_inhibitor_domain1 cd03236
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ...
 26-207 8.65e-15

The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI), is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI s are not transport proteins and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLIs have an N-terminal Fe-S domain and two nucleotide binding domains which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.


Pssm-ID: 213203 [Multi-domain]  Cd Length: 255  Bit Score: 73.17  E-value: 8.65e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037402861  26 VKDGEFVVFVGPSGCGKSTLLRMIAG------------------LEDITSGELQIG-GRVVNDvepaDRGIAMVFQSYAL 86
Cdd:cd03236    23 PREGQVLGLVGPNGIGKSTALKILAGklkpnlgkfddppdwdeiLDEFRGSELQNYfTKLLEG----DVKVIVKPQYVDL 98

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037402861  87 YPHL---TVEENLSfglrmngnpKADTERRVSHVAEILQITELMKRRPKQLSGGQRQRVAIGRAIVREPEVFLFDEPLSN 163
Cdd:cd03236    99 IPKAvkgKVGELLK---------KKDERGKLDELVDQLELRHVLDRNIDQLSGGELQRVAIAAALARDADFYFFDEPSSY 169

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 1037402861 164 LDAELRVQMRVEISRLHKKlGTTMIYVTHDQTEAMTLADRIVVL 207
Cdd:cd03236   170 LDIKQRLNAARLIRELAED-DNYVLVVEHDLAVLDYLSDYIHCL 212
ABCC_NFT1 cd03369
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ...
 3-218 9.14e-15

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: 72.44  E-value: 9.14e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037402861   3 ELSLSNIVKRFGGF--EIIHGANLEVKDGEFVVFVGPSGCGKSTLLRMIAGLEDITSGELQIGGRVVNDVEPAD--RGIA 78
Cdd:cd03369     6 EIEVENLSVRYAPDlpPVLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDGIDISTIPLEDlrSSLT 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037402861  79 MVFQSYALYPHlTVEENLsfglrmngnpkaDTERRVS--HVAEILQITElmkrRPKQLSGGQRQRVAIGRAIVREPEVFL 156
Cdd:cd03369    86 IIPQDPTLFSG-TIRSNL------------DPFDEYSdeEIYGALRVSE----GGLNLSQGQRQLLCLARALLKRPRVLV 148

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1037402861 157 FDEPLSNL----DAELRVQMRVEISrlhkklGTTMIYVTHdQTEAMTLADRIVVLRAGNIEQIGAP 218
Cdd:cd03369   149 LDEATASIdyatDALIQKTIREEFT------NSTILTIAH-RLRTIIDYDKILVMDAGEVKEYDHP 207
ABCC_SUR1_N cd03290
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ...
 23-210 1.34e-14

ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The sulfonylurea receptor SUR is an ATP transporter of the ABCC/MRP family with tandem ATPase binding domains. Unlike other ABC proteins, it has no intrinsic transport function, neither active nor passive, but associates with the potassium channel proteins Kir6.1 or Kir6.2 to form the ATP-sensitive potassium (K(ATP)) channel. Within the channel complex, SUR serves as a regulatory subunit that fine-tunes the gating of Kir6.x in response to alterations in cellular metabolism. It constitutes a major pharmaceutical target as it binds numerous drugs, K(ATP) channel openers and blockers, capable of up- or down-regulating channel activity.


Pssm-ID: 213257 [Multi-domain]  Cd Length: 218  Bit Score: 71.98  E-value: 1.34e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037402861  23 NLEVKDGEFVVFVGPSGCGKSTLLRMIAGLEDITSGELQIGGRVVNDVEPADRG------IAMVFQSYALYpHLTVEENL 96
Cdd:cd03290    21 NIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWSNKNESEPSFEATRsrnrysVAYAAQKPWLL-NATVEENI 99

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037402861  97 SFGLRMNgnpkadtERRVSHVAEILQI------------TELmKRRPKQLSGGQRQRVAIGRAIVREPEVFLFDEPLSNL 164
Cdd:cd03290   100 TFGSPFN-------KQRYKAVTDACSLqpdidllpfgdqTEI-GERGINLSGGQRQRICVARALYQNTNIVFLDDPFSAL 171

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 1037402861 165 DAELRVQ-MRVEISRLHKKLGTTMIYVTHdQTEAMTLADRIVVLRAG 210
Cdd:cd03290   172 DIHLSDHlMQEGILKFLQDDKRTLVLVTH-KLQYLPHADWIIAMKDG 217
PRK11176 PRK11176
lipid A ABC transporter ATP-binding protein/permease MsbA;
23-221 2.05e-14

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


Pssm-ID: 183016 [Multi-domain]  Cd Length: 582  Bit Score: 74.28  E-value: 2.05e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037402861  23 NLEVKDGEFVVFVGPSGCGKSTLLRMIAGLEDITSGELQIGGRVVNDVEPAD--RGIAMVFQSYALYpHLTVEENLSFGl 100
Cdd:PRK11176  363 NFKIPAGKTVALVGRSGSGKSTIANLLTRFYDIDEGEILLDGHDLRDYTLASlrNQVALVSQNVHLF-NDTIANNIAYA- 440

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037402861 101 RMNGNPKADTER--RVSHVAEILQITE-----LMKRRPKQLSGGQRQRVAIGRAIVREPEVFLFDEPLSNLDAELRVQMR 173
Cdd:PRK11176  441 RTEQYSREQIEEaaRMAYAMDFINKMDngldtVIGENGVLLSGGQRQRIAIARALLRDSPILILDEATSALDTESERAIQ 520

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 1037402861 174 VEISRLHKKlgTTMIYVTHdQTEAMTLADRIVVLRAGNIEQIGAPLDL 221
Cdd:PRK11176  521 AALDELQKN--RTSLVIAH-RLSTIEKADEILVVEDGEIVERGTHAEL 565
ABCC_CFTR1 cd03291
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ...
 23-210 3.18e-14

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: 72.20  E-value: 3.18e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037402861  23 NLEVKDGEFVVFVGPSGCGKSTLLRMIAGLEDITSGELQIGGRvvndvepadrgIAMVFQSYALYPHlTVEENLSFGLRM 102
Cdd:cd03291    57 NLKIEKGEMLAITGSTGSGKTSLLMLILGELEPSEGKIKHSGR-----------ISFSSQFSWIMPG-TIKENIIFGVSY 124

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037402861 103 NgnpkadtERRVSHVAEILQITELMKRRPKQ-----------LSGGQRQRVAIGRAIVREPEVFLFDEPLSNLDaeLRVQ 171
Cdd:cd03291   125 D-------EYRYKSVVKACQLEEDITKFPEKdntvlgeggitLSGGQRARISLARAVYKDADLYLLDSPFGYLD--VFTE 195

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 1037402861 172 MRVEISRLHKKLGT-TMIYVThDQTEAMTLADRIVVLRAG 210
Cdd:cd03291   196 KEIFESCVCKLMANkTRILVT-SKMEHLKKADKILILHEG 234
ABC_ABC_ChvD TIGR03719
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ...
 8-169 4.47e-14

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: 73.05  E-value: 4.47e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037402861   8 NIVKRFGGFEIIHGANLEVKDGEFVVFVGPSGCGKSTLLRMIAGLEDITSGELQIGGRVVndvepadrgIAMVFQSY-AL 86
Cdd:TIGR03719 327 NLTKAFGDKLLIDDLSFKLPPGGIVGVIGPNGAGKSTLFRMITGQEQPDSGTIEIGETVK---------LAYVDQSRdAL 397

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037402861  87 YPHLTVEENLSFGL--------RMNG-------NPK-ADTERRVshvaeilqitelmkrrpKQLSGGQRQRVAIGRAIVR 150
Cdd:TIGR03719 398 DPNKTVWEEISGGLdiiklgkrEIPSrayvgrfNFKgSDQQKKV-----------------GQLSGGERNRVHLAKTLKS 460

                         170       180
                  ....*....|....*....|
gi 1037402861 151 EPEVFLFDEPLSNLDAE-LR 169
Cdd:TIGR03719 461 GGNVLLLDEPTNDLDVEtLR 480
PRK13540 PRK13540
cytochrome c biogenesis protein CcmA; Provisional
 36-192 1.36e-13

cytochrome c biogenesis protein CcmA; Provisional


Pssm-ID: 184127 [Multi-domain]  Cd Length: 200  Bit Score: 68.82  E-value: 1.36e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037402861  36 GPSGCGKSTLLRMIAGLEDITSGELQIGGRVVN-DVEPADRGIAMVFQSYALYPHLTVEENLSFGLRMngnpkADTERRV 114
Cdd:PRK13540   34 GSNGAGKTTLLKLIAGLLNPEKGEILFERQSIKkDLCTYQKQLCFVGHRSGINPYLTLRENCLYDIHF-----SPGAVGI 108

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1037402861 115 SHVAEILQITELMKRRPKQLSGGQRQRVAIGRAIVREPEVFLFDEPLSNLDaELRVQMRVEISRLHKKLGTTMIYVTH 192
Cdd:PRK13540  109 TELCRLFSLEHLIDYPCGLLSSGQKRQVALLRLWMSKAKLWLLDEPLVALD-ELSLLTIITKIQEHRAKGGAVLLTSH 185
PLN03232 PLN03232
ABC transporter C family member; Provisional
 23-222 1.97e-13

ABC transporter C family member; Provisional


Pssm-ID: 215640 [Multi-domain]  Cd Length: 1495  Bit Score: 71.93  E-value: 1.97e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037402861   23 NLEVKDGEFVVFVGPSGCGKSTLLRMIAGleditsgelqiggrvvnDVEPADRGIAMVFQSYALYPHL------TVEENL 96
Cdd:PLN03232   637 NLEIPVGSLVAIVGGTGEGKTSLISAMLG-----------------ELSHAETSSVVIRGSVAYVPQVswifnaTVRENI 699

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037402861   97 SFGLRMNGNP--KADTERRVSHVAEIL---QITELmKRRPKQLSGGQRQRVAIGRAIVREPEVFLFDEPLSNLDAELRVQ 171
Cdd:PLN03232   700 LFGSDFESERywRAIDVTALQHDLDLLpgrDLTEI-GERGVNISGGQKQRVSMARAVYSNSDIYIFDDPLSALDAHVAHQ 778

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|.
gi 1037402861  172 MRVEISRlHKKLGTTMIYVThDQTEAMTLADRIVVLRAGNIEQIGAPLDLY 222
Cdd:PLN03232   779 VFDSCMK-DELKGKTRVLVT-NQLHFLPLMDRIILVSEGMIKEEGTFAELS 827
PRK10522 PRK10522
multidrug transporter membrane component/ATP-binding component; Provisional
 3-215 2.21e-13

multidrug transporter membrane component/ATP-binding component; Provisional


Pssm-ID: 236707 [Multi-domain]  Cd Length: 547  Bit Score: 71.16  E-value: 2.21e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037402861   3 ELSLSNIVKRFG--GFEIiHGANLEVKDGEFVVFVGPSGCGKSTLLRMIAGLEDITSGELQIGGRVVNDVEPAD--RGIA 78
Cdd:PRK10522  322 TLELRNVTFAYQdnGFSV-GPINLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKPVTAEQPEDyrKLFS 400

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037402861  79 MVFQSYALYPHLtveenlsfglrMNGNPKADTERRVSHVAEILQitelMKRRPK---------QLSGGQRQRVAIGRAIV 149
Cdd:PRK10522  401 AVFTDFHLFDQL-----------LGPEGKPANPALVEKWLERLK----MAHKLEledgrisnlKLSKGQKKRLALLLALA 465

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1037402861 150 REPEVFLFDEPLSNLDAELRVQMRVEISRLHKKLGTTMIYVTHDQtEAMTLADRIVVLRAGNIEQI 215
Cdd:PRK10522  466 EERDILLLDEWAADQDPHFRREFYQVLLPLLQEMGKTIFAISHDD-HYFIHADRLLEMRNGQLSEL 530
rim_protein TIGR01257
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ...
 26-242 3.72e-13

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: 70.81  E-value: 3.72e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037402861   26 VKDGEFVVFVGPSGCGKSTLLRMIAGLEDITSGELQIGGR-VVNDVEPADRGIAMVFQSYALYPHLTVEENLSFGLRMNG 104
Cdd:TIGR01257 1962 VRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAGKsILTNISDVHQNMGYCPQFDAIDDLLTGREHLYLYARLRG 2041

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037402861  105 NPKADTERRVSHVAEILQITELMKRRPKQLSGGQRQRVAIGRAIVREPEVFLFDEPLSNLDAELRVQMRVEISRLHKKlG 184
Cdd:TIGR01257 2042 VPAEEIEKVANWSIQSLGLSLYADRLAGTYSGGNKRKLSTAIALIGCPPLVLLDEPTTGMDPQARRMLWNTIVSIIRE-G 2120

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 1037402861  185 TTMIYVTHDQTEAMTLADRIVVLRAGNIEQIGAPLDLYDDPANQFVAGF-VGSPKMNFL 242
Cdd:TIGR01257 2121 RAVVLTSHSMEECEALCTRLAIMVKGAFQCLGTIQHLKSKFGDGYIVTMkIKSPKDDLL 2179
ABC2_perm_RbbA NF033858
ribosome-associated ATPase/putative transporter RbbA;
5-160 4.89e-13

ribosome-associated ATPase/putative transporter RbbA;


Pssm-ID: 468210 [Multi-domain]  Cd Length: 907  Bit Score: 70.15  E-value: 4.89e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037402861   5 SLSNIVKRFGGFEIIHGANLEVKDGEFVVFVGPSGCGKSTLLRMIAGLEDITSGELQI-GGrvvnDVepADRG------- 76
Cdd:NF033858    3 RLEGVSHRYGKTVALDDVSLDIPAGCMVGLIGPDGVGKSSLLSLIAGARKIQQGRVEVlGG----DM--ADARhrravcp 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037402861  77 -IAMVFQSYA--LYPHLTVEENLSFGLRMNGNPKADTERRvshVAEILQITEL--MKRRP-KQLSGGQRQRVAIGRAIVR 150
Cdd:NF033858   77 rIAYMPQGLGknLYPTLSVFENLDFFGRLFGQDAAERRRR---IDELLRATGLapFADRPaGKLSGGMKQKLGLCCALIH 153

                         170
                  ....*....|
gi 1037402861 151 EPEVFLFDEP 160
Cdd:NF033858  154 DPDLLILDEP 163
CFTR_protein TIGR01271
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ...
 23-210 5.39e-13

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: 70.32  E-value: 5.39e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037402861   23 NLEVKDGEFVVFVGPSGCGKSTLLRMIAGLEDITSGELQIGGRvvndvepadrgIAMVFQSYALYPHlTVEENLSFGLRM 102
Cdd:TIGR01271  446 SFKLEKGQLLAVAGSTGSGKSSLLMMIMGELEPSEGKIKHSGR-----------ISFSPQTSWIMPG-TIKDNIIFGLSY 513

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037402861  103 NgnpkadtERRVSHVAEILQITELMKRRPKQ-----------LSGGQRQRVAIGRAIVREPEVFLFDEPLSNLDaelrVQ 171
Cdd:TIGR01271  514 D-------EYRYTSVIKACQLEEDIALFPEKdktvlgeggitLSGGQRARISLARAVYKDADLYLLDSPFTHLD----VV 582

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|..
gi 1037402861  172 MRVEI--SRLHKKLGT-TMIYVThDQTEAMTLADRIVVLRAG 210
Cdd:TIGR01271  583 TEKEIfeSCLCKLMSNkTRILVT-SKLEHLKKADKILLLHEG 623
3a01205 TIGR00956
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
 26-210 6.17e-13

Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]


Pssm-ID: 273362 [Multi-domain]  Cd Length: 1394  Bit Score: 70.14  E-value: 6.17e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037402861   26 VKDGEFVVFVGPSGCGKSTLLRMIAGLED---ITSGELQIGGRVVNdvEPADRGIAMVFQSYALYPHLTVEENLSFGLRM 102
Cdd:TIGR00956  786 VKPGTLTALMGASGAGKTTLLNVLAERVTtgvITGGDRLVNGRPLD--SSFQRSIGYVQQQDLHLPTSTVRESLRFSAYL 863

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037402861  103 ---NGNPKADTERRVSHVAEILQITE----LMKRRPKQLSGGQRQRVAIGRAIVREPEVFLF-DEPLSNLDAelrvQMRV 174
Cdd:TIGR00956  864 rqpKSVSKSEKMEYVEEVIKLLEMESyadaVVGVPGEGLNVEQRKRLTIGVELVAKPKLLLFlDEPTSGLDS----QTAW 939

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|.
gi 1037402861  175 EISRLHKKL---GTTMIYVTHdQTEAMTLA--DRIVVLRAG 210
Cdd:TIGR00956  940 SICKLMRKLadhGQAILCTIH-QPSAILFEefDRLLLLQKG 979
SapD COG4170
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms];
23-215 7.13e-13

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


Pssm-ID: 443330 [Multi-domain]  Cd Length: 331  Bit Score: 68.78  E-value: 7.13e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037402861  23 NLEVKDGEFVVFVGPSGCGKSTLLRMIAGLED----ITSGELQIGGRVVNDVEPADR------GIAMVFQ--SYALYPHL 90
Cdd:COG4170    27 SLTLNEGEIRGLVGESGSGKSLIAKAICGITKdnwhVTADRFRWNGIDLLKLSPRERrkiigrEIAMIFQepSSCLDPSA 106

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037402861  91 TVEENL-------SFGLRMNGNPKADTERRVS--HVAEILQITELMKRRPKQLSGGQRQRVAIGRAIVREPEVFLFDEPL 161
Cdd:COG4170   107 KIGDQLieaipswTFKGKWWQRFKWRKKRAIEllHRVGIKDHKDIMNSYPHELTEGECQKVMIAMAIANQPRLLIADEPT 186

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037402861 162 SNLDAELRVQMRVEISRLHKKLGTTMIYVTHDQTEAMTLADRIVVL------RAGNIEQI 215
Cdd:COG4170   187 NAMESTTQAQIFRLLARLNQLQGTSILLISHDLESISQWADTITVLycgqtvESGPTEQI 246
GguA NF040905
sugar ABC transporter ATP-binding protein;
4-235 8.44e-13

sugar ABC transporter ATP-binding protein;


Pssm-ID: 468840 [Multi-domain]  Cd Length: 500  Bit Score: 69.05  E-value: 8.44e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037402861   4 LSLSNIVKRFGGFEIIHGANLEVKDGEFVVFVGPSGCGKSTLLRMIAGLEDITS--GELQIGGRVV-----NDVEpaDRG 76
Cdd:NF040905    2 LEMRGITKTFPGVKALDDVNLSVREGEIHALCGENGAGKSTLMKVLSGVYPHGSyeGEILFDGEVCrfkdiRDSE--ALG 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037402861  77 IAMVFQSYALYPHLTVEENLSFglrmnGNPKA--------DTERRVshvaeilqiTELMKR---------RPKQLSGGQR 139
Cdd:NF040905   80 IVIIHQELALIPYLSIAENIFL-----GNERAkrgvidwnETNRRA---------RELLAKvgldespdtLVTDIGVGKQ 145

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037402861 140 QRVAIGRAIVREPEVFLFDEP-----------LSNLDAELRVQmrveisrlhkklGTTMIYVTHDQTEAMTLADRIVVLR 208
Cdd:NF040905  146 QLVEIAKALSKDVKLLILDEPtaalneedsaaLLDLLLELKAQ------------GITSIIISHKLNEIRRVADSITVLR 213

                         250       260       270
                  ....*....|....*....|....*....|
gi 1037402861 209 AGN-IEQigapLDLYDDPANQ--FVAGFVG 235
Cdd:NF040905  214 DGRtIET----LDCRADEVTEdrIIRGMVG 239
PRK11147 PRK11147
ABC transporter ATPase component; Reviewed
 1-212 8.73e-13

ABC transporter ATPase component; Reviewed


Pssm-ID: 236861 [Multi-domain]  Cd Length: 635  Bit Score: 69.21  E-value: 8.73e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037402861   1 MAELSLSNIVKRFGGFEIIHGANLEVKDGEFVVFVGPSGCGKSTLLRMIAG---LEDitsGELQIGGRVV---------N 68
Cdd:PRK11147    1 MSLISIHGAWLSFSDAPLLDNAELHIEDNERVCLVGRNGAGKSTLMKILNGevlLDD---GRIIYEQDLIvarlqqdppR 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037402861  69 DVEPA-----DRGIAMVFQSYALYPHLT--VEENLSfglRMNGNPKADTERRVSHV------AEILQITELMKRRPKQ-- 133
Cdd:PRK11147   78 NVEGTvydfvAEGIEEQAEYLKRYHDIShlVETDPS---EKNLNELAKLQEQLDHHnlwqleNRINEVLAQLGLDPDAal 154

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037402861 134 --LSGGQRQRVAIGRAIVREPEVFLFDEPLSNLDAElrvqmrvEISRLHKKLGT---TMIYVTHDQTEAMTLADRIVVLR 208
Cdd:PRK11147  155 ssLSGGWLRKAALGRALVSNPDVLLLDEPTNHLDIE-------TIEWLEGFLKTfqgSIIFISHDRSFIRNMATRIVDLD 227


                  ....
gi 1037402861 209 AGNI 212
Cdd:PRK11147  228 RGKL 231
sufC PRK09580
cysteine desulfurase ATPase component; Reviewed
 4-165 1.35e-12

cysteine desulfurase ATPase component; Reviewed


Pssm-ID: 181965 [Multi-domain]  Cd Length: 248  Bit Score: 66.74  E-value: 1.35e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037402861   4 LSLSNIVKRFGGFEIIHGANLEVKDGEFVVFVGPSGCGKSTLLRMIAGLED--ITSGELQIGGRVVNDVEPADR---GIA 78
Cdd:PRK09580    2 LSIKDLHVSVEDKAILRGLNLEVRPGEVHAIMGPNGSGKSTLSATLAGREDyeVTGGTVEFKGKDLLELSPEDRageGIF 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037402861  79 MVFQsyalYP--------HLTVEENLSFGLRMNGNP---KADTERRVSHVAEILQITELMKRRPKQL--SGGQRQRVAIG 145
Cdd:PRK09580   82 MAFQ----YPveipgvsnQFFLQTALNAVRSYRGQEpldRFDFQDLMEEKIALLKMPEDLLTRSVNVgfSGGEKKRNDIL 157

                         170       180
                  ....*....|....*....|
gi 1037402861 146 RAIVREPEVFLFDEPLSNLD 165
Cdd:PRK09580  158 QMAVLEPELCILDESDSGLD 177
PRK10938 PRK10938
putative molybdenum transport ATP-binding protein ModF; Provisional
 1-207 1.39e-12

putative molybdenum transport ATP-binding protein ModF; Provisional


Pssm-ID: 182852 [Multi-domain]  Cd Length: 490  Bit Score: 68.50  E-value: 1.39e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037402861   1 MAELSLSNIVKRFGGFEIIHGANLEVKDGEFVVFVGPSGCGKSTLLRMIAGLEDITSGELQiggrvvNDvepadrgiamv 80
Cdd:PRK10938    1 MSSLQISQGTFRLSDTKTLQLPSLTLNAGDSWAFVGANGSGKSALARALAGELPLLSGERQ------SQ----------- 63

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037402861  81 FQSYALYP-----HLTVEENLSFGLRMNGNPKADTERRVSHV--------------AEILQITELMKRRPKQLSGGQRQR 141
Cdd:PRK10938   64 FSHITRLSfeqlqKLVSDEWQRNNTDMLSPGEDDTGRTTAEIiqdevkdparceqlAQQFGITALLDRRFKYLSTGETRK 143

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1037402861 142 VAIGRAIVREPEVFLFDEPLSNLDAELRVQMRVEISRLHKKlGTTMIYVTHDQTEAMTLADRIVVL 207
Cdd:PRK10938  144 TLLCQALMSEPDLLILDEPFDGLDVASRQQLAELLASLHQS-GITLVLVLNRFDEIPDFVQFAGVL 208
PTZ00265 PTZ00265
multidrug resistance protein (mdr1); Provisional
 57-214 1.80e-12

multidrug resistance protein (mdr1); Provisional


Pssm-ID: 240339 [Multi-domain]  Cd Length: 1466  Bit Score: 68.90  E-value: 1.80e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037402861   57 SGELQIGGRVVNDVEPAD-RGIAMVFQSYALYPHLTVEENLSFGlrmngnpKADTERR-VSHVAEILQITELMKRRP--- 131
Cdd:PTZ00265  1276 SGKILLDGVDICDYNLKDlRNLFSIVSQEPMLFNMSIYENIKFG-------KEDATREdVKRACKFAAIDEFIESLPnky 1348

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037402861  132 --------KQLSGGQRQRVAIGRAIVREPEVFLFDEPLSNLDAELRVQMRVEISRLHKKLGTTMIYVTHdQTEAMTLADR 203
Cdd:PTZ00265  1349 dtnvgpygKSLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDIKDKADKTIITIAH-RIASIKRSDK 1427

                          170
                   ....*....|....*
gi 1037402861  204 IVVL----RAGNIEQ 214
Cdd:PTZ00265  1428 IVVFnnpdRTGSFVQ 1442
ABCG_PDR_domain2 cd03232
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ...
 17-210 9.03e-12

Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding cassette transporters; The pleiotropic drug resistance (PDR) is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. This PDR subfamily represents domain I of its (ABC-IM)2 organization. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds including sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.


Pssm-ID: 213199 [Multi-domain]  Cd Length: 192  Bit Score: 63.42  E-value: 9.03e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037402861  17 EIIHGANLEVKDGEFVVFVGPSGCGKSTLLRMIAGLED--ITSGELQIGGRVVNDVEPadRGIAMVFQSYALYPHLTVEE 94
Cdd:cd03232    21 QLLNNISGYVKPGTLTALMGESGAGKTTLLDVLAGRKTagVITGEILINGRPLDKNFQ--RSTGYVEQQDVHSPNLTVRE 98

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037402861  95 NLSFGLRMNGnpkadterrvshvaeilqitelmkrrpkqLSGGQRQRVAIGRAIVREPEVFLFDEPLSNLDAelrvQMRV 174
Cdd:cd03232    99 ALRFSALLRG-----------------------------LSVEQRKRLTIGVELAAKPSILFLDEPTSGLDS----QAAY 145

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 1037402861 175 EISRLHKKL---GTTMIYVTHdQTEAMTLA--DRIVVLRAG 210
Cdd:cd03232   146 NIVRFLKKLadsGQAILCTIH-QPSASIFEkfDRLLLLKRG 185
PTZ00265 PTZ00265
multidrug resistance protein (mdr1); Provisional
 17-207 9.85e-12

multidrug resistance protein (mdr1); Provisional


Pssm-ID: 240339 [Multi-domain]  Cd Length: 1466  Bit Score: 66.59  E-value: 9.85e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037402861   17 EIIHGANLEVKDGEFVVFVGPSGCGKSTLLRMIAGLEDITSGELqiggrVVNDVEPAD--------RGIAMVFQ------ 82
Cdd:PTZ00265   399 EIYKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDI-----IINDSHNLKdinlkwwrSKIGVVSQdpllfs 473

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037402861   83 -------SYALYPhLTVEENLSFGLRMNGNP-----------KADTERRVSHVAEILQITELMKRRPK------------ 132
Cdd:PTZ00265   474 nsiknniKYSLYS-LKDLEALSNYYNEDGNDsqenknkrnscRAKCAGDLNDMSNTTDSNELIEMRKNyqtikdsevvdv 552

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037402861  133 --------------------------QLSGGQRQRVAIGRAIVREPEVFLFDEPLSNLDAELRVQMRVEISRLHKKLGTT 186
Cdd:PTZ00265   553 skkvlihdfvsalpdkyetlvgsnasKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQKTINNLKGNENRI 632

                          250       260
                   ....*....|....*....|.
gi 1037402861  187 MIYVTHdQTEAMTLADRIVVL 207
Cdd:PTZ00265   633 TIIIAH-RLSTIRYANTIFVL 652
3a01205 TIGR00956
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
 16-210 1.18e-11

Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]


Pssm-ID: 273362 [Multi-domain]  Cd Length: 1394  Bit Score: 66.29  E-value: 1.18e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037402861   16 FEIIHGANLEVKDGEFVVFVGPSGCGKSTLLRMIAGLED----ITSGELQIGGRVVNDVEPADRG-IAMVFQSYALYPHL 90
Cdd:TIGR00956   74 FDILKPMDGLIKPGELTVVLGRPGSGCSTLLKTIASNTDgfhiGVEGVITYDGITPEEIKKHYRGdVVYNAETDVHFPHL 153

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037402861   91 TVEENLSFGLRMNG---NPKA-DTERRVSHVAEI------LQITELMK---RRPKQLSGGQRQRVAIGRAIVREPEVFLF 157
Cdd:TIGR00956  154 TVGETLDFAARCKTpqnRPDGvSREEYAKHIADVymatygLSHTRNTKvgnDFVRGVSGGERKRVSIAEASLGGAKIQCW 233

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1037402861  158 DEPLSNLDAELRVQ-MRV--EISRLHKKLGTTMIYvtHDQTEAMTLADRIVVLRAG 210
Cdd:TIGR00956  234 DNATRGLDSATALEfIRAlkTSANILDTTPLVAIY--QCSQDAYELFDKVIVLYEG 287
PvdE COG4615
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ...
 23-218 1.45e-11

ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion transport and metabolism];


Pssm-ID: 443659 [Multi-domain]  Cd Length: 547  Bit Score: 65.59  E-value: 1.45e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037402861  23 NLEVKDGEfVVF-VGPSGCGKSTLLRMIAGLEDITSGELQIGGRVVNDVEPAD-RG-IAMVFQSYALYPHLtveenlsfg 99
Cdd:COG4615   352 DLTIRRGE-LVFiVGGNGSGKSTLAKLLTGLYRPESGEILLDGQPVTADNREAyRQlFSAVFSDFHLFDRL--------- 421

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037402861 100 lrMNGNPKADTErRVSHVAEILQI---TELMKRR--PKQLSGGQRQRVAIGRAIVREPEVFLFDEPLSNLDAELR-VQMR 173
Cdd:COG4615   422 --LGLDGEADPA-RARELLERLELdhkVSVEDGRfsTTDLSQGQRKRLALLVALLEDRPILVFDEWAADQDPEFRrVFYT 498

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 1037402861 174 VEISRLhKKLGTTMIYVTHDQTeAMTLADRIVVLRAGNIEQIGAP 218
Cdd:COG4615   499 ELLPEL-KARGKTVIAISHDDR-YFDLADRVLKMDYGKLVELTGP 541
PRK11819 PRK11819
putative ABC transporter ATP-binding protein; Reviewed
 8-169 2.14e-11

putative ABC transporter ATP-binding protein; Reviewed


Pssm-ID: 236992 [Multi-domain]  Cd Length: 556  Bit Score: 65.14  E-value: 2.14e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037402861   8 NIVKRFGGFEIIHGANLEVKDGEFVVFVGPSGCGKSTLLRMIAGLEDITSGELQIGGRVVndvepadrgIAMVFQSY-AL 86
Cdd:PRK11819  329 NLSKSFGDRLLIDDLSFSLPPGGIVGIIGPNGAGKSTLFKMITGQEQPDSGTIKIGETVK---------LAYVDQSRdAL 399

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037402861  87 YPHLTVEENLSFGL--------RMNG-------NPK-ADTERRVshvaeilqitelmkrrpKQLSGGQRQRVAIGRAIVR 150
Cdd:PRK11819  400 DPNKTVWEEISGGLdiikvgnrEIPSrayvgrfNFKgGDQQKKV-----------------GVLSGGERNRLHLAKTLKQ 462

                         170       180
                  ....*....|....*....|
gi 1037402861 151 EPEVFLFDEPLSNLDAE-LR 169
Cdd:PRK11819  463 GGNVLLLDEPTNDLDVEtLR 482
hmuV PRK13547
heme ABC transporter ATP-binding protein;
18-221 2.20e-11

heme ABC transporter ATP-binding protein;


Pssm-ID: 184132 [Multi-domain]  Cd Length: 272  Bit Score: 63.69  E-value: 2.20e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037402861  18 IIHGANLEVKDGEFVVFVGPSGCGKSTLLRMIAGleDITSGELQIGGRVVNDV----EP---------ADRGIAMVFQSY 84
Cdd:PRK13547   16 ILRDLSLRIEPGRVTALLGRNGAGKSTLLKALAG--DLTGGGAPRGARVTGDVtlngEPlaaidaprlARLRAVLPQAAQ 93

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037402861  85 ALYPhLTVEENLSFGLRMNGNPKADTERR----VSHVAEILQITELMKRRPKQLSGGQRQRVAIGRAI---------VRE 151
Cdd:PRK13547   94 PAFA-FSAREIVLLGRYPHARRAGALTHRdgeiAWQALALAGATALVGRDVTTLSGGELARVQFARVLaqlwpphdaAQP 172

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037402861 152 PEVFLFDEPLSNLDAELRVQMRVEISRLHKKLGTTMIYVTHDQTEAMTLADRIVVLRAGNIEQIGAPLDL 221
Cdd:PRK13547  173 PRYLLLDEPTAALDLAHQHRLLDTVRRLARDWNLGVLAIVHDPNLAARHADRIAMLADGAIVAHGAPADV 242
PRK10982 PRK10982
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
 19-215 2.26e-11

galactose/methyl galaxtoside transporter ATP-binding protein; Provisional


Pssm-ID: 182880 [Multi-domain]  Cd Length: 491  Bit Score: 64.75  E-value: 2.26e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037402861  19 IHGANLEVKDGEFVVFVGPSGCGKSTLLRMIAGLEDITSGELQIGGRVVND---VEPADRGIAMVFQ---SYALYPHLTV 92
Cdd:PRK10982  264 IRDVSFDLHKGEILGIAGLVGAKRTDIVETLFGIREKSAGTITLHGKKINNhnaNEAINHGFALVTEerrSTGIYAYLDI 343

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037402861  93 EENL----------SFGLRMNGNPKADTE-----RRV---SHVAEIlqitelmkrrpKQLSGGQRQRVAIGRAIVREPEV 154
Cdd:PRK10982  344 GFNSlisnirnyknKVGLLDNSRMKSDTQwvidsMRVktpGHRTQI-----------GSLSGGNQQKVIIGRWLLTQPEI 412

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1037402861 155 FLFDEPLSNLDAELRVQMRVEISRLHKKlGTTMIYVTHDQTEAMTLADRIVVLRAGNIEQI 215
Cdd:PRK10982  413 LMLDEPTRGIDVGAKFEIYQLIAELAKK-DKGIIIISSEMPELLGITDRILVMSNGLVAGI 472
ABC_ABC_ChvD TIGR03719
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ...
 35-193 2.43e-11

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: 64.96  E-value: 2.43e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037402861  35 VGPSGCGKSTLLRMIAGLEDITSGE--LQIGGRVvndvepadrgiAMVFQSYALYPHLTVEENLSFGL--------RMN- 103
Cdd:TIGR03719  37 LGLNGAGKSTLLRIMAGVDKDFNGEarPQPGIKV-----------GYLPQEPQLDPTKTVRENVEEGVaeikdaldRFNe 105

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037402861 104 -----GNPKADTERRVSHVAEI---------------LQITELMKRRP------KQLSGGQRQRVAIGRAIVREPEVFLF 157
Cdd:TIGR03719 106 isakyAEPDADFDKLAAEQAELqeiidaadawdldsqLEIAMDALRCPpwdadvTKLSGGERRRVALCRLLLSKPDMLLL 185

                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 1037402861 158 DEPLSNLDAElrvqmrvEISRLHKKLGT---TMIYVTHD 193
Cdd:TIGR03719 186 DEPTNHLDAE-------SVAWLERHLQEypgTVVAVTHD 217
PRK13541 PRK13541
cytochrome c biogenesis protein CcmA; Provisional
 36-169 2.89e-11

cytochrome c biogenesis protein CcmA; Provisional


Pssm-ID: 184128 [Multi-domain]  Cd Length: 195  Bit Score: 61.81  E-value: 2.89e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037402861  36 GPSGCGKSTLLRMIAGLEDITSGELQIGGRVVNDVepADRGIAMVFQSYALYPHLTVEENLSFGLRMngnpkADTERRVS 115
Cdd:PRK13541   33 GANGCGKSSLLRMIAGIMQPSSGNIYYKNCNINNI--AKPYCTYIGHNLGLKLEMTVFENLKFWSEI-----YNSAETLY 105

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1037402861 116 HVAEILQITELMKRRPKQLSGGQRQRVAIGRAIVREPEVFLFDEPLSNLDAELR 169
Cdd:PRK13541  106 AAIHYFKLHDLLDEKCYSLSSGMQKIVAIARLIACQSDLWLLDEVETNLSKENR 159
PRK11819 PRK11819
putative ABC transporter ATP-binding protein; Reviewed
 35-193 3.12e-10

putative ABC transporter ATP-binding protein; Reviewed


Pssm-ID: 236992 [Multi-domain]  Cd Length: 556  Bit Score: 61.29  E-value: 3.12e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037402861  35 VGPSGCGKSTLLRMIAGLEDITSGE--LQIGGRVvndvepadrGIAMvfQSYALYPHLTVEENLSFGL--------RMN- 103
Cdd:PRK11819   39 LGLNGAGKSTLLRIMAGVDKEFEGEarPAPGIKV---------GYLP--QEPQLDPEKTVRENVEEGVaevkaaldRFNe 107

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037402861 104 -----GNPKADT----------------------ERRVSHVAEILqitelmkRRP------KQLSGGQRQRVAIGRAIVR 150
Cdd:PRK11819  108 iyaayAEPDADFdalaaeqgelqeiidaadawdlDSQLEIAMDAL-------RCPpwdakvTKLSGGERRRVALCRLLLE 180

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 1037402861 151 EPEVFLFDEPLSNLDAElrvqmrvEISRLHKKLGT---TMIYVTHD 193
Cdd:PRK11819  181 KPDMLLLDEPTNHLDAE-------SVAWLEQFLHDypgTVVAVTHD 219
PRK15064 PRK15064
ABC transporter ATP-binding protein; Provisional
 4-212 3.30e-10

ABC transporter ATP-binding protein; Provisional


Pssm-ID: 237894 [Multi-domain]  Cd Length: 530  Bit Score: 61.06  E-value: 3.30e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037402861   4 LSLSNIVKRFGGFEIIHGANLEVKDGEFVVFVGPSGCGKSTLLRMIAGleditsgELQIGGRVVNDVEPADRGiamvfqs 83
Cdd:PRK15064  320 LEVENLTKGFDNGPLFKNLNLLLEAGERLAIIGENGVGKTTLLRTLVG-------ELEPDSGTVKWSENANIG------- 385

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037402861  84 YalYPHLTVEEnlsFGLRMN--------GNPKADTERRVSHVAEILQITELMKRRPKQLSGGQRQRVAIGRAIVREPEVF 155
Cdd:PRK15064  386 Y--YAQDHAYD---FENDLTlfdwmsqwRQEGDDEQAVRGTLGRLLFSQDDIKKSVKVLSGGEKGRMLFGKLMMQKPNVL 460

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037402861 156 LFDEPLSNLDAElrvqmrvEISRLH---KKLGTTMIYVTHDQTEAMTLADRIVVLRAGNI 212
Cdd:PRK15064  461 VMDEPTNHMDME-------SIESLNmalEKYEGTLIFVSHDREFVSSLATRIIEITPDGV 513
PRK11147 PRK11147
ABC transporter ATPase component; Reviewed
 8-193 3.48e-10

ABC transporter ATPase component; Reviewed


Pssm-ID: 236861 [Multi-domain]  Cd Length: 635  Bit Score: 61.50  E-value: 3.48e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037402861   8 NIVKRFggfeiihgaNLEVKDGEFVVFVGPSGCGKSTLLRMIAGLEDITSGELQIGGRvvndVEPAdrgiamVFQSY--A 85
Cdd:PRK11147  333 QLVKDF---------SAQVQRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRIHCGTK----LEVA------YFDQHraE 393

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037402861  86 LYPHLTVEENLSFG---LRMNGNPKadterrvsHVAEILQ---ITELMKRRP-KQLSGGQRQRVAIGRAIVREPEVFLFD 158
Cdd:PRK11147  394 LDPEKTVMDNLAEGkqeVMVNGRPR--------HVLGYLQdflFHPKRAMTPvKALSGGERNRLLLARLFLKPSNLLILD 465

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 1037402861 159 EPLSNLDaelrvqmrVEISRLHKKL-----GTTMIyVTHD 193
Cdd:PRK11147  466 EPTNDLD--------VETLELLEELldsyqGTVLL-VSHD 496
MRP_assoc_pro TIGR00957
multi drug resistance-associated protein (MRP); This model describes multi drug ...
 23-221 6.45e-10

multi drug resistance-associated protein (MRP); This model describes multi drug resistance-associated protein (MRP) in eukaryotes. The multidrug resistance-associated protein is an integral membrane protein that causes multidrug resistance when overexpressed in mammalian cells. It belongs to ABC transporter superfamily. The protein topology and function was experimentally demonstrated by epitope tagging and immunofluorescence. Insertion of tags in the critical regions associated with drug efflux, abrogated its function. The C-terminal domain seem to highly conserved. [Transport and binding proteins, Other]


Pssm-ID: 188098 [Multi-domain]  Cd Length: 1522  Bit Score: 60.73  E-value: 6.45e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037402861   23 NLEVKDGEFVVFVGPSGCGKSTLLRMIAGLEDITSGELQIGGRVVNDVEPAD--RGIAMVFQSYALYphltveenlSFGL 100
Cdd:TIGR00957 1306 NVTIHGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGLNIAKIGLHDlrFKITIIPQDPVLF---------SGSL 1376

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037402861  101 RMNGNPKAD-TERRVSHVAEILQITELMKRRP-----------KQLSGGQRQRVAIGRAIVREPEVFLFDEPLSNLDAE- 167
Cdd:TIGR00957 1377 RMNLDPFSQySDEEVWWALELAHLKTFVSALPdkldhecaeggENLSVGQRQLVCLARALLRKTKILVLDEATAAVDLEt 1456

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1037402861  168 -------LRVQMR-VEISRLHKKLGTTMIYVthdqteamtladRIVVLRAGNIEQIGAPLDL 221
Cdd:TIGR00957 1457 dnliqstIRTQFEdCTVLTIAHRLNTIMDYT------------RVIVLDKGEVAEFGAPSNL 1506
OB_MalK pfam17912
MalK OB fold domain; This entry corresponds to one of two OB-fold domains found in the MalK ...
 235-289 6.71e-10

MalK OB fold domain; This entry corresponds to one of two OB-fold domains found in the MalK transport protein.


Pssm-ID: 465563 [Multi-domain]  Cd Length: 53  Bit Score: 54.13  E-value: 6.71e-10
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1037402861 235 GSPKMNFLKAVVVEAQpgraviALESDANMRLPLP----VAAPIETGAKVTLGIRPEHF 289
Cdd:pfam17912   1 GSPPMNFLPATVVEDG------LLVLGGGVTLPLPegqvLALKLYVGKEVILGIRPEHI 53
3a01203 TIGR00954
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ...
 23-192 7.54e-10

Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]


Pssm-ID: 273360 [Multi-domain]  Cd Length: 659  Bit Score: 60.15  E-value: 7.54e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037402861  23 NLEVKDGEFVVFVGPSGCGKSTLLRMIAGLEDITSGELQIggrvvndvePADRGIAMVFQSyalyPHLTVEE-------- 94
Cdd:TIGR00954 472 SFEVPSGNNLLICGPNGCGKSSLFRILGELWPVYGGRLTK---------PAKGKLFYVPQR----PYMTLGTlrdqiiyp 538

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037402861  95 NLSFGLRMNGNPKADTERrvshVAEILQITELMKRR---------PKQLSGGQRQRVAIGRAIVREPEVFLFDEPLSnld 165
Cdd:TIGR00954 539 DSSEDMKRRGLSDKDLEQ----ILDNVQLTHILEREggwsavqdwMDVLSGGEKQRIAMARLFYHKPQFAILDECTS--- 611

                         170       180
                  ....*....|....*....|....*..
gi 1037402861 166 aELRVQMRVEISRLHKKLGTTMIYVTH 192
Cdd:TIGR00954 612 -AVSVDVEGYMYRLCREFGITLFSVSH 637
PLN03232 PLN03232
ABC transporter C family member; Provisional
 18-250 8.08e-10

ABC transporter C family member; Provisional


Pssm-ID: 215640 [Multi-domain]  Cd Length: 1495  Bit Score: 60.37  E-value: 8.08e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037402861   18 IIHGANLEVKDGEFVVFVGPSGCGKSTLLRMIAGLEDITSGELQIGGRVVNDVEPAD--RGIAMVFQSYALYphltveen 95
Cdd:PLN03232  1251 VLHGLSFFVSPSEKVGVVGRTGAGKSSMLNALFRIVELEKGRIMIDDCDVAKFGLTDlrRVLSIIPQSPVLF-------- 1322

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037402861   96 lSFGLRMNGNPKAD-TERRVSHVAEILQITELMKRRP-----------KQLSGGQRQRVAIGRAIVREPEVFLFDEPLSN 163
Cdd:PLN03232  1323 -SGTVRFNIDPFSEhNDADLWEALERAHIKDVIDRNPfgldaevseggENFSVGQRQLLSLARALLRRSKILVLDEATAS 1401

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037402861  164 LDAELRVQMRVEISRLHKKlgTTMIYVTHdQTEAMTLADRIVVLRAGNIEQIGAPLDLYDDPANQF--VAGFVGSPKMNF 241
Cdd:PLN03232  1402 VDVRTDSLIQRTIREEFKS--CTMLVIAH-RLNTIIDCDKILVLSSGQVLEYDSPQELLSRDTSAFfrMVHSTGPANAQY 1478


                   ....*....
gi 1037402861  242 LKAVVVEAQ 250
Cdd:PLN03232  1479 LSNLVFERR 1487
40850658_otr NF000106
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
4-212 1.16e-09

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


Pssm-ID: 411078 [Multi-domain]  Cd Length: 351  Bit Score: 58.98  E-value: 1.16e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037402861   4 LSLSNIVKRFGGFEIIHGANLEVKDGEFVVFVGPSGCG--KSTLLRMIAGLE--------DITSGELQIGGRVVNDVEPA 73
Cdd:NF000106   14 VEVRGLVKHFGEVKAVDGVDLDVREGTVLGVLGP*GAA**RGALPAHV*GPDagrrpwrf*TWCANRRALRRTIG*HRPV 93

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037402861  74 DRGIAMVFQSyalyphltvEENLSFGLRMNGNPKADTERRVSHVAEILQITELMKRRPKQLSGGQRQRVAIGRAIVREPE 153
Cdd:NF000106   94 R*GRRESFSG---------RENLYMIGR*LDLSRKDARARADELLERFSLTEAAGRAAAKYSGGMRRRLDLAASMIGRPA 164

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1037402861 154 VFLFDEPLSNLDAELRVQMRVEISRLHKKlGTTMIYVTHDQTEAMTLADRIVVLRAGNI 212
Cdd:NF000106  165 VLYLDEPTTGLDPRTRNEVWDEVRSMVRD-GATVLLTTQYMEEAEQLAHELTVIDRGRV 222
PRK15093 PRK15093
peptide ABC transporter ATP-binding protein SapD;
1-225 1.72e-09

peptide ABC transporter ATP-binding protein SapD;


Pssm-ID: 185049 [Multi-domain]  Cd Length: 330  Bit Score: 58.28  E-value: 1.72e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037402861   1 MAELSLSNIVKRF----GGFEIIHGANLEVKDGEFVVFVGPSGCGKSTLLRMIAGLED----ITSGELQIggrvvNDVE- 71
Cdd:PRK15093    1 MPLLDIRNLTIEFktsdGWVKAVDRVSMTLTEGEIRGLVGESGSGKSLIAKAICGVTKdnwrVTADRMRF-----DDIDl 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037402861  72 ----PADR------GIAMVFQSyalyPHLTVEENLSFGLRMNGNPKADT------------ERR---VSHVAEILQITEL 126
Cdd:PRK15093   76 lrlsPRERrklvghNVSMIFQE----PQSCLDPSERVGRQLMQNIPGWTykgrwwqrfgwrKRRaieLLHRVGIKDHKDA 151

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037402861 127 MKRRPKQLSGGQRQRVAIGRAIVREPEVFLFDEPLSNLDAELRVQMRVEISRLHKKLGTTMIYVTHDQTEAMTLADRIVV 206
Cdd:PRK15093  152 MRSFPYELTEGECQKVMIAIALANQPRLLIADEPTNAMEPTTQAQIFRLLTRLNQNNNTTILLISHDLQMLSQWADKINV 231

                         250
                  ....*....|....*....
gi 1037402861 207 LRAGNIEQIGAPLDLYDDP 225
Cdd:PRK15093  232 LYCGQTVETAPSKELVTTP 250
PRK10938 PRK10938
putative molybdenum transport ATP-binding protein ModF; Provisional
 6-197 1.05e-08

putative molybdenum transport ATP-binding protein ModF; Provisional


Pssm-ID: 182852 [Multi-domain]  Cd Length: 490  Bit Score: 56.56  E-value: 1.05e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037402861   6 LSNIVKRFGGFEIIHGANLEVKDGEFVVFVGPSGCGKSTLLRMIAG------LEDIT-------SGE------------- 59
Cdd:PRK10938  263 LNNGVVSYNDRPILHNLSWQVNPGEHWQIVGPNGAGKSTLLSLITGdhpqgySNDLTlfgrrrgSGEtiwdikkhigyvs 342

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037402861  60 --LQIGGRV---VNDVEpadrgIAMVFQSYALYphltveenlsfglrmngnpKADTERRVSHVAE---ILQITELMKRRP 131
Cdd:PRK10938  343 ssLHLDYRVstsVRNVI-----LSGFFDSIGIY-------------------QAVSDRQQKLAQQwldILGIDKRTADAP 398

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1037402861 132 -KQLSGGQRQRVAIGRAIVREPEVFLFDEPLSNLDAELRVQMRVEISRLHKKLGTTMIYVTHDQTEA 197
Cdd:PRK10938  399 fHSLSWGQQRLALIVRALVKHPTLLILDEPLQGLDPLNRQLVRRFVDVLISEGETQLLFVSHHAEDA 465
tagH PRK13545
teichoic acids export protein ATP-binding subunit; Provisional
 23-233 2.61e-08

teichoic acids export protein ATP-binding subunit; Provisional


Pssm-ID: 184130 [Multi-domain]  Cd Length: 549  Bit Score: 55.28  E-value: 2.61e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037402861  23 NLEVKDGEFVVFVGPSGCGKSTLLRMIAGLEDITSGELQIGGRVvndvepadrgiAMVFQSYALYPHLTVEENLSFGLRM 102
Cdd:PRK13545   44 SFEVPEGEIVGIIGLNGSGKSTLSNLIAGVTMPNKGTVDIKGSA-----------ALIAISSGLNGQLTGIENIELKGLM 112

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037402861 103 NGNPKADTERRVSHVAEILQITELMKRRPKQLSGGQRQRVAIGRAIVREPEVFLFDEPLSNLDAELRVQMRVEISRLhKK 182
Cdd:PRK13545  113 MGLTKEKIKEIIPEIIEFADIGKFIYQPVKTYSSGMKSRLGFAISVHINPDILVIDEALSVGDQTFTKKCLDKMNEF-KE 191

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1037402861 183 LGTTMIYVTHDQTEAMTLADRIVVLRAGNIEQIGAPLDLYDDpANQFVAGF 233
Cdd:PRK13545  192 QGKTIFFISHSLSQVKSFCTKALWLHYGQVKEYGDIKEVVDH-YDEFLKKY 241
xylG TIGR02633
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ...
 26-213 4.00e-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: 54.83  E-value: 4.00e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037402861  26 VKDGEFVVFVGPSGCGKSTLLRMIAGL-EDITSGELQIGGRVVNDVEPAD---RGIAMVFQS---YALYPHLTVEENLSF 98
Cdd:TIGR02633 283 LRRGEILGVAGLVGAGRTELVQALFGAyPGKFEGNVFINGKPVDIRNPAQairAGIAMVPEDrkrHGIVPILGVGKNITL 362

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037402861  99 GL--RMNGNPKADTERRVSHVAEILQITELMKRRP----KQLSGGQRQRVAIGRAIVREPEVFLFDEPLSNLDaelrVQM 172
Cdd:TIGR02633 363 SVlkSFCFKMRIDAAAELQIIGSAIQRLKVKTASPflpiGRLSGGNQQKAVLAKMLLTNPRVLILDEPTRGVD----VGA 438

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 1037402861 173 RVEISRLHKKL---GTTMIYVTHDQTEAMTLADRIVVLRAGNIE 213
Cdd:TIGR02633 439 KYEIYKLINQLaqeGVAIIVVSSELAEVLGLSDRVLVIGEGKLK 482
PRK15439 PRK15439
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
 23-212 4.32e-08

autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional


Pssm-ID: 185336 [Multi-domain]  Cd Length: 510  Bit Score: 54.67  E-value: 4.32e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037402861  23 NLEVKDGEFVVFVGPSGCGKSTLLRMIAGLEDITSGELQIGGRVVNDVEPADR-GIAMVF-----QSYALYPHLTVEENL 96
Cdd:PRK15439  283 SLEVRAGEILGLAGVVGAGRTELAETLYGLRPARGGRIMLNGKEINALSTAQRlARGLVYlpedrQSSGLYLDAPLAWNV 362

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037402861  97 SfGLRMNGNPKADTERRVSHVAE----ILQITELMKRRP-KQLSGGQRQRVAIGRAIVREPEVFLFDEPLSNLDaelrVQ 171
Cdd:PRK15439  363 C-ALTHNRRGFWIKPARENAVLEryrrALNIKFNHAEQAaRTLSGGNQQKVLIAKCLEASPQLLIVDEPTRGVD----VS 437

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 1037402861 172 MRVEISRLHKKL---GTTMIYVTHDQTEAMTLADRIVVLRAGNI 212
Cdd:PRK15439  438 ARNDIYQLIRSIaaqNVAVLFISSDLEEIEQMADRVLVMHQGEI 481
PRK13546 PRK13546
teichoic acids export ABC transporter ATP-binding subunit TagH;
28-216 4.74e-08

teichoic acids export ABC transporter ATP-binding subunit TagH;


Pssm-ID: 184131 [Multi-domain]  Cd Length: 264  Bit Score: 53.67  E-value: 4.74e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037402861  28 DGEFVVFVGPSGCGKSTLLRMIAGLEDITSGELQIGGRVvndvepadrgiAMVFQSYALYPHLTVEENLSFGLRMNGNPK 107
Cdd:PRK13546   49 EGDVIGLVGINGSGKSTLSNIIGGSLSPTVGKVDRNGEV-----------SVIAISAGLSGQLTGIENIEFKMLCMGFKR 117

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037402861 108 ADTERRVSHVAEILQITELMKRRPKQLSGGQRQRVAIGRAIVREPEVFLFDEPLSNLDAELRVQMRVEISRLhKKLGTTM 187
Cdd:PRK13546  118 KEIKAMTPKIIEFSELGEFIYQPVKKYSSGMRAKLGFSINITVNPDILVIDEALSVGDQTFAQKCLDKIYEF-KEQNKTI 196

                         170       180
                  ....*....|....*....|....*....
gi 1037402861 188 IYVTHDQTEAMTLADRIVVLRAGNIEQIG 216
Cdd:PRK13546  197 FFVSHNLGQVRQFCTKIAWIEGGKLKDYG 225
AAA smart00382
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ...
 29-219 1.42e-07

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


Pssm-ID: 214640 [Multi-domain]  Cd Length: 148  Bit Score: 50.45  E-value: 1.42e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037402861   29 GEFVVFVGPSGCGKSTLLRMIAGLEDITSGELqiggrvvndvepadrgiamvfqsyalyphltveenlsfgLRMNGNPKA 108
Cdd:smart00382   2 GEVILIVGPPGSGKTTLARALARELGPPGGGV---------------------------------------IYIDGEDIL 42

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037402861  109 DTERRVSHVaeilqitELMKRRPKQLSGGQRQRVAIGRAIVREPEVFLFDEPLSNLDAELRVQMRVEIS-----RLHKKL 183
Cdd:smart00382  43 EEVLDQLLL-------IIVGGKKASGSGELRLRLALALARKLKPDVLILDEITSLLDAEQEALLLLLEElrlllLLKSEK 115

                          170       180       190
                   ....*....|....*....|....*....|....*.
gi 1037402861  184 GTTMIYVTHDQTeamTLADRIVVLRAGNIEQIGAPL 219
Cdd:smart00382 116 NLTVILTTNDEK---DLGPALLRRRFDRRIVLLLIL 148
PRK13549 PRK13549
xylose transporter ATP-binding subunit; Provisional
 17-212 1.71e-07

xylose transporter ATP-binding subunit; Provisional


Pssm-ID: 184134 [Multi-domain]  Cd Length: 506  Bit Score: 52.62  E-value: 1.71e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037402861  17 EIIHGANLEVKDGEFVVFVGPSGCGKSTLLRMIAGL-EDITSGELQIGGRVVNDVEPAD---RGIAMVFQS---YALYPH 89
Cdd:PRK13549  276 KRVDDVSFSLRRGEILGIAGLVGAGRTELVQCLFGAyPGRWEGEIFIDGKPVKIRNPQQaiaQGIAMVPEDrkrDGIVPV 355

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037402861  90 LTVEENL------SFGLRMngnpkadterRVSHVAEILQITELMKR----------RPKQLSGGQRQRVAIGRAIVREPE 153
Cdd:PRK13549  356 MGVGKNItlaaldRFTGGS----------RIDDAAELKTILESIQRlkvktaspelAIARLSGGNQQKAVLAKCLLLNPK 425

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1037402861 154 VFLFDEPLSNLDaelrVQMRVEISRLHKKL---GTTMIYVTHDQTEAMTLADRIVVLRAGNI 212
Cdd:PRK13549  426 ILILDEPTRGID----VGAKYEIYKLINQLvqqGVAIIVISSELPEVLGLSDRVLVMHEGKL 483
ABCC_CFTR2 cd03289
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ...
 3-214 1.99e-06

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: 48.70  E-value: 1.99e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037402861   3 ELSLSNIVKRF--GGFEIIHGANLEVKDGEFVVFVGPSGCGKSTLLRMIAGLEDiTSGELQIGGRVVNDV--EPADRGIA 78
Cdd:cd03289     2 QMTVKDLTAKYteGGNAVLENISFSISPGQRVGLLGRTGSGKSTLLSAFLRLLN-TEGDIQIDGVSWNSVplQKWRKAFG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037402861  79 MVFQSYALYphltveenlSFGLRMNGNPKAD-TERRVSHVAEILQITELMKRRPKQ-----------LSGGQRQRVAIGR 146
Cdd:cd03289    81 VIPQKVFIF---------SGTFRKNLDPYGKwSDEEIWKVAEEVGLKSVIEQFPGQldfvlvdggcvLSHGHKQLMCLAR 151

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1037402861 147 AIVREPEVFLFDEPLSNLDAelrVQMRVEISRLHKKLGTTMIYVTHDQTEAMTLADRIVVLRAGNIEQ 214
Cdd:cd03289   152 SVLSKAKILLLDEPSAHLDP---ITYQVIRKTLKQAFADCTVILSEHRIEAMLECQRFLVIEENKVRQ 216
ABCC_SUR2 cd03288
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The ...
 23-221 2.07e-06

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: 48.37  E-value: 2.07e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037402861  23 NLEVKDGEFVVFVGPSGCGKSTLLRMIAGLEDITSGELQIGGRVVNDV--EPADRGIAMVFQSYALYphltveenlSFGL 100
Cdd:cd03288    41 KAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVIDGIDISKLplHTLRSRLSIILQDPILF---------SGSI 111

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037402861 101 RMNGNPKAD-TERRVSHVAEILQITELMKRRPKQL-----------SGGQRQRVAIGRAIVREPEVFLFDEPLSNLD-AE 167
Cdd:cd03288   112 RFNLDPECKcTDDRLWEALEIAQLKNMVKSLPGGLdavvteggenfSVGQRQLFCLARAFVRKSSILIMDEATASIDmAT 191

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1037402861 168 LRVQMRVEISRLHKKLGTTMIYVTHDQTEamtlADRIVVLRAGNIEQIGAPLDL 221
Cdd:cd03288   192 ENILQKVVMTAFADRTVVTIAHRVSTILD----ADLVLVLSRGILVECDTPENL 241
PLN03140 PLN03140
ABC transporter G family member; Provisional
 29-166 2.12e-06

ABC transporter G family member; Provisional


Pssm-ID: 215599 [Multi-domain]  Cd Length: 1470  Bit Score: 49.84  E-value: 2.12e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037402861   29 GEFVVFVGPSGCGKSTLLRMIAGLED--ITSGELQIGGRVVNDvEPADRGIAMVFQSYALYPHLTVEENLSFG--LRMng 104
Cdd:PLN03140   906 GVLTALMGVSGAGKTTLMDVLAGRKTggYIEGDIRISGFPKKQ-ETFARISGYCEQNDIHSPQVTVRESLIYSafLRL-- 982

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1037402861  105 nPK-ADTERRVSHVAEILQITELMKRRPK--------QLSGGQRQRVAIGRAIVREPEVFLFDEPLSNLDA 166
Cdd:PLN03140   983 -PKeVSKEEKMMFVDEVMELVELDNLKDAivglpgvtGLSTEQRKRLTIAVELVANPSIIFMDEPTSGLDA 1052
CFTR_protein TIGR01271
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ...
 14-214 3.06e-06

cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis fibrosis transmembrane conductor regulator (CFTR) in eukaryotes. The principal role of this protein is chloride ion conductance. The protein is predicted to consist of 12 transmembrane domains. Mutations or lesions in the genetic loci have been linked to the aetiology of asthma, bronchiectasis, chronic obstructive pulmonary disease etc. Disease-causing mutations have been studied by 36Cl efflux assays in vitro cell cultures and electrophysiology, all of which point to the impairment of chloride channel stability and not the biosynthetic processing per se. [Transport and binding proteins, Anions]


Pssm-ID: 273530 [Multi-domain]  Cd Length: 1490  Bit Score: 49.14  E-value: 3.06e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037402861   14 GGFEIIHGANLEVKDGEFVVFVGPSGCGKSTLLRMIAGLEDiTSGELQIGGRVVNDV--EPADRGIAMVFQSYALyphlt 91
Cdd:TIGR01271 1230 AGRAVLQDLSFSVEGGQRVGLLGRTGSGKSTLLSALLRLLS-TEGEIQIDGVSWNSVtlQTWRKAFGVIPQKVFI----- 1303

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037402861   92 veenLSFGLRMNGNPKAD-TERRVSHVAEILQITELMKRRPKQL-----------SGGQRQRVAIGRAIVREPEVFLFDE 159
Cdd:TIGR01271 1304 ----FSGTFRKNLDPYEQwSDEEIWKVAEEVGLKSVIEQFPDKLdfvlvdggyvlSNGHKQLMCLARSILSKAKILLLDE 1379

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1037402861  160 PLSNLDAelrVQMRVEISRLHKKLGTTMIYVTHDQTEAMTLADRIVVLRAGNIEQ 214
Cdd:TIGR01271 1380 PSAHLDP---VTLQIIRKTLKQSFSNCTVILSEHRVEALLECQQFLVIEGSSVKQ 1431
PLN03073 PLN03073
ABC transporter F family; Provisional
 3-192 3.20e-06

ABC transporter F family; Provisional


Pssm-ID: 215558 [Multi-domain]  Cd Length: 718  Bit Score: 49.09  E-value: 3.20e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037402861   3 ELSLSNIVKRFGGFEIIHGANLEVKDGEFVVFVGPSGCGKSTLLRMIA--GLEDITSG--ELQIGGRVVNDVEPA----- 73
Cdd:PLN03073  177 DIHMENFSISVGGRDLIVDASVTLAFGRHYGLVGRNGTGKTTFLRYMAmhAIDGIPKNcqILHVEQEVVGDDTTAlqcvl 256

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037402861  74 ----DRGIAMVFQSYALYPHLTVEENLSFG---LRMNGNPKADT--------------------ERRVSHVAEILQIT-E 125
Cdd:PLN03073  257 ntdiERTQLLEEEAQLVAQQRELEFETETGkgkGANKDGVDKDAvsqrleeiykrlelidaytaEARAASILAGLSFTpE 336

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1037402861 126 LMKRRPKQLSGGQRQRVAIGRAIVREPEVFLFDEPLSNLDaeLRVQMRVEISRLhkKLGTTMIYVTH 192
Cdd:PLN03073  337 MQVKATKTFSGGWRMRIALARALFIEPDLLLLDEPTNHLD--LHAVLWLETYLL--KWPKTFIVVSH 399
PLN03073 PLN03073
ABC transporter F family; Provisional
 32-165 3.34e-06

ABC transporter F family; Provisional


Pssm-ID: 215558 [Multi-domain]  Cd Length: 718  Bit Score: 49.09  E-value: 3.34e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037402861  32 VVFVGPSGCGKSTLLRMIAGLEDITSGELQIGGRVvndvepadrGIAMVFQSYALYPHLTVEENLSFglrMNGNPKADTE 111
Cdd:PLN03073  538 IAMVGPNGIGKSTILKLISGELQPSSGTVFRSAKV---------RMAVFSQHHVDGLDLSSNPLLYM---MRCFPGVPEQ 605

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1037402861 112 RRVSHVAEILQITELMKRRPKQLSGGQRQRVAIGRAIVREPEVFLFDEPLSNLD 165
Cdd:PLN03073  606 KLRAHLGSFGVTGNLALQPMYTLSGGQKSRVAFAKITFKKPHILLLDEPSNHLD 659
ABC_UvrA cd03238
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ...
 134-205 9.83e-06

ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins, and UvrB having one ATP binding site that is structurally related to that of helicases.


Pssm-ID: 213205 [Multi-domain]  Cd Length: 176  Bit Score: 45.39  E-value: 9.83e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1037402861 134 LSGGQRQRVAIGRAIVREPE--VFLFDEPLSNLDAELRVQMRVEISRLhKKLGTTMIYVTHDQTeAMTLADRIV 205
Cdd:cd03238    88 LSGGELQRVKLASELFSEPPgtLFILDEPSTGLHQQDINQLLEVIKGL-IDLGNTVILIEHNLD-VLSSADWII 159
PLN03130 PLN03130
ABC transporter C family member; Provisional
 18-248 5.29e-05

ABC transporter C family member; Provisional


Pssm-ID: 215595 [Multi-domain]  Cd Length: 1622  Bit Score: 45.50  E-value: 5.29e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037402861   18 IIHGANLEVKDGEFVVFVGPSGCGKSTLLRMIAGLEDITSGELQIGGRVVNDVEPAD--RGIAMVFQSYALYphltveen 95
Cdd:PLN03130  1254 VLHGLSFEISPSEKVGIVGRTGAGKSSMLNALFRIVELERGRILIDGCDISKFGLMDlrKVLGIIPQAPVLF-------- 1325

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037402861   96 lSFGLRMNGNPKadTERRVSHVAEILQ---ITELMKRRPKQL-----------SGGQRQRVAIGRAIVREPEVFLFDEPL 161
Cdd:PLN03130  1326 -SGTVRFNLDPF--NEHNDADLWESLErahLKDVIRRNSLGLdaevseagenfSVGQRQLLSLARALLRRSKILVLDEAT 1402

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037402861  162 SNLDAELRVQMRVEISRLHKklGTTMIYVTHdQTEAMTLADRIVVLRAGNIEQIGAPLDLYDDPANQFvAGFV---GSPK 238
Cdd:PLN03130  1403 AAVDVRTDALIQKTIREEFK--SCTMLIIAH-RLNTIIDCDRILVLDAGRVVEFDTPENLLSNEGSAF-SKMVqstGAAN 1478

                          250
                   ....*....|
gi 1037402861  239 MNFLKAVVVE 248
Cdd:PLN03130  1479 AQYLRSLVFG 1488
ABC_Rad50 cd03240
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ...
 28-205 1.27e-04

ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ATP-binding cassette of ABC transporters, but are not associated with membrane-spanning domains. The conserved ATP-binding motifs common to Rad50 and the ABC transporter family include the Walker A and Walker B motifs, the Q loop, a histidine residue in the switch region, a D-loop, and a conserved LSGG sequence. This conserved sequence, LSGG, is the most specific and characteristic motif of this family and is thus known as the ABC signature sequence.


Pssm-ID: 213207 [Multi-domain]  Cd Length: 204  Bit Score: 42.59  E-value: 1.27e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037402861  28 DGEFVVFVGPSGCGKSTLlrmIAGLEDITSGEL---QIGGRVVNDV--EPADRG-IAMVFQS-----YALYPHLTVEENL 96
Cdd:cd03240    21 FSPLTLIVGQNGAGKTTI---IEALKYALTGELppnSKGGAHDPKLirEGEVRAqVKLAFENangkkYTITRSLAILENV 97

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037402861  97 SFglrmngnpkadterrvSHVAEILQITELMkrrPKQLSGGQRQ------RVAIGRAIVREPEVFLFDEPLSNLDAELRV 170
Cdd:cd03240    98 IF----------------CHQGESNWPLLDM---RGRCSGGEKVlasliiRLALAETFGSNCGILALDEPTTNLDEENIE 158

                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 1037402861 171 QMRVEISRLHKKLGT-TMIYVTHDQtEAMTLADRIV 205
Cdd:cd03240   159 ESLAEIIEERKSQKNfQLIVITHDE-ELVDAADHIY 193
ABC_SMC3_euk cd03272
ATP-binding cassette domain of eukaryotic SMC3 proteins; The structural maintenance of ...
 122-204 1.85e-04

ATP-binding cassette domain of eukaryotic SMC3 proteins; The structural maintenance of chromosomes (SMC) proteins are large (approximately 110 to 170 kDa), and each is arranged into five recognizable domains. Amino-acid sequence homology of SMC proteins between species is largely confined to the amino- and carboxy-terminal globular domains. The amino-terminal domain contains a 'Walker A' nucleotide-binding domain (GxxGxGKS/T, in the single-letter amino-acid code), which by mutational studies has been shown to be essential in several proteins. The carboxy-terminal domain contains a sequence (the DA-box) that resembles a 'Walker B' motif, and a motif with homology to the signature sequence of the ATP-binding cassette (ABC) family of ATPases. The sequence homology within the carboxy-terminal domain is relatively high within the SMC1-SMC4 group, whereas SMC5 and SMC6 show some divergence in both of these sequences. In eukaryotic cells, the proteins are found as heterodimers of SMC1 paired with SMC3, SMC2 with SMC4, and SMC5 with SMC6 (formerly known as Rad18).


Pssm-ID: 213239 [Multi-domain]  Cd Length: 243  Bit Score: 42.63  E-value: 1.85e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037402861 122 QITEL------MKRRPKQLSGGQRQRVAIGR--AIVR-EPEVF-LFDEPLSNLDAelrvQMRVEISRLHKKL-GTTMIYV 190
Cdd:cd03272   141 KINSLtnmkqdEQQEMQQLSGGQKSLVALALifAIQKcDPAPFyLFDEIDAALDA----QYRTAVANMIKELsDGAQFIT 216

                          90
                  ....*....|....
gi 1037402861 191 THDQTEAMTLADRI 204
Cdd:cd03272   217 TTFRPELLEVADKF 230
ABC_Class2 cd03227
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ...
 14-205 2.51e-04

ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems involved in cellular processes other than transport. These families are characterized by the fact that the ABC subunit is made up of duplicated, fused ABC modules (ABC2). No known transmembrane proteins or domains are associated with these proteins.


Pssm-ID: 213194 [Multi-domain]  Cd Length: 162  Bit Score: 41.19  E-value: 2.51e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037402861  14 GGFEIIHGAN-LEVKDGEFVVFVGPSGCGKSTLLRMIAgleditsgelqiggrvvndvepadrgiamvfqsyalyphltv 92
Cdd:cd03227     5 GRFPSYFVPNdVTFGEGSLTIITGPNGSGKSTILDAIG------------------------------------------ 42

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037402861  93 eenLSFGLRMNGNPKADTERRVSHVAeiLQITELMKRRPkQLSGGQRQRVAI-----GRAIVREPeVFLFDEPLSNLDAE 167
Cdd:cd03227    43 ---LALGGAQSATRRRSGVKAGCIVA--AVSAELIFTRL-QLSGGEKELSALalilaLASLKPRP-LYILDEIDRGLDPR 115

                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 1037402861 168 lRVQMRVEISRLHKKLGTTMIYVTHDQtEAMTLADRIV 205
Cdd:cd03227   116 -DGQALAEAILEHLVKGAQVIVITHLP-ELAELADKLI 151
ABC_UvrA_I cd03270
ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair ...
 23-205 1.07e-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: 39.93  E-value: 1.07e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037402861  23 NLEVKDGEFVVFVGPSGCGKSTL----------LRMIAGLEdiTSGELQIGGRVVNDVEPADrgiamvfqsyALYPHLTV 92
Cdd:cd03270    15 DVDIPRNKLVVITGVSGSGKSSLafdtiyaegqRRYVESLS--AYARQFLGQMDKPDVDSIE----------GLSPAIAI 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037402861  93 EENlsfglRMNGNPKAD----TE---------RRVSHVAEILQITEL------MKRRPKQLSGGQRQRVAIGRAIVREPE 153
Cdd:cd03270    83 DQK-----TTSRNPRSTvgtvTEiydylrllfARVGIRERLGFLVDVglgyltLSRSAPTLSGGEAQRIRLATQIGSGLT 157

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1037402861 154 --VFLFDEPLSNLDAELRVQMRVEISRLhKKLGTTMIYVTHDQtEAMTLADRIV 205
Cdd:cd03270   158 gvLYVLDEPSIGLHPRDNDRLIETLKRL-RDLGNTVLVVEHDE-DTIRAADHVI 209
TOBE_2 pfam08402
TOBE domain; The TOBE domain (Transport-associated OB) always occurs as a dimer as the ...
 282-352 1.48e-03

TOBE domain; The TOBE domain (Transport-associated OB) always occurs as a dimer as the C-terminal strand of each domain is supplied by the partner. Probably involved in the recognition of small ligands such as molybdenum and sulphate. Found in ABC transporters immediately after the ATPase domain. In this family a strong RPE motif is found at the presumed N-terminus of the domain.


Pssm-ID: 462465 [Multi-domain]  Cd Length: 73  Bit Score: 36.83  E-value: 1.48e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1037402861 282 LGIRPEHfVDAGMGDADLTVAIDVAEHLGNTSYIYAAIGSEQLIIERPESRTAGNR---ETLTVGLPARHTFLF 352
Cdd:pfam08402   1 LAIRPEK-IRLAAAANGLSGTVTDVEYLGDHTRYHVELAGGEELVVRVPNAHARPPapgDRVGLGWDPEDAHVL 73
YjeQ_EngC cd01854
Ribosomal interacting GTPase YjeQ/EngC, a circularly permuted subfamily of the Ras GTPases; ...
 29-59 1.55e-03

Ribosomal interacting GTPase YjeQ/EngC, a circularly permuted subfamily of the Ras GTPases; YjeQ (YloQ in Bacillus subtilis) is a ribosomal small subunit-dependent GTPase; hence also known as RsgA. YjeQ is a late-stage ribosomal biogenesis factor involved in the 30S subunit maturation, and it represents a protein family whose members are broadly conserved in bacteria and have been shown to be essential to the growth of E. coli and B. subtilis. Proteins of the YjeQ family contain all sequence motifs typical of the vast class of P-loop-containing GTPases, but show a circular permutation, with a G4-G1-G3 pattern of motifs as opposed to the regular G1-G3-G4 pattern seen in most GTPases. All YjeQ family proteins display a unique domain architecture, which includes an N-terminal OB-fold RNA-binding domain, the central permuted GTPase domain, and a zinc knuckle-like C-terminal cysteine domain.


Pssm-ID: 206747 [Multi-domain]  Cd Length: 211  Bit Score: 39.30  E-value: 1.55e-03
                          10        20        30
                  ....*....|....*....|....*....|.
gi 1037402861  29 GEFVVFVGPSGCGKSTLLRMIAGLEDITSGE 59
Cdd:cd01854    85 GKTSVLVGQSGVGKSTLLNALLPELVLATGE 115
 
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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