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Conserved domains on  [gi|2544519355|ref|WP_300307749|]
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ATP-binding cassette domain-containing protein, partial [Candidatus Thioglobus sp.]

Protein Classification

excinuclease ABC subunit UvrA( domain architecture ID 1000295)

excinuclease ABC subunit UvrA is a DNA-binding ATPase that recognizes DNA adducts in the nucleotide excision repair process catalyzed by the UvrABC excinuclease repair system

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
UvrA super family cl33793
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair];
1-208 1.06e-170

Excinuclease UvrABC ATPase subunit [Replication, recombination and repair];


The actual alignment was detected with superfamily member COG0178:

Pssm-ID: 439948 [Multi-domain]  Cd Length: 941  Bit Score: 493.00  E-value: 1.06e-170
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2544519355   1 FNVKGGRCEACKGDGLIKVEMHFLPDIYVPCDVCHGNRYNRETLEITYKGKNISEVLDMTVEKAVVFFEPIPKIKQKLQT 80
Cdd:COG0178   730 FNVKGGRCEACQGDGVIKIEMHFLPDVYVPCEVCKGKRYNRETLEVKYKGKNIADVLDMTVEEALEFFENIPKIARKLQT 809
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2544519355  81 LMDVGLSYITLGQNATTLSGGEAQRIKLAKELSKLDTGQTLYILDEPTTGLHFHDIKQLLSVINRLRERENTIVIIEHNL 160
Cdd:COG0178   810 LQDVGLGYIKLGQPATTLSGGEAQRVKLASELSKRSTGKTLYILDEPTTGLHFHDIRKLLEVLHRLVDKGNTVVVIEHNL 889
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 2544519355 161 DVIKTADWIVDVGPEGGDKGGHIVATGTPEKVSAVEGSYTGQYLKSYL 208
Cdd:COG0178   890 DVIKTADWIIDLGPEGGDGGGEIVAEGTPEEVAKVKASYTGRYLKEYL 937
 
Name Accession Description Interval E-value
UvrA COG0178
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair];
1-208 1.06e-170

Excinuclease UvrABC ATPase subunit [Replication, recombination and repair];


Pssm-ID: 439948 [Multi-domain]  Cd Length: 941  Bit Score: 493.00  E-value: 1.06e-170
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2544519355   1 FNVKGGRCEACKGDGLIKVEMHFLPDIYVPCDVCHGNRYNRETLEITYKGKNISEVLDMTVEKAVVFFEPIPKIKQKLQT 80
Cdd:COG0178   730 FNVKGGRCEACQGDGVIKIEMHFLPDVYVPCEVCKGKRYNRETLEVKYKGKNIADVLDMTVEEALEFFENIPKIARKLQT 809
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2544519355  81 LMDVGLSYITLGQNATTLSGGEAQRIKLAKELSKLDTGQTLYILDEPTTGLHFHDIKQLLSVINRLRERENTIVIIEHNL 160
Cdd:COG0178   810 LQDVGLGYIKLGQPATTLSGGEAQRVKLASELSKRSTGKTLYILDEPTTGLHFHDIRKLLEVLHRLVDKGNTVVVIEHNL 889
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 2544519355 161 DVIKTADWIVDVGPEGGDKGGHIVATGTPEKVSAVEGSYTGQYLKSYL 208
Cdd:COG0178   890 DVIKTADWIIDLGPEGGDGGGEIVAEGTPEEVAKVKASYTGRYLKEYL 937
uvrA PRK00349
excinuclease ABC subunit UvrA;
1-208 1.59e-170

excinuclease ABC subunit UvrA;


Pssm-ID: 234734 [Multi-domain]  Cd Length: 943  Bit Score: 492.67  E-value: 1.59e-170
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2544519355   1 FNVKGGRCEACKGDGLIKVEMHFLPDIYVPCDVCHGNRYNRETLEITYKGKNISEVLDMTVEKAVVFFEPIPKIKQKLQT 80
Cdd:PRK00349  734 FNVKGGRCEACQGDGVIKIEMHFLPDVYVPCDVCKGKRYNRETLEVKYKGKNIADVLDMTVEEALEFFEAIPKIARKLQT 813
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2544519355  81 LMDVGLSYITLGQNATTLSGGEAQRIKLAKELSKLDTGQTLYILDEPTTGLHFHDIKQLLSVINRLRERENTIVIIEHNL 160
Cdd:PRK00349  814 LVDVGLGYIKLGQPATTLSGGEAQRVKLAKELSKRSTGKTLYILDEPTTGLHFEDIRKLLEVLHRLVDKGNTVVVIEHNL 893
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 2544519355 161 DVIKTADWIVDVGPEGGDKGGHIVATGTPEKVSAVEGSYTGQYLKSYL 208
Cdd:PRK00349  894 DVIKTADWIIDLGPEGGDGGGEIVATGTPEEVAKVEASYTGRYLKPVL 941
uvra TIGR00630
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ...
1-193 5.64e-137

excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of proteins of which all members for which functions are known except the UvrA proteins are involved in the transport of material through membranes. UvrA orthologs are involved in the recognition of DNA damage as a step in nucleotide excision repair. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]


Pssm-ID: 273184 [Multi-domain]  Cd Length: 925  Bit Score: 405.55  E-value: 5.64e-137
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2544519355   1 FNVKGGRCEACKGDGLIKVEMHFLPDIYVPCDVCHGNRYNRETLEITYKGKNISEVLDMTVEKAVVFFEPIPKIKQKLQT 80
Cdd:TIGR00630 733 FNVKGGRCEACQGDGVIKIEMHFLPDVYVPCEVCKGKRYNRETLEVKYKGKNIADVLDMTVEEAYEFFEAVPSISRKLQT 812
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2544519355  81 LMDVGLSYITLGQNATTLSGGEAQRIKLAKELSKLDTGQTLYILDEPTTGLHFHDIKQLLSVINRLRERENTIVIIEHNL 160
Cdd:TIGR00630 813 LCDVGLGYIRLGQPATTLSGGEAQRIKLAKELSKRSTGRTLYILDEPTTGLHFDDIKKLLEVLQRLVDKGNTVVVIEHNL 892
                         170       180       190
                  ....*....|....*....|....*....|...
gi 2544519355 161 DVIKTADWIVDVGPEGGDKGGHIVATGTPEKVS 193
Cdd:TIGR00630 893 DVIKTADYIIDLGPEGGDGGGTVVASGTPEEVA 925
ABC_UvrA_II cd03271
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair ...
31-189 9.61e-111

ATP-binding cassette domain II 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: 213238 [Multi-domain]  Cd Length: 261  Bit Score: 317.25  E-value: 9.61e-111
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2544519355  31 CDVCHGNRYNRETLEITYKGKNISEVLDMTVEKAVVFFEPIPKIKQKLQTLMDVGLSYITLGQNATTLSGGEAQRIKLAK 110
Cdd:cd03271   103 CEVCKGKRYNRETLEVRYKGKSIADVLDMTVEEALEFFENIPKIARKLQTLCDVGLGYIKLGQPATTLSGGEAQRIKLAK 182
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2544519355 111 ELSKLDTGQTLYILDEPTTGLHFHDIKQLLSVINRLRERENTIVIIEHNLDVIKTADWIVDVGPEGGDKGGHIVATGTP 189
Cdd:cd03271   183 ELSKRSTGKTLYILDEPTTGLHFHDVKKLLEVLQRLVDKGNTVVVIEHNLDVIKCADWIIDLGPEGGDGGGQVVASGTP 261
ABC_tran pfam00005
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ...
78-129 1.51e-06

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: 46.10  E-value: 1.51e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 2544519355  78 LQTLMDVGLSYITLGQNATTLSGGEAQRIKLAKELSkldTGQTLYILDEPTT 129
Cdd:pfam00005 102 LEKLGLGDLADRPVGERPGTLSGGQRQRVAIARALL---TKPKLLLLDEPTA 150
GguA NF040905
sugar ABC transporter ATP-binding protein;
84-169 1.61e-04

sugar ABC transporter ATP-binding protein;


Pssm-ID: 468840 [Multi-domain]  Cd Length: 500  Bit Score: 41.70  E-value: 1.61e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2544519355  84 VGLSyitlgQNATTLSG----GEAQRIKLAKELSKldtGQTLYILDEPTTGLHFHDIKQLLSVINRLRERENTIVIIEHN 159
Cdd:NF040905  127 VGLD-----ESPDTLVTdigvGKQQLVEIAKALSK---DVKLLILDEPTAALNEEDSAALLDLLLELKAQGITSIIISHK 198
                          90
                  ....*....|.
gi 2544519355 160 L-DVIKTADWI 169
Cdd:NF040905  199 LnEIRRVADSI 209
ABC2_perm_RbbA NF033858
ribosome-associated ATPase/putative transporter RbbA;
121-198 1.31e-03

ribosome-associated ATPase/putative transporter RbbA;


Pssm-ID: 468210 [Multi-domain]  Cd Length: 907  Bit Score: 38.95  E-value: 1.31e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2544519355 121 LYILDEPTTGLhfhDI---KQLLSVINRLR-ERENTIVIiehnldvIKTA--------DWIV--DvgpeggdkGGHIVAT 186
Cdd:NF033858  157 LLILDEPTTGV---DPlsrRQFWELIDRIRaERPGMSVL-------VATAymeeaerfDWLVamD--------AGRVLAT 218
                          90
                  ....*....|..
gi 2544519355 187 GTPEKVSAVEGS 198
Cdd:NF033858  219 GTPAELLARTGA 230
 
Name Accession Description Interval E-value
UvrA COG0178
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair];
1-208 1.06e-170

Excinuclease UvrABC ATPase subunit [Replication, recombination and repair];


Pssm-ID: 439948 [Multi-domain]  Cd Length: 941  Bit Score: 493.00  E-value: 1.06e-170
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2544519355   1 FNVKGGRCEACKGDGLIKVEMHFLPDIYVPCDVCHGNRYNRETLEITYKGKNISEVLDMTVEKAVVFFEPIPKIKQKLQT 80
Cdd:COG0178   730 FNVKGGRCEACQGDGVIKIEMHFLPDVYVPCEVCKGKRYNRETLEVKYKGKNIADVLDMTVEEALEFFENIPKIARKLQT 809
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2544519355  81 LMDVGLSYITLGQNATTLSGGEAQRIKLAKELSKLDTGQTLYILDEPTTGLHFHDIKQLLSVINRLRERENTIVIIEHNL 160
Cdd:COG0178   810 LQDVGLGYIKLGQPATTLSGGEAQRVKLASELSKRSTGKTLYILDEPTTGLHFHDIRKLLEVLHRLVDKGNTVVVIEHNL 889
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 2544519355 161 DVIKTADWIVDVGPEGGDKGGHIVATGTPEKVSAVEGSYTGQYLKSYL 208
Cdd:COG0178   890 DVIKTADWIIDLGPEGGDGGGEIVAEGTPEEVAKVKASYTGRYLKEYL 937
uvrA PRK00349
excinuclease ABC subunit UvrA;
1-208 1.59e-170

excinuclease ABC subunit UvrA;


Pssm-ID: 234734 [Multi-domain]  Cd Length: 943  Bit Score: 492.67  E-value: 1.59e-170
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2544519355   1 FNVKGGRCEACKGDGLIKVEMHFLPDIYVPCDVCHGNRYNRETLEITYKGKNISEVLDMTVEKAVVFFEPIPKIKQKLQT 80
Cdd:PRK00349  734 FNVKGGRCEACQGDGVIKIEMHFLPDVYVPCDVCKGKRYNRETLEVKYKGKNIADVLDMTVEEALEFFEAIPKIARKLQT 813
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2544519355  81 LMDVGLSYITLGQNATTLSGGEAQRIKLAKELSKLDTGQTLYILDEPTTGLHFHDIKQLLSVINRLRERENTIVIIEHNL 160
Cdd:PRK00349  814 LVDVGLGYIKLGQPATTLSGGEAQRVKLAKELSKRSTGKTLYILDEPTTGLHFEDIRKLLEVLHRLVDKGNTVVVIEHNL 893
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 2544519355 161 DVIKTADWIVDVGPEGGDKGGHIVATGTPEKVSAVEGSYTGQYLKSYL 208
Cdd:PRK00349  894 DVIKTADWIIDLGPEGGDGGGEIVATGTPEEVAKVEASYTGRYLKPVL 941
uvra TIGR00630
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ...
1-193 5.64e-137

excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of proteins of which all members for which functions are known except the UvrA proteins are involved in the transport of material through membranes. UvrA orthologs are involved in the recognition of DNA damage as a step in nucleotide excision repair. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]


Pssm-ID: 273184 [Multi-domain]  Cd Length: 925  Bit Score: 405.55  E-value: 5.64e-137
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2544519355   1 FNVKGGRCEACKGDGLIKVEMHFLPDIYVPCDVCHGNRYNRETLEITYKGKNISEVLDMTVEKAVVFFEPIPKIKQKLQT 80
Cdd:TIGR00630 733 FNVKGGRCEACQGDGVIKIEMHFLPDVYVPCEVCKGKRYNRETLEVKYKGKNIADVLDMTVEEAYEFFEAVPSISRKLQT 812
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2544519355  81 LMDVGLSYITLGQNATTLSGGEAQRIKLAKELSKLDTGQTLYILDEPTTGLHFHDIKQLLSVINRLRERENTIVIIEHNL 160
Cdd:TIGR00630 813 LCDVGLGYIRLGQPATTLSGGEAQRIKLAKELSKRSTGRTLYILDEPTTGLHFDDIKKLLEVLQRLVDKGNTVVVIEHNL 892
                         170       180       190
                  ....*....|....*....|....*....|...
gi 2544519355 161 DVIKTADWIVDVGPEGGDKGGHIVATGTPEKVS 193
Cdd:TIGR00630 893 DVIKTADYIIDLGPEGGDGGGTVVASGTPEEVA 925
ABC_UvrA_II cd03271
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair ...
31-189 9.61e-111

ATP-binding cassette domain II 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: 213238 [Multi-domain]  Cd Length: 261  Bit Score: 317.25  E-value: 9.61e-111
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2544519355  31 CDVCHGNRYNRETLEITYKGKNISEVLDMTVEKAVVFFEPIPKIKQKLQTLMDVGLSYITLGQNATTLSGGEAQRIKLAK 110
Cdd:cd03271   103 CEVCKGKRYNRETLEVRYKGKSIADVLDMTVEEALEFFENIPKIARKLQTLCDVGLGYIKLGQPATTLSGGEAQRIKLAK 182
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2544519355 111 ELSKLDTGQTLYILDEPTTGLHFHDIKQLLSVINRLRERENTIVIIEHNLDVIKTADWIVDVGPEGGDKGGHIVATGTP 189
Cdd:cd03271   183 ELSKRSTGKTLYILDEPTTGLHFHDVKKLLEVLQRLVDKGNTVVVIEHNLDVIKCADWIIDLGPEGGDGGGQVVASGTP 261
UvrA COG0178
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair];
28-204 2.02e-68

Excinuclease UvrABC ATPase subunit [Replication, recombination and repair];


Pssm-ID: 439948 [Multi-domain]  Cd Length: 941  Bit Score: 224.91  E-value: 2.02e-68
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2544519355  28 YVPCDVCHGNRYNRETLEITYKGKNISEVLDMTVEKAVVFFE-------------PIPK-IKQKLQTLMDVGLSYITLGQ 93
Cdd:COG0178   402 ETPCPACKGARLKPEALAVKIGGKNIAELTALSIDEALEFFEnleltereaeiaeRILKeIRSRLGFLVDVGLDYLTLDR 481
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2544519355  94 NATTLSGGEAQRIKLAKEL-SKLdTGqTLYILDEPTTGLHFHDIKQLLSVINRLRERENTIVIIEHNLDVIKTADWIVDV 172
Cdd:COG0178   482 SAGTLSGGEAQRIRLATQIgSGL-VG-VLYVLDEPSIGLHQRDNDRLIETLKRLRDLGNTVIVVEHDEDTIRAADYIIDI 559
                         170       180       190
                  ....*....|....*....|....*....|..
gi 2544519355 173 GPEGGDKGGHIVATGTPEKVSAVEGSYTGQYL 204
Cdd:COG0178   560 GPGAGEHGGEVVAQGTPEEILKNPDSLTGQYL 591
PRK00635 PRK00635
excinuclease ABC subunit A; Provisional
1-192 7.20e-64

excinuclease ABC subunit A; Provisional


Pssm-ID: 234806 [Multi-domain]  Cd Length: 1809  Bit Score: 213.54  E-value: 7.20e-64
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2544519355    1 FNVKGGRCEACKGDGLIKVEMHFLPdiyVPCDVCHGNRYNRETLEITYKGKNISEVLDMTVEKAVVFFEPIPKIKQKLQT 80
Cdd:PRK00635   716 FNTPLGACAECQGLGSITTTDNRTS---IPCPSCLGKRFLPQVLEVRYKGKNIADILEMTAYEAEKFFLDEPSIHEKIHA 792
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2544519355   81 LMDVGLSYITLGQNATTLSGGEAQRIKLAKELSKLDTGQTLYILDEPTTGLHFHDIKQLLSVINRLRERENTIVIIEHNL 160
Cdd:PRK00635   793 LCSLGLDYLPLGRPLSSLSGGEIQRLKLAYELLAPSKKPTLYVLDEPTTGLHTHDIKALIYVLQSLTHQGHTVVIIEHNM 872
                          170       180       190
                   ....*....|....*....|....*....|..
gi 2544519355  161 DVIKTADWIVDVGPEGGDKGGHIVATGTPEKV 192
Cdd:PRK00635   873 HVVKVADYVLELGPEGGNLGGYLLASCSPEEL 904
uvrA PRK00349
excinuclease ABC subunit UvrA;
29-204 6.36e-62

excinuclease ABC subunit UvrA;


Pssm-ID: 234734 [Multi-domain]  Cd Length: 943  Bit Score: 206.85  E-value: 6.36e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2544519355  29 VPCDVCHGNRYNRETLEITYKGKNISEVLDMTVEKAVVFFE-------------PIPK-IKQKLQTLMDVGLSYITLGQN 94
Cdd:PRK00349  407 RPCPSCKGKRLKPEALAVKVGGKNIGEVSELSIGEALEFFEnlklseqeakiaePILKeIRERLKFLVDVGLDYLTLSRS 486
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2544519355  95 ATTLSGGEAQRIKLAKEL-SKLdTGqTLYILDEPTTGLHFHDIKQLLSVINRLRERENTIVIIEHNLDVIKTADWIVDVG 173
Cdd:PRK00349  487 AGTLSGGEAQRIRLATQIgSGL-TG-VLYVLDEPSIGLHQRDNDRLIETLKHLRDLGNTLIVVEHDEDTIRAADYIVDIG 564
                         170       180       190
                  ....*....|....*....|....*....|.
gi 2544519355 174 PEGGDKGGHIVATGTPEKVSAVEGSYTGQYL 204
Cdd:PRK00349  565 PGAGVHGGEVVASGTPEEIMKNPNSLTGQYL 595
uvra TIGR00630
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ...
28-204 4.15e-58

excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of proteins of which all members for which functions are known except the UvrA proteins are involved in the transport of material through membranes. UvrA orthologs are involved in the recognition of DNA damage as a step in nucleotide excision repair. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]


Pssm-ID: 273184 [Multi-domain]  Cd Length: 925  Bit Score: 196.39  E-value: 4.15e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2544519355  28 YVPCDVCHGNRYNRETLEITYKGKNISEVLDMTVEKAVVFF-------------EPIPK-IKQKLQTLMDVGLSYITLGQ 93
Cdd:TIGR00630 405 ERPCPSCGGTRLKPEALAVTVGGKSIADVSELSIREAHEFFnqltltpeekkiaEEVLKeIRERLGFLIDVGLDYLSLSR 484
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2544519355  94 NATTLSGGEAQRIKLAKEL-SKLdTGqTLYILDEPTTGLHFHDIKQLLSVINRLRERENTIVIIEHNLDVIKTADWIVDV 172
Cdd:TIGR00630 485 AAGTLSGGEAQRIRLATQIgSGL-TG-VLYVLDEPSIGLHQRDNRRLINTLKRLRDLGNTLIVVEHDEDTIRAADYVIDI 562
                         170       180       190
                  ....*....|....*....|....*....|..
gi 2544519355 173 GPEGGDKGGHIVATGTPEKVSAVEGSYTGQYL 204
Cdd:TIGR00630 563 GPGAGEHGGEVVASGTPEEILANPDSLTGQYL 594
ABC_UvrA cd03238
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ...
77-187 7.01e-48

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: 154.79  E-value: 7.01e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2544519355  77 KLQTLMDVGLSYITLGQNATTLSGGEAQRIKLAKELSKlDTGQTLYILDEPTTGLHFHDIKQLLSVINRLRERENTIVII 156
Cdd:cd03238    67 QLQFLIDVGLGYLTLGQKLSTLSGGELQRVKLASELFS-EPPGTLFILDEPSTGLHQQDINQLLEVIKGLIDLGNTVILI 145
                          90       100       110
                  ....*....|....*....|....*....|.
gi 2544519355 157 EHNLDVIKTADWIVDVGPEGGDKGGHIVATG 187
Cdd:cd03238   146 EHNLDVLSSADWIIDFGPGSGKSGGKVVFSG 176
ABC_UvrA_I cd03270
ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair ...
74-187 1.25e-44

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: 148.17  E-value: 1.25e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2544519355  74 IKQKLQTLMDVGLSYITLGQNATTLSGGEAQRIKLAKEL-SKLdTGqTLYILDEPTTGLHFHDIKQLLSVINRLRERENT 152
Cdd:cd03270   114 IRERLGFLVDVGLGYLTLSRSAPTLSGGEAQRIRLATQIgSGL-TG-VLYVLDEPSIGLHPRDNDRLIETLKRLRDLGNT 191
                          90       100       110
                  ....*....|....*....|....*....|....*
gi 2544519355 153 IVIIEHNLDVIKTADWIVDVGPEGGDKGGHIVATG 187
Cdd:cd03270   192 VLVVEHDEDTIRAADHVIDIGPGAGVHGGEIVAQG 226
PRK00635 PRK00635
excinuclease ABC subunit A; Provisional
28-208 3.27e-38

excinuclease ABC subunit A; Provisional


Pssm-ID: 234806 [Multi-domain]  Cd Length: 1809  Bit Score: 139.96  E-value: 3.27e-38
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2544519355   28 YVPCDVCHGNRYNRETLEITYKGKNISEVLDMTVEKAVVFFEPIPK-----------IKQKLQTLMDVGLSYITLGQNAT 96
Cdd:PRK00635   396 ATSCPRCQGTGLGDYANAATWHGKTFAEFQQMSLQELFIFLSQLPSkslsieevlqgLKSRLSILIDLGLPYLTPERALA 475
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2544519355   97 TLSGGEAQRIKLAKELSKLDTGQTlYILDEPTTGLHFHDIKQLLSVINRLRERENTIVIIEHNLDVIKTADWIVDVGPEG 176
Cdd:PRK00635   476 TLSGGEQERTALAKHLGAELIGIT-YILDEPSIGLHPQDTHKLINVIKKLRDQGNTVLLVEHDEQMISLADRIIDIGPGA 554
                          170       180       190
                   ....*....|....*....|....*....|..
gi 2544519355  177 GDKGGHIVATGTPEKVSAVEGSYTGQYLKSYL 208
Cdd:PRK00635   555 GIFGGEVLFNGSPREFLAKSDSLTAKYLRQEL 586
PRK00635 PRK00635
excinuclease ABC subunit A; Provisional
2-208 3.46e-33

excinuclease ABC subunit A; Provisional


Pssm-ID: 234806 [Multi-domain]  Cd Length: 1809  Bit Score: 125.71  E-value: 3.46e-33
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2544519355    2 NVKGGRCEACKGDGLIKVEMHFLPDIYVPCDVCHGNRYNRETLEITYKGKNISEVLDMTVEKAVVFFEPIPKIKQKLQTL 81
Cdd:PRK00635  1604 NTKQGQCSDCWGLGYQWIDRAFYALEKRPCPTCSGFRIQPLAQEVVYEGKHFGQLLQTPIEEVAETFPFLKKIQKPLQAL 1683
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2544519355   82 MDVGLSYITLGQNATTLSGGEAQRIKLAKELSKLDTGQTLYILDEPTTGLHFHDIKQLLSVINRLRERENTIVIIEHNLD 161
Cdd:PRK00635  1684 IDNGLGYLPLGQNLSSLSLSEKIAIKIAKFLYLPPKHPTLFLLDEIATSLDNQQKSALLVQLRTLVSLGHSVIYIDHDPA 1763
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*..
gi 2544519355  162 VIKTADWIVDVGPEGGDKGGHIVATGTPEKVSAVEGSytgqYLKSYL 208
Cdd:PRK00635  1764 LLKQADYLIEMGPGSGKTGGKILFSGPPKDISASKDS----LLKTYM 1806
PRK00635 PRK00635
excinuclease ABC subunit A; Provisional
71-196 2.10e-21

excinuclease ABC subunit A; Provisional


Pssm-ID: 234806 [Multi-domain]  Cd Length: 1809  Bit Score: 91.43  E-value: 2.10e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2544519355   71 IPKIKQKLQTLMDVGLSYITLGQNATTLSGGEAQRIKLAKELSkldTGQT--LYILDEPTTGLHFHDIKQLLSVINRLRE 148
Cdd:PRK00635  1361 IQDLLNRLTFIDKVGLSYITLGQEQDTLSDGEHYRLHLAKKIS---SNLTdiIYLLEDPLSGLHPQDAPTLLQLIKELVT 1437
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*...
gi 2544519355  149 RENTIVIIEHNLDVIKTADWIVDVGPEGGDKGGHIVATgTPEKVSAVE 196
Cdd:PRK00635  1438 NNNTVIATDRSGSLAEHADHLIHLGPGSGPQGGYLLST-SALKQSQPD 1484
ABC_Class2 cd03227
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ...
84-175 4.38e-17

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: 75.09  E-value: 4.38e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2544519355  84 VGLSYITLGQNATTLSGGEAQRIKLAKELSKLDTGQ-TLYILDEPTTGLHFHDIKQLLSVINRLRERENTIVIIEHNLDV 162
Cdd:cd03227    64 VAAVSAELIFTRLQLSGGEKELSALALILALASLKPrPLYILDEIDRGLDPRDGQALAEAILEHLVKGAQVIVITHLPEL 143
                          90
                  ....*....|...
gi 2544519355 163 IKTADWIVDVGPE 175
Cdd:cd03227   144 AELADKLIHIKKV 156
CydD COG4988
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ...
91-197 2.71e-16

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: 76.34  E-value: 2.71e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2544519355  91 LGQNATTLSGGEAQRIKLAKELskLDTGQtLYILDEPTTGLhfhDI---KQLLSVINRLReRENTIVIIEHNLDVIKTAD 167
Cdd:COG4988   467 LGEGGRGLSGGQAQRLALARAL--LRDAP-LLLLDEPTAHL---DAeteAEILQALRRLA-KGRTVILITHRLALLAQAD 539
                          90       100       110
                  ....*....|....*....|....*....|
gi 2544519355 168 WIVDVgpeggdKGGHIVATGTPEKVSAVEG 197
Cdd:COG4988   540 RILVL------DDGRIVEQGTHEELLAKNG 563
ABC_cobalt_CbiO_domain1 cd03225
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ...
60-170 3.24e-16

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: 73.66  E-value: 3.24e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2544519355  60 TVEKAVVF-FE----PIPKIKQKLQTLMDVGLSYITLGQNATTLSGGEAQRIKLAkelSKLDTGQTLYILDEPTTGLHFH 134
Cdd:cd03225    92 TVEEEVAFgLEnlglPEEEIEERVEEALELVGLEGLRDRSPFTLSGGQKQRVAIA---GVLAMDPDILLLDEPTAGLDPA 168
                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 2544519355 135 DIKQLLSVINRLRERENTIVIIEHNLDVIKT-ADWIV 170
Cdd:cd03225   169 GRRELLELLKKLKAEGKTIIIVTHDLDLLLElADRVI 205
EcfA2 COG1122
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ...
79-192 6.29e-16

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: 73.14  E-value: 6.29e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2544519355  79 QTLMDVGLSYItLGQNATTLSGGEAQRIKLAkelSKLDTGQTLYILDEPTTGLHFHDIKQLLSVINRLRERENTIVIIEH 158
Cdd:COG1122   117 EALELVGLEHL-ADRPPHELSGGQKQRVAIA---GVLAMEPEVLVLDEPTAGLDPRGRRELLELLKRLNKEGKTVIIVTH 192
                          90       100       110
                  ....*....|....*....|....*....|....*
gi 2544519355 159 NLD-VIKTADWIVDVgpeggdKGGHIVATGTPEKV 192
Cdd:COG1122   193 DLDlVAELADRVIVL------DDGRIVADGTPREV 221
ABC_Metallic_Cations cd03235
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ...
55-170 1.32e-14

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: 69.48  E-value: 1.32e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2544519355  55 EVLDMTVEKAVVFFEPIPKI-KQKLQTLMD-VGLSYItLGQNATTLSGGEAQRIKLAKELSkldTGQTLYILDEPTTGLH 132
Cdd:cd03235    89 DVVLMGLYGHKGLFRRLSKAdKAKVDEALErVGLSEL-ADRQIGELSGGQQQRVLLARALV---QDPDLLLLDEPFAGVD 164
                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 2544519355 133 FHDIKQLLSVINRLRERENTIVIIEHNLD-VIKTADWIV 170
Cdd:cd03235   165 PKTQEDIYELLRELRREGMTILVVTHDLGlVLEYFDRVL 203
ABC_ATPase cd00267
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ...
98-172 1.48e-14

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: 68.04  E-value: 1.48e-14
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2544519355  98 LSGGEAQRIKLAKELSKLDTgqtLYILDEPTTGLHFHDIKQLLSVINRLRERENTIVIIEHNLDVIKTA-DWIVDV 172
Cdd:cd00267    81 LSGGQRQRVALARALLLNPD---LLLLDEPTSGLDPASRERLLELLRELAEEGRTVIIVTHDPELAELAaDRVIVL 153
CcmA COG1131
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
58-194 7.41e-14

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


Pssm-ID: 440746 [Multi-domain]  Cd Length: 236  Bit Score: 67.78  E-value: 7.41e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2544519355  58 DMTVEKAVVFF-----EPIPKIKQKLQTLMD-VGLSyITLGQNATTLSGGEAQRIKLAKELSkldtGQT-LYILDEPTTG 130
Cdd:COG1131    87 DLTVRENLRFFarlygLPRKEARERIDELLElFGLT-DAADRKVGTLSGGMKQRLGLALALL----HDPeLLILDEPTSG 161
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2544519355 131 LhfhD---IKQLLSVINRLRERENTIVIIEHNLDVI-KTADWIVDVgpeggdKGGHIVATGTPEKVSA 194
Cdd:COG1131   162 L---DpeaRRELWELLRELAAEGKTVLLSTHYLEEAeRLCDRVAII------DKGRIVADGTPDELKA 220
SunT COG2274
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ...
91-199 4.40e-13

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: 67.17  E-value: 4.40e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2544519355  91 LGQNATTLSGGEAQRIKLAkelskldtgQTLY------ILDEPTTGLhfhDIKQLLSVINRLREREN--TIVIIEHNLDV 162
Cdd:COG2274   605 VGEGGSNLSGGQRQRLAIA---------RALLrnprilILDEATSAL---DAETEAIILENLRRLLKgrTVIIIAHRLST 672
                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 2544519355 163 IKTADWIVDVgpeggdKGGHIVATGTPEKVSAVEGSY 199
Cdd:COG2274   673 IRLADRIIVL------DKGRIVEDGTHEELLARKGLY 703
GsiA COG1123
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ...
78-192 1.18e-12

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: 65.69  E-value: 1.18e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2544519355  78 LQTLMDVGLSYItLGQNATTLSGGEAQRIKLAkelSKLDTGQTLYILDEPTTGLHFHDIKQLLSVINRL-RERENTIVII 156
Cdd:COG1123   124 LELLEAVGLERR-LDRYPHQLSGGQRQRVAIA---MALALDPDLLIADEPTTALDVTTQAEILDLLRELqRERGTTVLLI 199
                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 2544519355 157 EHNLDVI-KTADWIVDVgpeggdKGGHIVATGTPEKV 192
Cdd:COG1123   200 THDLGVVaEIADRVVVM------DDGRIVEDGPPEEI 230
GsiA COG1123
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ...
59-192 2.52e-12

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: 64.92  E-value: 2.52e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2544519355  59 MTVEKAVVF----FEPIPK--IKQKLQTLMD-VGLSYITLGQNATTLSGGEAQRIKLAKELSkldTGQTLYILDEPTTGL 131
Cdd:COG1123   359 MTVGDIIAEplrlHGLLSRaeRRERVAELLErVGLPPDLADRYPHELSGGQRQRVAIARALA---LEPKLLILDEPTSAL 435
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2544519355 132 hfhDIK---QLLSVINRLREREN-TIVIIEHNLDVIKT-ADWIVDVgpeggdKGGHIVATGTPEKV 192
Cdd:COG1123   436 ---DVSvqaQILNLLRDLQRELGlTYLFISHDLAVVRYiADRVAVM------YDGRIVEDGPTEEV 492
ABC_Carb_Monos_I cd03216
First domain of the ATP-binding cassette component of monosaccharide transport system; This ...
98-170 4.30e-12

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: 61.68  E-value: 4.30e-12
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2544519355  98 LSGGEAQRIKLAKELSkldTGQTLYILDEPTTGLHFHDIKQLLSVINRLRERENTIVIIEHNLD-VIKTADWIV 170
Cdd:cd03216    83 LSVGERQMVEIARALA---RNARLLILDEPTAALTPAEVERLFKVIRRLRAQGVAVIFISHRLDeVFEIADRVT 153
ABC_MTABC3_MDL1_MDL2 cd03249
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ...
91-199 2.16e-11

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: 61.02  E-value: 2.16e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2544519355  91 LGQNATTLSGGEAQRIKLAKELSKldtGQTLYILDEPTTGLHFHDIKQLLSVINRLReRENTIVIIEHNLDVIKTADWIV 170
Cdd:cd03249   133 VGERGSQLSGGQKQRIAIARALLR---NPKILLLDEATSALDAESEKLVQEALDRAM-KGRTTIVIAHRLSTIRNADLIA 208
                          90       100
                  ....*....|....*....|....*....
gi 2544519355 171 DVGpeggdkGGHIVATGTPEKVSAVEGSY 199
Cdd:cd03249   209 VLQ------NGQVVEQGTHDELMAQKGVY 231
ABC_Iron-Siderophores_B12_Hemin cd03214
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ...
78-187 2.64e-11

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: 59.76  E-value: 2.64e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2544519355  78 LQTLMDVGLSYItLGQNATTLSGGEAQRIKLAKELskldTGQT-LYILDEPTTGLhfhDIK---QLLSVINRL-RERENT 152
Cdd:cd03214    79 PQALELLGLAHL-ADRPFNELSGGERQRVLLARAL----AQEPpILLLDEPTSHL---DIAhqiELLELLRRLaRERGKT 150
                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 2544519355 153 IVIIEHNLD-VIKTADWIVDVgpeggdKGGHIVATG 187
Cdd:cd03214   151 VVMVLHDLNlAARYADRVILL------KDGRIVAQG 180
ABC_Mj1267_LivG_branched cd03219
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ...
95-194 5.84e-11

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: 59.76  E-value: 5.84e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2544519355  95 ATTLSGGEAQRIKLAKELSkldTGQTLYILDEPTTGLHFHDIKQLLSVINRLRERENTIVIIEHNLDVIKT-ADWIV--D 171
Cdd:cd03219   141 AGELSYGQQRRLEIARALA---TDPKLLLLDEPAAGLNPEETEELAELIRELRERGITVLLVEHDMDVVMSlADRVTvlD 217
                          90       100
                  ....*....|....*....|...
gi 2544519355 172 vgpeggdkGGHIVATGTPEKVSA 194
Cdd:cd03219   218 --------QGRVIAEGTPDEVRN 232
FetA COG4619
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
45-164 6.76e-11

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


Pssm-ID: 443661 [Multi-domain]  Cd Length: 209  Bit Score: 59.06  E-value: 6.76e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2544519355  45 EITYKGKNISEV------------------LDMTVEKAVVF---FEPIPKIKQKLQTLMD-VGLSYITLGQNATTLSGGE 102
Cdd:COG4619    56 EIYLDGKPLSAMpppewrrqvayvpqepalWGGTVRDNLPFpfqLRERKFDRERALELLErLGLPPDILDKPVERLSGGE 135
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2544519355 103 AQRIKLAKELSkldTGQTLYILDEPTTGLhfhDIK---QLLSVINRLREREN-TIVIIEHNLDVIK 164
Cdd:COG4619   136 RQRLALIRALL---LQPDVLLLDEPTSAL---DPEntrRVEELLREYLAEEGrAVLWVSHDPEQIE 195
cbiO PRK13646
energy-coupling factor transporter ATPase;
54-192 2.40e-10

energy-coupling factor transporter ATPase;


Pssm-ID: 184205 [Multi-domain]  Cd Length: 286  Bit Score: 58.64  E-value: 2.40e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2544519355  54 SEVLDMTVEKAVVF----FE-PIPKIKQK-LQTLMDVGLSYITLGQNATTLSGGEAQRIKLakeLSKLDTGQTLYILDEP 127
Cdd:PRK13646   96 SQLFEDTVEREIIFgpknFKmNLDEVKNYaHRLLMDLGFSRDVMSQSPFQMSGGQMRKIAI---VSILAMNPDIIVLDEP 172
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2544519355 128 TTGLHFHDIKQLLSVINRLREREN-TIVIIEHNL-DVIKTADWIVDVgpeggdKGGHIVATGTPEKV 192
Cdd:PRK13646  173 TAGLDPQSKRQVMRLLKSLQTDENkTIILVSHDMnEVARYADEVIVM------KEGSIVSQTSPKEL 233
PRK11174 PRK11174
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
85-197 2.68e-10

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


Pssm-ID: 236870 [Multi-domain]  Cd Length: 588  Bit Score: 59.09  E-value: 2.68e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2544519355  85 GLSYiTLGQNATTLSGGEAQRIKLAKELskLDTGQtLYILDEPTTGLHFHDIKQLLSVINRLRERENTIvIIEHNLDVIK 164
Cdd:PRK11174  474 GLDT-PIGDQAAGLSVGQAQRLALARAL--LQPCQ-LLLLDEPTASLDAHSEQLVMQALNAASRRQTTL-MVTHQLEDLA 548
                          90       100       110
                  ....*....|....*....|....*....|....*
gi 2544519355 165 TAD--WIVDvgpeggdkGGHIVATGTPEKVSAVEG 197
Cdd:PRK11174  549 QWDqiWVMQ--------DGQIVQQGDYAELSQAGG 575
PRK13409 PRK13409
ribosome biogenesis/translation initiation ATPase RLI;
91-208 3.58e-10

ribosome biogenesis/translation initiation ATPase RLI;


Pssm-ID: 184037 [Multi-domain]  Cd Length: 590  Bit Score: 58.67  E-value: 3.58e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2544519355  91 LGQNATTLSGGEAQRIKLAKELSKlDTgqTLYILDEPTTGLhfhDIKQLLSVINRLRE--RENTIVIIEHNLDVIktaDW 168
Cdd:PRK13409  206 LDRDISELSGGELQRVAIAAALLR-DA--DFYFFDEPTSYL---DIRQRLNVARLIRElaEGKYVLVVEHDLAVL---DY 276
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 2544519355 169 IVDVgpeggdkgGHIVaTGTPE---KVSAVEGSYTG--QYLKSYL 208
Cdd:PRK13409  277 LADN--------VHIA-YGEPGaygVVSKPKGVRVGinEYLKGYL 312
PRK10535 PRK10535
macrolide ABC transporter ATP-binding protein/permease MacB;
98-198 4.10e-10

macrolide ABC transporter ATP-binding protein/permease MacB;


Pssm-ID: 182528 [Multi-domain]  Cd Length: 648  Bit Score: 58.58  E-value: 4.10e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2544519355  98 LSGGEAQRIKLAKELskLDTGQTLyILDEPTTGLHFHDIKQLLSVINRLRERENTIVIIEHNLDVIKTADWIVDVgpegg 177
Cdd:PRK10535  145 LSGGQQQRVSIARAL--MNGGQVI-LADEPTGALDSHSGEEVMAILHQLRDRGHTVIIVTHDPQVAAQAERVIEI----- 216
                          90       100
                  ....*....|....*....|.
gi 2544519355 178 dKGGHIVATGTPEKVSAVEGS 198
Cdd:PRK10535  217 -RDGEIVRNPPAQEKVNVAGG 236
ABCC_SUR1_N cd03290
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ...
24-170 4.42e-10

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: 56.96  E-value: 4.42e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2544519355  24 LPDIYVPCDVCHGNRYNretleITYKGKNiSEVLDMTVEKAVVFFEPIPKIKQK-------LQTLMDVgLSY---ITLGQ 93
Cdd:cd03290    64 NESEPSFEATRSRNRYS-----VAYAAQK-PWLLNATVEENITFGSPFNKQRYKavtdacsLQPDIDL-LPFgdqTEIGE 136
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2544519355  94 NATTLSGGEAQRIKLAKELSKldtGQTLYILDEPTTGLHFHDIKQLLS--VINRLRERENTIVIIEHNLDVIKTADWIV 170
Cdd:cd03290   137 RGINLSGGQRQRICVARALYQ---NTNIVFLDDPFSALDIHLSDHLMQegILKFLQDDKRTLVLVTHKLQYLPHADWII 212
CydD TIGR02857
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ...
91-172 5.95e-10

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: 58.07  E-value: 5.95e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2544519355  91 LGQNATTLSGGEAQRIKLAKELskLDTGQTLyILDEPTTGLHFHDIKQLLSVINRLREREnTIVIIEHNLDVIKTADWIV 170
Cdd:TIGR02857 452 IGEGGAGLSGGQAQRLALARAF--LRDAPLL-LLDEPTAHLDAETEAEVLEALRALAQGR-TVLLVTHRLALAALADRIV 527

                  ..
gi 2544519355 171 DV 172
Cdd:TIGR02857 528 VL 529
ABC_cobalt_CbiO_domain2 cd03226
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ...
69-170 1.03e-09

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: 55.73  E-value: 1.03e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2544519355  69 EPIPKIKQKLQTLM-DVGLSYITLgQNATTLSGGEAQRIKLAkelSKLDTGQTLYILDEPTTGLHFHDIKQLLSVINRLR 147
Cdd:cd03226    98 KELDAGNEQAETVLkDLDLYALKE-RHPLSLSGGQKQRLAIA---AALLSGKDLLIFDEPTSGLDYKNMERVGELIRELA 173
                          90       100
                  ....*....|....*....|....
gi 2544519355 148 ERENTIVIIEHNLDVI-KTADWIV 170
Cdd:cd03226   174 AQGKAVIVITHDYEFLaKVCDRVL 197
MdlB COG1132
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
91-199 1.20e-09

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


Pssm-ID: 440747 [Multi-domain]  Cd Length: 579  Bit Score: 57.10  E-value: 1.20e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2544519355  91 LGQNATTLSGGEAQRIKLAKELSKlDTGqtLYILDEPTTGLhfhDIK---QLLSVINRLReRENTIVIIEHNLDVIKTAD 167
Cdd:COG1132   470 VGERGVNLSGGQRQRIAIARALLK-DPP--ILILDEATSAL---DTEteaLIQEALERLM-KGRTTIVIAHRLSTIRNAD 542
                          90       100       110
                  ....*....|....*....|....*....|..
gi 2544519355 168 WIVDVgpeggdKGGHIVATGTPEKVSAVEGSY 199
Cdd:COG1132   543 RILVL------DDGRIVEQGTHEELLARGGLY 568
PRK13409 PRK13409
ribosome biogenesis/translation initiation ATPase RLI;
43-171 1.41e-09

ribosome biogenesis/translation initiation ATPase RLI;


Pssm-ID: 184037 [Multi-domain]  Cd Length: 590  Bit Score: 56.74  E-value: 1.41e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2544519355  43 TLEITYKGKNISEVLDMTVEKavvFFEPIPK----------IKQKLQ--TLMDvglsyitlgQNATTLSGGEAQRIKLAK 110
Cdd:PRK13409  399 ELKISYKPQYIKPDYDGTVED---LLRSITDdlgssyykseIIKPLQleRLLD---------KNVKDLSGGELQRVAIAA 466
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2544519355 111 ELSK-LDtgqtLYILDEPTTGLhfhDIKQLLSV---INRL-RERENTIVIIEHNLDVIktaDWIVD 171
Cdd:PRK13409  467 CLSRdAD----LYLLDEPSAHL---DVEQRLAVakaIRRIaEEREATALVVDHDIYMI---DYISD 522
ABCC_Protease_Secretion cd03246
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ...
98-172 1.58e-09

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: 54.92  E-value: 1.58e-09
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2544519355  98 LSGGEAQRIKLAKELSKldtGQTLYILDEPTTGLHFHDIKQLLSVINRLRERENTIVIIEHNLDVIKTADWIVDV 172
Cdd:cd03246    97 LSGGQRQRLGLARALYG---NPRILVLDEPNSHLDVEGERALNQAIAALKAAGATRIVIAHRPETLASADRILVL 168
ABC_TM1139_LivF_branched cd03224
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ...
91-194 2.44e-09

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: 55.13  E-value: 2.44e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2544519355  91 LGQNATTLSGGEAQRIKLAKELSkldTGQTLYILDEPTTGLHFHDIKQLLSVINRLRERENTIVIIEHNLDVI-KTAD-- 167
Cdd:cd03224   126 RKQLAGTLSGGEQQMLAIARALM---SRPKLLLLDEPSEGLAPKIVEEIFEAIRELRDEGVTILLVEQNARFAlEIADra 202
                          90       100
                  ....*....|....*....|....*..
gi 2544519355 168 WIVDvgpeggdkGGHIVATGTPEKVSA 194
Cdd:cd03224   203 YVLE--------RGRVVLEGTAAELLA 221
ArpD COG4618
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ...
91-192 2.63e-09

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: 55.91  E-value: 2.63e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2544519355  91 LGQNATTLSGGEAQRIKLAKelskldtgqTLY------ILDEPTTGLhfhD---IKQLLSVINRLRERENTIVIIEHNLD 161
Cdd:COG4618   461 IGEGGARLSGGQRQRIGLAR---------ALYgdprlvVLDEPNSNL---DdegEAALAAAIRALKARGATVVVITHRPS 528
                          90       100       110
                  ....*....|....*....|....*....|.
gi 2544519355 162 VIKTADWIVDVgpeggdKGGHIVATGTPEKV 192
Cdd:COG4618   529 LLAAVDKLLVL------RDGRVQAFGPRDEV 553
ABCC_Hemolysin cd03252
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ...
91-199 2.70e-09

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: 55.18  E-value: 2.70e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2544519355  91 LGQNATTLSGGEAQRIKLAKELSkldTGQTLYILDEPTTGLHF---HDIKQLLSVINRLRerenTIVIIEHNLDVIKTAD 167
Cdd:cd03252   132 VGEQGAGLSGGQRQRIAIARALI---HNPRILIFDEATSALDYeseHAIMRNMHDICAGR----TVIIIAHRLSTVKNAD 204
                          90       100       110
                  ....*....|....*....|....*....|..
gi 2544519355 168 WIVDVgpeggdKGGHIVATGTPEKVSAVEGSY 199
Cdd:cd03252   205 RIIVM------EKGRIVEQGSHDELLAENGLY 230
ABCC_MRP_Like cd03228
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ...
98-170 2.75e-09

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: 53.93  E-value: 2.75e-09
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2544519355  98 LSGGEAQRIKLAKEL---SKldtgqtLYILDEPTTGLhfhDI---KQLLSVINRLReRENTIVIIEHNLDVIKTADWIV 170
Cdd:cd03228    97 LSGGQRQRIAIARALlrdPP------ILILDEATSAL---DPeteALILEALRALA-KGKTVIVIAHRLSTIRDADRII 165
PRK11176 PRK11176
lipid A ABC transporter ATP-binding protein/permease MsbA;
82-199 3.27e-09

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


Pssm-ID: 183016 [Multi-domain]  Cd Length: 582  Bit Score: 55.80  E-value: 3.27e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2544519355  82 MDVGLSYItLGQNATTLSGGEAQRIKLAKELskLDTGQTLyILDEPTTGLHFHDIKQLLSVINRLReRENTIVIIEHNLD 161
Cdd:PRK11176  466 MDNGLDTV-IGENGVLLSGGQRQRIAIARAL--LRDSPIL-ILDEATSALDTESERAIQAALDELQ-KNRTSLVIAHRLS 540
                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 2544519355 162 VIKTADWIVDVgpeggdKGGHIVATGTPEKVSAVEGSY 199
Cdd:PRK11176  541 TIEKADEILVV------EDGEIVERGTHAELLAQNGVY 572
NatA COG4555
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ...
93-197 3.28e-09

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: 54.86  E-value: 3.28e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2544519355  93 QNATTLSGGEAQRIKLAKELSKlDTgqTLYILDEPTTGLHFHDIKQLLSVINRLRERENTIVIIEHNLDVI-KTADWIVD 171
Cdd:COG4555   128 RRVGELSTGMKKKVALARALVH-DP--KVLLLDEPTNGLDVMARRLLREILRALKKEGKTVLFSSHIMQEVeALCDRVVI 204
                          90       100
                  ....*....|....*....|....*.
gi 2544519355 172 VgpeggdKGGHIVATGTPEKVSAVEG 197
Cdd:COG4555   205 L------HKGKVVAQGSLDELREEIG 224
PTZ00265 PTZ00265
multidrug resistance protein (mdr1); Provisional
54-169 3.85e-09

multidrug resistance protein (mdr1); Provisional


Pssm-ID: 240339 [Multi-domain]  Cd Length: 1466  Bit Score: 55.81  E-value: 3.85e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2544519355   54 SEVLDmtVEKAVVFFEPIPKIKQKLQTLmdvglsyitLGQNATTLSGGEAQRIKLAKELSKldtGQTLYILDEPTTGLHF 133
Cdd:PTZ00265   547 SEVVD--VSKKVLIHDFVSALPDKYETL---------VGSNASKLSGGQKQRISIARAIIR---NPKILILDEATSSLDN 612
                           90       100       110
                   ....*....|....*....|....*....|....*..
gi 2544519355  134 HDIKQLLSVINRLRERENTI-VIIEHNLDVIKTADWI 169
Cdd:PTZ00265   613 KSEYLVQKTINNLKGNENRItIIIAHRLSTIRYANTI 649
ABC_NikE_OppD_transporters cd03257
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ...
59-187 4.40e-09

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: 54.43  E-value: 4.40e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2544519355  59 MTVEKAVVffEPIP----------KIKQKLQTLMDVGLSYITLGQNATTLSGGEAQRIKLAKELSkldTGQTLYILDEPT 128
Cdd:cd03257    99 MTIGEQIA--EPLRihgklskkeaRKEAVLLLLVGVGLPEEVLNRYPHELSGGQRQRVAIARALA---LNPKLLIADEPT 173
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2544519355 129 TGLhfhDIK---QLLSVINRLREREN-TIVIIEHNLDVIK-TADWIVDVgpeggdKGGHIVATG 187
Cdd:cd03257   174 SAL---DVSvqaQILDLLKKLQEELGlTLLFITHDLGVVAkIADRVAVM------YAGKIVEEG 228
PRK10247 PRK10247
putative ABC transporter ATP-binding protein YbbL; Provisional
72-178 4.71e-09

putative ABC transporter ATP-binding protein YbbL; Provisional


Pssm-ID: 182331 [Multi-domain]  Cd Length: 225  Bit Score: 54.33  E-value: 4.71e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2544519355  72 PKIKQKLQTLMDVGLSYITLGQNATTLSGGEAQRIKLAKELSKLDtgQTLyILDEPTTGLHFHDIKQLLSVINRLREREN 151
Cdd:PRK10247  112 PDPAIFLDDLERFALPDTILTKNIAELSGGEKQRISLIRNLQFMP--KVL-LLDEITSALDESNKHNVNEIIHRYVREQN 188
                          90       100
                  ....*....|....*....|....*...
gi 2544519355 152 TIVI-IEHNLDVIKTADWIVDVGPEGGD 178
Cdd:PRK10247  189 IAVLwVTHDKDEINHADKVITLQPHAGE 216
btuD PRK09536
corrinoid ABC transporter ATPase; Reviewed
93-192 5.39e-09

corrinoid ABC transporter ATPase; Reviewed


Pssm-ID: 236554 [Multi-domain]  Cd Length: 402  Bit Score: 54.85  E-value: 5.39e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2544519355  93 QNATTLSGGEAQRIKLAKELSKldtgQT-LYILDEPTTGLHFHDIKQLLSVINRLRERENTIVIIEHNLDV-IKTADWIV 170
Cdd:PRK09536  135 RPVTSLSGGERQRVLLARALAQ----ATpVLLLDEPTASLDINHQVRTLELVRRLVDDGKTAVAAIHDLDLaARYCDELV 210
                          90       100
                  ....*....|....*....|..
gi 2544519355 171 DVGpeggdkGGHIVATGTPEKV 192
Cdd:PRK09536  211 LLA------DGRVRAAGPPADV 226
cbiO PRK13634
cobalt transporter ATP-binding subunit; Provisional
60-192 6.03e-09

cobalt transporter ATP-binding subunit; Provisional


Pssm-ID: 237454 [Multi-domain]  Cd Length: 290  Bit Score: 54.64  E-value: 6.03e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2544519355  60 TVEKAVVF----FE-PIPKIKQKLQTLMD-VGLSYITLGQNATTLSGGEAQRIKLAKELSkLDTgQTLyILDEPTTGLHF 133
Cdd:PRK13634  102 TVEKDICFgpmnFGvSEEDAKQKAREMIElVGLPEELLARSPFELSGGQMRRVAIAGVLA-MEP-EVL-VLDEPTAGLDP 178
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2544519355 134 HDIKQLLSVINRL-RERENTIVIIEHNL-DVIKTADWIVdVGPEGGdkgghIVATGTPEKV 192
Cdd:PRK13634  179 KGRKEMMEMFYKLhKEKGLTTVLVTHSMeDAARYADQIV-VMHKGT-----VFLQGTPREI 233
ABCC_ATM1_transporter cd03253
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ...
91-199 7.05e-09

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: 53.77  E-value: 7.05e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2544519355  91 LGQNATTLSGGEAQRIKLAKELSKldtGQTLYILDEPTTGLHFHDIKQLLSVINRLRERENTIViIEHNLDVIKTADWIV 170
Cdd:cd03253   131 VGERGLKLSGGEKQRVAIARAILK---NPPILLLDEATSALDTHTEREIQAALRDVSKGRTTIV-IAHRLSTIVNADKII 206
                          90       100
                  ....*....|....*....|....*....
gi 2544519355 171 DVgpeggdKGGHIVATGTPEKVSAVEGSY 199
Cdd:cd03253   207 VL------KDGRIVERGTHEELLAKGGLY 229
ABC_YhbG cd03218
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ...
31-192 7.17e-09

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: 53.70  E-value: 7.17e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2544519355  31 CDVCHGNRYNRETLEITYKGKNISEVLDMTVE---KAVVFFEPIPK--IKQKLQTLM-DVGLSYItLGQNATTLSGGEAQ 104
Cdd:cd03218    62 QDITKLPMHKRARLGIGYLPQEASIFRKLTVEeniLAVLEIRGLSKkeREEKLEELLeEFHITHL-RKSKASSLSGGERR 140
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2544519355 105 RIKLAKELSkldTGQTLYILDEPTTG---LHFHDIKQLlsvINRLRERENTIVIIEHN----LDVIKTADWIVDvgpegg 177
Cdd:cd03218   141 RVEIARALA---TNPKFLLLDEPFAGvdpIAVQDIQKI---IKILKDRGIGVLITDHNvretLSITDRAYIIYE------ 208
                         170
                  ....*....|....*
gi 2544519355 178 dkgGHIVATGTPEKV 192
Cdd:cd03218   209 ---GKVLAEGTPEEI 220
ABC_RNaseL_inhibitor_domain2 cd03237
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ...
77-171 7.78e-09

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: 53.95  E-value: 7.78e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2544519355  77 KLQTLMDvglsyitlgQNATTLSGGEAQRIKLAKELSKlDTgqTLYILDEPTTGLhfhDIKQLL---SVINRLREREN-T 152
Cdd:cd03237   104 QIEQILD---------REVPELSGGELQRVAIAACLSK-DA--DIYLLDEPSAYL---DVEQRLmasKVIRRFAENNEkT 168
                          90
                  ....*....|....*....
gi 2544519355 153 IVIIEHnlDVIkTADWIVD 171
Cdd:cd03237   169 AFVVEH--DII-MIDYLAD 184
fecE PRK11231
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
96-192 1.16e-08

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


Pssm-ID: 183044 [Multi-domain]  Cd Length: 255  Bit Score: 53.48  E-value: 1.16e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2544519355  96 TTLSGGEAQRIKLAKELSKlDTgqTLYILDEPTTGLHFHDIKQLLSVINRLRERENTIVIIEHNLD-VIKTADWIVDVgp 174
Cdd:PRK11231  137 TDLSGGQRQRAFLAMVLAQ-DT--PVVLLDEPTTYLDINHQVELMRLMRELNTQGKTVVTVLHDLNqASRYCDHLVVL-- 211
                          90
                  ....*....|....*...
gi 2544519355 175 eggdKGGHIVATGTPEKV 192
Cdd:PRK11231  212 ----ANGHVMAQGTPEEV 225
Rli1 COG1245
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ...
42-171 1.27e-08

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: 54.02  E-value: 1.27e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2544519355  42 ETLEITYKGKNISEVLDMTVEkaVVFFEPIPK----------IKQKLQ--TLMDvglsyitlgQNATTLSGGEAQRIKLA 109
Cdd:COG1245   399 EDLKISYKPQYISPDYDGTVE--EFLRSANTDdfgssyykteIIKPLGleKLLD---------KNVKDLSGGELQRVAIA 467
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2544519355 110 KELSK-LDtgqtLYILDEPTTGLhfhDIKQLLSV---INRL-RERENTIVIIEHNLDVIktaDWIVD 171
Cdd:COG1245   468 ACLSRdAD----LYLLDEPSAHL---DVEQRLAVakaIRRFaENRGKTAMVVDHDIYLI---DYISD 524
ABC_DR_subfamily_A cd03230
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ...
98-170 1.33e-08

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: 52.40  E-value: 1.33e-08
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2544519355  98 LSGGEAQRIKLAKELSkldTGQTLYILDEPTTGLhfhDIK---QLLSVINRLRERENTIVIIEHNLDVI-KTADWIV 170
Cdd:cd03230    96 LSGGMKQRLALAQALL---HDPELLILDEPTSGL---DPEsrrEFWELLRELKKEGKTILLSSHILEEAeRLCDRVA 166
ABCC_MsbA cd03251
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ...
91-203 1.36e-08

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: 53.00  E-value: 1.36e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2544519355  91 LGQNATTLSGGEAQRIKLAKELSKldtGQTLYILDEPTTGLHFHDIKQLLSVINRLRERENTIViIEHNLDVIKTADWIV 170
Cdd:cd03251   132 IGERGVKLSGGQRQRIAIARALLK---DPPILILDEATSALDTESERLVQAALERLMKNRTTFV-IAHRLSTIENADRIV 207
                          90       100       110
                  ....*....|....*....|....*....|...
gi 2544519355 171 DVgpeggDKGGhIVATGTPEKVSAVEGSYTGQY 203
Cdd:cd03251   208 VL-----EDGK-IVERGTHEELLAQGGVYAKLH 234
ABC_Org_Solvent_Resistant cd03261
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ...
98-192 1.70e-08

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: 52.89  E-value: 1.70e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2544519355  98 LSGGEAQRIKLAKELSkLDTgqTLYILDEPTTGLH---FHDIKQLlsvINRLREREN-TIVIIEHNLD-VIKTADWIVDV 172
Cdd:cd03261   137 LSGGMKKRVALARALA-LDP--ELLLYDEPTAGLDpiaSGVIDDL---IRSLKKELGlTSIMVTHDLDtAFAIADRIAVL 210
                          90       100
                  ....*....|....*....|
gi 2544519355 173 GpeggdkGGHIVATGTPEKV 192
Cdd:cd03261   211 Y------DGKIVAEGTPEEL 224
MglA COG1129
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
73-193 1.95e-08

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


Pssm-ID: 440745 [Multi-domain]  Cd Length: 497  Bit Score: 53.48  E-value: 1.95e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2544519355  73 KIKQKLQTLMD-VGLSyITLGQNATTLSGGEAQRIKLAKELSKldtGQTLYILDEPTTGLHFHDIKQLLSVINRLREREN 151
Cdd:COG1129   116 AMRRRARELLArLGLD-IDPDTPVGDLSVAQQQLVEIARALSR---DARVLILDEPTASLTEREVERLFRIIRRLKAQGV 191
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 2544519355 152 TIVIIEHNLD-VIKTADWIV---DvgpeggdkgGHIVATGTPEKVS 193
Cdd:COG1129   192 AIIYISHRLDeVFEIADRVTvlrD---------GRLVGTGPVAELT 228
livF PRK11614
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
38-201 1.96e-08

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


Pssm-ID: 183231 [Multi-domain]  Cd Length: 237  Bit Score: 52.57  E-value: 1.96e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2544519355  38 RYNRETLEITYKGKNISEvlDMTVEKAVV---FFEPIPKIKQKLQTLMDVGLS-YITLGQNATTLSGGEAQRIKLAKELS 113
Cdd:PRK11614   76 KIMREAVAIVPEGRRVFS--RMTVEENLAmggFFAERDQFQERIKWVYELFPRlHERRIQRAGTMSGGEQQMLAIGRALM 153
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2544519355 114 kldTGQTLYILDEPTTGLHFHDIKQLLSVINRLRERENTIVIIEHNLD-VIKTAD--WIVDvgpeggdkGGHIVATGTPE 190
Cdd:PRK11614  154 ---SQPRLLLLDEPSLGLAPIIIQQIFDTIEQLREQGMTIFLVEQNANqALKLADrgYVLE--------NGHVVLEDTGD 222
                         170
                  ....*....|....
gi 2544519355 191 KV---SAVEGSYTG 201
Cdd:PRK11614  223 ALlanEAVRSAYLG 236
cbiO PRK13644
energy-coupling factor transporter ATPase;
60-192 2.07e-08

energy-coupling factor transporter ATPase;


Pssm-ID: 106587 [Multi-domain]  Cd Length: 274  Bit Score: 53.07  E-value: 2.07e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2544519355  60 TVEKAVVFFEP---IPKIKqkLQTLMDVGLSYITLGQ----NATTLSGGEAQRIKLAKELSkldTGQTLYILDEPTTGLH 132
Cdd:PRK13644   94 TVEEDLAFGPEnlcLPPIE--IRKRVDRALAEIGLEKyrhrSPKTLSGGQGQCVALAGILT---MEPECLIFDEVTSMLD 168
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 2544519355 133 FHDIKQLLSVINRLRERENTIVIIEHNLDVIKTADWIVDVgpeggDKgGHIVATGTPEKV 192
Cdd:PRK13644  169 PDSGIAVLERIKKLHEKGKTIVYITHNLEELHDADRIIVM-----DR-GKIVLEGEPENV 222
ABCC_cytochrome_bd cd03247
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ...
45-170 2.42e-08

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: 51.55  E-value: 2.42e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2544519355  45 EITYKGKNISEVLDmTVEKAVVFfepipkIKQKlqtlmdVGLSYITLGQN-ATTLSGGEAQRIKLAKELSKlDTgqTLYI 123
Cdd:cd03247    58 EITLDGVPVSDLEK-ALSSLISV------LNQR------PYLFDTTLRNNlGRRFSGGERQRLALARILLQ-DA--PIVL 121
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 2544519355 124 LDEPTTGLHFHDIKQLLSVI-NRLRERenTIVIIEHNLDVIKTADWIV 170
Cdd:cd03247   122 LDEPTVGLDPITERQLLSLIfEVLKDK--TLIWITHHLTGIEHMDKIL 167
Rli1 COG1245
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ...
48-208 2.74e-08

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: 52.86  E-value: 2.74e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2544519355  48 YKGKnISEVLDMTVEKAVVffepiPKIKQKLqtlmdvGLSYItLGQNATTLSGGEAQRIKLAKELSKlDTgqTLYILDEP 127
Cdd:COG1245   176 FKGT-VRELLEKVDERGKL-----DELAEKL------GLENI-LDRDISELSGGELQRVAIAAALLR-DA--DFYFFDEP 239
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2544519355 128 TTGLhfhDIKQLLSV---INRLRERENTIVIIEHNLDVIktaDWIVDVgpeggdkgGHIVaTGTPE---KVSAVEGSYTG 201
Cdd:COG1245   240 SSYL---DIYQRLNVarlIRELAEEGKYVLVVEHDLAIL---DYLADY--------VHIL-YGEPGvygVVSKPKSVRVG 304

                  ....*....
gi 2544519355 202 --QYLKSYL 208
Cdd:COG1245   305 inQYLDGYL 313
cbiO PRK13649
energy-coupling factor transporter ATPase;
54-192 2.96e-08

energy-coupling factor transporter ATPase;


Pssm-ID: 184208 [Multi-domain]  Cd Length: 280  Bit Score: 52.44  E-value: 2.96e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2544519355  54 SEVLDMTVEKAVVF----FEPIPKIKQKL--QTLMDVGLSYITLGQNATTLSGGEAQRIKLAkelSKLDTGQTLYILDEP 127
Cdd:PRK13649   96 SQLFEETVLKDVAFgpqnFGVSQEEAEALarEKLALVGISESLFEKNPFELSGGQMRRVAIA---GILAMEPKILVLDEP 172
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2544519355 128 TTGLHFHDIKQLLSVINRLRERENTIVIIEHNL-DVIKTADWIVDVgpeggdKGGHIVATGTPEKV 192
Cdd:PRK13649  173 TAGLDPKGRKELMTLFKKLHQSGMTIVLVTHLMdDVANYADFVYVL------EKGKLVLSGKPKDI 232
hmuV PRK13548
hemin importer ATP-binding subunit; Provisional
96-192 3.53e-08

hemin importer ATP-binding subunit; Provisional


Pssm-ID: 237422 [Multi-domain]  Cd Length: 258  Bit Score: 52.08  E-value: 3.53e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2544519355  96 TTLSGGEAQRIKLAKELSKL----DTGQTLyILDEPTTGL---HFHDIKQLLSviNRLRERENTIVIIEHNLDV-IKTAD 167
Cdd:PRK13548  133 PQLSGGEQQRVQLARVLAQLwepdGPPRWL-LLDEPTSALdlaHQHHVLRLAR--QLAHERGLAVIVVLHDLNLaARYAD 209
                          90       100
                  ....*....|....*....|....*
gi 2544519355 168 WIVDVgpeggdKGGHIVATGTPEKV 192
Cdd:PRK13548  210 RIVLL------HQGRLVADGTPAEV 228
ABCF_EF-3 cd03221
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ...
98-176 8.08e-08

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: 49.37  E-value: 8.08e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2544519355  98 LSGGEAQRIKLAKELSKldtGQTLYILDEPTTGLhfhDIKQLLSVINRLRERENTIVIIEHNLDVI-KTADWIVDVGPEG 176
Cdd:cd03221    71 LSGGEKMRLALAKLLLE---NPNLLLLDEPTNHL---DLESIEALEEALKEYPGTVILVSHDRYFLdQVATKIIELEDGK 144
ABC_FeS_Assembly cd03217
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ...
45-190 8.69e-08

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: 50.22  E-value: 8.69e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2544519355  45 EITYKGKNIsevLDMTV-EKA-----VVFFEP--IPKIKqklqtLMDVgLSYITLGqnattLSGGEAQRIKLAkELSKLD 116
Cdd:cd03217    58 EILFKGEDI---TDLPPeERArlgifLAFQYPpeIPGVK-----NADF-LRYVNEG-----FSGGEKKRNEIL-QLLLLE 122
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2544519355 117 TgqTLYILDEPTTGLHFHDIKQLLSVINRLRERENTIVIIEHN---LDVIKTadwivdvgpeggDKG-----GHIVATGT 188
Cdd:cd03217   123 P--DLAILDEPDSGLDIDALRLVAEVINKLREEGKSVLIITHYqrlLDYIKP------------DRVhvlydGRIVKSGD 188

                  ..
gi 2544519355 189 PE 190
Cdd:cd03217   189 KE 190
cbiO PRK13640
energy-coupling factor transporter ATPase;
60-192 8.89e-08

energy-coupling factor transporter ATPase;


Pssm-ID: 184200 [Multi-domain]  Cd Length: 282  Bit Score: 50.95  E-value: 8.89e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2544519355  60 TVEKAVVF-FE----PIPKIKQKL-QTLMDVG-LSYITlgQNATTLSGGEAQRIKLAKELSkldTGQTLYILDEPTTGLH 132
Cdd:PRK13640  101 TVGDDVAFgLEnravPRPEMIKIVrDVLADVGmLDYID--SEPANLSGGQKQRVAIAGILA---VEPKIIILDESTSMLD 175
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2544519355 133 FHDIKQLLSVINRLREREN-TIVIIEHNLDVIKTADWIVDVgpeggDKgGHIVATGTPEKV 192
Cdd:PRK13640  176 PAGKEQILKLIRKLKKKNNlTVISITHDIDEANMADQVLVL-----DD-GKLLAQGSPVEI 230
ModF COG1119
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ...
58-192 9.69e-08

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: 50.85  E-value: 9.69e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2544519355  58 DMTVEKAVV--FF-------EPIPKIKQKLQTLMD-VGLSYItLGQNATTLSGGEAQRIKLAKELSKldtGQTLYILDEP 127
Cdd:COG1119    94 DETVLDVVLsgFFdsiglyrEPTDEQRERARELLElLGLAHL-ADRPFGTLSQGEQRRVLIARALVK---DPELLILDEP 169
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2544519355 128 TTGLHFHDIKQLLSVINRLREREN-TIVIIEHNLDVIktadwivdvgPEGGD-----KGGHIVATGTPEKV 192
Cdd:COG1119   170 TAGLDLGARELLLALLDKLAAEGApTLVLVTHHVEEI----------PPGIThvlllKDGRVVAAGPKEEV 230
ABC_RNaseL_inhibitor_domain1 cd03236
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ...
47-172 1.42e-07

The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI), is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI s are not transport proteins and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLIs have an N-terminal Fe-S domain and two nucleotide binding domains which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.


Pssm-ID: 213203 [Multi-domain]  Cd Length: 255  Bit Score: 50.44  E-value: 1.42e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2544519355  47 TYKGKnISEVLDMTVEKAvvffepipkikqKLQTLMDV-GLSYItLGQNATTLSGGEAQRIKLAKELSKldtGQTLYILD 125
Cdd:cd03236   102 AVKGK-VGELLKKKDERG------------KLDELVDQlELRHV-LDRNIDQLSGGELQRVAIAAALAR---DADFYFFD 164
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 2544519355 126 EPTTGLhfhDIKQLLS---VINRLRERENTIVIIEHNLDVIktaDWIVDV 172
Cdd:cd03236   165 EPSSYL---DIKQRLNaarLIRELAEDDNYVLVVEHDLAVL---DYLSDY 208
PRK03695 PRK03695
vitamin B12-transporter ATPase; Provisional
91-192 1.50e-07

vitamin B12-transporter ATPase; Provisional


Pssm-ID: 235150 [Multi-domain]  Cd Length: 248  Bit Score: 50.32  E-value: 1.50e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2544519355  91 LGQNATTLSGGEAQRIKLAKEL----SKLDTGQTLYILDEPTTGLhfhDIKQ---LLSVINRLRERENTIVIIEHNLD-V 162
Cdd:PRK03695  120 LGRSVNQLSGGEWQRVRLAAVVlqvwPDINPAGQLLLLDEPMNSL---DVAQqaaLDRLLSELCQQGIAVVMSSHDLNhT 196
                          90       100       110
                  ....*....|....*....|....*....|..
gi 2544519355 163 IKTAD--WIVdvgpeggdKGGHIVATGTPEKV 192
Cdd:PRK03695  197 LRHADrvWLL--------KQGKLLASGRRDEV 220
MlaF COG1127
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ...
98-204 1.62e-07

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: 49.98  E-value: 1.62e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2544519355  98 LSGGEAQRIKLAKELSkLDTgqTLYILDEPTTGLhfhD------IKQLlsvINRLREREN-TIVIIEHNLD-VIKTADWI 169
Cdd:COG1127   142 LSGGMRKRVALARALA-LDP--EILLYDEPTAGL---DpitsavIDEL---IRELRDELGlTSVVVTHDLDsAFAIADRV 212
                          90       100       110
                  ....*....|....*....|....*....|....*
gi 2544519355 170 VDVgpeggdKGGHIVATGTPEKVSAVEGSYTGQYL 204
Cdd:COG1127   213 AVL------ADGKIIAEGTPEELLASDDPWVRQFL 241
cbiO PRK13631
cobalt transporter ATP-binding subunit; Provisional
60-192 1.88e-07

cobalt transporter ATP-binding subunit; Provisional


Pssm-ID: 237451 [Multi-domain]  Cd Length: 320  Bit Score: 50.23  E-value: 1.88e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2544519355  60 TVEKAVVFfEPI----PKIKQKLQT---LMDVGLSYITLGQNATTLSGGEAQRIKLAKELSkldTGQTLYILDEPTTGLH 132
Cdd:PRK13631  133 TIEKDIMF-GPValgvKKSEAKKLAkfyLNKMGLDDSYLERSPFGLSGGQKRRVAIAGILA---IQPEILIFDEPTAGLD 208
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2544519355 133 FHDIKQLLSVINRLRERENTIVIIEHNLD-VIKTADWIVDVgpeggDKgGHIVATGTPEKV 192
Cdd:PRK13631  209 PKGEHEMMQLILDAKANNKTVFVITHTMEhVLEVADEVIVM-----DK-GKILKTGTPYEI 263
ABC_ModC_like cd03299
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ...
59-192 2.49e-07

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: 49.26  E-value: 2.49e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2544519355  59 MTVEKAVVF-----FEPIPKIKQK-LQTLMDVGLSYItLGQNATTLSGGEAQRIKLAKELSkldTGQTLYILDEPTTGLH 132
Cdd:cd03299    86 MTVYKNIAYglkkrKVDKKEIERKvLEIAEMLGIDHL-LNRKPETLSGGEQQRVAIARALV---VNPKILLLDEPFSALD 161
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2544519355 133 FHDIKQLLSVINRLRERENTIVI-IEHNLDVIKT-ADWIVDVgpeggdKGGHIVATGTPEKV 192
Cdd:cd03299   162 VRTKEKLREELKKIRKEFGVTVLhVTHDFEEAWAlADKVAIM------LNGKLIQVGKPEEV 217
Uup COG0488
ATPase components of ABC transporters with duplicated ATPase domains [General function ...
79-172 2.51e-07

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


Pssm-ID: 440254 [Multi-domain]  Cd Length: 520  Bit Score: 50.06  E-value: 2.51e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2544519355  79 QTLMDVGLSYITLGQNATTLSGGEAQRIKLAKEL-SKLDtgqtLYILDEPTTGLhfhDIKqllSVI---NRLRERENTIV 154
Cdd:COG0488   134 EILSGLGFPEEDLDRPVSELSGGWRRRVALARALlSEPD----LLLLDEPTNHL---DLE---SIEwleEFLKNYPGTVL 203
                          90       100
                  ....*....|....*....|.
gi 2544519355 155 IIEHN---LDviKTADWIVDV 172
Cdd:COG0488   204 VVSHDryfLD--RVATRILEL 222
cbiO PRK13648
cobalt transporter ATP-binding subunit; Provisional
97-192 2.78e-07

cobalt transporter ATP-binding subunit; Provisional


Pssm-ID: 184207 [Multi-domain]  Cd Length: 269  Bit Score: 49.36  E-value: 2.78e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2544519355  97 TLSGGEAQRIKLAkelSKLDTGQTLYILDEPTTGLHFHDIKQLLSVINRLREREN-TIVIIEHNLDVIKTADWIVDVGPe 175
Cdd:PRK13648  142 ALSGGQKQRVAIA---GVLALNPSVIILDEATSMLDPDARQNLLDLVRKVKSEHNiTIISITHDLSEAMEADHVIVMNK- 217
                          90
                  ....*....|....*..
gi 2544519355 176 ggdkgGHIVATGTPEKV 192
Cdd:PRK13648  218 -----GTVYKEGTPTEI 229
PRK10253 PRK10253
iron-enterobactin ABC transporter ATP-binding protein;
92-196 3.17e-07

iron-enterobactin ABC transporter ATP-binding protein;


Pssm-ID: 182336 [Multi-domain]  Cd Length: 265  Bit Score: 49.21  E-value: 3.17e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2544519355  92 GQNATTLSGGEAQRIKLAKELSKldtGQTLYILDEPTTGL---HFHDIKQLLSVINrlRERENTIVIIEHNLD-VIKTAD 167
Cdd:PRK10253  138 DQSVDTLSGGQRQRAWIAMVLAQ---ETAIMLLDEPTTWLdisHQIDLLELLSELN--REKGYTLAAVLHDLNqACRYAS 212
                          90       100
                  ....*....|....*....|....*....
gi 2544519355 168 WIVDVgpeggdKGGHIVATGTPEKVSAVE 196
Cdd:PRK10253  213 HLIAL------REGKIVAQGAPKEIVTAE 235
NupO COG3845
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ...
59-194 3.35e-07

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


Pssm-ID: 443055 [Multi-domain]  Cd Length: 504  Bit Score: 49.64  E-value: 3.35e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2544519355  59 MTV--------EKAVVFFEPIPKIKQKLQTLMD-VGLSyITLGQNATTLSGGEAQRIKLAKelskldtgqTLY------I 123
Cdd:COG3845    95 LTVaenivlglEPTKGGRLDRKAARARIRELSErYGLD-VDPDAKVEDLSVGEQQRVEILK---------ALYrgarilI 164
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2544519355 124 LDEPTTGLHFHDIKQLLSVINRLRERENTIVIIEHNLDVIKT-ADWIVDVgpeggdKGGHIVATGTPEKVSA 194
Cdd:COG3845   165 LDEPTAVLTPQEADELFEILRRLAAEGKSIIFITHKLREVMAiADRVTVL------RRGKVVGTVDTAETSE 230
cbiO PRK13652
cobalt transporter ATP-binding subunit; Provisional
98-192 5.78e-07

cobalt transporter ATP-binding subunit; Provisional


Pssm-ID: 172200 [Multi-domain]  Cd Length: 277  Bit Score: 48.65  E-value: 5.78e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2544519355  98 LSGGEAQRIKLAKELSKldTGQTLyILDEPTTGLHFHDIKQLLSVINRLREREN-TIVIIEHNLDVI-KTADWIVDVgpe 175
Cdd:PRK13652  138 LSGGEKKRVAIAGVIAM--EPQVL-VLDEPTAGLDPQGVKELIDFLNDLPETYGmTVIFSTHQLDLVpEMADYIYVM--- 211
                          90
                  ....*....|....*..
gi 2544519355 176 ggDKgGHIVATGTPEKV 192
Cdd:PRK13652  212 --DK-GRIVAYGTVEEI 225
ABCC_MRP_domain1 cd03250
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ...
92-170 6.12e-07

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: 47.85  E-value: 6.12e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2544519355  92 GQNATTLSGGEAQRIKLAKEL-SKLDtgqtLYILDEPTTGLHFHDIKQLL-SVINRLRERENTIVIIEHNLDVIKTADWI 169
Cdd:cd03250   122 GEKGINLSGGQKQRISLARAVySDAD----IYLLDDPLSAVDAHVGRHIFeNCILGLLLNNKTRILVTHQLQLLPHADQI 197

                  .
gi 2544519355 170 V 170
Cdd:cd03250   198 V 198
znuC PRK09544
high-affinity zinc transporter ATPase; Reviewed
98-194 6.52e-07

high-affinity zinc transporter ATPase; Reviewed


Pssm-ID: 181939 [Multi-domain]  Cd Length: 251  Bit Score: 48.19  E-value: 6.52e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2544519355  98 LSGGEAQRIKLAKELskLDTGQTLyILDEPTTGLHFHDIKQLLSVINRLREREN-TIVIIEHNLD-VIKTADWIVDVgpe 175
Cdd:PRK09544  121 LSGGETQRVLLARAL--LNRPQLL-VLDEPTQGVDVNGQVALYDLIDQLRRELDcAVLMVSHDLHlVMAKTDEVLCL--- 194
                          90
                  ....*....|....*....
gi 2544519355 176 ggdkGGHIVATGTPEKVSA 194
Cdd:PRK09544  195 ----NHHICCSGTPEVVSL 209
DppD COG0444
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ...
98-170 6.98e-07

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: 48.51  E-value: 6.98e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2544519355  98 LSGGEAQRIKLAKELS---KLdtgqtLyILDEPTTGLhfhDI---KQLLSVINRLREREN-TIVIIEHNLDVIK-TADWI 169
Cdd:COG0444   151 LSGGMRQRVMIARALAlepKL-----L-IADEPTTAL---DVtiqAQILNLLKDLQRELGlAILFITHDLGVVAeIADRV 221

                  .
gi 2544519355 170 V 170
Cdd:COG0444   222 A 222
cbiO PRK13635
energy-coupling factor ABC transporter ATP-binding protein;
98-192 8.00e-07

energy-coupling factor ABC transporter ATP-binding protein;


Pssm-ID: 184195 [Multi-domain]  Cd Length: 279  Bit Score: 48.09  E-value: 8.00e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2544519355  98 LSGGEAQRIKLAKELSkldTGQTLYILDEPTTGLHFHDIKQLLSVINRLRERENTIVI-IEHNLDVIKTADWIVDVgpeg 176
Cdd:PRK13635  141 LSGGQKQRVAIAGVLA---LQPDIIILDEATSMLDPRGRREVLETVRQLKEQKGITVLsITHDLDEAAQADRVIVM---- 213
                          90
                  ....*....|....*.
gi 2544519355 177 gdKGGHIVATGTPEKV 192
Cdd:PRK13635  214 --NKGEILEEGTPEEI 227
ABC_PhnC_transporter cd03256
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ...
66-194 8.48e-07

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: 47.95  E-value: 8.48e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2544519355  66 VFFEPIPKI-KQK-LQTLMDVGLS-YITlgQNATTLSGGEAQRIKLAKELSKldtGQTLYILDEPTTGLHFHDIKQLLSV 142
Cdd:cd03256   112 SLFGLFPKEeKQRaLAALERVGLLdKAY--QRADQLSGGQQQRVAIARALMQ---QPKLILADEPVASLDPASSRQVMDL 186
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 2544519355 143 INRLRERENTIVIIE-HNLDVIKT-ADWIVdvgpegGDKGGHIVATGTPEKVSA 194
Cdd:cd03256   187 LKRINREEGITVIVSlHQVDLAREyADRIV------GLKDGRIVFDGPPAELTD 234
PRK10895 PRK10895
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
90-196 9.04e-07

lipopolysaccharide ABC transporter ATP-binding protein; Provisional


Pssm-ID: 182817 [Multi-domain]  Cd Length: 241  Bit Score: 47.97  E-value: 9.04e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2544519355  90 TLGQnatTLSGGEAQRIKLAKELSkldTGQTLYILDEPTTGLHFHDIKQLLSVINRLRERENTIVIIEHN----LDVIKT 165
Cdd:PRK10895  133 SMGQ---SLSGGERRRVEIARALA---ANPKFILLDEPFAGVDPISVIDIKRIIEHLRDSGLGVLITDHNvretLAVCER 206
                          90       100       110
                  ....*....|....*....|....*....|.
gi 2544519355 166 AdWIVdvgpeggdKGGHIVATGTPEKVSAVE 196
Cdd:PRK10895  207 A-YIV--------SQGHLIAHGTPTEILQDE 228
CydC TIGR02868
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ...
91-160 9.69e-07

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: 48.51  E-value: 9.69e-07
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2544519355  91 LGQNATTLSGGEAQRIKLAKELSkldTGQTLYILDEPTTGLHFHDIKQLLSVINRLrERENTIVIIEHNL 160
Cdd:TIGR02868 465 LGEGGARLSGGERQRLALARALL---ADAPILLLDEPTEHLDAETADELLEDLLAA-LSGRTVVLITHHL 530
PRK13549 PRK13549
xylose transporter ATP-binding subunit; Provisional
98-164 1.14e-06

xylose transporter ATP-binding subunit; Provisional


Pssm-ID: 184134 [Multi-domain]  Cd Length: 506  Bit Score: 48.00  E-value: 1.14e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2544519355  98 LSGGEAQRIKLAKELSKldtGQTLYILDEPTTGLHFHDIKQLLSVINRLRERENTIVIIEHNLDVIK 164
Cdd:PRK13549  144 LGLGQQQLVEIAKALNK---QARLLILDEPTASLTESETAVLLDIIRDLKAHGIACIYISHKLNEVK 207
ABC_tran pfam00005
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ...
78-129 1.51e-06

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: 46.10  E-value: 1.51e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 2544519355  78 LQTLMDVGLSYITLGQNATTLSGGEAQRIKLAKELSkldTGQTLYILDEPTT 129
Cdd:pfam00005 102 LEKLGLGDLADRPVGERPGTLSGGQRQRVAIARALL---TKPKLLLLDEPTA 150
PRK13651 PRK13651
cobalt transporter ATP-binding subunit; Provisional
84-161 1.51e-06

cobalt transporter ATP-binding subunit; Provisional


Pssm-ID: 184210 [Multi-domain]  Cd Length: 305  Bit Score: 47.39  E-value: 1.51e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2544519355  84 VGLSYITLGQNATTLSGGEAQRIKLAKELS-KLDtgqtLYILDEPTTGLHFHDIKQLLSVINRLRERENTIVIIEHNLD 161
Cdd:PRK13651  152 VGLDESYLQRSPFELSGGQKRRVALAGILAmEPD----FLVFDEPTAGLDPQGVKEILEIFDNLNKQGKTIILVTHDLD 226
hmuV PRK13547
heme ABC transporter ATP-binding protein;
91-192 1.52e-06

heme ABC transporter ATP-binding protein;


Pssm-ID: 184132 [Multi-domain]  Cd Length: 272  Bit Score: 47.51  E-value: 1.52e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2544519355  91 LGQNATTLSGGEAQRIKLAKELSKL------DTGQTLYILDEPTTGLHFHDIKQLLSVINRL-RERENTIVIIEHNLDV- 162
Cdd:PRK13547  139 VGRDVTTLSGGELARVQFARVLAQLwpphdaAQPPRYLLLDEPTAALDLAHQHRLLDTVRRLaRDWNLGVLAIVHDPNLa 218
                          90       100       110
                  ....*....|....*....|....*....|
gi 2544519355 163 IKTADWIVDVGpeggdkGGHIVATGTPEKV 192
Cdd:PRK13547  219 ARHADRIAMLA------DGAIVAHGAPADV 242
cbiO PRK13645
energy-coupling factor transporter ATPase;
60-189 1.57e-06

energy-coupling factor transporter ATPase;


Pssm-ID: 184204 [Multi-domain]  Cd Length: 289  Bit Score: 47.31  E-value: 1.57e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2544519355  60 TVEKAVVFfEPI------PKIKQKLQTLMD-VGLSYITLGQNATTLSGGEAQRIKLAKELSkLDtGQTLyILDEPTTGLH 132
Cdd:PRK13645  107 TIEKDIAF-GPVnlgenkQEAYKKVPELLKlVQLPEDYVKRSPFELSGGQKRRVALAGIIA-MD-GNTL-VLDEPTGGLD 182
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 2544519355 133 FHDIKQLLSVINRL-RERENTIVIIEHNLD-VIKTADWIVdVGPEggdkgGHIVATGTP 189
Cdd:PRK13645  183 PKGEEDFINLFERLnKEYKKRIIMVTHNMDqVLRIADEVI-VMHE-----GKVISIGSP 235
cbiO PRK13643
energy-coupling factor transporter ATPase;
54-192 2.11e-06

energy-coupling factor transporter ATPase;


Pssm-ID: 184203 [Multi-domain]  Cd Length: 288  Bit Score: 47.04  E-value: 2.11e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2544519355  54 SEVLDMTVEKAVVF----FEPIPKIKQKL--QTLMDVGLSYITLGQNATTLSGGEAQRIKLAKELSkldTGQTLYILDEP 127
Cdd:PRK13643   95 SQLFEETVLKDVAFgpqnFGIPKEKAEKIaaEKLEMVGLADEFWEKSPFELSGGQMRRVAIAGILA---MEPEVLVLDEP 171
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2544519355 128 TTGLHFHDIKQLLSVINRLRERENTIVIIEHNL-DVIKTADWIVDVgpeggdKGGHIVATGTPEKV 192
Cdd:PRK13643  172 TAGLDPKARIEMMQLFESIHQSGQTVVLVTHLMdDVADYADYVYLL------EKGHIISCGTPSDV 231
cbiO PRK13637
energy-coupling factor transporter ATPase;
74-192 2.24e-06

energy-coupling factor transporter ATPase;


Pssm-ID: 237455 [Multi-domain]  Cd Length: 287  Bit Score: 46.96  E-value: 2.24e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2544519355  74 IKQKLQTLMD-VGLSYITL-GQNATTLSGGEAQRIKLAKELSkldTGQTLYILDEPTTGLHFHDIKQLLSVINRLRER-E 150
Cdd:PRK13637  119 IENRVKRAMNiVGLDYEDYkDKSPFELSGGQKRRVAIAGVVA---MEPKILILDEPTAGLDPKGRDEILNKIKELHKEyN 195
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 2544519355 151 NTIVIIEHNL-DVIKTADWIVDVgpeggdKGGHIVATGTPEKV 192
Cdd:PRK13637  196 MTIILVSHSMeDVAKLADRIIVM------NKGKCELQGTPREV 232
ABC_Carb_Monos_II cd03215
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ...
90-170 2.37e-06

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: 45.89  E-value: 2.37e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2544519355  90 TLGQNATT---LSGGEAQRIKLAKELSkldTGQTLYILDEPTTGLHFHDIKQLLSVINRLRERENTIVIIEHNLD-VIKT 165
Cdd:cd03215    94 SVAENIALsslLSGGNQQKVVLARWLA---RDPRVLILDEPTRGVDVGAKAEIYRLIRELADAGKAVLLISSELDeLLGL 170

                  ....*
gi 2544519355 166 ADWIV 170
Cdd:cd03215   171 CDRIL 175
ycf16 CHL00131
sulfate ABC transporter protein; Validated
40-164 2.39e-06

sulfate ABC transporter protein; Validated


Pssm-ID: 214372 [Multi-domain]  Cd Length: 252  Bit Score: 46.56  E-value: 2.39e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2544519355  40 NRETLEITYKGKNISEVLDMTveKAVVFFEpipKIKQKLQTlmdVGLSYITLGQNATT-LSGGEAQRIKLAkELSKLDTg 118
Cdd:CHL00131  101 NADFLRLAYNSKRKFQGLPEL--DPLEFLE---IINEKLKL---VGMDPSFLSRNVNEgFSGGEKKRNEIL-QMALLDS- 170
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 2544519355 119 qTLYILDEPTTGLHFHDIKQLLSVINRLRERENTIVIIEHN---LDVIK 164
Cdd:CHL00131  171 -ELAILDETDSGLDIDALKIIAEGINKLMTSENSIILITHYqrlLDYIK 218
PhnL COG4778
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ...
96-174 2.67e-06

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: 46.27  E-value: 2.67e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2544519355  96 TTLSGGEAQRIKLAKELSKldtGQTLYILDEPTTGLHFHDIKQLLSVINRLRERENTIVIIEHNLDVIKT-ADWIVDVGP 174
Cdd:COG4778   151 ATFSGGEQQRVNIARGFIA---DPPLLLLDEPTASLDAANRAVVVELIEEAKARGTAIIGIFHDEEVREAvADRVVDVTP 227
PRK15134 PRK15134
microcin C ABC transporter ATP-binding protein YejF; Provisional
98-164 2.80e-06

microcin C ABC transporter ATP-binding protein YejF; Provisional


Pssm-ID: 237917 [Multi-domain]  Cd Length: 529  Bit Score: 47.01  E-value: 2.80e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2544519355  98 LSGGEAQRIKLAKELSkldTGQTLYILDEPTTGLHFHDIKQLLSVINRLREREN-TIVIIEHNLDVIK 164
Cdd:PRK15134  157 LSGGERQRVMIAMALL---TRPELLIADEPTTALDVSVQAQILQLLRELQQELNmGLLFITHNLSIVR 221
bacteriocin_ABC TIGR01193
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ...
71-199 3.10e-06

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: 47.04  E-value: 3.10e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2544519355  71 IPKIKQKLQTlmdvglsyiTLGQNATTLSGGEAQRIKLAKELskLDTGQTLyILDEPTTGLHFHDIKQLLSviNRLRERE 150
Cdd:TIGR01193 594 IENMPLGYQT---------ELSEEGSSISGGQKQRIALARAL--LTDSKVL-ILDESTSNLDTITEKKIVN--NLLNLQD 659
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 2544519355 151 NTIVIIEHNLDVIKTADWIVDVgpeggDKGGhIVATGTPEKVSAVEGSY 199
Cdd:TIGR01193 660 KTIIFVAHRLSVAKQSDKIIVL-----DHGK-IIEQGSHDELLDRNGFY 702
artP PRK11124
arginine transporter ATP-binding subunit; Provisional
98-205 4.37e-06

arginine transporter ATP-binding subunit; Provisional


Pssm-ID: 182980 [Multi-domain]  Cd Length: 242  Bit Score: 45.78  E-value: 4.37e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2544519355  98 LSGGEAQRIKLAKELskLDTGQTLyILDEPTTGLHFHDIKQLLSVINRLRERENTIVIIEHNLDVI-KTADWIVDVgpeg 176
Cdd:PRK11124  142 LSGGQQQRVAIARAL--MMEPQVL-LFDEPTAALDPEITAQIVSIIRELAETGITQVIVTHEVEVArKTASRVVYM---- 214
                          90       100
                  ....*....|....*....|....*....
gi 2544519355 177 gdKGGHIVATGTPEKVSAVEGSYTGQYLK 205
Cdd:PRK11124  215 --ENGHIVEQGDASCFTQPQTEAFKNYLS 241
ABC_MetN_methionine_transporter cd03258
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ...
73-164 4.90e-06

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: 45.65  E-value: 4.90e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2544519355  73 KIKQKLQTLMD-VGLS-----YITlgqnatTLSGGEAQRIKLAKELSkldTGQTLYILDEPTTGLH---FHDIKQLLSVI 143
Cdd:cd03258   116 EIEERVLELLElVGLEdkadaYPA------QLSGGQKQRVGIARALA---NNPKVLLCDEATSALDpetTQSILALLRDI 186
                          90       100
                  ....*....|....*....|.
gi 2544519355 144 NRlrERENTIVIIEHNLDVIK 164
Cdd:cd03258   187 NR--ELGLTIVLITHEMEVVK 205
PTZ00265 PTZ00265
multidrug resistance protein (mdr1); Provisional
91-205 4.97e-06

multidrug resistance protein (mdr1); Provisional


Pssm-ID: 240339 [Multi-domain]  Cd Length: 1466  Bit Score: 46.56  E-value: 4.97e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2544519355   91 LGQNATTLSGGEAQRIKLAKELSKldtGQTLYILDEPTTGLHFHDIKQLLSVINRLRER-ENTIVIIEHNLDVIKTADWI 169
Cdd:PTZ00265  1352 VGPYGKSLSGGQKQRIAIARALLR---EPKILLLDEATSSLDSNSEKLIEKTIVDIKDKaDKTIITIAHRIASIKRSDKI 1428
                           90       100       110
                   ....*....|....*....|....*....|....*..
gi 2544519355  170 VDVgpEGGDKGGHIV-ATGTPEKVSAVEGSYTGQYLK 205
Cdd:PTZ00265  1429 VVF--NNPDRTGSFVqAHGTHEELLSVQDGVYKKYVK 1463
PRK11160 PRK11160
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
78-199 5.37e-06

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


Pssm-ID: 236865 [Multi-domain]  Cd Length: 574  Bit Score: 46.36  E-value: 5.37e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2544519355  78 LQTLMDVGLSYIT---------LGQNATTLSGGEAQRIKLAKELskLDTGQtLYILDEPTTGLHFHDIKQLLSVinrLRE 148
Cdd:PRK11160  447 IEVLQQVGLEKLLeddkglnawLGEGGRQLSGGEQRRLGIARAL--LHDAP-LLLLDEPTEGLDAETERQILEL---LAE 520
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 2544519355 149 --RENTIVIIEHNLDVIKTADWIV--DvgpeggdkGGHIVATGTPEKVSAVEGSY 199
Cdd:PRK11160  521 haQNKTVLMITHRLTGLEQFDRICvmD--------NGQIIEQGTHQELLAQQGRY 567
PRK10790 PRK10790
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
91-203 5.63e-06

SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;


Pssm-ID: 182733 [Multi-domain]  Cd Length: 592  Bit Score: 46.25  E-value: 5.63e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2544519355  91 LGQNATTLSGGEAQRIKLAKELskLDTGQTLyILDEPTTGLHF---HDIKQLLSVInrlREReNTIVIIEHNLDVIKTAD 167
Cdd:PRK10790  470 LGEQGNNLSVGQKQLLALARVL--VQTPQIL-ILDEATANIDSgteQAIQQALAAV---REH-TTLVVIAHRLSTIVEAD 542
                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 2544519355 168 WIVDVgpeggdKGGHIVATGTPEKVSAVEGSYTGQY 203
Cdd:PRK10790  543 TILVL------HRGQAVEQGTHQQLLAAQGRYWQMY 572
ABC_MJ0796_LolCDE_FtsE cd03255
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ...
72-170 6.22e-06

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: 45.17  E-value: 6.22e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2544519355  72 PKIKQKLQTLMD-VGLSYItLGQNATTLSGGEAQRIKLAKELskldTGQTLYIL-DEPTTGLHFHDIKQLLSVINRL-RE 148
Cdd:cd03255   115 KERRERAEELLErVGLGDR-LNHYPSELSGGQQQRVAIARAL----ANDPKIILaDEPTGNLDSETGKEVMELLRELnKE 189
                          90       100
                  ....*....|....*....|..
gi 2544519355 149 RENTIVIIEHNLDVIKTADWIV 170
Cdd:cd03255   190 AGTTIVVVTHDPELAEYADRII 211
ABC_RNaseL_inhibitor cd03222
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ...
98-163 9.80e-06

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: 44.10  E-value: 9.80e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2544519355  98 LSGGEAQRIKLAKELSKldtGQTLYILDEPTTGLhfhDIKQLLS---VINRLRER-ENTIVIIEHNLDVI 163
Cdd:cd03222    72 LSGGELQRVAIAAALLR---NATFYLFDEPSAYL---DIEQRLNaarAIRRLSEEgKKTALVVEHDLAVL 135
PRK10575 PRK10575
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
97-192 1.02e-05

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


Pssm-ID: 182561 [Multi-domain]  Cd Length: 265  Bit Score: 44.78  E-value: 1.02e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2544519355  97 TLSGGEAQRIKLAKELSKldtGQTLYILDEPTTGLHFHDIKQLLSVINRL-RERENTIVIIEHNLDV-IKTADWIVDVgp 174
Cdd:PRK10575  147 SLSGGERQRAWIAMLVAQ---DSRCLLLDEPTSALDIAHQVDVLALVHRLsQERGLTVIAVLHDINMaARYCDYLVAL-- 221
                          90
                  ....*....|....*...
gi 2544519355 175 eggdKGGHIVATGTPEKV 192
Cdd:PRK10575  222 ----RGGEMIAQGTPAEL 235
PRK15134 PRK15134
microcin C ABC transporter ATP-binding protein YejF; Provisional
76-164 1.15e-05

microcin C ABC transporter ATP-binding protein YejF; Provisional


Pssm-ID: 237917 [Multi-domain]  Cd Length: 529  Bit Score: 45.08  E-value: 1.15e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2544519355  76 QKLQTLMDVGLSYITLGQNATTLSGGEAQRIKLAKELSkldTGQTLYILDEPTTGLHFHDIKQLLSVINRLRERENTIVI 155
Cdd:PRK15134  404 QVIAVMEEVGLDPETRHRYPAEFSGGQRQRIAIARALI---LKPSLIILDEPTSSLDKTVQAQILALLKSLQQKHQLAYL 480
                          90
                  ....*....|
gi 2544519355 156 -IEHNLDVIK 164
Cdd:PRK15134  481 fISHDLHVVR 490
PRK14258 PRK14258
phosphate ABC transporter ATP-binding protein; Provisional
57-160 1.23e-05

phosphate ABC transporter ATP-binding protein; Provisional


Pssm-ID: 184593 [Multi-domain]  Cd Length: 261  Bit Score: 44.64  E-value: 1.23e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2544519355  57 LDMTVEKAVVFFEPIPKIKQKLQtlmdvglsyitlgQNATTLSGGEAQRIKLAKELSkldTGQTLYILDEPTTGLHFHDI 136
Cdd:PRK14258  123 IDDIVESALKDADLWDEIKHKIH-------------KSALDLSGGQQQRLCIARALA---VKPKVLLMDEPCFGLDPIAS 186
                          90       100
                  ....*....|....*....|....*
gi 2544519355 137 KQLLSVINRLRER-ENTIVIIEHNL 160
Cdd:PRK14258  187 MKVESLIQSLRLRsELTMVIVSHNL 211
PRK09700 PRK09700
D-allose ABC transporter ATP-binding protein AlsA;
73-164 1.25e-05

D-allose ABC transporter ATP-binding protein AlsA;


Pssm-ID: 182036 [Multi-domain]  Cd Length: 510  Bit Score: 45.16  E-value: 1.25e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2544519355  73 KIKQKLQTLMD-VGLSyITLGQNATTLSGGEAQRIKLAKELSkLDTgqTLYILDEPTTGLHFHDIKQLLSVINRLREREN 151
Cdd:PRK09700  121 EMRVRAAMMLLrVGLK-VDLDEKVANLSISHKQMLEIAKTLM-LDA--KVIIMDEPTSSLTNKEVDYLFLIMNQLRKEGT 196
                          90
                  ....*....|...
gi 2544519355 152 TIVIIEHNLDVIK 164
Cdd:PRK09700  197 AIVYISHKLAEIR 209
cbiO PRK13638
energy-coupling factor ABC transporter ATP-binding protein;
93-194 1.26e-05

energy-coupling factor ABC transporter ATP-binding protein;


Pssm-ID: 184198 [Multi-domain]  Cd Length: 271  Bit Score: 44.61  E-value: 1.26e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2544519355  93 QNATTLSGGEAQRIKLAKELskldTGQTLYIL-DEPTTGLHFHDIKQLLSVINRLRERENTIVIIEHNLDVIKTADWIVD 171
Cdd:PRK13638  132 QPIQCLSHGQKKRVAIAGAL----VLQARYLLlDEPTAGLDPAGRTQMIAIIRRIVAQGNHVIISSHDIDLIYEISDAVY 207
                          90       100
                  ....*....|....*....|...
gi 2544519355 172 VgpeggDKGGHIVATGTPEKVSA 194
Cdd:PRK13638  208 V-----LRQGQILTHGAPGEVFA 225
ABCG_White cd03234
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ...
59-156 1.58e-05

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: 44.18  E-value: 1.58e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2544519355  59 MTVEKAVVFFEPIP-------KIKQKL---QTLMDVGLSYITlGQNATTLSGGEAQRIKLAKELSKlDTGqtLYILDEPT 128
Cdd:cd03234    96 LTVRETLTYTAILRlprkssdAIRKKRvedVLLRDLALTRIG-GNLVKGISGGERRRVSIAVQLLW-DPK--VLILDEPT 171
                          90       100
                  ....*....|....*....|....*...
gi 2544519355 129 TGLHFHDIKQLLSVINRLrERENTIVII 156
Cdd:cd03234   172 SGLDSFTALNLVSTLSQL-ARRNRIVIL 198
cbiO PRK13639
cobalt transporter ATP-binding subunit; Provisional
98-192 1.63e-05

cobalt transporter ATP-binding subunit; Provisional


Pssm-ID: 184199 [Multi-domain]  Cd Length: 275  Bit Score: 44.30  E-value: 1.63e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2544519355  98 LSGGEAQRIKLAKELSkldTGQTLYILDEPTTGLHFHDIKQLLSVINRLRERENTIVIIEHNLDVIKT-ADWIVDVGpeg 176
Cdd:PRK13639  138 LSGGQKKRVAIAGILA---MKPEIIVLDEPTSGLDPMGASQIMKLLYDLNKEGITIIISTHDVDLVPVyADKVYVMS--- 211
                          90
                  ....*....|....*.
gi 2544519355 177 gdkGGHIVATGTPEKV 192
Cdd:PRK13639  212 ---DGKIIKEGTPKEV 224
PRK10762 PRK10762
D-ribose transporter ATP binding protein; Provisional
97-163 1.89e-05

D-ribose transporter ATP binding protein; Provisional


Pssm-ID: 236755 [Multi-domain]  Cd Length: 501  Bit Score: 44.61  E-value: 1.89e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2544519355  97 TLSGGEAQRIKLAKELSkldTGQTLYILDEPTTGLHFHDIKQLLSVINRLRERENTIVIIEHNLDVI 163
Cdd:PRK10762  141 ELSIGEQQMVEIAKVLS---FESKVIIMDEPTDALTDTETESLFRVIRELKSQGRGIVYISHRLKEI 204
xylG TIGR02633
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ...
12-164 1.95e-05

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: 44.43  E-value: 1.95e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2544519355  12 KGDGLIKVEMHFLPDIYVPCDVCHGNrynretlEITYKGKNISEvldmtvekavvffepiPKIKQKLQTLM-DVGLSYIT 90
Cdd:TIGR02633  78 AGIVIIHQELTLVPELSVAENIFLGN-------EITLPGGRMAY----------------NAMYLRAKNLLrELQLDADN 134
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2544519355  91 LGQNATTLSGGEAQRIKLAKELSKldtGQTLYILDEPTTGLHFHDIKQLLSVINRLRERENTIVIIEHNLDVIK 164
Cdd:TIGR02633 135 VTRPVGDYGGGQQQLVEIAKALNK---QARLLILDEPSSSLTEKETEILLDIIRDLKAHGVACVYISHKLNEVK 205
livG PRK11300
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
95-192 1.99e-05

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


Pssm-ID: 183080 [Multi-domain]  Cd Length: 255  Bit Score: 43.83  E-value: 1.99e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2544519355  95 ATTLSGGEAQRIKLAKELSkldTGQTLYILDEPTTGLHFHDIKQLLSVINRLREREN-TIVIIEHNLD-VIKTADWIVDV 172
Cdd:PRK11300  151 AGNLAYGQQRRLEIARCMV---TQPEILMLDEPAAGLNPKETKELDELIAELRNEHNvTVLLIEHDMKlVMGISDRIYVV 227
                          90       100
                  ....*....|....*....|
gi 2544519355 173 gpeggdKGGHIVATGTPEKV 192
Cdd:PRK11300  228 ------NQGTPLANGTPEEI 241
ABC_Class3 cd03229
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ...
98-170 2.52e-05

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: 42.94  E-value: 2.52e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2544519355  98 LSGGEAQRIKLAKELSkldTGQTLYILDEPTTGLHFHDIKQLLSVINRLREREN-TIVIIEHNLDVIKT-ADWIV 170
Cdd:cd03229   101 LSGGQQQRVALARALA---MDPDVLLLDEPTSALDPITRREVRALLKSLQAQLGiTVVLVTHDLDEAARlADRVV 172
ABCC_TAP cd03248
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ...
92-170 2.72e-05

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: 43.61  E-value: 2.72e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2544519355  92 GQNATTLSGGEAQRIKLAKELskLDTGQTLyILDEPTTGLHF---HDIKQLLSVINRLRerenTIVIIEHNLDVIKTADW 168
Cdd:cd03248   145 GEKGSQLSGGQKQRVAIARAL--IRNPQVL-ILDEATSALDAeseQQVQQALYDWPERR----TVLVIAHRLSTVERADQ 217

                  ..
gi 2544519355 169 IV 170
Cdd:cd03248   218 IL 219
ABC_ModC_molybdenum_transporter cd03297
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ...
59-161 2.73e-05

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: 43.44  E-value: 2.73e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2544519355  59 MTVEKAVVF---FEPIPKIKQKLQTLMD-VGLSYItLGQNATTLSGGEAQRIKLAKELSkldTGQTLYILDEPTTGLHFH 134
Cdd:cd03297    90 LNVRENLAFglkRKRNREDRISVDELLDlLGLDHL-LNRYPAQLSGGEKQRVALARALA---AQPELLLLDEPFSALDRA 165
                          90       100
                  ....*....|....*....|....*...
gi 2544519355 135 DIKQLLSVINRLRERENTIVI-IEHNLD 161
Cdd:cd03297   166 LRLQLLPELKQIKKNLNIPVIfVTHDLS 193
PRK13633 PRK13633
energy-coupling factor transporter ATPase;
98-196 2.93e-05

energy-coupling factor transporter ATPase;


Pssm-ID: 237453 [Multi-domain]  Cd Length: 280  Bit Score: 43.54  E-value: 2.93e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2544519355  98 LSGGEAQRIKLAKELSkldTGQTLYILDEPTTGLHFHDIKQLLSVINRLREREN-TIVIIEHNLDVIKTADWIVDVgpeg 176
Cdd:PRK13633  145 LSGGQKQRVAIAGILA---MRPECIIFDEPTAMLDPSGRREVVNTIKELNKKYGiTIILITHYMEEAVEADRIIVM---- 217
                          90       100
                  ....*....|....*....|.
gi 2544519355 177 gdKGGHIVATGTPEKV-SAVE 196
Cdd:PRK13633  218 --DSGKVVMEGTPKEIfKEVE 236
YejF COG4172
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ...
98-192 2.99e-05

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: 43.90  E-value: 2.99e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2544519355  98 LSGGEAQRIKLAKELSkldTGQTLYILDEPTTGLhfhDI---KQLLSVINRLRERENT-IVIIEHNLDVI-KTADWIVDV 172
Cdd:COG4172   157 LSGGQRQRVMIAMALA---NEPDLLIADEPTTAL---DVtvqAQILDLLKDLQRELGMaLLLITHDLGVVrRFADRVAVM 230
                          90       100
                  ....*....|....*....|
gi 2544519355 173 gpeggdKGGHIVATGTPEKV 192
Cdd:COG4172   231 ------RQGEIVEQGPTAEL 244
ABC_OpuCA_Osmoprotection cd03295
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ...
59-192 3.04e-05

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: 43.44  E-value: 3.04e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2544519355  59 MTVEKAVVFF-----EPIPKIKQKLQTLM-DVGLSYITLGQN-ATTLSGGEAQRIKLAKELSkldTGQTLYILDEPTTGL 131
Cdd:cd03295    90 MTVEENIALVpkllkWPKEKIRERADELLaLVGLDPAEFADRyPHELSGGQQQRVGVARALA---ADPPLLLMDEPFGAL 166
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2544519355 132 HFHDIKQLLSVINRL-RERENTIVIIEHNLD-VIKTADWIVDVgpeggdKGGHIVATGTPEKV 192
Cdd:cd03295   167 DPITRDQLQEEFKRLqQELGKTIVFVTHDIDeAFRLADRIAIM------KNGEIVQVGTPDEI 223
CcmA COG4133
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ...
97-158 3.71e-05

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: 42.85  E-value: 3.71e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2544519355  97 TLSGGEAQRIKLAKELSkldTGQTLYILDEPTTGLHFHDIKQLLSVINRLRERENTIVIIEH 158
Cdd:COG4133   131 QLSAGQKRRVALARLLL---SPAPLWLLDEPFTALDAAGVALLAELIAAHLARGGAVLLTTH 189
ABC_ThiQ_thiamine_transporter cd03298
ATP-binding cassette domain of the thiamine transport system; Part of the ...
97-187 5.39e-05

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: 42.48  E-value: 5.39e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2544519355  97 TLSGGEAQRIKLAKELSKldtGQTLYILDEPTTGLHFHDIKQLLSVINRL-RERENTIVIIEHNL-DVIKTADWIVDVgp 174
Cdd:cd03298   128 ELSGGERQRVALARVLVR---DKPVLLLDEPFAALDPALRAEMLDLVLDLhAETKMTVLMVTHQPeDAKRLAQRVVFL-- 202
                          90
                  ....*....|...
gi 2544519355 175 eggdKGGHIVATG 187
Cdd:cd03298   203 ----DNGRIAAQG 211
ABC_BcrA_bacitracin_resist cd03268
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ...
59-170 5.93e-05

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: 42.20  E-value: 5.93e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2544519355  59 MTVEKAVVFFEPIPKIKQKL--QTLMDVGLSYITlGQNATTLSGGEAQRIKLAkeLSKLDTGQTLyILDEPTTGLHFHDI 136
Cdd:cd03268    87 LTARENLRLLARLLGIRKKRidEVLDVVGLKDSA-KKKVKGFSLGMKQRLGIA--LALLGNPDLL-ILDEPTNGLDPDGI 162
                          90       100       110
                  ....*....|....*....|....*....|....*
gi 2544519355 137 KQLLSVINRLRERENTIVIIEHNL-DVIKTADWIV 170
Cdd:cd03268   163 KELRELILSLRDQGITVLISSHLLsEIQKVADRIG 197
cbiO PRK13632
cobalt transporter ATP-binding subunit; Provisional
98-192 6.32e-05

cobalt transporter ATP-binding subunit; Provisional


Pssm-ID: 237452 [Multi-domain]  Cd Length: 271  Bit Score: 42.67  E-value: 6.32e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2544519355  98 LSGGEAQRIKLAkelSKLDTGQTLYILDEPTTGLHFHDIKQLLSVINRLRE-RENTIVIIEHNLDVIKTADWIVDVgpeg 176
Cdd:PRK13632  143 LSGGQKQRVAIA---SVLALNPEIIIFDESTSMLDPKGKREIKKIMVDLRKtRKKTLISITHDMDEAILADKVIVF---- 215
                          90
                  ....*....|....*.
gi 2544519355 177 gdKGGHIVATGTPEKV 192
Cdd:PRK13632  216 --SEGKLIAQGKPKEI 229
PRK10619 PRK10619
histidine ABC transporter ATP-binding protein HisP;
81-161 6.46e-05

histidine ABC transporter ATP-binding protein HisP;


Pssm-ID: 182592 [Multi-domain]  Cd Length: 257  Bit Score: 42.65  E-value: 6.46e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2544519355  81 LMDVGLSYITLGQNATTLSGGEAQRIKLAKELSkldTGQTLYILDEPTTGLHFHDIKQLLSVINRLRERENTIVIIEHNL 160
Cdd:PRK10619  136 LAKVGIDERAQGKYPVHLSGGQQQRVSIARALA---MEPEVLLFDEPTSALDPELVGEVLRIMQQLAEEGKTMVVVTHEM 212

                  .
gi 2544519355 161 D 161
Cdd:PRK10619  213 G 213
PRK10982 PRK10982
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
97-163 7.21e-05

galactose/methyl galaxtoside transporter ATP-binding protein; Provisional


Pssm-ID: 182880 [Multi-domain]  Cd Length: 491  Bit Score: 42.79  E-value: 7.21e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2544519355  97 TLSGGEAQRIKLAKELSkldTGQTLYILDEPTTGLHFHDIKQLLSVINRLRERENTIVIIEHNLDVI 163
Cdd:PRK10982  134 TLSVSQMQMIEIAKAFS---YNAKIVIMDEPTSSLTEKEVNHLFTIIRKLKERGCGIVYISHKMEEI 197
3a01208 TIGR00958
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
92-199 7.35e-05

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


Pssm-ID: 273363 [Multi-domain]  Cd Length: 711  Bit Score: 42.79  E-value: 7.35e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2544519355  92 GQNATTLSGGEAQRIKLAKELSKldtGQTLYILDEPTTGLHFhDIKQLLSVINRLRERenTIVIIEHNLDVIKTADWIVD 171
Cdd:TIGR00958 612 GEKGSQLSGGQKQRIAIARALVR---KPRVLILDEATSALDA-ECEQLLQESRSRASR--TVLLIAHRLSTVERADQILV 685
                          90       100
                  ....*....|....*....|....*...
gi 2544519355 172 VgpeggdKGGHIVATGTPEKVSAVEGSY 199
Cdd:TIGR00958 686 L------KKGSVVEMGTHKQLMEDQGCY 707
araG PRK11288
L-arabinose ABC transporter ATP-binding protein AraG;
98-163 7.47e-05

L-arabinose ABC transporter ATP-binding protein AraG;


Pssm-ID: 183077 [Multi-domain]  Cd Length: 501  Bit Score: 42.59  E-value: 7.47e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2544519355  98 LSGGEAQRIKLAKELSKldtGQTLYILDEPTTGLHFHDIKQLLSVINRLRERENTIVIIEHNLDVI 163
Cdd:PRK11288  141 LSIGQRQMVEIAKALAR---NARVIAFDEPTSSLSAREIEQLFRVIRELRAEGRVILYVSHRMEEI 203
PRK14243 PRK14243
phosphate transporter ATP-binding protein; Provisional
48-192 7.59e-05

phosphate transporter ATP-binding protein; Provisional


Pssm-ID: 184588 [Multi-domain]  Cd Length: 264  Bit Score: 42.46  E-value: 7.59e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2544519355  48 YKGkNISEVLDMTVEKAVVFFEpipkIKQKLQtlmdvglsyitlgQNATTLSGGEAQRIKLAKELSKldtgQTLYIL-DE 126
Cdd:PRK14243  120 YKG-DMDELVERSLRQAALWDE----VKDKLK-------------QSGLSLSGGQQQRLCIARAIAV----QPEVILmDE 177
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2544519355 127 PTTGLHFHDIKQLLSVINRLREREnTIVIIEHNLDVI-----KTADWIVDVGpEGGDKGGHIVATGTPEKV 192
Cdd:PRK14243  178 PCSALDPISTLRIEELMHELKEQY-TIIIVTHNMQQAarvsdMTAFFNVELT-EGGGRYGYLVEFDRTEKI 246
PRK15056 PRK15056
manganese/iron ABC transporter ATP-binding protein;
98-190 8.81e-05

manganese/iron ABC transporter ATP-binding protein;


Pssm-ID: 185016 [Multi-domain]  Cd Length: 272  Bit Score: 42.18  E-value: 8.81e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2544519355  98 LSGGEAQRIKLAKELSKldTGQTLyILDEPTTGLHFHDIKQLLSVINRLRERENTIVIIEHNL-DVIKTADWIVDVgpeg 176
Cdd:PRK15056  143 LSGGQKKRVFLARAIAQ--QGQVI-LLDEPFTGVDVKTEARIISLLRELRDEGKTMLVSTHNLgSVTEFCDYTVMV---- 215
                          90
                  ....*....|....
gi 2544519355 177 gdkGGHIVATGTPE 190
Cdd:PRK15056  216 ---KGTVLASGPTE 226
ABC_PstB_phosphate_transporter cd03260
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ...
93-160 1.19e-04

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: 41.40  E-value: 1.19e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2544519355  93 QNATTLSGGEAQRIKLAKELSkldTGQTLYILDEPTTGLHFH---DIKQLlsvINRLReRENTIVIIEHNL 160
Cdd:cd03260   137 LHALGLSGGQQQRLCLARALA---NEPEVLLLDEPTSALDPIstaKIEEL---IAELK-KEYTIVIVTHNM 200
PRK14246 PRK14246
phosphate ABC transporter ATP-binding protein; Provisional
45-169 1.21e-04

phosphate ABC transporter ATP-binding protein; Provisional


Pssm-ID: 172734 [Multi-domain]  Cd Length: 257  Bit Score: 41.57  E-value: 1.21e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2544519355  45 EITYKGKNISEVLDMTVEKAV--VFFEPIP-------------------KIKQKLQTLMD-----VGL---SYITLGQNA 95
Cdd:PRK14246   72 KVLYFGKDIFQIDAIKLRKEVgmVFQQPNPfphlsiydniayplkshgiKEKREIKKIVEeclrkVGLwkeVYDRLNSPA 151
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2544519355  96 TTLSGGEAQRIKLAKELSkldTGQTLYILDEPTTGLHFHDIKQLLSVINRLReRENTIVIIEHN-LDVIKTADWI 169
Cdd:PRK14246  152 SQLSGGQQQRLTIARALA---LKPKVLLMDEPTSMIDIVNSQAIEKLITELK-NEIAIVIVSHNpQQVARVADYV 222
met_CoM_red_A2 TIGR03269
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ...
95-195 1.21e-04

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: 42.10  E-value: 1.21e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2544519355  95 ATTLSGGEAQRIKLAKELSKldtGQTLYILDEPTTGLhfhDIKQLLSVINRLRErentiVIIEHNLDVIKTADWiVDVGP 174
Cdd:TIGR03269 166 ARDLSGGEKQRVVLARQLAK---EPFLFLADEPTGTL---DPQTAKLVHNALEE-----AVKASGISMVLTSHW-PEVIE 233
                          90       100
                  ....*....|....*....|....*.
gi 2544519355 175 EGGDKG-----GHIVATGTPEKVSAV 195
Cdd:TIGR03269 234 DLSDKAiwlenGEIKEEGTPDEVVAV 259
ABC_ABC_ChvD TIGR03719
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ...
93-172 1.32e-04

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: 41.84  E-value: 1.32e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2544519355  93 QNATTLSGGEAQRIKLAKEL-SKLDtgqtLYILDEPTTGLhfhDIKQLLSVINRLRERENTIVIIEHN---LDVIktADW 168
Cdd:TIGR03719 157 ADVTKLSGGERRRVALCRLLlSKPD----MLLLDEPTNHL---DAESVAWLERHLQEYPGTVVAVTHDryfLDNV--AGW 227

                  ....
gi 2544519355 169 IVDV 172
Cdd:TIGR03719 228 ILEL 231
ABCG_EPDR cd03213
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ...
98-158 1.40e-04

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: 41.00  E-value: 1.40e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2544519355  98 LSGGEAQRIKLAKELSkldTGQTLYILDEPTTGLHFHDIKQLLSVINRLRERENTIVIIEH 158
Cdd:cd03213   112 LSGGERKRVSIALELV---SNPSLLFLDEPTSGLDSSSALQVMSLLRRLADTGRTIICSIH 169
ABC_DrrA cd03265
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ...
86-190 1.42e-04

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: 41.20  E-value: 1.42e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2544519355  86 LSYITLGQNA----TTLSGGEAQRIKLAKELskLDTGQTLYiLDEPTTGLHFHDIKQLLSVINRLREREN-TIVIIEHNL 160
Cdd:cd03265   116 LDFVGLLEAAdrlvKTYSGGMRRRLEIARSL--VHRPEVLF-LDEPTIGLDPQTRAHVWEYIEKLKEEFGmTILLTTHYM 192
                          90       100       110
                  ....*....|....*....|....*....|.
gi 2544519355 161 D-VIKTADWIVDVgpeggdKGGHIVATGTPE 190
Cdd:cd03265   193 EeAEQLCDRVAII------DHGRIIAEGTPE 217
ABC_ABC_ChvD TIGR03719
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ...
98-200 1.45e-04

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: 41.84  E-value: 1.45e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2544519355  98 LSGGEAQRIKLAKELSkldTGQTLYILDEPTTGLhfhDIKQLLSVINRLRERENTIVIIEHN---LDVIKTadwivdvgp 174
Cdd:TIGR03719 444 LSGGERNRVHLAKTLK---SGGNVLLLDEPTNDL---DVETLRALEEALLNFAGCAVVISHDrwfLDRIAT--------- 508
                          90       100
                  ....*....|....*....|....*.
gi 2544519355 175 eggdkggHIVATGTPEKVSAVEGSYT 200
Cdd:TIGR03719 509 -------HILAFEGDSHVEWFEGNFS 527
ABC_CcmA_heme_exporter cd03231
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ...
59-158 1.47e-04

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: 40.94  E-value: 1.47e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2544519355  59 MTVEKAVVFFEPIPKIKQKLQTLMDVGLS---YITLGQnattLSGGEAQRIKLAKELSkldTGQTLYILDEPTTGLHFHD 135
Cdd:cd03231    88 LSVLENLRFWHADHSDEQVEEALARVGLNgfeDRPVAQ----LSAGQQRRVALARLLL---SGRPLWILDEPTTALDKAG 160
                          90       100
                  ....*....|....*....|...
gi 2544519355 136 IKQLLSVINRLRERENTIVIIEH 158
Cdd:cd03231   161 VARFAEAMAGHCARGGMVVLTTH 183
cbiO PRK13641
energy-coupling factor transporter ATPase;
76-192 1.60e-04

energy-coupling factor transporter ATPase;


Pssm-ID: 237456 [Multi-domain]  Cd Length: 287  Bit Score: 41.35  E-value: 1.60e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2544519355  76 QKLQTLMDVGLSYITLGQNATTLSGGEAQRIKLAKELSklDTGQTLyILDEPTTGLHFHDIKQLLSVINRLRERENTIVI 155
Cdd:PRK13641  124 KALKWLKKVGLSEDLISKSPFELSGGQMRRVAIAGVMA--YEPEIL-CLDEPAAGLDPEGRKEMMQLFKDYQKAGHTVIL 200
                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 2544519355 156 IEHNL-DVIKTADWIVDVgpeggdKGGHIVATGTPEKV 192
Cdd:PRK13641  201 VTHNMdDVAEYADDVLVL------EHGKLIKHASPKEI 232
GguA NF040905
sugar ABC transporter ATP-binding protein;
84-169 1.61e-04

sugar ABC transporter ATP-binding protein;


Pssm-ID: 468840 [Multi-domain]  Cd Length: 500  Bit Score: 41.70  E-value: 1.61e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2544519355  84 VGLSyitlgQNATTLSG----GEAQRIKLAKELSKldtGQTLYILDEPTTGLHFHDIKQLLSVINRLRERENTIVIIEHN 159
Cdd:NF040905  127 VGLD-----ESPDTLVTdigvGKQQLVEIAKALSK---DVKLLILDEPTAALNEEDSAALLDLLLELKAQGITSIIISHK 198
                          90
                  ....*....|.
gi 2544519355 160 L-DVIKTADWI 169
Cdd:NF040905  199 LnEIRRVADSI 209
PRK10789 PRK10789
SmdA family multidrug ABC transporter permease/ATP-binding protein;
92-203 1.62e-04

SmdA family multidrug ABC transporter permease/ATP-binding protein;


Pssm-ID: 182732 [Multi-domain]  Cd Length: 569  Bit Score: 41.62  E-value: 1.62e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2544519355  92 GQNATTLSGGEAQRIKLAKELsKLDTgqTLYILDEPTTGLHFHDIKQLLSVINRLRErENTIVIIEHNLDVIKTADWIVD 171
Cdd:PRK10789  446 GERGVMLSGGQKQRISIARAL-LLNA--EILILDDALSAVDGRTEHQILHNLRQWGE-GRTVIISAHRLSALTEASEILV 521
                          90       100       110
                  ....*....|....*....|....*....|..
gi 2544519355 172 VgpeggdKGGHIVATGTPEKVSAVEGSYTGQY 203
Cdd:PRK10789  522 M------QHGHIAQRGNHDQLAQQSGWYRDMY 547
PRK15439 PRK15439
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
93-167 1.67e-04

autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional


Pssm-ID: 185336 [Multi-domain]  Cd Length: 510  Bit Score: 41.58  E-value: 1.67e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2544519355  93 QNATTLSGGEAQRIKLAKELSkldTGQTLYILDEPTTGLHF---HDIKQLlsvINRLRERENTIVIIEHNLD-VIKTAD 167
Cdd:PRK15439  399 QAARTLSGGNQQKVLIAKCLE---ASPQLLIVDEPTRGVDVsarNDIYQL---IRSIAAQNVAVLFISSDLEeIEQMAD 471
oppD PRK09473
oligopeptide transporter ATP-binding component; Provisional
99-163 1.83e-04

oligopeptide transporter ATP-binding component; Provisional


Pssm-ID: 181888 [Multi-domain]  Cd Length: 330  Bit Score: 41.25  E-value: 1.83e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2544519355  99 SGGEAQRIKLAKEL---SKLdtgqtlYILDEPTTGLHFHDIKQLLSVINRLRERENT-IVIIEHNLDVI 163
Cdd:PRK09473  163 SGGMRQRVMIAMALlcrPKL------LIADEPTTALDVTVQAQIMTLLNELKREFNTaIIMITHDLGVV 225
PRK13657 PRK13657
glucan ABC transporter ATP-binding protein/ permease;
92-197 2.00e-04

glucan ABC transporter ATP-binding protein/ permease;


Pssm-ID: 184214 [Multi-domain]  Cd Length: 588  Bit Score: 41.49  E-value: 2.00e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2544519355  92 GQNATTLSGGEAQRIKLAKELSKldtGQTLYILDEPTTGLHFHDIKQLLSVINRLRERENTIvIIEHNLDVIKTADWIVD 171
Cdd:PRK13657  466 GERGRQLSGGERQRLAIARALLK---DPPILILDEATSALDVETEAKVKAALDELMKGRTTF-IIAHRLSTVRNADRILV 541
                          90       100
                  ....*....|....*....|....*.
gi 2544519355 172 VgpeggDKgGHIVATGTPEKVSAVEG 197
Cdd:PRK13657  542 F-----DN-GRVVESGSFDELVARGG 561
PRK11264 PRK11264
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
98-160 2.03e-04

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


Pssm-ID: 183063 [Multi-domain]  Cd Length: 250  Bit Score: 40.89  E-value: 2.03e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2544519355  98 LSGGEAQRIKLAKELSKldtgQTLYIL-DEPTTGLHFHDIKQLLSVINRLRERENTIVIIEHNL 160
Cdd:PRK11264  145 LSGGQQQRVAIARALAM----RPEVILfDEPTSALDPELVGEVLNTIRQLAQEKRTMVIVTHEM 204
PRK09984 PRK09984
phosphonate ABC transporter ATP-binding protein;
67-161 2.08e-04

phosphonate ABC transporter ATP-binding protein;


Pssm-ID: 182182 [Multi-domain]  Cd Length: 262  Bit Score: 41.15  E-value: 2.08e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2544519355  67 FFEPIPKiKQKLQTLMDVGLSYITlGQNATTLSGGEAQRIKLAKELSKldtgQTLYIL-DEPTTGLHFHDIKQLLSVINR 145
Cdd:PRK09984  124 WFTREQK-QRALQALTRVGMVHFA-HQRVSTLSGGQQQRVAIARALMQ----QAKVILaDEPIASLDPESARIVMDTLRD 197
                          90
                  ....*....|....*..
gi 2544519355 146 LREREN-TIVIIEHNLD 161
Cdd:PRK09984  198 INQNDGiTVVVTLHQVD 214
ABC_putative_ATPase cd03269
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ...
97-161 2.12e-04

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: 40.73  E-value: 2.12e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2544519355  97 TLSGGEAQRIKLAkelSKLDTGQTLYILDEPTTGLHFHDIKQLLSVINRLRERENTIVIIEHNLD 161
Cdd:cd03269   128 ELSKGNQQKVQFI---AAVIHDPELLILDEPFSGLDPVNVELLKDVIRELARAGKTVILSTHQME 189
ATM1 COG5265
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ...
98-199 2.92e-04

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: 40.96  E-value: 2.92e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2544519355  98 LSGGEAQRIKLAKELSKldtGQTLYILDEPTTGLHFHDIKQLLSVINRLRERENTIViIEHNLDVIKTADWIVDVgpegg 177
Cdd:COG5265   495 LSGGEKQRVAIARTLLK---NPPILIFDEATSALDSRTERAIQAALREVARGRTTLV-IAHRLSTIVDADEILVL----- 565
                          90       100
                  ....*....|....*....|..
gi 2544519355 178 dKGGHIVATGTPEKVSAVEGSY 199
Cdd:COG5265   566 -EAGRIVERGTHAELLAQGGLY 586
met_CoM_red_A2 TIGR03269
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ...
97-192 3.12e-04

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: 40.94  E-value: 3.12e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2544519355  97 TLSGGEAQRIKLAKELSKldtGQTLYILDEPT-TGLHFHDIKQLLSVINRLRERENTIVIIEHNLdviktaDWIVDVGPE 175
Cdd:TIGR03269 427 ELSEGERHRVALAQVLIK---EPRIVILDEPTgTMDPITKVDVTHSILKAREEMEQTFIIVSHDM------DFVLDVCDR 497
                          90
                  ....*....|....*...
gi 2544519355 176 GG-DKGGHIVATGTPEKV 192
Cdd:TIGR03269 498 AAlMRDGKIVKIGDPEEI 515
AAA_21 pfam13304
AAA domain, putative AbiEii toxin, Type IV TA system; Several members are annotated as being ...
94-163 3.13e-04

AAA domain, putative AbiEii toxin, Type IV TA system; Several members are annotated as being of the abortive phage resistance system, in which case the family would be acting as the toxin for a type IV toxin-antitoxin resistance system.


Pssm-ID: 433102 [Multi-domain]  Cd Length: 303  Bit Score: 40.84  E-value: 3.13e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2544519355  94 NATTLSGGEAQRIKLAKELSKLDTGQTLYILDEPTTGLHFHDIKQLLSVINRLRERENTIVIIEHNLDVI 163
Cdd:pfam13304 233 PAFELSDGTKRLLALLAALLSALPKGGLLLIDEPESGLHPKLLRRLLELLKELSRNGAQLILTTHSPLLL 302
PRK15079 PRK15079
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
59-164 4.14e-04

oligopeptide ABC transporter ATP-binding protein OppF; Provisional


Pssm-ID: 185037 [Multi-domain]  Cd Length: 331  Bit Score: 40.46  E-value: 4.14e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2544519355  59 MTV-----EKAVVFFEPIPK--IKQKLQTLMD-VGLSYITLGQNATTLSGGEAQRIKLAKEL---SKldtgqtLYILDEP 127
Cdd:PRK15079  115 MTIgeiiaEPLRTYHPKLSRqeVKDRVKAMMLkVGLLPNLINRYPHEFSGGQCQRIGIARALilePK------LIICDEP 188
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 2544519355 128 TTGLhfhDIKQLLSVINRLRE--REN--TIVIIEHNLDVIK 164
Cdd:PRK15079  189 VSAL---DVSIQAQVVNLLQQlqREMglSLIFIAHDLAVVK 226
ABC_Carb_Solutes_like cd03259
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ...
59-187 4.41e-04

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: 39.81  E-value: 4.41e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2544519355  59 MTVEKAVVF-----FEPIPKIKQKLQTLMD-VGLSyITLGQNATTLSGGEAQRIKLAKELSKldtGQTLYILDEPTTGLH 132
Cdd:cd03259    87 LTVAENIAFglklrGVPKAEIRARVRELLElVGLE-GLLNRYPHELSGGQQQRVALARALAR---EPSLLLLDEPLSALD 162
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 2544519355 133 FHDIKQLLSVINRL-RERENTIVIIEHNL-DVIKTADWIVDVgpeggdKGGHIVATG 187
Cdd:cd03259   163 AKLREELREELKELqRELGITTIYVTHDQeEALALADRIAVM------NEGRIVQVG 213
phnK PRK11701
phosphonate C-P lyase system protein PhnK; Provisional
96-192 4.41e-04

phosphonate C-P lyase system protein PhnK; Provisional


Pssm-ID: 183280 [Multi-domain]  Cd Length: 258  Bit Score: 39.91  E-value: 4.41e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2544519355  96 TTLSGGEAQRIKLAKELSkldTGQTLYILDEPTTGLHFHDIKQLLSVINRL-RERENTIVIIEHNLDVIK-TADWIVDVg 173
Cdd:PRK11701  150 TTFSGGMQQRLQIARNLV---THPRLVFMDEPTGGLDVSVQARLLDLLRGLvRELGLAVVIVTHDLAVARlLAHRLLVM- 225
                          90
                  ....*....|....*....
gi 2544519355 174 peggdKGGHIVATGTPEKV 192
Cdd:PRK11701  226 -----KQGRVVESGLTDQV 239
ABCD_peroxisomal_ALDP cd03223
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ...
97-177 4.94e-04

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: 39.06  E-value: 4.94e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2544519355  97 TLSGGEAQRIKLAKELSkldTGQTLYILDEPTTGLhfhDIKQLLSVINRLRERENTIVIIEHNLDVIKTADWIVDVGPEG 176
Cdd:cd03223    91 VLSGGEQQRLAFARLLL---HKPKFVFLDEATSAL---DEESEDRLYQLLKELGITVISVGHRPSLWKFHDRVLDLDGEG 164

                  .
gi 2544519355 177 G 177
Cdd:cd03223   165 G 165
ABC_FtsE cd03292
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ...
98-165 5.19e-04

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: 39.70  E-value: 5.19e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2544519355  98 LSGGEAQRIKLAKELSKldtGQTLYILDEPTTGLHFHDIKQLLSVINRLRERENTIVIIEHNLDVIKT 165
Cdd:cd03292   137 LSGGEQQRVAIARAIVN---SPTILIADEPTGNLDPDTTWEIMNLLKKINKAGTTVVVATHAKELVDT 201
3a01204 TIGR00955
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ...
98-158 7.01e-04

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


Pssm-ID: 273361 [Multi-domain]  Cd Length: 617  Bit Score: 40.03  E-value: 7.01e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2544519355  98 LSGGEAQRIKLAKELSkldTGQTLYILDEPTTGLHFHDIKQLLSVINRLRERENTIVIIEH 158
Cdd:TIGR00955 167 LSGGERKRLAFASELL---TDPPLLFCDEPTSGLDSFMAYSVVQVLKGLAQKGKTIICTIH 224
ABC_Rad50 cd03240
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ...
97-176 7.34e-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: 39.13  E-value: 7.34e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2544519355  97 TLSGGE------AQRIKLAKEL-SKLDtgqtLYILDEPTTGL-HFHDIKQLLSVINRLREREN-TIVIIEHNLDVIKTAD 167
Cdd:cd03240   115 RCSGGEkvlaslIIRLALAETFgSNCG----ILALDEPTTNLdEENIEESLAEIIEERKSQKNfQLIVITHDEELVDAAD 190

                  ....*....
gi 2544519355 168 WIVDVGPEG 176
Cdd:cd03240   191 HIYRVEKDG 199
dppD PRK11022
dipeptide transporter ATP-binding subunit; Provisional
98-206 7.64e-04

dipeptide transporter ATP-binding subunit; Provisional


Pssm-ID: 182906 [Multi-domain]  Cd Length: 326  Bit Score: 39.34  E-value: 7.64e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2544519355  98 LSGGEAQRIKLAKELSkldTGQTLYILDEPTTGLHFHDIKQLLSVINRLREREN-TIVIIEHNLD-VIKTADWIVDVgpe 175
Cdd:PRK11022  154 LSGGMSQRVMIAMAIA---CRPKLLIADEPTTALDVTIQAQIIELLLELQQKENmALVLITHDLAlVAEAAHKIIVM--- 227
                          90       100       110
                  ....*....|....*....|....*....|..
gi 2544519355 176 ggdKGGHIVATGTPEKV-SAVEGSYTGQYLKS 206
Cdd:PRK11022  228 ---YAGQVVETGKAHDIfRAPRHPYTQALLRA 256
AbcC COG1135
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
72-164 7.76e-04

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


Pssm-ID: 440750 [Multi-domain]  Cd Length: 339  Bit Score: 39.29  E-value: 7.76e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2544519355  72 PKIKQKLQTLMD-VGLS-----YitLGQnattLSGGEAQRIKLAKELSkldTGQTLYILDEPTTGLHFHDIKQLLSVINR 145
Cdd:COG1135   115 AEIRKRVAELLElVGLSdkadaY--PSQ----LSGGQKQRVGIARALA---NNPKVLLCDEATSALDPETTRSILDLLKD 185
                          90       100
                  ....*....|....*....|
gi 2544519355 146 LREREN-TIVIIEHNLDVIK 164
Cdd:COG1135   186 INRELGlTIVLITHEMDVVR 205
ABC_drug_resistance_like cd03264
ABC-type multidrug transport system, ATPase component; The biological function of this family ...
97-187 8.39e-04

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: 39.10  E-value: 8.39e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2544519355  97 TLSGGEAQRIKLAKELSKLdtgQTLYILDEPTTGLhfhDIKQLLSVINRLRE-RENTIVIIEHNL--DVIKTADWIVDVg 173
Cdd:cd03264   130 SLSGGMRRRVGIAQALVGD---PSILIVDEPTAGL---DPEERIRFRNLLSElGEDRIVILSTHIveDVESLCNQVAVL- 202
                          90
                  ....*....|....
gi 2544519355 174 peggdKGGHIVATG 187
Cdd:cd03264   203 -----NKGKLVFEG 211
ABCC_bacteriocin_exporters cd03245
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ...
91-187 8.46e-04

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: 39.11  E-value: 8.46e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2544519355  91 LGQNATTLSGGEAQRIKLAKELskLDTGQTLyILDEPTTGLhfhDIKQLLSVINRLRE--RENTIVIIEHNLDVIKTADW 168
Cdd:cd03245   134 IGERGRGLSGGQRQAVALARAL--LNDPPIL-LLDEPTSAM---DMNSEERLKERLRQllGDKTLIIITHRPSLLDLVDR 207
                          90
                  ....*....|....*....
gi 2544519355 169 IVDVgpeggDKGGhIVATG 187
Cdd:cd03245   208 IIVM-----DSGR-IVADG 220
PRK10851 PRK10851
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
74-192 9.12e-04

sulfate/thiosulfate ABC transporter ATP-binding protein CysA;


Pssm-ID: 182778 [Multi-domain]  Cd Length: 353  Bit Score: 39.30  E-value: 9.12e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2544519355  74 IKQKLQTLMD-VGLSYITlGQNATTLSGGEAQRIKLAKELSKldTGQTLyILDEPTTGLHFHDIKQLLSVINRLRER-EN 151
Cdd:PRK10851  113 IKAKVTQLLEmVQLAHLA-DRYPAQLSGGQKQRVALARALAV--EPQIL-LLDEPFGALDAQVRKELRRWLRQLHEElKF 188
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 2544519355 152 TIVIIEHNL-DVIKTADWIVDVGPeggdkgGHIVATGTPEKV 192
Cdd:PRK10851  189 TSVFVTHDQeEAMEVADRVVVMSQ------GNIEQAGTPDQV 224
MglA COG1129
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
90-156 9.80e-04

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


Pssm-ID: 440745 [Multi-domain]  Cd Length: 497  Bit Score: 39.23  E-value: 9.80e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2544519355  90 TLGQNATTLSGGEAQRIKLAKELSkldTGQTLYILDEPTTGLhfhDI---KQLLSVINRLRERENTIVII 156
Cdd:COG1129   387 SPEQPVGNLSGGNQQKVVLAKWLA---TDPKVLILDEPTRGI---DVgakAEIYRLIRELAAEGKAVIVI 450
metN PRK11153
DL-methionine transporter ATP-binding subunit; Provisional
73-164 9.90e-04

DL-methionine transporter ATP-binding subunit; Provisional


Pssm-ID: 236863 [Multi-domain]  Cd Length: 343  Bit Score: 39.01  E-value: 9.90e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2544519355  73 KIKQKLQTLMD-VGLS-----YitlgqnATTLSGGEAQRIKLAKELSkldTGQTLYILDEPTTGLhfhD------IKQLL 140
Cdd:PRK11153  116 EIKARVTELLElVGLSdkadrY------PAQLSGGQKQRVAIARALA---SNPKVLLCDEATSAL---DpattrsILELL 183
                          90       100
                  ....*....|....*....|....
gi 2544519355 141 SVINRlrERENTIVIIEHNLDVIK 164
Cdd:PRK11153  184 KDINR--ELGLTIVLITHEMDVVK 205
PLN03211 PLN03211
ABC transporter G-25; Provisional
98-158 1.01e-03

ABC transporter G-25; Provisional


Pssm-ID: 215634 [Multi-domain]  Cd Length: 659  Bit Score: 39.48  E-value: 1.01e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2544519355  98 LSGGEAQRIKLAKELSkldTGQTLYILDEPTTGLHFHDIKQLLSVINRLRERENTIVIIEH 158
Cdd:PLN03211  207 ISGGERKRVSIAHEML---INPSLLILDEPTSGLDATAAYRLVLTLGSLAQKGKTIVTSMH 264
PRK13539 PRK13539
cytochrome c biogenesis protein CcmA; Provisional
80-159 1.04e-03

cytochrome c biogenesis protein CcmA; Provisional


Pssm-ID: 237421 [Multi-domain]  Cd Length: 207  Bit Score: 38.70  E-value: 1.04e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2544519355  80 TLMDVGLSYITlGQNATTLSGGEAQRIKLAKELSkldTGQTLYILDEPTTGLHFHDIKQLLSVINRLRERENTIVIIEHN 159
Cdd:PRK13539  111 ALEAVGLAPLA-HLPFGYLSAGQKRRVALARLLV---SNRPIWILDEPTAALDAAAVALFAELIRAHLAQGGIVIAATHI 186
ABC_NatA_sodium_exporter cd03266
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ...
98-161 1.09e-03

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: 38.50  E-value: 1.09e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2544519355  98 LSGGEAQRIKLAKELskLDTGQTLyILDEPTTGLHFHDIKQLLSVINRLRERENTIVIIEHNLD 161
Cdd:cd03266   137 FSTGMRQKVAIARAL--VHDPPVL-LLDEPTTGLDVMATRALREFIRQLRALGKCILFSTHIMQ 197
PRK15439 PRK15439
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
73-169 1.14e-03

autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional


Pssm-ID: 185336 [Multi-domain]  Cd Length: 510  Bit Score: 39.26  E-value: 1.14e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2544519355  73 KIKQKLQTLMdvglSYITLGQNATTLSGGEAQRIKLAKELSKldtGQTLYILDEPTTGLHFHDIKQLLSVINRLRERENT 152
Cdd:PRK15439  120 KMKQLLAALG----CQLDLDSSAGSLEVADRQIVEILRGLMR---DSRILILDEPTASLTPAETERLFSRIRELLAQGVG 192
                          90
                  ....*....|....*...
gi 2544519355 153 IVIIEHNL-DVIKTADWI 169
Cdd:PRK15439  193 IVFISHKLpEIRQLADRI 210
PRK14239 PRK14239
phosphate transporter ATP-binding protein; Provisional
43-160 1.15e-03

phosphate transporter ATP-binding protein; Provisional


Pssm-ID: 184585 [Multi-domain]  Cd Length: 252  Bit Score: 38.60  E-value: 1.15e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2544519355  43 TLEITYKGKNI----SEVLDMTVEKAVVFFEPIP------------------KIKQKLQTLMDVGLSYIT--------LG 92
Cdd:PRK14239   64 TGSIVYNGHNIysprTDTVDLRKEIGMVFQQPNPfpmsiyenvvyglrlkgiKDKQVLDEAVEKSLKGASiwdevkdrLH 143
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2544519355  93 QNATTLSGGEAQRIKLAKELSkldTGQTLYILDEPTTGLHFHDIKQLLSVINRLRErENTIVIIEHNL 160
Cdd:PRK14239  144 DSALGLSGGQQQRVCIARVLA---TSPKIILLDEPTSALDPISAGKIEETLLGLKD-DYTMLLVTRSM 207
nikE PRK10419
nickel ABC transporter ATP-binding protein NikE;
98-160 1.26e-03

nickel ABC transporter ATP-binding protein NikE;


Pssm-ID: 236689 [Multi-domain]  Cd Length: 268  Bit Score: 38.90  E-value: 1.26e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2544519355  98 LSGGEAQRIKLAKELSkldTGQTLYILDEPTTGLHFHDIKQLLSVINRLRERENT-IVIIEHNL 160
Cdd:PRK10419  152 LSGGQLQRVCLARALA---VEPKLLILDEAVSNLDLVLQAGVIRLLKKLQQQFGTaCLFITHDL 212
xylG TIGR02633
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ...
96-194 1.31e-03

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: 39.04  E-value: 1.31e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2544519355  96 TTLSGGEAQRIKLAKELSkldTGQTLYILDEPTTGLHFHDIKQLLSVINRLRERENTIVIIEHNL-DVIKTADWIVDVGp 174
Cdd:TIGR02633 402 GRLSGGNQQKAVLAKMLL---TNPRVLILDEPTRGVDVGAKYEIYKLINQLAQEGVAIIVVSSELaEVLGLSDRVLVIG- 477
                          90       100
                  ....*....|....*....|
gi 2544519355 175 EGGDKGGHIVATGTPEKVSA 194
Cdd:TIGR02633 478 EGKLKGDFVNHALTQEQVLA 497
ABC2_perm_RbbA NF033858
ribosome-associated ATPase/putative transporter RbbA;
121-198 1.31e-03

ribosome-associated ATPase/putative transporter RbbA;


Pssm-ID: 468210 [Multi-domain]  Cd Length: 907  Bit Score: 38.95  E-value: 1.31e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2544519355 121 LYILDEPTTGLhfhDI---KQLLSVINRLR-ERENTIVIiehnldvIKTA--------DWIV--DvgpeggdkGGHIVAT 186
Cdd:NF033858  157 LLILDEPTTGV---DPlsrRQFWELIDRIRaERPGMSVL-------VATAymeeaerfDWLVamD--------AGRVLAT 218
                          90
                  ....*....|..
gi 2544519355 187 GTPEKVSAVEGS 198
Cdd:NF033858  219 GTPAELLARTGA 230
glnQ PRK09493
glutamine ABC transporter ATP-binding protein GlnQ;
75-158 1.62e-03

glutamine ABC transporter ATP-binding protein GlnQ;


Pssm-ID: 181906 [Multi-domain]  Cd Length: 240  Bit Score: 38.15  E-value: 1.62e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2544519355  75 KQKLQTLMDVGLSYiTLGQNATTLSGGEAQRIKLAKELSkldTGQTLYILDEPTTGLHFHDIKQLLSVINRLRERENTIV 154
Cdd:PRK09493  115 KQARELLAKVGLAE-RAHHYPSELSGGQQQRVAIARALA---VKPKLMLFDEPTSALDPELRHEVLKVMQDLAEEGMTMV 190

                  ....
gi 2544519355 155 IIEH 158
Cdd:PRK09493  191 IVTH 194
modC PRK11144
molybdenum ABC transporter ATP-binding protein ModC;
97-192 1.81e-03

molybdenum ABC transporter ATP-binding protein ModC;


Pssm-ID: 182993 [Multi-domain]  Cd Length: 352  Bit Score: 38.32  E-value: 1.81e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2544519355  97 TLSGGEAQRIKLAKELSkldTGQTLYILDEPTTGLhfhDI---KQLLSVINRLRERENT-IVIIEHNLD-VIKTADWIVD 171
Cdd:PRK11144  128 SLSGGEKQRVAIGRALL---TAPELLLMDEPLASL---DLprkRELLPYLERLAREINIpILYVSHSLDeILRLADRVVV 201
                          90       100
                  ....*....|....*....|.
gi 2544519355 172 VgpeggDKgGHIVATGTPEKV 192
Cdd:PRK11144  202 L-----EQ-GKVKAFGPLEEV 216
MRP_assoc_pro TIGR00957
multi drug resistance-associated protein (MRP); This model describes multi drug ...
91-207 1.99e-03

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: 38.77  E-value: 1.99e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2544519355   91 LGQNATTLSGGEAQRIKLAKEL-SKLDtgqtLYILDEPTTGLHFHDIKQLL-SVINRLREREN-TIVIIEHNLDVIKTAD 167
Cdd:TIGR00957  754 IGEKGVNLSGGQKQRVSLARAVySNAD----IYLFDDPLSAVDAHVGKHIFeHVIGPEGVLKNkTRILVTHGISYLPQVD 829
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|
gi 2544519355  168 WIVDVGpeggdkGGHIVATGTPEKVSAVEGSYtGQYLKSY 207
Cdd:TIGR00957  830 VIIVMS------GGKISEMGSYQELLQRDGAF-AEFLRTY 862
ccmA TIGR01189
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ...
58-131 2.32e-03

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: 37.72  E-value: 2.32e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2544519355  58 DMTVEKAVVFFEPIPKIKQK--LQTLMDVGLSYITlGQNATTLSGGEAQRIKLAKELSkldTGQTLYILDEPTTGL 131
Cdd:TIGR01189  87 ELSALENLHFWAAIHGGAQRtiEDALAAVGLTGFE-DLPAAQLSAGQQRRLALARLWL---SRRPLWILDEPTTAL 158
thiQ PRK10771
thiamine ABC transporter ATP-binding protein ThiQ;
98-161 2.50e-03

thiamine ABC transporter ATP-binding protein ThiQ;


Pssm-ID: 182716 [Multi-domain]  Cd Length: 232  Bit Score: 37.64  E-value: 2.50e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2544519355  98 LSGGEAQRIKLAKELSKldtGQTLYILDEPTTGLH---FHDIKQLLSVInrLRERENTIVIIEHNLD 161
Cdd:PRK10771  130 LSGGQRQRVALARCLVR---EQPILLLDEPFSALDpalRQEMLTLVSQV--CQERQLTLLMVSHSLE 191
PRK09700 PRK09700
D-allose ABC transporter ATP-binding protein AlsA;
73-170 2.61e-03

D-allose ABC transporter ATP-binding protein AlsA;


Pssm-ID: 182036 [Multi-domain]  Cd Length: 510  Bit Score: 38.23  E-value: 2.61e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2544519355  73 KIKQKLQTLMDVGLSyiTLGQNATTLSGGEAQRIKLAKELSkldTGQTLYILDEPTTGLHFHDIKQLLSVINRLRERENT 152
Cdd:PRK09700  387 RTAENQRELLALKCH--SVNQNITELSGGNQQKVLISKWLC---CCPEVIIFDEPTRGIDVGAKAEIYKVMRQLADDGKV 461
                          90
                  ....*....|....*....
gi 2544519355 153 IVIIEHNL-DVIKTADWIV 170
Cdd:PRK09700  462 ILMVSSELpEIITVCDRIA 480
CFTR_protein TIGR01271
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ...
89-170 2.70e-03

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: 38.35  E-value: 2.70e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2544519355   89 ITLGQNATTLSGGEAQRIKLAKELSKldtGQTLYILDEPTTGLHFHDIKQLL-SVINRLRERENTIVIIEhNLDVIKTAD 167
Cdd:TIGR01271  540 TVLGEGGITLSGGQRARISLARAVYK---DADLYLLDSPFTHLDVVTEKEIFeSCLCKLMSNKTRILVTS-KLEHLKKAD 615

                   ...
gi 2544519355  168 WIV 170
Cdd:TIGR01271  616 KIL 618
nickel_nikE TIGR02769
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a ...
75-160 2.84e-03

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: 37.48  E-value: 2.84e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2544519355  75 KQKLQTLMD-VGLSYITLGQNATTLSGGEAQRIKLAKELSkldTGQTLYILDEPTTGLHFHDIKQLLSVINRLRERENT- 152
Cdd:TIGR02769 127 KARIAELLDmVGLRSEDADKLPRQLSGGQLQRINIARALA---VKPKLIVLDEAVSNLDMVLQAVILELLRKLQQAFGTa 203

                  ....*...
gi 2544519355 153 IVIIEHNL 160
Cdd:TIGR02769 204 YLFITHDL 211
ABC_CysA_sulfate_importer cd03296
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ...
59-192 2.92e-03

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: 37.32  E-value: 2.92e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2544519355  59 MTVEKAVVF---------FEPIPKIKQKLQTLMD-VGLSYitLGQN-ATTLSGGEAQRIKLAKELSkldTGQTLYILDEP 127
Cdd:cd03296    89 MTVFDNVAFglrvkprseRPPEAEIRAKVHELLKlVQLDW--LADRyPAQLSGGQRQRVALARALA---VEPKVLLLDEP 163
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2544519355 128 TTGLHFHDIKQLLSVINRLREREN-TIVIIEHN----LDViktADWIVDVgpeggdKGGHIVATGTPEKV 192
Cdd:cd03296   164 FGALDAKVRKELRRWLRRLHDELHvTTVFVTHDqeeaLEV---ADRVVVM------NKGRIEQVGTPDEV 224
YejF COG4172
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ...
79-192 3.50e-03

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: 37.74  E-value: 3.50e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2544519355  79 QTLMDVGLSYITLGQNATTLSGGEAQRIKLAKEL---SKLdtgqtlYILDEPTTGLhfhDI---KQLLSVINRLREREN- 151
Cdd:COG4172   407 EALEEVGLDPAARHRYPHEFSGGQRQRIAIARALilePKL------LVLDEPTSAL---DVsvqAQILDLLRDLQREHGl 477
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 2544519355 152 TIVIIEHNLDVIKT-ADWIVDVgpeggdKGGHIVATGTPEKV 192
Cdd:COG4172   478 AYLFISHDLAVVRAlAHRVMVM------KDGKVVEQGPTEQV 513
PRK13536 PRK13536
nodulation factor ABC transporter ATP-binding protein NodI;
98-158 3.83e-03

nodulation factor ABC transporter ATP-binding protein NodI;


Pssm-ID: 237419 [Multi-domain]  Cd Length: 340  Bit Score: 37.50  E-value: 3.83e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2544519355  98 LSGGEAQRIKLAKELskLDTGQTLyILDEPTTGLHFHDIKQLLSVINRLRERENTIVIIEH 158
Cdd:PRK13536  173 LSGGMKRRLTLARAL--INDPQLL-ILDEPTTGLDPHARHLIWERLRSLLARGKTILLTTH 230
PLN03232 PLN03232
ABC transporter C family member; Provisional
53-170 4.37e-03

ABC transporter C family member; Provisional


Pssm-ID: 215640 [Multi-domain]  Cd Length: 1495  Bit Score: 37.65  E-value: 4.37e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2544519355   53 ISEVLDMTVEKAVVF---FEPIPKIK----QKLQTLMDV--GLSYITLGQNATTLSGGEAQRIKLAKELSkldTGQTLYI 123
Cdd:PLN03232   687 VSWIFNATVRENILFgsdFESERYWRaidvTALQHDLDLlpGRDLTEIGERGVNISGGQKQRVSMARAVY---SNSDIYI 763
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*..
gi 2544519355  124 LDEPTTGLHFHDIKQLLSVINRLRERENTIVIIEHNLDVIKTADWIV 170
Cdd:PLN03232   764 FDDPLSALDAHVAHQVFDSCMKDELKGKTRVLVTNQLHFLPLMDRII 810
CysA COG1118
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ...
59-192 4.70e-03

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


Pssm-ID: 440735 [Multi-domain]  Cd Length: 348  Bit Score: 37.05  E-value: 4.70e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2544519355  59 MTVEKAVVFF---EPIPK--IKQKLQTLMD-VGLSyiTLG-----QnattLSGGEAQRIKLAKELS---KLdtgqtLyIL 124
Cdd:COG1118    90 MTVAENIAFGlrvRPPSKaeIRARVEELLElVQLE--GLAdrypsQ----LSGGQRQRVALARALAvepEV-----L-LL 157
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2544519355 125 DEPTTGLHFH---DIKQLLSVInrLRERENTIVIIEHNLD-VIKTADWIVDVgpeggdKGGHIVATGTPEKV 192
Cdd:COG1118   158 DEPFGALDAKvrkELRRWLRRL--HDELGGTTVFVTHDQEeALELADRVVVM------NQGRIEQVGTPDEV 221
PstB COG1117
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ...
91-160 4.93e-03

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


Pssm-ID: 440734 [Multi-domain]  Cd Length: 258  Bit Score: 36.94  E-value: 4.93e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2544519355  91 LGQNATTLSGGEAQRIKLAKelskldtgqTLYI------LDEPTTGLhfhD------IKQLlsvINRLRErENTIVIIEH 158
Cdd:COG1117   148 LKKSALGLSGGQQQRLCIAR---------ALAVepevllMDEPTSAL---DpistakIEEL---ILELKK-DYTIVIVTH 211

                  ..
gi 2544519355 159 NL 160
Cdd:COG1117   212 NM 213
cbiO PRK13650
energy-coupling factor transporter ATPase;
98-192 5.67e-03

energy-coupling factor transporter ATPase;


Pssm-ID: 184209 [Multi-domain]  Cd Length: 279  Bit Score: 36.63  E-value: 5.67e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2544519355  98 LSGGEAQRIKLAKELSkldTGQTLYILDEPTTGLHFHDIKQLLSVINRLRERENTIVI-IEHNLDVIKTADWIVDVgpeg 176
Cdd:PRK13650  141 LSGGQKQRVAIAGAVA---MRPKIIILDEATSMLDPEGRLELIKTIKGIRDDYQMTVIsITHDLDEVALSDRVLVM---- 213
                          90
                  ....*....|....*.
gi 2544519355 177 gdKGGHIVATGTPEKV 192
Cdd:PRK13650  214 --KNGQVESTSTPREL 227
PRK10261 PRK10261
glutathione transporter ATP-binding protein; Provisional
98-163 5.97e-03

glutathione transporter ATP-binding protein; Provisional


Pssm-ID: 182342 [Multi-domain]  Cd Length: 623  Bit Score: 37.14  E-value: 5.97e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2544519355  98 LSGGEAQRIKLAKELSkldTGQTLYILDEPTTGLHFHDIKQLLSVINRL-RERENTIVIIEHNLDVI 163
Cdd:PRK10261  169 LSGGMRQRVMIAMALS---CRPAVLIADEPTTALDVTIQAQILQLIKVLqKEMSMGVIFITHDMGVV 232
FtsE COG2884
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
58-164 6.67e-03

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


Pssm-ID: 442130 [Multi-domain]  Cd Length: 223  Bit Score: 36.18  E-value: 6.67e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2544519355  58 DMTVEKAVVFF-----EPIPKIKQKLQTLMD-VGLSYItLGQNATTLSGGEAQRIKLAKEL-SKLDtgqtLYILDEPTTG 130
Cdd:COG2884    93 DRTVYENVALPlrvtgKSRKEIRRRVREVLDlVGLSDK-AKALPHELSGGEQQRVAIARALvNRPE----LLLADEPTGN 167
                          90       100       110
                  ....*....|....*....|....*....|....
gi 2544519355 131 LHFHDIKQLLSVINRLRERENTIVIIEHNLDVIK 164
Cdd:COG2884   168 LDPETSWEIMELLEEINRRGTTVLIATHDLELVD 201
ABC_HisP_GlnQ cd03262
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ...
97-158 8.03e-03

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: 35.97  E-value: 8.03e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2544519355  97 TLSGGEAQRIKLAKELSkldTGQTLYILDEPTTGLHFHDIKQLLSVINRLRERENTIVIIEH 158
Cdd:cd03262   135 QLSGGQQQRVAIARALA---MNPKVMLFDEPTSALDPELVGEVLDVMKDLAEEGMTMVVVTH 193
ABCC_CFTR1 cd03291
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ...
60-170 8.37e-03

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: 36.37  E-value: 8.37e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2544519355  60 TVEKAVVFFEPIPKIKQKlqtlmdvglSYITLGQNATTLSGGEAQRIKLAKELSKldtGQTLYILDEPTTGLHFHDIKQL 139
Cdd:cd03291   131 SVVKACQLEEDITKFPEK---------DNTVLGEGGITLSGGQRARISLARAVYK---DADLYLLDSPFGYLDVFTEKEI 198
                          90       100       110
                  ....*....|....*....|....*....|....*
gi 2544519355 140 L-SVINRLRERENTIVI---IEHnldvIKTADWIV 170
Cdd:cd03291   199 FeSCVCKLMANKTRILVtskMEH----LKKADKIL 229
 
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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